LiteFold/InterPro · Datasets at Hugging Face

IPR002279

2,279

Melatonin receptor type 1C

Mel_rcpt_1C

Family

658

false

Melatonin is a naturally occurring compound found in animals, plants, and microbes [ , ]. In animals melatonin is secreted by the pineal gland during darkness [ , ]. It regulates a variety of neuroendocrine functions and is thought to play an essential role in circadian rhythms [ ]. Drugs that modify the action of mela...

[ "GO:0008502", "GO:0007186", "GO:0016020" ]

[ "melatonin receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PRINTS" ]

[ "PR01150" ]

[ "MELATONIN1CR" ]

[ 658 ]

1

[]

0

[]

0

[ "PUB00004315", "PUB00066873", "PUB00066874", "PUB00066875", "PUB00066876", "PUB00066877", "PUB00066878", "PUB00066879", "PUB00066880", "PUB00066881", "PUB00066882" ]

[ "7576645", "15206778", "19033551", "1649044", "17901231", "17298593", "16473858", "15992934", "8936344", "15357831", "9933574" ]

[ "Melatonin receptors are for the birds: molecular analysis of two receptor subtypes differentially expressed in chick brain.", "Melatonin in plants.", "Phytomelatonin: a review.", "Pineal melatonin: cell biology of its synthesis and of its physiological interactions.", "Minireview: Entrainment of the suprac...

[ 1995, 2003, 2009, 1991, 2007, 2007, 2006, 2005, 1996, 2004, 1999 ]

11

[]

0

null

[ "Gnathostomata" ]

[ 658 ]

1

[ "Danio rerio" ]

[ 1 ]

1

true

Family

Melatonin receptor type 1C

Mel_rcpt_1C

9

IPR002280

2,280

Melatonin-related receptor 1X

Mel_rcpt_1X

Family

198

false

Melatonin is a naturally occurring compound found in animals, plants, and microbes [ , ]. In animals melatonin is secreted by the pineal gland during darkness [ , ]. It regulates a variety of neuroendocrine functions and is thought to play an essential role in circadian rhythms [ ]. Drugs that modify the action of mela...

[ "GO:0004930", "GO:0007186", "GO:0016020" ]

[ "G protein-coupled receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PRINTS" ]

[ "PR01151" ]

[ "MELATONIN1XR" ]

[ 198 ]

1

[]

0

[]

0

[ "PUB00001701", "PUB00066873", "PUB00066874", "PUB00066875", "PUB00066876", "PUB00066877", "PUB00066878", "PUB00066879", "PUB00066880", "PUB00066881", "PUB00066882", "PUB00066887" ]

[ "8647286", "15206778", "19033551", "1649044", "17901231", "17298593", "16473858", "15992934", "8936344", "15357831", "9933574", "18400093" ]

[ "Cloning of a melatonin-related receptor from human pituitary.", "Melatonin in plants.", "Phytomelatonin: a review.", "Pineal melatonin: cell biology of its synthesis and of its physiological interactions.", "Minireview: Entrainment of the suprachiasmatic clockwork in diurnal and nocturnal mammals.", "Mel...

[ 1996, 2003, 2009, 1991, 2007, 2007, 2006, 2005, 1996, 2004, 1999, 2008 ]

12

[ "IPR000025" ]

[]

1

0

1

[ "Euteleostomi" ]

[ 198 ]

1

[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 3, 1, 3 ]

3

true

Family

Melatonin-related receptor 1X

Mel_rcpt_1X

9

IPR002281

2,281

Protease-activated receptor 2

Pro_rcpt_2

Family

876

false

G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can...

[ "GO:0015057", "GO:0070493", "GO:0016020" ]

[ "thrombin-activated receptor activity", "thrombin-activated receptor signaling pathway", "membrane" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PRINTS" ]

[ "PR01152" ]

[ "PROTEASEAR2" ]

[ 876 ]

1

[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "348", "R-HSA-375276", "R-HSA-416476", "R-MMU-375276", "R-MMU-416476", "R-RNO-375276", "R-RNO-416476" ]

[ "IUPHAR:348", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-416476", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-416476", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-416476" ]

7

[ "5nj6", "8zmd", "8zme", "9d0a", "9e7r" ]

5

[ "PUB00000131", "PUB00000542", "PUB00002477", "PUB00002945", "PUB00004960", "PUB00004961", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]

[ "2111655", "8615752", "2830256", "7890726", "8386361", "8170923", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]

[ "G proteins in signal transduction.", "Molecular cloning, expression and potential functions of the human proteinase-activated receptor-2.", "G protein involvement in receptor-effector coupling.", "The mouse proteinase-activated receptor-2 cDNA and gene. Molecular cloning and functional expression.", "Desig...

[ 1990, 1996, 1988, 1995, 1993, 1994, 2003, 1994, 2005, 2009, 2006, 2013 ]

12

[ "IPR003912" ]

[]

1

0

1

[ "Vertebrata" ]

[ 876 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 4, 2, 4, 2 ]

4

true

Family

Protease-activated receptor 2

Pro_rcpt_2

8

IPR002285

2,285

GPCR, family 2, pituitary adenylate cyclase activating polypeptide type 1 receptor

GPCR_2_PACAP_1_rcpt

Family

2,302

false

G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can...

[ "GO:0004999", "GO:0007186", "GO:0016020" ]

[ "vasoactive intestinal polypeptide receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PRINTS" ]

[ "PR01156" ]

[ "PACAPRECEPTR" ]

[ 2302 ]

1

[ "GP", "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "GenProp2094", "370", "R-BTA-418555", "R-BTA-420092", "R-HSA-187024", "R-HSA-418555", "R-HSA-420092", "R-MMU-418555", "R-MMU-420092", "R-RNO-420092" ]

[ "GP:GenProp2094", "IUPHAR:370", "REACTOME:R-BTA-418555", "REACTOME:R-BTA-420092", "REACTOME:R-HSA-187024", "REACTOME:R-HSA-418555", "REACTOME:R-HSA-420092", "REACTOME:R-MMU-418555", "REACTOME:R-MMU-420092", "REACTOME:R-RNO-420092" ]

10

[ "2jod", "6lpb", "6m1h", "6m1i", "6p9y", "7jqd", "8e3x" ]

7

[ "PUB00001208", "PUB00003458", "PUB00003459", "PUB00004310", "PUB00004822", "PUB00004961", "PUB00005147", "PUB00005148", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]

[ "1646711", "8933357", "8784257", "1314625", "8392197", "8170923", "1658940", "1658941", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]

[ "Molecular cloning and expression of a cDNA encoding the secretin receptor.", "Tissue specific expression of different human receptor types for pituitary adenylate cyclase activating polypeptide and vasoactive intestinal polypeptide: implications for their role in human physiology.", "Differential expression of...

[ 1991, 1996, 1996, 1992, 1993, 1994, 1991, 1991, 2003, 1994, 2005, 2009, 2006, 2013 ]

14

[ "IPR000832" ]

[]

1

0

1

[ "Gnathostomata" ]

[ 2302 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 6, 5, 9, 7 ]

4

true

Family

GPCR, family 2, pituitary adenylate cyclase activating polypeptide type 1 receptor

GPCR_2_PACAP_1_rcpt

2

IPR002288

2,288

DNA gyrase B subunit, C-terminal

DNA_gyrase_B_C

Domain

48,296

false

This entry represents the C-terminal of the DNA gyrase B. The N terminus of eukaryotic and prokaryotic DNA topoisomerase II are similar, but they have a different C terminus. The N-terminal of the DNA gyrase B protein is thought to catalyse the ATP-dependent super-coiling of DNA. The C-terminal end supports the complex...

[ "GO:0003677", "GO:0003918", "GO:0005524", "GO:0006265" ]

[ "DNA binding", "DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity", "ATP binding", "DNA topological change" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "PFAM" ]

[ "PF00986" ]

[ "DNA_gyraseB_C" ]

[ 48296 ]

1

[ "EC", "REACTOME", "REACTOME" ]

[ "5.6.2.2", "R-HSA-9638771", "R-HSA-9913143" ]

[ "EC:5.6.2.2", "REACTOME:R-HSA-9638771", "REACTOME:R-HSA-9913143" ]

3

[ "2xco", "2xcq", "2xcr", "2xcs", "2xct", "2xkj", "2xkk", "2zjt", "3foe", "3fof", "3ig0", "3k9f", "3ksa", "3ksb", "3ltn", "3m4i", "3nuh", "3rad", "3rae", "3raf", "4bul", "4i3h", "4juo", "4koe", "4kpe", "4kpf", "4plb", "4tma", "4z2c", "4z2d", "4z2e", "4z3o"...

98

[ "PUB00004227", "PUB00005437" ]

[ "8538787", "7770916" ]

[ "Structure and mechanism of DNA topoisomerase II.", "The mechanisms of DNA topoisomerases." ]

[ 1996, 1995 ]

2

[]

0

null

[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]

[ 558, 45747, 59, 1021, 911 ]

5

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 9, 2, 3, 4 ]

4

true

Domain

DNA gyrase B subunit, C-terminal

DNA_gyrase_B_C

4

IPR002291

2,291

Phosphorylase kinase, gamma catalytic subunit

Phosph_kin_gamma

Family

2,722

false

null

[ "GO:0004689", "GO:0005516", "GO:0005524", "GO:0005977", "GO:0006468", "GO:0005964" ]

[ "phosphorylase kinase activity", "calmodulin binding", "ATP binding", "glycogen metabolic process", "protein phosphorylation", "phosphorylase kinase complex" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "biological_process", "cellular_component" ]

6

[ "PRINTS" ]

[ "PR01049" ]

[ "PHOSPHBKNASE" ]

[ 2722 ]

1

[ "EC", "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.7.11", "2.7.11.19", "GenProp2089", "R-BTA-70221", "R-HSA-70221", "R-MMU-70221", "R-RNO-70221" ]

[ "EC:2.7.11", "EC:2.7.11.19", "GP:GenProp2089", "REACTOME:R-BTA-70221", "REACTOME:R-HSA-70221", "REACTOME:R-MMU-70221", "REACTOME:R-RNO-70221" ]

7

[ "1phk", "1ql6", "2phk", "2y7j", "8jfk", "8jfl", "8xy7", "8xya", "8xyb", "8z5m", "8z5p", "8z5q", "8z5r", "8z5t" ]

14

[ "PUB00000241", "PUB00000744", "PUB00001685", "PUB00003467", "PUB00004318", "PUB00005088", "PUB00005115", "PUB00015362", "PUB00020114", "PUB00034898", "PUB00034899" ]

[ "7857257", "8590760", "7729511", "7562285", "9553951", "8944243", "3291115", "12368087", "12471243", "15078142", "15320712" ]

[ "Phosphorylation/activation of phosphorylase b kinase by cAMP/Ca2(+)-independent, autophosphorylation-dependent protein kinase.", "[Association of rabbit skeletal muscle phosphorylase kinase with sarcoplasmic reticulum membranes]", "Does phosphorylase kinase control glycogen biosynthesis in skeletal muscle?", ...

[ 1995, 1995, 1995, 1995, 1998, 1996, 1988, 2002, 2002, 2004, 2004 ]

11

[]

0

null

[ "Eukaryota" ]

[ 2722 ]

1

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 1, 14, 5, 8, 2, 8 ]

6

true

Family

Phosphorylase kinase, gamma catalytic subunit

Phosph_kin_gamma

1

IPR002295

2,295

N4/N6-methyltransferase, Type III restriction-modification enzyme EcoPI Mod subunit-like

N4/N6-MTase_EcoPI_Mod-like

Family

11,196

false

This protein family includes SAM-dependent beta subtype DNA methyltransferases that methylate exocyclic nitrogens and form either N4-methylcytosine (N4-MTases) or N6-methyladenine (N6-MTases) [ ], including Type III restriction-modification enzyme EcoPI Mod subunit from Escherichia phage P1, a component of the beta sub...

[ "GO:0003677", "GO:0008170" ]

[ "DNA binding", "N-methyltransferase activity" ]

[ "molecular_function", "molecular_function" ]

2

[ "PIRSF", "PRINTS" ]

[ "PIRSF015855", "PR00506" ]

[ "TypeIII_Mtase_mKpnI", "D21N6MTFRASE" ]

[ 4920, 10619 ]

2

[ "EC" ]

[ "2.1.1.72" ]

[ "EC:2.1.1.72" ]

1

[ "1eg2", "1nw5", "1nw6", "1nw7", "1nw8", "4zcf", "6k0w", "7dsu" ]

8

[ "PUB00000092", "PUB00008667", "PUB00100376" ]

[ "7663118", "11178902", "18541145" ]

[ "Structure and function of DNA methyltransferases.", "Subunit assembly and mode of DNA cleavage of the type III restriction endonucleases EcoP1I and EcoP15I.", "The human mitochondrial translation release factor HMRF1L is methylated in the GGQ motif by the methyltransferase HMPrmC." ]

[ 1995, 2001, 2008 ]

3

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]

[ 167, 10345, 213, 143, 328 ]

5

[ "Homo sapiens" ]

[ 3 ]

1

true

Family

N4/N6-methyltransferase, Type III restriction-modification enzyme EcoPI Mod subunit-like

N4/N6-MTase_EcoPI_Mod-like

6

IPR002297

2,297

DNA-directed DNA-polymerase, family A, mitochondria

DNA-dir_DNA_pol_A_mt

Family

4,149

false

DNA carries the biological information that instructs cells how to exist in an ordered fashion. Accurate replication is thus one of the most important events in the cell life cycle. This function is mediated by DNA-directed DNA-polymerases, which add nucleotide triphosphate (dNTP) residues to the 5'-end of the growing ...

[ "GO:0003677", "GO:0006260", "GO:0005760" ]

[ "DNA binding", "DNA replication", "gamma DNA polymerase complex" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PIRSF", "PRINTS", "PANTHER" ]

[ "PIRSF000797", "PR00867", "PTHR10267" ]

[ "DNA_pol_mt", "DNAPOLG", "" ]

[ 181, 3751, 4148 ]

3

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.7.7.7", "R-DME-9913635", "R-HSA-9913635", "R-MMU-9913635", "R-RNO-9913635" ]

[ "EC:2.7.7.7", "REACTOME:R-DME-9913635", "REACTOME:R-HSA-9913635", "REACTOME:R-MMU-9913635", "REACTOME:R-RNO-9913635" ]

5

[ "3ikm", "4ztu", "4ztz", "5c51", "5c52", "5c53", "8d33", "8d37", "8d3r", "8d42", "8g5i", "8g5j", "8g5k", "8g5l", "8g5m", "8g5n", "8g5o", "8g5p", "8t7e", "8udk", "8udl", "8v54", "8v55", "8v5d", "8v5r", "9c51", "9c52", "9c53", "9d2i", "9g74", "9g75", "9g77"...

42

[ "PUB00002437", "PUB00004647", "PUB00004955" ]

[ "3522588", "3479792", "2196557" ]

[ "A nuclear mutant of Saccharomyces cerevisiae deficient in mitochondrial DNA replication and polymerase activity.", "Bacteriophage PRD1 DNA polymerase: evolution of DNA polymerases.", "An attempt to unify the structure of polymerases." ]

[ 1986, 1987, 1990 ]

3

[]

0

null

[ "Caudoviricetes", "Eukaryota", "Floridanema" ]

[ 15, 4132, 2 ]

3

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strai...

[ 1, 7, 1, 26, 13, 1, 4, 1, 1 ]

9

true

Family

DNA-directed DNA-polymerase, family A, mitochondria

DNA-dir_DNA_pol_A_mt

5

IPR002298

2,298

DNA polymerase A

DNA_polymerase_A

Family

45,208

false

DNA carries the biological information that instructs cells how to exist in an ordered fashion. Accurate replication is thus one of the most important events in the cell life cycle. This function is mediated by DNA-directed DNA polymerases, which add nucleotide triphosphate (dNTP) residues to the 3'-end of the growing ...

[ "GO:0003887", "GO:0006261" ]

[ "DNA-directed DNA polymerase activity", "DNA-templated DNA replication" ]

[ "molecular_function", "biological_process" ]

2

[ "PRINTS", "PANTHER" ]

[ "PR00868", "PTHR10133" ]

[ "DNAPOLI", "" ]

[ 37917, 45004 ]

2

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.7.7.7", "R-DME-5685939", "R-HSA-5685939", "R-HSA-6783310", "R-MMU-5685939", "R-MMU-6783310" ]

[ "EC:2.7.7.7", "REACTOME:R-DME-5685939", "REACTOME:R-HSA-5685939", "REACTOME:R-HSA-6783310", "REACTOME:R-MMU-5685939", "REACTOME:R-MMU-6783310" ]

6

[ "1bgx", "1d8y", "1d9d", "1d9f", "1dpi", "1jxe", "1kfd", "1kfs", "1kln", "1krp", "1ksp", "1ktq", "1l3s", "1l3t", "1l3u", "1l3v", "1l5u", "1lv5", "1njw", "1njx", "1njy", "1njz", "1nk0", "1nk4", "1nk5", "1nk6", "1nk7", "1nk8", "1nk9", "1nkb", "1nkc", "1nke"...

292

[ "PUB00004647", "PUB00004955" ]

[ "3479792", "2196557" ]

[ "Bacteriophage PRD1 DNA polymerase: evolution of DNA polymerases.", "An attempt to unify the structure of polymerases." ]

[ 1987, 1990 ]

2

[]

[ "IPR018320", "IPR034699" ]

0

2

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 17, 32160, 6496, 5070, 1465 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]

[ 17, 1, 2, 1, 1, 8, 11, 13, 8, 44 ]

10

true

Family

DNA polymerase A

DNA_polymerase_A

9

IPR002299

2,299

Porin, Neisseria sp. type

Porin_Neis

Family

18,712

false

Porins are found in the outer membranes of Gram-negative bacteria, mitochondria and chloroplasts, where they form ion-selective channels for small hydrophilic molecules (up to ~600 D) [ , ]. X-ray structure analyses of several bacterial porins [ , , ] have revealed a large 16-stranded anti-parallel β-barrel structure e...

[ "GO:0015288", "GO:0055085", "GO:0016020" ]

[ "porin activity", "transmembrane transport", "membrane" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PRINTS" ]

[ "PR00184" ]

[ "NEISSPPORIN" ]

[ 18712 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-HSA-1236974", "R-HSA-166058", "R-HSA-168179", "R-HSA-3000484", "R-HSA-5602498", "R-HSA-5603041" ]

[ "REACTOME:R-HSA-1236974", "REACTOME:R-HSA-166058", "REACTOME:R-HSA-168179", "REACTOME:R-HSA-3000484", "REACTOME:R-HSA-5602498", "REACTOME:R-HSA-5603041" ]

6

[ "1e54", "2fgq", "2fgr", "3a2s", "3vy8", "3vy9", "3vzt", "3vzu", "3vzw", "3wi4", "3wi5", "4aui", "7de8", "8jto", "8wv0" ]

15

[ "PUB00001604", "PUB00003334", "PUB00003475", "PUB00003829", "PUB00005073" ]

[ "1707373", "7525973", "1725488", "1373213", "2178269" ]

[ "The structure of porin from Rhodobacter capsulatus at 1.8 A resolution.", "Refined structure of the porin from Rhodopseudomonas blastica. Comparison with the porin from Rhodobacter capsulatus.", "A common channel-forming motif in evolutionarily distant porins.", "Porins and specific channels of bacterial out...

[ 1991, 1994, 1991, 1992, 1990 ]

5

[ "IPR001702" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 18629, 8, 75 ]

3

[]

0

true

Family

Porin, Neisseria sp. type

Porin_Neis

8

IPR002300

2,300

Aminoacyl-tRNA synthetase, class Ia

aa-tRNA-synth_Ia

Domain

118,798

false

Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [ ]. The 20 aminoacyl-tRNA synth...

[ "GO:0000166", "GO:0004812", "GO:0005524", "GO:0006418" ]

[ "nucleotide binding", "aminoacyl-tRNA ligase activity", "ATP binding", "tRNA aminoacylation for protein translation" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "PFAM" ]

[ "PF00133" ]

[ "tRNA-synt_1" ]

[ 118798 ]

1

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "6.1.1", "R-DDI-9837999", "R-DDI-9856649", "R-HSA-2408522", "R-HSA-379716", "R-HSA-379726", "R-HSA-9837999", "R-HSA-9856649", "R-MMU-9837999", "R-MMU-9856649", "R-SCE-9837999", "R-SPO-9837999" ]

[ "EC:6.1.1", "REACTOME:R-DDI-9837999", "REACTOME:R-DDI-9856649", "REACTOME:R-HSA-2408522", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-379726", "REACTOME:R-HSA-9837999", "REACTOME:R-HSA-9856649", "REACTOME:R-MMU-9837999", "REACTOME:R-MMU-9856649", "REACTOME:R-SCE-9837999", "REACTOME:R-SPO-9837999"...

12

[ "1ffy", "1gax", "1h3n", "1ile", "1ivs", "1iyw", "1jzq", "1jzs", "1obc", "1obh", "1qu2", "1qu3", "1wkb", "1wz2", "2bte", "2byt", "2v0c", "2v0g", "3zgz", "3ziu", "3zjt", "3zju", "3zjv", "4aq7", "4arc", "4ari", "4as1", "4cqn", "5ah5", "5omw", "5on2", "5on3"...

90

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00055442", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "10673435", "2203971", "10447505", "11590011", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 2000, 1990, 1999, 2001, 2000, 2002 ]

10

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 3194, 80562, 32561, 64, 2417 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 36, 8, 8, 12, 3, 73, 30, 5, 36, 23, 5, 6, 117 ]

13

true

Domain

Aminoacyl-tRNA synthetase, class Ia

aa-tRNA-synth_Ia

7

IPR002301

2,301

Isoleucine-tRNA ligase

Ile-tRNA-ligase

Family

39,944

false

Isoleucine-tRNA ligase (also known as Isoleucyl-tRNA synthetase)( ) is an alpha monomer that belongs to class Ia. The enzyme, isoleucine-tRNA ligase, activates not only the cognate substrate L-isoleucine but also the minimally distinct L-valine in the first, aminoacylation step. Then, in a second, "editing" step, the l...

[ "GO:0000166", "GO:0004822", "GO:0005524", "GO:0006428" ]

[ "nucleotide binding", "isoleucine-tRNA ligase activity", "ATP binding", "isoleucyl-tRNA aminoacylation" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "PRINTS", "NCBIFAM" ]

[ "PR00984", "TIGR00392" ]

[ "TRNASYNTHILE", "ileS" ]

[ 39706, 36459 ]

2

[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "6.1.1.5", "GenProp0258", "R-DDI-9837999", "R-DDI-9856649", "R-HSA-2408522", "R-HSA-379716", "R-HSA-379726", "R-HSA-9837999", "R-HSA-9856649", "R-MMU-9837999", "R-MMU-9856649", "R-SCE-9837999", "R-SPO-9837999" ]

[ "EC:6.1.1.5", "GP:GenProp0258", "REACTOME:R-DDI-9837999", "REACTOME:R-DDI-9856649", "REACTOME:R-HSA-2408522", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-379726", "REACTOME:R-HSA-9837999", "REACTOME:R-HSA-9856649", "REACTOME:R-MMU-9837999", "REACTOME:R-MMU-9856649", "REACTOME:R-SCE-9837999", "R...

13

[ "1ffy", "1ile", "1jzq", "1jzs", "1qu2", "1qu3", "1wk8", "6ldk", "7d5c", "8c8u", "8c8v", "8c8w", "8c9d", "8c9e", "8c9f", "8c9g", "8wnd", "8wnf", "8wng", "8wni", "8wnj", "8wo2", "8wo3", "8z1p" ]

24

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006404", "PUB00006454", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "9554847", "10446055", "10673435", "2203971", "10447505", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 1998, 1999, 2000, 1990, 1999, 2000, 2002 ]

11

[]

[ "IPR023585", "IPR023586" ]

0

2

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 976, 27872, 10403, 36, 657 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 12, 3, 2, 3, 1, 17, 6, 2, 8, 5, 2, 2, 41 ]

13

true

Family

Isoleucine-tRNA ligase

Ile-tRNA-ligase

4

IPR002302

2,302

Leucine-tRNA ligase

Leu-tRNA-ligase

Family

35,391

false

Leucine-tRNA ligase ( ) is an alpha monomer that belongs to class Ia. The crystal structure of leucine-tRNA ligase from the hyperthermophile Thermus thermophilus has an overall architecture that is similar to that of isoleucine-tRNA ligase, except that the putative editing domain is inserted at a different position in ...

[ "GO:0000166", "GO:0004823", "GO:0005524", "GO:0006429" ]

[ "nucleotide binding", "leucine-tRNA ligase activity", "ATP binding", "leucyl-tRNA aminoacylation" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "HAMAP", "PRINTS", "PANTHER", "NCBIFAM" ]

[ "MF_00049_B", "PR00985", "PTHR43740", "TIGR00396" ]

[ "Leu_tRNA_synth_B", "TRNASYNTHLEU", "", "leuS_bact" ]

[ 28452, 33537, 35376, 29313 ]

4

[ "EC", "GP", "REACTOME" ]

[ "6.1.1.4", "GenProp0258", "R-HSA-379726" ]

[ "EC:6.1.1.4", "GP:GenProp0258", "REACTOME:R-HSA-379726" ]

3

[ "1h3n", "1obc", "1obh", "2ajg", "2ajh", "2aji", "2bte", "2byt", "2v0c", "2v0g", "3o0a", "3pz0", "3pz5", "3zgz", "3ziu", "3zjt", "3zju", "3zjv", "4aq7", "4arc", "4ari", "4as1", "4cqn", "4k47", "4k48", "5agr", "5ags", "5agt", "5ah5", "5omw", "5on2", "5on3"...

74

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006477", "PUB00006534", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "10673435", "10811626", "2203971", "10447505", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 2000, 2000, 1990, 1999, 2000, 2002 ]

10

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences", "uncultured marine phage" ]

[ 389, 28749, 5353, 899, 1 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 8, 3, 1, 1, 1, 6, 7, 1, 4, 4, 1, 1, 4 ]

13

true

Family

Leucine-tRNA ligase

Leu-tRNA-ligase

5

IPR002303

2,303

Valine-tRNA ligase

Valyl-tRNA_ligase

Family

41,045

false

Valine-tRNA ligase (also known as Valyl-tRNA synthetase) ( ) is an alpha monomer that belongs to class Ia aminoacyl-tRNA ligase. Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ ...

[ "GO:0000166", "GO:0004832", "GO:0005524", "GO:0006438" ]

[ "nucleotide binding", "valine-tRNA ligase activity", "ATP binding", "valyl-tRNA aminoacylation" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "HAMAP", "PRINTS", "PANTHER", "NCBIFAM" ]

[ "MF_02004", "PR00986", "PTHR11946", "TIGR00422" ]

[ "Val_tRNA_synth_type1", "TRNASYNTHVAL", "", "valS" ]

[ 29031, 37891, 41030, 32565 ]

4

[ "EC", "GP", "REACTOME", "REACTOME" ]

[ "6.1.1.9", "GenProp0258", "R-HSA-379716", "R-HSA-379726" ]

[ "EC:6.1.1.9", "GP:GenProp0258", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-379726" ]

4

[ "1gax", "1ivs", "1iyw", "1wk9", "1wka", "4xkz" ]

6

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "10673435", "2203971", "10447505", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 2000, 1990, 1999, 2000, 2002 ]

9

[]

[ "IPR022874" ]

0

1

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 1023, 28747, 10276, 16, 983 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 14, 2, 4, 5, 1, 31, 11, 1, 17, 11, 1, 2, 48 ]

13

true

Family

Valine-tRNA ligase

Valyl-tRNA_ligase

9

IPR002305

2,305

Aminoacyl-tRNA synthetase, class Ic

aa-tRNA-synth_Ic

Family

82,070

false

Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [ ]. The 20 aminoacyl-tRNA synth...

[ "GO:0000166", "GO:0004812", "GO:0005524", "GO:0006418" ]

[ "nucleotide binding", "aminoacyl-tRNA ligase activity", "ATP binding", "tRNA aminoacylation for protein translation" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "PFAM" ]

[ "PF00579" ]

[ "tRNA-synt_1b" ]

[ 82070 ]

1

[ "EC", "REACTOME", "REACTOME" ]

[ "6.1.1.1", "R-HSA-379716", "R-HSA-379726" ]

[ "EC:6.1.1.1", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-379726" ]

3

[ "1d2r", "1h3e", "1h3f", "1i6k", "1i6l", "1i6m", "1j1u", "1jii", "1jij", "1jik", "1jil", "1m83", "1mau", "1maw", "1mb2", "1n3l", "1o5t", "1q11", "1r6t", "1r6u", "1tya", "1tyb", "1tyc", "1tyd", "1u7d", "1u7x", "1ulh", "1vbm", "1vbn", "1wq3", "1wq4", "1x8x"...

203

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00055442", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "10673435", "2203971", "10447505", "11590011", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 2000, 1990, 1999, 2001, 2000, 2002 ]

10

[]

[ "IPR002306", "IPR002307" ]

0

2

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 2072, 58135, 20405, 82, 1376 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 24, 5, 13, 7, 2, 19, 16, 4, 33, 26, 4, 4, 36 ]

13

true

Family

Aminoacyl-tRNA synthetase, class Ic

aa-tRNA-synth_Ic

2

IPR002306

2,306

Tryptophan-tRNA ligase

Trp-tRNA-ligase

Family

41,440

false

This entry represents tryptophan-tRNA ligase (TrpRS; also known as tryptophanyl-tRNA synthetase) ( ). The enzyme is widely distributed, being found in archaea, bacteria and eukaryotes. TrpRS is a homodimer which attaches Tyr to the appropriate tRNA. TrpRS is a class I tRNA synthetase, so it aminoacylates the 2'-OH of t...

[ "GO:0000166", "GO:0004830", "GO:0005524", "GO:0006436" ]

[ "nucleotide binding", "tryptophan-tRNA ligase activity", "ATP binding", "tryptophanyl-tRNA aminoacylation" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "PRINTS", "NCBIFAM", "CDD" ]

[ "PR01039", "TIGR00233", "cd00806" ]

[ "TRNASYNTHTRP", "trpS", "TrpRS_core" ]

[ 41193, 39518, 37702 ]

3

[ "EC", "GP", "REACTOME", "REACTOME" ]

[ "6.1.1.2", "GenProp0258", "R-HSA-379716", "R-HSA-379726" ]

[ "EC:6.1.1.2", "GP:GenProp0258", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-379726" ]

4

[ "1d2r", "1i6k", "1i6l", "1i6m", "1m83", "1mau", "1maw", "1mb2", "1o5t", "1r6t", "1r6u", "1ulh", "1yi8", "1yia", "1yid", "2a4m", "2ake", "2azx", "2dr2", "2el7", "2g36", "2ip1", "2ov4", "2quh", "2qui", "2quj", "2quk", "2yy5", "3a04", "3a05", "3fhj", "3fi0"...

96

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006477", "PUB00006480", "PUB00007191", "PUB00007363", "PUB00055442", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "10673435", "10716174", "2203971", "10447505", "11590011", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 2000, 2000, 1990, 1999, 2001, 2000, 2002 ]

11

[ "IPR002305" ]

[ "IPR020653", "IPR024109" ]

1

2

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 1088, 30088, 9590, 23, 651 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 13, 2, 8, 5, 1, 9, 7, 2, 10, 12, 2, 2, 10 ]

13

true

Family

Tryptophan-tRNA ligase

Trp-tRNA-ligase

5

IPR002307

2,307

Tyrosine-tRNA ligase

Tyr-tRNA-ligase

Family

36,866

false

Tyrosine-tRNA ligases (TyrRS; also known as Tyrosyl-tRNA synthetases) ( ) are widely distributed, being found in archaea, bacteria and eukaryotes. TyrRS is a homodimer which attaches Tyr to the appropriate tRNA. TyrRS is a class I tRNA synthetases, so it aminoacylates the 2'-OH of the nucleotide at the 3' end of the tR...

[ "GO:0000166", "GO:0004831", "GO:0005524", "GO:0006437" ]

[ "nucleotide binding", "tyrosine-tRNA ligase activity", "ATP binding", "tyrosyl-tRNA aminoacylation" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "PRINTS", "NCBIFAM", "CDD" ]

[ "PR01040", "TIGR00234", "cd00805" ]

[ "TRNASYNTHTYR", "tyrS", "TyrRS_core" ]

[ 36267, 36514, 32083 ]

3

[ "EC", "GP", "REACTOME", "REACTOME" ]

[ "6.1.1.1", "GenProp0258", "R-HSA-379716", "R-HSA-379726" ]

[ "EC:6.1.1.1", "GP:GenProp0258", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-379726" ]

4

[ "1h3e", "1h3f", "1j1u", "1jii", "1jij", "1jik", "1jil", "1n3l", "1q11", "1tya", "1tyb", "1tyc", "1tyd", "1u7d", "1u7x", "1vbm", "1vbn", "1wq3", "1wq4", "1x8x", "1y42", "1zh0", "1zh6", "2ag6", "2cya", "2cyb", "2cyc", "2dlc", "2hgz", "2jan", "2pid", "2pxh"...

90

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006465", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00055442", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "10630994", "10673435", "2203971", "10447505", "11590011", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 2000, 2000, 1990, 1999, 2001, 2000, 2002 ]

11

[ "IPR002305" ]

[ "IPR023617", "IPR024088" ]

1

2

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 820, 27496, 7965, 32, 553 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 4, 3, 5, 2, 1, 7, 5, 2, 3, 10, 2, 2, 3 ]

13

true

Family

Tyrosine-tRNA ligase

Tyr-tRNA-ligase

4

IPR002310

2,310

Glycine-tRNA ligase, alpha subunit

Gly-tRNA_ligase_asu

Family

15,027

false

This entry represents the alpha subunit of glycine-tRNA ligase (also known as glycyl-tRNA synthetase alpha subunit). It is responsible for the attachment of glycine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-ad...

[ "GO:0000166", "GO:0004820", "GO:0005524", "GO:0006426", "GO:0005737" ]

[ "nucleotide binding", "glycine-tRNA ligase activity", "ATP binding", "glycyl-tRNA aminoacylation", "cytoplasm" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

5

[ "HAMAP", "PFAM", "PRINTS", "NCBIFAM", "CDD" ]

[ "MF_00254", "PF02091", "PR01044", "TIGR00388", "cd00733" ]

[ "Gly_tRNA_synth_alpha", "tRNA-synt_2e", "TRNASYNTHGA", "glyQ", "GlyRS_alpha_core" ]

[ 14388, 15022, 14708, 14392, 13072 ]

5

[ "EC", "GP" ]

[ "6.1.1.14", "GenProp0258" ]

[ "EC:6.1.1.14", "GP:GenProp0258" ]

2

[ "1j5w", "3rf1", "3rgl", "3ufg", "5f5w", "7eiv", "7lu4", "7qcf", "7xjy", "7xjz", "7xk0", "7xk1", "7xof", "7yse", "8h1c", "8ie2" ]

16

[ "PUB00000386", "PUB00000723", "PUB00002277", "PUB00002392", "PUB00002880", "PUB00004391", "PUB00005365", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "7665503", "6309809", "7962006", "1852601", "2053131", "10673435", "2203971", "10447505", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "The glycyl-tRNA synthetase of Chlamydia trachomatis.", "Primary structures of both subunits of Escherichia coli glycyl-tRNA synthetase.", "Human glyc...

[ 1993, 1993, 1995, 1983, 1994, 1991, 1991, 2000, 1990, 1999, 2000, 2002 ]

12

[ "IPR006194" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 3, 13942, 857, 225 ]

4

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 7, 1, 2, 3 ]

4

true

Family

Glycine-tRNA ligase, alpha subunit

Gly-tRNA_ligase_asu

4

IPR002312

2,312

Aspartyl/Asparaginyl-tRNA synthetase, class IIb

Asp/Asn-tRNA-synth_IIb

Family

63,648

false

Aspartyl tRNA synthetase is an alpha2 dimer that belongs to class IIb. Structural analysis combined with mutagenesis and enzymology data on the yeast enzyme point to a tRNA binding process that starts by a recognition event between the tRNA anticodon loop and the synthetase anticodon binding module [ ]. Aminoacyl-tRNA ...

[ "GO:0000166", "GO:0004812", "GO:0005524", "GO:0006418" ]

[ "nucleotide binding", "aminoacyl-tRNA ligase activity", "ATP binding", "tRNA aminoacylation for protein translation" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "PRINTS" ]

[ "PR01042" ]

[ "TRNASYNTHASP" ]

[ 63648 ]

1

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "6.1.1", "R-DDI-9856649", "R-HSA-2408522", "R-HSA-379716", "R-HSA-379726", "R-HSA-9856649", "R-MMU-9856649", "R-RNO-9856649" ]

[ "EC:6.1.1", "REACTOME:R-DDI-9856649", "REACTOME:R-HSA-2408522", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-379726", "REACTOME:R-HSA-9856649", "REACTOME:R-MMU-9856649", "REACTOME:R-RNO-9856649" ]

8

[ "1asy", "1asz", "1b8a", "1c0a", "1efw", "1eov", "1eqr", "1g51", "1il2", "1l0w", "1n9w", "1wyd", "1x54", "1x55", "1x56", "2xgt", "2xti", "3i7f", "3kfu", "3m4p", "3m4q", "3nel", "3nem", "3nen", "4ah6", "4j15", "4o2d", "4rmf", "4wj3", "4wj4", "5w25", "5xix"...

53

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006477", "PUB00006538", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873", "PUB00084175" ]

[ "8364025", "8274143", "1852601", "2053131", "10673435", "10873455", "2203971", "10447505", "10704480", "12458790", "9582288" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 2000, 2000, 1990, 1999, 2000, 2002, 1998 ]

11

[]

[ "IPR004522", "IPR004523", "IPR004524" ]

0

3

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 1168, 40746, 20801, 41, 892 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 27, 4, 6, 6, 2, 25, 15, 5, 16, 21, 4, 4, 32 ]

13

true

Family

Aspartyl/Asparaginyl-tRNA synthetase, class IIb

Asp/Asn-tRNA-synth_IIb

3

IPR002313

2,313

Lysine-tRNA ligase, class II

Lys-tRNA-ligase_II

Family

30,349

false

This entry represents lysine-tRNA ligase class II. Lysine-tRNA synthesis is catalysed by two unrelated families of tRNA ligases: class-I or class-II. In eubacteria and eukaryota lysine-tRNA ligases belong to class II, the same family as aspartyl tRNA ligase. The lysine-tRNA ligase class Ic family is present in archaea ...

[ "GO:0004824", "GO:0005524", "GO:0006430" ]

[ "lysine-tRNA ligase activity", "ATP binding", "lysyl-tRNA aminoacylation" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_00252", "TIGR00499" ]

[ "Lys_tRNA_synth_class2", "lysS_bact" ]

[ 29470, 29998 ]

2

[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "6.1.1.6", "GenProp0258", "R-CEL-9856649", "R-HSA-2408522", "R-HSA-379716", "R-HSA-379726", "R-HSA-9856649", "R-MMU-9856649", "R-RNO-9856649", "R-SCE-9856649", "R-SPO-9856649" ]

[ "EC:6.1.1.6", "GP:GenProp0258", "REACTOME:R-CEL-9856649", "REACTOME:R-HSA-2408522", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-379726", "REACTOME:R-HSA-9856649", "REACTOME:R-MMU-9856649", "REACTOME:R-RNO-9856649", "REACTOME:R-SCE-9856649", "REACTOME:R-SPO-9856649" ]

11

[ "1bbu", "1bbw", "1e1o", "1e1t", "1e22", "1e24", "1lyl", "3a74", "3bju", "3e9h", "3e9i", "4dpg", "4ex5", "4h02", "4pg3", "4up7", "4up8", "4up9", "4upa", "4ycu", "4ycv", "4ycw", "5eln", "5elo", "5hgq", "5vl1", "5yzx", "5zh2", "5zh3", "5zh4", "5zh5", "6agt"...

84

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00005800", "PUB00006477", "PUB00006540", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "9353192", "10673435", "10913247", "2203971", "10447505", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 1997, 2000, 2000, 1990, 1999, 2000, 2002 ]

11

[]

[ "IPR034762" ]

0

1

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 170, 23122, 6629, 12, 416 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 7, 2, 3, 3, 2, 1, 7, 1, 8, 2, 2, 2, 17 ]

13

true

Family

Lysine-tRNA ligase, class II

Lys-tRNA-ligase_II

2

IPR002314

2,314

Aminoacyl-tRNA synthetase, class II (G/ P/ S/T)

aa-tRNA-synt_IIb

Domain

137,186

false

Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [ ]. The 20 aminoacyl-tRNA synth...

[ "GO:0000166", "GO:0004812", "GO:0005524", "GO:0006418" ]

[ "nucleotide binding", "aminoacyl-tRNA ligase activity", "ATP binding", "tRNA aminoacylation for protein translation" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "PFAM" ]

[ "PF00587" ]

[ "tRNA-synt_2b" ]

[ 137186 ]

1

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "6.1.1", "R-DME-9856649", "R-HSA-2408522", "R-HSA-2408557", "R-HSA-379716", "R-HSA-379726", "R-HSA-6782315", "R-HSA-9856649", "R-MMU-9856649" ]

[ "EC:6.1.1", "REACTOME:R-DME-9856649", "REACTOME:R-HSA-2408522", "REACTOME:R-HSA-2408557", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-379726", "REACTOME:R-HSA-6782315", "REACTOME:R-HSA-9856649", "REACTOME:R-MMU-9856649" ]

9

[ "1ati", "1b76", "1evk", "1evl", "1fyf", "1ggm", "1h4q", "1h4s", "1h4t", "1hc7", "1kog", "1nj1", "1nj2", "1nj5", "1nj6", "1nj8", "1nyq", "1nyr", "1qf6", "1ser", "1ses", "1set", "1sry", "1wle", "2dq0", "2dq3", "2i4l", "2i4m", "2i4n", "2i4o", "2j3l", "2j3m"...

238

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "10673435", "2203971", "10447505", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 2000, 1990, 1999, 2000, 2002 ]

9

[ "IPR006195" ]

[ "IPR033721", "IPR033728", "IPR033729", "IPR033730", "IPR033731" ]

1

5

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 3749, 95414, 35686, 53, 2284 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 45, 10, 18, 15, 3, 35, 19, 6, 29, 41, 7, 6, 79 ]

13

true

Domain

Aminoacyl-tRNA synthetase, class II (G/ P/ S/T)

aa-tRNA-synt_IIb

2

IPR002315

2,315

Glycyl-tRNA synthetase

tRNA-synt_gly

Family

17,439

false

In eubacteria, glycine-tRNA ligase ( ) is an alpha2/beta2 tetramer composed of 2 different subunits [ , , ]. In some eubacteria, in archaea and eukaryotes, glycine-tRNA ligase is an alpha2 dimer, this family. It belongs to class IIc and is one of the most complex ligases. What is most interesting is the lack of similar...

[ "GO:0000166", "GO:0004820", "GO:0005524", "GO:0006426", "GO:0005737" ]

[ "nucleotide binding", "glycine-tRNA ligase activity", "ATP binding", "glycyl-tRNA aminoacylation", "cytoplasm" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

5

[ "NCBIFAM" ]

[ "TIGR00389" ]

[ "glyS_dimeric" ]

[ 17439 ]

1

[ "EC", "GP", "REACTOME", "REACTOME" ]

[ "6.1.1.14", "GenProp0258", "R-HSA-379716", "R-HSA-379726" ]

[ "EC:6.1.1.14", "GP:GenProp0258", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-379726" ]

4

[ "1ati", "2pme", "2pmf", "2q5h", "2q5i", "2zt5", "2zt6", "2zt7", "2zt8", "2zxf", "4kqe", "4kr2", "4kr3", "4qei", "5e6m", "8sld", "8slf", "8slg", "8slh", "8t5n", "8u2p", "8u2q" ]

22

[ "PUB00000386", "PUB00000723", "PUB00002277", "PUB00002392", "PUB00002880", "PUB00004391", "PUB00005365", "PUB00006333", "PUB00006477", "PUB00006561", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "7665503", "6309809", "7962006", "1852601", "2053131", "7556056", "10673435", "10064708", "2203971", "10447505", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "The glycyl-tRNA synthetase of Chlamydia trachomatis.", "Primary structures of both subunits of Escherichia coli glycyl-tRNA synthetase.", "Human glyc...

[ 1993, 1993, 1995, 1983, 1994, 1991, 1991, 1995, 2000, 1999, 1990, 1999, 2000, 2002 ]

14

[ "IPR027031" ]

[ "IPR022960", "IPR022961" ]

1

2

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 923, 10730, 5510, 15, 261 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 9, 2, 1, 1, 11, 1, 1, 7, 3, 2, 1, 21 ]

12

true

Family

Glycyl-tRNA synthetase

tRNA-synt_gly

1

IPR002316

2,316

Proline-tRNA ligase, class IIa

Pro-tRNA-ligase_IIa

Family

33,563

false

Proline-tRNA ligase (also known as Prolyl-tRNA synthetase) belongs to class IIa aminoacyl-tRNA synthetases. Prolyl-tRNA synthetase ( ) exists in two forms, which are loosely related. The first form is present in the majority of eubacteria species. The second one, present in some eubacteria, is essentially present in ar...

[ "GO:0004827", "GO:0005524", "GO:0006433", "GO:0005737" ]

[ "proline-tRNA ligase activity", "ATP binding", "prolyl-tRNA aminoacylation", "cytoplasm" ]

[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

4

[ "PRINTS" ]

[ "PR01046" ]

[ "TRNASYNTHPRO" ]

[ 33563 ]

1

[ "EC", "REACTOME" ]

[ "6.1.1.15", "R-HSA-379726" ]

[ "EC:6.1.1.15", "REACTOME:R-HSA-379726" ]

2

[ "1h4q", "1h4s", "1h4t", "1hc7", "1nj1", "1nj2", "1nj5", "1nj6", "1nj8", "2i4l", "2i4m", "2i4n", "2i4o", "2j3l", "2j3m", "3ial", "4hvc", "4k86", "4k87", "4k88", "4ncx", "4olf", "4q15", "4twa", "4wi1", "4ydq", "5f9y", "5f9z", "5ifu", "5ucm", "5v58", "5vad"...

102

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006366", "PUB00006477", "PUB00006573", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "9062123", "10673435", "10666604", "2203971", "10447505", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 1997, 2000, 2000, 1990, 1999, 2000, 2002 ]

11

[]

[ "IPR004499", "IPR004500" ]

0

2

0

[ "Archaea", "Bacteria", "Eukaryota", "Megaviricetes", "unclassified sequences" ]

[ 931, 24840, 7263, 8, 521 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 8, 3, 2, 3, 1, 2, 3, 2, 6, 5, 2, 2, 18 ]

13

true

Family

Proline-tRNA ligase, class IIa

Pro-tRNA-ligase_IIa

3

IPR002317

2,317

Serine-tRNA ligase, type1

Ser-tRNA-ligase_type_1

Family

39,217

false

Serine-tRNA ligase ( ) exists as monomer and belongs to the aminoacyl-tRNA synthetase class IIa [ ]. It catalyses the attachment of serine to tRNA (Ser). It is also able to aminoacylate tRNA (Sec) with serine, to form the misacylated tRNA L-seryl-tRNA (Sec), which will be further converted into selenocysteinyl-tRNA (Se...

[ "GO:0000166", "GO:0004828", "GO:0005524", "GO:0006434" ]

[ "nucleotide binding", "serine-tRNA ligase activity", "ATP binding", "seryl-tRNA aminoacylation" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "HAMAP", "PIRSF", "PRINTS", "PANTHER", "NCBIFAM" ]

[ "MF_00176", "PIRSF001529", "PR00981", "PTHR11778", "TIGR00414" ]

[ "Ser_tRNA_synth_type1", "Ser-tRNA-synth_IIa", "TRNASYNTHSER", "", "serS" ]

[ 22300, 34724, 37576, 17377, 35595 ]

5

[ "EC", "GP", "GP", "METACYC", "REACTOME", "REACTOME", "REACTOME" ]

[ "6.1.1.11", "GenProp0258", "GenProp1499", "PWY-6281", "R-HSA-2408557", "R-HSA-379716", "R-HSA-379726" ]

[ "EC:6.1.1.11", "GP:GenProp0258", "GP:GenProp1499", "METACYC:PWY-6281", "REACTOME:R-HSA-2408557", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-379726" ]

7

[ "1ser", "1ses", "1set", "1sry", "1wle", "2dq0", "2dq3", "2zr2", "2zr3", "3err", "3lsq", "3lss", "3qne", "3qo5", "3qo7", "3qo8", "3vbb", "4l87", "4rqe", "4rqf", "6blj", "6gir", "6h9x", "6hdz", "6he1", "6he3", "6hhy", "6hhz", "6hi0", "6ote", "6r1m", "6r1n"...

53

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006326", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873", "PUB00088641", "PUB00088642" ]

[ "8364025", "8274143", "1852601", "2053131", "7540217", "10673435", "2203971", "10447505", "10704480", "12458790", "19734148", "15364939" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 1995, 2000, 1990, 1999, 2000, 2002, 2009, 2004 ]

12

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 795, 26642, 11142, 19, 619 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 13, 3, 5, 5, 1, 11, 7, 2, 12, 8, 2, 2, 45 ]

13

true

Family

Serine-tRNA ligase, type1

Ser-tRNA-ligase_type_1

4

IPR002318

2,318

Alanine-tRNA ligase, class IIc

Ala-tRNA-lgiase_IIc

Family

39,415

false

Alanine-tRNA ligase (also known as alanyl-tRNA synthetase) ( ) is an alpha4 tetramer that belongs to class IIc. Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzyme...

[ "GO:0000166", "GO:0005737" ]

[ "nucleotide binding", "cytoplasm" ]

[ "molecular_function", "cellular_component" ]

2

[ "PRINTS", "NCBIFAM" ]

[ "PR00980", "TIGR00344" ]

[ "TRNASYNTHALA", "alaS" ]

[ 39119, 34525 ]

2

[ "EC", "GP", "PROSITEDOC", "REACTOME", "REACTOME" ]

[ "6.1.1.7", "GenProp0258", "PDOC00363", "R-HSA-379716", "R-HSA-379726" ]

[ "EC:6.1.1.7", "GP:GenProp0258", "PROSITEDOC:PDOC00363", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-379726" ]

5

[ "1riq", "1yfr", "1yfs", "1yft", "1ygb", "2ztg", "2zze", "2zzf", "2zzg", "3htz", "3hxu", "3hxv", "3hxw", "3hxx", "3hxy", "3hxz", "3hy0", "3hy1", "3wqy", "3wqz", "4xem", "4xeo", "5knn", "5v59", "9jc7", "9jdn" ]

26

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "10673435", "2203971", "10447505", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 2000, 1990, 1999, 2000, 2002 ]

9

[]

[ "IPR022429", "IPR023033" ]

0

2

0

[ "Archaea", "Bacteria", "Eukaryota", "Mimiviridae", "unclassified sequences" ]

[ 950, 27747, 10076, 11, 631 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 10, 2, 13, 5, 1, 18, 5, 1, 6, 7, 1, 1, 22 ]

13

true

Family

Alanine-tRNA ligase, class IIc

Ala-tRNA-lgiase_IIc

1

IPR002319

2,319

Phenylalanyl-tRNA synthetase

Phenylalanyl-tRNA_Synthase

Domain

39,989

false

Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [ ]. The 20 aminoacyl-tRNA synth...

[ "GO:0000049", "GO:0004812", "GO:0005524", "GO:0043039" ]

[ "tRNA binding", "aminoacyl-tRNA ligase activity", "ATP binding", "tRNA aminoacylation" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "PFAM" ]

[ "PF01409" ]

[ "tRNA-synt_2d" ]

[ 39989 ]

1

[ "EC", "EC", "REACTOME", "REACTOME" ]

[ "6.1.1", "6.1.1.20", "R-HSA-379716", "R-HSA-379726" ]

[ "EC:6.1.1", "EC:6.1.1.20", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-379726" ]

4

[ "1b70", "1b7y", "1eiy", "1jjc", "1pys", "2akw", "2aly", "2amc", "2du3", "2du4", "2du5", "2du6", "2du7", "2e3c", "2iy5", "2odr", "2q7e", "2q7g", "2q7h", "2rhq", "2rhs", "2zce", "2zim", "2zin", "2zio", "2zni", "2znj", "3cmq", "3dsq", "3hfv", "3hfz", "3l4g"...

117

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006305", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "8199244", "10673435", "2203971", "10447505", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 1993, 2000, 1990, 1999, 2000, 2002 ]

10

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 1285, 27566, 10397, 12, 729 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 7, 4, 2, 2, 1, 8, 11, 2, 9, 12, 2, 2, 19 ]

13

true

Domain

Phenylalanyl-tRNA synthetase

Phenylalanyl-tRNA_Synthase

4

IPR002321

2,321

Cytochrome c, class II

Cyt_c_II

Family

6,629

false

Cytochromes c (cytC) can be defined as electron-transfer proteins having one or several haem c groups, bound to the protein by one or, more generally, two thioether bonds involving sulphydryl groups of cysteine residues. The fifth haem iron ligand is always provided by a histidine residue. CytC possess a wide range of ...

[ "GO:0005506", "GO:0009055", "GO:0020037" ]

[ "iron ion binding", "electron transfer activity", "heme binding" ]

[ "molecular_function", "molecular_function", "molecular_function" ]

3

[ "PFAM", "PROFILE" ]

[ "PF01322", "PS51009" ]

[ "Cytochrom_C_2", "CYTCII" ]

[ 5781, 6565 ]

2

[ "PROSITEDOC" ]

[ "PDOC00169" ]

[ "PROSITEDOC:PDOC00169" ]

1

[ "1a7v", "1bbh", "1cgn", "1cgo", "1cpq", "1cpr", "1e83", "1e84", "1e85", "1e86", "1eky", "1gqa", "1jaf", "1mqv", "1nbb", "1rcp", "1s05", "2bc5", "2ccy", "2j8w", "2j9b", "2qla", "2xl6", "2xl8", "2xld", "2xle", "2xlh", "2xlm", "2xlo", "2xlv", "2xlw", "2xm0"...

131

[ "PUB00000609", "PUB00000610", "PUB00000611", "PUB00003313" ]

[ "1646016", "1646017", "1646027", "8230224" ]

[ "Bacterial 4-alpha-helical bundle cytochromes.", "Sequence variability in bacterial cytochromes c.", "Ligand binding properties of cytochromes c'.", "Atomic structure of a cytochrome c' with an unusual ligand-controlled dimer dissociation at 1.8 A resolution." ]

[ 1991, 1991, 1991, 1993 ]

4

[]

[ "IPR012127" ]

0

1

0

[ "Bacteria", "Eukaryota", "Spodoptera exigua multiple nucleopolyhedrovirus", "unclassified sequences" ]

[ 6441, 99, 1, 88 ]

4

[]

0

true

Family

Cytochrome c, class II

Cyt_c_II

9

IPR002322

2,322

Cytochrome c, class III

Cyt_c_III

Family

1,061

false

null

[ "GO:0009055", "GO:0020037" ]

[ "electron transfer activity", "heme binding" ]

[ "molecular_function", "molecular_function" ]

2

[ "PRINTS" ]

[ "PR00609" ]

[ "CYTOCHROMEC3" ]

[ 1061 ]

1

[]

0

[ "19hc", "1a2i", "1aqe", "1czj", "1duw", "1ehj", "1f22", "1gm4", "1gmb", "1gws", "1gx7", "1h29", "1hh5", "1i77", "1it1", "1j0o", "1j0p", "1kwj", "1l3o", "1lm2", "1mdv", "1new", "1ofw", "1ofy", "1os6", "1qn0", "1qn1", "1up9", "1upd", "1w7o", "1wad", "1wr5"...

74

[ "PUB00000610", "PUB00003572", "PUB00053356" ]

[ "1646017", "7830606", "9293186" ]

[ "Sequence variability in bacterial cytochromes c.", "Tetraheme cytochromes.", "Biogenesis of respiratory cytochromes in bacteria." ]

[ 1991, 1994, 1997 ]

3

[]

[ "IPR054813" ]

0

1

0

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 1043, 3, 15 ]

3

[]

0

true

Family

Cytochrome c, class III

Cyt_c_III

2

IPR002323

2,323

Cytochrome c, class IE

Cyt_CIE

Family

6,075

false

null

[ "GO:0005506", "GO:0009055", "GO:0020037" ]

[ "iron ion binding", "electron transfer activity", "heme binding" ]

[ "molecular_function", "molecular_function", "molecular_function" ]

3

[ "PRINTS" ]

[ "PR00607" ]

[ "CYTCHROMECIE" ]

[ 6075 ]

1

[]

0

[ "1cc5", "1gks", "1kx2", "1kx7", "2zon", "4j20", "5b6q", "6k7c", "8hn3", "8smr", "8snh" ]

11

[ "PUB00000610", "PUB00003208" ]

[ "1646017", "2993632" ]

[ "Sequence variability in bacterial cytochromes c.", "Crystal structure of Azotobacter cytochrome c5 at 2.5 A resolution." ]

[ 1991, 1985 ]

2

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 5943, 17, 115 ]

3

[]

0

true

Family

Cytochrome c, class IE

Cyt_CIE

2

IPR002324

2,324

Cytochrome c, class ID

Cyt_c_ID

Family

6,152

false

null

[ "GO:0005506", "GO:0009055", "GO:0020037" ]

[ "iron ion binding", "electron transfer activity", "heme binding" ]

[ "molecular_function", "molecular_function", "molecular_function" ]

3

[ "PRINTS" ]

[ "PR00606" ]

[ "CYTCHROMECID" ]

[ 6152 ]

1

[]

0

[ "1a56", "1a8c", "1ayg", "1cch", "1cor", "1dvv", "1fi3", "1ynr", "2ai5", "2d0s", "2exv", "2i8f", "2pac", "2zxy", "351c", "3vym", "3x15", "3x39", "3zow", "3zox", "3zoy", "451c", "4jcg", "4zid", "5aur", "5aus", "5xec", "5xed", "6kq1" ]

29

[ "PUB00000610", "PUB00004589" ]

[ "1646017", "96440" ]

[ "Sequence variability in bacterial cytochromes c.", "Pseudomonas cytochrome c551 at 2.0 A resolution: enlargement of the cytochrome c family." ]

[ 1991, 1978 ]

2

[]

0

null

[ "Bacteria", "Eukaryota", "metagenomes" ]

[ 6048, 6, 98 ]

3

[]

0

true

Family

Cytochrome c, class ID

Cyt_c_ID

3

IPR002325

2,325

Cytochrome f

Cyt_f

Family

15,515

false

The cytochrome b6f integral membrane protein complex transfers electrons between the two reaction centre complexes of oxygenic photosynthetic membranes, and participates in formation of the transmembrane electrochemical proton gradient by also transferring protons from the stromal to the internal lumen compartment. The...

[ "GO:0005506", "GO:0009055", "GO:0020037", "GO:0015979", "GO:0042651" ]

[ "iron ion binding", "electron transfer activity", "heme binding", "photosynthesis", "thylakoid membrane" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

5

[ "HAMAP", "PFAM", "PRINTS", "PROFILE" ]

[ "MF_00610", "PF01333", "PR00610", "PS51010" ]

[ "Cytb6_f_cytF", "Apocytochr_F_C", "CYTOCHROMEF", "CYTF" ]

[ 14187, 14958, 15282, 15403 ]

4

[ "GP", "PROSITEDOC" ]

[ "GenProp1353", "PDOC00169" ]

[ "GP:GenProp1353", "PROSITEDOC:PDOC00169" ]

2

[ "1cfm", "1ci3", "1ctm", "1e2v", "1e2w", "1e2z", "1ewh", "1hcz", "1q90", "1tkw", "1tu2", "1vf5", "2d2c", "2e74", "2e75", "2e76", "2jxm", "2pcf", "2zt9", "4h0l", "4h13", "4h44", "4i7z", "4ogq", "4pv1", "6rqf", "7qrm", "7r0w", "7zxy", "7zyv", "9es7", "9es8"...

33

[ "PUB00002369", "PUB00005442" ]

[ "8027021", "7631417" ]

[ "Structural aspects of the cytochrome b6f complex; structure of the lumen-side domain of cytochrome f.", "Cytochrome f revealed." ]

[ 1994, 1995 ]

2

[]

0

null

[ "Bacteria", "Eukaryota", "marine sediment metagenome" ]

[ 394, 15120, 1 ]

3

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 7, 10, 16 ]

3

true

Family

Cytochrome f

Cyt_f

4

IPR002327

2,327

Cytochrome c, class IA/ IB

Cyt_c_1A/1B

Family

17,252

false

Cytochromes c (cytC) can be defined as electron-transfer proteins having one or several haem c groups, bound to the protein by one or, more generally, two thioether bonds involving sulfhydryl groups of cysteine residues. The fifth haem iron ligand is always provided by a histidine residue. CytC possess a wide range of ...

[ "GO:0009055", "GO:0020037" ]

[ "electron transfer activity", "heme binding" ]

[ "molecular_function", "molecular_function" ]

2

[ "PRINTS", "PANTHER" ]

[ "PR00604", "PTHR11961" ]

[ "CYTCHRMECIAB", "" ]

[ 16316, 16488 ]

2

[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...

[ "GenProp2021", "R-BTA-111457", "R-BTA-111458", "R-BTA-111459", "R-BTA-2151201", "R-BTA-3299685", "R-BTA-5620971", "R-BTA-5628897", "R-BTA-611105", "R-BTA-9627069", "R-BTA-9707564", "R-CEL-111457", "R-CEL-3299685", "R-CEL-5620971", "R-CEL-611105", "R-CFA-111457", "R-CFA-111458", "R-...

[ "GP:GenProp2021", "REACTOME:R-BTA-111457", "REACTOME:R-BTA-111458", "REACTOME:R-BTA-111459", "REACTOME:R-BTA-2151201", "REACTOME:R-BTA-3299685", "REACTOME:R-BTA-5620971", "REACTOME:R-BTA-5628897", "REACTOME:R-BTA-611105", "REACTOME:R-BTA-9627069", "REACTOME:R-BTA-9707564", "REACTOME:R-CEL-1114...

118

[ "155c", "1akk", "1c2n", "1c2r", "1c7m", "1ccr", "1chh", "1chi", "1chj", "1cie", "1cif", "1cig", "1cih", "1co6", "1cot", "1crc", "1crg", "1crh", "1cri", "1crj", "1cry", "1csu", "1csv", "1csw", "1csx", "1cty", "1ctz", "1cxa", "1cxc", "1cyc", "1fhb", "1fi7"...

207

[ "PUB00000610", "PUB00095221" ]

[ "1646017", "24758379" ]

[ "Sequence variability in bacterial cytochromes c.", "Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers." ]

[ 1991, 2014 ]

2

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 10267, 6878, 107 ]

3

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 6, 2, 1, 4, 3, 5, 1, 5, 5, 2, 1, 22 ]

12

true

Family

Cytochrome c, class IA/ IB

Cyt_c_1A/1B

7

IPR002328

2,328

Alcohol dehydrogenase, zinc-type, conserved site

ADH_Zn_CS

Conserved_site

183,405

false

null

[ "GO:0008270", "GO:0016491" ]

[ "zinc ion binding", "oxidoreductase activity" ]

[ "molecular_function", "molecular_function" ]

2

[ "PROSITE" ]

[ "PS00059" ]

[ "ADH_ZINC" ]

[ 183405 ]

1

[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...

[ "1.1.1", "PDOC00058", "R-BTA-5652227", "R-BTA-5661270", "R-BTA-71384", "R-CEL-2161541", "R-CEL-5365859", "R-CEL-71384", "R-DDI-2161541", "R-DDI-5365859", "R-DDI-71384", "R-DME-2161541", "R-DME-5365859", "R-DME-71384", "R-GGA-5652227", "R-GGA-5661270", "R-HSA-2161541", "R-HSA-536585...

[ "EC:1.1.1", "PROSITEDOC:PDOC00058", "REACTOME:R-BTA-5652227", "REACTOME:R-BTA-5661270", "REACTOME:R-BTA-71384", "REACTOME:R-CEL-2161541", "REACTOME:R-CEL-5365859", "REACTOME:R-CEL-71384", "REACTOME:R-DDI-2161541", "REACTOME:R-DDI-5365859", "REACTOME:R-DDI-71384", "REACTOME:R-DME-2161541", "R...

41

[ "1a71", "1a72", "1adb", "1adc", "1adf", "1adg", "1agn", "1axe", "1axg", "1bto", "1bxz", "1cdo", "1d1s", "1d1t", "1deh", "1e3e", "1e3i", "1e3j", "1e3l", "1ee2", "1f8f", "1h2b", "1hdx", "1hdy", "1hdz", "1het", "1heu", "1hf3", "1hld", "1hso", "1hsz", "1ht0"...

286

[ "PUB00001354", "PUB00001658", "PUB00003420" ]

[ "3622514", "8504864", "1593644" ]

[ "Characteristics of alcohol/polyol dehydrogenases. The zinc-containing long-chain alcohol dehydrogenases.", "Dual relationships of xylitol and alcohol dehydrogenases in families of two protein types.", "Progressive sequence alignment and molecular evolution of the Zn-containing alcohol dehydrogenase family." ]

[ 1987, 1993, 1992 ]

3

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 2599, 121499, 57744, 27, 1536 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 73, 6, 13, 4, 12, 33, 17, 15, 56, 31, 12, 5, 90 ]

13

true

Conserved_site

Alcohol dehydrogenase, zinc-type, conserved site

ADH_Zn_CS

8

IPR002330

2,330

Lipoprotein lipase

Lipo_Lipase

Family

2,800

false

Lipoprotein lipase (LPL) is a key enzyme of lipid metabolism that hydrolyses triglycerides, providing free fatty acids for cells and affecting the maturation of circulating lipoproteins [ ]. The enzyme is thought to play a role in the development of obesity and atherosclerosis [ ]. Human LPL contains 448 amino acids; s...

[ "GO:0004465", "GO:0006629" ]

[ "lipoprotein lipase activity", "lipid metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PRINTS", "NCBIFAM" ]

[ "PR00822", "TIGR03230" ]

[ "LIPOLIPASE", "lipo_lipase" ]

[ 2797, 1102 ]

2

[ "EC", "EC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "3.1.1.32", "3.1.1.34", "PWY-6803", "PWY-8051", "R-BTA-8963889", "R-BTA-8963901", "R-BTA-975634", "R-GGA-8963889", "R-HSA-381340", "R-HSA-8963889", "R-HSA-8963901", "R-HSA-8964058", "R-HSA-975634", "R-HSA-9841922", "R-MMU-8963889", "R-MMU-8963901", "R-MMU-8964058", "R-MMU-975634", ...

[ "EC:3.1.1.32", "EC:3.1.1.34", "METACYC:PWY-6803", "METACYC:PWY-8051", "REACTOME:R-BTA-8963889", "REACTOME:R-BTA-8963901", "REACTOME:R-BTA-975634", "REACTOME:R-GGA-8963889", "REACTOME:R-HSA-381340", "REACTOME:R-HSA-8963889", "REACTOME:R-HSA-8963901", "REACTOME:R-HSA-8964058", "REACTOME:R-HSA-...

22

[ "6e7k", "6oau", "6oaz", "6ob0", "6u7m", "8erl", "9nrn" ]

7

[ "PUB00002888", "PUB00003189", "PUB00005099" ]

[ "8308035", "1479292", "3823907" ]

[ "Lipoprotein lipase. Molecular model based on the pancreatic lipase x-ray structure: consequences for heparin binding and catalysis.", "Molecular basis of familial chylomicronemia: mutations in the lipoprotein lipase and apolipoprotein C-II genes.", "Human lipoprotein lipase complementary DNA sequence." ]

[ 1994, 1992, 1987 ]

3

[ "IPR016272" ]

[]

1

0

1

[ "Vertebrata" ]

[ 2800 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 7, 17, 25, 6 ]

4

true

Family

Lipoprotein lipase

Lipo_Lipase

1

IPR002331

2,331

Pancreatic lipase

Lipase_panc

Family

3,039

false

Triglyceride lipases ( ) are lipolytic enzymes that hydrolyse ester linkages of triglycerides [ ]. Lipases are widely distributed in animals, plants and prokaryotes. At least three tissue-specific isozymes exist in higher vertebrates: pancreatic, hepatic and gastric/lingual. These lipases are closely related to each ot...

[ "GO:0004806", "GO:0006629" ]

[ "triacylglycerol lipase activity", "lipid metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PRINTS" ]

[ "PR00823" ]

[ "PANCLIPASE" ]

[ 3039 ]

1

[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "3.1.1.3", "PWY-6857", "R-BTA-192456", "R-HSA-192456", "R-HSA-975634", "R-HSA-9925561", "R-MMU-192456", "R-MMU-975634", "R-RNO-192456", "R-RNO-975634" ]

[ "EC:3.1.1.3", "METACYC:PWY-6857", "REACTOME:R-BTA-192456", "REACTOME:R-HSA-192456", "REACTOME:R-HSA-975634", "REACTOME:R-HSA-9925561", "REACTOME:R-MMU-192456", "REACTOME:R-MMU-975634", "REACTOME:R-RNO-192456", "REACTOME:R-RNO-975634" ]

10

[ "1bu8", "1eth", "1gpl", "1hpl", "1lpa", "1lpb", "1n8s", "1rp1", "1w52", "2oxe", "2ppl", "2pvs" ]

12

[ "PUB00000684", "PUB00001369", "PUB00002523", "PUB00004055" ]

[ "3147715", "2917565", "2479644", "2106079" ]

[ "Minireview on pancreatic lipase and colipase.", "Structural features of lipoprotein lipase. Lipase family relationships, binding interactions, non-equivalence of lipase cofactors, vitellogenin similarities and functional subdivision of lipoprotein lipase.", "Cloning and characterization of human pancreatic lip...

[ 1988, 1989, 1989, 1990 ]

4

[ "IPR016272" ]

[]

1

0

1

[ "Eumetazoa" ]

[ 3039 ]

1

[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 14, 6, 14 ]

3

true

Family

Pancreatic lipase

Lipase_panc

9

IPR002332

2,332

Nitrogen regulatory protein P-II, urydylation site

N-reg_PII_urydylation_site

PTM

19,774

false

The P-II protein (gene glnB) is a bacterial protein important for the control of glutamine synthetase [ , , ]. In nitrogen-limiting conditions, when the ratio of glutamine to 2-ketoglutarate decreases, P-II is uridylylated on a tyrosine residue to form P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase...

[ "GO:0030234", "GO:0006808" ]

[ "enzyme regulator activity", "regulation of nitrogen utilization" ]

[ "molecular_function", "biological_process" ]

2

[ "PROSITE" ]

[ "PS00496" ]

[ "PII_GLNB_UMP" ]

[ 19774 ]

1

[ "PROSITEDOC" ]

[ "PDOC00439" ]

[ "PROSITEDOC:PDOC00439" ]

1

[ "1gnk", "1hwu", "1pil", "1qy7", "1ul3", "2gnk", "2gw8", "2jj4", "2nuu", "2pii", "2v5h", "2xbp", "2xg8", "2xul", "2xzw", "3bzq", "3lf0", "3mhy", "3n5b", "3o5t", "4aff", "4c3k", "4c3l", "4c3m", "4cny", "4cnz", "4co0", "4co1", "4co2", "4co3", "4co4", "4co5"...

36

[ "PUB00000687", "PUB00001837", "PUB00002236", "PUB00003730", "PUB00005249" ]

[ "2574599", "7904973", "8282685", "2907369", "7866749" ]

[ "Regulation of transcription of the glnALG operon of Escherichia coli by protein phosphorylation.", "Cloning and organization of the abc and mdl genes of Escherichia coli: relationship to eukaryotic multidrug resistance.", "The nitrogen-regulated Bacillus subtilis nrgAB operon encodes a membrane protein and a p...

[ 1989, 1993, 1994, 1988, 1994 ]

5

[]

0

null

[ "Bacteria", "Eukaryota", "Methanoregulaceae", "unclassified sequences" ]

[ 19315, 41, 2, 416 ]

4

[ "Escherichia coli (strain K12)" ]

[ 2 ]

1

true

PTM

Nitrogen regulatory protein P-II, urydylation site

N-reg_PII_urydylation_site

8

IPR002333

2,333

Hepatic lipase

Lipase_hep

Family

1,131

false

Triglyceride lipases ( ) are lipolytic enzymes that hydrolyse ester linkages of triglycerides [ ]. Lipases are widely distributed in animals, plants and prokaryotes. At least three tissue-specific isozymes exist in higher vertebrates: pancreatic, hepatic and gastric/lingual. These lipases are closely related to each ot...

[ "GO:0004806", "GO:0006629" ]

[ "triacylglycerol lipase activity", "lipid metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PRINTS" ]

[ "PR00824" ]

[ "HEPLIPASE" ]

[ 1131 ]

1

[ "EC", "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "3.1.1.3", "3.1.1.32", "3.1.1.5", "PWY-6803", "PWY-6857", "PWY-7409", "PWY-8051", "R-BTA-8963889", "R-BTA-8964026", "R-HSA-8963889", "R-HSA-8964026", "R-MMU-8963889", "R-MMU-8964026", "R-RNO-8963889", "R-RNO-8964026" ]

[ "EC:3.1.1.3", "EC:3.1.1.32", "EC:3.1.1.5", "METACYC:PWY-6803", "METACYC:PWY-6857", "METACYC:PWY-7409", "METACYC:PWY-8051", "REACTOME:R-BTA-8963889", "REACTOME:R-BTA-8964026", "REACTOME:R-HSA-8963889", "REACTOME:R-HSA-8964026", "REACTOME:R-MMU-8963889", "REACTOME:R-MMU-8964026", "REACTOME:R...

15

[]

0

[ "PUB00000314", "PUB00000684", "PUB00001369", "PUB00002005", "PUB00005099" ]

[ "2605236", "3147715", "2917565", "1301939", "3823907" ]

[ "Structure of the human hepatic triglyceride lipase gene.", "Minireview on pancreatic lipase and colipase.", "Structural features of lipoprotein lipase. Lipase family relationships, binding interactions, non-equivalence of lipase cofactors, vitellogenin similarities and functional subdivision of lipoprotein lip...

[ 1989, 1988, 1989, 1992, 1987 ]

5

[ "IPR016272" ]

[]

1

0

1

[ "Vertebrata" ]

[ 1131 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 1, 6, 3, 5 ]

4

true

Family

Hepatic lipase

Lipase_hep

5

IPR002334

2,334

Vespid venom allergen phospholipase A1

Allerg_PlipaseA1

Family

683

false

The two principal allergenic proteins in vespid venoms are antigen 5s and phospholipases. The complete amino acid sequences of the venom phospholipase A1 from the yellow jacket, Vespula maculifrons, and the more acidic isoenzyme from the white faced hornet, Dolichovespula maculata, have been determined [ , ]. The prote...

[ "GO:0016298", "GO:0006629" ]

[ "lipase activity", "lipid metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PRINTS" ]

[ "PR00825" ]

[ "DOLALLERGEN" ]

[ 683 ]

1

[ "EC", "METACYC", "METACYC" ]

[ "3.1.1.32", "PWY-6803", "PWY-8051" ]

[ "EC:3.1.1.32", "METACYC:PWY-6803", "METACYC:PWY-8051" ]

3

[ "4qnn" ]

1

[ "PUB00001653", "PUB00002040", "PUB00071782", "PUB00071785" ]

[ "8458431", "8199462", "23159790", "15753912" ]

[ "Sequence similarity of a hornet (D. maculata) venom allergen phospholipase A1 with mammalian lipases.", "Allergens in hymenoptera venom. XXVI: The complete amino acid sequences of two vespid venom phospholipases.", "Purification and structural characterisation of phospholipase A1 (Vespapase, Ves a 1) from Thai...

[ 1993, 1994, 2013, 2005 ]

4

[ "IPR000734" ]

[]

1

0

1

[ "Eumetazoa" ]

[ 683 ]

1

[ "Drosophila melanogaster" ]

[ 7 ]

1

true

Family

Vespid venom allergen phospholipase A1

Allerg_PlipaseA1

6

IPR002335

2,335

Myoglobin

Family

1,473

false

Globins are haem-containing proteins involved in binding and/or transporting oxygen. They belong to a very large and well studied family that is widely distributed in many organisms [ ]. Globins have evolved from a common ancestor and can be divided into three groups: single-domain globins, and two types of chimeric gl...

[ "GO:0019825", "GO:0020037", "GO:0015671" ]

[ "oxygen binding", "heme binding", "oxygen transport" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "PRINTS", "PANTHER" ]

[ "PR00613", "PTHR47132" ]

[ "MYOGLOBIN", "" ]

[ 1428, 1256 ]

2

[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "1.11.1.-", "PWY-5292", "R-BTA-8981607", "R-DRE-8981607", "R-GGA-8981607", "R-HSA-8981607", "R-MMU-8981607", "R-RNO-8981607", "R-SSC-8981607" ]

[ "EC:1.11.1.-", "METACYC:PWY-5292", "REACTOME:R-BTA-8981607", "REACTOME:R-DRE-8981607", "REACTOME:R-GGA-8981607", "REACTOME:R-HSA-8981607", "REACTOME:R-MMU-8981607", "REACTOME:R-RNO-8981607", "REACTOME:R-SSC-8981607" ]

9

[ "101m", "102m", "103m", "104m", "105m", "106m", "107m", "108m", "109m", "110m", "111m", "112m", "1a6g", "1a6k", "1a6m", "1a6n", "1abs", "1ajg", "1ajh", "1azi", "1bje", "1bvc", "1bvd", "1bz6", "1bzp", "1bzr", "1ch1", "1ch2", "1ch3", "1ch5", "1ch7", "1ch9"...

542

[ "PUB00016016", "PUB00029465", "PUB00035865", "PUB00035866", "PUB00035867", "PUB00035868", "PUB00035869", "PUB00035870", "PUB00035871", "PUB00035872", "PUB00035873", "PUB00035877", "PUB00035895", "PUB00035896", "PUB00035897", "PUB00055462", "PUB00055463", "PUB00153677" ]

[ "15096613", "12962627", "16600051", "17540514", "11092893", "11481493", "15598488", "16888280", "15598493", "15339940", "15804833", "17084861", "15528401", "9804424", "17495223", "17540516", "17701548", "21495624" ]

[ "Ancestral hemoglobins in Archaea.", "Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity.", "A phylogenomic profile of globins.", "A model of globin evolution.", "Flavohemoglobin, a globin with a peroxidase-like catalytic site.", "Globin-coupled sensors: a class of he...

[ 2004, 2003, 2006, 2007, 2001, 2001, 2005, 2006, 2005, 2004, 2004, 2007, 2004, 1998, 2007, 2007, 2007, 2011 ]

18

[]

0

null

[ "Bilateria" ]

[ 1473 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 2, 12, 4, 2 ]

4

true

Family

Myoglobin

2

IPR002336

2,336

Erythrocruorin

Family

696

false

Globins are haem-containing proteins involved in binding and/or transporting oxygen. They belong to a very large and well studied family that is widely distributed in many organisms [ ]. Globins have evolved from a common ancestor and can be divided into three groups: single-domain globins, and two types of chimeric gl...

[ "GO:0020037", "GO:0015671", "GO:0005576", "GO:0005833" ]

[ "heme binding", "oxygen transport", "extracellular region", "hemoglobin complex" ]

[ "molecular_function", "biological_process", "cellular_component", "cellular_component" ]

4

[ "PRINTS" ]

[ "PR00611" ]

[ "ERYTHCRUORIN" ]

[ 696 ]

1

[]

0

[ "1b0b", "1dm1", "1ebt", "1eca", "1ecd", "1ecn", "1eco", "1flp", "1hlb", "1mba", "1moh", "1x46", "1x9f", "2d2m", "2d2n", "2fal", "2fam", "2gtl", "2zfo", "2zs0", "2zs1", "3mba", "3wct", "3wcu", "3wcv", "3wcw", "4mba", "4u8u", "4v93", "5m3l", "5mba", "7e96"...

40

[ "PUB00016016", "PUB00029465", "PUB00032355", "PUB00035865", "PUB00035866", "PUB00035867", "PUB00035868", "PUB00035869", "PUB00035870", "PUB00035871", "PUB00035872", "PUB00035873", "PUB00035877", "PUB00035894", "PUB00055462", "PUB00055463", "PUB00153677" ]

[ "15096613", "12962627", "15504406", "16600051", "17540514", "11092893", "11481493", "15598488", "16888280", "15598493", "15339940", "15804833", "17084861", "10860978", "17540516", "17701548", "21495624" ]

[ "Ancestral hemoglobins in Archaea.", "Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity.", "Crystal structure of the hemoglobin dodecamer from Lumbricus erythrocruorin: allosteric core of giant annelid respiratory complexes.", "A phylogenomic profile of globins.", "A m...

[ 2004, 2003, 2004, 2006, 2007, 2001, 2001, 2005, 2006, 2005, 2004, 2004, 2007, 2000, 2007, 2007, 2011 ]

17

[]

[ "IPR011367" ]

0

1

0

[ "Bacteria", "Opisthokonta" ]

[ 8, 688 ]

2

[]

0

true

Family

Erythrocruorin

4

IPR002337

2,337

Hemoglobin, beta-type

Hemoglobin_b

Family

5,459

false

In vertebrates, hemoglobins (Hb) function to transport oxygen in blood plasma. Hb binds oxygen in the reduced [Fe(II)] state. Hb is composed of four globins in a tetrahedral arrangement, typically two alpha and two beta globins, where each monomer binds a heme group. The alpha and beta subunits are highly similar in se...

[ "GO:0020037", "GO:0015671", "GO:0005833" ]

[ "heme binding", "oxygen transport", "hemoglobin complex" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PRINTS", "CDD" ]

[ "PR00814", "cd08925" ]

[ "BETAHAEM", "Hb-beta-like" ]

[ 5425, 4828 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-BTA-1237044", "R-BTA-1247673", "R-BTA-2168880", "R-BTA-6798695", "R-BTA-9707564", "R-BTA-9707616", "R-DRE-1237044", "R-DRE-1247673", "R-DRE-2168880", "R-DRE-6798695", "R-DRE-9707564", "R-DRE-9707616", "R-GGA-1237044", "R-GGA-1247673", "R-GGA-2168880", "R-GGA-6798695", "R-GGA-97075...

[ "REACTOME:R-BTA-1237044", "REACTOME:R-BTA-1247673", "REACTOME:R-BTA-2168880", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-9707564", "REACTOME:R-BTA-9707616", "REACTOME:R-DRE-1237044", "REACTOME:R-DRE-1247673", "REACTOME:R-DRE-2168880", "REACTOME:R-DRE-6798695", "REACTOME:R-DRE-9707564", "REACTOM...

40

[ "1a00", "1a01", "1a0u", "1a0z", "1a3n", "1a3o", "1a4f", "1a9w", "1abw", "1aby", "1aj9", "1b86", "1bab", "1bbb", "1bij", "1buw", "1bz0", "1bz1", "1bzz", "1c40", "1c7b", "1c7c", "1c7d", "1cbl", "1cbm", "1cg5", "1cg8", "1ch4", "1cls", "1cmy", "1coh", "1dke"...

496

[ "PUB00000422", "PUB00002385", "PUB00022057", "PUB00035882", "PUB00099929", "PUB00099931" ]

[ "7599114", "6157691", "12093902", "1445857", "17656582", "23209182" ]

[ "The D-helix in myoglobin and in the beta subunit of hemoglobin is required for the retention of heme.", "Complete amino acid sequences of the major early embryonic alpha-like globins of the chicken.", "The crystal structure of a tetrameric hemoglobin in a partial hemichrome state.", "Cooperative oxygen bindi...

[ 1995, 1980, 2002, 1992, 2007, 2012 ]

6

[]

0

null

[ "Bacteria", "Eukaryota" ]

[ 4, 5455 ]

2

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 8, 71, 37, 33 ]

4

true

Family

Hemoglobin, beta-type

Hemoglobin_b

9

IPR002338

2,338

Hemoglobin, alpha-type

Hemoglobin_a-typ

Family

5,642

false

In vertebrates, hemoglobins (Hb) function to transport oxygen in blood plasma. Hb binds oxygen in the reduced [Fe(II)] state. Hb is composed of four globins in a tetrahedral arrangement, typically two alpha and two beta globins, where each monomer binds a heme group. The alpha and beta subunits are highly similar in se...

[ "GO:0020037", "GO:0015671", "GO:0005833" ]

[ "heme binding", "oxygen transport", "hemoglobin complex" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PRINTS", "CDD" ]

[ "PR00612", "cd08927" ]

[ "ALPHAHAEM", "Hb-alpha-like" ]

[ 5598, 5105 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-BTA-1237044", "R-BTA-1247673", "R-BTA-2168880", "R-BTA-9707564", "R-BTA-9707616", "R-GGA-1237044", "R-GGA-1247673", "R-GGA-2168880", "R-GGA-9707564", "R-GGA-9707616", "R-HSA-1237044", "R-HSA-1247673", "R-HSA-2168880", "R-HSA-9707564", "R-HSA-9707616", "R-HSA-9927020", "R-MMU-12370...

[ "REACTOME:R-BTA-1237044", "REACTOME:R-BTA-1247673", "REACTOME:R-BTA-2168880", "REACTOME:R-BTA-9707564", "REACTOME:R-BTA-9707616", "REACTOME:R-GGA-1237044", "REACTOME:R-GGA-1247673", "REACTOME:R-GGA-2168880", "REACTOME:R-GGA-9707564", "REACTOME:R-GGA-9707616", "REACTOME:R-HSA-1237044", "REACTOM...

31

[ "1a00", "1a01", "1a0u", "1a0z", "1a3n", "1a3o", "1a4f", "1a9w", "1abw", "1aby", "1aj9", "1b86", "1bab", "1bbb", "1bij", "1buw", "1bz0", "1bz1", "1bzz", "1c40", "1c7b", "1c7c", "1c7d", "1cg5", "1cg8", "1cls", "1cmy", "1coh", "1dke", "1dxt", "1dxu", "1dxv"...

497

[ "PUB00000422", "PUB00002385", "PUB00022057", "PUB00035882", "PUB00099929", "PUB00099931" ]

[ "7599114", "6157691", "12093902", "1445857", "17656582", "23209182" ]

[ "The D-helix in myoglobin and in the beta subunit of hemoglobin is required for the retention of heme.", "Complete amino acid sequences of the major early embryonic alpha-like globins of the chicken.", "The crystal structure of a tetrameric hemoglobin in a partial hemichrome state.", "Cooperative oxygen bindi...

[ 1995, 1980, 2002, 1992, 2007, 2012 ]

6

[]

[ "IPR002339", "IPR002340" ]

0

2

0

[ "Bacteria", "Bilateria" ]

[ 2, 5640 ]

2

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 25, 36, 17, 16 ]

4

true

Family

Hemoglobin, alpha-type

Hemoglobin_a-typ

5

IPR002340

2,340

Hemoglobin, zeta

Hemoglobin_zeta

Family

282

false

This entry represents the zeta-hemoglobin subunit, which is expressed exclusively in the primitive erythroblasts of the embryonic yolk sac and is selectively silenced during the transition from primitive to definitive erythropoiesis [ , , ]. In vertebrates, hemoglobins (Hb) function to transport oxygen in blood plasma....

[ "GO:0005506", "GO:0019825", "GO:0020037", "GO:0015671", "GO:0005833" ]

[ "iron ion binding", "oxygen binding", "heme binding", "oxygen transport", "hemoglobin complex" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

5

[ "PRINTS" ]

[ "PR00816" ]

[ "ZETAHAEM" ]

[ 282 ]

1

[]

0

[ "1jeb", "3w4u" ]

2

[ "PUB00000422", "PUB00002385", "PUB00022057", "PUB00035882", "PUB00035884", "PUB00035885", "PUB00099929", "PUB00099931" ]

[ "7599114", "6157691", "12093902", "1445857", "9668527", "9528789", "17656582", "23209182" ]

[ "The D-helix in myoglobin and in the beta subunit of hemoglobin is required for the retention of heme.", "Complete amino acid sequences of the major early embryonic alpha-like globins of the chicken.", "The crystal structure of a tetrameric hemoglobin in a partial hemichrome state.", "Cooperative oxygen bindi...

[ 1995, 1980, 2002, 1992, 1998, 1998, 2007, 2012 ]

8

[ "IPR002338" ]

[]

1

0

1

[ "Euteleostomi" ]

[ 282 ]

1

[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 3, 2, 2 ]

3

true

Family

Hemoglobin, zeta

Hemoglobin_zeta

8

IPR002343

2,343

Paraneoplastic encephalomyelitis antigen

Hud_Sxl_RNA

Family

20,453

false

Many eukaryotic proteins that are either known or thought to bind single-stranded RNA contain one or more copies of a putative RNA-binding domain of about 90 amino acids [ , ]. This region has been found in, for example, heterogeneous nuclear ribonucleoproteins, small nuclear ribonucleoproteins, pre-RNA and mRNA associ...

[ "GO:0003723", "GO:1990904" ]

[ "RNA binding", "ribonucleoprotein complex" ]

[ "molecular_function", "cellular_component" ]

2

[ "PRINTS" ]

[ "PR00961" ]

[ "HUDSXLRNA" ]

[ 20453 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-DME-450520", "R-HSA-450520", "R-MMU-450520", "R-RNO-450520", "R-XTR-450520" ]

[ "REACTOME:R-DME-450520", "REACTOME:R-HSA-450520", "REACTOME:R-MMU-450520", "REACTOME:R-RNO-450520", "REACTOME:R-XTR-450520" ]

5

[ "1b7f", "1d8z", "1d9a", "1fnx", "1fxl", "1g2e", "1sxl", "1x5o", "2dhs", "2sxl", "3hi9", "3nmr", "3nna", "3nnc", "3nnh", "3sxl", "4ed5", "4egl", "4fxv", "4lmz", "4qqb", "5szw", "6m75", "7c36", "9urh" ]

25

[ "PUB00000396", "PUB00001891", "PUB00005341" ]

[ "7524663", "2470643", "3072706" ]

[ "Resonance assignments and solution structure of the second RNA-binding domain of sex-lethal determined by multidimensional heteronuclear magnetic resonance.", "RNA-binding proteins as developmental regulators.", "Heterogeneous nuclear ribonucleoprotein particles and the pathway of mRNA formation." ]

[ 1994, 1989, 1988 ]

3

[]

[ "IPR006546", "IPR006548" ]

0

2

0

[ "Bacteria", "Eukaryota", "ecological metagenomes" ]

[ 26, 20424, 3 ]

3

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]

[ 10, 1, 169, 26, 45, 47, 10, 64, 24 ]

9

true

Family

Paraneoplastic encephalomyelitis antigen

Hud_Sxl_RNA

3

IPR002344

2,344

Lupus La protein

Lupus_La

Family

10,389

false

The La protein is a 47kDa polypeptide that often acts as an autoantigen in systemic lupus erythematosus and Sjogren's syndrome patients [ ]. It occurs in both the nucleus and the cytoplasm, where it takes on different roles [ ]. In the nucleus, La facilitates the production of tRNAs, acting as a RNA polymerase III (RNA...

[ "GO:0003723", "GO:0006396", "GO:0005634", "GO:1990904" ]

[ "RNA binding", "RNA processing", "nucleus", "ribonucleoprotein complex" ]

[ "molecular_function", "biological_process", "cellular_component", "cellular_component" ]

4

[ "PRINTS" ]

[ "PR00302" ]

[ "LUPUSLA" ]

[ 10389 ]

1

[ "REACTOME", "REACTOME" ]

[ "R-HSA-73980", "R-HSA-749476" ]

[ "REACTOME:R-HSA-73980", "REACTOME:R-HSA-749476" ]

2

[ "1s29", "1s79", "1s7a", "1yty", "1zh5", "2m5w", "2mtf", "2vod", "2von", "2voo", "2vop", "4wkr", "7slp", "7slq", "9ngx" ]

15

[ "PUB00014753", "PUB00014754", "PUB00014755", "PUB00014756", "PUB00014757", "PUB00014758", "PUB00014760" ]

[ "15016896", "14636586", "14690589", "12086614", "12560814", "11416181", "15004549" ]

[ "A peptide from autoantigen La blocks poliovirus and hepatitis C virus cap-independent translation and reveals a single tyrosine critical for La RNA binding and translation stimulation.", "Differential phosphorylation and subcellular localization of La RNPs associated with precursor tRNAs and translation-related ...

[ 2004, 2003, 2003, 2002, 2003, 2001, 2004 ]

7

[ "IPR045180" ]

[]

1

0

1

[ "Eukaryota" ]

[ 10389 ]

1

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 17, 1, 8, 5, 20, 11, 1, 19, 14, 1, 1, 42 ]

12

true

Family

Lupus La protein

Lupus_La

6

IPR002345

2,345

Lipocalin

Family

6,088

false

The lipocalins are a diverse, interesting, yet poorly understood family of proteins composed, in the main, of extracellular ligand-binding proteins displaying high specificity for small hydrophobic molecules [ ]. Functions of these proteins include transport of nutrients, control of cell regulation, pheromone transport...

[ "GO:0036094" ]

[ "small molecule binding" ]

[ "molecular_function" ]

1

[ "PANTHER" ]

[ "PTHR11430" ]

[ "" ]

[ 6088 ]

1

[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "PDOC00187", "R-BTA-2162123", "R-HSA-2162123", "R-HSA-6785807", "R-HSA-6798695", "R-HSA-6799990", "R-HSA-804914", "R-HSA-917937", "R-HSA-9690406", "R-MMU-2162123", "R-MMU-6798695", "R-MMU-6799990", "R-MMU-804914", "R-MMU-917937", "R-RNO-2162123", "R-RNO-6798695", "R-RNO-6799990", "...

[ "PROSITEDOC:PDOC00187", "REACTOME:R-BTA-2162123", "REACTOME:R-HSA-2162123", "REACTOME:R-HSA-6785807", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-6799990", "REACTOME:R-HSA-804914", "REACTOME:R-HSA-917937", "REACTOME:R-HSA-9690406", "REACTOME:R-MMU-2162123", "REACTOME:R-MMU-6798695", "REACTOME:R-...

20

[ "1a3y", "1b0o", "1b8e", "1beb", "1bj7", "1bso", "1bsq", "1bsy", "1cj5", "1df3", "1dfv", "1dv9", "1dzj", "1dzk", "1dzm", "1dzp", "1e00", "1e02", "1e06", "1e5p", "1epa", "1epb", "1ew3", "1exs", "1g85", "1gm6", "1gt1", "1gt3", "1gt4", "1gt5", "1gx8", "1gx9"...

286

[ "PUB00000205", "PUB00003448", "PUB00005013", "PUB00005094", "PUB00083135" ]

[ "1834059", "8573354", "7684291", "2580349", "4708098" ]

[ "Mouse oncogene protein 24p3 is a member of the lipocalin protein family.", "Multiple molecular recognition properties of the lipocalin protein family.", "Structure and sequence relationships in the lipocalins and related proteins.", "Homology of beta-lactoglobulin, serum retinol-binding protein, and protein ...

[ 1991, 1995, 1993, 1985, 1973 ]

5

[]

[ "IPR002447", "IPR002448", "IPR002450", "IPR002971", "IPR003087" ]

0

5

0

[ "Eukaryota", "Limosilactobacillus urinaemulieris" ]

[ 6086, 2 ]

2

[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]

[ 2, 6, 1, 42, 77, 5, 93, 3 ]

8

true

Family

Lipocalin

5

IPR002346

2,346

Molybdopterin dehydrogenase, FAD-binding

Mopterin_DH_FAD-bd

Domain

49,693

false

Oxidoreductases, that also bind molybdopterin, have essentially no similarity outside this common domain. They include aldehyde oxidase ( ), that converts an aldehyde and water to an acid and hydrogen peroxide, and xanthine dehydrogenase ( ), that converts xanthine to urate. These enzymes require molybdopterin and FAD ...

[ "GO:0016491" ]

[ "oxidoreductase activity" ]

[ "molecular_function" ]

1

[ "PFAM" ]

[ "PF00941" ]

[ "FAD_binding_5" ]

[ 49693 ]

1

[ "GP", "GP", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "GenProp1236", "GenProp1255", "GenProp1469", "GenProp1753", "R-CEL-964975", "R-DDI-74259", "R-DDI-964975", "R-DDI-9748787", "R-DME-74259", "R-DME-964975", "R-DME-9748787", "R-GGA-421178", "R-HSA-74259", "R-HSA-8851680", "R-HSA-964975", "R-HSA-9748787", "R-MMU-74259", "R-MMU-8851680...

[ "GP:GenProp1236", "GP:GenProp1255", "GP:GenProp1469", "GP:GenProp1753", "REACTOME:R-CEL-964975", "REACTOME:R-DDI-74259", "REACTOME:R-DDI-964975", "REACTOME:R-DDI-9748787", "REACTOME:R-DME-74259", "REACTOME:R-DME-964975", "REACTOME:R-DME-9748787", "REACTOME:R-GGA-421178", "REACTOME:R-HSA-7425...

24

[ "1ffu", "1ffv", "1fiq", "1fo4", "1jro", "1jrp", "1n5w", "1n5x", "1n60", "1n61", "1n62", "1n63", "1rm6", "1sb3", "1t3q", "1v97", "1vdv", "1wyg", "1zxi", "2ckj", "2e1q", "2e3t", "2w3r", "2w3s", "2w54", "2w55", "3am9", "3amz", "3an1", "3ax7", "3ax9", "3b9j"...

73

[]

0

[ "IPR016166" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 492, 34669, 13821, 711 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 38, 3, 4, 7, 3, 6, 16, 1, 20, 23, 79 ]

11

true

Domain

Molybdopterin dehydrogenase, FAD-binding

Mopterin_DH_FAD-bd

6

IPR002347

2,347

Short-chain dehydrogenase/reductase SDR

SDR_fam

Family

1,182,974

false

The short-chain dehydrogenases/reductases family (SDR) [ , ] is a very large family of enzymes, most of which are known to be NAD- or NADP-dependent oxidoreductases. As the first member of this family to be characterised was Drosophila alcohol dehydrogenase, this family used to be called [ , , ] 'insect-type', or 'shor...

[]

0

[ "PFAM", "PFAM", "PRINTS", "PRINTS" ]

[ "PF00106", "PF13561", "PR00080", "PR00081" ]

[ "adh_short", "adh_short_C2", "SDRFAMILY", "GDHRDH" ]

[ 650195, 541883, 773049, 1108557 ]

4

[ "EC", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REA...

[ "1.1.1", "GenProp0457", "GenProp1217", "GenProp1228", "GenProp1240", "GenProp1246", "GenProp1287", "GenProp1308", "GenProp1316", "GenProp1321", "GenProp1336", "GenProp1338", "GenProp1376", "GenProp1423", "GenProp1458", "GenProp1533", "GenProp1544", "GenProp1569", "GenProp1594", ...

[ "EC:1.1.1", "GP:GenProp0457", "GP:GenProp1217", "GP:GenProp1228", "GP:GenProp1240", "GP:GenProp1246", "GP:GenProp1287", "GP:GenProp1308", "GP:GenProp1316", "GP:GenProp1321", "GP:GenProp1336", "GP:GenProp1338", "GP:GenProp1376", "GP:GenProp1423", "GP:GenProp1458", "GP:GenProp1533", "G...

212

[ "1a27", "1a4u", "1ae1", "1ahh", "1ahi", "1b14", "1b15", "1b16", "1b2l", "1bdb", "1bhs", "1bvr", "1c14", "1cwu", "1cyd", "1d7o", "1d8a", "1dfg", "1dfh", "1dfi", "1dhr", "1dht", "1dir", "1doh", "1e3s", "1e3w", "1e6w", "1e7w", "1e92", "1edo", "1eno", "1enp"...

1,405

[ "PUB00000419", "PUB00001371", "PUB00001399", "PUB00001408", "PUB00004592", "PUB00075490" ]

[ "7742302", "2707261", "1889416", "1740120", "6789320", "25526675" ]

[ "Short-chain dehydrogenases/reductases (SDR).", "The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc.", "Characteristics of short-chain alcohol dehydrogenases and related enzymes.", "cis-diol dehydrogen...

[ 1995, 1989, 1991, 1992, 1981, 2015 ]

6

[]

[ "IPR002425", "IPR002426", "IPR002427", "IPR003560", "IPR005979", "IPR006393", "IPR011283", "IPR011284", "IPR011285", "IPR011286", "IPR011294", "IPR011348", "IPR014007", "IPR014058", "IPR014358", "IPR017619", "IPR023985", "IPR027533", "IPR030981", "IPR042829", "IPR045000", "...

0

31

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "plasmids", "unclassified sequences" ]

[ 8674, 786302, 375225, 149, 4, 12620 ]

6

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 447, 86, 196, 204, 18, 259, 171, 68, 347, 237, 17, 23, 462 ]

13

true

Family

Short-chain dehydrogenase/reductase SDR

SDR_fam

8

IPR002350

2,350

Kazal domain

Kazal_dom

Domain

61,859

false

This entry represents the Kazal domain. Canonical serine proteinase inhibitors are distributed in a wide range of organisms from all kingdoms of life and play crucial role in various physiological mechanisms [ ]. They interact from the canonical proteinase-inhibitor binding loop, where P1 residue has a predominant role...

[ "GO:0005515" ]

[ "protein binding" ]

[ "molecular_function" ]

1

[ "PFAM", "PFAM", "PROSITE", "PROFILE", "SMART" ]

[ "PF00050", "PF07648", "PS00282", "PS51465", "SM00280" ]

[ "Kazal_1", "Kazal_2", "KAZAL_1", "KAZAL_2", "KAZAL" ]

[ 14284, 44505, 8825, 59740, 41586 ]

5

[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...

[ "PDOC00254", "R-BTA-114608", "R-BTA-201451", "R-BTA-2473224", "R-BTA-3000178", "R-BTA-3000497", "R-BTA-381426", "R-BTA-6809371", "R-BTA-879518", "R-BTA-8957275", "R-CEL-114608", "R-CEL-3000178", "R-CEL-381426", "R-CEL-8957275", "R-DME-6798695", "R-DME-879518", "R-DRE-2473224", "R-G...

[ "PROSITEDOC:PDOC00254", "REACTOME:R-BTA-114608", "REACTOME:R-BTA-201451", "REACTOME:R-BTA-2473224", "REACTOME:R-BTA-3000178", "REACTOME:R-BTA-3000497", "REACTOME:R-BTA-381426", "REACTOME:R-BTA-6809371", "REACTOME:R-BTA-879518", "REACTOME:R-BTA-8957275", "REACTOME:R-CEL-114608", "REACTOME:R-CEL...

113

[ "1an1", "1bmo", "1bus", "1cgi", "1cgj", "1cho", "1cso", "1ct0", "1ct2", "1ct4", "1ds2", "1ds3", "1h0z", "1hja", "1hpt", "1iw4", "1iy5", "1iy6", "1kma", "1ldt", "1lr7", "1lr8", "1lr9", "1m8b", "1m8c", "1nub", "1omt", "1omu", "1ovo", "1pce", "1ppf", "1r0r"...

142

[ "PUB00000032", "PUB00029611", "PUB00063941" ]

[ "6996568", "6752426", "10708867" ]

[ "Protein inhibitors of proteinases.", "Crystallographic refinement of Japanese quail ovomucoid, a Kazal-type inhibitor, and model building studies of complexes with serine proteases.", "What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme substrate complexes?" ]

[ 1980, 1982, 2000 ]

3

[]

[ "IPR048719" ]

0

1

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]

[ 51, 1043, 60720, 9, 36 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus" ]

[ 5, 12, 250, 64, 134, 146, 2, 226 ]

8

true

Domain

Kazal domain

Kazal_dom

7

IPR002351

2,351

Nitrophorin domain

Nitrophorin_domain

Domain

194

false

This entry represents the nitrophorin structural domain. Nitrophorins are haemoproteins found in saliva of blood-feeding insects [ , ]. Saliva of the blood-sucking bug Rhodnius prolixus (Triatomid bug) contains four homologous nitrophorins, designated NP1 to NP4 in order of their relative abundance in the glands [ ]. A...

[ "GO:0051381", "GO:0070026" ]

[ "histamine binding", "nitric oxide binding" ]

[ "molecular_function", "molecular_function" ]

2

[ "PFAM" ]

[ "PF02087" ]

[ "Nitrophorin" ]

[ 194 ]

1

[]

0

[ "1d2u", "1d3s", "1eqd", "1erx", "1euo", "1ike", "1ikj", "1koi", "1ml7", "1np1", "1np4", "1pee", "1pm1", "1sxu", "1sxw", "1sxx", "1sxy", "1sy0", "1sy1", "1sy2", "1sy3", "1t68", "1u0x", "1u17", "1u18", "1x8n", "1x8o", "1x8p", "1x8q", "1ywa", "1ywb", "1ywc"...

79

[ "PUB00000545", "PUB00008042", "PUB00008043", "PUB00008044", "PUB00008045" ]

[ "8761444", "10093938", "11058753", "7721773", "9716517" ]

[ "The lipocalin protein family: structure and function.", "Novel nitric oxide-liberating heme proteins from the saliva of bloodsucking insects.", "Nitrophorins and related antihemostatic lipocalins from Rhodnius prolixus and other blood-sucking arthropods.", "Purification, partial characterization, and cloning...

[ 1996, 1999, 2000, 1995, 1998 ]

5

[]

0

null

[ "Arthropoda" ]

[ 194 ]

1

[]

0

true

Domain

Nitrophorin domain

Nitrophorin_domain

8

IPR002352

2,352

Eosinophil major basic protein

Eosinophil_major_basic

Family

620

false

Eosinophil granule major basic protein (MBP) is a low molecular weight cationic protein present in the crystalloid core of the eosinophil granule [ ]. It is a potent toxin for helminths and mammalian cells, and may have important roles in allergic and inflammatory reactions, it can release histamine from mast cells and...

[ "GO:0006955" ]

[ "immune response" ]

[ "biological_process" ]

1

[ "PRINTS" ]

[ "PR00770" ]

[ "EMAJORBASICP" ]

[ 620 ]

1

[ "REACTOME", "REACTOME", "REACTOME" ]

[ "R-HSA-6798695", "R-MMU-6798695", "R-RNO-6798695" ]

[ "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-6798695", "REACTOME:R-RNO-6798695" ]

3

[ "1h8u", "2brs", "7y5n", "8hgg", "9dkz", "9ppv", "9pse", "9psk" ]

8

[ "PUB00001786", "PUB00002461", "PUB00003105", "PUB00003779" ]

[ "2323577", "3410852", "3171483", "1565101" ]

[ "Cloning and sequence analysis of the human gene encoding eosinophil major basic protein.", "Biochemical and amino acid sequence analysis of human eosinophil granule major basic protein.", "Acidic precursor revealed in human eosinophil granule major basic protein cDNA.", "Purification and cDNA cloning of a no...

[ 1990, 1988, 1988, 1992 ]

4

[]

0

null

[ "Eumetazoa", "bird metagenome" ]

[ 619, 1 ]

2

[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 4, 3, 5 ]

3

true

Family

Eosinophil major basic protein

Eosinophil_major_basic

2

IPR002353

2,353

Type-2 ice-structuring protein

AntifreezeII

Family

1,009

false

Marine teleosts from polar oceans can be protected from freezing in icy sea-water by serum antifreeze proteins (AFPs) or glycoproteins (AFGPs) [ ]. These function by binding to, and preventing the growth of, ice crystals within the fish. Despite functional similarity, the proteins are structurally diverse and include g...

[]

0

[ "PRINTS" ]

[ "PR00356" ]

[ "ANTIFREEZEII" ]

[ 1009 ]

1

[]

0

[ "2afp", "2py2", "2zib", "6jk4", "6jk5" ]

5

[ "PUB00005033" ]

[ "7540906" ]

[ "Comparative modeling of the three-dimensional structure of type II antifreeze protein." ]

[ 1995 ]

1

[]

0

null

[ "Eumetazoa" ]

[ 1009 ]

1

[ "Danio rerio" ]

[ 26 ]

1

true

Family

Type-2 ice-structuring protein

AntifreezeII

6

IPR002354

2,354

Interleukin-4

IL-4

Family

592

false

Cytokines are protein messengers that carry information from cell to cell [ ]. Interleukin is one such molecule, and participates in several B-cell activation processes: e.g., it enhances production and secretion of IgG1 and IgE [ ]; it induces expression of class II major histocompatability complex (MHC) molecules on ...

[ "GO:0005136", "GO:0008083", "GO:0006955", "GO:0005576" ]

[ "interleukin-4 receptor binding", "growth factor activity", "immune response", "extracellular region" ]

[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

4

[ "PFAM", "PIRSF", "PRINTS", "PANTHER" ]

[ "PF00727", "PIRSF001941", "PR00431", "PTHR47401" ]

[ "IL4", "Interleukin_4", "INTERLEUKIN4", "" ]

[ 542, 205, 341, 572 ]

4

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-BTA-6785807", "R-CFA-6785807", "R-HSA-6785807", "R-HSA-9012546", "R-MMU-6785807", "R-RNO-6785807", "R-SSC-6785807" ]

[ "REACTOME:R-BTA-6785807", "REACTOME:R-CFA-6785807", "REACTOME:R-HSA-6785807", "REACTOME:R-HSA-9012546", "REACTOME:R-MMU-6785807", "REACTOME:R-RNO-6785807", "REACTOME:R-SSC-6785807" ]

7

[ "1bbn", "1bcn", "1cyl", "1hij", "1hik", "1hzi", "1iar", "1iti", "1itl", "1itm", "1rcb", "2b8u", "2b8x", "2b8y", "2b8z", "2b90", "2b91", "2cyk", "2d48", "2int", "3bpl", "3bpn", "3qb7", "4ydy", "5fhx", "6oel", "8a4f", "8cgf", "8ch7" ]

29

[ "PUB00000339", "PUB00002742", "PUB00003320", "PUB00004616" ]

[ "1993171", "1400355", "8151703", "3083412" ]

[ "Disulfide assignments in recombinant mouse and human interleukin 4.", "Crystal structure of recombinant human interleukin-4.", "Aspects of receptor binding and signalling of interleukin-4 investigated by site-directed mutagenesis and NMR spectroscopy.", "Isolation and characterization of a mouse interleukin ...

[ 1991, 1992, 1994, 1986 ]

4

[ "IPR001325" ]

[]

1

0

1

[ "Euteleostomi" ]

[ 592 ]

1

[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 8, 3, 5 ]

3

true

Family

Interleukin-4

IL-4

8

IPR002355

2,355

Multicopper oxidase, copper-binding site

Cu_oxidase_Cu_BS

Binding_site

59,677

false

The entry represents a conserved region containing the Cu-binding site found in multicopper oxidases. Multicopper oxidases oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre; dioxygen binds to the trinuclear centre and, following the transfe...

[ "GO:0005507" ]

[ "copper ion binding" ]

[ "molecular_function" ]

1

[ "PROSITE" ]

[ "PS00080" ]

[ "MULTICOPPER_OXIDASE2" ]

[ 59677 ]

1

[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "PDOC00076", "R-HSA-381426", "R-HSA-425410", "R-HSA-5619049", "R-HSA-5619060", "R-HSA-5655799", "R-HSA-8957275", "R-HSA-917937", "R-MMU-381426", "R-MMU-425410", "R-MMU-8957275", "R-MMU-917937", "R-RNO-381426", "R-RNO-425410", "R-RNO-8957275", "R-RNO-917937" ]

[ "PROSITEDOC:PDOC00076", "REACTOME:R-HSA-381426", "REACTOME:R-HSA-425410", "REACTOME:R-HSA-5619049", "REACTOME:R-HSA-5619060", "REACTOME:R-HSA-5655799", "REACTOME:R-HSA-8957275", "REACTOME:R-HSA-917937", "REACTOME:R-MMU-381426", "REACTOME:R-MMU-425410", "REACTOME:R-MMU-8957275", "REACTOME:R-MMU...

16

[ "1a65", "1aoz", "1aso", "1asp", "1asq", "1gw0", "1hfu", "1kcw", "1kv7", "1n68", "1pf3", "1v10", "1zpu", "2fqd", "2fqe", "2fqf", "2fqg", "2ih8", "2ih9", "2j5w", "2q9o", "2xu9", "2xuw", "2xvb", "2yae", "2yaf", "2yah", "2yam", "2yao", "2yap", "2yaq", "2yar"...

177

[ "PUB00001382", "PUB00001602", "PUB00011817", "PUB00035911", "PUB00035912", "PUB00035913" ]

[ "2404764", "1995346", "11867755", "14572631", "11041837", "16234932" ]

[ "The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships.", "A structure-derived sequence pattern for the detection of type I copper binding domains in distantly related proteins.", "Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase r...

[ 1990, 1991, 2002, 2003, 2000, 2005 ]

6

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 160, 23602, 35733, 182 ]

4

[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae...

[ 76, 5, 15, 1, 16, 9, 9, 67, 11, 3, 1, 97 ]

12

true

Binding_site

Multicopper oxidase, copper-binding site

Cu_oxidase_Cu_BS

7

IPR002358

2,358

Large ribosomal subunit protein uL6, conserved site

Ribosomal_uL6_CS

Conserved_site

26,009

false

This entry represents a conserved region of the large ribosomal subunit protein uL6 previously known as ribosomal protein L6. In Escherichia coli, L6 is known to bind directly to the 23S rRNA and is located at the aminoacyl-tRNA binding site of the peptidyltransferase centre. It belongs to a family of ribosomal protein...

[ "GO:0003735", "GO:0006412", "GO:0005840" ]

[ "structural constituent of ribosome", "translation", "ribosome" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PROSITE" ]

[ "PS00525" ]

[ "RIBOSOMAL_L6_1" ]

[ 26009 ]

1

[ "PROSITEDOC" ]

[ "PDOC00454" ]

[ "PROSITEDOC:PDOC00454" ]

1

[ "1c04", "1eg0", "1ml5", "1rl6", "2j28", "2rdo", "3bbx", "3j3v", "3j3w", "3j5l", "3j6b", "3j7z", "3j8g", "3j9w", "3j9y", "3j9z", "3ja1", "3jbu", "3jbv", "3jcd", "3jce", "3jcj", "3jcn", "487d", "4csu", "4u1u", "4u1v", "4u20", "4u24", "4u25", "4u26", "4u27"...

803

[ "PUB00001046", "PUB00001241", "PUB00001794", "PUB00007068", "PUB00007069", "PUB00007070" ]

[ "8358820", "8262035", "2227441", "11297922", "11290319", "11114498" ]

[ "Molecular cloning and analysis of the nuclear gene MRP-L6 coding for a putative mitochondrial ribosomal protein from Saccharomyces cerevisiae.", "Ribosomal protein L6: structural evidence of gene duplication from a primitive RNA binding protein.", "The primary structure of rat ribosomal protein L9.", "Atomic...

[ 1993, 1993, 1990, 2001, 2001, 2000 ]

6

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 22191, 3452, 366 ]

3

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]

[ 6, 1, 1, 10, 1, 1, 11 ]

7

true

Conserved_site

Large ribosomal subunit protein uL6, conserved site

Ribosomal_uL6_CS

8

IPR002359

2,359

Large ribosomal subunit protein uL6, conserved site-2

Ribosomal_uL6_CS2

Conserved_site

5,413

false

This entry represents a conserved region found in the large ribosomal subunit protein uL6 from archaea (previously known as ribosomal protein L6) and some eukaryotic species (in which this proteins is also called L9) [ ]. In Escherichia coli, L6 is known to bind directly to the 23S rRNA and is located at the aminoacyl-...

[ "GO:0003735", "GO:0006412", "GO:0005840" ]

[ "structural constituent of ribosome", "translation", "ribosome" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PROSITE" ]

[ "PS00700" ]

[ "RIBOSOMAL_L6_2" ]

[ 5413 ]

1

[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...

[ "PDOC00454", "R-BTA-156827", "R-BTA-1799339", "R-BTA-6791226", "R-BTA-72689", "R-BTA-72706", "R-BTA-975956", "R-BTA-975957", "R-CEL-156827", "R-CEL-1799339", "R-CEL-72689", "R-CEL-72706", "R-CEL-975956", "R-CEL-975957", "R-DDI-156827", "R-DDI-1799339", "R-DDI-72689", "R-DDI-72706",...

[ "PROSITEDOC:PDOC00454", "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-6791226", "REACTOME:R-BTA-72689", "REACTOME:R-BTA-72706", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-975957", "REACTOME:R-CEL-156827", "REACTOME:R-CEL-1799339", "REACTOME:R-CEL-72689", "REACTOME:R-CEL-7270...

65

[ "1ffk", "1jj2", "1k73", "1k8a", "1k9m", "1kc8", "1kd1", "1kqs", "1m1k", "1m90", "1n8r", "1nji", "1q7y", "1q81", "1q82", "1q86", "1qvf", "1qvg", "1s72", "1vq4", "1vq5", "1vq6", "1vq7", "1vq8", "1vq9", "1vqk", "1vql", "1vqm", "1vqn", "1vqo", "1vqp", "1w2b"...

636

[ "PUB00001046", "PUB00001241", "PUB00001794", "PUB00007068", "PUB00007069", "PUB00007070", "PUB00080279" ]

[ "8358820", "8262035", "2227441", "11297922", "11290319", "11114498", "24524803" ]

[ "Molecular cloning and analysis of the nuclear gene MRP-L6 coding for a putative mitochondrial ribosomal protein from Saccharomyces cerevisiae.", "Ribosomal protein L6: structural evidence of gene duplication from a primitive RNA binding protein.", "The primary structure of rat ribosomal protein L9.", "Atomic...

[ 1993, 1993, 1990, 2001, 2001, 2000, 2014 ]

7

[]

0

null

[ "Archaea", "Eukaryota", "ecological metagenomes" ]

[ 636, 4774, 3 ]

3

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 8, 1, 2, 2, 7, 5, 1, 4, 6, 2, 2, 15 ]

12

true

Conserved_site

Large ribosomal subunit protein uL6, conserved site-2

Ribosomal_uL6_CS2

2

IPR002361

2,361

Antenna complex, alpha subunit conserved site

Antenna_alpha_CS

Conserved_site

801

false

This entry represents a conserved site found in the alpha subunit which includes the conserved histidine residue. The antenna complexes of photosynthetic bacteria function as light-harvesting systems that absorb light and transfer the excitation energy to the reaction centres. The antenna complexes usually comprise 2 p...

[ "GO:0019684", "GO:0016020", "GO:0019866", "GO:0030077" ]

[ "photosynthesis, light reaction", "membrane", "organelle inner membrane", "plasma membrane light-harvesting complex" ]

[ "biological_process", "cellular_component", "cellular_component", "cellular_component" ]

4

[ "PROSITE" ]

[ "PS00968" ]

[ "ANTENNA_COMP_ALPHA" ]

[ 801 ]

1

[ "PROSITEDOC" ]

[ "PDOC00748" ]

[ "PROSITEDOC:PDOC00748" ]

1

[ "1ijd", "1kzu", "1lgh", "1nkz", "1xrd", "2fkw", "3wmm", "4v8k", "4v9g", "5b5m", "5b5n", "5y5s", "5yq7", "6et5", "6z5r", "6z5s", "7c52", "7ddq", "7eqd", "7f0l", "7o0u", "7o0v", "7o0w", "7o0x", "7oy8", "7pbw", "7pil", "7pqd", "7tuw", "7tv3", "7va9", "7vb9"...

81

[ "PUB00001417", "PUB00003468", "PUB00153105", "PUB00153106" ]

[ "1577009", "1460542", "36738736", "36792596" ]

[ "The primary structure of the antenna polypeptides of Ectothiorhodospira halochloris and Ectothiorhodospira halophila. Four core-type antenna polypeptides in E. halochloris and E. halophila.", "Structure, function and organization of antenna polypeptides and antenna complexes from the three families of Rhodospiri...

[ 1992, 1992, 2023, 2023 ]

4

[]

0

null

[ "Bacteria", "Hemiselmis andersenii", "marine sediment metagenome" ]

[ 799, 1, 1 ]

3

[]

0

true

Conserved_site

Antenna complex, alpha subunit conserved site

Antenna_alpha_CS

9

IPR002362

2,362

Light-harvesting protein B beta chain

LHB-1/5

Family

1,150

false

This family represents the Light-harvesting protein B (also known as Antenna pigment protein) beta chain. The antenna complexes of photosynthetic bacteria function as light-harvesting systems that absorb light and transfer the excitation energy to the reaction centres. The antenna complexes usually comprise 2 polypepti...

[ "GO:0019684", "GO:0016020", "GO:0030077" ]

[ "photosynthesis, light reaction", "membrane", "plasma membrane light-harvesting complex" ]

[ "biological_process", "cellular_component", "cellular_component" ]

3

[ "NCBIFAM", "PIRSF", "PRINTS" ]

[ "NF040862", "PIRSF002900", "PR00674" ]

[ "pufB_517_ASD", "Antenna_beta", "LIGHTHARVSTB" ]

[ 1042, 807, 1137 ]

3

[ "PROSITEDOC" ]

[ "PDOC00748" ]

[ "PROSITEDOC:PDOC00748" ]

1

[ "1dx7", "1ijd", "1jo5", "1kzu", "1lgh", "1nkz", "1wrg", "2fkw", "3wmm", "4v8k", "4v9g", "5b5m", "5b5n", "5y5s", "5yq7", "6et5", "6q53", "6z5r", "6z5s", "6zxa", "7c52", "7c9r", "7ddq", "7eqd", "7f0l", "7o0u", "7o0v", "7o0w", "7o0x", "7oy8", "7pbw", "7pil"...

90

[ "PUB00001417", "PUB00003468", "PUB00153105", "PUB00153106" ]

[ "1577009", "1460542", "36738736", "36792596" ]

[ "The primary structure of the antenna polypeptides of Ectothiorhodospira halochloris and Ectothiorhodospira halophila. Four core-type antenna polypeptides in E. halochloris and E. halophila.", "Structure, function and organization of antenna polypeptides and antenna complexes from the three families of Rhodospiri...

[ 1992, 1992, 2023, 2023 ]

4

[]

0

null

[ "Bacteria", "freshwater sediment metagenome" ]

[ 1149, 1 ]

2

[]

0

true

Family

Light-harvesting protein B beta chain

LHB-1/5

5

IPR002363

2,363

Large ribosomal subunit protein uL10, conserved site, bacteria

Ribosomal_uL10_CS_bac

Conserved_site

16,222

false

This entry represents a conserved region located in the N-terminal section of the Large ribosomal subunit protein uL10, previously known as Ribosomal protein L10. This protein of 162 to 185 amino-acid residues is found in bacteria. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organis...

[ "GO:0003735", "GO:0006412", "GO:0015934" ]

[ "structural constituent of ribosome", "translation", "large ribosomal subunit" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PROSITE" ]

[ "PS01109" ]

[ "RIBOSOMAL_L10" ]

[ 16222 ]

1

[ "PROSITEDOC" ]

[ "PDOC00853" ]

[ "PROSITEDOC:PDOC00853" ]

1

[ "1zav", "1zaw", "1zax", "3j7z", "3j9w", "3j9y", "3j9z", "3ja1", "3jcj", "4uy8", "4v6n", "4v6o", "4v6p", "4v6q", "4v6r", "4v6s", "4v6v", "4v7b", "4v7c", "4v7d", "4v85", "4v89", "4v9o", "4v9p", "4ybb", "5ady", "5afi", "5gad", "5gae", "5gaf", "5gag", "5gah"...

286

[ "PUB00007068", "PUB00007069", "PUB00007070" ]

[ "11297922", "11290319", "11114498" ]

[ "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins." ]

[ 2001, 2001, 2000 ]

3

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Gallid alphaherpesvirus 2", "unclassified sequences" ]

[ 7, 15935, 32, 2, 246 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Conserved_site

Large ribosomal subunit protein uL10, conserved site, bacteria

Ribosomal_uL10_CS_bac

6

IPR002364

2,364

Quinone oxidoreductase/zeta-crystallin, conserved site

Quin_OxRdtase/zeta-crystal_CS

Conserved_site

49,750

false

null

[ "GO:0008270", "GO:0016491" ]

[ "zinc ion binding", "oxidoreductase activity" ]

[ "molecular_function", "molecular_function" ]

2

[ "PROSITE" ]

[ "PS01162" ]

[ "QOR_ZETA_CRYSTAL" ]

[ 49750 ]

1

[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "PDOC00058", "R-DRE-6798695", "R-HSA-6798695", "R-MMU-6798695", "R-RNO-6798695" ]

[ "PROSITEDOC:PDOC00058", "REACTOME:R-DRE-6798695", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-6798695", "REACTOME:R-RNO-6798695" ]

5

[ "1qor", "1yb5", "2c0c", "2vn8", "2wek", "2x1h", "2x7h", "3fbg", "3jyl", "3jyn", "3qwa", "3qwb", "3slk", "3tqh", "4a0s", "4a10", "4a27", "4eye", "4ida", "4idb", "4idc", "4idd", "4ide", "4idf", "4j6f", "4y0k", "4y1b", "5k1s", "6k9y", "6lhr", "6lii", "7zej"...

33

[ "PUB00001655" ]

[ "8486156" ]

[ "Zeta-crystallin versus other members of the alcohol dehydrogenase super-family. Variability as a functional characteristic." ]

[ 1993 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]

[ 330, 35941, 13218, 261 ]

4

[ "Arabidopsis thaliana", "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)...

[ 17, 3, 1, 19, 18, 2, 8, 16, 1, 26 ]

10

true

Conserved_site

Quinone oxidoreductase/zeta-crystallin, conserved site

Quin_OxRdtase/zeta-crystal_CS

5

IPR002365

2,365

Terpene synthase, conserved site

Terpene_synthase_CS

Conserved_site

8,844

false

Several enzymes catalyse mechanistically related reactions which involve the highly complex cyclic rearrangement of squalene or its 2,3 oxide. Lanosterol synthase ( ) (oxidosqualene--lanosterol cyclase) catalyzes the cyclization of (S)-2,3-epoxysqualene to lanosterol, the initial precursor of cholesterol, steroid hormo...

[ "GO:0016866" ]

[ "intramolecular transferase activity" ]

[ "molecular_function" ]

1

[ "PROSITE" ]

[ "PS01074" ]

[ "TERPENE_SYNTHASES" ]

[ 8844 ]

1

[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "5.4.99", "PDOC00825", "R-DDI-191273", "R-HSA-191273", "R-HSA-2426168", "R-MMU-191273", "R-RNO-191273", "R-SCE-191273", "R-SPO-191273" ]

[ "EC:5.4.99", "PROSITEDOC:PDOC00825", "REACTOME:R-DDI-191273", "REACTOME:R-HSA-191273", "REACTOME:R-HSA-2426168", "REACTOME:R-MMU-191273", "REACTOME:R-RNO-191273", "REACTOME:R-SCE-191273", "REACTOME:R-SPO-191273" ]

9

[ "1gsz", "1h35", "1h36", "1h37", "1h39", "1h3a", "1h3b", "1h3c", "1o6h", "1o6q", "1o6r", "1o79", "1sqc", "1ump", "1w6j", "1w6k", "2sqc", "3sqc" ]

18

[ "PUB00004809" ]

[ "7505443" ]

[ "Isolation of an Arabidopsis thaliana gene encoding cycloartenol synthase by functional expression in a yeast mutant lacking lanosterol synthase by the use of a chromatographic screen." ]

[ 1993 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 1668, 7142, 34 ]

3

[ "Arabidopsis thaliana", "Danio rerio", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]

[ 70, 1, 4, 1, 25, 4, 1, 1, 53 ]

9

true

Conserved_site

Terpene synthase, conserved site

Terpene_synthase_CS

2

IPR002366

2,366

Alpha-defensin, N-terminal

Alpha-defensin_N

Domain

662

false

This entry represents the N-terminal domain of a group of alpha defensins and similar sequences mainly found in mammals. Defensins are 2-6kDa, cationic, microbicidal peptides active against many Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses [ , ] containing three pairs of intramolecular disulph...

[ "GO:0006952" ]

[ "defense response" ]

[ "biological_process" ]

1

[ "PFAM", "SMART" ]

[ "PF00879", "SM01418" ]

[ "Defensin_propep", "Defensin_propep" ]

[ 643, 652 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-HSA-1461973", "R-HSA-1462054", "R-HSA-6798695", "R-HSA-9841251", "R-MMU-1461973", "R-MMU-1462054", "R-MMU-6798695", "R-RNO-1461973", "R-RNO-1462054", "R-RNO-6798695" ]

[ "REACTOME:R-HSA-1461973", "REACTOME:R-HSA-1462054", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-9841251", "REACTOME:R-MMU-1461973", "REACTOME:R-MMU-1462054", "REACTOME:R-MMU-6798695", "REACTOME:R-RNO-1461973", "REACTOME:R-RNO-1462054", "REACTOME:R-RNO-6798695" ]

10

[]

0

[ "PUB00001093", "PUB00007192", "PUB00007193", "PUB00100838" ]

[ "8528769", "12072367", "12021776", "30658057" ]

[ "Structure, function, and membrane integration of defensins.", "Mammalian defensins in immunity: more than just microbicidal.", "Paneth cell trypsin is the processing enzyme for human defensin-5.", "Systematic mutational analysis of human neutrophil α-defensin HNP4." ]

[ 1995, 2002, 2002, 2019 ]

4

[]

0

null

[ "Opisthokonta", "Pseudomonadati" ]

[ 649, 13 ]

2

[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 6, 65, 22 ]

3

true

Domain

Alpha-defensin, N-terminal

Alpha-defensin_N

6

IPR002367

2,367

Nociceptin

Family

873

false

Vertebrate endogenous opioid neuropeptides are released by post-translational proteolytic cleavage of precursor proteins. The precursors consist of the following components: a signal sequence that precedes a conserved region of about 50 residues; a variable-length region; and the sequence of the neuropeptide itself. Th...

[ "GO:0007218", "GO:0007268" ]

[ "neuropeptide signaling pathway", "chemical synaptic transmission" ]

[ "biological_process", "biological_process" ]

2

[ "PRINTS" ]

[ "PR01031" ]

[ "ORPHNNPRCRSR" ]

[ 873 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-BTA-375276", "R-BTA-418594", "R-HSA-375276", "R-HSA-418594", "R-MMU-375276", "R-MMU-418594", "R-RNO-375276", "R-RNO-418594" ]

[ "REACTOME:R-BTA-375276", "REACTOME:R-BTA-418594", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-418594" ]

8

[]

0

[ "PUB00000251", "PUB00004901" ]

[ "7503733", "8710928" ]

[ "N23K, a gene transiently up-regulated during neural differentiation, encodes a precursor protein for a newly identified neuropeptide nociceptin.", "Structure, tissue distribution, and chromosomal localization of the prepronociceptin gene." ]

[ 1995, 1996 ]

2

[ "IPR006024" ]

[]

1

0

1

[ "Euteleostomi" ]

[ 873 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 1, 4, 4, 4 ]

4

true

Family

Nociceptin

1

IPR002368

2,368

Outer membrane protein, OmpA

OmpA

Family

2,937

false

The OmpA outer membrane proteins in this group all contain the OmpA-like transmembrane domain at the N-terminal and the conserved bacterial outer membrane protein domain at the C-terminal. The outer membrane protein A of Escherichia coli (OmpA), is one of the most studied proteins in this group [ ]. It has a multifunct...

[ "GO:0015288", "GO:0009279", "GO:0016020" ]

[ "porin activity", "cell outer membrane", "membrane" ]

[ "molecular_function", "cellular_component", "cellular_component" ]

3

[ "HAMAP", "PRINTS" ]

[ "MF_00842", "PR01022" ]

[ "OmpA", "OUTRMMBRANEA" ]

[ 1641, 2932 ]

2

[]

0

[ "1bxw", "1g90", "1qjp", "2ge4", "2jmm", "2k0l", "2mqe", "3nb3", "4erh", "4rha", "5nhx", "5ves", "9fzc", "9fzd" ]

14

[ "PUB00006249", "PUB00006571", "PUB00094442", "PUB00094443" ]

[ "1974149", "10554771", "24673644", "30713026" ]

[ "The role of the mature part of secretory proteins in translocation across the plasma membrane and in regulation of their synthesis in Escherichia coli.", "Expression and secretion of proteins in E. coli.", "OmpA and OmpC are critical host factors for bacteriophage Sf6 entry in Shigella.", "Binding from Both ...

[ 1990, 1999, 2014, 2019 ]

4

[]

0

null

[ "Bacteria", "Opisthokonta", "ecological metagenomes" ]

[ 2930, 2, 5 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Outer membrane protein, OmpA

OmpA

8

IPR002369

2,369

Integrin beta subunit, VWA domain

Integrin_bsu_VWA

Domain

14,805

false

This domain corresponds to the integrin beta VWA domain. Integrin beta subunits consist of an extracellular domain with a head region, a stalk/leg section, a transmembrane domain, and a cytoplasmic tail. The head region contains a β-I-like domain inserted into a hybrid domain, connected to a plexin-semaphorin-integrin ...

[]

0

[ "PFAM", "SMART" ]

[ "PF00362", "SM00187" ]

[ "Integrin_beta", "INB" ]

[ 14679, 14424 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-BTA-1566948", "R-BTA-166016", "R-BTA-198933", "R-BTA-202733", "R-BTA-2129379", "R-BTA-216083", "R-BTA-2173789", "R-BTA-3000178", "R-BTA-6798695", "R-CEL-114608", "R-CEL-1236973", "R-CEL-2129379", "R-CEL-216083", "R-CEL-2173789", "R-CEL-3000157", "R-CEL-3000170", "R-CEL-3000178", ...

[ "REACTOME:R-BTA-1566948", "REACTOME:R-BTA-166016", "REACTOME:R-BTA-198933", "REACTOME:R-BTA-202733", "REACTOME:R-BTA-2129379", "REACTOME:R-BTA-216083", "REACTOME:R-BTA-2173789", "REACTOME:R-BTA-3000178", "REACTOME:R-BTA-6798695", "REACTOME:R-CEL-114608", "REACTOME:R-CEL-1236973", "REACTOME:R-C...

158

[ "1jv2", "1l5g", "1m1x", "1tye", "1u8c", "2iue", "2p26", "2vc2", "2vdk", "2vdl", "2vdm", "2vdn", "2vdo", "2vdp", "2vdq", "2vdr", "3fcs", "3fcu", "3ije", "3k6s", "3k71", "3k72", "3nid", "3nif", "3nig", "3t3m", "3t3p", "3v4p", "3v4v", "3vi3", "3vi4", "3zdx"...

167

[ "PUB00001505", "PUB00006148", "PUB00006149", "PUB00006150", "PUB00009789", "PUB00015915", "PUB00015985", "PUB00035000", "PUB00035002", "PUB00057248", "PUB00160425" ]

[ "2199285", "9009218", "9535848", "9818167", "12297042", "14689578", "2467745", "12361595", "12234368", "12388743", "28510180" ]

[ "Integrins and other cell adhesion molecules.", "A structure prediction for the ligand-binding region of the integrin beta subunit: evidence for the presence of a von Willebrand factor A domain.", "Identification of pactolus, an integrin beta subunit-like cell-surface protein preferentially expressed by cells o...

[ 1990, 1997, 1998, 1998, 2002, 2004, 1989, 2002, 2002, 2002, 2014 ]

11

[]

0

null

[ "Bacteria", "Eukaryota", "Geoglobus acetivorans", "marine sediment metagenome" ]

[ 83, 14718, 2, 2 ]

4

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 1, 28, 6, 73, 22, 35 ]

6

true

Domain

Integrin beta subunit, VWA domain

Integrin_bsu_VWA

9

IPR002371

2,371

Flagellar hook-associated protein 1

FlgK

Family

14,905

false

Within the bacterial flagellum, the basal-body rod, the hook, the hook- associated proteins (HAPs), and the helical filament together constitute an axial substructure whose elements share structural features and a common export pathway [ ]. This entry represents the hook-associated protein 1 (HAP1, also known as FlgK) ...

[ "GO:0005198", "GO:0044780", "GO:0009424" ]

[ "structural molecule activity", "bacterial-type flagellum assembly", "bacterial-type flagellum hook" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PRINTS", "PANTHER", "NCBIFAM" ]

[ "PR01005", "PTHR30033", "TIGR02492" ]

[ "FLGHOOKAP1", "", "flgK_ends" ]

[ 11086, 14660, 13595 ]

3

[ "GP" ]

[ "GenProp0882" ]

[ "GP:GenProp0882" ]

1

[ "2d4y", "4ut1", "5xbj", "9go6", "9gsx" ]

5

[ "PUB00003259", "PUB00076713", "PUB00076714" ]

[ "2193164", "25645451", "16810745" ]

[ "Flagellar hook and hook-associated proteins of Salmonella typhimurium and their relationship to other axial components of the flagellum.", "From crystal structure to in silico epitope discovery in the Burkholderia pseudomallei flagellar hook-associated protein FlgK.", "Characterization of flgK gene and FlgK pr...

[ 1990, 2015, 2006 ]

3

[]

0

null

[ "Acidiplasma", "Bacteria", "Eukaryota", "unclassified sequences", "uncultured Caudovirales phage" ]

[ 3, 14667, 33, 201, 1 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Flagellar hook-associated protein 1

FlgK

9

IPR002372

2,372

Pyrrolo-quinoline quinone repeat domain

PQQ_rpt_dom

Domain

62,773

false

This entry represents a β-propeller composed of the so-called PQQ repeats and found in a group of functionally diverse proteins. Pyrrolo-quinoline quinone (PQQ) is a redox coenzyme, which serves as a cofactor for a number of enzymes (quinoproteins) and particularly for some bacterial dehydrogenases [ , , ]. A number of...

[]

0

[ "PFAM", "PFAM", "PFAM" ]

[ "PF01011", "PF13360", "PF13570" ]

[ "PQQ", "PQQ_2", "Beta-prop_ACSF4" ]

[ 19086, 42806, 2675 ]

3

[ "GP", "REACTOME" ]

[ "GenProp0170", "R-HSA-9760173" ]

[ "GP:GenProp0170", "REACTOME:R-HSA-9760173" ]

2

[ "1flg", "1g72", "1h4i", "1h4j", "1kb0", "1kv9", "1lrw", "1w6s", "1yiq", "2ad6", "2ad7", "2ad8", "2d0v", "2yh3", "2yms", "3hxj", "3p1l", "3prw", "3q54", "3q7m", "3q7n", "3q7o", "4aah", "4cvb", "4cvc", "4hdj", "4imm", "4mae", "4mh1", "4pk1", "4tqo", "4xga"...

168

[ "PUB00000066", "PUB00005344", "PUB00094370" ]

[ "2549854", "2572081", "18838797" ]

[ "Quinoproteins, enzymes with pyrrolo-quinoline quinone as cofactor.", "PQQ, the elusive coenzyme.", "A tightly bound quinone functions in the ubiquinone reaction sites of quinoprotein alcohol dehydrogenase of an acetic acid bacterium, Gluconobacter suboxydans." ]

[ 1989, 1989, 2008 ]

3

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 4048, 51573, 5541, 19, 1592 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]

[ 10, 3, 2, 2, 2, 5, 2, 9, 3, 21 ]

10

true

Domain

Pyrrolo-quinoline quinone repeat domain

PQQ_rpt_dom

9

IPR002374

2,374

cGMP-dependent kinase

cGMP_dep_kinase

Family

5,018

false

Guanosine cyclase 3',5'-dependent protein kinases are known to play a role in smooth muscle relaxation, ion fluxes in kidneys and intestines, and neuronal function. The predominant form of cGMP-dependent protein kinase is a dimer of identical 75kDa subunits, although larger subunits of 86 and 130kDa have been found [ ]...

[ "GO:0004692", "GO:0005524" ]

[ "cGMP-dependent protein kinase activity", "ATP binding" ]

[ "molecular_function", "molecular_function" ]

2

[ "PIRSF", "PRINTS" ]

[ "PIRSF000559", "PR00104" ]

[ "cGMP-dep_kinase", "CGMPKINASE" ]

[ 3661, 4101 ]

2

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.7.11.12", "R-BTA-392517", "R-BTA-418457", "R-CEL-392517", "R-DME-1474151", "R-DME-392517", "R-DME-9648002", "R-HSA-1474151", "R-HSA-392517", "R-HSA-4086398", "R-HSA-418457", "R-HSA-9648002", "R-MMU-1474151", "R-MMU-392517", "R-MMU-418457", "R-MMU-9648002", "R-RNO-1474151", "R-RN...

[ "EC:2.7.11.12", "REACTOME:R-BTA-392517", "REACTOME:R-BTA-418457", "REACTOME:R-CEL-392517", "REACTOME:R-DME-1474151", "REACTOME:R-DME-392517", "REACTOME:R-DME-9648002", "REACTOME:R-HSA-1474151", "REACTOME:R-HSA-392517", "REACTOME:R-HSA-4086398", "REACTOME:R-HSA-418457", "REACTOME:R-HSA-9648002"...

19

[ "3shr", "4ku7", "4ku8", "4qx5", "4qxk", "4rz7", "4z07", "5bv6", "5dyk", "5dyl", "5dzc", "5ezr", "5f0a", "5fet", "5j48", "5jax", "5jd7", "5jix", "5jiz", "5l0n", "6bq8", "7lv3", "7ssb", "7t4t", "7t4u", "7t4v", "7t4w", "8em8" ]

28

[ "PUB00002494" ]

[ "2732245" ]

[ "cGMP-dependent protein kinase genes in Drosophila." ]

[ 1989 ]

1

[]

0

null

[ "Eukaryota" ]

[ 5018 ]

1

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 5, 22, 14, 6, 7, 8 ]

6

true

Family

cGMP-dependent kinase

cGMP_dep_kinase

7

IPR002376

2,376

Formyl transferase, N-terminal

Formyl_transf_N

Domain

96,474

false

A number of formyl transferases belong to this group. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl minoacyl-tRNA. The formyl group appears to play a dual role in the initiator identity of N-ormylmethionyl-tRNA by promoting its recognition by IF2 a...

[ "GO:0009058" ]

[ "biosynthetic process" ]

[ "biological_process" ]

1

[ "PFAM" ]

[ "PF00551" ]

[ "Formyl_trans_N" ]

[ 96474 ]

1

[ "EC", "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.1.2", "2.1.2.9", "R-BTA-73817", "R-DME-73817", "R-GGA-419140", "R-HSA-196757", "R-HSA-5368286", "R-HSA-73817", "R-MMU-196757", "R-MMU-73817", "R-RNO-196757", "R-XTR-196757" ]

[ "EC:2.1.2", "EC:2.1.2.9", "REACTOME:R-BTA-73817", "REACTOME:R-DME-73817", "REACTOME:R-GGA-419140", "REACTOME:R-HSA-196757", "REACTOME:R-HSA-5368286", "REACTOME:R-HSA-73817", "REACTOME:R-MMU-196757", "REACTOME:R-MMU-73817", "REACTOME:R-RNO-196757", "REACTOME:R-XTR-196757" ]

12

[ "1c2t", "1c3e", "1cdd", "1cde", "1fmt", "1gar", "1grc", "1jkx", "1mej", "1men", "1meo", "1njs", "1rbm", "1rbq", "1rby", "1rbz", "1rc0", "1rc1", "1s3i", "1yrw", "1z7e", "1zgh", "1zlx", "1zly", "2bln", "2bw0", "2cfi", "2fmt", "2gar", "2ywr", "3auf", "3av3"...

149

[]

0

[]

[ "IPR041711", "IPR041729" ]

0

2

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 1287, 79293, 14205, 28, 1661 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 19, 2, 8, 8, 4, 21, 13, 3, 14, 14, 2, 2, 19 ]

13

true

Domain

Formyl transferase, N-terminal

Formyl_transf_N

3

IPR002379

2,379

V-ATPase proteolipid subunit C-like domain

ATPase_proteolipid_c-like_dom

Domain

65,500

false

The F-ATPases (or F1F0-ATPases) and V-ATPases (or V1V0-ATPases) are each composed of two linked complexes: the F1 or V1 complex contains the catalytic core that synthesizes/hydrolyses ATP, and the F0 or V0 complex that forms the membrane-spanning pore. The F- and V-ATPases all contain rotary motors, one that drives pro...

[ "GO:0015078", "GO:1902600", "GO:0033177" ]

[ "proton transmembrane transporter activity", "proton transmembrane transport", "proton-transporting two-sector ATPase complex, proton-transporting domain" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PFAM" ]

[ "PF00137" ]

[ "ATP-synt_C" ]

[ 65500 ]

1

[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...

[ "GenProp0128", "R-BTA-1222556", "R-BTA-1268020", "R-BTA-163210", "R-BTA-77387", "R-BTA-8949613", "R-BTA-917977", "R-BTA-9639288", "R-BTA-983712", "R-CEL-1222556", "R-CEL-1268020", "R-CEL-163210", "R-CEL-6798695", "R-CEL-77387", "R-CEL-8949613", "R-CEL-917977", "R-CEL-9639288", "R-C...

[ "GP:GenProp0128", "REACTOME:R-BTA-1222556", "REACTOME:R-BTA-1268020", "REACTOME:R-BTA-163210", "REACTOME:R-BTA-77387", "REACTOME:R-BTA-8949613", "REACTOME:R-BTA-917977", "REACTOME:R-BTA-9639288", "REACTOME:R-BTA-983712", "REACTOME:R-CEL-1222556", "REACTOME:R-CEL-1268020", "REACTOME:R-CEL-16321...

68

[ "1a91", "1aty", "1c0v", "1c17", "1c99", "1ijp", "1l6t", "1qo1", "1wu0", "1yce", "2bl2", "2cyd", "2db4", "2w5j", "2wgm", "2wie", "2wpd", "2x2v", "2xnd", "2xok", "2xqs", "2xqt", "2xqu", "3aou", "3j9t", "3j9u", "3j9v", "3u2f", "3u2y", "3u32", "3ud0", "3v3c"...

426

[ "PUB00009752", "PUB00020603", "PUB00020604", "PUB00020609", "PUB00020629", "PUB00020631", "PUB00056210", "PUB00068786", "PUB00068787", "PUB00068788", "PUB00068789" ]

[ "11309608", "15473999", "15078220", "15629643", "15951435", "14635779", "19783985", "20450191", "18937357", "1385979", "9741106" ]

[ "Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.", "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.", "Mechanisms of ATPases--a multi-disciplinary approach.", "A structural model of the v...

[ 2001, 2004, 2004, 2005, 2005, 2003, 2009, 2010, 2008, 1992, 1998 ]

11

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 955, 26824, 37079, 642 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 30, 5, 6, 14, 1, 15, 17, 5, 22, 20, 4, 4, 32 ]

13

true

Domain

V-ATPase proteolipid subunit C-like domain

ATPase_proteolipid_c-like_dom

3

IPR002381

2,381

Ribonuclease PH, bacterial-type

RNase_PH_bac-type

Family

17,475

false

Prokaryotic ribonuclease PH ( ) (RNase PH) is a phosphorolytic exoribonuclease that participates in tRNA maturation by removing nucleotide residues following the -CCA terminus of tRNA [ ]. It also has synthetic activity, adding nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates [ ]....

[ "GO:0000049", "GO:0009022", "GO:0008033" ]

[ "tRNA binding", "tRNA nucleotidyltransferase activity", "tRNA processing" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP", "NCBIFAM", "CDD" ]

[ "MF_00564", "TIGR01966", "cd11362" ]

[ "RNase_PH", "RNasePH", "RNase_PH_bact" ]

[ 17280, 17474, 16258 ]

3

[ "EC", "GP", "PROSITEDOC" ]

[ "2.7.7.56", "GenProp1360", "PDOC00983" ]

[ "EC:2.7.7.56", "GP:GenProp1360", "PROSITEDOC:PDOC00983" ]

3

[ "1oyp", "1oyr", "1oys", "1r6l", "1r6m", "1udn", "1udo", "1udq", "1uds", "3b4t", "3dd6" ]

11

[ "PUB00022776", "PUB00030555", "PUB00080485", "PUB00080487", "PUB00088306" ]

[ "12746447", "14573594", "15983136", "1707683", "28808133" ]

[ "Crystal structure of the tRNA processing enzyme RNase PH from Aquifex aeolicus.", "Probing the functional importance of the hexameric ring structure of RNase PH.", "Ribonuclease PH plays a major role in the exonucleolytic maturation of CCA-containing tRNA precursors in Bacillus subtilis.", "RNase PH catalyze...

[ 2003, 2004, 2005, 1990, 2017 ]

5

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Myoviridae sp. ct2798", "unclassified sequences" ]

[ 16, 17013, 38, 1, 407 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Ribonuclease PH, bacterial-type

RNase_PH_bac-type

4

IPR002384

2,384

Osteocalcin/matrix Gla protein

Osteocalcin/MGP

Family

670

false

Bone gamma-carboxyglutamic acid protein (BGP), also known as osteocalcin, and matrix gamma-carboxyglutamic acid protein (MGP) are the only vitamin K-dependent proteins that have been isolated from bone. MGP is a small protein found in bone, dentin and cartilage. It contains five gamma-carboxyglutamic acid (Gla) residue...

[ "GO:0030500", "GO:0005576" ]

[ "regulation of bone mineralization", "extracellular region" ]

[ "biological_process", "cellular_component" ]

2

[ "PRINTS" ]

[ "PR00002" ]

[ "GLABONE" ]

[ 670 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-HSA-159740", "R-HSA-159763", "R-HSA-159782", "R-HSA-8940973", "R-MMU-159740", "R-MMU-159763", "R-MMU-159782", "R-RNO-159740", "R-RNO-159763", "R-RNO-159782", "R-XTR-159740", "R-XTR-159763", "R-XTR-159782" ]

[ "REACTOME:R-HSA-159740", "REACTOME:R-HSA-159763", "REACTOME:R-HSA-159782", "REACTOME:R-HSA-8940973", "REACTOME:R-MMU-159740", "REACTOME:R-MMU-159763", "REACTOME:R-MMU-159782", "REACTOME:R-RNO-159740", "REACTOME:R-RNO-159763", "REACTOME:R-RNO-159782", "REACTOME:R-XTR-159740", "REACTOME:R-XTR-15...

13

[ "1q3m", "1q8h", "1vzm", "4mzz", "8i74", "8i75", "8i76", "9bur", "9bux", "9l23", "9mqb", "9mqc", "9mqe" ]

13

[ "PUB00004648" ]

[ "3317405" ]

[ "Molecular cloning of matrix Gla protein: implications for substrate recognition by the vitamin K-dependent gamma-carboxylase." ]

[ 1987 ]

1

[]

[ "IPR027118", "IPR039176" ]

0

2

0

[ "Euteleostomi" ]

[ 670 ]

1

[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 2, 7, 7 ]

3

true

Family

Osteocalcin/matrix Gla protein

Osteocalcin/MGP

6

IPR002386

2,386

Amicyanin/Pseudoazurin

Family

3,729

false

Based on their primary sequences and their unique metabolic role, amicyanins are considered as a distinct subclass of cupredoxins, although they appear to be closely related to the plant plastocyanins [ ]. The structure of amicyanin is a β-sandwich, built from nine β-strands. The copper atom is located between three lo...

[ "GO:0005507", "GO:0009055" ]

[ "copper ion binding", "electron transfer activity" ]

[ "molecular_function", "molecular_function" ]

2

[ "PRINTS" ]

[ "PR00155" ]

[ "AMICYANIN" ]

[ 3729 ]

1

[]

0

[ "1aac", "1aaj", "1aan", "1adw", "1bqk", "1bqr", "1bxa", "1id2", "1mda", "1mg2", "1mg3", "1paz", "1pmy", "1py0", "1pza", "1pzb", "1pzc", "1sf3", "1sf5", "1sfd", "1sfh", "1t5k", "1zia", "1zib", "2gb2", "2gba", "2gc4", "2gc7", "2idq", "2ids", "2idt", "2idu"...

83

[ "PUB00003327", "PUB00036459", "PUB00038898", "PUB00081025", "PUB00081026", "PUB00081027" ]

[ "8035459", "10364229", "8138527", "16138306", "22910335", "15475344" ]

[ "Solution structure of the type 1 blue copper protein amicyanin from Thiobacillus versutus.", "Crystal structure determinations of oxidized and reduced pseudoazurins from Achromobacter cycloclastes. Concerted movement of copper site in redox forms with the rearrangement of hydrogen bond at a remote histidine.", ...

[ 1994, 1999, 1993, 2005, 2012, 2004 ]

6

[ "IPR001235" ]

[ "IPR012745", "IPR035668" ]

1

2

0

[ "Archaea", "Bacteria", "Eukaryota", "ecological metagenomes", "unclassified Marseilleviridae" ]

[ 698, 2978, 7, 44, 2 ]

5

[]

0

true

Family

Amicyanin/Pseudoazurin

6

IPR002387

2,387

Plastocyanin

Family

2,129

false

Blue or 'type-1' copper proteins are small proteins which bind a single copper atom and which are characterised by an intense electronic absorption band near 600 nm [ , ]. The most well known members of this class of proteins are the plant chloroplastic plastocyanins, and the distantly related bacterial azurins, which ...

[ "GO:0005507", "GO:0009055" ]

[ "copper ion binding", "electron transfer activity" ]

[ "molecular_function", "molecular_function" ]

2

[ "PRINTS", "NCBIFAM", "CDD" ]

[ "PR00157", "TIGR02656", "cd04219" ]

[ "PLASTOCYANIN", "cyanin_plasto", "Plastocyanin" ]

[ 2115, 1223, 1104 ]

3

[]

0

[ "1ag6", "1b3i", "1baw", "1bxu", "1bxv", "1byo", "1byp", "1fa4", "1iuz", "1j5c", "1j5d", "1jxd", "1jxf", "1jxg", "1kdi", "1kdj", "1m9w", "1nin", "1oow", "1pcs", "1pla", "1plb", "1plc", "1pnc", "1pnd", "1tef", "1teg", "1tkw", "1tu2", "1ylb", "2b3i", "2bz7"...

68

[ "PUB00003327", "PUB00003425", "PUB00014468", "PUB00081028" ]

[ "8035459", "8433378", "14567714", "8027022" ]

[ "Solution structure of the type 1 blue copper protein amicyanin from Thiobacillus versutus.", "Evolution of protein complexity: the blue copper-containing oxidases and related proteins.", "Electron transfer between membrane complexes and soluble proteins in photosynthesis.", "Plastocyanin: structural and func...

[ 1994, 1993, 2003, 1994 ]

4

[ "IPR001235" ]

[ "IPR023511" ]

1

0

[ "Bacteria", "Caudoviricetes", "Eukaryota", "Methanobacteriati", "ecological metagenomes" ]

[ 474, 84, 848, 712, 11 ]

5

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 6, 1, 6 ]

3

true

Family

Plastocyanin

5

IPR002388

2,388

Annexin A1

ANX1

Family

881

false

The annexins (or lipocortins) are a family of proteins that bind to phospholipids in a calcium-dependent manner [ ]. The 12 annexins common to vertebrates are classified in the annexin A family and named as annexins A1-A13 (or ANXA1-ANXA13), leaving A12 unassigned in the official nomenclature. Annexins outside vertebra...

[ "GO:0004859", "GO:0005509", "GO:0005544" ]

[ "phospholipase inhibitor activity", "calcium ion binding", "calcium-dependent phospholipid binding" ]

[ "molecular_function", "molecular_function", "molecular_function" ]

3

[ "PRINTS" ]

[ "PR00197" ]

[ "ANNEXINI" ]

[ 881 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-HSA-416476", "R-HSA-418594", "R-HSA-444473", "R-HSA-445355", "R-HSA-6785807", "R-HSA-9925563", "R-MMU-416476", "R-MMU-418594", "R-MMU-444473", "R-RNO-416476", "R-RNO-418594", "R-RNO-444473" ]

[ "REACTOME:R-HSA-416476", "REACTOME:R-HSA-418594", "REACTOME:R-HSA-444473", "REACTOME:R-HSA-445355", "REACTOME:R-HSA-6785807", "REACTOME:R-HSA-9925563", "REACTOME:R-MMU-416476", "REACTOME:R-MMU-418594", "REACTOME:R-MMU-444473", "REACTOME:R-RNO-416476", "REACTOME:R-RNO-418594", "REACTOME:R-RNO-4...

12

[ "1ain", "1hm6", "1mcx", "5vfw" ]

4

[ "PUB00001395", "PUB00013921", "PUB00015121" ]

[ "1646719", "9797403", "15059252" ]

[ "Amino acid sequence analysis of the annexin super-gene family of proteins.", "Identification of the first fungal annexin: analysis of annexin gene duplications and implications for eukaryotic evolution.", "The annexins." ]

[ 1991, 1998, 2004 ]

3

[ "IPR001464" ]

[]

1

0

1

[ "Bilateria" ]

[ 881 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 2, 28, 7, 4 ]

4

true

Family

Annexin A1

ANX1

3

IPR002390

2,390

Annexin A3

ANX3

Family

1,019

false

The annexins (or lipocortins) are a family of proteins that bind to phospholipids in a calcium-dependent manner [ ]. The 12 annexins common to vertebrates are classified in the annexin A family and named as annexins A1-A13 (or ANXA1-ANXA13), leaving A12 unassigned in the official nomenclature. Annexins outside vertebra...

[ "GO:0004859", "GO:0005509", "GO:0005544" ]

[ "phospholipase inhibitor activity", "calcium ion binding", "calcium-dependent phospholipid binding" ]

[ "molecular_function", "molecular_function", "molecular_function" ]

3

[ "PRINTS" ]

[ "PR00199" ]

[ "ANNEXINIII" ]

[ 1019 ]

1

[ "REACTOME" ]

[ "R-HSA-9925563" ]

[ "REACTOME:R-HSA-9925563" ]

1

[ "1aii", "1axn" ]

2

[ "PUB00001395", "PUB00013921", "PUB00015121" ]

[ "1646719", "9797403", "15059252" ]

[ "Amino acid sequence analysis of the annexin super-gene family of proteins.", "Identification of the first fungal annexin: analysis of annexin gene duplications and implications for eukaryotic evolution.", "The annexins." ]

[ 1991, 1998, 2004 ]

3

[ "IPR001464" ]

[]

1

0

1

[ "Bilateria" ]

[ 1019 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 2, 5, 7, 7 ]

4

true

Family

Annexin A3

ANX3

6

IPR002391

2,391

Annexin A4

ANX4

Family

1,630

false

The annexins (or lipocortins) are a family of proteins that bind to phospholipids in a calcium-dependent manner [ ]. The 12 annexins common to vertebrates are classified in the annexin A family and named as annexins A1-A13 (or ANXA1-ANXA13), leaving A12 unassigned in the official nomenclature. Annexins outside vertebra...

[ "GO:0005509", "GO:0005544" ]

[ "calcium ion binding", "calcium-dependent phospholipid binding" ]

[ "molecular_function", "molecular_function" ]

2

[ "PRINTS" ]

[ "PR00200" ]

[ "ANNEXINIV" ]

[ 1630 ]

1

[]

0

[ "1ann", "1aow", "1i4a", "2zhi", "2zhj", "2zoc", "9ga6", "9ga7", "9ga8" ]

9

[ "PUB00001395", "PUB00013921", "PUB00015121", "PUB00035094" ]

[ "1646719", "9797403", "15059252", "12912993" ]

[ "Amino acid sequence analysis of the annexin super-gene family of proteins.", "Identification of the first fungal annexin: analysis of annexin gene duplications and implications for eukaryotic evolution.", "The annexins.", "Intron disruption of the annexin IV gene reveals novel transcripts." ]

[ 1991, 1998, 2004, 2003 ]

4

[ "IPR001464" ]

[]

1

0

1

[ "Metazoa" ]

[ 1630 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 2, 6, 9, 7 ]

4

true

Family

Annexin A4

ANX4

2

IPR002392

2,392

Annexin A5

ANX5

Family

2,007

false

The annexins (or lipocortins) are a family of proteins that bind to phospholipids in a calcium-dependent manner [ ]. The 12 annexins common to vertebrates are classified in the annexin A family and named as annexins A1-A13 (or ANXA1-ANXA13), leaving A12 unassigned in the official nomenclature. Annexins outside vertebra...

[ "GO:0005509", "GO:0005544", "GO:0050819" ]

[ "calcium ion binding", "calcium-dependent phospholipid binding", "negative regulation of coagulation" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "PRINTS" ]

[ "PR00201" ]

[ "ANNEXINV" ]

[ 2007 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-GGA-114608", "R-HSA-114608", "R-MMU-114608", "R-RNO-114608" ]

[ "REACTOME:R-GGA-114608", "REACTOME:R-HSA-114608", "REACTOME:R-MMU-114608", "REACTOME:R-RNO-114608" ]

4

[ "1a8a", "1a8b", "1ala", "1anw", "1anx", "1avh", "1avr", "1bc0", "1bc1", "1bc3", "1bcw", "1bcy", "1bcz", "1g5n", "1hak", "1hvd", "1hve", "1hvf", "1hvg", "1n41", "1n42", "1n44", "1sav", "1yii", "1yj0", "2h0k", "2h0l", "2h0m", "2ie6", "2ie7", "2ran", "2xo2"...

39

[ "PUB00001395", "PUB00013921", "PUB00015121" ]

[ "1646719", "9797403", "15059252" ]

[ "Amino acid sequence analysis of the annexin super-gene family of proteins.", "Identification of the first fungal annexin: analysis of annexin gene duplications and implications for eukaryotic evolution.", "The annexins." ]

[ 1991, 1998, 2004 ]

3

[ "IPR001464" ]

[]

1

0

1

[ "Bilateria", "Salinarimonas soli" ]

[ 2006, 1 ]

2

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 2, 6, 2, 11 ]

4

true

Family

Annexin A5

ANX5

6

IPR002393

2,393

Annexin A6

ANX6

Family

1,638

false

The annexins (or lipocortins) are a family of proteins that bind to phospholipids in a calcium-dependent manner [ ]. The 12 annexins common to vertebrates are classified in the annexin A family and named as annexins A1-A13 (or ANXA1-ANXA13), leaving A12 unassigned in the official nomenclature. Annexins outside vertebra...

[ "GO:0005509", "GO:0005544" ]

[ "calcium ion binding", "calcium-dependent phospholipid binding" ]

[ "molecular_function", "molecular_function" ]

2

[ "PRINTS" ]

[ "PR00202" ]

[ "ANNEXINVI" ]

[ 1638 ]

1

[ "REACTOME" ]

[ "R-HSA-445355" ]

[ "REACTOME:R-HSA-445355" ]

1

[ "1avc", "1m9i" ]

2

[ "PUB00001395", "PUB00013921", "PUB00015121" ]

[ "1646719", "9797403", "15059252" ]

[ "Amino acid sequence analysis of the annexin super-gene family of proteins.", "Identification of the first fungal annexin: analysis of annexin gene duplications and implications for eukaryotic evolution.", "The annexins." ]

[ 1991, 1998, 2004 ]

3

[ "IPR001464" ]

[]

1

0

1

[ "Gnathostomata" ]

[ 1638 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 4, 14, 8, 9 ]

4

true

Family

Annexin A6

ANX6

7

IPR002394

2,394

Nicotinic acetylcholine receptor

Nicotinic_acetylcholine_rcpt

Family

27,685

false

Nicotinic acetylcholine receptors are ligand-gated ion channels that mediate signal transduction at the post-synaptic membrane of cholinergic synapses, such as the neuromuscular junction [ ]. They belong to a family of neurotransmitter-gated receptors, including glycine, gamma-aminobutyric-acid (GABA), serotonin 5HT3 r...

[ "GO:0005216", "GO:0022848", "GO:0006811", "GO:0016020", "GO:0045211" ]

[ "monoatomic ion channel activity", "acetylcholine-gated monoatomic cation-selective channel activity", "monoatomic ion transport", "membrane", "postsynaptic membrane" ]

[ "molecular_function", "molecular_function", "biological_process", "cellular_component", "cellular_component" ]

5

[ "PRINTS" ]

[ "PR00254" ]

[ "NICOTINICR" ]

[ 27685 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-BTA-629587", "R-BTA-629594", "R-BTA-629597", "R-CEL-112314", "R-CEL-629587", "R-CEL-629594", "R-CEL-629597", "R-CEL-6798695", "R-DME-629587", "R-DME-629594", "R-DME-629597", "R-DME-6798695", "R-DRE-629594", "R-DRE-629597", "R-GGA-629587", "R-GGA-629594", "R-GGA-629597", "R-HSA-6...

[ "REACTOME:R-BTA-629587", "REACTOME:R-BTA-629594", "REACTOME:R-BTA-629597", "REACTOME:R-CEL-112314", "REACTOME:R-CEL-629587", "REACTOME:R-CEL-629594", "REACTOME:R-CEL-629597", "REACTOME:R-CEL-6798695", "REACTOME:R-DME-629587", "REACTOME:R-DME-629594", "REACTOME:R-DME-629597", "REACTOME:R-DME-67...

30

[ "2bg9", "2qc1", "3sq6", "3sq9", "4aq5", "4aq9", "4bog", "4boi", "4bon", "4boo", "4bor", "4bot", "4d01", "4hqp", "4uxu", "4uy2", "5afh", "5afj", "5afk", "5afl", "5afm", "5afn", "5fjv", "5hbt", "5hbv", "5kxi", "5oug", "5ouh", "5oui", "6cnj", "6cnk", "6hy7"...

123

[ "PUB00001202", "PUB00002675", "PUB00003060", "PUB00003455", "PUB00009775", "PUB00010340", "PUB00044612", "PUB00044613", "PUB00044614", "PUB00044615" ]

[ "2311580", "1721053", "2465296", "1846404", "12436411", "10026168", "18446614", "15383648", "18760291", "15165736" ]

[ "Expression of the acetylcholine receptor delta-subunit gene in differentiating chick muscle cells is activated by an element that contains two 16 bp copies of a segment of the alpha-subunit enhancer.", "Determination of the tyrosine phosphorylation sites of the nicotinic acetylcholine receptor.", "Identificati...

[ 1990, 1991, 1989, 1991, 2002, 1999, 2008, 2004, 2008, 2004 ]

10

[ "IPR006201" ]

[]

1

0

1

[ "Eukaryota", "bird metagenome" ]

[ 27684, 1 ]

2

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 28, 58, 42, 53, 51, 67 ]

6

true

Family

Nicotinic acetylcholine receptor

Nicotinic_acetylcholine_rcpt

6

IPR002395

2,395

HMW kininogen

Kininogen

Family

1,427

false

The kininogens are multidomain proteins, belonging to the Type 3 cystatin family [ ]. It contains three tandemly repeated type 2-like cystatin domains of which only the second and third (D2 and D3) exhibit cysteine peptidase inhibitory activity, and which belong to MEROPS inhibitor family I25B.

[]

0

[ "PRINTS" ]

[ "PR00334" ]

[ "KININOGEN" ]

[ 1427 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-DDI-264876", "R-DDI-435368", "R-HSA-114608", "R-HSA-140837", "R-HSA-375276", "R-HSA-381426", "R-HSA-416476", "R-HSA-418594", "R-HSA-8957275", "R-RNO-114608", "R-RNO-140837", "R-RNO-375276", "R-RNO-381426", "R-RNO-416476", "R-RNO-418594", "R-RNO-8957275" ]

[ "REACTOME:R-DDI-264876", "REACTOME:R-DDI-435368", "REACTOME:R-HSA-114608", "REACTOME:R-HSA-140837", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-381426", "REACTOME:R-HSA-416476", "REACTOME:R-HSA-418594", "REACTOME:R-HSA-8957275", "REACTOME:R-RNO-114608", "REACTOME:R-RNO-140837", "REACTOME:R-RNO-37...

16

[]

0

[ "PUB00000274", "PUB00005000", "PUB00005310", "PUB00014312", "PUB00014527", "PUB00014528" ]

[ "7407043", "1304876", "3217925", "14587292", "1733668", "2066106" ]

[ "Functional sites of bovine high molecular weight kininogen as a cofactor in kaolin-mediated activation of factor XII (Hageman factor).", "The sequence HGLGHGHEQQHGLGHGH in the light chain of high molecular weight kininogen serves as a primary structural feature for zinc-dependent binding to an anionic surface.",...

[ 1980, 1992, 1988, 2003, 1992, 1991 ]

6

[]

0

null

[ "Bacteria", "Eukaryota", "Halobacteriales" ]

[ 399, 1018, 10 ]

3

[ "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus" ]

[ 1, 2, 4, 1, 1, 7 ]

6

true

Family

HMW kininogen

Kininogen

6

IPR002396

2,396

Selectin superfamily

Selectin_superfamily

Family

2,780

false

Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. C-type lectins display a wide range of specificities. They require Ca 2+ for their activity. They are found predominantly but not exclu...

[ "GO:0007155", "GO:0016020" ]

[ "cell adhesion", "membrane" ]

[ "biological_process", "cellular_component" ]

2

[ "PRINTS" ]

[ "PR00343" ]

[ "SELECTIN" ]

[ 2780 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-BTA-202733", "R-HSA-114608", "R-HSA-198933", "R-HSA-202733", "R-HSA-6798695", "R-MMU-114608", "R-MMU-198933", "R-MMU-202733", "R-MMU-6798695", "R-RNO-114608", "R-RNO-198933", "R-RNO-202733", "R-RNO-6798695", "R-SSC-202733" ]

[ "REACTOME:R-BTA-202733", "REACTOME:R-HSA-114608", "REACTOME:R-HSA-198933", "REACTOME:R-HSA-202733", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-114608", "REACTOME:R-MMU-198933", "REACTOME:R-MMU-202733", "REACTOME:R-MMU-6798695", "REACTOME:R-RNO-114608", "REACTOME:R-RNO-198933", "REACTOME:R-RNO-2...

14

[ "4c16", "4csy", "6eyi", "6eyj", "6eyk", "8r5l", "8r5m" ]

7

[ "PUB00001115" ]

[ "1372169" ]

[ "Characterization of cDNA and genomic sequences encoding rabbit ELAM-1: conservation of structure and functional interactions with leukocytes." ]

[ 1992 ]

1

[]

[ "IPR016348" ]

0

1

0

[ "Eumetazoa" ]

[ 2780 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 11, 23, 13, 19 ]

4

true

Family

Selectin superfamily

Selectin_superfamily

2

IPR002397

2,397

Cytochrome P450, B-class

Cyt_P450_B

Family

83,715

false

This entry represents class B cytochrome P450 proteins, which are part of 3-component systems in bacteria, mitochondria and certain fungal enzymes. Cytochrome P450 enzymes are a superfamily of haem-containing mono-oxygenases that are found in all kingdoms of life, and which show extraordinary diversity in their reactio...

[ "GO:0004497", "GO:0005506", "GO:0016705", "GO:0020037" ]

[ "monooxygenase activity", "iron ion binding", "oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen", "heme binding" ]

[ "molecular_function", "molecular_function", "molecular_function", "molecular_function" ]

4

[ "PRINTS" ]

[ "PR00359" ]

[ "BP450" ]

[ 83715 ]

1

[]

0

[ "1akd", "1c8j", "1cl6", "1cmj", "1cmn", "1cp4", "1cpt", "1dz4", "1dz6", "1dz8", "1dz9", "1egy", "1ehe", "1ehf", "1ehg", "1eup", "1f24", "1f25", "1f26", "1f4t", "1f4u", "1geb", "1ged", "1gei", "1gej", "1gek", "1gem", "1gjm", "1gwi", "1io7", "1io8", "1io9"...

788

[ "PUB00033965", "PUB00033966", "PUB00033967", "PUB00033969" ]

[ "16042601", "17023115", "15128046", "8637843" ]

[ "Biodiversity of cytochrome P450 redox systems.", "Cytochrome P450--redox partner fusion enzymes.", "Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants.", "Structural domains of P450-containi...

[ 2005, 2007, 2004, 1995 ]

4

[ "IPR001128" ]

[ "IPR030904", "IPR031023" ]

1

2

0

[ "Archaea", "Bacteria", "Eukaryota", "Sym plasmid", "unclassified sequences", "uncultured Caudovirales phage" ]

[ 159, 79815, 2584, 2, 1154, 1 ]

6

[ "Arabidopsis thaliana", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 13, 1, 1, 12, 14 ]

5

true

Family

Cytochrome P450, B-class

Cyt_P450_B

7

IPR002398

2,398

Peptidase C14 family

Pept_C14

Family

14,686

false

This group of sequences represent the p45 (45kDa) precursor of caspases, which can be processed to produce the active p20 (20kDa) and p10 (10kDa) subunits. Caspases (Cysteine-dependent ASPartyl-specific proteASE) are cysteine peptidases that belong to the MEROPS peptidase family C14 (caspase family, clan CD) based on t...

[ "GO:0004197", "GO:0006508" ]

[ "cysteine-type endopeptidase activity", "proteolysis" ]

[ "molecular_function", "biological_process" ]

2

[ "PANTHER", "PANTHER" ]

[ "PTHR10454", "PTHR47901" ]

[ "", "" ]

[ 8222, 6464 ]

2

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...

[ "3.4.22", "R-BTA-5620971", "R-CEL-111465", "R-CEL-140342", "R-CEL-198323", "R-CEL-2028269", "R-CEL-264870", "R-CEL-351906", "R-CEL-418889", "R-CEL-5357905", "R-DME-111458", "R-DME-111459", "R-DME-111465", "R-DME-111469", "R-DME-140342", "R-DME-198323", "R-DME-2028269", "R-DME-26487...

[ "EC:3.4.22", "REACTOME:R-BTA-5620971", "REACTOME:R-CEL-111465", "REACTOME:R-CEL-140342", "REACTOME:R-CEL-198323", "REACTOME:R-CEL-2028269", "REACTOME:R-CEL-264870", "REACTOME:R-CEL-351906", "REACTOME:R-CEL-418889", "REACTOME:R-CEL-5357905", "REACTOME:R-DME-111458", "REACTOME:R-DME-111459", "...

96

[ "1bmq", "1cp3", "1dgn", "1f1j", "1gfw", "1gqf", "1i3o", "1i4o", "1i51", "1ibc", "1ice", "1jxq", "1k86", "1k88", "1kmc", "1m72", "1nme", "1nmq", "1nms", "1nw9", "1pau", "1pyo", "1qx3", "1re1", "1rhj", "1rhk", "1rhm", "1rhq", "1rhr", "1rhu", "1rwk", "1rwm"...

302

[ "PUB00011704", "PUB00014747", "PUB00014748", "PUB00015006", "PUB00015008" ]

[ "11517925", "15077141", "15066636", "10578171", "10872455" ]

[ "Evolutionary lines of cysteine peptidases.", "Caspase activation - stepping on the gas or releasing the brakes? Lessons from humans and flies.", "Death without caspases, caspases without death.", "Caspase structure, proteolytic substrates, and function during apoptotic cell death.", "Mammalian caspases: st...

[ 2001, 2004, 2004, 1999, 1999 ]

5

[]

0

null

[ "Ascovirus", "Eukaryota" ]

[ 6, 14680 ]

2

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 2, 42, 9, 53, 33, 45 ]

6

true

Family

Peptidase C14 family

Pept_C14

3

IPR002399

2,399

Cytochrome P450, mitochondrial

Cyt_P450_mitochondrial

Family

325

false

Cytochrome P450 enzymes are a superfamily of haem-containing mono-oxygenases that are found in all kingdoms of life, and which show extraordinary diversity in their reaction chemistry. In mammals, these proteins are found primarily in microsomes of hepatocytes and other cell types, where they oxidise steroids, fatty ac...

[ "GO:0004497", "GO:0005506", "GO:0016705", "GO:0020037", "GO:0005739" ]

[ "monooxygenase activity", "iron ion binding", "oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen", "heme binding", "mitochondrion" ]

[ "molecular_function", "molecular_function", "molecular_function", "molecular_function", "cellular_component" ]

5

[ "PRINTS" ]

[ "PR00408" ]

[ "MITP450" ]

[ 325 ]

1

[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "1.14.15.4", "PWY-8202", "R-HSA-193993", "R-HSA-194002", "R-HSA-211976", "R-HSA-5579009", "R-HSA-5579017", "R-MMU-193993", "R-MMU-194002", "R-MMU-211976", "R-RNO-193993", "R-RNO-194002", "R-RNO-211976" ]

[ "EC:1.14.15.4", "METACYC:PWY-8202", "REACTOME:R-HSA-193993", "REACTOME:R-HSA-194002", "REACTOME:R-HSA-211976", "REACTOME:R-HSA-5579009", "REACTOME:R-HSA-5579017", "REACTOME:R-MMU-193993", "REACTOME:R-MMU-194002", "REACTOME:R-MMU-211976", "REACTOME:R-RNO-193993", "REACTOME:R-RNO-194002", "REA...

13

[ "4dvq", "4fdh", "4zgx", "6m7x", "6xz8", "6xz9", "7m8i" ]

7

[ "PUB00033965", "PUB00033966", "PUB00033967", "PUB00033969" ]

[ "16042601", "17023115", "15128046", "8637843" ]

[ "Biodiversity of cytochrome P450 redox systems.", "Cytochrome P450--redox partner fusion enzymes.", "Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants.", "Structural domains of P450-containi...

[ 2005, 2007, 2004, 1995 ]

4

[ "IPR001128" ]

[]

1

0

1

[ "Gnathostomata", "bird metagenome" ]

[ 324, 1 ]

2

[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 6, 4, 15 ]

3

true

Family

Cytochrome P450, mitochondrial

Cyt_P450_mitochondrial

8

IPR002401

2,401

Cytochrome P450, E-class, group I

Cyt_P450_E_grp-I

Family

368,128

false

This entry represents class E cytochrome P450 proteins that fall into sequence cluster group I. Group I is richest in members, consisting of cytochrome P450 families CYP1, CYP2, CYP17, CYP21 and CYP71. The members of the first four families are of vertebrate origin, while those from CYP71 are derived from plants. CYP1 ...

[ "GO:0004497", "GO:0005506", "GO:0016705", "GO:0020037" ]

[ "monooxygenase activity", "iron ion binding", "oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen", "heme binding" ]

[ "molecular_function", "molecular_function", "molecular_function", "molecular_function" ]

4

[ "PRINTS" ]

[ "PR00463" ]

[ "EP450I" ]

[ 368128 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-BTA-193048", "R-BTA-193993", "R-BTA-194002", "R-BTA-211935", "R-BTA-211958", "R-BTA-211976", "R-BTA-211981", "R-BTA-211999", "R-BTA-9027307", "R-BTA-9749641", "R-CEL-196791", "R-CEL-211916", "R-CEL-211935", "R-CEL-211945", "R-CEL-211958", "R-CEL-211981", "R-CEL-211999", "R-CEL-2...

[ "REACTOME:R-BTA-193048", "REACTOME:R-BTA-193993", "REACTOME:R-BTA-194002", "REACTOME:R-BTA-211935", "REACTOME:R-BTA-211958", "REACTOME:R-BTA-211976", "REACTOME:R-BTA-211981", "REACTOME:R-BTA-211999", "REACTOME:R-BTA-9027307", "REACTOME:R-BTA-9749641", "REACTOME:R-CEL-196791", "REACTOME:R-CEL-2...

176

[ "1bu7", "1bvy", "1dt6", "1fag", "1fah", "1izo", "1jme", "1jpz", "1n6b", "1n97", "1nr6", "1og2", "1og5", "1p0v", "1p0w", "1p0x", "1po5", "1pq2", "1r9o", "1smi", "1smj", "1suo", "1wiy", "1yqo", "1yqp", "1z10", "1z11", "1zo4", "1zo9", "1zoa", "2bdm", "2bmh"...

416

[ "PUB00033965", "PUB00033966", "PUB00033967", "PUB00033969", "PUB00082317", "PUB00094546", "PUB00094547" ]

[ "16042601", "17023115", "15128046", "8637843", "23932525", "26941773", "29229969" ]

[ "Biodiversity of cytochrome P450 redox systems.", "Cytochrome P450--redox partner fusion enzymes.", "Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants.", "Structural domains of P450-containi...

[ 2005, 2007, 2004, 1995, 2013, 2016, 2017 ]

7

[ "IPR001128" ]

[ "IPR008066", "IPR008067", "IPR008068", "IPR008069", "IPR008070", "IPR008071", "IPR020469", "IPR039983", "IPR044225" ]

1

9

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]

[ 604, 16548, 350843, 34, 99 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 1125, 82, 212, 159, 287, 193, 23, 901, 256, 1, 1, 878 ]

12

true

Family

Cytochrome P450, E-class, group I

Cyt_P450_E_grp-I

4

IPR002402

2,402

Cytochrome P450, E-class, group II

Cyt_P450_E_grp-II

Family

9,114

false

This entry represents class E cytochrome P450 proteins that fall into sequence cluster group II. Group II enzymes are distributed widely in life, i.e., in bacteria (family CYP102), cyanobacteria (CYP110), fungi (CYP52, CYP53 and CYP56), insects (CYP4 and CYP6) and mammals (CYP3, CYP4 and CYP5). Many group II enzymes ca...

[ "GO:0004497", "GO:0005506", "GO:0016705", "GO:0020037" ]

[ "monooxygenase activity", "iron ion binding", "oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen", "heme binding" ]

[ "molecular_function", "molecular_function", "molecular_function", "molecular_function" ]

4

[ "PRINTS" ]

[ "PR00464" ]

[ "EP450II" ]

[ 9114 ]

1

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...

[ "1.14.14", "R-CFA-211945", "R-CFA-211958", "R-CFA-211981", "R-CFA-5423646", "R-CFA-9027307", "R-CFA-9749641", "R-CFA-9754706", "R-CFA-9757110", "R-HSA-211945", "R-HSA-211958", "R-HSA-211981", "R-HSA-5423646", "R-HSA-9027307", "R-HSA-9749641", "R-HSA-9754706", "R-HSA-9757110", "R-MM...

[ "EC:1.14.14", "REACTOME:R-CFA-211945", "REACTOME:R-CFA-211958", "REACTOME:R-CFA-211981", "REACTOME:R-CFA-5423646", "REACTOME:R-CFA-9027307", "REACTOME:R-CFA-9749641", "REACTOME:R-CFA-9754706", "REACTOME:R-CFA-9757110", "REACTOME:R-HSA-211945", "REACTOME:R-HSA-211958", "REACTOME:R-HSA-211981", ...

33

[ "1tqn", "1w0e", "1w0f", "1w0g", "2j0d", "2v0m", "3nxu", "3tjs", "3ua1", "4d6z", "4d75", "4d78", "4d7d", "4i3q", "4i4g", "4i4h", "4k9t", "4k9u", "4k9v", "4k9w", "4k9x", "4ny4", "5a1p", "5a1r", "5g5j", "5te8", "5vc0", "5vcc", "5vcd", "5vce", "5vcg", "5veu"...

127

[ "PUB00033965", "PUB00033966", "PUB00033967", "PUB00033969" ]

[ "16042601", "17023115", "15128046", "8637843" ]

[ "Biodiversity of cytochrome P450 redox systems.", "Cytochrome P450--redox partner fusion enzymes.", "Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants.", "Structural domains of P450-containi...

[ 2005, 2007, 2004, 1995 ]

4

[ "IPR001128" ]

[ "IPR008072" ]

1

0

[ "Cotesia sesamiae Mombasa bracovirus", "Eukaryota", "Halobium palmae", "Lacinutrix neustonica" ]

[ 1, 9111, 1, 1 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]

[ 3, 1, 1, 19, 25, 18, 1, 5, 22, 4 ]

10

true

Family

Cytochrome P450, E-class, group II

Cyt_P450_E_grp-II

1

IPR002404

2,404

IRS-type PTB domain

IRS_PTB

Domain

25,524

false

Insulin receptor substrate (IRS) molecules are mediators in insulin signaling and play a role in maintaining basic cellular functions such as growth and metabolism. They act as docking proteins between the insulin receptor and a complex network of intracellular signaling molecules containing Src homology 2 (SH2) domain...

[]

0

[ "PFAM", "PRINTS", "PROFILE", "SMART", "CDD" ]

[ "PF02174", "PR00628", "PS51064", "SM00310", "cd01204" ]

[ "IRS", "INSULINRSI", "IRS_PTB", "PTBI", "PTB_IRS" ]

[ 25380, 4234, 13672, 12586, 3988 ]

5

[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...

[ "PDOC51064", "R-BTA-210993", "R-BTA-8853659", "R-CEL-2453902", "R-DME-109704", "R-DME-110478", "R-DME-112399", "R-DME-112412", "R-DME-1257604", "R-DME-2453902", "R-DME-5673001", "R-DME-6811558", "R-DME-74749", "R-DME-9006335", "R-DME-9027276", "R-DME-9027284", "R-HSA-109704", "R-HS...

[ "PROSITEDOC:PDOC51064", "REACTOME:R-BTA-210993", "REACTOME:R-BTA-8853659", "REACTOME:R-CEL-2453902", "REACTOME:R-DME-109704", "REACTOME:R-DME-110478", "REACTOME:R-DME-112399", "REACTOME:R-DME-112412", "REACTOME:R-DME-1257604", "REACTOME:R-DME-2453902", "REACTOME:R-DME-5673001", "REACTOME:R-DME...

147

[ "1irs", "1j0w", "1mix", "1miz", "1mk7", "1mk9", "1p5t", "1qqg", "1uef", "1xr0", "1y19", "2dlw", "2g35", "2h7d", "2h7e", "2k00", "2kgx", "2kup", "2kuq", "2mfq", "2mwn", "2v76", "2ys5", "2yt2", "3g9w", "3ivf", "3ml4", "4f7g", "5ejr", "5ejs", "5mv9", "5u1m"...

48

[ "PUB00000936", "PUB00003928", "PUB00018031", "PUB00018519", "PUB00081240" ]

[ "8646778", "8599766", "15567406", "14607833", "10610414" ]

[ "Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor.", "Structural basis for IL-4 receptor phosphopeptide recognition by the IRS-1 PTB domain.", "Structural and evolutionary division of phosphotyrosine binding (PTB) domains.", "Structural basis for the specific recogni...

[ 1996, 1996, 2005, 2004, 1999 ]

5

[]

[ "IPR037748", "IPR037751", "IPR038742" ]

0

3

0

[ "Eukaryota" ]

[ 25524 ]

1

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]

[ 5, 16, 67, 32, 46, 38, 1, 55, 40 ]

9

true

Domain

IRS-type PTB domain

IRS_PTB

2

IPR002406

2,406

Natriuretic peptide, C type

C_natriurtcpep

Family

867

false

Atrial natriuretic peptides (ANPs) are vertebrate hormones that play an important role in the control of cardiovascular homeostatis, and sodium and water balance in general [ , ]. There are different NPs that vary in length but share a common core. All are processed from a single precursor. A disulphide bond resident i...

[ "GO:0005179", "GO:0005576" ]

[ "hormone activity", "extracellular region" ]

[ "molecular_function", "cellular_component" ]

2

[ "PRINTS" ]

[ "PR00713" ]

[ "CNATPEPTIDE" ]

[ 867 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-BTA-5578768", "R-HSA-5578768", "R-MMU-5578768", "R-RNO-5578768", "R-SSC-5578768" ]

[ "REACTOME:R-BTA-5578768", "REACTOME:R-HSA-5578768", "REACTOME:R-MMU-5578768", "REACTOME:R-RNO-5578768", "REACTOME:R-SSC-5578768" ]

5

[]

0

[ "PUB00000076", "PUB00001609", "PUB00002530", "PUB00002722" ]

[ "1652921", "1828035", "2536732", "1352773" ]

[ "Atrial natriuretic factor and related peptide hormones.", "A novel natriuretic peptide isolated from eel cardiac ventricles.", "Atrial natriuretic factor.", "A new member of the natriuretic peptide family is present in the venom of the green mamba (Dendroaspis angusticeps)." ]

[ 1991, 1991, 1989, 1992 ]

4

[ "IPR000663" ]

[]

1

0

1

[ "Vertebrata" ]

[ 867 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 2, 2, 3, 3 ]

4

true

Family

Natriuretic peptide, C type

C_natriurtcpep

4

IPR002407

2,407

Natriuretic peptide, atrial type

Natriuretic_peptide_atrial

Family

441

false

null

[ "GO:0005179", "GO:0005576" ]

[ "hormone activity", "extracellular region" ]

[ "molecular_function", "cellular_component" ]

2

[ "PRINTS" ]

[ "PR00711" ]

[ "ANATPEPTIDE" ]

[ 441 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-BTA-5578768", "R-CFA-5578768", "R-HSA-2032785", "R-HSA-5578768", "R-HSA-977225", "R-MMU-5578768", "R-RNO-5578768" ]

[ "REACTOME:R-BTA-5578768", "REACTOME:R-CFA-5578768", "REACTOME:R-HSA-2032785", "REACTOME:R-HSA-5578768", "REACTOME:R-HSA-977225", "REACTOME:R-MMU-5578768", "REACTOME:R-RNO-5578768" ]

7

[]

0

[ "PUB00000076", "PUB00001609", "PUB00002530", "PUB00002722" ]

[ "1652921", "1828035", "2536732", "1352773" ]

[ "Atrial natriuretic factor and related peptide hormones.", "A novel natriuretic peptide isolated from eel cardiac ventricles.", "Atrial natriuretic factor.", "A new member of the natriuretic peptide family is present in the venom of the green mamba (Dendroaspis angusticeps)." ]

[ 1991, 1991, 1989, 1992 ]

4

[ "IPR000663" ]

[]

1

0

1

[ "Vertebrata" ]

[ 441 ]

1

[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 2, 3, 3 ]

3

true

Family

Natriuretic peptide, atrial type

Natriuretic_peptide_atrial

9

IPR002408

2,408

Natriuretic peptide, brain type

Natriuretic_peptide_brain

Family

1,469

false

Atrial natriuretic peptides (ANPs) are vertebrate hormones that play an important role in the control of cardiovascular homeostatis, and sodium and water balance in general [ , ]. There are different NPs that vary in length but share a common core. All are processed from a single precursor. A disulphide bond resident i...

[ "GO:0005179", "GO:0005576" ]

[ "hormone activity", "extracellular region" ]

[ "molecular_function", "cellular_component" ]

2

[ "PRINTS" ]

[ "PR00712" ]

[ "BNATPEPTIDE" ]

[ 1469 ]

1

[]

0

[ "1jdp", "1q01", "3n56", "3n57", "7brg", "7brh", "7brk", "8s9y", "8tg9", "9bcq", "9rbd", "9rbw" ]

12

[ "PUB00000076", "PUB00001609", "PUB00002530", "PUB00002722", "PUB00153669", "PUB00153670" ]

[ "1652921", "1828035", "2536732", "1352773", "37049825", "10876042" ]

[ "Atrial natriuretic factor and related peptide hormones.", "A novel natriuretic peptide isolated from eel cardiac ventricles.", "Atrial natriuretic factor.", "A new member of the natriuretic peptide family is present in the venom of the green mamba (Dendroaspis angusticeps).", "Taipan Natriuretic Peptides A...

[ 1991, 1991, 1989, 1992, 2023, 2000 ]

6

[ "IPR000663" ]

[]

1

0

1

[ "Bilateria" ]

[ 1469 ]

1

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 3, 1, 4, 3 ]

4

true

Family

Natriuretic peptide, brain type

Natriuretic_peptide_brain

6

IPR002410

2,410

Peptidase S33

Peptidase_S33

Family

32,113

false

Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes [ ]. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identif...

[ "GO:0008233", "GO:0006508" ]

[ "peptidase activity", "proteolysis" ]

[ "molecular_function", "biological_process" ]

2

[ "PRINTS" ]

[ "PR00793" ]

[ "PROAMNOPTASE" ]

[ 32113 ]

1

[ "EC" ]

[ "3.4.11.5" ]

[ "EC:3.4.11.5" ]

1

[ "1azw", "1mt3", "1mtz", "1mu0", "1qtr", "1wm1", "1x2b", "1x2e", "1xqv", "1xqw", "1xqx", "1xqy", "1xrl", "1xrm", "1xrn", "1xro", "1xrp", "1xrq", "1xrr", "2yys", "3nwo", "3wmr", "5yhp", "7a6g", "8jgm", "8jgn" ]

26

[ "PUB00000522", "PUB00003576" ]

[ "8439290", "7845208" ]

[ "Evolutionary families of peptidases.", "Families of serine peptidases." ]

[ 1993, 1994 ]

2

[]

[ "IPR005944", "IPR005945" ]

0

2

0

[ "Archaea", "Bacteria", "Escherichia phage 2G7b", "Eukaryota", "metagenomes" ]

[ 100, 26251, 1, 5523, 238 ]

5

[ "Arabidopsis thaliana", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 13, 2, 1, 1, 1, 9 ]

6

true

Family

Peptidase S33

Peptidase_S33

3

IPR002411

2,411

Cereal allergen/alpha-amylase inhibitor, rice type

Allergen/amylase_inhib_rice

Family

83

false

Seeds of cereals contain a variety of serine protease and alpha-amylase inhibitors. These inhibitors can be grouped into families based on structural similarities. Rice seed allergenic proteins (RA) have sequence homology to seed trypsin/alpha-amylase inhibitors. Some have serine peptidase activity or alpha-amylase, an...

[ "GO:0004867" ]

[ "serine-type endopeptidase inhibitor activity" ]

[ "molecular_function" ]

1

[ "PRINTS" ]

[ "PR00809" ]

[ "RAGALLERGEN" ]

[ 83 ]

1

[]

0

[]

0

[ "PUB00004537", "PUB00004563", "PUB00014133", "PUB00014156" ]

[ "2102817", "7678765", "14705960", "11137459" ]

[ "Cloning and characterization of a cDNA encoding the wheat (Triticum durum Desf.) CM16 protein.", "Gene structure and expression of rice seed allergenic proteins belonging to the alpha-amylase/trypsin inhibitor family.", "Evolutionary families of peptidase inhibitors.", "Purification, biochemical characterisa...

[ 1990, 1993, 2004, 2000 ]

4

[ "IPR006106" ]

[]

1

0

1

[ "BOP clade", "Undibacterium flavidum" ]

[ 82, 1 ]

2

[ "Oryza sativa subsp. japonica" ]

[ 14 ]

1

true

Family

Cereal allergen/alpha-amylase inhibitor, rice type

Allergen/amylase_inhib_rice

2

IPR002413

2,413

Venom allergen 5-like

V5_allergen-like

Family

12,571

false

Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS All...

[]

0

[ "PRINTS" ]

[ "PR00838" ]

[ "V5ALLERGEN" ]

[ 12571 ]

1

[ "REACTOME", "REACTOME", "REACTOME" ]

[ "R-HSA-1989781", "R-HSA-6798695", "R-MMU-6798695" ]

[ "REACTOME:R-HSA-1989781", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-6798695" ]

3

[ "1qnx", "1rc9", "1u53", "1wvr", "2ddb", "2epf", "2vzn", "3nt8", "3q2r", "3q2u", "4ly5", "4nui", "4nuk", "4nun", "4nuo", "4p27", "6any", "6imf" ]

18

[ "PUB00002052", "PUB00003182" ]

[ "8227862", "8454859" ]

[ "Allergens in Hymenoptera venom. XXV: The amino acid sequences of antigen 5 molecules and the structural basis of antigenic cross-reactivity.", "Sequence analysis and antigenic cross-reactivity of a venom allergen, antigen 5, from hornets, wasps, and yellow jackets." ]

[ 1993, 1993 ]

2

[ "IPR001283" ]

[]

1

0

1

[ "Bacteria", "Candidatus Nitrosocosmicus", "Eukaryota", "Mimiviridae", "metagenomes" ]

[ 423, 4, 12129, 6, 9 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]

[ 36, 20, 10, 8, 9, 6, 29, 10, 19 ]

9

true

Family

Venom allergen 5-like

V5_allergen-like

9

IPR002415

2,415

H/ACA ribonucleoprotein complex, subunit Nhp2-like

H/ACA_rnp_Nhp2-like

Family

7,823

false

This entry represents H/ACA ribonucleoprotein complex subunit NHP2 and similar proteins from eukaryotes, including NHP2-like protein 1 from mammals (SNU13 homologue) and 13 kDa ribonucleoprotein-associated protein (SNU13) from yeast. Nhp2 is part of a complex which catalyses pseudouridylation of rRNA and is required fo...

[ "GO:0003723", "GO:0005730" ]

[ "RNA binding", "nucleolus" ]

[ "molecular_function", "cellular_component" ]

2

[ "PRINTS" ]

[ "PR00883" ]

[ "NUCLEARHMG" ]

[ 7823 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-BTA-171319", "R-BTA-6791226", "R-BTA-72163", "R-CEL-6791226", "R-DDI-6791226", "R-DME-6791226", "R-HSA-171319", "R-HSA-6790901", "R-HSA-6791226", "R-HSA-72163", "R-MMU-171319", "R-MMU-6791226", "R-MMU-72163", "R-RNO-6791226", "R-RNO-72163", "R-SCE-6791226", "R-SPO-6791226" ]

[ "REACTOME:R-BTA-171319", "REACTOME:R-BTA-6791226", "REACTOME:R-BTA-72163", "REACTOME:R-CEL-6791226", "REACTOME:R-DDI-6791226", "REACTOME:R-DME-6791226", "REACTOME:R-HSA-171319", "REACTOME:R-HSA-6790901", "REACTOME:R-HSA-6791226", "REACTOME:R-HSA-72163", "REACTOME:R-MMU-171319", "REACTOME:R-MMU...

17

[ "1e7k", "1zwz", "2aif", "2ale", "2jnb", "2lbw", "2lbx", "2ozb", "3jcm", "3jcr", "3o85", "3siu", "3siv", "4nut", "5ewr", "5gan", "5gap", "5nrl", "5o9z", "5oql", "5tzs", "5wlc", "5wyj", "5wyk", "5zwm", "5zwo", "6ah0", "6ahd", "6ke6", "6lqp", "6lqq", "6lqr"...

102

[ "PUB00047033", "PUB00053435", "PUB00053436", "PUB00062919", "PUB00088317", "PUB00090272", "PUB00099949", "PUB00099950", "PUB00099951" ]

[ "17631273", "16647858", "19917616", "17412961", "10871366", "28781166", "14730029", "12215523", "15044956" ]

[ "Analysis of pre-mRNA and pre-rRNA processing factor Snu13p structure and mutants.", "How a single protein complex accommodates many different H/ACA RNAs.", "The box H/ACA ribonucleoprotein complex: interplay of RNA and protein structures in post-transcriptional RNA modification.", "Binding of the human Prp31...

[ 2007, 2006, 2009, 2007, 2000, 2017, 2004, 2002, 2004 ]

9

[ "IPR018492" ]

[]

1

0

1

[ "Eukaryota" ]

[ 7823 ]

1

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 15, 2, 3, 2, 8, 2, 1, 9, 8, 2, 2, 42 ]

12

true

Family

H/ACA ribonucleoprotein complex, subunit Nhp2-like

H/ACA_rnp_Nhp2-like

2

IPR002416

2,416

Type II secretion system protein GspH-like

T2SS_protein-GspH

Family

5,256

false

This entry includes type II secretion system protein H and closely related proteins. The proteins of the type II secretion system (T2SS) are named Gsp in general and Eps in V. cholerae. EpsH is a GspH homologue and one of the minor pseudopilin components of the T2SS. This protein has been structurally characterised [ ,...

[ "GO:0015628", "GO:0015627" ]

[ "protein secretion by the type II secretion system", "type II protein secretion system complex" ]

[ "biological_process", "cellular_component" ]

2

[ "PRINTS" ]

[ "PR00885" ]

[ "BCTERIALGSPH" ]

[ 5256 ]

1

[ "GP" ]

[ "GenProp0053" ]

[ "GP:GenProp0053" ]

1

[]

0

[ "PUB00049160", "PUB00051842", "PUB00093998", "PUB00094002", "PUB00094004", "PUB00094008" ]

[ "18241884", "19217396", "30767847", "28258547", "22523076", "24316251" ]

[ "Structure of the minor pseudopilin EpsH from the Type 2 secretion system of Vibrio cholerae.", "Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody.", "Architecture, Function, and Substrates of the Type II Secretion System.", "1H, 15N and 13C...

[ 2008, 2009, 2019, 2017, 2012, 2014 ]

6

[]

[ "IPR049875" ]

0

1

0

[ "Bacteria", "Caudoviricetes", "Opisthokonta", "unclassified sequences" ]

[ 5160, 3, 2, 91 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Type II secretion system protein GspH-like

T2SS_protein-GspH

2

IPR002417

2,417

Viral spike glycoprotein

Spike_prot

Family

1,211

false

The glycoproteins of viral haemorrhagic scepticaemia virus [ ] and of infectious hematopoietic necrosis virus [ ] are similar, and are responsible for forming spikes on the surface of the virion. The glycoprotein mediates binding of the virus to susceptible host cells and induces uptake of the virus by the cell. The in...

[ "GO:0019031" ]

[ "viral envelope" ]

[ "cellular_component" ]

1

[ "PRINTS" ]

[ "PR00796" ]

[ "SPIKEPROTEIN" ]

[ 1211 ]

1

[]

0

[]

0

[ "PUB00000573", "PUB00003479" ]

[ "1954257", "3033264" ]

[ "Sequence of a cDNA carrying the glycoprotein gene and part of the matrix protein M2 gene of viral haemorrhagic scepticaemia virus, a fish rhabdovirus.", "Nucleotide sequence of a cDNA clone carrying the glycoprotein gene of infectious hematopoietic necrosis virus, a fish rhabdovirus." ]

[ 1991, 1987 ]

2

[]

0

null

[ "Riboviria" ]

[ 1211 ]

1

[]

0

true

Family

Viral spike glycoprotein

Spike_prot

4

IPR002418

2,418

Transcription regulator Myc

Tscrpt_reg_Myc

Family

5,328

false

The class III basic helix-turn-helix (bHLH) transcription factors have proliferative and apoptotic roles and are characterised by the presence of a leucine zipper adjacent to the bHLH domain. The myc oncogene was first discovered in small-cell lung cancer cell lines where it is found to be deregulated [ ]. The Myc prot...

[ "GO:0003700", "GO:0006355" ]

[ "DNA-binding transcription factor activity", "regulation of DNA-templated transcription" ]

[ "molecular_function", "biological_process" ]

2

[ "PIRSF", "PRINTS" ]

[ "PIRSF001705", "PR00044" ]

[ "Myc_protein", "LEUZIPPRMYC" ]

[ 2624, 5296 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-BTA-5689880", "R-BTA-8866911", "R-DRE-8866911", "R-GGA-5689880", "R-GGA-8866911", "R-HSA-1362277", "R-HSA-201556", "R-HSA-2122947", "R-HSA-2173796", "R-HSA-2644606", "R-HSA-2894862", "R-HSA-4411364", "R-HSA-5687128", "R-HSA-5689880", "R-HSA-6785807", "R-HSA-69202", "R-HSA-69656", ...

[ "REACTOME:R-BTA-5689880", "REACTOME:R-BTA-8866911", "REACTOME:R-DRE-8866911", "REACTOME:R-GGA-5689880", "REACTOME:R-GGA-8866911", "REACTOME:R-HSA-1362277", "REACTOME:R-HSA-201556", "REACTOME:R-HSA-2122947", "REACTOME:R-HSA-2173796", "REACTOME:R-HSA-2644606", "REACTOME:R-HSA-2894862", "REACTOME...

28

[ "1nkp", "5i4z", "5i50", "6g6j", "6g6k", "6g6l", "8ots", "8ott" ]

8

[ "PUB00003650", "PUB00005465", "PUB00005562", "PUB00096614" ]

[ "2827002", "9175477", "3018999", "22464321" ]

[ "Structure and expression of the human L-myc gene reveal a complex pattern of alternative mRNA processing.", "Myc target genes.", "Conservation of the c-myc coding sequence in transduced feline v-myc genes.", "MYC on the path to cancer." ]

[ 1988, 1997, 1986, 2012 ]

4

[]

0

null

[ "Eukaryota", "Retroviridae" ]

[ 5311, 17 ]

2

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 1, 9, 2, 67, 15, 16 ]

6

true

Family

Transcription regulator Myc

Tscrpt_reg_Myc

6

IPR002420

2,420

C2 phosphatidylinositol 3-kinase-type domain

PI3K-type_C2_dom

Domain

16,125

false

Phosphatidylinositol 3-kinases (PI3Ks) are lipid kinases that phosphorylate 4,5-bisphonate (PI(4,5) P2 or PIP2) at the 3-position of the inositol ring, and thus generate phosphatidylinositol 3,4,5-trisphosphate (PIP3), which, in turns, initiates a vast array of signaling events. PI3Ks can be grouped into three classes ...

[]

0

[ "PFAM", "PROFILE", "SMART" ]

[ "PF00792", "PS51547", "SM00142" ]

[ "PI3K_C2", "C2_PI3K", "PI3K_C2" ]

[ 15295, 15999, 13770 ]

3

[ "EC", "EC", "GP", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...

[ "2.7.1", "2.7.1.137", "GenProp1758", "PWY-6352", "R-BTA-109704", "R-BTA-112399", "R-BTA-114604", "R-BTA-1250342", "R-BTA-1257604", "R-BTA-1433557", "R-BTA-1660499", "R-BTA-180292", "R-BTA-186763", "R-BTA-1963642", "R-BTA-198203", "R-BTA-201556", "R-BTA-202424", "R-BTA-2029485", "...

[ "EC:2.7.1", "EC:2.7.1.137", "GP:GenProp1758", "METACYC:PWY-6352", "REACTOME:R-BTA-109704", "REACTOME:R-BTA-112399", "REACTOME:R-BTA-114604", "REACTOME:R-BTA-1250342", "REACTOME:R-BTA-1257604", "REACTOME:R-BTA-1433557", "REACTOME:R-BTA-1660499", "REACTOME:R-BTA-180292", "REACTOME:R-BTA-186763...

251

[ "1e7u", "1e7v", "1e8w", "1e8x", "1e8y", "1e8z", "1e90", "1he8", "2a4z", "2a5u", "2chw", "2chx", "2chz", "2enq", "2rd0", "2v4l", "2wxf", "2wxg", "2wxh", "2wxi", "2wxj", "2wxk", "2wxl", "2wxm", "2wxn", "2wxo", "2wxp", "2wxq", "2wxr", "2x38", "2y3a", "3apc"...

328

[ "PUB00043265", "PUB00046181", "PUB00049324", "PUB00054408" ]

[ "17626883", "10580505", "18079394", "20081827" ]

[ "Mechanism of two classes of cancer mutations in the phosphoinositide 3-kinase catalytic subunit.", "Structural insights into phosphoinositide 3-kinase catalysis and signalling.", "The structure of a human p110alpha/p85alpha complex elucidates the effects of oncogenic PI3Kalpha mutations.", "The p110 delta st...

[ 2007, 1999, 2007, 2010 ]

4

[]

0

null

[ "Eukaryota", "Viruses", "bird metagenome" ]

[ 16122, 2, 1 ]

3

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 5, 3, 31, 8, 48, 34, 1, 8, 33, 1, 1, 11 ]

12

true

Domain

C2 phosphatidylinositol 3-kinase-type domain

PI3K-type_C2_dom

8

IPR002421

2,421

5'-3' exonuclease

5-3_exonuclease

Domain

40,965

false

This entry represents flap endonucleases from eukaryotes, bacteria, viruses and archaea. Flap endonucleases (FENs) catalyse the exonucleolytic hydrolysis of blunt-ended duplex DNA substrates and the endonucleolytic cleavage of 5'-bifurcated nucleic acids at the junction formed between single and double-stranded DNA [ ]...

[ "GO:0003677", "GO:0008409" ]

[ "DNA binding", "5'-3' exonuclease activity" ]

[ "molecular_function", "molecular_function" ]

2

[ "SMART" ]

[ "SM00475" ]

[ "53EXOc" ]

[ 40965 ]

1

[ "REACTOME", "REACTOME", "REACTOME" ]

[ "R-GGA-5685939", "R-PFA-5651801", "R-PFA-69166" ]

[ "REACTOME:R-GGA-5685939", "REACTOME:R-PFA-5651801", "REACTOME:R-PFA-69166" ]

3

[ "1bgx", "1exn", "1rxv", "1rxw", "1taq", "1tau", "1tfr", "1ut5", "1ut8", "1xo1", "3h8j", "3h8s", "3zd8", "3zd9", "3zda", "3zdb", "3zdc", "3zdd", "3zde", "5hml", "5hmm", "5hnk", "5hp4", "6c33", "6c34", "6c35", "6c36", "6vde", "9l55", "9l56" ]

30

[ "PUB00011714", "PUB00031897", "PUB00047705", "PUB00053938", "PUB00053939", "PUB00053941", "PUB00069558", "PUB00069563", "PUB00094486", "PUB00094488" ]

[ "9874768", "15077103", "17693399", "9592142", "9840179", "17567612", "23821668", "19000038", "10364212", "17559871" ]

[ "Mutagenesis of conserved lysine residues in bacteriophage T5 5'-3' exonuclease suggests separate mechanisms of endo-and exonucleolytic cleavage.", "Roles of divalent metal ions in flap endonuclease-substrate interactions.", "Crystal structure of bacteriophage T4 5' nuclease in complex with a branched DNA revea...

[ 1999, 2004, 2007, 1998, 1998, 2007, 2013, 2009, 1999, 2007 ]

10

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 199, 36251, 2806, 711, 998 ]

5

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 24, 2, 12, 33 ]

4

true

Domain

5'-3' exonuclease

5-3_exonuclease

2