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
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|---|---|---|---|---|---|---|
Q6GL39 | WDR82_XENTR | WD repeat-containing protein 82 | Silurana | MKLTDNVLRSFRVAKVFRENSDKINCFDFSPTGETVISSSDDDSIVLYDCQEGKPKRTLYSKKYGVDLIRYTHAANTVVYSSNKIDDTIRYLSLHDNKYIRYFPGHSKRVVALSMSPVDDTFISGSLDKTIRLWDLRSPNCQGLMHLQGKPVCSFDPEGLIFAAGVNSEMVKLYDLRSFDKGPFATFKMQYDRTCEWTALKFSNDGKLILMSTNGGFLRLVDAFKGAVMHTFGGYNNSKAVTLEATFTPDSQFIMIGSEDGKIHVWNCESGMKVAVLDGKHTGPITCLQFNPKFMTFTSACSNMAFWLPTIDD | Regulatory component of the SET1 complex implicated in the tethering of this complex to transcriptional start sites of active genes. Facilitates histone H3 'Lys-4' methylation (H3K4me) via recruitment of the SETD1A or SETD1B to the 'Ser-5' phosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A). Part of a transcription termination checkpoint that promotes transcription termination of long non-coding RNAs (lncRNAs). | Q6GL39 |
P37752 | TRMO_EIKCO | tRNA methyltransferase O | Eikenella | SFSHIWVQFVFHGVAGAGWQPLVRPPRLGGNRKMGVFATRSPFRPNPLGLSLLKLERIETEGGVRLWCGGADLLDGTPVLDIKPYLPFVEAQPDAAPGFAAVPPVPLEVAWADEISAASLPPPNRLLIEQSIAQDPRPAYQDTPQRVYKMAVDDWEVAFRIEKGMALIEAVMAVEG | S-adenosyl-L-methionine-dependent methyltransferase responsible for the addition of the methyl group in the formation of N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of the tRNA anticodon loop of tRNA(Thr)(GGU). The methyl group of m(6)t(6)A37 appears to slightly improve the efficiency of the tRNA decoding ability. Binds to tRNA. | P37752 |
P05483 | U7AB_CONGE | Shaker peptides GVIIA/GVIIB | Gastridium | CKSPGTPCSRGMRDCCTSCLLYSNKCRRY | Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav). | P05483 |
P29962 | Y1784_RHOCB | ORF124 | Rhodobacter | MAPREPGFAGALPIDGYGPGFFRIAGAVHRGGLLIHAEAAMPWTGFDDLAALRALAGQVDLLLCGMGADIAHLPKGLQVELEALGVMAEPMSTASAARHYNVLLSEGRRVGAALLPMPGAVPTA | Not required for the biogenesis of c-type cytochromes. | P29962 |
Q13454 | TUSC3_HUMAN | Protein N33 | Homo | MGARGAPSRRRQAGRRLRYLPTGSFPFLLLLLLLCIQLGGGQKKKENLLAEKVEQLMEWSSRRSIFRMNGDKFRKFIKAPPRNYSMIVMFTALQPQRQCSVCRQANEEYQILANSWRYSSAFCNKLFFSMVDYDEGTDVFQQLNMNSAPTFMHFPPKGRPKRADTFDLQRIGFAAEQLAKWIADRTDVHIRVFRPPNYSGTIALALLVSLVGGLLYLRRNNLEFIYNKTGWAMVSLCIVFAMTSGQMWNHIRGPPYAHKNPHNGQVSYIHGSSQAQFVAESHIILVLNAAITMGMVLLNEAATSKGDVGKRRIICLVGLGLVVFFFSFLLSIFRSKYHGYPYSDLDFE | Magnesium transporter. | Q13454 |
Q88W46 | TARI_LACPL | Ribitol-5-phosphate cytidylyltransferase | Lactiplantibacillus | MIYAQILAGGKGTRMGNVPMPKQFLLLADKPILIHTIEKFTLESRFDAILVVCPADWVSHTEDIIKKYITDERVHVVVGGADRNETLMSGINYIQDHYGIQDDDVVVTHDAVRPFITQRIINDNIVAVLENKAVDTVVPAIDTIVRGANDQVTDIPVRSEMYQGQTPQSFHIKILIDSYNALSSEQKASLSDSCKICSLAGQKVSLVRGENYNFKITTPFDLRVASALVEKRS | Catalyzes the transfer of the cytidylyl group of CTP to D-ribitol 5-phosphate. | Q88W46 |
B3CU37 | YQGF_ORITI | Putative pre-16S rRNA nuclease | Orientia | MIINSIIEFLQAADIKKQILGIDFGEKKVGVAISNIEHTVAMPLQTIFATNQDRINKIQEIAVAYNIGAIVIGLPFKLDGTETSQTHRVKDFANKLANKLLLPIFLCDERLTSKAANNLLKMGNIKRKVRNAIDDRVAASIILEGTLKRMQNSKSYF | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | B3CU37 |
P29037 | TBP_MOUSE | Transcription initiation factor TFIID TBP subunit | Mus | MDQNNSLPPYAQGLASPQGAMTPGIPIFSPMMPYGTGLTPQPIQNTNSLSILEEQQRQQQQQQQQQQQQQAVATAAASVQQSTSQQPTQGASGQTPQLFHSQTLTTAPLPGTTPLYPSPMTPMTPITPATPASESSGIVPQLQNIVSTVNLGCKLDLKTIALRARNAEYNPKRFAAVIMRIREPRTTALIFSSGKMVCTGAKSEEQSRLAARKYARVVQKLGFPAKFLDFKIQNMVGSCDVKFPIRLEGLVLTHQQFSSYEPELFPGLIYRMIKPRIVLLIFVSGKVVLTGAKVRAEIYEAFENIYPILKGFRKTT | General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II. Component of a BRF2-containing transcription factor complex that regulates transcription mediated by RNA polymerase III. Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (pre-initiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1 with the rDNA promoter. SL1 is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA. | P29037 |
O74000 | Y106A_PYRHO | Putative antitoxin PH1062.1 | Pyrococcus | MSKTITIADDVYYELVKMKGKRSFSEVLRELIGKKKEGNLDVLMIAFGTMDEEEAKELEEKIKEVGKWLNSWTPV | Possibly the antitoxin component of a type II toxin-antitoxin (TA) system. | O74000 |
B1LE44 | YDIB_ECOSM | NAD-dependent shikimate 5-dehydrogenase | Escherichia | MNVTAKYELIGLMAYPIRHSLSPEMQNKALEKAGLPFTYMAFEVDNDSFPAAIEGLKALKMRGTGVSMPNKQLACEYVDELTPAAKLVGAINTIVNDDGYLRGYNTDGTGHIRAIKESGFDIKGKTMVLLGAGGASTAIGAQGAIEGLKEIKLFNRRDEFFDKALAFAQRVNENTDCVVTVTDLADQQAFAEALASADILTNGTKVGMKPLENESLVHDISLLHPGLLVTECVYNPHMTKLLQQAQQAGCKTIDGYGMLLWQGAEQFTLWTGKDFPLEYVKQVMGFGA | The actual biological function of YdiB remains unclear, nor is it known whether 3-dehydroshikimate or quinate represents the natural substrate. Catalyzes the reversible NAD-dependent reduction of both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate (SA) and quinate, respectively. It can use both NAD or NADP for catalysis, however it has higher catalytic efficiency with NAD. | B1LE44 |
B2I7H1 | TTCA_XYLF2 | tRNA 2-thiocytidine biosynthesis protein TtcA | Xylella | MDATFPSQHNITARPAPGRIRREQCKLAKRLRRQVGQAIADFGMIEANDKIMVCLSGGKDSYTLLDMLLQLRAKAPVPFELTAVNLDQKQPGFPKHVLPEYLSSIGVPYHIIEQDTYSVVTRVVPEGKTLCALCSRMRRGALYAYAETQGFTKIALGHHRDDMVATFFMNLFHHAKLSGMPPKLRSDNGKHVVIRPLAYVSETDIIAYADAREFPIIPCNLCGSQENLQRKQVGVMLKAWEKEYPGRIEQIARALGNIRPSQLADQSLFDFLALGRHSNTPLPNAHAWLAGDLANDTAP | Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. | B2I7H1 |
Q4V7R0 | TIGAR_XENLA | TP53-induced glycolysis and apoptosis regulator | Xenopus | MARFALTIVRHGETRYNKEKLLQGQGIDEPLSEMGFKQADAAGRFLSNVRFTHVFSSDLIRAKQTACAIMRNNQLSEDIKIMYDPRLRERKYGDAEGRPLSELKVMAKKAGGQCPSYTPPGGETLEQVRACAKDFFEYLCQLVMAESSVKEKSELGASGMVGIMSTDLAPFVNHNKEPTIFGESRDVTLDASVLLVSHGAYMRNWIKYFVEDLQFTFPPELKKSRELSVSPNTGISHFIVTVGSGATRKPEIQCVCINLHGHLSDIDADTSHYQV | Fructose-bisphosphatase hydrolyzing fructose-2,6-bisphosphate as well as fructose-1,6-bisphosphate. Acts as a negative regulator of glycolysis by lowering intracellular levels of fructose-2,6-bisphosphate in a p53/TP53-dependent manner, resulting in the pentose phosphate pathway (PPP) activation and NADPH production. Contributes to the generation of reduced glutathione to cause a decrease in intracellular reactive oxygen species (ROS) content, correlating with its ability to protect cells from oxidative or metabolic stress-induced cell death. May play a role in mitophagy inhibition. | Q4V7R0 |
Q28K11 | TRUB_JANSC | tRNA-uridine isomerase | unclassified Jannaschia | MARRNKGRDISGWVLVDKPAGLTSTAVVNKVRWCFDAKKAGHAGTLDPDATGMLPVALGEATKTIAYMSDDLKAYTFRVRLGVSTKTDDAEGEVLETSDTRPTDTEIEAALPAFVGDIQQVPPQFSAVKVDGERAYDIARGGGEMELAARDLYVESLSVIGRPDADHVDLEFVCGSGGYVRSIARDLGQVLGCFGHVLWLRRTWVGAFDIEDAVGLDRVEALARTDALYALLQPVGLALHALPELRVTDAGAARLRNGNPGGVLPGNVEYGDLAWASLNGTPVAVGRYRSGELHPERVFNL | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | Q28K11 |
Q984P3 | UVRC_RHILO | Excinuclease ABC subunit C | Mesorhizobium | MSPLDQKNKPRGGADDLPPEIDLEDEALEEIVEPTGPDVAFTAIDWTPHAGDAEGMVGAEVIQTLVKRLPNAPGVYRMMNAAGDVLYVGKARSLKKRVTNYAQGRFHTNRIGRMVRETSTMEFVVTRTEIEALLLEANLIKRLRPRFNVLMRDDKSFPYILLTGDHVSPGIYKHRGARSRKGDYFGPFASAGAVGRTINSLQRAFLLRSCTNSFYENRTRPCLLYQIKRCAGPCTGEISHEGYAELVAEAKDFLSGRSQKVKTEISAAMQQASEDLDFERAAIYRDRLAALSHVQSHQGINPATVDEADVFAIHQEGGQVCIQVFFFRTGQNWGNRAYFPKADPALEAAEVLGSFLAQFYDDKPTPRNILLSRGVEDQELLGEALSTRAGRKVTISVPQRGEKKDLTDNALQNAREALGRRLAETSTQGRLLAGFAETFGLAKPPVRIEVYDNSHIMGTNAVGAMVVAGPEGFVKNQYRKFNIRSTEITPGDDFGMMREVMERRFSRLLKEHGDVAPNDAASAEAGDDIEDDISGSFPAWPDVILIDGGQGQMTAVRKILADLGIEDRVVAIGIAKGQDRDAGRERFFVKGRDSFSLPVRDPVLYFVQRLRDEVHRFAIGSHRARRKKEMVKSPLDEIAGIGPGRKRALLLAFGTAKAVSRAAIEDLRKVDGISEQVAKLVYNHFHES | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | Q984P3 |
Q5NYM6 | YCIB_AROAE | Inner membrane-spanning protein YciB | Aromatoleum | MKILFDLLPVILFFVAYKIAGGNQAFAHELASRWLGDGIAVTQAPILLATAVAILATIAQIGWVWMRHRKVDTMLWISLAIIAVFGGATLFFHNPTFIKWKPTALYWLFGGTLTVSAVIFRRNLIRKMLEAQIRLPEPVWKRLNLAWAGFFILMGFLNLYVAYNFSEEAWVNFKLFGGMGLMLLFVLGQGFYLSRHIQEETT | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | Q5NYM6 |
Q641Q2 | WAC2A_HUMAN | WASH complex subunit 2A | Homo | MMNRTTPDQELAPASEPVWERPWSVEEIRRSSQSWSLAADAGLLQFLQEFSQQTISRTHEIKKQVDGLIRETKATDCRLHNVFNDFLMLSNTQFIENRVYDEEVEEPVLKAEAEKTEQEKTREQKEVDLIPKVQEAVNYGLQVLDSAFEQLDIKAGNSDSEEDDANGRVELILEPKDLYIDRPLPYLIGSKLFMEQEDVGLGELSSEEGSVGSDRGSIVDTEEEKEEEESDEDFAHHSDNEQNRHTTQMSDEEEDDDGCDLFADSEKEEEDIEDIEENTRPKRSRPTSFADELAARIKGDAVGRVDEEPTTLPSGEAKPRKTLKEKKERRTPSDDEEDNLFAPPKLTDEDFSPFGSGGGLFSGGKGLFDDEDEESDLFTEAPQDRQAGASVKEESSSSKPGKKIPAGAVSVFLGDTDVFGAASVPSMKEPQKPEQPTPRKSPYGPPPTGLFDDDDGDDDDDFFSAPHSKPSKTGKVQSTADIFGDEEGDLFKEKAVASPEATVSQTDENKARAEKKVTLSSSKNLKPSSETKTQKGLFSDEEDSEDLFSSQSASKLKGASLLPGKLPTLVSLFDDEDEEDNLFGGTAAKKQTLCLQAQREEKAKASELSKKKASALLFSSDEEDQWNIPASQTHLASDSRSKGEPRDSGTLQSQEAKAVKKTSLFEEDEEDDLFAIAKDSQKKTQRVSLLFEDDVDSGGSLFGSPPTSVPPATKKKETVSEAPPLLFSDEEEKEAQLGVKSVDKKVESAKESLKFGRTDVAESEKEGLLTRSAQETVKHSDLFSSSSPWDKGTKPRTKTVLSLFDEEEDKMEDQNIIQAPQKEVGKGRDPDAHPKSTGVFQDEELLFSHKLQKDNDPDVDLFAGTKKTKLLEPSVGSLFGDDEDDDLFSSAKSQPLVQEKKRVVKKDHSVDSFKNQKHPESIQGSKEKGIWKPETPQDSSGLAPFKTKEPSTRIGKIQANLAINPAALLPTAASQISEVKPVLPELAFPSSEHRRSHGLESVPVLPGSGEAGVSFDLPAQADTLHSANKSRVKMRGKRRPQTRAARRLAAQESSETEDMSVPRGPIAQWADGAISPNGHRPQLRAASGEDSTEEALAAAAAPWEGGPVPGVDRSPFAKSLGHSRGEADLFDSGDIFSTGTGSQSVERTKPKAKIAENPANPPVGGKAKSPMFPALGEASSDDDLFQSAKPKPAKKTNPFPLLEDEDDLFTDQKVKKNETKSNSQQDVILTTQDIFEDDIFATEAIKPSQKTREKEKTLESNLFDDNIDIFADLTVKPKEKSKKKVEAKSIFDDDMDDIFSSGIQAKTTKPKSRSAQAAPEPRFEHKVSNIFDDPLNAFGGQ | Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes inhibits WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization and is involved in the fission of tubules that serve as transport intermediates during endosome sorting. Mediates the recruitment of the WASH core complex to endosome membranes via binding to phospholipids and VPS35 of the retromer CSC. Mediates the recruitment of the F-actin-capping protein dimer to the WASH core complex probably promoting localized F-actin polymerization needed for vesicle scission. Via its C-terminus binds various phospholipids, most strongly phosphatidylinositol 4-phosphate (PtdIns-(4)P), phosphatidylinositol 5-phosphate (PtdIns-(5)P) and phosphatidylinositol 3,5-bisphosphate (PtdIns-(3,5)P2). Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1. Required for the association of DNAJC13, ENTR1, ANKRD50 with retromer CSC subunit VPS35. Required for the endosomal recruitment of CCC complex subunits COMMD1 and CCDC93 as well as the retriever complex subunit VPS35L. | Q641Q2 |
Q5D7I5 | TRIM5_CEBPY | TRIM5alpha | Cebuella | MASRILVNIKEEVTCPICLELLTEPLSLDCGHSFCQACITANHKESTLHQGERSCPLCRMSYPSENLRPNRHLANIVERLKEVMLSPEEGQKVDHCARHGEKLLLFCQQDGNVICWLCERSQEHRGHHTFLVEEVAEKYQGKLQVALEMMRQKQQDAEKLEADVREEQASWKIQIQNDKTNIMAEFKQLRDILDCEESKELQNLEKEEKNILKRLVQSESDMVLQTQSIRVLISDLERRLQGSVMELLQGVDDVIKRIEKVTLQKPKTFLNEKRRVFRAPDLKGMLQAFKELTEVQRYWAHVTLVPSHPSCTVISEDERQVRYQVPIHQPLVKVKYFYGVLGSLSITSGKHYWEVDVSNKRGWILGVCGSWKCNAKWNVLRPENYQPKNGYWVIGLRNTDNYSAFQDAVKYSDVQDGSRSVSSGPLIVPLFMTICPNRVGVFLDYEACTISFFNVTSNGFLIYKFSNCHFSYPVFPYFSPTTCELPMTLCSPSS | Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. | Q5D7I5 |
A0A291PQG3 | UGT4_DACCO | UDP-glucosyltransferase 4 | Dactylopius | MTLLRDLLLLYINSLLFINPSIGENILVFLPTKTYSHFKPLEPLFQELAMRGHNVTVFSGFSLTKNISNYSSIVFSAEIEFVNIGMGNLRKQSRIYNWIYVHNELQNYFTQLISDNQLQELLSNKDTQFDLIFIELYHVDGVFALSHRFNCPIIGLSFQPVLPIYNWLIGNPTTFSYIPHVYLPFTDIMSFWKRIINAVFSIFTAAFYNFVSTKGYQKHVDLLLRQTESPKLNIEELSESLSLILAEFHFSSAYTRPNLPNVIDIAGIHIQSPKPLPQDLLDFLDQSEHGVIYVSLGTLIDPIHTDHLGLNLINVFRKLRQRVIWKWKKEFFHDVPKNVLIGEWFPQIDILNHPRCKLFISHGGYHSMLESIYSSVPILGIPFFTDQHHNTAIIEKLKIGKKASTEASEEDLLTAVKELLSNETFKRNSQHQSSIFRDRPMSPMDTAIYWTEYILRYKGASHMKSAVIDLYWFQYILLDIILFYSLIVLILLCILRIFFRMLTK | Catalyzes the transfer of a glycosyl group from a UDP-sugar to an acceptor molecule. | A0A291PQG3 |
Q03Y35 | YBEY_LEUMM | Endoribonuclease YbeY | Leuconostoc | MDLAIIDQTKAGVNQYHQDLVRCVLDYAGKYLELPDNTEMSVTFMNNEEIHQYNKKYRGIDKPTDVISFAIEEDGDDLPVLPDELMDAELAKNIGDILVSVDIINSQAEYLGHSYERELGFLVVHGFLHLNGYDHMLGDAEEKEMFDLQREILDNYGLKR | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | Q03Y35 |
A1K2P1 | UBIA_AZOSB | 4-HB polyprenyltransferase | Azoarcus | MTLSDRLPLYGRLMRLDKPIGSLLLLWPTLWALWLAADGKPPLHVLVIFTIGTVLMRSAGCVINDYADRDFDGHVERTRNRPLATRAVSTREALALAAGLSALSFVLILPLDPLVIWLSFPALFLAASYPFTKRFFAIPQAYLGIAFGFGIPMGFAAVQGEVPPIAWVMLLANIFWAVAYDTEYAMVDRPDDLKIGIKTSAITFGRFDVAAVMLCYAVALGLLGWVGAQAGRGALYFAGLAVAAGMALYHYTLIRHRERAPCFKAFRHNNWLGAAVFAGLALDYLIG | Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate. | A1K2P1 |
Q9FH40 | TA14B_ARATH | TBP-associated factor 14b | Arabidopsis | MTNSSSSKKQAQDQPETSEPTLKSLKTKMTKSDEKQKKLKDIEISVPIVYGNVAFWLGKKASEYQSHKWAVYVRGATNEDISVVVKKVVFQLHSSFNSPTRVIEEPPFEVSESGWGEFEIAMTLHFHSDVCDKPLSLYHHLKLYPEDESGPLTMKKPVVVESYDEIVFPDPSESFLARVQNHPALTFPRLPSGYNLPAPMQVEDTGKKKRGDTKDHSLGQWFMSFSEADELLQLAAARQQVQAHIAKLRRQISLLEGQNQTVKTGSDL | Negative regulator of flowering controlling the H4K5 acetylation levels in the FLC and FT chromatin. Positively regulates FLC expression. Component of the transcription factor IID (TFIID) complex that is essential for mediating regulation of RNA polymerase transcription. Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of a NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4 and H2A. | Q9FH40 |
Q7T046 | VM3CX_MACLB | Coagulation factor X-activating enzyme heavy chain alternate form | Macrovipera | MMQVLLVTISLAVFPYQGSSIILESGNVNDYEVVYPQKITALPEEAVQQPEQKYEDTMQYEFEVNGEPVVLHLEKNKDLFSEDYSETRYSPDGRETTTKPPVQDHCYYHGRIQNDAYSSASISACNGLKGHFKLQGETYLIEPLKIPDSEAHAVYKYENIEKEDEAPKMCGVTQTNWESDEPIKKASQLVATSAKRKFHKTFIELVIVVDHRVVKKYDSAATNTKIYEIVNTVNEIFIPLNIRLTLIGVEFWCNRDLINVTSSADDTLDSFGEWRGSDLLNRKRHDNAQLFTDMKFDLSTLGITFLDGMCQAYRSVGIVQEHGNKNFKTAVIMAHELGHNLGMYHDRKNCICNDSSCIMSAVLSSQPSKLFSNCSNHDYRRYLTTYKPKCILNPPLRKDIASPPICGNEIWEEGEECDCGSPKDCQNPCCDAATCKLTPGAECGNGLCCEKCKIKTAGTVCRRARDECDVPEHCTGQSAECPADGFHANGQPCQNNNGYCYNGDCPIMTKQCISLFGSRATVAEDSCFQENQKGSYYGYCRKENGRKIPCAPQDIKCGRLYCLDNSPGNKNPCKMHYRCRDQHKGMVEPGTKCEDGKVCNNKRQCVDVNTAY | Catalytic subunit of blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) by cleaving the Arg(234)-Ile(235) bond, activates coagulation factor IX (F9) by cleaving the Arg(226)-Val(227) bond and is also able to activate protein C (PROC). | Q7T046 |
P13388 | XMRK_XIPMA | Melanoma receptor tyrosine-protein kinase | Xiphophorus | MEFLRGGAALLQLLLVLSISRCCSTDPDRKVCQGTSNQMTMLDNHYLKMKKMYSGCNVVLENLEITYTQENQDLSFLQSIQEVGGYVLIAMNEVSTIPLVNLRLIRGQNLYEGNFTLLVMSNYQKNPSSPDVYQVGLKQLQLSNLTEILSGGVKVSHNPLLCNVETINWWDIVDKTSNPTMNLIPHAFERQCQKCDHGCVNGSCWAPGPGHCQKFTKLLCAEQCNRRCRGPKPIDCCNEHCAGGCTGPRATDCLACRDFNDDGTCKDTCPPPKIYDIVSHQVVDNPNIKYTFGAACVKECPSNYVVTEGACVRSCSAGMLEVDENGKRSCKPCDGVCPKVCDGIGIGSLSNTIAVNSTNIRSFSNCTKINGDIILNRNSFEGDPHYKIGTMDPEHLWNLTTVKEITGYLVIMWWPENMTSLSVFQNLEIIRGRTTFSRGFSFVVVQVRHLQWLGLRSLKEVSAGNVILKNTLQLRYANTINWRRLFRSEDQSIEYDARTENQTCNNECSEDGCWGPGPTMCVSCLHVDRGGRCVASCNLLQGEPREAQVDGRCVQCHQECLVQTDSLTCYGPGPANCSKSAHFQDGPQCIPRCPHGILGDGDTLIWKYADKMGQCQPCHQNCTQGCSGPGLSGCRGDIVSHSSLAVGLVSGLLITVIVALLIVVLLRRRRIKRKRTIRCLLQEKELVEPLTPSGQAPNQAFLRILKETEFKKDRVLGSGAFGTVYKGLWNPDGENIRIPVAIKVLREATSPKVNQEVLDEAYVMASVDHPHVCRLLGICLTSAVQLVTQLMPYGCLLDYVRQHQERICGQWLLNWCVQIAKGMNYLEERHLVHRDLAARNVLLKNPNHVKITDFGLSKLLTADEKEYQADGGKVPIKWMALESILQWTYTHQSDVWSYGVTVWELMTFGSKPYDGIPAKEIASVLENGERLPQPPICTIEVYMIILKCWMIDPSSRPRFRELVGEFSQMARDPSRYLVIQGNLPSLSDRRLFSRLLSSDDDVVDADEYLLPYKRINRQGSEPCIPPTGHPVRENSITLRNISDPTQNALEKDLDGHEYVNQPGSETSSRLSDIYNPNYEDLTDGWGPVSLSSQEAETNFSRPEYLNTNQNSLPLVSSGSMDDPDYQAGYQAAFLPQTGALTGNGMFLPAAENLEYLGQGGALYTPVR | Probable receptor with tyrosine-protein kinase activity. | P13388 |
Q63HD6 | TILS_BACCZ | tRNA(Ile)-lysidine synthetase | Bacillus cereus group | MKDTFVEKVDDFVKQHDVLKEHSTIVVGVSGGPDSLALLYYLLEKRAAKQFEIVVAHVDHMFRGDESHEDLQFVQDLCKGLGVICETIRINVSQYQQQYGMNAQVAARECRYAFLERIMKKYDARYVALGHHGDDQVETILMRLVRGSTPKGYAGIAVKRPFHNGYLIRPLLGVTKEEIVDYCNKLKIIPRIDPSNKKEVYTRNRLRKYVLPHLKEENPQVHEKFQKFSMQMQEDEAYLQELAFEKMNKVITKKSDKQISLSIPAFESMSMPLQRRGIQLILNYLYEYKIPSSLSSIHIDKVIEFFKRTQPSGSLDFPGDLKIVRAYEECSFGFKQEIVSPFLQDLSVPGTITLSNGDKLVTEVSEDIPSDMNETVFVAKYNDISYPLRIRSRENGDRMSIQGMNGTKKIKAIFIEAKVPREKREEWPVVCDASGNVIWLPLLKRSAFAISKETAKKDKYMIIHYKSKESSGRIMK | Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. | Q63HD6 |
Q52377 | UVRC_PSEU2 | Excinuclease ABC subunit C | Pseudomonas syringae | MTQTFDPGAFLATCSGRPGVYRMFDAEATLLYVGKAKNLKKRLASYFRKTGHAPKTGALVSRIAQIETTITGNETEALLLEQTLIKEWRPPYNILLRDDKSYPYVFLSDNAFPRLSIHRGTKKAKGRYFGPYPSAGAIRESLSLLQKTFQVRQCEDSYFKNRTRPCLQYQIKRCKGPCVGLVEPEVYAEDVRHSVMFLEGRSNALSDELNASMEKAAMALDFERAAELRDQVALLRRVQDQQSMDGGTGDVDVVAAFVNPGGACVHLISVRGGRVLGSKNFFPQVGIEEEVGEVMSAFLAQYFLGGIDRELPGEVIVNVINDDFPAFVDAVEELRGVEMVISHRVRGTRARWQQMAVTNAEQALTARLANRQHVASRFEALAKVLGLEDPPMRLECYDISHSSGEATVASCVVFGPEGPIKSDYRRFNIEGVTAGDDYAAMHQALTRRYSRIKAGEGKLPDVLLVDGGKGQMSMARDVLNELQVPELILLGVAKGTTRKAGFETLYLNDSAHEFTLPGDSPALHLIQQIRDEAHRFAITGHRARRGKTRRTSTLEGVAGVGPTRRRDLLKHFGGLQELSRASIDEIAKAPGISKKLAESIYANLHSE | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | Q52377 |
Q4N938 | TCTP_THEPA | Translationally-controlled tumor protein homolog | Theileria | MKVYKDLYSNDEVCSDAYDHHDPFDNADLSSVAFEVKTSKVPKGEEDYGIGYNDEEGADQMNVDPNVEMVVDVVDKFGLQSLSLTKKDYSSYIRKYIQRLVATLQEKNPERVEPFKTTVSDFVKHVLANFEDFEFYVGESLDYEAGLVYAYYKGEEVSPRLVFLKDGLVEERY | Involved in calcium binding and microtubule stabilization. | Q4N938 |
Q17WX3 | TRUD_HELAH | tRNA-uridine isomerase D | Helicobacter | MNLNFMPLLHAYNHASIDFHFNSSARDFCVHEVPLYEFSNKGEHAIIQVRKSGLSTLEMLQIFSQILGVKIAELGYAGLKDKNALTTQFVSLPKKYAPLLEKNTSNFQERNLKILSLNYHHNKIKLGHLKGNRFFMRFKKMTPLNAHKTKQVLEQIVQFGMPNYFGSQRFGKFNDNHKEGLKILQNEAKFKNQKLNAFLISSYQSYLFNSLLSKRLEISKIISDFSLKEGLEFFKQKNLNIHSNALKALKNQDHPFKILEGDVMCHYPYGKFFDALELEKESERFLKKEAVPMGLLDGKKALYAKNLSLEIEKEFQNHILSDHAKTLGSRRFFWVFVENLTSKYIKEKVQFELEFYLPKGSYASALLKEIKHQKGENNDEF | Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. | Q17WX3 |
O00300 | TR11B_HUMAN | Osteoprotegerin | Homo | MNNLLCCALVFLDISIKWTTQETFPPKYLHYDEETSHQLLCDKCPPGTYLKQHCTAKWKTVCAPCPDHYYTDSWHTSDECLYCSPVCKELQYVKQECNRTHNRVCECKEGRYLEIEFCLKHRSCPPGFGVVQAGTPERNTVCKRCPDGFFSNETSSKAPCRKHTNCSVFGLLLTQKGNATHDNICSGNSESTQKCGIDVTLCEEAFFRFAVPTKFTPNWLSVLVDNLPGTKVNAESVERIKRQHSSQEQTFQLLKLWKHQNKDQDIVKKIIQDIDLCENSVQRHIGHANLTFEQLRSLMESLPGKKVGAEDIEKTIKACKPSDQILKLLSLWRIKNGDQDTLKGLMHALKHSKTYHFPKTVTQSLKKTIRFLHSFTMYKLYQKLFLEMIGNQVQSVKISCL | Acts as decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF10/TRAIL and protect against apoptosis. TNFSF10/TRAIL binding blocks the inhibition of osteoclastogenesis. | O00300 |
Q25113 | TBXT_HEMPU | Protein T | Hemicentrotus | MPAMSADALRAPSYNVSHLLNAVQSEMNRGSEKGDPSEEGLKVRLDDVELWKKFHKLTNEMIVTKSGRRMFPVLSASIAGLDPNSMYSVLLDFSAADDHRWKYVNGEWIPGGKPDGSPPTTAYIHPDSPNFGAHWMKQAVNFSKVKLSNKLNGSGQVMLNSLHKYEPRIHIIRVGGREKQRLVGSYSFTETRFIAVTAYQNEDITQLKIKYNPFAKAFLDIKDKNDGHDLFDDVHDFQGSKYPQFGGWFLPGSGAFGPTPHQFNPSIGLPSHAGCDRYGGLRSHRTSPYPPPPYHQKYSAAGAGYGAEASAGLSSSISLLAADSWSSLANSTSAASSMPACSQYGSMWPSTAATSGFSHVSSPQSPLPTGLFRNPHPTSSHQHNLASTAHGMAPVASGLPSAAVTTANSSEAHALSQSVMAPGECRASDNAGYL | Involved in the transcriptional regulation of genes required for mesoderm differentiation. | Q25113 |
Q5BBK9 | VPS27_EMENI | Vacuolar protein sorting-associated protein 27 | Aspergillus subgen. Nidulantes | MAGWFSSASPLDEQIERATASSLEDIALNLEISDLIRSKGVQPKDAMRSLKRRLENKNPNIQIATLKLTDTCVKNGGTHFLAEIASREFMDNLVSLLKAEGVPLNSSVRDLMLALIQDWAMAAQGRMDLSYLGETYRKLQMEGFQFPPKSAISGSMLESSAPPEWIDSDVCMRCRTPFSFMNRKHHCRNCGNVFDAQCSSKTLPLPHLGILQPVRVDDGCYAKLTSKPFNQGSLADRSTFKNNSITKSNVLEPRAARVESGFDEDLRRALQMSLEEAQNKSSSGYVPQPKPAQAPANTQPQPSTDEEEDADLKAAIEASLRDMEEHKQKYAAALKNNTSAESSRETPAAASLPKNPYELSPVEVENIHLFSTLVDRLQHQPPGTILREPQIQELYESIGALRPKLARSYGETMSKHDTLLDLHAKLSTVVRYYDRMLEERLSSAYSQHNLGYGPVPGGAQYPNIYPSMPSTTAEVRPGAENFYYGNSGVEPPAPARTPYSQPPLERENGVVSSSMHPPLQQPSSGPYWNPNNHSIASPQPNVNAFNSNNTPYPGPGAPSQFYTSSAYQEPEKLFQQPRQGEPESPYQPSPVTNRDSYYQSAGLPSNPVEQQPPVDHGQSPGHAQPADSRSSQSGQPKATEPSAQSYYLPQEQQQQQQQQQQQSAQGTGYQGYPQGNTNYQAPYGGDVSPISAPPPVQYQQPAAPRPVVEESLIEL | Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane. | Q5BBK9 |
B0RYY8 | TTCA_XANCB | tRNA 2-thiocytidine biosynthesis protein TtcA | Xanthomonas | MTAVLPLPLPLADPAPRTPRLQREPLRLAKRLRHAVGQAIADFGMIAPGDKVMVCLSGGKDSYTLLDMLLQLQRSAPVPFTLVAVNLDQKQPDFPADVLPTYLRAQQVPFDIIEQDTYSVVSRVIPQGKTMCSLCSRLRRGALYAYAQAHGVTKIALGHHRDDIVATFFMNLFHHARLAAMAPKLRSDDGAHVVIRPLAYVREADIAAYAQARHFPIIPCNLCGSQENLQRQQVGRMLQQWDREQPGRVDQIARALGDVRPEQLADRTLFDFPGLGGGADAPLPDAAGWLAGSAAEHARD | Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. | B0RYY8 |
Q7NFD4 | UVRC_GLOVI | Excinuclease ABC subunit C | Gloeobacter | MPNLIADPERLKERLELLPTSAGVYLMRDEAGEILYVGKAKNLRNRVRSYFQPGHDHSPRIAIMVGKVHDFELILTDTEAEALVLEDNLIKTHKPRYNVLLKDDKQYPYLCITWSEEYPRIFVTRRRGSGHPEDRYFGPYTDAGALHSTLGLLKKLFPLRQRNTPVFKDRPCINYEMGRCPGLCQRLISPQEYRATIRQIQMILQGRTAELLAQLEDQMQTAAAAMNFEHAARLRDRITGLNQLGAHQKITVPDSSVSRDAVALAADAALVSIQLFQVRSGKLIGRLGFSAAASGEDPGHILQRVLEEHYRASASEEIPLEVLTQHPLPEADILATWLAEKKGRKVEIHAPQRQIKAELVEMVARNAEAELQRLERFSRRQEKGLLNLAEALELPSVPRRMECYDISHIQGTDTVASRVVFVDGAPAKQYYRHYKIRDPRIVAGRPDDFASMAEVISRRFARAESEPEGDLPDLVVIDGGKGQLSAARAVMEELSYGDVPTIGLAKRLEEVFLPGRSDPVLIAQGDPALHLLQRIRDEAHRFAVSFHREQRGKRMTRSSLDDIPGIGPAKRKILLDTFRSVPVLEKASFEEIAKTPGIGSRLAQVIHTYFHGEPEAVARALEAEQAAN | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | Q7NFD4 |
B6JCL3 | UPPP_AFIC5 | Undecaprenyl pyrophosphate phosphatase | Afipia | MLFDLFKALVLGIVEGVTEFLPVSSTGHILLAERIFDLDQDNFWKTFAVLIQLGAILAILAIYFQRLWRVATHMFTDPAARRFVIGVLVAFLPAVILGLIFGTFIKEVLFNPWVVCFSLIAGGAVLLWVDQQDVNPRHHDAMAFPLPMYLGIGIAQCAAMVPGVSRSGASIVAAMLFGADKRAAAEFSFFLAIPTMLGAFVYDVYKSRGDMTMDHAFIIIVGFVVSFITAIVVVKTFLDFVTKNGFTFFAWWRVIVGTLGLIALALGA | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | B6JCL3 |
Q87BK9 | UVRA_XYLFT | Excinuclease ABC subunit A | Xylella | MTALIRIRGARTHNLKNLDLDLPRNTLIVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLSVMEKPDVDHIEGLSPAISIEQKSTSHNPRSTVGTITEIYDYLRLLYARVGQPRCPEHHYPLEAQTVSQMVDHVLTLDPEQRYMLLAPVVRERKGEHTQVFEQLRAQGFVRVRVDGELYEIDAVPTLTLRQKHTIEAVIDRFRPREDIKQRLAESFETALKLGNGMASVQTLDTTTATPHLFSSKYSCPVCDYSLPELEPRLFSFNAPMGACPACNGLGVTEFFDPAKVVIHPDLSLSAGAVRGWDRRNAYYFQLIASLAKHYTFDIDASWESLPEEIRHTILFGSGDEQINFTYLTEAGGRTKRKHRFEGIVPNLERRYRETESAAVREELAKYVSTRTCPECGGTRLNRAARNVFVADRTLPELTVLPINDALEFFKTLRLSGWRGEIAIKIVKEIGERLGFLVDVGLDYLTLERKADTLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLTRLRDLGNTVIVVEHDEDAIRQADHILDIGPGAGVHGGEICAQGSLEQIMAAPRSLTGQYLSGRRRIEIPKQRHPPNATKMLHLRGACGNNLKGVNLDIPEGLFTCITGVSGSGKSTLINDTLFTLAANEINGASHPIAPYASVDGLELFDKVVDIDQSPIGRTPRSNPATYTGMFTPLRELFAQVPEARARGYSPGRFSFNVRGGRCEACEGDGLIKVEMHFLPDVYVPCDICHGKRYNRETLEIRYKGYNINDVLEMTVEDALKLFEAVPAIARKLETLVDVGLSYLKLGQSATTLSGGEAQRVKLSKELSRRDTGHTLYILDEPTTGLHFYDIEALLAVMHKLRDAGNTVIVIEHNLDVIKTADWVIDLGPEGGGRGGEILVAGTPETVAAHPHSHTGHFLAKLLPPKDVSNCGHRNPKEEVDIAKTVHR | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. | Q87BK9 |
Q6SJR1 | TAF4_ARATH | TBP-associated factor 4 | Arabidopsis | MDLSIVKLLEEDEEVDSKHSEDDLQMFQDSLIRDIEGSNLKSINNTTGNESEKPQPRYMKLQKMSSKETPWVEKTVDPVNHNLRLARVTDLLRTVVDHQPGKKTHCLNLHYKLKRKELTMEEFMRQLRDLVGDQIIRSVISQLPQLKPGNMGIKVPGRSNHDKVSKSAEFTAQESDPREVHVNQLSSTTSGTLNSSTTVQGLNKHPEQHMQLPSSSFHMDTKSGSLNPYPGTNVTSPGSSSRAKLPDFQHRENNQNVGIASVGGPTKSTINMTTVPKFERPTFVNGPSRVQDGPISDFPKNSSFPLYSAPWQGSVTKDHTVGPSSSVIHVEHKLIDQSFEQAHKPRYLVQQGVTNVPLKQKNAIPISSNDDLEKQSSKMGLFTSTTSASSVFPSMTTQLDSSTMVNMPAPSETIPKIANVTVTPKMPSVGQKKPLEALGSSLPPSRKKQKICGTSSDESIEKFNDVTAVSGINLREEEKQLLDSGPKKNDRVSKAYRRLVHGEEERTLLQKIPLQRKLTEIMGKSGLKHIDHDVERCLSLCVEERMRGLLFNIIRISKQRTDAEKCRNRTFITSDIRKEINEMNQKVKEEWEKKHSGEEKNKENDTEKEDQRSNEVKANKKDEDKERAKAANVAVRAAVGGDDRFSKWKLMAEARQRSSPGPGRNSKKLSGGTQFGKNQGLPKVVRSISVKDVIAVVEKEPQMSRSTLLYRVYNRICSDV | TAFs are components of the transcription factor IID (TFIID) complex that is essential for mediating regulation of RNA polymerase transcription. | Q6SJR1 |
O26024 | Y1491_HELPY | Putative phosphate permease HP_1491 | Helicobacter | MEIKNIKEFEKASKKLQKDTLKIALALLFLIGAALLALIFGQANSKGLLLIFAAVIGGYMAMNIGANDVSNNVGPAVGSKAISMGGAILIAAICEMLGAIIAGGEVVSTIKGRIVSPEFINDAHIFINVMLASLLSGALWLHVATLIGAPVSTSHSVVGGIMGAGMAAAGMVAVNWHFLSGIVASWVISPLMGALIAMFFLMLIKKTIAYKEDKKSAALKVVPYLVALMSLTFSWYLIVKVLKRLYALNFEIQLACGCILALLIFILFKRFVLKKAPQLENSHESINELFNVPLIFAAALLSFAHGANDVANAIGPLAAISQTLEDANSPIGNTLSSVPLWIMVVGAAGIALGLSLYGPKLIKTVGSEITELDKMQAFCIALSAVITVLLASQLGLPVSSTHIVVGAVFGVGFLRERLREQSRRRFARIRDNIVAAHFGEDLEEIEGFLERFDKANLKEKSLMLESLKKSKNTAIALELKKKEKKSLKKVYKEEVIKRSILKKIVTAWLVTVPVSALLGALLFVALGFIEKYF | Potential transporter for phosphate. | O26024 |
P31058 | YADC_ECOLI | Uncharacterized fimbrial-like protein YadC | Escherichia | MKTIFRYILFLALYSCCNTVSAYTSFIVGNNAGVDNYRGPSTAAQMTFNYTSTASNLVFYKPTQLGPTGVKMYWSYLDTGTGGGILYCNTSGRANPGPITIENAMVYSGKDYGGHKLFNTSVPGLYYTMLISRVWSAYDTITDIQSPGIYIGDPSNQEFFFSVTDSDLQTKGCNKADDYDKFWAIGGIVHNITVEFYTDTNFDPTLNQQVQLSSSSNYLYSFKAYSPGTKVVDHSNHIYVNFTLNNVKLTLPTCFTSILTGPSVNGSTVRMGEYSSGTIKNGASPVPFDISLQNCIRVRNIETKLVTGKVGTQNTQLLGNTLTGSTAAKGVGVLIEGLATSKNPLMTLKPNDTNSVYIDYETEDDTSDGVYPNQGNGTSQPLHFQATLKQDGNIAIEPGEFKATSTFQVTYP | Part of the yadCKLM-htrE-yadVN fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. | P31058 |
A7A047 | TVP38_YEAS7 | TLG2-vesicle protein of 38 kDa | Saccharomyces | MSQSYEAGNANMGQGEDDEFDGYFEDFDNDIMPNSNNGQRVGTNAGLSFNDEVNVNDDDFLDIYNMSPRERLMHNIRKNVQKLQFYFYSLRLWQQIIIVLLGIMLMIMGILLLVFHNAILHKVVVTSNDLREKMSTHFILMVLIFFVAFPPMIGYSLLSTTTGLIYGVSFEGWVTLALGSVTGSIASFVVFKTILHSRAEKLVHLNRRFEALASILQENNSYWILALLRLCPFPYSLTNGAIAGVYGISVRNFSIANIITTPKLFIYLFIGSRVKSLAESESTGSRVFDLVSIIITLLILSLTAWLLYFKTKKRYLELQNRDRQVSTDQLPELSFEV | Golgi membrane protein involved in vesicular trafficking and spindle migration. | A7A047 |
O58762 | TRET_PYRHO | Trehalose-synthesizing glycosyltransferase | Pyrococcus | MMYEVKEFSSGKRKLEDYKSIIGEEEVSKIQEKAEKLKGRSFVHVNSTSFGGGVAEILHSLVPLLRSIGIEARWFVIEGPTEFFNVTKTFHNALQGNESLKLTEEMKELYLNVNRENSKFIDLSSFDYVLVHDPQPAALIEFYEKKSPWLWRCHIDLSSPNREFWEFLRRFVEKYDRYIFHLPEYVQPELDRNKAVIMPPSIDPLSEKNVELKQTEILRILERFDVDPEKPIITQVSRFDPWKGIFDVIEIYRKVKEKIPGVQLLLVGVMAHDDPEGWIYFEKTLRKIGEDYDVKVLTNLIGVHAREVNAFQRASDVILQMSIREGFGLTVTEAMWKGKPVIGRAVGGIKFQIVDGETGFLVRDANEAVEKVLYLLKHPEVSKEMGAKAKERVRKNFIITKHMERYLDILNSLGG | Synthesizes trehalose from ADP-, UDP- or GDP-glucose and glucose. | O58762 |
Q9JJD0 | THA11_MOUSE | Ronin | Mus | MPGFTCCVPGCYNNSHRDKALHFYTFPKDAELRRLWLKNVSRAGVSGCFSTFQPTTGHRLCSVHFQGGRKTYTVRVPTIFPLRGVNERKVARRPAGAAAARRRQQQQQQQQQQQQQQQLQQQQPSPSSSTAQTTQLQPNLVSASAAVLLTLQAAVDSNQAPGSVVPVSTTPSGDDVKPIDLTVQVEFAAAEGAAAAAAASELEAATAGLEAAECTLGPQLVVVGEEGFPDTGSDHSYSLSSGTTEEELLRKLNEQRDILALMEVKMKEMKGSIRHLRLTEAKLREELREKDRLLAMAVIRKKHGM | Transcriptional repressor that plays a central role for embryogenesis and the pluripotency of embryonic stem (ES) cells. Sequence-specific DNA-binding factor that represses gene expression in pluripotent ES cells by directly binding to key genetic loci and recruiting epigenetic modifiers. | Q9JJD0 |
P70901 | VLP12_BORHE | Variable large protein 12 | Borrelia | MRKRISAIIMTLFMVLASCSNQLEAEKLAAESKNTFFDSLVKIGQGFQDIFGIFGNAIGDALGFNAVKSDDKRSKVGEHFEGVGKGLKDTKIKLDELLKEVTAAPHADTTEVKSVINSASAVLTKLIDSVTKLAGAVGNTDIADGVSIANGAAAEEASVKTVIEGVKEIIDVATNSGVKIEKGNAGTAVANANGPKAIIHNAQAAAGDATKLADEVAKADPWAMIDKIKNAKTKNGIAAANDDAGQLATATNAANNNGTAATNADLAAAVALKAMAKGGKFTQPAANEDGAVKAAAASAVNKVLGILDVIIRKAVNLELGKIKEAVKGIKYSEATGEATESDTAQPITNKSSN | The Vlp and Vsp proteins are antigenically distinct proteins, only one vlp or vsp gene is transcriptionally active at any one time. Switching between these genes is a mechanism of host immune response evasion. | P70901 |
Q291E4 | VIR_DROPS | Protein virilizer | Sophophora | MTEVDDGAELLFFDTFSHEDITDINLDLVQFPKPVFITQVRIIPLGARVQADFPGGVRLGATNPSKFDLEFFVNDLGMPGASAFENLGLLRYNQNDCIHLDCSREKIPTDGLVLRGWYSTITLAVYGILTNSVTQPIASPTLPCEPAGPEMCNLSTEAHNVLLQEEVLKDDWAEPIPTELLVPHKAVVVSDYEHDDIEYGLSREHQHYHQHVDEEQREMRRLRRSTHSTDRSPPPPPMRTHTHSESNEREYIRCSRDKGSRDWSRSPEYSSHRSRRKRSDRSRSDADEHKWPRTPPASIDSPIRPRSPDAMDYDDDDSRSHYKMQASRGYRHSSESLHRDRDDEERSGTPQEQFEPILSDDEIIGDDEEDEAEDVAAAAEYERELEFAAAVAPPAIDAFEPWQRPLLVYEGDLAAHLNKELETLRLLFKKLSLQTRCESVTAFSDEHGLSADEREQFVYLGEQLNNQLGYLSQHYKRRNFVLQQFFSHDDAHLRQAANVLQVALSFQAACMQPQPAFKIRHIKLGARMAELLGSNEQLFGHLLQEQDFDLFEAVLSLYKEPYMALSIKLQLLKAVYAMLDTRLGVQNFLSPKTNGYQMVMDFLKTAKLTRTKYALQAIIKKLHLYEALASVQQCCRQIFLDTDASVPETTPDPNRLDVCQKIEFAFQMLMDALTDSQLSYQQPRRFLPVSKKFEVLTDPTAQRSFGNALQSYFVQHSLAEALLVILSNPKEVPASTFLCTLDLMHTLLRSHVGIDYFVDDAFPVTQMIVSILLGLEEVPSQPRVVEAKPEGKEDKPMDDSVEQKPDEGKAAGIRAAEEPKMAPPPVVRKPILRPVLPRLARLGIELSYKVQTRYHLDAITFTAACPEYDTIKIATHMHSIYSQTCDPSGRQHTIEVLGLNNNLKIFMDLIKKEQRLQTQRQLLSSPGTKYKSPVLSYAVDMVDACVRYCEQLDYLIEHGGVILELAKNHETFEPSVSAVLQEMYVYMKPLEAINVFVYDDIMPLVEVIGRSLDYLTTFPGDLIMALRILRFLAISKPRQKSHGTEELKHRFVALQLYAADGVQLLLQIMERLCTHFEQPGIHAPALMTIQGVHCCQIMLPTLQILRELLSYAILCRDGTYKDLTAIDHLVKVYYLLYYYPSRCQAGAEVEQCKLEVVKSLLAYTQPHEQDAESLHKSLWTLMVREVLKNIDGPAHFIPGLKLLAELLPLPLPMPQPLCDQLKQQHKQRLIIERKLWSAHLHPQSGQIAKLVEALAPSSFPQLAELLQRVCMQLSDLAPNMTLLIAKTITELLCTEYQTSNCIPTTNLERLLRFSTRLCAFAPLKSSMLSILSGKFWELFQSLLALNEFNEVVTNCQEAVHRILDSFLDSGISLISHKSTAQPALNLSAALPPKELIPRIIDAVFSNLTSVEVTHGISILAVRNLVILTEHDFTFYHLAQLLKQKLTEFQAWMERVILHNETVEYHANIESLILLLRSLTQIEPPPPMCAMPNRTLKLGAMELAQLVEFQDIDMARPPVLARILRVLEKYKLLANEAALCDLKQLIVLHASRQEAMGSASMETPAVETENDGANPAASCSTSSSGGSLNVEPFLPQAEGIVTQYDARPIFTRYCATAENPQLTARYWLEPLPIELIEDMNEPLYERIACDLTDLANVCLNPDLATSGESKRTLNLSGSPQSNREMTPTAPCFRTRRVEVEPATGRPEKKMFLSSVRGRGFARPPPSRGDLFRSRPPNTSRPPSLHVDDFLALETCGAQPTGPTGYNKIPSMLRGSRVGRNRGSRISAAAAFRQKKMMRIGSPSSWTESGGGSYRSTSESHFGGSDSHYSSPHYSGRSRGRGLRSRPPYLR | Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of mRNAs, a modification that plays a role in the efficiency of mRNA splicing and is required for sex determination. Required for sex determination and dosage compensation via Sxl alternative splicing: m6A methylation acts as a key regulator of Sxl pre-mRNA and promotes female-specific alternative splicing of Sxl, which determines female physiognomy. M6A methylation is also required for neuronal functions. Required for proper inclusion of regulated exons in Ubx transcripts, leading to isoforms Ia/b and IIa/b. | Q291E4 |
Q29VN1 | TPS3_MAIZE | Probable terpene synthase 3, chloroplastic | Zea | MYSLPGATMSAAPARVISSSSSSSFVEPLLLAAASSAAANSHHQVRQRGHLVRTLAASSSSNTLLRSDFDLQEGLTTDVKRMLRQRQKKSGGGREMLVTIDNLKRLCIDHFFEEEIEGAMATGACTRLLHSDDLFDATLAFRLLREAGHDVSAKEDVLRRFIDGVSGDFKLSLNNDVRGLLGLHDMSHLDVGGEEAALLHRAKEFSSSHLASAVRYQDNPSLAEYVRQSLDHPYHLSLTQYKARHHLRYLQSLPSSCRDAAVERLAVAEFQLNKSLHQREMREIKRWWMDLGLAEEIPVVRDQVMKWYMWSMAALQGSSFSRYRVYVVDDIFDLVGTLEELSAFTEAVKMWDTAAADSLPSCMRSCYKALHTVTNEIAEIAHKEHGSNPINRLRKAWVVLFDGFMVEARWLATDQVPTAEDYLRNGVVTSGVPLTFLHIFSMLGYDDPSTEEEEEAIIDHMPSIISCPAKILRLWDDMGSAEDEAQEGFDGSYRDFYLMENPSRSPGEAEAHMRGLIAREWVELNRECFCRRTFPSDIAQVCLNTARMVSVMYSYNKEQRLLVLEDYAAMMLVL | Probable terpene synthase. | Q29VN1 |
Q757R0 | VAC8_ASHGO | Vacuolar protein 8 | Eremothecium | MGGCCSCLKESQDDATVLPIAENEREAVTSLLGYLEDKDNYDFYSGGPLKALTTLVYSDNLNLQRSAALAFAEITEKYVRPVDREVLEPILILLQSHDPQIQIAACAALGNLAVNNENKILIVEMGGLEPLIEQMKSNNVEVQCNAVGCITNLATQDDNKAKIAHSGALVPLTKLAKSKNIRVQRNATGALLNMTHSGENRKELVDAGAVPVLVSLLSSSDADVQYYCTTALSNIAVDESNRRKLSQTEPRLVSKLVVLTDSPSARVKCQATLALRNLASDTGYQLEIVRAGGLSHLVKLIQCNSMPLVLASVACIRNISIHPLNEGLIVDAGFLKPLVKLLDYNDNEEIQCHAVSTLRNLAASSEKNRQEFFESGAVEKCKQLALVSPISVQSEISACFAILALADNSKLELLDANILEALIPMTFSTNQEVAGNAAAALANLCSRINNYEKIIESWTEPSKGVCGFLIRFLQSEYPTFEHIALWTILQLLESHNETMLGLIKSNKEIVKSIKRLSDINYENAQKASSLHSRLQQVNGGSVASGSEQYEHASLELYNITQQIMQFLN | Functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole. | Q757R0 |
Q6BQJ1 | TVP38_DEBHA | Golgi apparatus membrane protein TVP38 | Debaryomyces | MPRLPSSSDPFQGHNELPQSNNFMSRTNSIIQDKLFLVRNVGQQTLDWYQSQPLWKRTLLQVLFVFNAIVVVLIMIFHKSIIQAIVVISDKWHGLKFGQGLLFTLVFMVGFPPLLGFSALSMLAGMVYGFVHGWILLACASISGSFCSFLVFRYLLHSRAERLMNSNKKFRAFSEILREDSSLFILVLLRLCPLPYSLSNGALAAIPELPATTYFLASLITSPKLMIHIFVGHKLKELGDDTKGKSTHLIDILSIIITGAAASLTTYIIYNKMQRKLEFYHQRGIIPRDDAIIFGNFEDIESANNVELNSADYDEDNFIIEDEDDENATDPDYVASKKNIQVHAEDQNKNGEFEIDENDGVDDLGLGEISKNSKQNTNGYRDY | Golgi membrane protein involved in vesicular trafficking and spindle migration. | Q6BQJ1 |
A1WUY5 | UPPP_HALHL | Undecaprenyl pyrophosphate phosphatase | Halorhodospira | MALWIAVLLGVVQGIFMFLPVSSTAHMVLLEHWLIGRDHPMPAPESAEMILFNLVVHVGTLVSIVVVFAPSLLRFTRYSLRDAYGWARAGRFQGPPLYARLFLLGMLSVLFTGVVGLTLKATFEQVFANPWMIAFTLILTGALLFWTDKLPPRRRGLRQTGVGTATLIGVAQGFALMPGLSRSAMTIVFGLFAGLKRRWAAEYSFFLAIPTICAATLLQAIEVYQLGGLESVSVAALITGFVVAAGVGIVSLKLVIYFLYRAQLKVFSFYVWALAAAILLGWIDLPI | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | A1WUY5 |
Q6ANL3 | UBIE_DESPS | Demethylmenaquinone methyltransferase | Desulfotalea | MRAQSCSLFLEMKCREEFVLSKGPGVEKMFDAIAGRYDLMNKVMTMGQDQRWRRFVVAKAGDPGAGQVLDLATGTGDIAALMHRSYPRAQVTGGDFSRNMLEEAKKRFAGQGIDWQVCDANKLPFADNTFEAVTFGYLLRNVDDASSVLAEVYRVLKPGGRCVCLDTTPPAKNIIYPFVQFYFRYGIPLLGRMIAADEAAYAYLSGSTMEFHSAEVLADLFRGAGFVDVHYKKFMLGTIGIHWGVK | Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2). | Q6ANL3 |
P25040 | TSR4_YEAST | 20S rRNA accumulation protein 4 | Saccharomyces | MSKIEELPPSDTDDHSYSSKPGDVFLAFVDAPVKETDDILVEDSFIGGEPKWLHPDSEPPAELLKCGACKSADNMKLLLQAFSPLDDEQMSAIQQRLGINNMSYINPQDDRVLYVFLCTECQRKGNSVRCIRGVKKNKNVDSLSEKMASTSLEKDFQINPFDLSNNSDSKCNAFSSNPFGGANANPFGADSINSNISQSKDEGKKKESATVSAKTARKLHDLQKDKEYDGNKCFKSCLLYVEEETFKNKKPAHLQLPKNLKIDKEALDLTGDEDLEKDPIKLDPRTEKLSKFLDDDTFQKFQEVVGYNPLQVLRYDLGGKPLLYAETKVDILSTVPRPGYNPSSQRIFEMQLMPKMIFDLEEVVSVDNGMEWGTILVFTDVENYMPEFDEHGVGYVEECVKVQWESRT | Required for processing of the 20S pre-rRNA at site D to generate mature 18S rRNA. | P25040 |
Q1BV59 | TYPH_BURCA | TdRPase | Burkholderia cepacia complex | MFLPQEFIRRKRDGQPLDRDDMAAFVRGVTDGSVTEGQVAAFAMAVYFNDLSTDERVALTLAQRDSGDVLDWRALDLGGPVIDKHSTGGVGDVVSLMLGPMVAACGGYVPMISGRGLGHTGGTLDKLSAIPGYDVMPDTDAFRRTVREVGVAIIGQTARLAPADKRIYAIRDVTATVESVAMITASILSKKLAAGLDGLVMDVKVGSGAFMPTAEKSAELARSIVDVGNGAGMKTTAILTDMNQSLAPCAGNALEVACAIDYLTGKSRPARLHDVTMALSAELLVTGGLARDAAHAREKLQQALDSGAAAERFARMVAALGGPADLLDAPARHLARAAVIVPVPAPVSGVVQRVDCRALGLAVVALGGGRTRAEDAIDVSVGLSALAEIGQRIEAGEPLGFVHARDEAAAAHAVDAIRRGYVLGETGEAPPTLYQRVD | The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis. | Q1BV59 |
A0R2W4 | ZFPP_MYCS2 | Z-isoprenyl diphosphate synthase | Mycolicibacterium | MDIIPPRLKEPAYRIYEMRLRHELVRSKAQLPRHIAVLCDGNRRWARDAGYDDVSIGYRKGAAKIAEMLRWCQAAGIEMATIYLLSTENLQRDPDELTALIEIITDVVEEICAPYNKWSVRTVGDLELLGDEPARRLREAVESTTTKGANFHVNVAVAYGGRQEIVDAVRSLLSKELANGATAEQLIEAVTVDGISENLYTSGQPDPDLVIRTSGEQRLSGFLLWQSAYSEMWFTEAYWPAFRRVDFLRALRDYTARHRRFGK | Catalyzes the condensation of only one isopentenyl pyrophosphate (IPP) unit in the cis configuration to E-geranyl diphosphate (E-GPP) generating the 15 carbon product (2Z,6E)-farnesyl diphosphate (Z-FPP or EZ-FPP). Z-FPP is the precursor of decaprenyl diphosphate, which has a central role in the biosynthesis of the mycobacterial cell wall. | A0R2W4 |
P53378 | TBG_YEAST | Gamma-tubulin | Saccharomyces | MGGEIITLQAGQCGNHVGKFLWSQLAKEHAIGTDGLSQLPDSSTERDDDTKPFFRENSRNKFTPRAIMMDSEPSVIADVENTFRGFFDPRNTWVASDGASAGNSWANGYDIGTRNQDDILNKIDKEIDSTDNFEGFQLLHSVAGGTGSGLGSNLLEALCDRYPKKILTTYSVFPARSSEVVVQSYNTILALRRLIEDSDATVVFDNASLLNISGKVFRNPNIDLQHTNQLISTIISSVTNSIRFPSYMYSSMSSIYSTLIPSPELHFLSPSFTPFTSDYIHDDIAHKGHSSYDVMLDLLDPSNSLVSTAMNNPTYFNVYNTIIGNVEPRQISRAMTKLQQRIKFPSWSSSAMHVNIGRRSPYLPLQPNENEVSGMMLSNMSTVVNVFENACNTFDKVFAKGAFLNNYNVGDLFQSMQNVQDEFAESREVVQSLMEDYVAAEQDSYLDDVLVDDENMVGELEEDLDADGDHKLV | Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly. TUB4 is an important spindle pole body component that organizes both cytoplasmic and nuclear microtubule arrays. | P53378 |
Q0HHM8 | TOLB_SHESM | Tol-Pal system protein TolB | Shewanella | MKILAKWLALAVLLCTMPAKAALDIVITEGVDAARPIAVMPFQWQGAGAPPQAIADVVMSDLIRSGTFKPLDELGLPQRGIGALAQFDASAWANVGAEAVVVGSVKPYGTDQFLVSFDLIDLVKAQNQALKGPTSATEFLMDSRQTVISAAQFRQYGHRISDIVYEKLTGIRGAFLTRISYVVVNHSQKAAYSLMIADYDGYNEQMLLRSPEPLMSPSWSPDGRRLAYVSFENKKAEIFVQDLYTQVRTKVSSFPGINGAPTFSPDGKSLAVTLSKDGQPEIYVIDIATKAAKRITNHYSIDTEPSWYPDGKSLLFTSERGGRPQLYRVDLNSGKVTRETFEGEWNLGGSITPDGRSMIFVNRTNGKFNIARMDLSTRFMQVLTSTRLDESPSVAPNGTMVIYGTTYQGKQVLAAVSTDGRFKARLPVGQGEVKSPSWSPFL | Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. | Q0HHM8 |
Q88NN6 | URODH_PSEPK | Hexuronate dehydrogenase | Pseudomonas | MTTTPFNRLLLTGAAGGLGKVLRERLKGYAEVLRLSDISPMAPAAGPHEEVITCDLADKAAVHTLVEGVDAIIHFGGVSTEHAFEEILGPNICGVFHVYEAARKHGVKRIIFASSNHTIGFYRQDERIDAHAPRRPDSYYGLSKCYGEDVASFYFDRYGIETVSIRIGSSFPQPQNLRMLCTWLSYDDLVQLIERGLFTPGVGHTIVYGASDNRTVWWDNRHAAHLGYVPKDSSETFRAAVEAQPAPAADDPSMVYQGGAFAVAGPFN | Catalyzes the oxidation of beta-D-galacturonate and beta-D-glucuronate to galactarate and D-glucarate, respectively. | Q88NN6 |
O84030 | TRMD_CHLTR | tRNA [GM37] methyltransferase | Chlamydia | MEIDILSLFPDYFASPLQATILGRAIKQGALSVRSRDIREFGLGKWKQVDDSPYNGEGMLLMAEPVVQAIRSIRRKKSKVIYLSPQGQLLSAKKSRELASCSHLVLLCGHYEGIDERALTAEVDEEISIGDYVLTNGCAAALVLVDALARFIPGVLGNQESAEYDSLENGLLEGPQYTRPRVFEGESVPEVLLCGDHQKIADWRKQVSLERTRERRPDLYLQYFYGNSACLSTQEDLPRIEVVSPKTFSVVLEVQDLRKAKKFYSRMFGKECWDGDKLFLLGKTSLYLQQTKETRGPTTVFIELETDHDFVRFLKRWEILGGELGEQGTGGFPLRQVFDLDGHIWVVSCVQK | Specifically methylates guanosine-37 in various tRNAs. | O84030 |
Q17ZL5 | Y048_HELAH | Nucleoid-associated protein Hac_0048 | Helicobacter | MDFSQLSGLLDGVKKEFSQLEEKNKDTIYTSKSGGGMVSVSFNGVGELVDLQIDDSLLEDKEAMQIYLMSALNDGYKSVEENRKNLAFSMLGNFAKL | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | Q17ZL5 |
Q6FYF1 | TSAD_BARQU | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Bartonella | MRLLGIETSCDETAAAVIEHNIEGNSQILSNIVWSQTDNHAPYGGVVPEIAARAHVEILDDLILKALTDAHTKLKDIDAIAVTSGPGLIGGLLVGVMSAKALSLATGKPFIAVNHLEGHALTAVLTHNVAFPYLLLLVSGGHTQTILVHEVGNYQRLGTTIDDALGEAFDKTAKLLGLPYPGGPALEKAALLGDKNRISLPRPLKGEKRLDFSFSGLKTAVRQAATAMSPLTENDVADIAASFQAAVTDTVYDRVHLALQYFTHQYPLSHYKGRRPPALVVAGGVAANQAIRLTLQELAHQHGFEFIAPPLSLCTDNAAMIAFAGAQKFARGEKNSFDIAPRSRWPLDEKAAPLIGTGRRGTKA | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. | Q6FYF1 |
Q0SX94 | ULAR_SHIF8 | HTH-type transcriptional regulator UlaR | Shigella | MTEAQRHQILLEMLAQLGFVTVEKVVERLGISPATARRDINKLGESGKLKKVRNGAEAITQQRPRWTPMNLHQAQNHDEKVRIAKAASQLVNPGESVVINCGSTAFLLGREMCGKPVQIITNYLPLANYLIDQEHDSVIIMGGQYNKSQSITLSPQGSENSLYAGHWMFTSGKGLTAEGLYKTDMLTAMAEQKMLSVVGKLVVLVDSSKIGERAGMLFSRADQIDMLITGKNANPEILQQLEAQGVSILRV | Represses ulaG and the ulaABCDEF operon. | Q0SX94 |
Q7VQU0 | UBIA_BLOFL | 4-HB polyprenyltransferase | Candidatus Blochmannia | MYKRCIGFIKLMRVHQPVGFFLLLWPTLWALWITNRGIPDFIVLSLFIVGVMCMRSAGCVINDYIDYDIDMCVQRTIRRPIVIGSVKKQEALWVFFILILIALIVVCVFNNIIAVFLSLIVLGLSIIYPYLKRYIYLPQLVLGIIFSWSILIVYTVMNCAVNKTTWLLFLANTIWVVLYDTEYAMVDRDDDKCIGIKSSALLFGKIDKIVIGILQLLTVFILYIIGIVEQLPIIFYLFSIVGASILFIWQQVLIFNRNREKCLWAFLSNSYVGMLIFVGIVLSF | Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate. | Q7VQU0 |
Q9Z964 | TRMD_CHLPN | tRNA [GM37] methyltransferase | Chlamydia | MKIDILSLFPGYFDGPLQTSILGRAIKQRLLDVQLTNLRDFGLGKWKQVDDTPFSGGGMLLMAEPVTSAIRSVRKENSKVIYLSPQGALLTAEKSRELAAASHLILLCGHYEGIDERAIESEVDEEISIGDYVLTNGGIAALVLIDAVSRFIPGVLGNQESAERDSLENGLLEGPQYTRPREFEGKEVPEVLLQGDHKAISQWRLEQSERRTYERRPDLYLNYLYKRSIDHKFDEETTTNRDHFKCDKISVVLEVNKLKRAKNFYCKVFGLDAMSCENKFCLPHEGKTIFWLREVQAEKKNIVTLSLSLDCACEEDFCYLLRRWELFGGKLLEKQADEHAVWALAQDLDGHAWIFSWHRMK | Specifically methylates guanosine-37 in various tRNAs. | Q9Z964 |
P47370 | THIO_MYCGE | Thioredoxin | Mycoplasma | MVTEIRSLKQLEEIFSAKKNVIVDFWAAWCGPCKLTSPEFQKAADEFSDAQFVKVNVDDHTDIAAAYNITSLPTIVVFENGVEKKRAIGFMPKTKIIDLFNN | Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | P47370 |
A1CEK1 | VPS27_ASPCL | Vacuolar protein sorting-associated protein 27 | Aspergillus subgen. Fumigati | MAGWFSSSSPLDEQVERATSSSLEDIALNLEISDLIRSKSVQPKEAMRSLKRRLENRNPNVQIATLKLTDTCVKNGGTHFLAEIASREYLDNMVSLLTAEGAPLNSDVKEKMLELIQDWAMAAQGRMDLNYLGETYRKLQSEGFRFPPKSEISGSMLESSAPPEWIDHDVCMRCRTPFSFMNRKHHCRNCGNVFDAQCSSKTLPLPHLGILQPVRVDDGCYAKLTSKSFTPSTLSDRSAFKNNSITKANAMEPRGARAEGGFDDDLRRALQMSLEEAQNRGSGGYIPQPKVNEPSNATIQPHPQDEEDADLKAAIEASLRDMEEHKKKHAAALKNNTVATDSTAQDTGSALPMPKNPYELSPVEVENIHLFAALVDRLQHQPPGTILRESQIQELYESIGTLRPKLARSYGETMSKHDTLLDLHAKLSTVVRYYDRMLEERLSSAYSQHSLGYGQAPGGSQYPNMYPSMPSQAVEGKSGAENFYYGNAVPERSPPAHSTYAYQQGIAPSGPMSSGMYPQPGQALPSNPAWNGNAPPTTASPQLSTSSTPFPNHPVGYPAPSAPTQYYAPTAPPEQDANTYSTPRPGETEVSHQASPVMRRDSYYQSAGAPPSAPEPSPPSEHGQSSGYMQYADSRTMPPNSQYPPQQQPSAQPYYSQQPPPQATPHTTYSQPPAAPYETHPVADVSPIGAPVPSAPYQQPAPTRPAVEESLIEL | Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane. | A1CEK1 |
P05823 | TNR0_ECOLX | Transposon Tn2501 resolvase | Escherichia | MSRVFAYCRVSTLEQTTENQRREIEAAGFAIRPQRLIEEHISGSVAASERPGFIRLLDRMENGDVLIVTKLDRLGRNAMDIRKTVEQLASSDIRVHCLALGGVDLTSAAGRMTMQVISAVAEFERDLLLERTHSGIARAKATGKRFGRPSALNEEQQLTVIARINAGISISAIAREFNTTRQTILRVKAGQQSS | Resolvase catalyzes the resolution (a site-specific recombination) of the cointegrated replicon to yield the final transposition products. | P05823 |
Q12NB8 | THIG_SHEDO | Thiazole synthase | Shewanella | MFTLADHTFSSRLLTGTGKFTNSHTMLASIVASESQIVTLAMKRIDLKLGQDDILTPLLAQGLTLLPNTSGARNAKEAIFAAELARDLLDTHWLKLEIHPDPKYLMPDPIETLLAAEKLCQMGFKVLPYVHADPVLCRRLEEVGCAAVMPLASPIGSNQGLATEAFLKIIIEQAKVPVIVDAGLGAPSQACRAMEMGADAVLVNTAIASSRSPIIMAKCFADAVKAGREAYLAGLGQVQPHASHTSPLTGFLQQMPAENTNTVEPL | Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. | Q12NB8 |
Q8FBI6 | TATC_ECOL6 | Sec-independent protein translocase protein TatC | Escherichia | MSVEDTQPLITHLIELRKRLLNCIISVIVIFLCLVYFANDIYHLVSAPLIKQLPQGSTMIATDVASPFFTPIKLTFMVSLILSAPVILYQVWAFIAPALYKHERRLVVPLLVSSSLLFYIGMAFAYFVVFPLAFGFLANTAPEGVQVSTDIASYLSFVMALFMAFGVSFEVPVAIVLLCWMGITSPEDLRKKRPYVLVGAFVVGMLLTPPDVFSQTLLAIPMYCLFEIGVFFSRFYVGKGRNREEENDAEAESEKTEE | Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides. | Q8FBI6 |
Q8FAJ3 | ULAA_ECOL6 | Ascorbate-specific permease IIC component UlaA | Escherichia | MEILYNIFTVFFNQVMTNAPLLLGIVTCLGYILLRKSVSVIIKGTIKTIIGFMLLQAGSGILTSTFKPVVAKMSEVYGINGAISDTYASMMATIERMGDAYSWVGYAVLLALALNICYVLLRRITGIRTIMLTGHIMFQQAGLIAVTLFIFGYSMWTTIICTAILVSLYWGITSNMMYKPTQEVTDGCGFSIGHQQQFASWIAYKVAPFLGKKEESVEDLKLPGWLNIFHDNIVSTAIVMTIFFGAILLSFGIDTVQAMAGKVNWTVYILQTGFSFAVAIFIITQGVRMFVAELSEAFNGISQRLIPGAVLAIDCAAIYSFAPNAVVWGFMWGTIGQLIAVGILVACGSSILIIPGFIPMFFSNATIGVFANHFGGWRAALKICLVMGMIEIFGCVWAVKLTGMSAWMGMADWSILAPPMMQGFFSIGIAFMAVIIVIALAYMFFAGRALRAEEDAEKQLAEQSA | The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate transport. | Q8FAJ3 |
A8F821 | THIC_PSELT | null | Pseudothermotoga | MTQMEIAQKGTSSEEMKRVAEYEEMNLEVIRQKLAYGKAVLPKNKLHKIEKPMIVGEGFTVKVNANIGTSQAFFSLEEEKEKARVAIEYGADSLMVLSTWGDLKEIRKAIIDLSAVPVGSVPIYDSAMKSYQLKKNVVDFSEKDFLNMVISHAEDGIDFMTIHAGITKKVLEHVKNSGRILKVVSRGGAIIAGWMIKNNKENPFYEYFDELLDIAKDYDITLSLGDGMRPGTVLDASDVQQFEELFVMRELVEKAREKGVQVMLEGPGHIPLNEVELNVKLMKKIGEDAPIFLLGPLPTDRAMGYDHIACAIGGALAGYYGADFLCYVTPSEHISLPTIEDVREGVIASKIAAAIADLARGNRKAWWLEKQMALSRKNFNWEEMFKLSLGKDLARKKYKERPYLHEGCSMCGPFCAIKIVEEFF | 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. | A8F821 |
P34710 | UNC6_CAEEL | Uncoordinated protein 6 | Caenorhabditis | MITSVLRYVLALYFCMGIAHGAYFSQFSMRAPDHDPCHDHTGRPVRCVPEFINAAFGKPVIASDTCGTNRPDKYCTVKEGPDGIIREQCDTCDARNHFQSHPASLLTDLNSIGNMTCWVSTPSLSPQNVSLTLSLGKKFELTYVSMHFCSRLPDSMALYKSADFGKTWTPFQFYSSECRRIFGRDPDVSITKSNEQEAVCTASHIMGPGGNRVAFPFLENRPSAQNFENSPVLQDWVTATDIKVVFSRLSPDQAELYGLSNDVNSYGNETDDEVKQRYFYSMGELAVGGRCKCNGHASRCIFDKMGRYTCDCKHNTAGTECEMCKPFHYDRPWGRATANSANSCVACNCNQHAKRCRFDAELFRLSGNRSGGVCLNCRHNTAGRNCHLCKPGFVRDTSLPMTHRKACKSCGCHPVGSLGKSCNQSSGQCVCKPGVTGTTCNRCAKGYQQSRSTVTPCIKIPTKADFIGSSHSEEQDQCSKCRIVPKRLNQKKFCKRDHAVQMVVVSREMVDGWAKYKIVVESVFKRGTENMQRGETSLWISPQGVICKCPKLRVGRRYLLLGKNDSDHERDGLMVNPQTVLVEWEDDIMDKVLRFSKKDKLGQCPEITSHRY | Component of an extracellular matrix cue that guides dorsoventral migrations on the epidermis . Required for the guidance of pioneer axons and migrating cells along the body wall . In particular, it is required for the guidance of axons from neurons, including SubL neurons and AIY interneurons, into the nerve ring . During gonad morphogenesis, involved in distal tip cell (DTC) migration from the dorsal side of the hermaphrodite body to the midbody to allow for formation of gonad arms . Its association with either unc-40 or unc-5 receptors will lead to axon attraction or repulsion, respectively . Involved in dendritic morphogenesis; may act by association with unc-40 at the tips of growing dendrites for interaction with unc-5 on the apposing branch to induce mutual repulsion . Involved in the positioning of ray 1, the most anterior ray sensilium, in the male tail . Required for the formation of synapses between the AVA interneurons and the PHB sensory neurons . | P34710 |
V9QFH8 | TXA2_STEGR | Latrodectin-2 | Steatoda | MFKLICIVFIATILSITSAADNEDELTIEDFLSYECNESMDIEELKEKDKVCSRCANLHKTQSVIERCRLNCFTSEYFKNCEDNLQAKEEEPEEETL | May increase the toxicity of alpha-latrotoxin and/or other venom components. Is non-toxic to mice and to the cockroach Periplaneta americana. | V9QFH8 |
Q6C705 | TRM82_YARLI | Transfer RNA methyltransferase 82 | Yarrowia | MKHPYHIVSLSPDGKTMYAAAARQVDRICLETGECKSTVVEESATRTTTKTGDKPAAAKRTKYLPTSVSHVRSLQLSKGGKYLLATTDETKSLVLLDPTTLEVIKKVQYPKRPSAVATDKEDLNIVLGDKFGDVYGESVEDLLKVEGELKDEPVLGHVSMLTALELGYDSKDRPYVISADRDEHIRISRFPASHVIEQFCFGHQQFVSSLLINDLDASILFSAGGDDEIFVWDWLNGKQLQKLSLREHVESYLNEAHIYVDKKGVATTHKEITVSSLQQIKDTPYLLVNVESTNAIIVLKIVDNKLEVASVFATEAHVISFSVAGNLLVTSEVGSEGVKAYTITDGVVTKSDKEIPFGSCEYEDDSELISLFSTKSLRKRGEF | Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit. | Q6C705 |
Q81XH4 | YIDC1_BACAN | Membrane protein YidC 1 | Bacillus cereus group | MLKSYRAVLVSLSLLLVFVLSGCSNATPIDAHSTGIWDHYFVYPISFMIQFVAHHIPGASFGIAIIIMTLVIRSAMIPLAVSQYRSQAKMKKMQPELQKLKQKYGDVSKDLEKQKQYQKEMSELMKSGGWNPLAGCWPLLIQMPIFSALYYAISRTEEIRTSTFLWVNLGHADPYHILPIIAALTTFIQMKVFQSNSTSGEQVQMLKMQQIMMPAMILFMGFAAPSGLVLYWITGNLFTMMQTIVLRKIMEREELQLQKA | Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. | Q81XH4 |
A1A1N2 | TPIS_BIFAA | Triose-phosphate isomerase | Bifidobacterium | MGPKRIPLVAGNWKMNFDHLEATYFVQQLAWNLRAIHFDYKRCEIALMPSFTSLRSVQVAVESDNLKIRYGAQAVSVTSQGAFTGDVSADMIAHLGCSYVIVGHSERRKYHPEDDANIVDQVRAVLAAGMQPILCVGESYEERRKGIELDFAVGQVHDVTRDLSDEEAAKLIVAYEPVWAIGTGMVATPQSAQDAARAIRNDLSDTFGTRVGETVRILYGGSVSSKNAVELINEPDVDGFLIGGSALKVDELTRICKLTLETTA | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | A1A1N2 |
A5DH87 | TVP38_PICGU | Golgi apparatus membrane protein TVP38 | Meyerozyma | MPRLHSASEPPATGFFARVRNELGNRTEGLHQINNQALDWYRSQSQIRQILIQIGGVVAIVIGVLVLIFHKYLIELLVIISDDWAKLPGGRLILFLLVFFVGFPPLIGYSALSLLAGMVYGFPYGWPLLASASVSGSFVAFLVFRYFLRSQGERLVNSNEKFRAFAEILREDSSLFLLVLIRLCPLPYSLSNGALAAIPELSAWVYLGASVITSPKMLIHLFVGHKIKEFGDAKTDTSTKIIDVISILVTGAAASLTTFIIYRKMQQKLHHNRAGANYDAFVFGNFDDLESGTNVELNSADFDQDNFIITDDELEEEEPNGSHTATATQVQVARRNCSKAMTICTLMFV | Golgi membrane protein involved in vesicular trafficking and spindle migration. | A5DH87 |
C5BAT7 | ZAPA_EDWI9 | Z ring-associated protein ZapA | Edwardsiella | MSAQPVDIQIFGRALRVNCPPEQLDALNQAAEDLNQRLQDLKVRTRVTNTEQLVFIAALNVCHELAQERLKTRDYAANMEQRIRMLQQTIEQALLEQGRITERPGTSFE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. | C5BAT7 |
O57486 | TDT_AMBME | Terminal deoxynucleotidyltransferase | Ambystoma | MYAFPTTRIAPRRKQPKCIKPPKCTSKYDIKFKDIAIYILERKMGASRRYFLMELARKKGFRVEPDLSEYVTHVVSEKNSGAEVLEWLQAKKAGSIPNVAILDISWFTDCMGAGQPVEIERKHRLTLQKICVCKSPSPVVPSRVGVSQYACQRKTTLDNKNTLFTDAFEILAENYEFRENERSCLSFRQAASVLKSLTFTIAGMADVDGLPGFGDHIRAVIEDLIEDGESSKVSEVLNDEVYRSLKLFTTIFGVGLRTAEKWHRLGIRTLEEIKSNENLKFSKMQIAGLQHYEDILGGVRKAEADAVAMVVRDAVWTFLPDAVVTLTGGFRRGNKTGHDVDMLITSPIQGKEKELLHKVINLWKKQDLLLCHTIHESTMDEDNLPSKSVNLLDHFQKCFAILKSNQHRGEISSCDGPHDSRERGKRIWKAIRVDLVFCPFEQYAFALLGWTGSRQFERDLRRYASHEKKMMIDNHALYDKTKRVFVKCESEEEIFGHLGLEYIDPVERNA | Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells. | O57486 |
B2UW67 | UREE_HELPS | Urease accessory protein UreE | Helicobacter | MIIERLIGNLRDLNPLDFSVDYVDLEWFETRKKIARFKTRQGKDIAIRLKDAPKLGLSQGDILFKEEKEIIAVNILDSEVIHIQAKSVAEVAKICYEIGNRHAALYYGESQFEFKTPFEKPTLALLEKLGVQNHVLSSKLDSKDRLTVSMPHSEPNFKVSLASDFKVVMK | Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. | B2UW67 |
Q9P4D3 | TPS2_ZYGRO | ZrTPS2 | Zygosaccharomyces | MVNSGHRRQRIINCVAQLPYKIQLGETNDEWNIVPATGSSSLYSSIEYLNSEEKAKDYEQHVLGWTGEIGRESLPSRLFNSKNRDKSENGEKGENDLHAKEEREKEEDPLYLTNDQIDGITKDLRRHGKSDDHYNVDNVHPVWLLRRDQKRWRGFAENVLWPTFHYILKFSSDSGEKENLSWYDYVRFNEAYAMKIGEIYEKGDIIWIHDYYLLLLPQLLRMKFNDQDLTIAYFHHSPWPSNEYFRVLPRRKQILDGLMGADRGWFQNEGFARHFVSSCKRLLDSTSRKSKNRLGMEQYQISAYGGDIVVDSLPIGINRVKLLEDTFTKDIAQKVLAIKDAFQGKKIIVGRDRLDSVRGVVQKLRAFETFLSMYPEWRDQVVLIQVSVPSMKGGTNQLIRLEQQVNELVTSINMQYGSLNFSPVHHYYMRIPKDVYLSLLRVADLCVIASVRDGTNTTALEYVTVKSHMSNYNCYGNPLILSEFSGTSTILKDAMIINPWDSVAVAKSINRALSLSRDEKRALEDKIWPQVPTIQKWTDQFLSTLSDIVDEAHNTTDRKMTPALNRPALLEHYRQSKRRLFLFDYDGTLTPIVQDPAAAIPSARLISILQKLASDPCNQIWIISGRDQAFLNKWLGSRLPQLGLSAEHGCFYKDVDEENWINLTEKFDMSWQEKVGSIMEEFTRRTPGSFIERKKVALTWHYRRADPELGEFYASELKKELDKICADYDLDVMEGKANIEVRPKFVNKGEIVKRLVWHHHGRRQDMLNTKKEELPISEMPDFTLCLGDDFTDEDMFNQLNDIEAVWKKQYEDEVNQWGGFGLYPCTVGSASKKTVAKAHLTDPQQVLDTLGLLVGDVSLFQSAGTVELDSRGHVKHSDSSIRSEQASARYAMKRQQSYKN | Phosphatase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-alpha-D-glucose in a two step process. | Q9P4D3 |
A4XYV5 | THIE_PSEMY | Thiamine-phosphate pyrophosphorylase | Pseudomonas | MTAALRGLYAITDTPLLAGGKLLPYAEAALIGGARLLQYRDKSGDAVRRLDEAQALAELCQRHGATLIINDDLELAAHLGVGLHLGQTDGSLAAARARLGADVVIGGTCHAQLELAERAVAEGASYIAFGRFFNSNTKPGAPAATVELLDQARTRFAQPIVAIGGVTLDNAPGLIARGASMVAVIHALFAADSALEVQDRARAFAALFD | Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). | A4XYV5 |
B4R966 | YQGF_PHEZH | Putative pre-16S rRNA nuclease | Phenylobacterium | MAVVDLIDLPAIAPPNTPLVGLDLGEKTIGVAVSDATRMVASPLGLIRKTKFTDDAKALFKLMESRRASGIVIGLPVNMDGTEGTRCQSNRAFARNLLRLREDLPIAFWDERMSTMAVNRMLVGEADMTRARRADVVDKMAAAWILQGALDRLRNL | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | B4R966 |
Q64P45 | TRMB_BACFR | tRNA(m7G46)-methyltransferase | Bacteroides | MGKNKLEKFADMASYPHVFEYPYSAVDNVPFDMKGKWHKEFFKNDNPIVLELGCGRGEYTVGLGRMFPDKNFIAVDIKGARMWTGATESLQAGMKNVAFLRTNIEIIDRFFAEGEVSEIWLTFSDPQMKKATKRLTSTYFMERYRKFLVSNGIIHLKTDSNFMFTYTKYMIEENGLPVEFITEDLYHSDLVDDILGIKTYYEQQWLDRGLSIKYIKFLLPQEGELREPDIEIELDSYRSYNRSKRSGLQTSK | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | Q64P45 |
Q6MTM6 | TMFO1_MYCMS | Folate-dependent tRNA(M-5-U54)-methyltransferase 1 | Mycoplasma | MKTIRIIGAGLSGCEAAYYLLKKGYFVELYEIKTIKKNPIQHYDYFCELAYSDSFRSTDLNTSVGTLKKELELLDSLIIKAAKYASINQNNELVVNRIEFSKYITNYLKTFNNLKIIEQEYLNIDLNIPTIIAIGPISTPSFLTNLKKIINKKNLKLFDTVEPTILKQSINKNICYSLDNNLDYLYCDLNKEQFEKFYNALISAKTFNSPLKNEIKLLEKNNYFSIESLAKNKQEFINHFKPINNNAYITITLKKDSVIDNLYTIVNFQTSLMWNEQLKVFSLIPGLENLKIMRYGVMHKNNYINTKKLLNLGVQLKTNKNIFFAGQIIGVDGYVESVCSGLISAINLDRYLNNKKMILPNKNSTIGSLYNYLLKTDSNFNPMRINWALVDLIDGFELSDNSKKFYSKRAIELIKQYLKKINYK | Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. | Q6MTM6 |
Q92GI1 | YBEY_RICCN | Endoribonuclease YbeY | spotted fever group | MINVEIVRNYNKWREHKQINKSLIKKITQNILLRFDNFSKIKQFELSILLTNAAEILTLNKQFRNIEKATNVLSFPSNELNWQDLYSKLEFLGDSDYMHLGDIAFCYEVIYNESCEQHKTFENHFIHLLIHSILHLIGFDHQNDTEANIMENLEIEILSYFGIFPPY | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | Q92GI1 |
Q5L5L8 | TRMD_CHLAB | tRNA [GM37] methyltransferase | Chlamydia | MKIDILSLFPEYFDSPLRSSILGRAIKRGLLDIQSRDIREFGLGKWKQVDDAPFNHDGMLLMAEPVVKAIRHVKRSDSKVVYLSPQGQLLTAKKSRELAQCSHLIFLCGHYEGIDERALESEVDEEISIGDYVLTNGGIAALVVIDALSRFIPGVLGNQESADKDSMENGLLEGPQYTRPRVFEGREVPEVLLHGDHQAIAKWRKQISLDRTRERRPDLYIRYLYDRENEEVTQQETDLKQSMLEGESAVILEVEDLHRSRKFYSKMFRLNQPVNNRLHIPGKTQMTIHLQEVGLKSKNIVLLSLRLGCKDDFFSFLGRWKMLGGTLEQADDRGEVRLVRDFDGHVWAISCKQAE | Specifically methylates guanosine-37 in various tRNAs. | Q5L5L8 |
Q9HSG5 | TRUD_HALSA | tRNA-uridine isomerase D | Halobacterium | MREAHPIERAVGMAYYASDSDGTGGRLRDSPADFRVRELEAFDTQPADAPTGDYPWLVVRATLHEWDTNDFARELANTVGMSRERVRWAGTKDRHAVTTQLFAVRDLDAAQVPEIRNADIEVVGRAGRGLEFGDLAGNAFEIVVRDPDAPERAAAVADELAAFGGGTVGTPNYFGQQRFGSKRPVTHEVGLAILRDDWEAAAMAYLGAPTEHEPADSQRAREYVAETRDWTGALAEFPQRLRYERTMLHELADGGSFRDAVETFPSNLQQLFVHAAQSYVFNRIVSERMARGLPFGEPVAGDVVWFADSDADAAVAQPDAARQQRVTDSRVDVMARHCERGRAFVTAPLVGTDTEFADGDPGEITRGVLDDLGLSRADFDLPGEFDSAGSRRAILLRPDLTVSHDPLAFEFALPSGSYATVVLREFLKPSPLAL | Could be responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. | Q9HSG5 |
Q9FPH3 | THA2_ARATH | Threonine aldolase 2 | Arabidopsis | MVTPTTIRTVDLRSDTVTKPTESMRSAMANAEVDDDVLGNDPTALRLEKEVAEIAGKEAAMFVPSGTMGNLISVLVHCDERGSEVILGDDSHIHIYENGGVSSLGGVHPRTVKNEEDGTMEIGAIEAAVRSPKGDLHHPVTKLICLENTQANCGGRCLPIEYIDKVGELAKKHGLKLHIDGARIFNASVALGVPVKRIVQAADSVSICLSKGIGAPVGSVIVGSKKFITKARWLRKTLGGGMRQIGVLCAAALVALHENVAKLEDDHKKARVLAEGLNRIERLRVNVAAVETNIIYVDIPEDPKFGAEEACKSLEDVGVLVIPQATFRIRIVLHHQISDVDVEYVLSCFEKIFHS | Threonine aldolase involved in threonine degradation to glycine. May play a role in the removal of L-allo-threonine. | Q9FPH3 |
B3EE09 | THIC_CHLL2 | Thiamine biosynthesis protein ThiC | Chlorobium | MNTFSDNIFCPEHRMYGNASKKTHTKGCIHPIEVGMRTLSLTKTYTCRGIEFSSIPLYDTSGPYSDPSVIINPEKGLNPLRDKWKFNSENTEPVSEQGNETAAARVPLRAKKGCSVTQLAFARKGIITPEMEYVAIRENQQLEEWIASFPIGGKTAEPFTAEFVRQEVAAGRAIIPANINHPELEPMIIGRNFRVKINANIGNSAMGSSIEEEVEKAVWACRWGADTVMDLSTGTNIHQTREWILRNSPVPIGTVPMYQALEKAGGVAENLTWELYRDTLVEQAEQGVDYFTIHAGILQEHLPAAGRRMTGIVSRGGAIMAKWCKTNNRENFLYTHFDEICEILRSYDIAISLGDALRPGCIADANDEAQFGELKVLGELTLLAWEHDVQVMIEGPGHVPLNLVEENMRKQLELCHGAPFYTLGPLITDIAAGYDHINSAIGGTLIAAYGCSMLCYVTPKEHLGLPDKNDVREGVVVHKVAAHAADIAKGNPTAWLQDELMSRARYAFAWEDQFNLSLDPVKARVLYAESRAASGQTDGNPDFCTMCGPDFCSMKRSQEK | 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. | B3EE09 |
A0AJ83 | TRPD_LISW6 | Anthranilate phosphoribosyltransferase | Listeria | MESLLQKVYDQENLTKAEMNILATEIFEGRLSKTKMAAFLMALKVKGETAEEMAGIAEAMQEVAIQVAFPAGTAMDNCGTGGDKSNSFNISTTSAFVLAAAGIPVAKHGNRSISSRSGSADVCQELGIDINMRPEDMTYLLEKVGIAFLFAPHVHPNMKYVMDVRKELGTPTIFNLIGPLTNPVHLETQLMGIYRRDLLKQTAEVLGQLGRKRAVVLNGAGFMDEASLAGENHYALYESGEVQLFTLSPEEVGLANYPLEAIRGGDAKENAAILRSVLEGEPGAHLDTVLLNAGFGLFASGKVATVKEGVNLARDLVRSGLAKQKLADLITYQKEVLTK | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | A0AJ83 |
Q03A83 | TARI_LACP3 | Ribitol-5-phosphate cytidylyltransferase | Lacticaseibacillus | MITAIVLAGGVGKRMGMEIPKQFVMVNEKPIIIYTLESFDRHPKIDQVVVVCKQGWADTMWGYIREFGIKKVKWVISGGSIVQKSINNAVQFLSDKCVEDDIVVIHDGIRPLVDEHVLSDVIVKCQEYGNAVTSLPYNEQIFIKETEKTTNKYIDRNTLRRVSTPQAYKYEVLHDAYDEAISQNIGMVDSAYTNTMMVDLGHTLYFAAGSDKNIKLTTTDDLALFKAYLREKEL | Catalyzes the transfer of the cytidylyl group of CTP to D-ribitol 5-phosphate. | Q03A83 |
O32125 | YUTF_BACSU | 5'-nucleotidase YutF | Bacillus | MKTYKGYLIDLDGTMYNGTEKIEEACEFVRTLKDRGVPYLFVTNNSSRTPKQVADKLVSFDIPATEEQVFTTSMATAQHIAQQKKDASVYVIGEEGIRQAIEENGLTFGGENADFVVVGIDRSITYEKFAVGCLAIRNGARFISTNGDIAIPTERGLLPGNGSLTSVLTVSTGVQPVFIGKPESIIMEQAMRVLGTDVSETLMVGDNYATDIMAGINAGMDTLLVHTGVTKREHMTDDMEKPTHAIDSLTEWIPYI | Catalyzes the hydrolysis of various purine and pyrimidine 5'-nucleotides, showing preference for 5'-nucleoside monophosphates and exhibiting the highest catalytic activity toward 5'-XMP . Shows also a relatively high phosphohydrolase activity toward the nucleotide precursors ribose-5-phosphate (R5P) and 5-phosphoribosyl-1-pyrophosphate (PRPP), and toward the non-natural substrate p-nitrophenyl phosphate (pNPP) . | O32125 |
B0U620 | UNG_XYLFM | Uracil-DNA glycosylase | Xylella | MNEQGEAINSSAESRIQLESSWKAHVGNWLLRPEMRDLSSFLRARKVAGVSVYPPGSQIFAAFEATPFQRVKAVILGQDPYHGQGQAHGLCFSVRPGMPLPPSLLNIYKELEEDLGLLRPDHGCLLPWANRGVLLLNAVLTVEDGRAGAHQGKGWEGFTDHVVDTLNREREGLVFMLWGSYAQAKGKVIDTRRHLVLKAPHPSPLSAHRGFLGCRHFSLCNQYLSQHGLGMVDWSLPPCIALDGAILNGRIAV | Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | B0U620 |
P60938 | UPPP_GEOSL | Undecaprenyl pyrophosphate phosphatase | Geobacter | MDIMHAAVLGILQGLTEILPISSSAHLILVPWLLGWPESGLTFDVGLHVGTLIALCVYFRRDIAYLISDAITGLREGFGSQTSRLPFFIIAGTVPAAIAGKTLEKPIEEFFRGSHTLIALLLIAFGLLLALADTTGPKRWRMDRVDLRGALLIGLAQCLALIPGVSRSGITITAALFLGFTRDTAARFSFLLSLPIVAGAGILKMGELARHGIPAGELAPLLAGMATSAVSGYLGVALLLRLVQRYSLYPFVWYRLLAGGAVLAYLFAR | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | P60938 |
Q6S9E0 | TTP_SHEEP | Zinc finger protein 36 | Ovis | MDLAAIYKSLLSLSPELPSDLGETESSTSWASSGPWSLSSSDSSLPEAAARLPGRSTSLVEGRSCGWVPPPPGFAPLAPRPSSELSPSPTSPTATPTTSSRYKTELCRTFSESGRCRYGAKCQFAHGLGELRQPSRHPKYKTELCHKFYLQGRCPYGSRCHFIHNPSEDLAAPGHPHVLRQSISFSGLPSGRRTSPPPASLAGPSVPSWSFSPSSSPPPPPGDLPLSPSAFSAAPGTPVSRRDPTPACCPSCRRATPNSVWGPVGGLARSPSAHSLGSDPDEYASSGSSLGGSDSPVFEAGVFGPPQPPAAPRRLPIFNRISVSE | Zinc-finger RNA-binding protein that destabilizes numerous cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis. Acts as an 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery. Recruits deadenylase CNOT7 (and probably the CCR4-NOT complex) via association with CNOT1, and hence promotes ARE-mediated mRNA deadenylation. Functions also by recruiting components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs. Self regulates by destabilizing its own mRNA. Binds to 3'-UTR ARE of numerous mRNAs. Binds also to ARE of its own mRNA. Plays a role in anti-inflammatory responses; suppresses tumor necrosis factor (TNF)-alpha production by stimulating ARE-mediated TNF-alpha mRNA decay and several other inflammatory ARE-containing mRNAs in interferon (IFN)- and/or lipopolysaccharide (LPS)-induced macrophages. Also plays a role in the regulation of dendritic cell maturation at the post-transcriptional level, and hence operates as part of a negative feedback loop to limit the inflammatory response. Promotes ARE-mediated mRNA decay of hypoxia-inducible factor HIF1A mRNA during the response of endothelial cells to hypoxia. Positively regulates early adipogenesis of preadipocytes by promoting ARE-mediated mRNA decay of immediate early genes (IEGs). Negatively regulates hematopoietic/erythroid cell differentiation by promoting ARE-mediated mRNA decay of the transcription factor STAT5B mRNA. Plays a role in maintaining skeletal muscle satellite cell quiescence by promoting ARE-mediated mRNA decay of the myogenic determination factor MYOD1 mRNA. Associates also with and regulates the expression of non-ARE-containing target mRNAs at the post-transcriptional level, such as MHC class I mRNAs. Participates in association with argonaute RISC catalytic components in the ARE-mediated mRNA decay mechanism; assists microRNA (miRNA) targeting ARE-containing mRNAs. May also play a role in the regulation of cytoplasmic mRNA decapping; enhances decapping of ARE-containing RNAs, in vitro. Involved in the delivery of target ARE-mRNAs to processing bodies (PBs). In addition to its cytosolic mRNA-decay function, affects nuclear pre-mRNA processing. Negatively regulates nuclear poly(A)-binding protein PABPN1-stimulated polyadenylation activity on ARE-containing pre-mRNA during LPS-stimulated macrophages. Also involved in the regulation of stress granule (SG) and P-body (PB) formation and fusion. Plays a role in the regulation of keratinocyte proliferation, differentiation and apoptosis. Plays a role as a tumor suppressor by inhibiting cell proliferation in breast cancer cells. | Q6S9E0 |
A5WDG7 | TRPA_PSYWF | Tryptophan synthase alpha chain | Psychrobacter | MTRIESTFETLKAQNKKALIPYVMAGDPSPNSFVDLLHDLVKHGADMIEVGLPFSDPMADGPTVALAGERALAGGTSTHQALAIVKKFREQDSSTPIILMGYLNPIEIIGYEAFIALCHESGVDGVLVVDLPPAESGNFVERLAAHDINKIFLLSPTTLPERRKQVMTHCGGYIYYVSLKGVTGSASLDTQAVGEQVQAIKQETNLPICVGFGIRDGQSAAAIGQYADGVIVGSELVKNFSGLSHTSRAEDIATAQASIMTKMDELRQALDALSA | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | A5WDG7 |
Q9KS29 | TTCA_VIBCH | tRNA 2-thiocytidine biosynthesis protein TtcA | Vibrio | MTAQTQELTKAQQYNFNKLQKRIRRNTGQAIADFNMIEDGDRIMVCLSGGKDSFTMLDILMSLQKSAPISFELVAVNLDQKQPGFPEHVLPEYLESLGVEYKIVEEDTYAIVQDKVPEGKTTCALCSRLRRGILYRTAKELGATKIALGHHRDDILETLFLNMFYGGKMKGMPPKLVSDNGEHVVIRPLAYCREKDIIKYSDMRGYPIIPCNLCGSQPNLQRQAVKQMLNDWDKRFPGRIETMFRAMQNVVPSHLADFSLFDFKSIDKNSGVINGGDIGFDKEEIAPQVVEDEDLVMEFDPSLQLNVTNI | Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. | Q9KS29 |
B0SB32 | YBEY_LEPBA | Endoribonuclease YbeY | Leptospira | MNPSLSVFTHWNDESNQSEIFSDPVISNCEKILRFLAPEFLHSLELSIYLVNDSLMAEINEERRGKPATTDVLSFPLYSEHPPIPVQILGEVVISMETCKKQAMEIGHGLVDEFYRLLVHGILHNFGYDHETNEEDALLMRKMEDECLDLVFAT | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | B0SB32 |
Q5CZA5 | ZN805_HUMAN | Zinc finger protein 805 | Homo | MAMALTDPAQVSVTFDDVAVTFTQEEWGQLDLAQRTLYQEVMLENCGLLVSLGCPVPRPELIYHLEHGQEPWTRKEDLSQGTCPGDKGKPKSTEPTTCELALSEGISFWGQLTQGASGDSQLGQPKDQDGFSEMQGERLRPGLDSQKEKLPGKMSPKHDGLGTADSVCSRIIQDRVSLGDDVHDCDSHGSGKNPVIQEEENIFKCNECEKVFNKKRLLARHERIHSGVKPYECTECGKTFSKSTYLLQHHMVHTGEKPYKCMECGKAFNRKSHLTQHQRIHSGEKPYKCSECGKAFTHRSTFVLHNRSHTGEKPFVCKECGKAFRDRPGFIRHYIIHSGENPYECFECGKVFKHRSYLMWHQQTHTGEKPYECSECGKAFCESAALIHHYVIHTGEKPFECLECGKAFNHRSYLKRHQRIHTGEKPYVCSECGKAFTHCSTFILHKRAHTGEKPFECKECGKAFSNRADLIRHFSIHTGEKPYECMECGKAFNRRSGLTRHQRIHSGEKPYECIECGKTFCWSTNLIRHSIIHTGEKPYECSECGKAFSRSSSLTQHQRMHTGRNPISVTDVGRPFTSGQTSVNIQELLLGKNFLNVTTEENLLQEEASYMASDRTYQRETPQVSSL | May be involved in transcriptional regulation. | Q5CZA5 |
Q0VLN5 | UBID_ALCBS | Polyprenyl p-hydroxybenzoate decarboxylase | Alcanivorax | MKYRDLRDFISQLEQLGELKRITVPVDPKLEMTEICDRTLRAGGPALLFENPVGFGTPVLGNLFGTERRVALGMGRDSVAELRELGELLAFLKEPEPPKGFRDAWEKLPVFRKVLSMSPKVSSSGPCQEKVLEGDEVDLYKLPIQTCWPDDAGPLVTWPLVITRGPNKERQNLGIYRQQLIGRNKLIMRWLSHRGGALDFQEWQQQHPGEPFPVSVALGADPATILGAVTPVPDTLSEYAFAGLLRGSKTELVKCIGNDLQVPASAEFVLEGFLYPGDMADEGPFGDHTGYYNEVERFPVFTVERITHRRNPIYHSTYTGRPPDEPAVLGVAMNEIFVPILKKQFPEIVDFYLPPEGCSYRMAVVTMKKQYPGHAKRVMMGVWSFLRQFMYTKFVIVCDDDVNARDWKDVIWAMTTRMDPARDTVMIENTPIDYLDFASPVAGLGSKMGMDATNKWAGETTREWGRAIAMDPAVKTRVDEMWSSLGIDTPE | Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis. | Q0VLN5 |
Q0HE99 | UBIB_SHESM | Ubiquinone biosynthesis protein UbiB | Shewanella | MTLASIRRGYHVIKTLLQYGLDDVLPPKMTPWYFKLARNSLFWIRNKHKGKSGGERLKLAMQELGPVYIKLGQMLSTRRDLLSDEWANELAMLQDKVPPFDGALARQAIETELKAPIESFFDDFNETPLASASISQVHTATLKSNGKAVVLKVLRPNVEAKIQADLLLMSQTAKIIDYLLGEGNRLRPSEVIEDYRVTILGELNLKLEALNAIKLRNNFLDSDALYIPYVYEEFCYPRLMVMERIYGIPVSDIAALKAQGTNFKLLAERGVELFFTQVFRDNFFHADMHPGNIFISRDHPENPYYIGLDCGIMGTLSEVDKRYLAENFLAFFNRDYHRIAQLYIESGWVSEKTDLQAFEQAIKVVCEPMFNKPLDEISFGHVLLELFRTARHFDIVVQPQLVLLEKTLLYIEGLGRQLYPQLDLWQTAKPFLEQWMAEQVGPKAMFKKVSTKLPYWSDKLPEFPELIYDNLKLGRKLLSSQQQMLDKYLKYQQQAHKSNYLLITSAILLICGTLLFNQDATLWSPYVCLISGAALWIIGWRSRPKNRKF | Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis. | Q0HE99 |
Q0ASJ7 | TRUA_MARMM | tRNA-uridine isomerase I | Maricaulis | MPRYRITIEYDGRPFSGWQRQDNAPSVQESLERAAEKLDGAPVLVYGAGRTDSGVHALAQVAHLDLAKDLSTDKVRDAINYHLKPDPVAVIEAARVSDDFHARFSATRRHYLYRMIDRRAPLTLDRGQVWRVTRKLDAEAMHHAAQALLGQHDFTTFRDAQCQAESPVKSLDAISVSRYGEEVQLTCSARSFLHRQVRSMVGSLVEVGVGKWSARDFKRALDAADRSRCGPVAPADGLYLTAVDYPGPA | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | Q0ASJ7 |
Q68W09 | YBEY_RICTY | Endoribonuclease YbeY | typhus group | MINVEIVRNYNKWREHRKINKGLIKKITQNVLVRFDHFDKIKQFELSILLTNTAEILTLNQQFRSIEKATNVLSFPNNELNWHNLYSKLEFLYYSDYMHLGDIAFCYEVIYNESCEQQKTFENHFIHMLIHSILHLIGFDHQNDTDANIMESLEIEILSYFGIPSPY | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | Q68W09 |
A5V9W7 | TRPA_RHIWR | Tryptophan synthase alpha chain | Rhizorhabdus | MTRLAETFARTRAEGRAALVTFVTGGDPTPGDMGPILDALVAGGADVIELGMPFTDPMADGPAIQRANLRALGAGTTTADLLAIAAAFRQRHPSVPLVLMGYANPMVRRGPEWFAAEAAKAGVDGVICVDIPPEQDGALGPALRAAGVAPIRLATPTTDAARLPAVLEGASGFLYYVSVAGITGMQQAGQASIEAAVARFKAATDLPVAVGFGVRGPEQAEAIGRVADGVVVGSAIVDLIGEHGAAAAGPVRDFTATLSAALRRAAQEKAA | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | A5V9W7 |
Subsets and Splits