accession stringlengths 6 10 | name stringlengths 6 11 | Full Name stringlengths 1 147 ⌀ | taxon stringlengths 3 46 ⌀ | sequence stringlengths 16 2.75k | function stringlengths 6 5.51k | AlphaFoldDB stringlengths 6 10 |
|---|---|---|---|---|---|---|
Q09163 | DLK1_MOUSE | Fetal antigen 1 | Mus | MIATGALLRVLLLLLAFGHSTYGAECDPPCDPQYGFCEADNVCRCHVGWEGPLCDKCVTAPGCVNGVCKEPWQCICKDGWDGKFCEIDVRACTSTPCANNGTCVDLEKGQYECSCTPGFSGKDCQHKAGPCVINGSPCQHGGACVDDEGQASHASCLCPPGFSGNFCEIVAATNSCTPNPCENDGVCTDIGGDFRCRCPAGFVDKTCSRPVSNCASGPCQNGGTCLQHTQVSFECLCKPPFMGPTCAKKRGASPVQVTHLPSGYGLTYRLTPGVHELPVQQPEQHILKVSMKELNKSTPLLTEGQAICFTILGVLTSLVV... | May have a role in neuroendocrine differentiation. Inhibits adipocyte differentiation. | Q09163 |
A4SFS4 | ISPE_CHLPM | 4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase | Chlorobium | MKIKTPLTVKAFAKINLGLFITRKRDDGYHTLSTLFAPIDWYDILSFSAADAIEMSCTNPDLPVDDSNLCVRAARLLQDEGGVKEGVSMLLDKRVPFGAGLGGGSSDAATVLRVLNSFWDINLSSVDLHRFAVSLGADVPYFLEMQGLAYAGGIGDELVDLNMTIPWFIVTVFPCEHISTAWAYGHFHRRFELERPDLRALAPQLSSDGKTELLPLFENDFESAVFEQFGNVRQVKTDLLSAGALFSSLSGSGSAVYGLFEGESAAREVMAAMEAKCYPVSLTPPGFSMRQ | Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. | A4SFS4 |
A4VHI1 | PDXA_PSEU5 | 4-(phosphohydroxy)-L-threonine dehydrogenase | Pseudomonas | MPTSRPFVLTPGEPAGIGPDLCLLLARQAQPRPLVAIASRALLAQRAEQLGLSIELRDAGPQDWPGEPAPANCLYVWDTPLATAVTAGQLDPRNAHYVLETLTRAGRGCLDGSFAGIITAPVHKGVINEAGIPFSGHTEFLAELTLTEQVVMMLATRGLRVALVTTHLPLRDVAEAITAERLQRVTRILHADLVSKFGIARPRILVCGLNPHAGEGGHLGREEIEVIEPTLAGLREEGIELIGPLPADTLFTPKHLEHCDAVLAMYHDQGLPVLKYKGFGAAVNVTLGLPIVRTSVDHGTALDLAGTGRVDIGSLQVALE... | Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP). | A4VHI1 |
Q59RH5 | HAT2_CANAL | Histone acetyltransferase type B subunit 2 | Candida | MSEQPTEPLSIKEEYQLWRKNCRYMYEFVSETALMWPSLTIQWLPNYTTTNGLIDAKLLLGTHTSNQSANQLKVASTQLSADPNVKANSKIKTVQKLENNAEICRARYMPQDANIVATINGLGEVDLYNLDTETRYSHFAPHTKNGYGLSWNPKQKGLLVTGADDNFVCVTDTTTNKTTFKSDIQKDIVNDVKWHQFNGNLFASVSEDSHVYLFDARDNKVVSQYYAESSNGINSLAFSPFAENLVAIGNTSSNINLLDLRKLGENSGLLHTMMGHSEGITCMEFSPHHDGILATGSQDRRIIIWDLFKVGEEQQQEDAE... | Regulatory subunit of the histone acetylase B (HAT-B) complex. The complex acetylates 'Lys-14' of histone H4 which is required for telomeric silencing. | Q59RH5 |
O24308 | TOP2_PEA | PsTopII | Pisum | MEKRPLQTSNAANIPSKTIEEMYQKKTQLEHILLRPDTYVGSIEKHTQNLWVYENDEMVHRAVSYVPGLYKIFDEILVNAADNKQRDPSMDSLKVTIDPEANTVSVYNNGDGVPVEIHQEEKVYVPELIFGHLLTSSNYDDNVKKTTGGRNGYGAKLTNIFSTEFIIETADGRRLKKYKQVFSNNMGTKCEPVITKCKASENWTKVTFKPDLEKFKMAYLEEDVVALMKKRVLDMAGCFGKTVKVELNGTLIRFKSFRDYADLFLKCAEKSKPMPLPRIHAKVGDRWEICISLSDGQFQQVSFVNSIATIKGGTHVDYIT... | Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. | O24308 |
Q9XD74 | SODF_RHIME | Superoxide dismutase [Mn] | Sinorhizobium | MAFELPNLPYDYDALAPYMSRETLEYHHDKHHLAYVTNGNKLAEEAGLSDLSLEDIVKKSYGTNQPLFNNAGQHYNHVHFWKWMKKGGGGTSLPGKLDAAIKSDLGGYDKFRADFSAAGAGQFGSGWAWLSVKNGKLEISKTPNGENPLVHGATPILGVDVWEHSYYIDYRNARPKYLEAFVDNLINWDYVLELYEAAAK | Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. | Q9XD74 |
Q8C432 | RN182_MOUSE | RING-type E3 ubiquitin transferase RNF182 | Mus | MASQPLEEPAESQASDELECKICYNRYNLKQRKPKVLECCHRVCAKCLYKIIDFGDSPQGVIVCPFCRFETCLPDDEVSSLPDDNNILVNLTCGGKGKKCLPENPTELLLTPKRLASLVSPSHTSSNCLVITIMEVQRESSPSLSSTPVVEFYRPASFDSVTTVSHNWTVWNCTSLLFQTSIRVLVWLLGLLYFSSLPLGIYLLVSKKVTLGVVFVSLVPSSLVILMVYGFCQCVCHEFLDCMALPS | E3 ubiquitin-protein ligase that mediates the ubiquitination of ATP6V0C and targets it to degradation via the ubiquitin-proteasome pathway. Also plays a role in the inhibition of TLR-triggered innate immune response by mediating 'Lys'-48-linked ubiquitination and subsequent degradation of NF-kappa-B component RELA. | Q8C432 |
B4HQJ2 | CLP1_DROSE | Protein CLP1 homolog | Sophophora | MSEDHGKDYTLESDSELRFEIEQKDAKVLVSLVSGFAELFGTELVKKKQYEFGVGAKVAIFTYQGCVLHVSGKMDVCYISKETPMVQYVNCHAALEQFRMEAEEKDRYGPVAMVVGPMDVGKSTLCRILLNYAVRVGRRPLYADLDVGQGSIAISGSVATILIERPANVEEGFAKTAPLVYHFGHKSPSGNSVLYNAVVSKMAEVTLQSLNSNKRTKSSGIIINTCGWVKGSGYAHLLHAAKAYGACAIFVLDQERLYNELLRDVPKEVHVVLLPKSGGVVERSKELRHEARDQRIKEYFYGNARAPFYPFSFEVKFQDL... | Required for endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation. | B4HQJ2 |
Q04338 | VTI1_YEAST | Vesicle transport v-SNARE protein VTI1 | Saccharomyces | MSSLLISYESDFKTTLEQAKASLAEAPSQPLSQRNTTLKHVEQQQDELFDLLDQMDVEVNNSIGDASERATYKAKLREWKKTIQSDIKRPLQSLVDSGDRDRLFGDLNASNIDDDQRQQLLSNHAILQKSGDRLKDASRIANETEGIGSQIMMDLRSQRETLENARQTLFQADSYVDKSIKTLKTMTRRLVANKFISYAIIAVLILLILLVLFSKFK | t-SNARE found in various SNARE complexes involved in multiple transport pathways. The composition of the t-SNARE complexes is specific for a limited number of v-SNAREs and therefore allows only the vesicles carrying the matching v-SNARE to fuse. | Q04338 |
A6KWD7 | RS6_PHOV8 | 30S ribosomal protein S6 | Phocaeicola | MNQYETVFILTPVLSDVQMKEAVEKFKGILTAEGAEIINEENWGLKKLAYPIQKKSTGFYQLIEFKAEPQVIEKLEINFRRDERVIRFLTFKMDKYAAEYAAKRRNVKSTKKED | Binds together with S18 to 16S ribosomal RNA. | A6KWD7 |
Q31JC9 | THIC_HYDCU | Thiamine biosynthesis protein ThiC | Hydrogenovibrio | MSTFKNALPASNDILTRDPLPASHKTYISGEIHPEIKVPMRAITLTNGETVTVYDTSGPYTDPNIEIDVAQGIPTVRKDWIANRNDVEAYEGRIIDPKDNGYKNRTQMETAIAGASSLMRQPLRAKAGQNVTQLHYARQGIITPEMEFIAIRENQRRDMTRRYLNDPEREARLKGENFGANLLEDITPEFVRKEVAEGRAVIPANINHPESEPMIIGRNFLVKVNANIGNSATTSSIGEEVEKMVWATRWGADTVMDLSTGQNIHTTRDWILRNAPVPIGTVPIYQALEKVNGVAEDLTWEIFRDTLIEQAEQGVDYFTI... | Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. | Q31JC9 |
A0T0M0 | PSAJ_PHATC | PSI-J | Phaeodactylum | MENFQKYLSTAPVLLTIWLTFTAGFIIEINRFFPDLLGLYF | May help in the organization of the PsaE and PsaF subunits. | A0T0M0 |
C0ZII4 | RS19_BREBN | 30S ribosomal protein S19 | Brevibacillus | MGRSLKKGPFVDDHLMKKVDEQNEKNEKRVIKTWSRRSTIFPDFVGHTFAVYDGRKHVPVYVSEDMVGHKLGEFAPTRTFKGHVDNDKKSKKR | Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. | C0ZII4 |
P70339 | FRAT1_MOUSE | Frequently rearranged in advanced T-cell lymphomas 1 | Mus | MPCRREEEEEAGDEAEGEEDDDSFLLLQQSVTLGGSTDVDQLIVQIGETLQLDAAHDRPASPCAAPGPPPPQVLAALPADKTGTPARRLLRPTGSAETGNPAPPGAVRCVLGERGRVRGRSAPYCVAEISPGASALPQQPGLDGPPGTGKLSTPQPLSGPCRRGWLRNAAASRRLQQRRGSQPETRTGDDDDPHRLLQQLVLSGNLIKEAVRRLHSRQLQLHAKLPAHPFLGPLSAPVHEPPSPGSPRAACSDPGAFMGRAQLRTGDDLLVPGS | Positively regulates the Wnt signaling pathway by stabilizing beta-catenin through the association with GSK-3. May play a role in tumor progression and collaborate with PIM1 and MYC in lymphomagenesis. | P70339 |
P17625 | GYS2_RAT | Glycogen [starch] synthase, liver | Rattus | MLRGRSLSVTSLGGLPAWEAERLPVEDLLLFEVSWEVTNKVGGICTVIQSKAKTTANEWGENYFLIGPYFEHNVKTQVEPCEPANDAVRKAVDAMNKHGCQVHFGRWLIEGSPYVVLFDISSSVWNLDRWKGDFWEACGVGIPHDDREANDMLIFGSLTAWFLKEVTDHADGKHVIAQFHEWQAGTGLILSRARKLPIATIFTTHATLLGRYLCAANIDFYNQLDKFNIDKEAGERQIYHRYCMERASVHCAHVFTTVSEITAIEADHMLKRKPDVVTPNGLNVKKFSAVHEFQNLHATYKARIQDFVRGHFYGHLDFDL... | Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan. | P17625 |
A0Q2Q0 | GATA_CLONN | Glutamyl-tRNA(Gln) amidotransferase subunit A | Clostridium | MELFNKTAHELIDMIKSKEVKVEEVVKSYIARTECIDEKIGAYLYLSKESALKEAKLLDEKIQRGEKLKGLWGVPVGIKDNISVSGMQNTCASKILENYISPYDATVISRLKENNGIILGKLNMDEFAMGSSNENSAFKIVRNPWDLERIPGGSSGGSTAAVASREIPLSLGSETGGSVRQPAALCGVVGLKPTYGRISRYGVISFASTLDQVGTIGRDVTDCAILTEVISGFDKRDSTSARVAVPNYKESLKKDLTGIRIGLPKEFFKEDLDESIRKQIEDAIKILEKNGAEIKICSLPLAEYSLSAYYIISTAEASSN... | Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). | A0Q2Q0 |
Q99PW5 | NEUR3_RAT | N-acetyl-alpha-neuraminidase 3 | Rattus | MEEVSSCSLRSTLFQQEEQNRITYRIPALLYIPPTHTFLAFAEMRTSSRDEDAVYLVFRRGVMKGCSVEWGPQQPLMEATLPGHRTMSPCPVWEKNTGRVYLFFICVQGHVSERWQLLWGRNAARLCFLYSEDSGCSWGEVKDLTEEVVGSEMKHWATFAVGPGHGIQLQSGRLLIPAYAYLISCWFLCFPCSVKPHSLMFYSDDLGVTWHCGKFIKPQVTGECQVAEVPGKAGNLVLYCSARTPNKFRAEAFSTDSGDCFQKPTLNQQLCEPRGGCQGSVVSTRPLKMPYTCQDSSGKDVPSTQKCPLMDRSLEVEEGA... | Exo-alpha-sialidase that catalyzes the hydrolytic cleavage of the terminal sialic acid (N-acetylneuraminic acid, Neu5Ac) of a glycan moiety in the catabolism of glycolipids, glycoproteins and oligosacharides. Displays high catalytic efficiency for gangliosides including alpha-(2->3)-sialylated GD1a and GM3 and alpha-(2... | Q99PW5 |
B9DX75 | UPP_CLOK1 | UPRTase | Clostridium | MSKVTQITHPLILHKLALIRDKRTGSKDFRELVEEVAMLMAYEVTRNLQTEEVEIETPICNTTCKMLSGKKVAVVPILRAGLGMVGGMLKLIPAAKVGHIGLYRDETTLKPVEYFCKLPQDIGEREVIVTDPMLATGGSAIDAITMLKQKGAKNIRLMCLIAAEDGIKSVTEAHPDVDIYTAAIDKELNKNGYIVPGLGDAGDRLYGTK | Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. | B9DX75 |
Q5SS80 | DHR13_MOUSE | Short chain dehydrogenase/reductase family 7C member 5 | Mus | MEMLLLGAGLLLGAYVLVYYNLVKAPSCGGIGSLRGRTVVVTGANSGIGKMTALELARRGARVVLACRSRERGEAAAFDLRQESGNNEVIFMALDLASLASVQAFATAFLSSEPRLDVLIHNAGISSCGRTRETFNLLLRVNHVGPFLLTHLLLPRLRSCAPSRVVIVSSAAHRRGRLDFTRLDCPVVGWQQELRAYADSKLANVLFARELATQLEGTGVTCYAAHPGPVNSELFLRHLPGWLRPILRPLAWLVLRAPQGGAQTPLYCALQEGIEPLSGRYFANCHVEEVSPAARDDQAAQRLWKATKKLAGLAPGDDDD... | Putative oxidoreductase. | Q5SS80 |
Q2S6N5 | ATP62_HAHCH | F-ATPase subunit 6 2 | Hahella | MAGENPTASEYIQHHLQNLTFGNHPEHGWSFAHTAQEAKEMGFWAVHVDSLGWSIALGALFVWLFRKAAVKATSGVPSGLQNFVEIMVDFVDKSVKETFHGKNAVIAPLALTVFCWIFLMNLMDLVPVDFLPRLFQVITGDDHAYFKVVPTTDVNVTLGMSLSVFFLIIYYSIKVKGVGGFLGELTLQPFGKWMLPFNLLLEGVGLIAKPISLALRLFGNLYAGELLFILIALMPFWAQWALSVPWAIFHILVIVLQAFIFMMLTIVYLSMAHEDH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Q2S6N5 |
Q72JA8 | ILVD_THET2 | Dihydroxy-acid dehydratase | Thermus | MRSDQIKKGLKQAPARAMLRAVGVGDEDFGRPFVGVVNTFTDGMPCNFHLRELAQHLKAGLREAGLFPFEFGAPAISDGISMGTPGMRASLVSREVIADSVELIAQGYLYDGMVGLSACDKTIPGTAMGVIRSGVPGMVLYGGTIAPGEWQGRKLTIVEVFEAVGQRAAGKISEEELLEIERRAIPGPGACGGQYTANTMAMALEALGLSPVGYNAIPAVHPEKERATKEAGKILAWAIAHDWKPKDFLTRKSFLNAVAAVAATGGSTNAVLHLLALAKEAGVELSLDDFDQISRKTPVIADLRPWGTYTAWELYEAGGT... | Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (... | Q72JA8 |
A1UI88 | TRPD_MYCSK | Anthranilate phosphoribosyltransferase | unclassified Mycobacterium | MAWEHLRVTDTPTWPSILGRLTTGQNLGTGQAAWAMDQIMTGTATPAQIAGFAVAMKLKRPTSAEVTELADVMLKHARRIPTDIIGNETVDIVGTGGDGANTVNLSTMAAIVVAAAGVPVMKHGNRAASSLSGGADTLEALGVRIDLGPEQVAASVAEVGIGFAFANQFHPSYKHASAVRRELGVPTVFNLLGPLTNPARPRAGLIGCAWAELAEVMAGVFASRNSSVLVVHGDDGLDELTTTTTSTIWRVQAGTVERLTFDPAAFGFQRAHLSELVGGDAEYNAAEVRAVLGGAKGAVRDAVVLNAAGALVAHAGLSSD... | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | A1UI88 |
A2C436 | SURE_PROM1 | Nucleoside 5'-monophosphate phosphohydrolase | Prochlorococcus | MKPLKILISNDDGVFAEGIRTLATSAASRGHKVTVVCPDQERSATGHGLTLHSPIRAEKADELFGGGIKAWGCTGTPADCVKLALNELLDQKPDLILSGINHGPNLGTDIFCSGTVAAALEGTLDGIPSIAVSVASFQWKNFSFAGKLSLDIAEKAIQQNWPKNLLLNLNIPPCEEKEMGDLVWTRLSIRQYEEQFIRRVDPRGNTYFWMAGEAVTDLQSAGEGPKGWPSDVSQIAICSPSLTPIQPDLFWRGNLDDLPNLI | Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates. | A2C436 |
Q057R6 | ACPS_BUCCC | 4'-phosphopantetheinyl transferase AcpS | Buchnera | MAIIGIGIDVINIFRFKKLIINYGIKIPKKILSKKELIEYSYTHKKEKFLAIRFSIKEAIAKAIGISIFKNNFLNNCEIFYNKKKKIQLTTLGYIKKIFKKSQVKKIFLSVTDSNKHTYAIAILEK | Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein. | Q057R6 |
P56361 | RR8_CHLVU | 30S ribosomal protein S8, chloroplastic | Chlorella | MVNDTISDMLTRIRNANLAKKTSVSLPKTKVHEKMCQILEQEGFIKTFSFSETNTNELIVDLKYQDFASFGNYGVGKPCITNLKRISKPGLRIYTNSREIPKVLGGMGILILSTSKGLMTDRQARKLCLGGEILCSVW | One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. | P56361 |
Q929W8 | TMCAL_LISIN | tRNA(Met) cytidine acetate ligase | Listeria | MKATGIVVEYNPFHNGHQLHLNKARELTKSDVVIAVMSGSFVQRGEPAIIPKWERTKMALAAGVDMVIELPVSFATQHATIFAEESIRLLDALHIDTLFFGSEHGVSEDFSTAAKTVVENEAAFNETIQLALGDKKTSYARAYTDAFTHLFGKELLDVTKPNNILGFHYALAIQKQNPSIALQTMPREHSGYHDAEASHDYIASATAIRKLLLAGNLEEASRYLPDSSIEVLNNYRGPFLSFEDYWPLLKFRLIQASSDELEGIRGVSEGIQNRMQLAAKKAHSFSDFIEIMKTKRYSNARLQRTALQILLNAQNTPPAE... | Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34. | Q929W8 |
B4ECN0 | EFTS_BURCJ | Elongation factor Ts | Burkholderia cepacia complex | MAAITASMVAELRAKTDAPMMECKKALTEADGDLAKAEELLRVKLGNKASKAASRVTAEGVVASFVGGNAGALVELNCETDFVAKNDDFLAFSKTVAELVATQNPADVAALSALPLDGSTVDAVRLALIGKIGENVSIRRFVRFETANKIATYLHGARIGVIVEYTGADEQVGKDVAMHIAAMKPVALSSADVPAELIETERRVAEQKAAESGKPAEIVAKMVDGSVQKYLKEVSLLNQTFVKNDKQTIEQMLKAANAAVQKFALFVVGEGIEKRQDDFAAEVAAQVAAAKQQ | Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. | B4ECN0 |
Q4L7Z6 | PTPB_STAHJ | Phosphotyrosine phosphatase B | Staphylococcus | MRITFVCTGNTCRSPIAESIAKKMLVDDTINSRGLFAIDGQSVSPESLEVIMEHNLPEPTVAKQFSEKDLNSDLILTMTDMHKQQLVSHYGDNGRIYQLSEYVGEIGDIVDPFGGSIDTYRQTFEQLLYLIGKLRTNS | Dephosphorylates the phosphotyrosine-containing proteins. | Q4L7Z6 |
B5YKI9 | NUOK_THEYD | NDH-1 subunit K | Thermodesulfovibrio | MIPLSWYLLLSATLFSIGLIGFVIRRDLIVMLMCLEIMFNAVNIAFASFSYYNSNLTGQIFVLFSIAVAACEAVIGLAIVLALVRNTGINHSDEIVNLRG | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are t... | B5YKI9 |
Q5HV17 | SYV_CAMJR | Valyl-tRNA synthetase | Campylobacter | MYDKNLEKEYYQICEERGYFEIDGNKTIQEKDKNFCIMMPPPNVTGVLHIGHALTFTLQDIMTRYKRMDGYKVLYQPGLDHAGIATQNVVEKQLLAQGIKKEELGREEFIEKVWEWKEQSGGKILDQMRTLGITPAWSRLRFTMDEGLVNAVKKAFVELYDKRLIVRGNYMINWCTHDGALSDIEVEYKENKGKLYHIKYFLKDSDEFLVVATTRPETFFGDTAVMVHPDDERYAKFVDKEVILPISKKAIKIIADEHVEKEFGTGVVKVTPAHDMNDYEVGLRHNLDFISVFDEKGILNEHCLEFQGLERLEAREKIVA... | Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner. | Q5HV17 |
Q17WU1 | ISPDF_HELAH | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | Helicobacter | MSLIRVNGEAFNLSLESLKEDPFETKKTLETLIKQTSVILLAAGESRRFSQTIKKQWLRSNHTPLWLSVYESFTEALDFKEVILVVSELDYTYIKRHYPKIKLVRGGISRQESVCNALKVISGAYTLTSDVARGLANIEMLNDLFLTLQNTNHYCIAPYLPCYDTAIYYNEALDREAIKLIQTPQLSHTKTLQLALNQGDFKDESSAILQAFPDLVSYIEGSKDLHKLTTSDDLKIFTPFFNPAKDTFIGMGFDTHAFIKDKPMVLGGVVLDCEFGLKAHSDGDALLHAMIDAILGAIKGGDIGEWFPDNDPKYKNASSK... | Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a ... | Q17WU1 |
Q9YEL4 | AROC_AERPE | 5-enolpyruvylshikimate-3-phosphate phospholyase | Aeropyrum | MASRDSLGEVFRVSIFGESHGPGVGALVTGVPPGLEVDEAYINRELERRRPGGPYASPRREADRVEILSGVFRGRTTGAPILLFIRNVDVKPGFYEEFRYKPRPGHADYVAYERYLGHQDYRGGGIFSGRRTAALVAAGAIAKLVLARYGVRVYAYVKSIGGVEARVEPRDSEEFRRAIDRDPLKCPDPEASERMRRLVEEARREGDSLGSVVEAVAFNVPPGLGDPPLGGVDALLARAVMAIPAAKAVEFGEGFALAFMRGSEAHDSPRAVGGRIVHETNRSGGIVGGLTNGMPIVFRVAFKPPSSIPKPRRTVDLRSL... | Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a s... | Q9YEL4 |
O67891 | PANC_AQUAE | Pantoate-activating enzyme | Aquifex | MPLLFKKIKDLRNFLKNKRCEGKEIGFVPTMGYLHEGHRQLIKLARMQNDIVVVSIFVNPTQFGEGEDYDRYPRDLERDLEICEEEGVDVVFAPEVDEIYPKGYRTKVCVGELGKVLEGEFRPGHFDGVATIVVKLFNIVQPNRAYFGEKDYQQLKIIEQVVEDLNIPVEIVPVPIVREEDGLAYSSRNVYLSPEERESALSIYKSFLLAEKMIKAGERDAKRIKEAIRAFIERHPHVKGVDYVEITDQNLNPKETVEKGDRILVAVRVGNARLIDNWKVQS | Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. | O67891 |
Q9H346 | O52D1_HUMAN | null | Homo | MSDSNLSDNHLPDTFFLTGIPGLEAAHFWIAIPFCAMYLVALVGNAALILVIAMDNALHAPMYLFLCLLSLTDLALSSTTVPKMLAILWLHAGEISFGGCLAQMFCVHSIYALESSILLAMAFDRYVAICNPLRYTTILNHAVIGRIGFVGLFRSVAIVSPFIFLLRRLPYCGHRVMTHTYCEHMGIARLACANITVNIVYGLTVALLAMGLDSILIAISYGFILHAVFHLPSHDAQHKALSTCGSHIGIILVFYIPAFFSFLTHRFGHHEVPKHVHIFLANLYVLVPPVLNPILYGARTKEIRSRLLKLLHLGKTSI | Odorant receptor. | Q9H346 |
A0Q562 | PSD_FRATN | Phosphatidylserine decarboxylase beta chain | Francisella | MRDNLFIYLQYLLPHALTSRLVSKLADSENKIIKNHLIKLAIKKFNINLVEAKETDISKYKSFNDFFIRELKDDLRPISNDKNVISSPADGVLSQFGTITDNSLIQAKGKLFSLESLIASSSTTNFTKFATIYLSPKDYHRVHMPIDGKLTKMVYIPGKLFSVNKITTSKVDNLFAKNERLICYFDTIIGEIAVIFVGALLVAGIETVWHGKIAPNYYKDIQTWDYNSAKFNIKFNKGDILGWFNFGSTVIILTSGNNVSFKFEENQNNIKIQVNQDLALITE | Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). | A0Q562 |
Q0B9R9 | 4HYPE_BURCM | 4-hydroxyproline 2-epimerase | Burkholderia cepacia complex | MMKRIQIIDSHTGGEPTRLVVSGFPSLGNGTMAERRDVLAREHNRYRTACILEPRGSDVMVGALLCEPVSPEAAAGVIFFNNSGYLGMCGHGTIGVVRTLHHMGRIEPGVHRIETPVGTVEATLHDDLSVSVRNVLAYRHAKAVAVDVPGYGPVKGDIAWGGNWFFLISDHGQRVAGDNVAALTAYSSAVREGLERAGITGANGGEIDHIELFADDAEHDSRSFVLCPGHAYDRSPCGTGTSAKLACLAADGKLEPGVVWRQASVIGSVFQASYAQADGGIVPTIRGSAHLSAEATLLIEEDDPFGWGIVS | Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a degradation pathway that converts t4LHyp to alpha-ketoglutarate. Displays no proline racemase activity. | Q0B9R9 |
A0B9X4 | ARGB_METTP | NAG kinase | Methanothrix | MKKEQVLIEALPYIREFYDSIMVIKIGGSIMTNHEILENFIQDIILLKYIGIHPVVVHGGGPEISETMKRLGKKAEFVAGLRVTDRETLEIARMVLLGNINAELVSLIGKHGGKGIGLSGKDGMLIVARKKPPMNVNGENVDLGYVGEVEEINPEILMITAGKGYIPVISPIAIDRDGNSLNVNADTVAGAVAVALRAKKLISITDVEGVREDPDDPGRVISQFSPSEFQRLVERGIIKGGMIPKVEACVRAVERGVEKAHIIDGRIPHAIILELLTDAGIGTMISNIT | Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. | A0B9X4 |
B2UVY4 | ENGB_HELPS | Probable GTP-binding protein EngB | Helicobacter | MIAIKDAHFLTSSGQLSQCPASLTSEMVILGRSNVGKSSFINTLLGKNLAKSSATPGKTRLANFFSTTWEDKENALRATFNVIDLPGFGYAKVSKSLKKEWEGFLWELLSVRVSIKLFIHLVDARHLNLEIDKNAKENIQALLRPDQAYLSLFTKFDKLNKNEQHRLFLNAPKPFLINSAHFNALSSKYPTLEVVRQTLLKYLLTNPL | Necessary for normal cell division and for the maintenance of normal septation. | B2UVY4 |
Q6A6M5 | RS10_CUTAK | 30S ribosomal protein S10 | Cutibacterium | MAGQKIRIRLRAYDHEVIDSSARKIVDTVTRTGAKVAGPVPLPTEKNVFCVIRSPHKYKDSREHFEMRTHKRLIDILEPTPKTVDSLMRLDLPAGVDIEIKLP | Involved in the binding of tRNA to the ribosomes. | Q6A6M5 |
B4GHY8 | CTU1_DROPE | Cytoplasmic tRNA adenylyltransferase 1 | Sophophora | MPINCKAKCGKAAALKRPKTGDALCKECFFAAFEAEIHHTITSSKLFRRGEKVAVAASGGKDSTVLAHVMKLLNERHDYGLELVLLSIDEGITGYRDDSLETVKQNRDDYKMPLKILSYEELYGWTMDRIVSQIGRSNNCTFCGVFRRQALDRGARLLCVDSIATGHNADDIAETVLMNVLRGDTARLRRCTDIRTGGGEDSIPRVKPLKYSYEKEIVMYAHYKKLVYFSTECVFAPNAYRGHARAFLKDLEKVRPSVIMDIIYSGEQLRFKDTAKNPVRGTCNRCGFISSQQPCKACVLLEGLNRGLPKLGIGKKSKGD... | Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thioca... | B4GHY8 |
P70541 | EI2BG_RAT | eIF-2B GDP-GTP exchange factor subunit gamma | Rattus | MEFQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKDVQKALCAEFKMKLKPDIVCIPDEADMGTADSLRHIYPKLKTDVLVLGCDLITDVALHEVVDLFRAYDASLAMLMRKGQESTEPVPGQKGKKKTVEQRDFIGVDSTGKRLLFMANEADLDEELVIKGSILQKHPRIHFQTGLVDAHLYCLKKYVVDFLMENKSITSIRSELIPYLVRKQFSSASSQQRQEDKEEDLKKKEPKSLDIYSFIKKDNTLTLAPYDACWNAFRRDKWEDLSRSQVRCYVHIMKEGLCSRVSTLGLYM... | Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP. | P70541 |
A7IBQ1 | KUP_XANP2 | Probable potassium transport system protein kup | Xanthobacter | MALSFSRDRTRPLPFAAEIGALGVVFGDIGTSPLYALKQGVLAVGGTNFLGGDVLGLLSLITWSIILSVTVKYVMLVLRADNDGEGGILALVTLLDLHRSALGMRWYLLAAGLLGAAMLIGDGVLTPAMSVLSAIEGLQVISPELEHWVVTLTVLVLLAVFLSQRLGTERIASFFGPIMLMWFGSLGALGVYGILQAPQVLAGLDPRYGIMLMVNHPGLAGVILGACFLAVTGGEALYADLGHFGRPVIARAWLFVAMPALLLNYFGQGAILLVDPNAVRNPFYDLCPDVFDIPLLFLATAATVIASQSIITGVFSLAKQ... | Transport of potassium into the cell. | A7IBQ1 |
P52430 | PON1_MOUSE | Serum aryldialkylphosphatase 1 | Mus | MAKLLALTLVGLVLALYKNHRSSYQTRLNAFREVTPVELPNCNLVKGIETGAEDLEILPNGLTFFSTGLKYPGIKSFDPSKPGKILLMDLNKKEPAVSELEIIGNTLDISSFNPHGISTFTDEDNTVYLLVVNHPDSSSTVEVFKFQEEERSLLHLKTITHELLPSINDIAAIGPESFYATNDHYFADPYLRSWEMYLGLSWSNVVYYSPDKVQVVAEGFDFANGIGISLDGKYVYIAELLAHKIHVYEKHANWTLTPLKVLNFDTLVDNISVDPVTGDLWVGCHPNGMRIFFYDAENPPGSEVLRIQNILSEDPKITVV... | Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification. | P52430 |
A9NCS8 | PURA_COXBR | IMP--aspartate ligase | Coxiella | MNIVILGTQWGDEGKGKIVDMLTEDVAAVVRFQGGHNAGHTLIIDGEKTILRLIPSGILREGVLCLIGNGVVLSPPALIEEIEELNAKGIPVTEQLRISSACNLLLPYHVALDKAREAELGTKAIGTTGRGIGPAYEDKVARRGIRAMDLLHPDQLLEKIKKATAYHNIQLEHYYHQTPLDYQSIYNQLMEFREKIKPMIGDVSALLGNLRRQNKHIIFEGAQGSLLDIDLGTYPYVTSSNTTAGSAATGSGFGPLYFDRVLGITKAYVTRVGAGPFPTELTNEEGKKMAKRGNEFGSVTGRPRRCGWFDVISMRRTIQI... | Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. | A9NCS8 |
Q6GM29 | SAC1_XENLA | Suppressor of actin mutations 1-like protein | Xenopus | MALAYENLKLHITPEKFYVEACDPGVEDVLTIDRVSTEVTLSGKKDIPPSAITRAIYGILGTIRLVAGMYLIVITRRKKVGDLLNHSIWKATDFDIISYKKTMLHLTDSQLQDNKAFLGMLSHVLSVDGFYFSVSYDLTHTLQRLANTSPEFQEMSLLERADQRFVWNGNLLREFSAQPEIQKFAIPVVHGFIAIHSCSINGKYFDWILISRRSCFRAGVRYYVRGIDSEGHAANFVETEQIVHYNGNKASFVQTRGSIPFYWSQRPNLKYKPKPQISKAVNHMDGFQRHFDSQVISYGKQVVLNLVNQKGSEKPLEQEF... | Phosphoinositide phosphatase which catalyzes the hydrolysis of phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol 3-phosphate (PtdIns(3)P) and has low activity towards phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2). | Q6GM29 |
A3MU14 | DPHB_PYRCJ | Diphthamide biosynthesis methyltransferase | Pyrobaculum | MLYIVGIGPGPGYATERAIRAIEEADCVFYEDYTGPIDVETLRRAAKTPPIRLTRRDLEDESGRKVLECLREGKRAVLATAGDPMLATAHAALIAAARARGHPVEVVPGVSIICAAFSAACLSIYKLGGVATVTYPRGGVYSTRPYELAEANLARGLHTLLLLDVREDGSFMPPRDAAEVLMALEERERRGVFTPQRPAVVVHRLGWGGGVVVGPLGAVAKWDGEGPAVLIIPAQLGPVEKECLEAVAQRI | S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosy... | A3MU14 |
Q2NTB6 | MINE_SODGM | Cell division topological specificity factor | Sodalis | MALLDFFLSRKKSTANIAKERLQIIVAERRRGDNEPHYLPQLKRDLLEVISKYVQIDPEMLSVQLEKKDGDISILELNVTLPETEETTK | Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell. | Q2NTB6 |
A4VQI5 | ADE_PSEU5 | Adenine aminohydrolase | Pseudomonas | MHDWLNNLPKAELHLHLEGSLEPELMFRLAERNKIALPWNDVEALRSAYNFGNLQEFLDLYYAGADVLRTEQDFYDLTWAYLQKCEEQNVVHTEPFFDPQTHTDRGVPFEAALNGISAALADGRELLGISSGLILSFLRHLPEEEAFKTLEQALPYRNAFFAVGLDSSEVGHPPSKFQRVFDKARGEGLLTVAHAGEEGPPEYIWQALDLLKVSRIDHGVRAAEDPKLIARLIEEQIPLTVCPLSNTKLKVFADMRQHNILDLLEQGVKVTVNSDDPAYFGGYVTENFVALHESLGMTEAQARRLAQNSLDARLAY | Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism. | A4VQI5 |
A7GTP6 | ACCD_BACCN | Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta | Bacillus cereus group | MLRDLFVKKKKYAAIPSEQVRKDVPDGVMTKCPKCKKIMYTKELLKNLKVCVNCGYHHPMNAWERLDSILDEGSFREYDKEMVSVNPLQFPNYEEKLENDRKKTELNEAVVTGEGTIDEMLVVVAVMDSRFRMGSMGSVVGEKIARAVEKAYELQVPFIIFTASGGARMQEGILSLMQMAKTSVALKKYSNAGGLFISVMTHPTTGGVSASFASLGDYNLAEPGALIGFAGRRVIEQTVREKLPEDFQTAEFLLEHGQLDAVVHRNEMRESLRKILEVHQGEGMAVWQN | Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA. | A7GTP6 |
P23326 | RK35_SPIOL | Chloroplastic large ribosomal subunit protein bL35c | Spinacia | MAMASATATLSFKTPSLSLSPPSTRCSAAQGISLTHFNKQLKSTLNLSSSSSISSSKVQPIVLKNKRISTVDSSVSTSSPSFTVFAAKGYKMKTHKASAKRFRVTGKGKIVRRRAGKQHLLAKKNTKRKNRLSKLIQVDRSDYDNVIGALPYLKVNRKV | Component of the chloroplast ribosome (chloro-ribosome), a dedicated translation machinery responsible for the synthesis of chloroplast genome-encoded proteins, including proteins of the transcription and translation machinery and components of the photosynthetic apparatus. | P23326 |
P57794 | NIFS_GLUDA | Nitrogenase metalloclusters biosynthesis protein NifS | Gluconacetobacter | MNAVYLDNNATTRVDPAAVSAMLPFFTEQFGNASSMHAFGAEVGGALHTARRQLQALLGAEFDHEIVYTAGGTESDNTAILSALETQAGRNEIVTSAVEHPAVLALCAWLEKTRGTRVHYIGVDARGRLDIDAYRRALSPRTAIASIMWANNETGTIFPVETLAAVAHEAGALFHTDAVQAVGKIPMNLRHSEIDMLSLSGHKLHAPKGIGALYVRRGVRLRPLIRGGHQERGRRAGTENVPGIIGLGVAAELARHHIDEENTRVRALRDRLEQGLLERIGNAWVTGDTENRLPNTANVAFEFIEGEAILLLMNKAGIAA... | Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Seems to participate in the biosynthesis of the nitrogenase metalloclusters by providing the inorganic sulfur required for the Fe-S core formation. | P57794 |
A4SIB9 | MGSA_AERS4 | Methylglyoxal synthase | Aeromonas | MELIAREMAPHKRVALVAHDNMKTPLLNWVMRRKEELKLHHLYATGTTGTMLGKQAQLLITCLFSGPMGGDQQLGALIAEGKIDVLIFFWDPLNAVPHDPDVKALLRLAAVWNIPVATNEATADFIMDCPHMRQAFSVQIPDYAGYLKARTE | Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate. | A4SIB9 |
Q8Z1R2 | ACTP_SALTI | Acetate transporter ActP | Salmonella | MKRVLTALAAALPFAAHAADAISGAVERQPTNWQAIIMFLIFVVFTLGITYWASKRVRSRSDYYTAGGNITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQGPIRILSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHIAVVLVGVLMMMYVLFGGMLATTWVQIIKAVLLLFGASFMAFMVMKHVGFSFNNLFTEAMAVHPKGTAIMSPGGLVQDPISALSLGLGLIFGTAGLPHILMRFFTVSDAREARKSVFYATGFMGYFYILTFIIGFGAI... | Transports acetate. | Q8Z1R2 |
Q9C1W4 | PMP3_SCHPO | Plasma membrane proteolipid 3 | Schizosaccharomyces | MALTGSDIFKVIFAIILPPLGVFLERGCGADVIINILLCCLGYVPGIIHALYIILKY | Plays a role in the regulation of membrane potential. Could mediate a proton leak. Regulated by the spc1-atf1 pathway and so expression is stress-induced. | Q9C1W4 |
P22571 | CNCG_BOVIN | Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma | Bos | MSDNTVLAPPTSNQGPTTPRKGPPKFKQRQTRQFKSKPPKKGVKGFGDDIPGMEGLGTDITVICPWEAFSHLELHELAQFGII | Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones. | P22571 |
Q8DI43 | EFG_THEVB | Elongation factor G | Thermosynechococcus | MARTTPLERVRNIGIAAHIDAGKTTTTERILFYSGVVHKIGEVHEGTTVTDWMEQERERGITITAAAISTSWRDHQINIIDTPGHVDFTIEVERSMRVLDGVIAVFCSVGGVQPQSETVWRQADRYSVPRIVFVNKMDRTGANFYKVHDQIRDRLRANAVPIQLPIGAEDQFKGIVDLVRMRAKIYKDDLGKEIEDTEIPAEMTELAQEYRTKLIEAVAETDDALMEKYFEGEELTEEEIRAALRKGTIAGTIVPMLCGSAFKNKGVQLLLDAVVDYLPAPIDIPAIKGRLPDGTEVERAADDDQPLAALAFKIMSDPYG... | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respective... | Q8DI43 |
B0BCC3 | HEMH_CHLTB | Protoheme ferro-lyase | Chlamydia | MVTYLLANFGGPRTSQEIVSFLQALLTDRDVTGGMIPSVLHRPLFSYIAKRRAPHVARQYAYLGGGSPIFQDTERLAQNLSQELQASVIPFHRYLPETHRETLQALQESQGSIVGIPLFPHYTFAVTGSIIRFFLQHLPEKPISWITQFGVHPQFVSCMQQHIRDCLAAQQIAVEDCYFLFSVHGLPQRHIRLGDPYAQQCQASFEALRGELEGEIAFQSKFGIGKWLDPSTQEVCQSLRTKKRYIVIVPFGFVSDHIETLYEIDHLYVPILLQKEYRVVRIPAINASSRWVSSLAAIVRSSPQETSLEPLLMP | Catalyzes the ferrous insertion into protoporphyrin IX. | B0BCC3 |
P29395 | RL11_THEMA | 50S ribosomal protein L11 | Thermotoga | MAKKVAAQIKLQLPAGKATPAPPVGPALGQHGVNIMEFCKRFNAETADKAGMILPVVITVYEDKSFTFIIKTPPASFLLKKAAGIEKGSSEPKRKIVGKVTRKQIEEIAKTKMPDLNANSLEAAMKIIEGTAKSMGIEVVD | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | P29395 |
B7GJ73 | RS3_ANOFW | 30S ribosomal protein S3 | Anoxybacillus | MGQKVNPIGLRIGIIRDWESRWYAEKDYADLLHEDLKIREYLTKRLSDAAVSRIEIERAANRVNITIHTAKPGMVIGKGGSEVEALRKALNELTGKRVHINIVEIKKPDLEAKLVAENIARQIENRVSFRRAQKQAIQRTMRAGAKGIKTMVSGRLGGADIARSEHYSEGTVPLHTLRADIDYATAEADTTYGKIGVKVWIYRGEVLPTKKKTEEGGN | Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation. | B7GJ73 |
Q74J32 | PYRC_LACJO | Dihydroorotase | Lactobacillus | MTTVIKNGTVYQNGHLIKADVLIDGQKIKAIGTDLEGEEIIDASGMIVSPGLVDVHVHYRDPGQTYKEDIKTGSQAAARGGFTTVGAMPNVTPVPNTAELMDKMVRENQKKGLVHILQYGPVTNDETTDIIPDYAALKKAGAFALSNDGHGVQSAQTMYLAMQKAKENNLIIAAHAQDDSLFNKGIVNEGIAAEKLDLPPVTELAETTQIARDLLLAQKTGVHYHICHVSTKTSVELVRLAKARGIKVTCEVAPHHILLTDSDIPEDNAYFKMNPPLRSKEDQVALLVGLLDGTIDLIATDHAPHAKAEKQGGMRGAAFG... | Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. | Q74J32 |
O36054 | RR4_SPASP | 30S ribosomal protein S4, chloroplastic | unclassified Sparaxis | RFKKIRRLGALPGLTSKRPRSGSDLKNQLRSGKRSQYRIRLEEKQKLRFHYGLTERQLLKYVHIAGKAKGSTGQILLQLLEMRLDNILFRLGMASTIPGARQLVNHRHILVNGRIVDIPSYRCKPRDIITTKNKQRSKALIQNFIASSPHQEELPNHLTIDPLQYKGLVNQIIDSKWIGLKIN | With S5 and S12 plays an important role in translational accuracy. | O36054 |
Q031I6 | RECU_LACLS | Recombination protein U homolog | Lactococcus cremoris subsp. cremoris | MVNYPNGRSQSYSAVPKKQKTLTELSVAKKSAPKSKSLVAFGKRGMNFEAEINATNDYYLSRGLAVIHKKPTPIQIVKVDYPQRSRAKITEAYFRQASTTDYSGVYKGHYVDFEAKETHQKTVFPLKNFHEHQIVHMSNVLAQRGIAFVLLHFADLEETYLLPSSYLITFYYEKNGLKSIPLAYIRENGYKIETNHIPRIPYLEIVNKLCEVQ | Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation. | Q031I6 |
Q6PAC4 | PCARE_MOUSE | Photoreceptor cilium actin regulator | Mus | MGCTPSHNVIVNSVAKSGIQFFKKPKAILPGCQWGSPKCPIPLLVQSSTFCDSGGELHLGERLVEETVSSSKKLQAMAEGVRQLPKAMEGLIPESQTFQVNKPQGHRATDISFRTEGSHGTQEVDFSGKESKENTPQETSKGNRESVCHQPDSQDHCRQSATESKGRVDFPEPLVKAHQHAYAYLHTSLSRYEAIVRLVQQASQTWGLLRPMLNFLLLCFEEAGQLLSEISKDGDVLLQEVRGDLAWPLRKGEPWEQHPDLLQQLLQYTVSKLRALHGTVAALTGSFLEGSSSCLRSTAGHLEGKLSTKRGIDECLLRAL... | Plays an essential role for normal photoreceptor cell maintenance and vision. | Q6PAC4 |
B2W244 | SEY1_PYRTR | Protein sey1 | Pyrenophora | MMNAHFAGVGDNADNAAYEHGIQVIDEDKMFNGNVSTYLNIEKVIPAGFNYHLISVFGSQSTGKSTLLNHLFGTQFGVMSEQERRQTTKGIWMSKNKRESGGSSMAENILVMDVEGTDGRERGEDQDFERKSALFALATSEVLIVNIWEHQVGLYQGANMGLLKTVFEVNLQLFVKDSQSTPRSLLFFVIRDHLGTTPLKNLQNTLVQDLSKLWSTISKPAGLENSRIEDYFDFAFVALPHKILQPEKFDEAVTQLSTRFKEGYNDPRKSGLIDEATAPIFLPQYHRRIPADGFSAYAEGVWDQIVNNKDLDLPTQQELL... | Cooperates with the reticulon proteins and tubule-shaping DP1 family proteins to generate and maintain the structure of the tubular endoplasmic reticulum network. Has GTPase activity, which is required for its function in ER organization. | B2W244 |
B3E6H3 | RS6_TRIL1 | 30S ribosomal protein S6 | Trichlorobacter | MRKYETIFILQPDLAEDDVKSVTDKVQDVVASLKGDFHRLDDWGTRKLAYAIRKFPRGRYYYLRFDGGAQLVAELERRLRLDEKVLRFLSVNITDEPEKKVAERKPVIEAAEAPEAAEAAAE | Binds together with S18 to 16S ribosomal RNA. | B3E6H3 |
O82201 | AP4S_ARATH | Sigma4-adaptin | Arabidopsis | MGIRFILMVNKQGQTRLAQYYEWLTLEERRALEGEIVRKCLARNDQQCSFVEHRNYKIVYRRYASLFFMVGVDDDENELAILEFIHLLVETMDKHFGNVCELDIMFHLEKAHFMLEEMVMNGCIVETSKANILSPIQLMDKAH | Subunit of novel type of clathrin- or non-clathrin-associated protein coat involved in targeting proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system. | O82201 |
P29438 | DPO3B_SERMA | DNA polymerase III subunit beta | Serratia | MKFIVEREHLLKPLQQVSSPLGGRPTLPILGNLLLQVTEGSLLLTGTDLEMEMVARVALSQPHEPGATTVPARKFFDI | Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalyti... | P29438 |
Q2T8V7 | FLGH2_BURTA | Basal body L-ring protein 2 | pseudomallei group | MRILLALTWLAWLGACTSIEQPRPDFADDDLPPIATAPAAGRSGGVFNAVTAWSLASDGRAYRPGDTLTVTLEETTQASKRADTKFGKNGDMAVKPGVLFGSTVPFDSSFGAKRNFDGGGSSSQQNTLRGEITVIVNQVLAGGLLQVKGEKVLSLNQGEEVMRLSGYVRQADIDTNNRVSSRRIANARIKYVGKGALSDSNSAGWLTRFFNSPWMPF | Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. | Q2T8V7 |
Q9M353 | CHX20_ARATH | Protein CATION/H+ EXCHANGER 20 | Arabidopsis | MPFNITSVKTSSNGVWQGDNPLNFAFPLLIVQTALIIAVSRFLAVLFKPLRQPKVIAEIVGGILLGPSALGRNMAYMDRIFPKWSMPILESVASIGLLFFLFLVGLELDLSSIRRSGKRAFGIAVAGITLPFIAGVGVAFVIRNTLYTAADKPGYAEFLVFMGVALSITAFPVLARILAELKLLTTQIGETAMAAAAFNDVAAWILLALAVALAGNGGEGGGEKKSPLVSLWVLLSGAGFVVFMLVVIRPGMKWVAKRGSPENDVVRESYVCLTLAGVMVSGFATDLIGIHSIFGAFVFGLTIPKDGEFGQRLIERIEDF... | Operates as a K(+)/H(+) antiporter that maintains K(+) homeostasis in guard cells and could regulate pH. Plays a critical role in osmoregulation through the control of stomates opening. | Q9M353 |
B1YD24 | RL22_PYRNV | 50S ribosomal protein L22 | Pyrobaculum | MPRHQNYSLSDEAAVQLVFRKYGVKVSAEQIAKAYAPEQKMSWKKSVEVARFIEGMTLRQAKSWLEDVVKMKRPIPIRTFKKKQAHHATPWSGWPVAKWPVKVARRFLDLLENLENNARFRGLDVERVVIVHAAAHKGYRIHNIMPRAFGRATRFDEQTVNVEVIAAELPQQVVPKRYRLNLVKR | The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. | B1YD24 |
Q48PH1 | AROK_PSE14 | Shikimate kinase | Pseudomonas | MRNLILVGPMGAGKSTIGRLLAKELRLPFKDSDKEIELRTGANIPWIFDKEGEPGFREREQAMIAELCEADGLVLATGGGAVMRGENRQALRAGGRVVYLHASIEQQVGRTARDRNRPLLRTADPARVLSELLAIRDPLYREIADVVIETDERPPRMVVLEILARLAELPPR | Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. | Q48PH1 |
Q0SRN4 | QUEA_CLOPS | Queuosine biosynthesis protein QueA | Clostridium | MKVSDFYFELPEELIAQYPLEKRDSSRLMVLDKKTGEIEHRKFHDILEYLNEGDTLVLNNTRVLPARLIGEKEETGGKIEFLLLKRIEGDKWECLAKPGRKAKVGTVFTFGEGKLKAIVREIGEEGNRIIEFKYDGIFEQVLDELGQMPLPPYIHEKLEDKERYQTVYSKEKGSAAAPTAGLHFTEDLLKEIKDKGVNIAYLTLHVGLGTFRPVKVDDVNNHVMHSEYYHLDKENAELINKTKEAGKRVIAVGTTSSRTLETIGDENGRVREQSGWTDIFIYPGYKFKIVDNLITNFHLPESTLIMLVSALAGQDNIMNA... | Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). | Q0SRN4 |
P68249 | PAHO_MELGA | Pancreatic polypeptide | Meleagris | GPSQPTYPGDDAPVEDLIRFYNDLQQYLNVVTRHRY | Pancreatic hormone is synthesized in pancreatic islets of Langerhans and acts as a regulator of pancreatic and gastrointestinal functions. | P68249 |
B6JNQ5 | QUEF_HELP2 | PreQ(0) reductase | Helicobacter | MTPELNLKSLGAKTPYIFEYNSQLLEAFPNPNPNLDPLITLECKEFTSLCPITSQPDFGVIFIRYIPKDKMVESKSLKLYLFSYRNHGSFHESCINTILLDLVRLLEPKYLEVYGDFASRGGIAIKPFVNYAIKEYQGFKEKRLLNAK | Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). | B6JNQ5 |
Q8IBZ9 | CRT_PLAF7 | Probable transporter cg10 | Plasmodium (Laverania) | MKFASKKNNQKNSSKNDERYRELDNLVQEGNGSRLGGGSCLGKCAHVFKLIFKEIKDNIFIYILSIIYLSVCVMNKIFAKRTLNKIGNYSFVTSETHNFICMIMFFIVYSLFGNKKGNSKERHRSFNLQFFAISMLDACSVILAFIGLTRTTGNIQSFVLQLSIPINMFFCFLILRYRYHLYNYLGAVIIVVTIALVEMKLSFETQEENSIIFNLVLISALIPVCFSNMTREIVFKKYKIDILRLNAMVSFFQLFTSCLILPVYTLPFLKQLHLPYNEIWTNIKNGFACLFLGRNTVVENCGLGMAKLCDDCDGAWKTFA... | May regulate endogenous transporter. | Q8IBZ9 |
Q8DDL3 | CRCB_VIBVU | Putative fluoride ion transporter CrcB | Vibrio | MSQFAILGFIALGGAFGACSRYLVSELCVVLLGRGFPYGTLTVNVVGSFIMGLLIAAFESELLATEPWRQIIGLGFLGALTTFSTFSMDNVLLMQQGAFFKMGLNVVLNVTLSITAAWVGFQLLKS | Important for reducing fluoride concentration in the cell, thus reducing its toxicity. | Q8DDL3 |
B3QBT1 | PQQD_RHOPT | Pyrroloquinoline quinone biosynthesis protein D | Rhodopseudomonas | MAPRRISVSETSRPVLPRHARLKFDETRQRWVILAPERVLAPDEIAVEILQLCDGARDVAAIIDALAVRYTADRAEIGRDVVAMLQDLADKGFLTEARETTP | Functions as a PqqA binding protein and presents PqqA to PqqE, in the pyrroloquinoline quinone (PQQ) biosynthetic pathway. | B3QBT1 |
A9A2Y8 | RL37_NITMS | 50S ribosomal protein L37e | Nitrosopumilus | MVKGTTSMGGFTKKKVHIRCRRCGKNSLHKRHHQCASCGFPEAKRRKYSWIKWYT | Binds to the 23S rRNA. | A9A2Y8 |
Q8YI71 | MURE_BRUME | UDP-N-acetylmuramyl-tripeptide synthetase | Brucella | MKLKEIALFNELAPGEAGEVEITGITSDSRAVQRGFLFAALKGVKADGAVFAADAAKRGAVAIIAGKDTAIADAGVPVLHVDDPRHVLAIAAAQFYGKQPEVMVAVTGTSGKTSVASFTRQIWAYAGFPAANIGTTGVFSPTRSDYNSLTTPDPVELHRVLAELASEGVTHAAMEASSHGLDQRRLDGVRLAAGAFTNLGRDHMDYHATIDEYLGAKMRLFNALLPKGAPAIIFADDQFSAQAIEAATLAGCDVKTVGRKGNFIALKRVEHERFRQHVEVRIGEEIFEIELPLAGDFQVANALVAAGLAMVTGVPAAAAM... | Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. | Q8YI71 |
A1JI06 | RRAA_YERE8 | Regulator of ribonuclease activity A | Yersinia | MKYDTSDLCDIYHEEVNVVEPLFSNFGGRTSFGGKITTVKCFEDNGLLFDLLEENGLGRVLVVDGGGSVRRALINAELADLALKNEWEGIVVYGAVRQVDELAELDIGIQAMAAIPVGAADEGIGESDIRVNFGGVTFFSGDHLYADNTGIILSEEPLDIE | Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. Modulates RNA-binding and helicase activities of the degradosome. | A1JI06 |
Q6HA08 | ASTL_HUMAN | ZP2-proteinase | Homo | MEGVGGLWPWVLGLLSLPGVILGAPLASSCAGACGTSFPDGLTPEGTQASGDKDIPAINQGLILEETPESSFLIEGDIIRPSPFRLLSATSNKWPMGGSGVVEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISIIPMYGCFSSVGRSGGMQVVSLAPTCLQKGRGIVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIKSQSSNMLTPYDYSSVMHYGRLAFSRRGLPTITPLWAPSVHIGQRWNLSASDITRVLKLYGCSPSGPRPRGRGSHAHSTGRSPAPASLSLQRLLEALSAES... | Oocyte-specific oolemmal receptor involved in sperm and egg adhesion and fertilization. Plays a role in the polyspermy inhibition. Probably acts as a protease for the post-fertilization cleavage of ZP2. Cleaves the sperm-binding ZP2 at the surface of the zona pellucida after fertilization and cortical granule exocytosi... | Q6HA08 |
Q8C6N3 | SYT15_MOUSE | Synaptotagmin XV | Mus | MAEQLAFLIGGIIGGLLLLIGVSCCLWRRFCATFTYEELPETSDPATISYFSRKEDRLYQYSGTPPGRLPSVPFVVPPSHQGRDWVPLHGGDWAVAPQDPCPVPEHMACTSSAKPGDACEMGSINPELYKSPEDTSETGFPDGCLGRLWFSVEYQQESERLLVGLIKAQQLQVPSETCSTLVKLHLLPDERRFLQSKTKHKICNPQFDENFIFQVSSKSVTQRVLKFSVYHVNKKRKHQLLGQVLFPLKNETLAGDHHRIIWRDLEAKNLEPPSEFGDIQFCLSYNDYLSRLTVVVLRAKGLQLQEDRSVVSVFVKVSLM... | May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. | Q8C6N3 |
Q0STW6 | COBQ_CLOPS | Cobyric acid synthase | Clostridium | MKYKSIMLLGTASSVGKSTVAAAFCRYFKKKGYRVAPYKALNISLNSFVTKDGDEIGRAQVVQAEACEIDPKEYMNPILMKPSAGFKTQVIVRGKVHCTMDAYKYKELNKYLKEKAKEAYDDISNDYDLIVLEGSGSCAEINLRETDIANMHTAKMADADVILVSDINRGGVFASIVGTIMLLTEEERKRVKGVIINKFRGKREFFEPAMRQIEEIIKIPVLGVMPYFDLDIEEEDSASIKLRKGNGKGIDIAIVRLPHMSNFTDFNSLGRIKDVCIRYAENPKDLENANMIIIPGSKNTIDDLIYLKESGFKEALINES... | Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. | Q0STW6 |
Q3BUY8 | SYS_XANC5 | Seryl-tRNA(Ser/Sec) synthetase | Xanthomonas | MLDPALLRQHPADLAERLRSTRSFDLNIAELELLESERKRIQVRTQELQSQRNSKSKAIGQAKAKGEDVAALMAEVAGFGDELKASEEALDAIRAKLEGIALGLPNLPAEDVPLGKDESENVEQSRWGTPRQFDFAVKDHVELGAPHGWLDGETAAKLSGARFTVLRGPVARLHRALAQFMLDLHVGEHGYEETNVPLLVNADSMRGTGQLPKFEDDLFQTEVGESRRYLIPTSEVPLTNIVRDEIIDAERLPLRMTAHSMCFRAEAGSGGRDTRGMIRQHQFEKVELVTACAPEDSDAEHQRMTRCAEVVLEQLGLPYR... | Catalyzes the attachment of serine to tRNA(Ser). 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(Sec). | Q3BUY8 |
Q9M1S3 | ARP1_ARATH | ABA-regulated RNA-binding protein 1 | Arabidopsis | MTTSNNVNGCFGDTKLTKVFVGGLAWDTHKEAMYDHFIKYGDILEAVIISDKLTRRSKGYGFVTFKDAKAATRACEDSTPIINGRRANCNLASLGGRLRKSPTMTSPQQGPKNGNRATPPHVGNHSQWYYPSGFTNQQHQQQNHQAVPFYGYPSAYVAPNMTFNQKVGYVGGTYMNGYYAQMQPQPQSQPQPQYYHHHMYGGGRVMVGAASPMVPFYTVYPYHQSQAIGFPQPSFSKPLSFSTPPISGTVGGESIQKKAIH | Probable RNA-binding protein involved in the regulation of abscisic acid (ABA) response during seed germination. May regulate transcript levels of several germination-responsive genes under ABA. | Q9M1S3 |
A8IQ73 | RLMN_AZOC5 | tRNA m2A37 methyltransferase | Azorhizobium | MYAPMMPSPTAVAAPVAALSILPSLAGLDREKLGLALAAIGVPERERKMRVNQLWHWIYLRGATDFAEMTNVSKTLRTQLAEHYSLARPEIVVEQVSQDGTRKWLLRLPAETPGERPHEVEAVYIPERDRGTLCVSSQVGCTLNCAFCHTGTQRLVRNLTAAEIVAQVLVARDRLGDYPGRERAVGPGLPTEGDRLVTNIVFMGMGEPLYAYDSVAEAIEILADGDGLGLGKRRITVSTSGVVPEIEKLGREVGPMLAISLHAVRDDLRDVLVPINKKYPIAELMEACRTYPAASNAKRITFEYVMLKGVNDSPADARAL... | Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. | A8IQ73 |
Q8K9R1 | RNC_BUCAP | Ribonuclease III | Buchnera | MNHIVANKIQQILGYTFTHQELLKQALTHRSASSKHNERLEFLGDSILSFVIANALYQHFPYIDEGDMSRMRATLVRGNTLAEIAYEFDLGEYLQLGQGELKSGGFRRESILANTVEALIGSIYLDSNIKTVEELILKWYEKRLEKISPGDTQKDPKTRLQEYLQSKHLSLPSYFIVEVYGEAHNQLFTIHCEVSTLSTSFIGKGTSRRKAEQDAARKALIKLGVE | Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism. | Q8K9R1 |
Q9I8B0 | SURF6_XENLA | Surfeit locus protein 6 homolog | Xenopus | MASLASKDSYLQKLAKKVCTQPSQEPRKRKNEFIKRDGSEEPGQPNKKKKKKPRNKKMKAQSDKRTWNVPQITSNPQKLAKNGQTPSSTGTAASSFSTVDILRKRLQEKIQESRSQLSNKSLTPEDAEKRRQRRKQERERKKRKRKELKKKAAQEPEGNEVKDTKESPETTKEKDPVPIVFNNVEVSDELPNKVMQKKAKKERVKGTITPMTGKNYKQLLSRLEARKCKLEELRAKDEGKAKEFESKIKWTNVLYKAEGVKIKDDEGMLKAALKRKEKKQKQREKRWDKRTELTADRMQQRQDKRRRNIMKKKQAKVDKK... | Involved in a nucleolar function. | Q9I8B0 |
A7X4P5 | MAZF_STAA1 | mRNA interferase MazF | Staphylococcus | MIRRGDVYLADLSPVQGSEQGGVRPVVIIQNDTGNKYSPTVIVAAITGRINKAKIPTHVEIEKKKYKLDKDSVILLEQIRTLDKKRLKEKLTYLSDDKMKEVDNALMISLGLNAVAHQKN | Toxic component of a type II toxin-antitoxin (TA) system. Ribosome-independent, sequence-specific endoribonuclease that cleaves mRNA, thus inhibiting protein synthesis and inducing bacterial stasis. It cuts between the first and nucleotides of 5'-UACAU-3' in single-stranded RNA. Neutralized by coexpression with cognate... | A7X4P5 |
A5GR40 | PETD_SYNR3 | 17 kDa polypeptide | unclassified Synechococcus | MHILKEPDLNDPKLRAKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTIACVVALAVLDPAMLADKADPFATPLEILPEWYLYPVFQILRVVPNKLLGIALQTMIPLGLMLVPFIESFNKFQNPFRRPVAMAVFLFGTAFTIYLGIGAALPIDKSLTLGLF | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. | A5GR40 |
A1U4C5 | HFQ_MARN8 | RNA-binding protein Hfq | Marinobacter | MSKGHSLQDPYLNALRKERIPVSIFLVNGIKLQGQIESFDQFVILLKNTVSQMVYKHAISTVVPARNVRLPQQNPAGEGESED | RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs. | A1U4C5 |
Q2IM61 | RL25_ANADE | General stress protein CTC | Anaeromyxobacter | MAENVLSAQKRTEQGKGPARRLRQQGLIPAVVYGGKREPTHVALDPATLLKAIETPHKFNTLLELQVEGASKHVLFKDYTVDPVTRKLLHADFLEVSMDQPVKVNVPVVTVGRAAGVAEGGILSVAAHAIVVEALPNKIPVRIEVDVTELKIGRSLHVSELKAPEGCKFKFQTDYVVVFVAVPEKEEVAAPVAAAVPGAAPAEGAAPAAGAAAPAAGAAPAAGAAPAKGGEAKGGDKGKK | This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. | Q2IM61 |
P22743 | HBB2_NAJNA | Hemoglobin beta-II chain | Naja | VHWSAEEKQLITSLWAKVDVPEVGAATLGKMMVMYPWTQRFFAHFGNLSGPSALCGNPQVRAHGKKVLTSFGEALKHLDNVKETFAKLSELHFDKLHVDPENFKLLGNVLIIVLAGHHGKEFTPSTHASFQKLVNVVAHALARRYH | Involved in oxygen transport from the lung to the various peripheral tissues. | P22743 |
A8ARM1 | COAD_CITK8 | Pantetheine-phosphate adenylyltransferase | Citrobacter | MQKRAIYPGTFDPITNGHIDIVTRATQMFDHVILAIAASPSKKPMFTLEERVALAQQATAHLGNVEVMGFSDLMANFARIQQANILIRGLRAVADFEYEMQLAHMNRHLMPQLESVFLMPSKEWSFISSSLVKEVARHQGDVTHFLPENVHQALMDKLK | Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. | A8ARM1 |
Q5L510 | DCUP_CHLAB | Uroporphyrinogen decarboxylase | Chlamydia | MSKFYDVIKPKASRPPVWFLRQVGRYMPQYRELKGSQTLKDFFHNTEAITEATLLGPSLLKVDAAILFADILSLLDGFNISYDFAPGPQISFSPKEELIFTNDPQDTFSYLLKAIKNLVKRLSVPLIAFAASPFTMACYLLEGGASKDFPKTMAFLYQHPERFDALLKQLAEATVIYLKEQIQAGASAIQLFESSSLRLPSALFSRYVTRPNTQLITQLKNSVSSPISLFCRCFDENFIDLYSTGADTLHPDYHVNLSQIYTAVTHPGSLQGNIDPALFLLPQDQFLNHLEKYLSVLKHQPKYIFNSGHGILPETPLENV... | Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | Q5L510 |
P77952 | GLSA_STRGR | Glutamine--scyllo-inositol transaminase | Streptomyces | MDSSLAISGGPRLSNREWPRWPQPGDRALKSLEDVLTSGRWTISCAYQGRDSYERQFASAFADYCGSAMCVPISTGTASLAIALEACGVGAGDEVIVPGLSWVASASAVLGINAVPVLVDVDPATYCLDPAATEAAITERTRAITVVHAYSAVADLDALLDIARRHGLPLIEDCAHAHGAGFRGRPVGAHGAAGVFSMQGSKLLTCGEGGALVTDDADVALRAEHLRADGRVVRREPVGVGEMELEETGRMMGSNACLSEFHAAVLLDQLELLDGQNARRTRAADHLTDRLSELGMTAQATAPGTTARAYYRYLVRLPDE... | Catalyzes the PLP-dependent transamination of scyllo-inosose to form scyllo-inosamine. | P77952 |
A1S1L6 | GPMI_SHEAM | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase | Shewanella | MTAKRPLALLILDGWGYREDQESNAIFHANTPVLDNLKANYPNGLISGSGHDVGLPDGQMGNSEVGHINLGSGRIVYQELTRISKAIEDGEFDDNPALCKAVDAAIAANGAVHIMGLLSPGGVHSHEEHIEAMIRMAAKRGATKVYLHAFLDGRDTPPRSAKGSLAHFTELFASLNAGRIASIVGRYFAMDRDNRWDRVVQAYDLITQGKGKHSATNAVDALEAAYARDENDEFVAPTAIVDANGDSVSLNDNDALIFMNFRADRARQISRSFTDPAFAGFERAVTPKTHFVMLTEYAGDIQGDIAFPSEDLVNTLGEVL... | Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. | A1S1L6 |
Q70XX4 | RK14_AMBTC | 50S ribosomal protein L14, chloroplastic | Amborella | MIQAQTYLNVADNSGARELMCIRIVGASNPRYAHIGDVIVAVIKEAVPNMPLERSEVIRAVIVRTCKELKRDNGIIIRYDDNAAVVIDPEGNPKGTRVFGSIAGELRHLNFTKIVSLAPEVF | Binds to 23S rRNA. | Q70XX4 |
Q2RXQ9 | QUEA_RHORT | Queuosine biosynthesis protein QueA | Rhodospirillum | MRVDLFDFDLPRDLIAVRPAVPRDSARLLLVEGESRRDLGVGDLPGLLDPGDILVFNDTRVIPARLKGRIGDGGVEVTLHKRVGPDAWDCFARPARKLKPGVVILFAEGFTATVAARGEDGEATLRFDRAGAALMAALEAYGHIPLPPYIKRPDDARDRADYQTIYAREDGAVAAPTAGLHFTPALLAALEARGVSRAMVTLHVGAGTFLPVKVEDTDDHRMHAETGTLTAQTAEAINAARAAGGKVVAVGTTAMRLLESATGADKVIRPFHGDTSIFITPGYRFNAVDRLMTNFHLPRSTLFMLVSAFAGASRMRNAYA... | Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). | Q2RXQ9 |
Q113E3 | GLGA_TRIEI | Starch [bacterial glycogen] synthase | Trichodesmium | MRILFVSAEATPLAKVGGMADVVGALPKVLRKMGHDVRIFMPYYGFLGDKMEVPEEPIWEGTAMYQNFKIYETVLPKSDVPLYLFGHPAFWPRHIYYGDDEDWRFTLFANGAAEFCWNGWKPEIVHCNDWHTGMIPVWMHETPDIKTVFTIHNLAYQGPWRWYLERITWCPWYMEGHNTMAAAVQFADRVTTVSPTYASQIQTPAYGENLDGLMSFITGKLHGILNGIDMNFYNPANDRYIPQTYDVNTLEKRVDNKIALQEEVGFEVNKNSFLMGMVSRLVEQKGLDLMLQVLDRFMAYTDTQFILLGTGDRFYETQMW... | Synthesizes alpha-1,4-glucan chains using ADP-glucose. | Q113E3 |
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