habdine/Prot2Text-Data · Datasets at Hugging Face

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
A1AWH8	PURA_RUTMC	IMP--aspartate ligase	Candidatus Ruthia	MSKNVVIIGTQWGDEGKGKVVDLITDKVASVVRFQGGHNAGHTLVINGKTTILHLIPSGILRNHVECLIGHGVVLSMSALLKEIAELEVADIDTTKRLKISPGCPLILPYHIELDNAREIKRGKAAIGTTGNGIGPAYEDKVARRGLRVSDLLDPNLFASKLKEVMEYHNFFLTHYYNANPVDYQTTLDEVLSQVEQTKHMIVDVTEQIHQHIANDENILFEGAQGALLDIDQGTYPFVTSSNTTSGAAVTGSGIGVTDIDYVLGIVKAYTTRVGGGPFPTELIYDVALDKGDEIGKVLGTVGHEFGATTGRQRRCGWLDMVTLKRSFNLNAVTGICLTKLDVMDTLETIKICTSYEIDGVETTIPPFSAEDYAKAKPIYIKIPGWKTSTIGTDSFDSLPVEAQSYIRKIEQLANLPVDILSTGPDRLQTLILKHPFE	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.	A1AWH8
O75081	MTG16_HUMAN	Zinc finger MYND domain-containing protein 4	Homo	MPASRLRDRAASSASGSTCGSMSQTHPVLESGLLASAGCSAPRGPRKGGPAPVDRKAKASAMPDSPAEVKTQPRSTPPSMPPPPPAASQGATRPPSFTPHTHREDGPATLPHGRFHGCLKWSMVCLLMNGSSHSPTAINGAPCTPNGFSNGPATSSTASLSTQHLPPACGARQLSKLKRFLTTLQQFGSDISPEIGERVRTLVLGLVNSTLTIEEFHSKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARLAKQTPAQYLAQHEQLLLDASASSPIDSSELLLEVNENGKRRTPDRTKENGSDRDPLHPEHLSKRPCTLNPAQRYSPSNGPPQPTPPPHYRLEDIAMAHHFRDAYRHPDPRELRERHRPLVVPGSRQEEVIDHKLTEREWAEEWKHLNNLLNCIMDMVEKTRRSLTVLRRCQEADREELNHWARRYSDAEDTKKGPAPAAARPRSSSAGPEGPQLDVPREFLPRTLTGYVPEDIWRKAEEAVNEVKRQAMSELQKAVSDAERKAHELITTERAKMERALAEAKRQASEDALTVINQQEDSSESCWNCGRKASETCSGCNAARYCGSFCQHRDWEKHHHVCGQSLQGPTAVVADPVPGPPEAAHSLGPSLPVGAASPSEAGSAGPSRPGSPSPPGPLDTVPR	Isoform 2 functions as an A-kinase-anchoring protein .	O75081
A0RQI7	RL10_CAMFF	50S ribosomal protein L10	Campylobacter	MTRNEKAEIISNLEAEFKTSDAIVVCDYKGLSVKKLEALRNSARELNVKVQVVKNTLANIALNNCGKSGMELKDTNIFVWGEDQLAVTKVVAKFEESNNELFKIKTAHIDGEVASVSKVVALSKMPSRDELIAMLLQVWNAPIQNFTIGLNALREKKEQTA	Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.	A0RQI7
A5IHB4	TRMB_LEGPC	tRNA(m7G46)-methyltransferase	Legionella	MQRKIKSYVLRAGRISNRQQQGLDLWLEDYELKFDSPSPWNFAKEFGRHDADTIVEIGFGMGTSLFTMAMNNPQCNYLGIEVHKAGVGSLVADLHEHQITNVRVVVHDAVDVLQTKIPENSLAGVQIFFPDPWHKKRHHKRRLIQSEFIQMLVKKIRPSGFIHCATDWEDYAEHILNVLSSESALFNQQKEGGYSPRPDSRPLTKFEQRGERLGHGVWDLVFIKK	Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.	A5IHB4
Q3KM49	TAL_CHLTA	Transaldolase	Chlamydia	MSSQFDQLKLWSVLVGDTGDPALIKTLGVQDATTNPSLILKVAQEPKYQSMLKEAISWGIRQNGDDVQTLTFVLDKIQVNLGLEILKHVPGRVSLEIDARLSFNTEAMVQRAIFLSQLFEKMGGDKKRLLVKIPGTWEGICAAEVLESQGIACNVTLIFNLVQAIAAAKAKVTLVSPFVGRIYDWWIAAYGAEGYSIEADPGVASVANIYSYYKKFDIPTQIMAASFRTKEQVLALAGCDFLTISPKLLEELKKDQQPVERKLSVEEAKKLDIQPVELSESVFRFLMNEDAMATEKLAEGIRIFSGDTQILESAVTEFIRQIAAQEA	Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.	Q3KM49
P60980	VSTX1_GRARO	Voltage sensor toxin 1	Grammostola	MKTSVFVLVLGLVLLFAVSFATEMEESARECGKFMWKCKNSNDCCKDLVCSSRWKWCVLASPF	Inhibits sodium channels Nav1.7/SCN9A and potassium channels Kv11.1/KCNH2. Also binds the voltage-sensor domain of the potassium channel KvAP (from the archaeon Aeropyrum pernix) with very slow apparent binding kinetics and affects channel gating. Reaches its target by dynamically partitioning into anionic or zwitterionic headgroup lipid membranes. May bind to the open state of KvAP.	P60980
A5CCV6	YQGF_ORITB	Putative pre-16S rRNA nuclease	Orientia	MIINSISEFLQAADIKKQILGIDFGEKKVGVAISNIEHTVAMPLQTILATNQDRVNKIQEIAVAYNIGAIVIGLPFKLDGTETSQTHRVKDFANKLANKLLLPIFLCDERLTSKAANNLLKIGNIKRKVRNAIDDRVAASIILEGALKRMQNSKSYF	Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.	A5CCV6
B3DI94	TM186_DANRE	Transmembrane protein 186	Danio	MDMMMMSTRLIHLSRHFPQYGFRCHPSGLISSARMQYNINNGLAHMGKQMPNTSTHTTRIHPASFSSDLASRKYSLIYAFPLIRGLRALSRLKLLQTGITVVLLPTVYYLHLQGQASVLVLNRSIGIALFAGVMLYSISHFVRRVVGMMYLDSTQTILKVSHLSFWGHRRDIYVPVSDVVTLGDSGDSRGESILRLKRYSTSNTMYFSTRLGRVVDRHAFGKVFGSLS	May be required for efficient assembly of the mitochondrial complex I.	B3DI94
Q5NRF6	YBEY_ZYMMO	Endoribonuclease YbeY	Zymomonas	MITVEADISDLWPEQSNWEALAQTACQQAVSVSASDFLLAKDYETEISVCFSDNDTVHALNKTWRDKDRPTNVLSFPMMEAEELAEIKNRVGSECLLGDIILAFDVAKKEALEKGISLENHVTHLITHGTLHLLGYDHILDNEAEIMEDLERKALAQLDIPDPYSDHETGKEGLDG	Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.	Q5NRF6
Q12LA0	TIG_SHEDO	PPIase	Shewanella	MQVSVETTEGLGRRLTISVPAEQIEKMVKDGITREAKRARLPGFRPGKVPLSEINKRYGQAIRQDVMGEVMQRNFIEAIIAEKLNPAGAPTFMPGKSVGESFEFVATFEIYPEITLTGLDTIAVEQPKAEVNDADLDAMIETLRKQHATFAVVERASAAGDKVKMNFVGSIDGEEFDGGKADDFELEIGSNRMIPGFETGVTGHKAGETFDIEVSFPEDYHAENLKGKAAKFAITLTEVQAAQLPEVNDEFATLFGITSGGVDALKAEIRKNMTRELEQALKANVKEQVINGLLAANDVTIPSALIDGEVEVLRKQAMQRFGGQTKNMPELPAELFTEQAERRVKIGLLLGEVIKTSELKAEDSRVQALIASMASAYEDPAEVVAYYNSNKEMMQNMRNVALEEQAVEALLKSAKVTTKEVAFEEFMNKASGRA	Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.	Q12LA0
Q110N2	TATA_TRIEI	Sec-independent protein translocase protein TatA	Trichodesmium	MNIFGIGLPEMIVILVVALLIFGPKKLPEIGRSLGQAINSFKAGARDFENEFKREAKHLEEGVKVSTSASEPEKVVDVSSATNTNKN	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. TatA could form the protein-conducting channel of the Tat system.	Q110N2
D0KWI6	TATC_HALNC	Sec-independent protein translocase protein TatC	Halothiobacillus	MTERDSSPEADKNGLADVVEETGMAGFLGHLVELRNRLLKGVLAVLVLFLILFPFRNELFTMLADPLSRHMPAGSTMIAVEVASPFFIPLKLTALTAVFIAIPFLLYQLWAFIAPGLYKHERKLVAPLVFSSTILFYLGAAFAYFVVFPVVFGFLSTAGPSDVNFAPDIGEYLSFVTSLFFAFGFVFEVPVAIVLLVIVGVVTPDKLAGFRRYAILIAFIIAAILTPPDVLSQFMMALPIIMLYEFGLFVSRFFYKAKLARAAEVEAEESGAADDESDEAVSARHAEYEAKAQTQADEPLDMDKAFDEAEADQRRLESDSSASDDGPESNTAGRTEEGEQPSTGSKPEDEPNAPSEPSPKKPDSPV	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.	D0KWI6
P11019	VATE1_BOVIN	Vacuolar proton pump subunit E 1	Bos	MALSDADVQKQIKHMMAFIEQEANEKAEEIDAKAEEEFNIEKGRLVQTQRLKIMEYYEKKEKQIEQQKKIQMSNLMNQARLKVLRARDDLITDLLNEAKQRLSKVVKDTTRYQVLLDGLVLQGLYQLLEPRMIVRCRKQDFPLVKAAVQKAIPVYKVATKRDVDVQIDQEAYLPEEIAGGVEIYNGDRKIKVSNTLESRLDLIAQQMMPEVRGALFGANANRKFLD	Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons . V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment .	P11019
Q2NW05	TYPH_SODGM	TdRPase	Sodalis	MFLAQEIIRKKRDGEPLSDEEIRFFINGVYDNTVSEGQIAALAMTIFFHDMDLQERVALTLAMRDSGHTLDWRREALGGPVVDKHSTGGVGDVTSLMLGPMIAACGGFVPMVSGRGLGHTGGTLDKLEAIPGLAIFLDDDAFRSQVKQVGVAIMGQTHSLAPADKRIYATRDITATVDSIPLITASILAKKLAEGLDALVMDVKVGSGALMPTLAGSEALAQAIVGVANGAGCRTIALLTDMNQVLASSAGNALEVREAVRFLTNDERNPRLFEVTMALCSEMLMIAGLAHSEDAARTALVRALDSGEAAERFGRMVAVQGGPADFVQRYDLYLPVATLSKPVFPAGEGYIRSMDTRALGMTVVALGGGRQRARDAIDYSVGLTEMARLGDYVDANTPLAVVHAASEESWARAAEAVRAAIQLGDVAPQALPVVYRRITAAAD	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.	Q2NW05
O94265	THI21_SCHPO	Hydroxymethylpyrimidine phosphate kinase 1	Schizosaccharomyces	MISTCITVAGSDCSGGAGVQADLKVFTAHSVYGMSAVTAITSQNTIGVNGVHLIPASYVEQQISACLLDVHCEVMKTGMLFNQQILKVIVESIDRFKIKKVVVDPLIATRKGALLVMPDYLELFVKELIPRAEVLIPNIAEALIILKHMTNEFVEIHHLEDVKAVGKKLIKAGCKNVVIRCDDIPFASDFFCSRETNMPPTWYLYVLCTSEGEVLLPQKWLASKTARGTSCALSSAVASNLAIGLDLVTATQNAVSYTQRALEMSFHLGRGANSLDYASALTRLPYEKGEFINFVRYHPSITPKWLSIVNHPFVEQLKAGTLSRLPFQKYLVLKYHMLINNAQAAGMMAFSSSSISAIEHSAKIIQAIKEENVTHLRICEQYGLSASQITKSKPEIVKSHSLFIHDTAQQDGLRGIQIAMLPFVFMIQEVVSQISASDGYPYVAWVEHCKDKSATSHIETLLESLETNSQIISLSKVQHLLGILEKSLDFERLVLDTSSSNESSVF	Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.	O94265
O22349	TBA3_ELEIN	Alpha-3-tubulin	Eleusine	MREIISIHIGQAGIQVGNACWELYCLEHGIEPDGTMPSDTSVGVAHDAFNTFFSETGSGKHVPRAIFVDLEPTVIDEVRTGSYRQLFHPEQLISGKEDAANNFARGHYTVGKEIVDLCLDRVRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQIISSLTTSLRFDGAINVDVTEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVPEITNAVFEPSSMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTVQFVDWCPTGFKCGINYQPPSVVPGGDLAKVQRAVCMISNNTAVAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGAEGADDEGDEGEDY	Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.	O22349
P93083	TDC2_CAMAC	Tryptophan decarboxylase TDC2	Camptotheca	MGSIDSNYDTESAGQCRPLEPEEFRKQAHQMVDFIADYYKNIESYPVLSQVEPGYLQSRLPETAPYRPEPFESILKDVHKDIIPGVTHWLSPNFFAYFPATVSSAAFVGEMLCTCFNAVGFNWLASPAELELEMVVMDWLASMLKLPNSFTFLGTGGGVIQGTTSEAILCTLIAARDRALESIGVDSIHKLVVYGSDQTHSTYAKACNLAGILPCNIRSIRTEAVANFSLSPDSLHREIEADVAAGMVPLYLCATVGTTSTTAIDSLSPLADVANDYGLWFHVDAAYAGSACICPEFRHYLDGIERADSLSLSPHKWLLSYLDCCCLWVKRPSVLVKALSTDPEYLKNKPSESNSVVDFKDWQVGTGRRFKALRLWFVMRSYGVANLQSHIRSDIQMAKMFEEFVNSDPRFEIVVPRVFSLVCFRLNPFSKSDPCNTELLNRKLLEWVNSTGQVYITHTKVGGVYMLRFAVGATLTEEHHVSAAWKLIREGADALLCS	Involved in the biosynthesis of tryptamine. Supplies tryptamine for the indole moiety of camptothecin (CPT), an anti-cancer monoterpene alkaloid. Represents a key step in monoterpene indole alkaloid biosynthesis. Is specific for tryptophan, and inactive against tyrosine, phenylalanine and 3,4-dihydroxyphenylalanine (dopa).	P93083
Q9S7B5	THRC1_ARATH	Protein METHIONINE OVER-ACCUMULATOR 2	Arabidopsis	MASSCLFNASVSSLNPKQDPIRRHRSTSLLRHRPVVISCTADGNNIKAPIETAVKPPHRTEDNIRDEARRNRSNAVNPFSAKYVPFNAAPGSTESYSLDEIVYRSRSGGLLDVEHDMEALKRFDGAYWRDLFDSRVGKSTWPYGSGVWSKKEWVLPEIDDDDIVSAFEGNSNLFWAERFGKQFLGMNDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMKRPVVGVGCASTGDTSAALSAYCASAGIPSIVFLPANKISMAQLVQPIANGAFVLSIDTDFDGCMKLIREITAELPIYLANSLNSLRLEGQKTAAIEILQQFDWQVPDWVIVPGGNLGNIYAFYKGFKMCQELGLVDRIPRMVCAQAANANPLYLHYKSGWKDFKPMTASTTFASAIQIGDPVSIDRAVYALKKCNGIVEEATEEELMDAMAQADSTGMFICPHTGVALTALFKLRNQGVIAPTDRTVVVSTAHGLKFTQSKIDYHSNAIPDMACRFSNPPVDVKADFGAVMDVLKSYLGSNTLTS	Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.	Q9S7B5
A6H2G3	TATA_FLAPJ	Sec-independent protein translocase protein TatA	Flavobacterium	MGRLGVTEILMILAVVLLLFGGKKIPELMKGLGSGLSEFKKAAKGDEVPDSKKDETKE	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. TatA could form the protein-conducting channel of the Tat system.	A6H2G3
Q2YS22	TYSY_BRUA2	Thymidylate synthase	Brucella	MRTYLDLLQHVLDHGVDRDDRTGTGTRSVFGYQMRFDLEEGFPVLTTKKLHLRSIIHELLWFLKGDTNIAYLKENGVTIWDEWADENGDLGPVYGYQWRSWPAPDGRHIDQIANLLKMLHTNPQSRRLIVSAWNPALVDEMALPPCHCLFQFYVANGRLSCQLYQRSADIFLGVPFNIASYALLTMMIAQVTGLKPGEFIHTLGDAHIYSNHFEQARLQLTRTPKKLPVMHINPDVKDLFAFRFEDFRLDGYEADPTIKAPIAV	Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.	Q2YS22
Q00063	THRC_ASHGO	Threonine synthase	Eremothecium	MSQVYRSTRSSSEDTKSFEEAVIQGLAEDGGLFLPAVIPRLREETLFEHWAHLSFQDLAMEIMKFYIADWEIPAPELRELIERSYSSFRSEEVTPLRKNVTGDDENLHILELFHGPTYAFKDVALQFVGNLFEYFLERKNRDVSEEERTHLTVVGATSGDTGSAAIYGLRGKQDVSVFILYPHGRISPIQEEQMTTVEDENVHTMAIEGSFDNCQDIVKSIFVDEEFNRKHNIAAVNSINWARILAQITYYFYSYFRATDGQPGRVKFIVPSGNFGDILAGFYAKQMGLPIEKLVIATNENDILDRFLREGVYERSEDVTATHSPAMDILVSSNFERLLWFFAREQLAQGDDQEAGSIVNRWFEQLREERRFDVPEHLLDAIRYHFDSERVDNYNTLASIRHIYEHAQNPERYVIDPHTAVGICAANRQIAHDQNNEIHYISLATAHPAKFADAVNEALSSYDDYNFDDVLPDRLRRLGDLEKRIKYVDNTDVDVIKSIIEEELINMGIYNP	Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.	Q00063
Q9VLN1	WDR82_DROME	WD repeat-containing protein 82	Sophophora	MKIKLIDSVVRSFKVAKIFRENTDKINAIDFAPNGEHLISCSEDDQIVIYDCEKGTQSRTVNSKKYGVDLIHFTHANNTAIHSSTKVDDTIRYLSLHDNKYLRYFPGHTKKVISLCISPVEDTFLSGSLDKTLRLWDLRSPNCQGLMHLSGRPIAAYDPEGLIFAAGVNSESIKLYDLRSFDKGPFVTFKLNQEKECDWTGLKFSRDGKTILISTNGSVIRLVDAFHGTPLQTFTGYPNNKGIPIEASFSPDSQFIFSGSTDGRVHIWNADTGNKVSVLNGDHPGPVQCVQFNPKYMMLASACTNMAFWLPTSEEGL	Component of the SET1 complex that specifically di- and trimethylates 'Lys-4' of histone H3 . Together with su(sable), part of a transcription termination checkpoint that promotes transcription termination of aberrant RNAs and their subsequent degradation by the nuclear exosome .	Q9VLN1
P70327	TBX6_MOUSE	T-box transcription factor TBX6	Mus	MYHPRELYPSLGTGYRLGHPQPGADSTFPPALTEGYRYPDLDTSKLDCFLSGIEAAPHTLAAAAPLPLLPSALGPETAPPPPEALHSLPGVSLSLENQELWKEFSAVGTEMIITKAGRRMFPACRVSVTGLDPEARYLFLLDVVPVDGARYRWQGQHWEPSGKAEPRLPDRVYIHPDSPATGAHWMRQPVSFHRVKLTNSTLDPHGHLILHSMHKYQPRIHLVRATQLCSQHWGGVASFRFPETTFISVTAYQNPRITQLKIAANPFAKGFRENGRNCKRERDARVKRKLRGPEPVATEACGSGDTPGGPCDSTLGGDIRDSDPEQAPTPQEAASASAPPCGGPSAEAYLLHPAAFHGAPSHLPARTPSFAEAPDPGRPAPYSAAFLDLQPGPGGSAYQAAPSVPSFAPHFIQGGPFPLPYPGPGGYLDMGSKPMY	T-box transcription factor that plays an essential role in the determination of the fate of axial stem cells: neural vs mesodermal. Acts in part by down-regulating, a specific enhancer (N1) of SOX2, to inhibit neural development. Seems to play also an essential role in left/right axis determination and acts through effects on Notch signaling around the node as well as through an effect on the morphology and motility of the nodal cilia.	P70327
P18728	ZG53_XENLA	Gastrula zinc finger protein XlCGF53.1	Xenopus	MGMWEEASDTGMKGKKKKKDKNEEEEEERGKKERMVNLTLEMIYLLTGEHYIPRKKSDDGGALHAPGSVIQKENNKNDEKILELMSNIIQLLTGEVAIRTHHVSIYFSLDEWDNIKGNKVLYEEGIKEEPQQLHPLDCEYEDKRDITADLGGTLCYNNETSKIGAEGTDFCAKENLTISPVEQPPPANRIKEERASCEEGNQSDCSINPLTEQIQGTDKPTPIMGYSLNNSSANYIKEEVVQCHEGNHSDMRIITAPESILETNTSAAMIRCNLNTSLSASCEGGNQSDCRINELTEQIQGTDTPTGNIVLYICSECQKHFSTKAGLARHQKTHSVFVGEEHAYGRIHTEEKPFPCSECGKRFARRQHLTDHQSSHTGEKPYACSQCEKYFPHRSNLNRHLKLHKGEKPFPCSQCGKRFPCVSDLNIHRRVHTGERPYSCSECGKCFKHHSNLTNHQRTHTREKPFSCTECGKGFKDRSSLTVHHRTHTGEKPFSCTECGKGFKDRSSLTVHHRTH	May be involved in transcriptional regulation.	P18728
C1CNW3	TRHO_STRZT	tRNA hydroxylation protein O	Streptococcus	MAKDIRVLLYYLYTPIENAEQFAADHLAFCKSIGLKGRILVADEGINGTVSGDYETTQKYMDYVHSLPGMEDLWFKIDEESEQAFKKMFVRYKKEIVHLGLEDNDFDNDINPLETTGAYLSPKEFKEALLDKDTVVLDTRNDYEYDLGHFRGAIRPDIRNFRELPQWVRDNKEKFMDKRVVVYCTGGVRCEKFSGWMVREGYKDVGQLHGGIATYGKDPEVQGELWDGKMYVFDERIAVDVNHVNPTIVGKDWFDGTPCERYVNCGNPFCNRRILTSEENEDKYLRGCSHECRVHPRNRYVSKNELTQAEVIERLAAIGESLDQAATV	Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.	C1CNW3
Q845X9	TRPD_BURM1	Anthranilate phosphoribosyltransferase	Burkholderia cepacia complex	MTITPQEALQRTIEHREIFHDEMLHLMRLIMRGDMSPVMAAAIITGLRVKKETIGEIAAAATVMREFANHVEVQDNSNFVDIVGTGGDGSHTFNISTASMFVTAAAGAKVAKHGNRGVSSKSGSADVLEALGVNIDLQPDQVAASIAETGMGFMFAPNHHPAMKNIAAVRRELGVRTIFNILGPLTNPAGAPNQLMGVFHPDLVGIQVRVMQRLGAQHVLVVYGKDGMDEVSLGAATLVGELRDGQVHEYEIHPEDFGLQMVSNRTLKVENAEESRAMLLGALDNQPGVAREIVTLNAGTALYAANVAGSIADGIQLAREAIASGKARAKVDELVRFTQQFKR	Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).	Q845X9
B7NVN0	TRPA_ECO7I	Tryptophan synthase alpha chain	Escherichia	MERYESLFIRLKERHEGAFVPFVTLGDPGIEQSLKIIDTLIEAGADALELGIPFSDPLADGPTIQNATLRAFAAGVTPAQCFEMLALIRQKHPTIPIGLLMYANLVFNKGVDEFYAQCEKVGVDSVLVADVPVEESAPFRQAALRHNVAPIFICPPNADDDLLRQIASYGRGYTYLLSRAGVTGAENRAALPLNHLVTKLKEYNAAPPLQGFGISAPDQVKAAIDAGAAGAISGSAIVKIIEQHINEPEKMLAALKAFVQPMKAATRS	The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.	B7NVN0
Q8U094	TRPA_PYRFU	Tryptophan synthase alpha chain	Pyrococcus	MFKDGSLIPYLTAGDPDKQSTLNFLLALDEYAGAIELGIPFSDPIADGKTIQESHYRALKNGFKLREAFWIVKEFRRHSSTPIVLMTYYNPIYRAGVRNFLAEAKASGVDGILVVDLPVFHAKEFTEIAREEGIKTVFLAAPNTPDERLKVIDDMTTGFVYLVSLYGTTGAREEIPKTAYDLLRRAKRICRNKVAVGFGVSKREHVVSLLKEGANGVVVGSALVKIIGEKGREATEFLKKKVEELLGI	The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.	Q8U094
Q9SLG3	ZIP3_ARATH	ZRT/IRT-like protein 3	Arabidopsis	MKTKNVKLLFFFFSVSLLLIAVVNAAEGHSHGGPKCECSHEDDHENKAGARKYKIAAIPTVLIAGIIGVLFPLLGKVFPSLRPETCFFFVTKAFAAGVILATGFMHVLPEAYEMLNSPCLTSEAWEFPFTGFIAMIAAILTLSVDTFATSSFYKSHCKASKRVSDGETGESSVDSEKVQILRTRVIAQVLELGIIVHSVVIGISLGASQSPDAAKALFIALMFHQCFEGLGLGGCIAQGKFKCLSVTIMSTFFAITTPIGIVVGMGIANSYDESSPTALIVQGVLNAASAGILIYMSLVDLLAADFTHPKMQSNTGLQIMAHIALLLGAGLMSLLAKWA	Mediates zinc uptake from the rhizosphere. May also transport other divalent cations.	Q9SLG3
B3Q867	TSAD_RHOPT	tRNA threonylcarbamoyladenosine biosynthesis protein TsaD	Rhodopseudomonas	MTSEQALLVLGIETTCDETAAAVVERRADGSGRLLSNIVRSQTDEHAPFGGVVPEIAARAHVDVLDGIIAAAMNEAGVAFASLSGVAAAAGPGLIGGVIVGLTTAKAIALVHGTPLIAVNHLEAHALTPRLTDAVEFPYCLFLASGGHTQIVAVLGVGNYVRLGTTVDDAIGEAFDKIAKMLGLPYPGGPQVERAAEAGDPNRFAFPRPMLGRQDANFSLSGLKTAVRNEAGKLTPLDPQDINDLCAGFQAAVLESVADRLGAGLRLFKERFGPPKALVAAGGAAANQAIRRMLREVAAKVQTTLIVPPPSLCTDNGAMIAWAGAERLALGLTDTMDTAPRARWLLDANATAPAKFANTRAGF	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.	B3Q867
Q8FHF8	YDEP_ECOL6	Protein YdeP	Escherichia	MKKKIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDKQVNASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDDVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAAFLYQLFAREYRSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGITEKPSAEFLDRLCERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAALPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTSSGKANFITSKGLLEDPSSAFNSKLVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRSSRRMDRLKVVIYPMADRSLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEPSN	Probably involved in acid resistance.	Q8FHF8
A8H738	TRUB_SHEPA	tRNA-uridine isomerase	Shewanella	MARRSRGRFIDGIVLLDKDTGMSSNFALQRVKRFFNANKAGHTGALDPLATGMLPICLGEATKFSQHLLDADKRYLVTAKLGQRTDTSDSDGEIVQTREVNFTQEQLDTALEYFRGETMQVPSMYSALKYQGQPLYKYAREGIEVPREARPINVFELNFISLEGDELTLDIHCSKGTYIRTITDDLGEMLGCGAHVIMLRRTQVAGYPYDKMVSLKQLEELVAKADAESLTLSEVLDPLLLPMDTAVSGFKEINVSDELATYLMNGNPVQVANLPVDELVRITIGDARQFVGIGQMNDDGLLAPKRLIVLREPQD	Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.	A8H738
Q9NSU2	TREX1_HUMAN	Deoxyribonuclease III	Homo	MGSQALPPGPMQTLIFFDMEATGLPFSQPKVTELCLLAVHRCALESPPTSQGPPPTVPPPPRVVDKLSLCVAPGKACSPAASEITGLSTAVLAAHGRQCFDDNLANLLLAFLRRQPQPWCLVAHNGDRYDFPLLQAELAMLGLTSALDGAFCVDSITALKALERASSPSEHGPRKSYSLGSIYTRLYGQSPPDSHTAEGDVLALLSICQWRPQALLRWVDAHARPFGTIRPMYGVTASARTKPRPSAVTTTAHLATTRNTSPSLGESRGTKDLPPVKDPGALSREGLLAPLGLLAILTLAVATLYGLSLATPGE	Major cellular 3'-to-5' DNA exonuclease which digests single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA) with mismatched 3' termini . Prevents cell-intrinsic initiation of autoimmunity . Acts by metabolizing DNA fragments from endogenous retroelements, including L1, LTR and SINE elements . Plays a key role in degradation of DNA fragments at cytosolic micronuclei arising from genome instability: its association with the endoplasmic reticulum membrane directs TREX1 to ruptured micronuclei, leading to micronuclear DNA degradation . Micronuclear DNA degradation is required to limit CGAS activation and subsequent inflammation . Unless degraded, these DNA fragments accumulate in the cytosol and activate the cGAS-STING innate immune signaling, leading to the production of type I interferon . Prevents chronic ATM-dependent checkpoint activation, by processing ssDNA polynucleotide species arising from the processing of aberrant DNA replication intermediates . Inefficiently degrades oxidized DNA, such as that generated upon antimicrobial reactive oxygen production or upon absorption of UV light . During GZMA-mediated cell death, contributes to DNA damage in concert with NME1 . NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair .	Q9NSU2
A5II09	TRHO_LEGPC	tRNA hydroxylation protein O	Legionella	MKDIIIASFYKFIPLNDFESLREPILTKMHEIGIKGTIILAHEGVNGGFAGNREQMNVFYDYLRSDSRFADLHFKETYDSKNPFDKAKVKLRKEIVTMGVQKVDPSYNAGTYLSPEEWHQFIQDPNVILLDTRNDYEYELGTFKNAINPDIENFREFPDYVQRNLIDKKDKKIAMFCTGGIRCEKTTAYMKELGFQHVYQLHDGILNYLESIPESESLWEGKCFVFDDRVAVDQKLDRVYPQLPQDYKYEREQK	Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.	A5II09
Q21BZ6	UBIG_RHOPB	3-demethylubiquinone 3-O-methyltransferase	Rhodopseudomonas	MSMQSNSSDASSATVDPAEIAKFSRLSAQWWDPTGKMAPLHKINPLRLSFIRDAACRKFERNAKSLNCLSGLRMIDIGCGAGLLCEPFTRLGAQVIGVDPSATNIAAAKLHAEKSQLLIDYRCTTVEQMDPRERFDIVLAMEVIEHVTDVGAFLARCAAITKPGGLMVVATLNRNWKSFALAIVGAEYVMRWLPRGTHQWDKFVTPDELTKHLHNNKLAVTEQAGLVYNPLADKWSLSADMDVNYMVVAETAAG	O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.	Q21BZ6
Q49ZD7	TRUA_STAS1	tRNA-uridine isomerase I	Staphylococcus	MRVLVNISYQGSQFLGFQIQQHGRTIQQQFEKILKRMHKHEVRIHPSSRTDRGVHAIEQYFHFDTELNIPEQQWQYAMNRALPDDIYVNDVSFVNDDFHCRYDCVGKSYRYKIYQSAHKDPFLCGLKTYVPEQLDIEKMNMAAQHFIGTHDFTGFCSQKTEVESKIRTLYESRIEKTESGFDYIVTGSGFLYNMVRVLIAFLIEVGKGKREPQEVPQLLEARDRNQVPFTAPAEGLYLEKIYLTPNELIQDFGNNIKIHQKKSSQNL	Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.	Q49ZD7
A9GP90	UREG_SORC5	Urease accessory protein UreG	Sorangium	MHDPGEHGHGRHDHDHDHDHVHDHDHDHDHVHGGGHRHAHEHEHAHEHAHGHEHGHAHAHAHAHAHEHAHGHTHEHWAHPGLFSERDAPKDRDFSARAFTVGIGGPVGSGKTALVLALCRALRDRMPLGVVTNDIFTQEDAEFLHRNKALPPERIRAVETGGCPHAAIREDISHNLVALDDLMDHVAPALLIVESGGDNLAAQYSRELVDYTIYVIDVAGGDKVPRKGGPGITQSDLLVINKTDLAPHVGADLGVMERDARRMRGDGPFLFAQCNRSQGVPEIIDHILSAMRRATTTAPPAK	Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.	A9GP90
A4FAI5	Y1742_SACEN	Putative S-adenosyl-L-methionine-dependent methyltransferase SACE_1742	Saccharopolyspora	MSANEQWDIVSGVGITALAVAVARARESRRDDRLIDDPYAEPLIRAAQPPVPMSGDGGEAGALWHEMTDYVSVRSRFFDEWFARACAAGTRQAVVLASGLDTRAFRLEWPEGFRVFEIDQPKVLEFKDGTLAAEGVRASCERHAVAVDLRDDWASALVKAGFDPALPTAWLAEGLLPYLPPEAEANLLATVHDLSARGSRIAIESIALARSALLGADLDDTAREWGIDLKGLFSLEDRPDPGDVLAQRGWRVHRDPVGDLAAGFRRPLSDRAQQLGAAGEMVTAQRD	Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.	A4FAI5
A3D3E2	TOLB_SHEB5	Tol-Pal system protein TolB	Shewanella	MRILAKWLALAVLLCTTPAKAALDIVITEGVDAARPIAVMPFVWQGSGAAPQAIADVVMSDLVRSGTFKPLDELGLPQRNIGTAAQFQANSWSSVGAEALVLGTVKPYGTDQYLVSFDLIDLVKAQNQALKGPVSATEFLMDSRQTVISAAQFRQYGHRISDIVYEKLTGIRGAFLTRISYVVVNHTQKAPYQLMVADYDGVNEQMLLRSPEPLMSPTWSPDGRRLAYVSFENKKAEIFVQDLYTQVRTKVSSFPGINGAPAFSPDGKSLAITLSKDGQPEIYIIDIATKAIKRITNHYAIDTEPSWYPDGKSLIFTSERGGRPQIYRVELSSGKVSRETFEGEWNLGGSITPDGRSMIFVNRTNGKFNIARMDLSTRFMQVLTSTRLDESPSVAPNGTMVIYGTTYQGKQVLAAVSTDGRFKARLPAGQGEVKSPSWSPFL	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.	A3D3E2
O00124	UBXN8_HUMAN	UBX domain-containing protein 6	Homo	MASRGVVGIFFLSAVPLVCLELRRGIPDIGIKDFLLLCGRILLLLALLTLIISVTTSWLNSFKSPQVYLKEEEEKNEKRQKLVRKKQQEAQGEKASRYIENVLKPHQEMKLRKLEERFYQMTGEAWKLSSGHKLGGDEGTSQTSFETSNREAAKSQNLPKPLTEFPSPAEQPTCKEIPDLPEEPSQTAEEVVTVALRCPSGNVLRRRFLKSYSSQVLFDWMTRIGYHISLYSLSTSFPRRPLAVEGGQSLEDIGITVDTVLILEEKEQTN	Involved in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins, possibly by tethering VCP to the endoplasmic reticulum membrane. May play a role in reproduction.	O00124
Q8EPB7	TPX_OCEIH	Thioredoxin-dependent peroxiredoxin	Oceanobacillus	MSNVTFKNDPVTLLGAEKKVGDSAPDFTVLANDLSKKHLSDYKGKVKVISVVPSIDTGVCSEQTRRFNQEATNLENVQILTISMDLPFAQKRWCAANGIDRVDTLSDHREADFGQKYGVIIEELRLLSRAVFVVDENDKITYVEYLSEVSNHPDYEAVLSHLNK	Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.	Q8EPB7
B0B9D4	TRMD_CHLT2	tRNA [GM37] methyltransferase	Chlamydia	MEIDILSLFPDYFASPLQATILGRAIKQGALSVRSRDIREFGLGKWKQVDDSPYNGEGMLLMAEPVVQAIRSIRRKKSKVIYLSPQGQLLSAKKSRELASCSHLVLLCGHYEGIDERALTAEVDEEISIGDYVLTNGCAAALVLVDALARFIPGILGNQESAEYDSLENGLLEGPQYTRPRVFEGESVPEVLLCGDHQKIADWRKQVSLERTRERRPDLYLQYFYGNSACLSTQEDLPRIEVVSPKTFSVVLEVQDLRKAKKFYSRMFGKECWDGDKLFLLGKTSLYLQQTKETRGPTTVFIELETDHDFVRFLKRWEMLGGELGEQGTGGFPLRQVFDLDGHIWVVSCVQK	Specifically methylates guanosine-37 in various tRNAs.	B0B9D4
A1UU52	TRUB_BARBK	tRNA-uridine isomerase	Bartonella	MSRQSKKKGRSISGWVILDKPKAMKSTEAVSKIKRLFNAQKAGHAGTLDPLASGLLPIALGEATKTVPYVMEGTKTYHFHVAWGEERSTDDLEGVVTKTSSKRPTQEEIFALLPKYTGVILQTPPQFSAIKIAGNRAYDLAREGEIFEIPPRQVKIDSLELIGTTDQGYSIFEMTCGKGTYVRSLARDMGHDLGCYGYIADLRRTAVAPFCENDLITWDALKAAIPHENTTDENCIPLKQNFSTLDGLLIETDVALKCLAHYTLNQIQAQRVRMGNSILLCDQNMPTSNIDICVTYKAQLLAIGTIDQNQFKPKRIFTTL	Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.	A1UU52
Q2SUP3	THIC_BURTA	Thiamine biosynthesis protein ThiC	pseudomallei group	MNANPKFLSADARVDAAAVAPLPNSRKVYVTGSQPDIRVPMREITQADTPTSFGGEKNPPIYVYDTSGPYTDPDAKIDIRAGLPALRQRWIDARGDTETLAGLTSEYGRERAADPATAELRFPDLHRHPRRAKAGRNVTQMHYARQGIITPEMEFIAIRENQRRAEYLESLKASGPNGAKLAAMMGRQHAGQAFGAAAFGANEAGTNMLTEITPEFVRSEVACGRAIIPANINHPETEPMIIGRNFLVKINANIGNSAVTSSIGEEVDKMTWAIRWGGDTVMDLSTGKHIHETREWIIRNSPVPIGTVPIYQALEKVNGKAEDLTWEIFRDTLIEQAEQGVDYFTIHAGVRLQYVPLTANRMTGIVSRGGSIMAKWCLAHHKESFLYEHFEEICEIMKAYDVSFSLGDGLRPGSIYDANDEAQLGELKTLGELTQIAWKHDVQVMIEGPGHVPMQLIKENMDLQLDWCKEAPFYTLGPLTTDIAPGYDHITSGIGAAMIGWFGTAMLCYVTPKEHLGLPNKDDVKEGIITYKLAAHAADLAKGHPGAQVRDNALSKARFEFRWEDQFNLGLDPDKAREFHDETLPKDSAKVAHFCSMCGPHFCSMKITQDVREFAAQQGMSEDDALKKGMEVKAVEFVKTGSEIYHRQ	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.	Q2SUP3
A3PBC8	YIDD_PROM0	Putative membrane protein insertion efficiency factor	Prochlorococcus	MFKTINKSITSILLLLISFYQKWFSPFFGPRCRFIPSCSSYGYEAITRHGPWKGGWLTLKRLSRCHPLTPCGCDPVPD	Could be involved in insertion of integral membrane proteins into the membrane.	A3PBC8
Q6AQH2	UPP_DESPS	UPRTase	Desulfotalea	MSLHIADHPLVKHKLGLMRQNDISTKDFRALASEIARLLTYEAVKDLPTEKHIVDGWAGPVEVDRLKGKKITIVPILRAGLGMMDGVIDLIPSAKVTVVGFYRDEETLEPVEYYVKTASEMSERVALIIDPMLATGGTLIATIDTLKKAGSKKIKGLFLVAAPEGIKKVQDAHPDVEIYVAAVDERLNEAGYILPGLGDAGDKIFGTR	Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.	Q6AQH2
C3L3F6	YBEY_CLOB6	Endoribonuclease YbeY	Clostridium	MIYIDNRQNKIKVNEEFENKIKEIIDYALKEEKVNIDYEISVVFIDNNSIKEINKDYRNIDKATDVLSFPMLDYEEGKVFKDVYLNYEFDESDLDEGNLILGDIALSLEKAEEQSKEFGHSFLRETCYLTIHSVLHLLGYDHMEEEEKAIMRQREEEILKSFNLRR	Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.	C3L3F6
Q8BH57	WDR48_MOUSE	USP1-associated factor 1	Mus	MAAHHRQNTAGRRKVQVSYVIRDEVEKYNRNGVNALQLDPALNRLFTAGRDSIIRIWSVNQHKQDPYIASMEHHTDWVNDVVLCCNGKTLISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTASNNTVTTSSLSGNKDSIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLHRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALQVNDAFTHVYSGGRDRKIYCTDLRNPDIRVLICEEKAPVLKMELDRSADPPPAIWVATTKSTVNKWTLKGIHNFRASGDYDNDCTNPITPLCTQPDQVIKGGASIIQCHILNDKRHILTKDTNNNVAYWDVLKACKVEDLGKVDFEDEIKKRFKMVYVPNWFSVDLKTGMLTITLDESDCFAAWVSAKDAGFSSPDGSDPKLNLGGLLLQALLEYWPRTHVTPMDEEENEVNHVSGGQESRVQKGNGYFQVPPHTPVIFGEAGGRTLFRLLCRDSGGETEAMLLNETVPQWVIDITVDKNMPKFNKIPFYLQPHASSGAKTLKKDRLSASDMLQVRKVMEHVYEKIINLDNESQTTSSSNNEKPEQEKEEDIAVLAEEKIELLCQDQVLDPNMDLRTVKHFIWKSGGDLTLHYRQKST	Regulator of deubiquitinating complexes, which acts as a strong activator of USP1, USP12 and USP46. Enhances the USP1-mediated deubiquitination of FANCD2; USP1 being almost inactive by itself. Activates deubiquitination by increasing the catalytic turnover without increasing the affinity of deubiquitinating enzymes for the substrate. Also activates deubiquitinating activity of complexes containing USP12. Docks at the distal end of the USP12 fingers domain and induces a cascade of structural changes leading to the activation of the enzyme. Together with RAD51AP1, promotes DNA repair by stimulating RAD51-mediated homologous recombination. Binds single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA). DNA-binding is required both for USP1-mediated deubiquitination of FANCD2 and stimulation of RAD51-mediated homologous recombination: both WDR48/UAF1 and RAD51AP1 have coordinated role in DNA-binding during these processes.Together with ATAD5 and by regulating USP1 activity, has a role in PCNA-mediated translesion synthesis (TLS) by deubiquitinating monoubiquitinated PCNA. Together with ATAD5, has a role in recruiting RAD51 to stalled forks during replication stress.	Q8BH57
A6LTL5	THIG_CLOB8	Thiazole synthase	Clostridium	MKKDVLTLGGHEFSSRFILGSGKYNLNLIKAAVENAGAQMITLALRRANTSGGENILDFIPEGVTLLPNTSGARNAEEAVRIARLARAMNCGDFVKVEIIHDSKYLLPDNYETIKATEILAKEGFIVMPYMHADLNVARDLVNAGAACIMPLASPIGSNKGLATKEFIKILVDEIDLPIIVDAGIGRPSQACEAMEMGVAAVMANTAIATAGDIPAMAGAFKQAIEAGRAAYLSGLGRVLDKGASASSPLTGFLED	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.	A6LTL5
Q21UL3	UBIG_ALBFT	3-demethylubiquinone 3-O-methyltransferase	Rhodoferax	MSHQPYFADNHPMTSTLNADPAELAKFSDLAHRWWDLEGEFRPLHQINPLRLEWINHLCPVAGQQVLDVGCGGGILADSMARLGAQVTGIDLASKALRVAQLHALEAQTPNLQYQEISVEALAAQQPGSFDVVTCMEMLEHVPDPASVVRACATLVKPGGWVFFSTLNRSPKSFVLAIVGAEYVLNLLPRGTHEYAKMIRPSELASYCRSVELDLRHTRGMQYNPLTRRYWMSDDTSVNYLFATQKSNAAIL	O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.	Q21UL3
Q0IHY4	TBC12_XENTR	TBC1 domain family member 12	Silurana	MVGPEDAGQGAVYRCGEERHGLTDAADEEEGEGEAGDRQTDILQLYISRPAIKMTNGDLNYLPQGGAGEGDMPSAGDMHSLSTHKEDIKQPNGGLLVADSTRPQGCACHRQCCSLSEAVPSPGTPPGSSPISSSSSSPVSARTVAGYFVSEEADRFRFLDVSRQSCRNTFEGSRRQSAPDHLADGLSLPAESPGTAEQDGDRPWKVGIAEFFSRNFFSKRTKDPKSSSSVPGWKLFGKVPPRETAQKDSKIIQQDDSSGSLSSVSTPNLLNTGEYEARTGRSCKAPSQSTRKKKFEFEPLSTTALILEDRPSNLPAKSVHETLRHRQEYDEMVAEAKKREVKEAQRRKKLMKERIRQEENIASAMVIWNTEILPNWDVMRSTRRVRDLWWQGLPPSIRGKVWSLAIGNELNITPELYEIFLSRAKERWKSFSETNSENENEDAGASLADREASLELIKLDISRTFPSLYIFQKGGPYHDLLHSILGAYTCYRPDVGYVQGMSFIAAVLILNLEEADAFIAFANLLNKPCQLAFFRVDHSMMLKYFAAFEVFFEENLPKLFFHFNAYSLTPDLYLIDWIFTLYSKSLPLDLACRVWDVFCRDGEEFLFRTALGILRLYEDILLQMDFIHIAQFLTKLPEDITSEKLFGCIAAIQMQNSNKKWTQVFTSLMKDYKEGDKMSQASKT	May act as a GTPase-activating protein for Rab family protein(s).	Q0IHY4
Q0TNU2	YBEY_CLOP1	Endoribonuclease YbeY	Clostridium	MIFIDNRQNKFEVTEELTKKLEEVISFVLKEEKVKEDCEVSLVFVDNEEIRGINNETRGIDRATDVLSFPMIDYPEDKVYKDVYLEHEFDKCYFDGDELILGDIVLSLERTKEQSIEFNHSFEREACYLVTHSVLHLLGYDHMEEEEKARMRGREEELLGKLNITRES	Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.	Q0TNU2
A9WLN5	UPP_RENSM	UPRTase	Renibacterium	MRVLVVDHPLVAHKLTVLRDKNTPSPVFRQLTEELVTLLAYEATREVRVEEVSIETPVTKTVGTGLVKPTPLVVPILRAGLGMLEGMTRLLPTAEVGFLGMARNEETLEAITYAERLPEDLTGRQVYVLDPMLATGATLREAIKFLFARRALDITCICLLGAPEGIEALREQHEGANVTIVLASIDEGLNEKAYIVPGLGDAGDRLYGVVG	Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.	A9WLN5
Q7JR49	VAS1_DROME	Vacuolar H(+) ATPase AC45 accessory subunit	Sophophora	MLWKSLIALCVIGAAVAEQTPVFLWGANSVAKPSLKTVSQVEFAEQLAALLEDHMVVAFEENGLSSKDFLCSNSQAQSCYAQLQGVSPKTYYTSVENPSEALRSVAAKREHNSIDASGKLTTPAKCAVGTALFVTFEDAAESREASLESHDAAIAAISKQFECKVAYLYLAAPSTAPVVQRRTRRDTAATTGGIMWKSTNQFQIFYTALLYNGNPITVTDLKLTNSSSTKLSVVMDTSVADKPITFDVVYNGGYFSLSNLVYDNNNFRSSGVNAPTTFSYSCGNLTLESAAVNNMYNTLSFKSLQLQAPFDGTYKEDFPFGDSWDCVGFVTPGILMGLFVVALLLVIMFVGVCWMMDINTMDRFDDPKGKTITINAAAE	Accessory subunit of the proton-transporting vacuolar (V)-ATPase protein pump, which is required for luminal acidification of secretory vesicles.	Q7JR49
A9HI81	UPPP_GLUDA	Undecaprenyl pyrophosphate phosphatase	Gluconacetobacter	MDSRTMTLIQAIVIAILQGATELFPVSSLGHAVIVPALLGWAFDPHGEIFLPFLVMLHLGTAIALLVYFRNDWAAIFQGLRGRDGSQRQAESIHILALLVVATIPAVIIGGLLEHWLRALFGTARYAAIFLFLNGLLLLLTERMKSRQPVQGGYAIASLTYADAAIIGLWQCLAFLPGISRSGATIIGALFRGLNHEGAARFSFLMAQPVIIAATVREALHMRHVAIPPGQMQVATIGAMVAAVTALASTAFLMRYFHNHERWALSPFGYYCVLAGAVSFFILGH	Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.	A9HI81
Q5M8X5	TPC2L_XENTR	Trafficking protein particle complex subunit 2-like protein	Silurana	MAVCVAVIAKENYPLYIRSTPTENQLKFHYTVHTSLDVVDEKISAMGKAVMDQRELYLGLLYPTEDYKVYGYVTNSKVKFVMVVDSSNTSLRDNEIRSMFRKLHNSYTDVMCNPFYNPGDPIQSRAFDNTVTSMMVPAC	May play a role in vesicular transport from endoplasmic reticulum to Golgi.	Q5M8X5
Q83RF3	YDEP_SHIFL	Protein YdeP	Shigella	MKKKIESYQGAAGGWGAVKSVANAVRKQMDIRHDVIAMFDMNKPEGFDCPGCAWPDPKNSASFDICENGAKAIAWEVTDKQVNASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAAFLYQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGITEKPSAEFLARLGERYGFPPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAALPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNSKLVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRSSRRMDRLKVVIYPMADRSLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEPSN	Probably involved in acid resistance.	Q83RF3
Q55031	TBP_SACSH	TATA-box factor	Saccharolobus	MSNSAVSYKPIVNIENIVATVTLEQSLDLYAMERSIPNIEYDPDQFPGLIFRLEQPKVTALIFKSGKMVVTGAKSTEELIKAVKRIIKTLKKYGIKIMGKPKIQIQNIVASANLHVNVNLDKAAFLLENNMYEPEQFPGLIFRMDDPRVVLLIFSSGKMVITGAKREDEVSKAVKRIFDKLAELDCVKPIEEEEELEL	General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation.	Q55031
B3GZ49	TORD_ACTP7	Chaperone protein TorD	Actinobacillus	MAHSQLLSSEERLFCYRWFHSLLAKELSEPQLQALQAGQFASFFALLAELGFQPQVTDLQNELAKLTAYDSPRLELAADFAQCFLLEGKLSALPYASYYLDERDLSENLAVMDQWLTKFQLKINRLHNEPSDHLCIYLEVLIKLIETEQPVQVQQQFIRQQLLGWLPQWAEKTAQIHSSTAFYQIISNLLLGFLQQDIA	Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor.	B3GZ49
P18734	ZG67_XENLA	Gastrula zinc finger protein XlCGF67.1	Xenopus	SDRKTVSCPECGKCFTSRTYLNVHKKVHTGQTYSCSECGKSFLSRSHLNTHLRTHTGEKPYSCSECGKCFTSSAILITHKRIHTGERPFSCQECGKSFSYRSVFMEHQKIHTGEKPFSCSDCGKCFRYRSHLKVHSRIH	May be involved in transcriptional regulation.	P18734
Q6INE8	VMP1_XENLA	Vacuole membrane protein 1	Xenopus	MAENGTDCEQRRVGMPKEQNNGSFQDPSFMCNRKRRDREERQSIVLWRKPLITLQYFILEVLINLKEWSVRLWHRRMMVVSVLLLLAVLSVAYYIEGEHQQCVQYIEKKCLWCAYWVGLGILSSVGLGTGLHTFLLYLGPHIASVTIAAYECNSVNFPEPPYPDEIICPDEEGTEGAISLWTIISKVRLEACMWGAGTAIGELPPYFMARAARLSGVETDDEEYAEFEEMLEHAQTAQDFATRAKLTVQNLVQKVGFLGILACASIPNPLFDLAGITCGHFLVPFWTFFGATLIGKAIIKMHIQKLFVIITFSKHIVEQMVSLIGVIPSIGPSLQKPFQEYLEAQRKKLHHKGDSGTPQSENWLSWAFEKLVIIMVFYFILSIINSMAQSYAKRVQQKKLSVEKTK	Phospholipid scramblase involved in lipid homeostasis and membrane dynamics processes. Has phospholipid scramblase activity toward cholesterol and phosphatidylserine, as well as phosphatidylethanolamine and phosphatidylcholine. Required for autophagosome formation: participates in early stages of autophagosome biogenesis at the endoplasmic reticulum (ER) membrane by reequilibrating the leaflets of the ER as lipids are extracted by atg2 (atg2a or atg2b) to mediate autophagosome assembly. In addition to autophagy, involved in other processes in which phospholipid scramblase activity is required. Modulates ER contacts with lipid droplets, mitochondria and endosomes.	Q6INE8
Q9Y5Q9	TF3C3_HUMAN	Transcription factor IIIC subunit gamma	Homo	MSGFSPELIDYLEGKISFEEFERRREERKTREKKSLQEKGKLSAEENPDDSEVPSSSGINSTKSQDKDVNEGETSDGVRKSVHKVFASMLGENEDDEEEEEEEEEEEEEEETPEQPTAGDVFVLEMVLNRETKKMMKEKRPRSKLPRALRGLMGEANIRFARGEREEAILMCMEIIRQAPLAYEPFSTLAMIYEDQGDMEKSLQFELIAAHLNPSDTEEWVRLAEMSLEQDNIKQAIFCYTKALKYEPTNVRYLWERSSLYEQMGDHKMAMDGYRRILNLLSPSDGERFMQLARDMAKSYYEANDVTSAINIIDEAFSKHQGLVSMEDVNIAAELYISNKQYDKALEIITDFSGIVLEKKTSEEGTSEENKAPENVTCTIPDGVPIDITVKLMVCLVHLNILEPLNPLLTTLVEQNPEDMGDLYLDVAEAFLDVGEYNSALPLLSALVCSERYNLAVVWLRHAECLKALGYMERAAESYGKVVDLAPLHLDARISLSTLQQQLGQPEKALEALEPMYDPDTLAQDANAAQQELKLLLHRSTLLFSQGKMYGYVDTLLTMLAMLLKVAMNRAQVCLISSSKSGERHLYLIKVSRDKISDSNDQESANCDAKAIFAVLTSVLTKDDWWNLLLKAIYSLCDLSRFQEAELLVDSSLEYYSFYDDRQKRKELEYFGLSAAILDKNFRKAYNYIRIMVMENVNKPQLWNIFNQVTMHSQDVRHHRFCLRLMLKNPENHALCVLNGHNAFVSGSFKHALGQYVQAFRTHPDEPLYSFCIGLTFIHMASQKYVLRRHALIVQGFSFLNRYLSLRGPCQESFYNLGRGLHQLGLIHLAIHYYQKALELPPLVVEGIELDQLDLRRDIAYNLSLIYQSSGNTGMAQTLLYTYCSI	Involved in RNA polymerase III-mediated transcription. Integral, tightly associated component of the DNA-binding TFIIIC2 subcomplex that directly binds tRNA and virus-associated RNA promoters.	Q9Y5Q9
P68424	TXH10_CYRSC	Huwentoxin-X	Cyriopagopus	MNMKILVLVAVLCLVVSTHAERHSKTDMEDMEDSPMIQERKCLPPGKPCYGATQKIPCCGVCSHNKCT	Reversibly blocks N-type calcium channels (Cav2.2/CACNA1B) in rat dorsal root ganglion cells (IC(50)=40 nM). Elicits no toxic symptoms in either vertebrates or invertebrates during a period of 48 hours post-injection, when it was assayed in vivo by direct injection into mice and cockroaches.	P68424
P58453	VARH_VIOAR	Varv peptide H	Viola	GLPVCGETCFGGTCNTPGCSCETWPVCSRN	Probably participates in a plant defense mechanism.	P58453
Q96NC0	ZMAT2_HUMAN	Zinc finger matrin-type protein 2	Homo	MASGSGTKNLDFRRKWDKDEYEKLAEKRLTEEREKKDGKPVQPVKRELLRHRDYKVDLESKLGKTIVITKTTPQSEMGGYYCNVCDCVVKDSINFLDHINGKKHQRNLGMSMRVERSTLDQVKKRFEVNKKKMEEKQKDYDFEERMKELREEEEKAKAYKKEKQKEKKRRAEEDLTFEEDDEMAAVMGFSGFGSTKKSY	Involved in pre-mRNA splicing as a component of the spliceosome.	Q96NC0
C5BCI2	THII_EDWI9	tRNA 4-thiouridine synthase	Edwardsiella	MKFIIKLFPEITIKSQSVRLRFIKILTGNIRNVLKPLVEDVAVTRHWDHIEVRAKEESRRDLVRDALTRIPGIHHILEVEDHPYTDMHDIFEQTLAMYREQLEEKTFCVRVKRRGKHTFTSIEVERYVGGGLNQNIPSARVRLNHPEVTVNLEIEDDRLLLVRGRFEGQGGYPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGSAHEIGVKQVAHYLWNRFGSSHRVRFVAIDFAPVVGEILEKVDDGQMGVVLKRMMVRAASRVAERYGIQALVTGEALGQVSSQTLTNLRLIDGVSDTLVLRPLIAHDKEHIIRLARNIGTEDFAKTMPEFCGVISKSPTVKAVKARIEAEEEHFDFAILDRVVDEAQTMDIRDIARQSEADVVEVETIESLAEGDVVLDIRAPDEQEAKPLQLADSEVICLPFYKLANAFGDLDQVRRYVLYCDRGVMSRLQALYLREQGYDNVRVYRP	Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.	C5BCI2
Q60493	ZN664_CAVPO	Zinc finger protein from organ of Corti	Cavia	MIYKCPMCREFFSERADLFMHQKVHTAEKPHKCDKCDKGFFHISELHIHWRDHTGEKVYKCDDCGKDFSTTTKLNRHKKIHTVEKPYKCYECGKAFNWSPHLQIHMRVHTGEKPYVCSECGRGFSNSSNLCMHQRVHTGEKPFKCEECGKAFRHTSSLCMHQRVHTGEKPYKCYECGKAFSQSSSLCIHQRVHTGEKPYRCCGCGKAFSQSSSLCIHQRVHTGEKPFKCDECGKAFSQSTSLCIHQRVHTKERNHLKISVI	May be involved in transcriptional regulation.	Q60493
P53061	ZIP2_YEAST	Zipping up meiotic chromosomes protein 2	Saccharomyces	MIIERWEVKLSKCNQNVGGYSVLSGNLKENIKLGRRAQKYLKELRNLQLKPLKIGGYENCGTINGEEYFLEVIHITSGRQKIDVAVGKTWNVTNIENDNKEELQYELFKEKLKVGKQDMLFFSWMKSLSVQLNAPLHQKMTEHGLADDNTRLEWFNIPLLRRSQYRKKVPYPSLRQMSSVLEVQCSTLTEEKLNFCVGFSDKPLSEWKPQIFEQTYNRYRLQRISPEKSFKYKSRCSKYNFKTSSQSWVVKVPEHDQQLNTFEKRYDELFDAQFNKLEFFKIRMKKLKKNKPIEKKNYKIWCLEKEDLKDLVWDPLKRICNHSRYAIFEHVTINREAYSIKPLRLTFQKLDSGSLDLIDNQKKTFGSIKLAMSMPDVKKTENQSIEESERHDETAIETQEFDENDCLSSKADINTSLAPQKRSFIDNELMSMLVTKKKIKKDKDVSDTGISSTSYLINSGTYANSHIEIPTSNSVYNGKEDCSFNNYSVKHSILEEDIENKCIAVNENKVIENQKVIQSLCKNSHLDLIEQSYFGECDFIINHSTCVYKIQASRFMQLRNNGSLHYDKAVNDLLTEFQRVIIIVEFSEIIQDVDPDLFWKIKLYLLNSRVDVFFIHETTDFFIDWMKYFIARWAFSYNDEKEKNIANADILLDLGFNILLVRKIFQTYSLEEFFMAIIKEESKAVKMLTVSQMTRLKKLLTLEW	Required for initiation of meiotic chromosome synapsis. Involved in synaptonemal complex formation, a structure that tethers a pair of homologous chromosomes along their lengths and plays a central role in recombination and homolog segregation during meiosis. Required for the normal localization of MSH4 to chromosomes.	P53061
A7E305	ZSWM8_BOVIN	Zinc finger SWIM domain-containing protein 8	Bos	MELMFAEWEDGERFSFEDSDRFEEDSLCSFISEAESLCQNWRGWRKQSAGPNSPTGGGGGGGSGGTRMRDGLVIPLVELSAKQVAFHIPFEVVEKVYPPVPEQLQLRIAFWSFPENEEDIRLYSCLANGSADEFQRGDQLFRMRAVKDPLQIGFHLSATVVPPQMVPPKGAYNVAVMFDRCRVTSCSCTCGAGAKWCTHVVALCLFRIHNASAVCLRAPVSESLSRLQRDQLQKFAQYLISELPQQILPTAQRLLDELLSSQSTAINTVCGAPDPTAGPSASDQSTWYLDESTLTDNIKKTLHKFCGPSPVVFSDVNSMYLSSTEPPAAAEWACLLRPLRGREPEGVWNLLSIVREMFKRRDSNAAPLLEILTVELAQDLLANPPDLKVEPPPAKGKKNKVSTSRQTWVATNTLTKAAFLLTVLSERPEHHNLAFRVGMFALELQRPPASTKALEVKLAYQESEVATLLKKIPLGPSEMSTVRCRAEELREGTLCDYRPVLPLMLASFIFDVLCAPVVSPTGSRPPSRNWNNEMPGDEELGFEAAVAALGMKTTVSEAEHPLLCEGTRREKGDLALALMITYKDDQARLKKILDKLLDRESQTHKPQTLSSFYSSSRPATASQRSPSKHGGPSAPGALQPLTSGSAGPAQPGSVAGAGPGPTEGFTEKNVPESSPHSPCEGLPPEAALTPRPEGKVPSRLALGSRGGYNGRGWGSPGRPKKKHTGMASIDSSAPETTSDSSPTLSRRPLRGGWAPTSWGRGQDSDSISSSSSDSLGSSSSSGSRRASASGGARAKTVEVGRYKGRRPESHAPHVPNQPSEAAAHFYFELAKTVLIKAGGNSSTSIFTHPSSSGGHQGPHRNLHLCAFEIGLYALGLHNFVSPNWLSRTYSSHVSWITGQAMEIGSAALTILVECWDGHLTPPEVASLADRASRARDSNMVRAAAELALSCLPHAHALNPNEIQRALVQCKEQDNLMLEKACMAVEEAAKGGGVYPEVLFEVAHQWFWLYEQTAGGSSTAREGATSCSASGIRAAGEAGRGLPEGRGGPGTEPVTVAAAAVTAATVVPVISVGSSLYPGPGLGHGHSPGLHPYTALQPHLPCSPQYLTHPAHPAHPMPHMPRPAVFPVASSAYPQGVHPAFLGAQYPYSVTPPSLAATAVSFPVPSMAPITVHPYHTEPGLPLPTSVALSSVHPASTFPAIQGASLPALTTQPSPLVSGGFPPPEEETHSQPVNPHSLHHLHAAYRVGMLALEMLGRRAHNDHPNNFSRSPPYTDDVKWLLGLAAKLGVNYVHQFCVGAAKGVLSPFVLQEIVMETLQRLSPAHAHNHLRAPAFHQLVQRCQQAYMQYIHHRLIHLTPADYDDFVNAIRSARSAFCLTPMGMMQFNDILQNLKRSKQTKELWQRVSLEMTTFSP	Substrate recognition component of a SCF-like E3 ubiquitin-protein ligase complex that promotes target-directed microRNA degradation (TDMD), a process that mediates degradation of microRNAs (miRNAs). The SCF-like E3 ubiquitin-protein ligase complex acts by catalyzing ubiquitination and subsequent degradation of AGO proteins (AGO1, AGO2, AGO3 and/or AGO4), thereby exposing miRNAs for degradation. Specifically recognizes and binds AGO proteins when they are engaged with a TDMD target. May also act as a regulator of axon guidance: specifically recognizes misfolded ROBO3 and promotes its ubiquitination and subsequent degradation.	A7E305
O32583	THIS_ECOLI	Thiamine biosynthesis protein ThiS	Escherichia	MQILFNDQAMQCAAGQTVHELLEQLDQRQAGAALAINQQIVPREQWAQHIVQDGDQILLFQVIAGG	Is the sulfur donor in the synthesis of the thiazole phosphate moiety of thiamine phosphate.	O32583
Q8A7D1	TILS_BACTN	tRNA(Ile)-lysidine synthetase	Bacteroides	MIQQRVIRYIEKEHLFLPDDKLLVALSGGADSVALLRVLHTAGYQCEAAHCNFHLRGEESNRDERFVRQLCQKYGIRLHITDFNTTQYATEKRISIEMAARELRYNWFEKIKEECGAHVIAVAHHQDDSVETMLFNLIRGTGITGLLGIRPRNGAIVRPLLCINREEIIRYLQQIGQDFVTDSTNLEDEYTRNKIRLNLLPLMQEINPSVKNSLIETSNHLNDVATIYNKVIDEAKTRIITPEGIRIDALLDEPAPEAFLFETLHPLGFNSAQIKDIANSLHGQPGKQFVSKEWRVIKDRNLLLLETIRPEDESTLPYQLIKEEREFTPDFRIPREKETACFDADKLNEEIHCRKWQAGDTFIPFGMTGKKKISDYLTDRKFSISQKERQWVLCCGERIAWLIGERTDNRFRIDETTKRVIIYKIV	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.	Q8A7D1
Q9KJF6	XERC_STAAU	Tyrosine recombinase XerC	Staphylococcus	MNHIQEAFLNTLKVERNFSEHTLKSYQDDLIQFNQFLEQEHLQLNTFEYRDARNYLSYLYLNHLKRTSVSRKISTLRTLYEYWMTLDENIINPFVHLVHPKKEKYLPQFSLEEEMEALFTTVEKDTSKNLRDRVILELLYATGIRVSELVNIKKQDIDFYANGVTVLGKGSKERFVPFGAYCRQSIENYLEHFKPIQSCNHDFLILNMKGEAITERGVRYVLNDIVKRTAGVSEIHPHKLRHTFATHLLNQGADLRTVQSLLGHVNLSTTGKYTHVSNQQLRKVYLNAHPRAKKENET	Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.	Q9KJF6
Q4A0A8	TARI_STAS1	Ribitol-5-phosphate cytidylyltransferase	Staphylococcus	MIYAGILAGGIGSRMGNVPLPKQFLDLDGKPILVHTVEKFLLTSEFDKIFIATPQKWISHTKDTLRKHHITDDRIEVVQGGSDRNETIMNIISAAEKENGISDDDVIITHDAVRPFLTRRIIKENIESVLKYGAVDTVITATDTIITSADGDSIQSIPVRSEMYQGQTPQSFNVNLLRNSYNDLSDEDKQIMTDACKILVVAGKQVKLVMGELYNIKITTPYDLKVANSIIKGGMLSD	Catalyzes the transfer of the cytidylyl group of CTP to D-ribitol 5-phosphate.	Q4A0A8
Q9P7B4	YI13_SCHPO	L-allo-threonine dehydrogenase	Schizosaccharomyces	MSRLDGKTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPKEFADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVYKNSEPLTPEDIAEVILFALTRRENVVIADTLVFPSHQGGANHVYRKQA	NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L-allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate.	Q9P7B4
P15120	UROK_CHICK	Urokinase-type plasminogen activator chain B	Gallus	MKLIIFLTVTLCTLVTGLDSVYIRQYYKLSHKHRPQHRECQCLNGGTCITYRFFSQIKRCLCPEGYGGLHCEIDTNSICYSGNGEDYRGMAEDPGCLYWDHPSVIRWGDYHADLKNALQLGLGKHNYCRNPNGRSRPWCYTKRRYSIQETPCSTIEKCERTCGQRSFSKYFKIVGGSQAEVETQPWIAGIFQNIMGTDQFLCGGSLIDPCWVLTAAHCFYNPTKKQPNKSVYKVFLGKSILNTNDEHEQVFMVDEIISHPDFTDHTGGNDNDIALIRIRTASGQCAVESNYVRTVCLPEKNLNLYDNTWCEIAGYGKQNSYDIYYAQRLMSATVNLISQDDCKNKYYDSTRVTDNMVCAGDPLWETDACKGDSGGPMVCEHNGRMTLYGIVSWGDGCAKKNKPGVYTRVTRYLNWIDSNMNAVFTKSRSFREPK	Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.	P15120
B5EFL1	UBIE_CITBB	Demethylmenaquinone methyltransferase	Citrifermentans	MYALSEKGERIRAMFGSIAPRYDLLNRLLSLGIDRRWRRFAVKKIGLNGSGRVLDVATGTGDVALEIASQTPASVSIVGIDFTPEMIELGRVKVKDSRHCGRITLQVAPCEEIPFDDGSFDAATISFGIRNVVDRIKGLAEMHRVLKNDGKIVILEFSTPTLPVFKDLYHFYFLKVLPKIGGAFSRFSAYQYLPDSVLEFPSREVFKGMMTQVGFKDVRHFDLTGGIATVYVGTK	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).	B5EFL1
Q89UF8	UREF_BRADU	Urease accessory protein UreF	Bradyrhizobium	MLMTTNEPVNAGDLAAREAAALYRLMTWLSPAFPVGGFSYSSGIEWAVEAGDITDTATLADWLDTMLGDGSGFCDATFLVQAYRATEAGEETSLRDIAELASAFVPSRERQLETTSQGRAFIDIARAAWDAEGLDAMVAACRTPLVYPVAVGVVAAMHGVPLAPTLHAFLHAVVSNWISAASRLIPLGQTDSQRVLVRLEAAVAATATRALSATLDDLGSATFRADLASLRHETQYTRLFRS	Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.	Q89UF8
Q5E2R0	YACG_ALIF1	DNA gyrase inhibitor YacG	Aliivibrio	MTKPTTEQPTTVKCPTCQSAVIWNAESPFRPFCSKKCQMIDFGEWADEEKSIPGAPDMSDSDGWSEDQY	Inhibits all the catalytic activities of DNA gyrase by preventing its interaction with DNA. Acts by binding directly to the C-terminal domain of GyrB, which probably disrupts DNA binding by the gyrase.	Q5E2R0
C5BHG1	TSAD_EDWI9	tRNA threonylcarbamoyladenosine biosynthesis protein TsaD	Edwardsiella	MRILGIETSCDETGIAIYDDEKGILANQLYSQIKLHADYGGVVPELASRDHVRKTVPLIQAALREADLTPADLDGVAYTAGPGLVGALLVGATVGRSLAFAWGVPAVPVHHMEGHLLAPMLEENPPAFPFVALLVSGGHTQLISVTGIGEYRLLGESIDDAAGEAFDKTAKLLGLDYPGGPVLSRMAQQGVPGRFVFPRPMTDRPGLDLSFSGLKTFAANTIHANGDDAQTRADIARAFEDAVVDTLAIKCRRALDQTGFQRLVMAGGVSANRALRGRLAQMMQQRGGAVFYARPEFCTDNGAMIAYAGMVRLKSGVDADLSISVRPRWPLAELPPVAARS	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.	C5BHG1
Q9A6Q5	THIC_CAUVC	Thiamine biosynthesis protein ThiC	Caulobacter	MNIQSTIKAVAETISTGPIPGSRKVYQAGELFPELRVPFREVAVHPSANEPPVTIYDPSGPYSDPAIQIDIEKGLPRTREALVVARGDVEEVADPRQVKPEDNGFAQGKHLAPEFPDTGRKIYRAKPGKLVTQLEYARAGIITAEMEYVAIRENLRREQDRPCVRDGEDFGASIPDFVTPEFVRQEIARGRAIIPANINHGELEPMAIGRNFLVKINANIGNSAVLSTVADEVDKLVWATRWGADTVMDLSTGRNIHNIRDWIIRNSSVPIGTVPIYQALEKVNGVAEDLNWEVFRDTLIEQCEQGVDYFTIHAGVRLPFIPMTAKRVTGIVSRGGSIMAKWCLAHHKENFLYERFDEICEIMRAYDVSFSLGDGLRPGSTADANDEAQFSELRTLGELTKVAWKHGVQVMIEGPGHVAMHKIKANMDEQLKHCHEAPFYTLGPLTTDIAPGYDHITSAIGAAMIGWFGTAMLCYVTPKEHLGLPDRDDVKTGVITYKLAAHAADLAKGHPGAAMWDDAISRARFEFRWEDQFNLGLDPETARKFHDETLPKEAHKTAHFCSMCGPKFCSMKISQEVRDFAAGKAPNSAELGMAEMSEKFREQGSEIYLKTE	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.	Q9A6Q5
Q91507	VSP1_PROMU	Tm-VIG	Protobothrops	MVLIRVLANLLILQLSYAQKSSELVIGGDECNINEHPFLVLVYYDDYQCGGTLLNEEWVLTAAHCNGKDMEIYLGVHSKKVPNKDVQRRVPKEKFFCDSSKTYTKWNKDIMLIRLDRPVRKSAHIAPLSLPSSPPSVGSVCRVMGWGTITSPQETYPDVPHCANINLLDYEVCRAAYAGLPATSRTLCAGILEGGKDSCVGDSGGPLICNGQFQGIVSWGGDPCAQPREPGVCTNVFDHLDWIKGIIAGNTDVTCPL	Snake venom serine protease with strong beta-fibrinogenolytic activities, angiotensin I (AGT)-degrading activities and strong kallikrein-like activities in vitro, releasing bradykinin from kininogen (KNG1). Intravenous injection strongly lowers blood pressure in experimental rats, which may be explained by the action on angiotensin I and kininogen.	Q91507
A3N0Y0	YCIB_ACTP2	Inner membrane-spanning protein YciB	Actinobacillus	MKQLLEFIPLILFFTVYKLYGVQQAAITLVIATVIQLIVLKVLYKKIEKSQWIMGIFAVFFGILTAYFNDLNFLKWKVTIINGLFAAVLLVSQFVFKKPIIQMLLGKELKLPTNVWNRLNLGWAGFFIICMLLNIVISYYFSDDVWATFKTFGFTGLSLIAAIATGVYLYPHLKNVENTNEQA	Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.	A3N0Y0
A4VGU2	XPT_PSEU5	Xanthine phosphoribosyltransferase	Pseudomonas	MEQLKDKIRSHGIVLSDRVLKVDAFLNHQIDPVLMQAIGREFARRFRDDGITKIVTIEASGIAPAVMAGLELGVPVIFARKHQSLTLHDNLLTATVYSFTKQVESTIAVSTQHLSANDRVLIIDDFLANGKAAKGLISIINQAGASIAGLGIVIEKSFQTGRKELEEAGYRVESLARVASLADGAVQFID	Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis.	A4VGU2
Q9BZM4	ULBP3_HUMAN	Retinoic acid early transcript 1N	Homo	MAAAASPAILPRLAILPYLLFDWSGTGRADAHSLWYNFTIIHLPRHGQQWCEVQSQVDQKNFLSYDCGSDKVLSMGHLEEQLYATDAWGKQLEMLREVGQRLRLELADTELEDFTPSGPLTLQVRMSCECEADGYIRGSWQFSFDGRKFLLFDSNNRKWTVVHAGARRMKEKWEKDSGLTTFFKMVSMRDCKSWLRDFLMHRKKRLEPTAPPTMAPGLAQPKAIATTLSPWSFLIILCFILPGI	Binds and activates the KLRK1/NKG2D receptor, mediating natural killer cell cytotoxicity.	Q9BZM4
Q9Y3C4	TPRKB_HUMAN	TP53RK-binding protein	Homo	MQLTHQLDLFPECRVTLLLFKDVKNAGDLRRKAMEGTIDGSLINPTVIVDPFQILVAANKAVHLYKLGKMKTRTLSTEIIFNLSPNNNISEALKKFGISANDTSILIVYIEEGEKQINQEYLISQVEGHQVSLKNLPEIMNITEVKKIYKLSSQEESIGTLLDAIICRMSTKDVL	Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine . The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37 . TPRKB acts as an allosteric effector that regulates the t(6)A activity of the complex. TPRKB is not required for tRNA modification .	Q9Y3C4
Q0VQH0	UPPP_ALCBS	Undecaprenyl pyrophosphate phosphatase	Alcanivorax	MDWFQALVLALIQGLTEFLPISSSAHLILPSQILGWPDQGLAFDVAVHLGTLLAVMMYYRRDLIAMVGGAGLAVQQRRMNDDLKLGLLVALATIPAVVFGFLGDDFIERELRSALVIAITTLVFGALLWASDAFGKREFSLARLGVAGAIFIGLAQALALIPGTSRSGITITAALALGYRREDAARFSFLLSIPVILGAGLLKTKDLIEQQVVVDWGMMALGVIVSAVTAYLTIVFFIRLLERVGMLPFVVYRLILGVALLFWLA	Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.	Q0VQH0
Q9I068	TSI4_PSEAE	Immune protein Tsi4	Pseudomonas	MTTSSGSRIGGLLHASLFSLLGLGLLLAGGFKTVERYHFLRTAQEAQGTVSALNAGGSHPQIDFTSVSGERISYPQGGFIFGYQVGEPVRVLYEAGRPAASAIVDDAGALWGTGAFLCGFGALFGIVGFRGLLGLRSSQPTSKGH	Immunity protein that plays a role in preventing early activation of toxin Tse4.	Q9I068
B1ICC8	VATB_STRPI	V-ATPase subunit B	Streptococcus	MSVIKEYRTASEVVGPLMIVEQVNNVSYNELVEIQLHNGEIRRGQVLEIHEDKAMVQLFEGSSGINLEKSKIRFAGHALELAVSEDMVGRIFNGMGKPIDGGPDLIPEKYLDIDGQAINPVSRDYPDEFIQTGISSIDHLNTLVRGQKLPVFSGSGLPHNELAAQIARQATVLNSDENFAVVFAAMGITFEEAEFFMEELRKTGAIDRSVLFMNLANDPAIERIATPRIALTAAEYLAFEKDMHVLVIMTDMTNYCEALREVSAARREVPGRRGYPGYLYTNLSTLYERAGRLVGKKGSVTQIPILTMPEDDITHPIPDLTGYITEGQIILSHELYNQGYRPPINVLPSLSRLKDKGSGEGKTRGDHAPTMNQLFAAYAQGKKVEELAVVLGESALSDVDKLYVKFTKRFEEEYINQGFYKNRNIEDTLNLGWELLSILPRTELKRIKDDLLDKYLPLVEV	Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit.	B1ICC8
Q05741	TRXB_STRCL	Thioredoxin reductase	Streptomyces	MSDVRNVIIIGSGPAGYTAALYTARASLQPLVFEGAVTAGGALMNTTDVENFPGFRDGIMGPDLMDNMRAQAERFGAELIPDDVVSVDLTGDIKTVTDSAGTVHRAKAVIVTTGSQHRKLGLPREDALSGRGVSWCATCDGFFFKDQDIVVVGGGDTAMEEATFLSRFAKSVTIVHRRDSLRASKAMQDRAFADPKISFAWNSEVATIHGEQKLTGLTLRDTKTGETRELAATGLFIAVGHDPRTELFKGQLDLDDEGYLKVASPSTRTNLTGVFAAGDVVDHTYRQAITAAGTGCSAALDAERYLAALADSEQIAEPAPAV	Component of the thioredoxin-thioredoxin reductase system which may be involved in biosynthesis of penicillins and cephalosporins and may be important in determining the thiol-disulfide redox balance.	Q05741
Q4XFJ8	TCTP_PLACH	Translationally-controlled tumor protein homolog	Plasmodium (Vinckeia)	MKVYKDIFTNDEVCSDSYAQEDPFGNPEFREIAFEVKSNKRIKGNDDYGIADNSEDAVEGMGADVEHVIDIVDSFQLTSTSLSKKEYSAYVKNFMQRILKHLEEKKPDRVEIFKTKAQPLIKHILTNFDDFEFYMGESLDMEAGLIYSYYKGEEITPRFVYISDGLFEEKY	Involved in calcium binding and microtubule stabilization.	Q4XFJ8
P62722	VIRG_AGRT9	Regulatory protein VirG	Agrobacterium tumefaciens complex	MIVHPSRENFSSAVNKGSDFRLKGEPLKHVLLVDDDVAMRHLIIEYLTIHAFKVTAVADSTQFTRVLSSATVDVVVVDLNLGREDGLEIVRNLAAKSDIPIIIISGDRLEETDKVVALELGASDFIAKPFSIREFLARIRVALRVRPNVVRSKDRRSFCFTDWTLNLRQRRLMSEAGGEVKLTAGEFNLLLAFLEKPRDVLSREQLLIASRVRDEEVYDRSIDVLILRLRRKLEADPSSPQLIKTARGAGYFFDADVQVSHGGTMAA	VirG is required for the positive regulation of at least two vir loci encoded by the Ti plasmid of A.tumefaciens.	P62722
A5W1B2	UVRC_PSEP1	Excinuclease ABC subunit C	Pseudomonas	MSQVFDASAFLATCSGRPGVYRMFDGEARLLYVGKAKNLKKRLASYFRKAGLAPKTAALVARIAQVETTITANETEALLLEQNLIKEWRPPYNILLRDDKSYPYVFLSDGEFPRLGIHRGAKKAKGRYFGPYPSAGAIRESLSLLQKAFSVRQCEDSYYANRTRPCLQYQIKRCKGPCTDLVTAEEYAEDVRHSVMFLEGRSQQLGNELNAEMEKAAMALDFEKAAELRDQIALLRRVQDQQYIEGGSGDVDVIAAFVNPGGACVHLISVRGGRVLGSKNFFPQVGIEEEVAEVMAAFLSQYYLGNAERELPGELIVNVVHEDFNAITEALHTLRGRELTISHRVRGTRARWQQLAVTNAEQALNARLANRQHMAARFEALAEVLGLDEVPQRLECYDISHSSGEATVASCVVFGPEGPIKSDYRRFNIEGVTAGDDYAAMHQALTRRYGRIKDGEGKLPDVLLVDGGKGQLNMARDVMQALGFTDLTLLGVAKGVTRKAGFETLYLNDVHHEFTLKGDSSALHLIQQIRDEAHRFAITGHRARRGKARRVSSLEDVAGVGPKRRRDLLKHFGGLQELNRASIDEIAKAPGISKKLAESIYASLHSE	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.	A5W1B2
C5BB99	TDH_EDWI9	L-threonine 3-dehydrogenase	Edwardsiella	MKALSKLKAEEGIWMTDVPLPALGHNDIMIKIRKAAICGTDVHIYNWDTWSQKTIPVPMVVGHEYVGEVVAVGQEVRGFRIGDRVSGEGHITCGHCRNCRAGRTHLCRNTIGVGVNRQGAFAEYLVIPAFNAFKIPDNIPDALAAIFDPFGNAVHTALSFDLVGEDVLVSGAGPIGIMAAAVCRHVGARHVVITDVNDYRLDLARKMGVTRAVNVSRESLPEVMQALGMSEGFDVGLEMSGAPPAFHTMLDTMNHGGKIAMLGIPPGDMAIDWNQVIFKGLLIKGIYGREMFETWYKMAALIQSGLDLTPIITHQYAIDDFQKGFDVMRSGHSGKVILNWS	Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.	C5BB99
Q5KWH6	UVRC_GEOKA	Excinuclease ABC subunit C	Geobacillus thermoleovorans group	MNERLKEKLAVLPEQPGCYLMKDKHGTVIYVGKAKSLKARVRSYFTGTHDGKTQRLVEEIADFEYIVTSSNAEALILEMNLIKKHDPKYNVMLKDDKSYPFIKITAEKHPRLLITRKVKKDGGKYFGPYPNVQAANETKKLLDRLYPLRKCSTLPSRACLYYHMGQCLAPCVHPVSDEQNKAMVEQIVRFLNGGYEDVKRELAEKMHEAAETLEFERAKEYRDQIAAIEMTMEKQKMMLNDFIDRDVFGYAYDKGWMCVQVFFLRQGKLIERDVSIFPLYQDPDEEMLTFLGQFYAKAHHLKPKEVVLPSDIDGELARELLGVAVVQPKKGKKKELVELASKNAAIALKEKFYFIERDEERTIKAVERLGERLGIPAPRRIEAFDNSNIYGADPVSALVVFLDGKPAKKEYRKYKVKTVAGPNDYETMREVVRRRYTRVLKEGLPLPDLIIIDGGKGHLSAVRDVLENELGLDVPLAGLAKDEKHRTSELLAGDPPDVVPLDRQSQEFYLLQRIQDEVHRFAVMFHRKTRQKTMFHSVLDDIPGVGEKRKKALLNYFGSVKKMKEATVEELQRANIPRAVAEKIYEKLHE	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.	Q5KWH6
Q6UXN9	WDR82_HUMAN	WD repeat-containing protein 82	Homo	MKLTDSVLRSFRVAKVFRENSDKINCFDFSPNGETVISSSDDDSIVLYDCQEGKPKRTLYSKKYGVDLIRYTHAANTVVYSSNKIDDTIRYLSLHDNKYIRYFPGHSKRVVALSMSPVDDTFISGSLDKTIRLWDLRSPNCQGLMHLQGKPVCSFDPEGLIFAAGVNSEMVKLYDLRSFDKGPFATFKMQYDRTCEWTGLKFSNDGKLILISTNGSFIRLIDAFKGVVMHTFGGYANSKAVTLEASFTPDSQFIMIGSEDGKIHVWNGESGIKVAVLDGKHTGPITCLQFNPKFMTFASACSNMAFWLPTIDD	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) . Component of PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase . Together with ZC3H4, but independently of the SET1 complex, part of a transcription termination checkpoint that promotes transcription termination of long non-coding RNAs (lncRNAs) . The transcription termination checkpoint is activated by the inefficiently spliced first exon of lncRNAs and promotes transcription termination of lncRNAs and their subsequent degradation by the exosome .	Q6UXN9
Q31ZU8	YCIB_SHIBS	Inner membrane-spanning protein YciB	Shigella	MKQFLDFLPLVVFFAFYKIYDIYAATAALIVATAIVLIYSWVRFRKVEKMALITFVLVVVFGGLTLFFHNDEFIKWKVTVIYALFAGALLVSQWVMKKPLIQRMLSKELTLPQPVWSKLNLAWAVFFILCGLANIYIAFWLPQNIWVNFKVFGLTALTLIFTLLSGIYIYRHMPQEDKS	Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.	Q31ZU8
A3MM33	UVRC_BURM7	Excinuclease ABC subunit C	pseudomallei group	MTSPDAPESRFEPKPILAQLPHLPGVYRYYDVQDAVLYVGKARDLKKRVSSYFTKTQLSPRIAMMITRIARIETTVTRSEAEALLLENNLIKALAPRYNILFRDDKSYPYLKLTGHRFPRMAYYRGAVDKKNQYFGPFPSAWAVRESIQILQRVFQLRTCEDSVFNNRTRPCLLHQIGRCSAPCVGAIGEEDYARDVDNASRFLLGRQGEVMGELERKMHAFAAELKFEQAAAVRNQMSSLAKVLHQQAIDVGGDSDVDILAVVAQGGRVCVNLAMVRGGRHLGDKAYFPAHVETALALAGDIEALAGEGAGDGVQAAAQPAQAPLATDADATDAAATEAKTVTAAAAARAGARTAQAAGARAAASAEGDVERRAEGETHARADAREAAALPDGAAAAQEADADVDAAPLETEVLEAFIAQHYLGNRVPPVLVVSHAPANRELIDLLVEQAGHKVAVVRQPQGQKRAWLTMAEQNARLALARLLSEQGSQQARTRSLADVLGYESDDLAQLRIECFDISHTMGEATQASCVVYHHHRMQSSEYRRYNIAGITPGDDYAAMRQVLTRRYEKMVEEAAAEASADEAAGIDGNAVHAAASAGRLPNVVLIDGGRGQVEIARQVFSELGLDISMLVGVAKGEGRKVGLETLIFADGRAPLELGKESAALMLVAQIRDEAHRFAITGMRAKRAKTRQTSRLEELEGVGAKRRQRLLARFGGLRGVVAASVDELASVEGISRALAEQIYRQLH	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.	A3MM33
Q9WZ09	TRPB2_THEMA	Tryptophan synthase beta chain 2	Thermotoga	MRIVVNLKPEEIPKHWYNVLADLPFKLDPPLDPETKQPISPEKLSVIFPMSLIEQEVSEERFIEIPEPVLKEYAVYRPTPLIRATFLEEYLQTPARIYYKYEGVSPTGSHKPNTAIAQAYYNKIEGVKRLVTETGAGQWGSALSYAGAKFGLEVKVFMVKVSYQQKPMRKYMMNLFGGKVTPSPSEETNFGRKILSEDPDNPGSLGIAISEALEVAVSDPNTKYSLGSVLNHVLLHQTVIGLEIKKQLELIGEKPDILLGCHGGGSNFGGTILPFVPDKLSGRDIRFVACEPAACPSLTKGNYDYDFGDTAGLTPLLKMYTLGKDFIPPKIHAGGLRYHGSAPIIARLVKEGLVEAQAFDQDETFEAAKIFAKLEGIIPAPESAHAIAGAIREAKKAKEEGKERVIVFTLSGHGLLDLTAYV	The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.	Q9WZ09
E2AIS8	TACHY_CAMFO	Tachykinin-related peptide 4	Camponotus	MQCDFRVHQDARLARVYYFTEVWWMFIFKFLEPKMLINSVLFLAIWSSSFAEESSSSDATSNKRAAMGFQDMRGNKNLIPTSLEHNKLSKRTLMDFQDNKDSNAPDIEDNLSHEFEKRAPMGFQGMRGKKGYLTPDFEDSYFRDEKRAPMGFQGMRGKKVVSDDDYYKRAPMGFQGMRGKKSLEEVLGEIEKKAAMDYYDTRDKKTYVFEYPEDYEKRLLASIRGKLKEFPMEWEKRAPMGFQGMRGKKSLLDEIEELEKRTIMGFQGMRGKKNALENYIDYYLDPDMDFDKRAPMGFQGMRGKKDSDKRAPMGFQGMRGKRNTGQRFDTGINFNIRSSNEYQGTNNRRNALASCQLEKRSPFRYFEMRGKKNPRWELRGMFVGVRGKKWATAPYEDDSPFISVFDNTERIGVDGDSPAILGNSIS	Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles.	E2AIS8
E0ZS45	URED_ORYSI	Urease accessory protein D	Oryza sativa	MEAEAAMAAAAAATGAVRVEKVRGRSAVTRCFAKYPLKLIAPSKAGRASSGAAWLYAITYGGGIVSGDIISCTVAVGDGCAAAMTTQASTKVYKAVDSKCSEQVLEARVGEDALFALIPDPVTCFSMARYHQKQVFHVFPNSNLVVVDWFTSGRYESGEKWNFSFYKSINHILLEDQPLFIDSVLLEQSSNFSIADRMQEYNVVAMVILLGPKLKHIQDQMQDEVKKMMSVQLRPPTSAGGRYSTRSQPLHPQRPPIIASCSPFGRMGTGMVARITAVSTESVYSFLRHHLAALEPFLGACPYPAS	Required for the maturation and activation of urease via the functional incorporation of the urease nickel metallocenter.	E0ZS45

A1AWH8

PURA_RUTMC

IMP--aspartate ligase

Candidatus Ruthia

MSKNVVIIGTQWGDEGKGKVVDLITDKVASVVRFQGGHNAGHTLVINGKTTILHLIPSGILRNHVECLIGHGVVLSMSALLKEIAELEVADIDTTKRLKISPGCPLILPYHIELDNAREIKRGKAAIGTTGNGIGPAYEDKVARRGLRVSDLLDPNLFASKLKEVMEYHNFFLTHYYNANPVDYQTTLDEVLSQVEQTKHMIVDVTEQIHQHIANDENILFEGAQGALLDIDQGTYPFVTSSNTTSGAAVTGSGIGVTDIDYVLGIVKAYTTRVGGGPFPTELIYDVALDKGDEIGKVLGTVGHEFGATTGRQRRCGWLDMVTLKRSFNLNAVTGICLTKLDVMDTLETIKICTSYEIDGVETTIPPFSAEDYAKAKPIYIKIPGWKTSTIGTDSFDSLPVEAQSYIRKIEQLANLPVDILSTGPDRLQTLILKHPFE

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.

A1AWH8

O75081

MTG16_HUMAN

Zinc finger MYND domain-containing protein 4

Homo

MPASRLRDRAASSASGSTCGSMSQTHPVLESGLLASAGCSAPRGPRKGGPAPVDRKAKASAMPDSPAEVKTQPRSTPPSMPPPPPAASQGATRPPSFTPHTHREDGPATLPHGRFHGCLKWSMVCLLMNGSSHSPTAINGAPCTPNGFSNGPATSSTASLSTQHLPPACGARQLSKLKRFLTTLQQFGSDISPEIGERVRTLVLGLVNSTLTIEEFHSKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARLAKQTPAQYLAQHEQLLLDASASSPIDSSELLLEVNENGKRRTPDRTKENGSDRDPLHPEHLSKRPCTLNPAQRYSPSNGPPQPTPPPHYRLEDIAMAHHFRDAYRHPDPRELRERHRPLVVPGSRQEEVIDHKLTEREWAEEWKHLNNLLNCIMDMVEKTRRSLTVLRRCQEADREELNHWARRYSDAEDTKKGPAPAAARPRSSSAGPEGPQLDVPREFLPRTLTGYVPEDIWRKAEEAVNEVKRQAMSELQKAVSDAERKAHELITTERAKMERALAEAKRQASEDALTVINQQEDSSESCWNCGRKASETCSGCNAARYCGSFCQHRDWEKHHHVCGQSLQGPTAVVADPVPGPPEAAHSLGPSLPVGAASPSEAGSAGPSRPGSPSPPGPLDTVPR

Isoform 2 functions as an A-kinase-anchoring protein .

O75081

A0RQI7

RL10_CAMFF

50S ribosomal protein L10

Campylobacter

MTRNEKAEIISNLEAEFKTSDAIVVCDYKGLSVKKLEALRNSARELNVKVQVVKNTLANIALNNCGKSGMELKDTNIFVWGEDQLAVTKVVAKFEESNNELFKIKTAHIDGEVASVSKVVALSKMPSRDELIAMLLQVWNAPIQNFTIGLNALREKKEQTA

Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.

A0RQI7

A5IHB4

TRMB_LEGPC

tRNA(m7G46)-methyltransferase

Legionella

MQRKIKSYVLRAGRISNRQQQGLDLWLEDYELKFDSPSPWNFAKEFGRHDADTIVEIGFGMGTSLFTMAMNNPQCNYLGIEVHKAGVGSLVADLHEHQITNVRVVVHDAVDVLQTKIPENSLAGVQIFFPDPWHKKRHHKRRLIQSEFIQMLVKKIRPSGFIHCATDWEDYAEHILNVLSSESALFNQQKEGGYSPRPDSRPLTKFEQRGERLGHGVWDLVFIKK

Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.

A5IHB4

Q3KM49

TAL_CHLTA

Transaldolase

Chlamydia

MSSQFDQLKLWSVLVGDTGDPALIKTLGVQDATTNPSLILKVAQEPKYQSMLKEAISWGIRQNGDDVQTLTFVLDKIQVNLGLEILKHVPGRVSLEIDARLSFNTEAMVQRAIFLSQLFEKMGGDKKRLLVKIPGTWEGICAAEVLESQGIACNVTLIFNLVQAIAAAKAKVTLVSPFVGRIYDWWIAAYGAEGYSIEADPGVASVANIYSYYKKFDIPTQIMAASFRTKEQVLALAGCDFLTISPKLLEELKKDQQPVERKLSVEEAKKLDIQPVELSESVFRFLMNEDAMATEKLAEGIRIFSGDTQILESAVTEFIRQIAAQEA

Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.

Q3KM49

P60980

VSTX1_GRARO

Voltage sensor toxin 1

Grammostola

MKTSVFVLVLGLVLLFAVSFATEMEESARECGKFMWKCKNSNDCCKDLVCSSRWKWCVLASPF

Inhibits sodium channels Nav1.7/SCN9A and potassium channels Kv11.1/KCNH2. Also binds the voltage-sensor domain of the potassium channel KvAP (from the archaeon Aeropyrum pernix) with very slow apparent binding kinetics and affects channel gating. Reaches its target by dynamically partitioning into anionic or zwitterionic headgroup lipid membranes. May bind to the open state of KvAP.

P60980

A5CCV6

YQGF_ORITB

Putative pre-16S rRNA nuclease

Orientia

MIINSISEFLQAADIKKQILGIDFGEKKVGVAISNIEHTVAMPLQTILATNQDRVNKIQEIAVAYNIGAIVIGLPFKLDGTETSQTHRVKDFANKLANKLLLPIFLCDERLTSKAANNLLKIGNIKRKVRNAIDDRVAASIILEGALKRMQNSKSYF

Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.

A5CCV6

B3DI94

TM186_DANRE

Transmembrane protein 186

Danio

MDMMMMSTRLIHLSRHFPQYGFRCHPSGLISSARMQYNINNGLAHMGKQMPNTSTHTTRIHPASFSSDLASRKYSLIYAFPLIRGLRALSRLKLLQTGITVVLLPTVYYLHLQGQASVLVLNRSIGIALFAGVMLYSISHFVRRVVGMMYLDSTQTILKVSHLSFWGHRRDIYVPVSDVVTLGDSGDSRGESILRLKRYSTSNTMYFSTRLGRVVDRHAFGKVFGSLS

May be required for efficient assembly of the mitochondrial complex I.

B3DI94

Q5NRF6

YBEY_ZYMMO

Endoribonuclease YbeY

Zymomonas

MITVEADISDLWPEQSNWEALAQTACQQAVSVSASDFLLAKDYETEISVCFSDNDTVHALNKTWRDKDRPTNVLSFPMMEAEELAEIKNRVGSECLLGDIILAFDVAKKEALEKGISLENHVTHLITHGTLHLLGYDHILDNEAEIMEDLERKALAQLDIPDPYSDHETGKEGLDG

Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.

Q5NRF6

Q12LA0

TIG_SHEDO

PPIase

Shewanella

MQVSVETTEGLGRRLTISVPAEQIEKMVKDGITREAKRARLPGFRPGKVPLSEINKRYGQAIRQDVMGEVMQRNFIEAIIAEKLNPAGAPTFMPGKSVGESFEFVATFEIYPEITLTGLDTIAVEQPKAEVNDADLDAMIETLRKQHATFAVVERASAAGDKVKMNFVGSIDGEEFDGGKADDFELEIGSNRMIPGFETGVTGHKAGETFDIEVSFPEDYHAENLKGKAAKFAITLTEVQAAQLPEVNDEFATLFGITSGGVDALKAEIRKNMTRELEQALKANVKEQVINGLLAANDVTIPSALIDGEVEVLRKQAMQRFGGQTKNMPELPAELFTEQAERRVKIGLLLGEVIKTSELKAEDSRVQALIASMASAYEDPAEVVAYYNSNKEMMQNMRNVALEEQAVEALLKSAKVTTKEVAFEEFMNKASGRA

Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.

Q12LA0

Q110N2

TATA_TRIEI

Sec-independent protein translocase protein TatA

Trichodesmium

MNIFGIGLPEMIVILVVALLIFGPKKLPEIGRSLGQAINSFKAGARDFENEFKREAKHLEEGVKVSTSASEPEKVVDVSSATNTNKN

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. TatA could form the protein-conducting channel of the Tat system.

Q110N2

D0KWI6

TATC_HALNC

Sec-independent protein translocase protein TatC

Halothiobacillus

MTERDSSPEADKNGLADVVEETGMAGFLGHLVELRNRLLKGVLAVLVLFLILFPFRNELFTMLADPLSRHMPAGSTMIAVEVASPFFIPLKLTALTAVFIAIPFLLYQLWAFIAPGLYKHERKLVAPLVFSSTILFYLGAAFAYFVVFPVVFGFLSTAGPSDVNFAPDIGEYLSFVTSLFFAFGFVFEVPVAIVLLVIVGVVTPDKLAGFRRYAILIAFIIAAILTPPDVLSQFMMALPIIMLYEFGLFVSRFFYKAKLARAAEVEAEESGAADDESDEAVSARHAEYEAKAQTQADEPLDMDKAFDEAEADQRRLESDSSASDDGPESNTAGRTEEGEQPSTGSKPEDEPNAPSEPSPKKPDSPV

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.

D0KWI6

P11019

VATE1_BOVIN

Vacuolar proton pump subunit E 1

Bos

MALSDADVQKQIKHMMAFIEQEANEKAEEIDAKAEEEFNIEKGRLVQTQRLKIMEYYEKKEKQIEQQKKIQMSNLMNQARLKVLRARDDLITDLLNEAKQRLSKVVKDTTRYQVLLDGLVLQGLYQLLEPRMIVRCRKQDFPLVKAAVQKAIPVYKVATKRDVDVQIDQEAYLPEEIAGGVEIYNGDRKIKVSNTLESRLDLIAQQMMPEVRGALFGANANRKFLD

Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons . V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment .

P11019

Q2NW05

TYPH_SODGM

TdRPase

Sodalis

MFLAQEIIRKKRDGEPLSDEEIRFFINGVYDNTVSEGQIAALAMTIFFHDMDLQERVALTLAMRDSGHTLDWRREALGGPVVDKHSTGGVGDVTSLMLGPMIAACGGFVPMVSGRGLGHTGGTLDKLEAIPGLAIFLDDDAFRSQVKQVGVAIMGQTHSLAPADKRIYATRDITATVDSIPLITASILAKKLAEGLDALVMDVKVGSGALMPTLAGSEALAQAIVGVANGAGCRTIALLTDMNQVLASSAGNALEVREAVRFLTNDERNPRLFEVTMALCSEMLMIAGLAHSEDAARTALVRALDSGEAAERFGRMVAVQGGPADFVQRYDLYLPVATLSKPVFPAGEGYIRSMDTRALGMTVVALGGGRQRARDAIDYSVGLTEMARLGDYVDANTPLAVVHAASEESWARAAEAVRAAIQLGDVAPQALPVVYRRITAAAD

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.

Q2NW05

O94265

THI21_SCHPO

Hydroxymethylpyrimidine phosphate kinase 1

Schizosaccharomyces

MISTCITVAGSDCSGGAGVQADLKVFTAHSVYGMSAVTAITSQNTIGVNGVHLIPASYVEQQISACLLDVHCEVMKTGMLFNQQILKVIVESIDRFKIKKVVVDPLIATRKGALLVMPDYLELFVKELIPRAEVLIPNIAEALIILKHMTNEFVEIHHLEDVKAVGKKLIKAGCKNVVIRCDDIPFASDFFCSRETNMPPTWYLYVLCTSEGEVLLPQKWLASKTARGTSCALSSAVASNLAIGLDLVTATQNAVSYTQRALEMSFHLGRGANSLDYASALTRLPYEKGEFINFVRYHPSITPKWLSIVNHPFVEQLKAGTLSRLPFQKYLVLKYHMLINNAQAAGMMAFSSSSISAIEHSAKIIQAIKEENVTHLRICEQYGLSASQITKSKPEIVKSHSLFIHDTAQQDGLRGIQIAMLPFVFMIQEVVSQISASDGYPYVAWVEHCKDKSATSHIETLLESLETNSQIISLSKVQHLLGILEKSLDFERLVLDTSSSNESSVF

Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.

O94265

O22349

TBA3_ELEIN

Alpha-3-tubulin

Eleusine

MREIISIHIGQAGIQVGNACWELYCLEHGIEPDGTMPSDTSVGVAHDAFNTFFSETGSGKHVPRAIFVDLEPTVIDEVRTGSYRQLFHPEQLISGKEDAANNFARGHYTVGKEIVDLCLDRVRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQIISSLTTSLRFDGAINVDVTEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVPEITNAVFEPSSMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTVQFVDWCPTGFKCGINYQPPSVVPGGDLAKVQRAVCMISNNTAVAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGAEGADDEGDEGEDY

Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.

O22349

P93083

TDC2_CAMAC

Tryptophan decarboxylase TDC2

Camptotheca

MGSIDSNYDTESAGQCRPLEPEEFRKQAHQMVDFIADYYKNIESYPVLSQVEPGYLQSRLPETAPYRPEPFESILKDVHKDIIPGVTHWLSPNFFAYFPATVSSAAFVGEMLCTCFNAVGFNWLASPAELELEMVVMDWLASMLKLPNSFTFLGTGGGVIQGTTSEAILCTLIAARDRALESIGVDSIHKLVVYGSDQTHSTYAKACNLAGILPCNIRSIRTEAVANFSLSPDSLHREIEADVAAGMVPLYLCATVGTTSTTAIDSLSPLADVANDYGLWFHVDAAYAGSACICPEFRHYLDGIERADSLSLSPHKWLLSYLDCCCLWVKRPSVLVKALSTDPEYLKNKPSESNSVVDFKDWQVGTGRRFKALRLWFVMRSYGVANLQSHIRSDIQMAKMFEEFVNSDPRFEIVVPRVFSLVCFRLNPFSKSDPCNTELLNRKLLEWVNSTGQVYITHTKVGGVYMLRFAVGATLTEEHHVSAAWKLIREGADALLCS

Involved in the biosynthesis of tryptamine. Supplies tryptamine for the indole moiety of camptothecin (CPT), an anti-cancer monoterpene alkaloid. Represents a key step in monoterpene indole alkaloid biosynthesis. Is specific for tryptophan, and inactive against tyrosine, phenylalanine and 3,4-dihydroxyphenylalanine (dopa).

P93083

Q9S7B5

THRC1_ARATH

Protein METHIONINE OVER-ACCUMULATOR 2

Arabidopsis

MASSCLFNASVSSLNPKQDPIRRHRSTSLLRHRPVVISCTADGNNIKAPIETAVKPPHRTEDNIRDEARRNRSNAVNPFSAKYVPFNAAPGSTESYSLDEIVYRSRSGGLLDVEHDMEALKRFDGAYWRDLFDSRVGKSTWPYGSGVWSKKEWVLPEIDDDDIVSAFEGNSNLFWAERFGKQFLGMNDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMKRPVVGVGCASTGDTSAALSAYCASAGIPSIVFLPANKISMAQLVQPIANGAFVLSIDTDFDGCMKLIREITAELPIYLANSLNSLRLEGQKTAAIEILQQFDWQVPDWVIVPGGNLGNIYAFYKGFKMCQELGLVDRIPRMVCAQAANANPLYLHYKSGWKDFKPMTASTTFASAIQIGDPVSIDRAVYALKKCNGIVEEATEEELMDAMAQADSTGMFICPHTGVALTALFKLRNQGVIAPTDRTVVVSTAHGLKFTQSKIDYHSNAIPDMACRFSNPPVDVKADFGAVMDVLKSYLGSNTLTS

Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.

Q9S7B5

A6H2G3

TATA_FLAPJ

Sec-independent protein translocase protein TatA

Flavobacterium

MGRLGVTEILMILAVVLLLFGGKKIPELMKGLGSGLSEFKKAAKGDEVPDSKKDETKE

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. TatA could form the protein-conducting channel of the Tat system.

A6H2G3

Q2YS22

TYSY_BRUA2

Thymidylate synthase

Brucella

MRTYLDLLQHVLDHGVDRDDRTGTGTRSVFGYQMRFDLEEGFPVLTTKKLHLRSIIHELLWFLKGDTNIAYLKENGVTIWDEWADENGDLGPVYGYQWRSWPAPDGRHIDQIANLLKMLHTNPQSRRLIVSAWNPALVDEMALPPCHCLFQFYVANGRLSCQLYQRSADIFLGVPFNIASYALLTMMIAQVTGLKPGEFIHTLGDAHIYSNHFEQARLQLTRTPKKLPVMHINPDVKDLFAFRFEDFRLDGYEADPTIKAPIAV

Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.

Q2YS22

Q00063

THRC_ASHGO

Threonine synthase

Eremothecium

MSQVYRSTRSSSEDTKSFEEAVIQGLAEDGGLFLPAVIPRLREETLFEHWAHLSFQDLAMEIMKFYIADWEIPAPELRELIERSYSSFRSEEVTPLRKNVTGDDENLHILELFHGPTYAFKDVALQFVGNLFEYFLERKNRDVSEEERTHLTVVGATSGDTGSAAIYGLRGKQDVSVFILYPHGRISPIQEEQMTTVEDENVHTMAIEGSFDNCQDIVKSIFVDEEFNRKHNIAAVNSINWARILAQITYYFYSYFRATDGQPGRVKFIVPSGNFGDILAGFYAKQMGLPIEKLVIATNENDILDRFLREGVYERSEDVTATHSPAMDILVSSNFERLLWFFAREQLAQGDDQEAGSIVNRWFEQLREERRFDVPEHLLDAIRYHFDSERVDNYNTLASIRHIYEHAQNPERYVIDPHTAVGICAANRQIAHDQNNEIHYISLATAHPAKFADAVNEALSSYDDYNFDDVLPDRLRRLGDLEKRIKYVDNTDVDVIKSIIEEELINMGIYNP

Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.

Q00063

Q9VLN1

WDR82_DROME

WD repeat-containing protein 82

Sophophora

MKIKLIDSVVRSFKVAKIFRENTDKINAIDFAPNGEHLISCSEDDQIVIYDCEKGTQSRTVNSKKYGVDLIHFTHANNTAIHSSTKVDDTIRYLSLHDNKYLRYFPGHTKKVISLCISPVEDTFLSGSLDKTLRLWDLRSPNCQGLMHLSGRPIAAYDPEGLIFAAGVNSESIKLYDLRSFDKGPFVTFKLNQEKECDWTGLKFSRDGKTILISTNGSVIRLVDAFHGTPLQTFTGYPNNKGIPIEASFSPDSQFIFSGSTDGRVHIWNADTGNKVSVLNGDHPGPVQCVQFNPKYMMLASACTNMAFWLPTSEEGL

Component of the SET1 complex that specifically di- and trimethylates 'Lys-4' of histone H3 . Together with su(sable), part of a transcription termination checkpoint that promotes transcription termination of aberrant RNAs and their subsequent degradation by the nuclear exosome .

Q9VLN1

P70327

TBX6_MOUSE

T-box transcription factor TBX6

Mus

MYHPRELYPSLGTGYRLGHPQPGADSTFPPALTEGYRYPDLDTSKLDCFLSGIEAAPHTLAAAAPLPLLPSALGPETAPPPPEALHSLPGVSLSLENQELWKEFSAVGTEMIITKAGRRMFPACRVSVTGLDPEARYLFLLDVVPVDGARYRWQGQHWEPSGKAEPRLPDRVYIHPDSPATGAHWMRQPVSFHRVKLTNSTLDPHGHLILHSMHKYQPRIHLVRATQLCSQHWGGVASFRFPETTFISVTAYQNPRITQLKIAANPFAKGFRENGRNCKRERDARVKRKLRGPEPVATEACGSGDTPGGPCDSTLGGDIRDSDPEQAPTPQEAASASAPPCGGPSAEAYLLHPAAFHGAPSHLPARTPSFAEAPDPGRPAPYSAAFLDLQPGPGGSAYQAAPSVPSFAPHFIQGGPFPLPYPGPGGYLDMGSKPMY

T-box transcription factor that plays an essential role in the determination of the fate of axial stem cells: neural vs mesodermal. Acts in part by down-regulating, a specific enhancer (N1) of SOX2, to inhibit neural development. Seems to play also an essential role in left/right axis determination and acts through effects on Notch signaling around the node as well as through an effect on the morphology and motility of the nodal cilia.

P70327

P18728

ZG53_XENLA

Gastrula zinc finger protein XlCGF53.1

Xenopus

MGMWEEASDTGMKGKKKKKDKNEEEEEERGKKERMVNLTLEMIYLLTGEHYIPRKKSDDGGALHAPGSVIQKENNKNDEKILELMSNIIQLLTGEVAIRTHHVSIYFSLDEWDNIKGNKVLYEEGIKEEPQQLHPLDCEYEDKRDITADLGGTLCYNNETSKIGAEGTDFCAKENLTISPVEQPPPANRIKEERASCEEGNQSDCSINPLTEQIQGTDKPTPIMGYSLNNSSANYIKEEVVQCHEGNHSDMRIITAPESILETNTSAAMIRCNLNTSLSASCEGGNQSDCRINELTEQIQGTDTPTGNIVLYICSECQKHFSTKAGLARHQKTHSVFVGEEHAYGRIHTEEKPFPCSECGKRFARRQHLTDHQSSHTGEKPYACSQCEKYFPHRSNLNRHLKLHKGEKPFPCSQCGKRFPCVSDLNIHRRVHTGERPYSCSECGKCFKHHSNLTNHQRTHTREKPFSCTECGKGFKDRSSLTVHHRTHTGEKPFSCTECGKGFKDRSSLTVHHRTH

May be involved in transcriptional regulation.

P18728

C1CNW3

TRHO_STRZT

tRNA hydroxylation protein O

Streptococcus

MAKDIRVLLYYLYTPIENAEQFAADHLAFCKSIGLKGRILVADEGINGTVSGDYETTQKYMDYVHSLPGMEDLWFKIDEESEQAFKKMFVRYKKEIVHLGLEDNDFDNDINPLETTGAYLSPKEFKEALLDKDTVVLDTRNDYEYDLGHFRGAIRPDIRNFRELPQWVRDNKEKFMDKRVVVYCTGGVRCEKFSGWMVREGYKDVGQLHGGIATYGKDPEVQGELWDGKMYVFDERIAVDVNHVNPTIVGKDWFDGTPCERYVNCGNPFCNRRILTSEENEDKYLRGCSHECRVHPRNRYVSKNELTQAEVIERLAAIGESLDQAATV

Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.

C1CNW3

Q845X9

TRPD_BURM1

Anthranilate phosphoribosyltransferase

Burkholderia cepacia complex

MTITPQEALQRTIEHREIFHDEMLHLMRLIMRGDMSPVMAAAIITGLRVKKETIGEIAAAATVMREFANHVEVQDNSNFVDIVGTGGDGSHTFNISTASMFVTAAAGAKVAKHGNRGVSSKSGSADVLEALGVNIDLQPDQVAASIAETGMGFMFAPNHHPAMKNIAAVRRELGVRTIFNILGPLTNPAGAPNQLMGVFHPDLVGIQVRVMQRLGAQHVLVVYGKDGMDEVSLGAATLVGELRDGQVHEYEIHPEDFGLQMVSNRTLKVENAEESRAMLLGALDNQPGVAREIVTLNAGTALYAANVAGSIADGIQLAREAIASGKARAKVDELVRFTQQFKR

Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).

Q845X9

B7NVN0

TRPA_ECO7I

Tryptophan synthase alpha chain

Escherichia

MERYESLFIRLKERHEGAFVPFVTLGDPGIEQSLKIIDTLIEAGADALELGIPFSDPLADGPTIQNATLRAFAAGVTPAQCFEMLALIRQKHPTIPIGLLMYANLVFNKGVDEFYAQCEKVGVDSVLVADVPVEESAPFRQAALRHNVAPIFICPPNADDDLLRQIASYGRGYTYLLSRAGVTGAENRAALPLNHLVTKLKEYNAAPPLQGFGISAPDQVKAAIDAGAAGAISGSAIVKIIEQHINEPEKMLAALKAFVQPMKAATRS

The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.

B7NVN0

Q8U094

TRPA_PYRFU

Tryptophan synthase alpha chain

Pyrococcus

MFKDGSLIPYLTAGDPDKQSTLNFLLALDEYAGAIELGIPFSDPIADGKTIQESHYRALKNGFKLREAFWIVKEFRRHSSTPIVLMTYYNPIYRAGVRNFLAEAKASGVDGILVVDLPVFHAKEFTEIAREEGIKTVFLAAPNTPDERLKVIDDMTTGFVYLVSLYGTTGAREEIPKTAYDLLRRAKRICRNKVAVGFGVSKREHVVSLLKEGANGVVVGSALVKIIGEKGREATEFLKKKVEELLGI

The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.

Q8U094

Q9SLG3

ZIP3_ARATH

ZRT/IRT-like protein 3

Arabidopsis

MKTKNVKLLFFFFSVSLLLIAVVNAAEGHSHGGPKCECSHEDDHENKAGARKYKIAAIPTVLIAGIIGVLFPLLGKVFPSLRPETCFFFVTKAFAAGVILATGFMHVLPEAYEMLNSPCLTSEAWEFPFTGFIAMIAAILTLSVDTFATSSFYKSHCKASKRVSDGETGESSVDSEKVQILRTRVIAQVLELGIIVHSVVIGISLGASQSPDAAKALFIALMFHQCFEGLGLGGCIAQGKFKCLSVTIMSTFFAITTPIGIVVGMGIANSYDESSPTALIVQGVLNAASAGILIYMSLVDLLAADFTHPKMQSNTGLQIMAHIALLLGAGLMSLLAKWA

Mediates zinc uptake from the rhizosphere. May also transport other divalent cations.

Q9SLG3

B3Q867

TSAD_RHOPT

tRNA threonylcarbamoyladenosine biosynthesis protein TsaD

Rhodopseudomonas

MTSEQALLVLGIETTCDETAAAVVERRADGSGRLLSNIVRSQTDEHAPFGGVVPEIAARAHVDVLDGIIAAAMNEAGVAFASLSGVAAAAGPGLIGGVIVGLTTAKAIALVHGTPLIAVNHLEAHALTPRLTDAVEFPYCLFLASGGHTQIVAVLGVGNYVRLGTTVDDAIGEAFDKIAKMLGLPYPGGPQVERAAEAGDPNRFAFPRPMLGRQDANFSLSGLKTAVRNEAGKLTPLDPQDINDLCAGFQAAVLESVADRLGAGLRLFKERFGPPKALVAAGGAAANQAIRRMLREVAAKVQTTLIVPPPSLCTDNGAMIAWAGAERLALGLTDTMDTAPRARWLLDANATAPAKFANTRAGF

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.

B3Q867

Q8FHF8

YDEP_ECOL6

Protein YdeP

Escherichia

MKKKIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDKQVNASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDDVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAAFLYQLFAREYRSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGITEKPSAEFLDRLCERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAALPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTSSGKANFITSKGLLEDPSSAFNSKLVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRSSRRMDRLKVVIYPMADRSLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEPSN

Probably involved in acid resistance.

Q8FHF8

A8H738

TRUB_SHEPA

tRNA-uridine isomerase

Shewanella

MARRSRGRFIDGIVLLDKDTGMSSNFALQRVKRFFNANKAGHTGALDPLATGMLPICLGEATKFSQHLLDADKRYLVTAKLGQRTDTSDSDGEIVQTREVNFTQEQLDTALEYFRGETMQVPSMYSALKYQGQPLYKYAREGIEVPREARPINVFELNFISLEGDELTLDIHCSKGTYIRTITDDLGEMLGCGAHVIMLRRTQVAGYPYDKMVSLKQLEELVAKADAESLTLSEVLDPLLLPMDTAVSGFKEINVSDELATYLMNGNPVQVANLPVDELVRITIGDARQFVGIGQMNDDGLLAPKRLIVLREPQD

Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.

A8H738

Q9NSU2

TREX1_HUMAN

Deoxyribonuclease III

Homo

MGSQALPPGPMQTLIFFDMEATGLPFSQPKVTELCLLAVHRCALESPPTSQGPPPTVPPPPRVVDKLSLCVAPGKACSPAASEITGLSTAVLAAHGRQCFDDNLANLLLAFLRRQPQPWCLVAHNGDRYDFPLLQAELAMLGLTSALDGAFCVDSITALKALERASSPSEHGPRKSYSLGSIYTRLYGQSPPDSHTAEGDVLALLSICQWRPQALLRWVDAHARPFGTIRPMYGVTASARTKPRPSAVTTTAHLATTRNTSPSLGESRGTKDLPPVKDPGALSREGLLAPLGLLAILTLAVATLYGLSLATPGE

Major cellular 3'-to-5' DNA exonuclease which digests single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA) with mismatched 3' termini . Prevents cell-intrinsic initiation of autoimmunity . Acts by metabolizing DNA fragments from endogenous retroelements, including L1, LTR and SINE elements . Plays a key role in degradation of DNA fragments at cytosolic micronuclei arising from genome instability: its association with the endoplasmic reticulum membrane directs TREX1 to ruptured micronuclei, leading to micronuclear DNA degradation . Micronuclear DNA degradation is required to limit CGAS activation and subsequent inflammation . Unless degraded, these DNA fragments accumulate in the cytosol and activate the cGAS-STING innate immune signaling, leading to the production of type I interferon . Prevents chronic ATM-dependent checkpoint activation, by processing ssDNA polynucleotide species arising from the processing of aberrant DNA replication intermediates . Inefficiently degrades oxidized DNA, such as that generated upon antimicrobial reactive oxygen production or upon absorption of UV light . During GZMA-mediated cell death, contributes to DNA damage in concert with NME1 . NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair .

Q9NSU2

A5II09

TRHO_LEGPC

tRNA hydroxylation protein O

Legionella

MKDIIIASFYKFIPLNDFESLREPILTKMHEIGIKGTIILAHEGVNGGFAGNREQMNVFYDYLRSDSRFADLHFKETYDSKNPFDKAKVKLRKEIVTMGVQKVDPSYNAGTYLSPEEWHQFIQDPNVILLDTRNDYEYELGTFKNAINPDIENFREFPDYVQRNLIDKKDKKIAMFCTGGIRCEKTTAYMKELGFQHVYQLHDGILNYLESIPESESLWEGKCFVFDDRVAVDQKLDRVYPQLPQDYKYEREQK

Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.

A5II09

Q21BZ6

UBIG_RHOPB

3-demethylubiquinone 3-O-methyltransferase

Rhodopseudomonas

MSMQSNSSDASSATVDPAEIAKFSRLSAQWWDPTGKMAPLHKINPLRLSFIRDAACRKFERNAKSLNCLSGLRMIDIGCGAGLLCEPFTRLGAQVIGVDPSATNIAAAKLHAEKSQLLIDYRCTTVEQMDPRERFDIVLAMEVIEHVTDVGAFLARCAAITKPGGLMVVATLNRNWKSFALAIVGAEYVMRWLPRGTHQWDKFVTPDELTKHLHNNKLAVTEQAGLVYNPLADKWSLSADMDVNYMVVAETAAG

O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.

Q21BZ6

Q49ZD7

TRUA_STAS1

tRNA-uridine isomerase I

Staphylococcus

MRVLVNISYQGSQFLGFQIQQHGRTIQQQFEKILKRMHKHEVRIHPSSRTDRGVHAIEQYFHFDTELNIPEQQWQYAMNRALPDDIYVNDVSFVNDDFHCRYDCVGKSYRYKIYQSAHKDPFLCGLKTYVPEQLDIEKMNMAAQHFIGTHDFTGFCSQKTEVESKIRTLYESRIEKTESGFDYIVTGSGFLYNMVRVLIAFLIEVGKGKREPQEVPQLLEARDRNQVPFTAPAEGLYLEKIYLTPNELIQDFGNNIKIHQKKSSQNL

Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.

Q49ZD7

A9GP90

UREG_SORC5

Urease accessory protein UreG

Sorangium

MHDPGEHGHGRHDHDHDHDHVHDHDHDHDHVHGGGHRHAHEHEHAHEHAHGHEHGHAHAHAHAHAHEHAHGHTHEHWAHPGLFSERDAPKDRDFSARAFTVGIGGPVGSGKTALVLALCRALRDRMPLGVVTNDIFTQEDAEFLHRNKALPPERIRAVETGGCPHAAIREDISHNLVALDDLMDHVAPALLIVESGGDNLAAQYSRELVDYTIYVIDVAGGDKVPRKGGPGITQSDLLVINKTDLAPHVGADLGVMERDARRMRGDGPFLFAQCNRSQGVPEIIDHILSAMRRATTTAPPAK

Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.

A9GP90

A4FAI5

Y1742_SACEN

Putative S-adenosyl-L-methionine-dependent methyltransferase SACE_1742

Saccharopolyspora

MSANEQWDIVSGVGITALAVAVARARESRRDDRLIDDPYAEPLIRAAQPPVPMSGDGGEAGALWHEMTDYVSVRSRFFDEWFARACAAGTRQAVVLASGLDTRAFRLEWPEGFRVFEIDQPKVLEFKDGTLAAEGVRASCERHAVAVDLRDDWASALVKAGFDPALPTAWLAEGLLPYLPPEAEANLLATVHDLSARGSRIAIESIALARSALLGADLDDTAREWGIDLKGLFSLEDRPDPGDVLAQRGWRVHRDPVGDLAAGFRRPLSDRAQQLGAAGEMVTAQRD

Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.

A4FAI5

A3D3E2

TOLB_SHEB5

Tol-Pal system protein TolB

Shewanella

MRILAKWLALAVLLCTTPAKAALDIVITEGVDAARPIAVMPFVWQGSGAAPQAIADVVMSDLVRSGTFKPLDELGLPQRNIGTAAQFQANSWSSVGAEALVLGTVKPYGTDQYLVSFDLIDLVKAQNQALKGPVSATEFLMDSRQTVISAAQFRQYGHRISDIVYEKLTGIRGAFLTRISYVVVNHTQKAPYQLMVADYDGVNEQMLLRSPEPLMSPTWSPDGRRLAYVSFENKKAEIFVQDLYTQVRTKVSSFPGINGAPAFSPDGKSLAITLSKDGQPEIYIIDIATKAIKRITNHYAIDTEPSWYPDGKSLIFTSERGGRPQIYRVELSSGKVSRETFEGEWNLGGSITPDGRSMIFVNRTNGKFNIARMDLSTRFMQVLTSTRLDESPSVAPNGTMVIYGTTYQGKQVLAAVSTDGRFKARLPAGQGEVKSPSWSPFL

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.

A3D3E2

O00124

UBXN8_HUMAN

UBX domain-containing protein 6

Homo

MASRGVVGIFFLSAVPLVCLELRRGIPDIGIKDFLLLCGRILLLLALLTLIISVTTSWLNSFKSPQVYLKEEEEKNEKRQKLVRKKQQEAQGEKASRYIENVLKPHQEMKLRKLEERFYQMTGEAWKLSSGHKLGGDEGTSQTSFETSNREAAKSQNLPKPLTEFPSPAEQPTCKEIPDLPEEPSQTAEEVVTVALRCPSGNVLRRRFLKSYSSQVLFDWMTRIGYHISLYSLSTSFPRRPLAVEGGQSLEDIGITVDTVLILEEKEQTN

Involved in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins, possibly by tethering VCP to the endoplasmic reticulum membrane. May play a role in reproduction.

O00124

Q8EPB7

TPX_OCEIH

Thioredoxin-dependent peroxiredoxin

Oceanobacillus

MSNVTFKNDPVTLLGAEKKVGDSAPDFTVLANDLSKKHLSDYKGKVKVISVVPSIDTGVCSEQTRRFNQEATNLENVQILTISMDLPFAQKRWCAANGIDRVDTLSDHREADFGQKYGVIIEELRLLSRAVFVVDENDKITYVEYLSEVSNHPDYEAVLSHLNK

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.

Q8EPB7

B0B9D4

TRMD_CHLT2

tRNA [GM37] methyltransferase

Chlamydia

MEIDILSLFPDYFASPLQATILGRAIKQGALSVRSRDIREFGLGKWKQVDDSPYNGEGMLLMAEPVVQAIRSIRRKKSKVIYLSPQGQLLSAKKSRELASCSHLVLLCGHYEGIDERALTAEVDEEISIGDYVLTNGCAAALVLVDALARFIPGILGNQESAEYDSLENGLLEGPQYTRPRVFEGESVPEVLLCGDHQKIADWRKQVSLERTRERRPDLYLQYFYGNSACLSTQEDLPRIEVVSPKTFSVVLEVQDLRKAKKFYSRMFGKECWDGDKLFLLGKTSLYLQQTKETRGPTTVFIELETDHDFVRFLKRWEMLGGELGEQGTGGFPLRQVFDLDGHIWVVSCVQK

Specifically methylates guanosine-37 in various tRNAs.

B0B9D4

A1UU52

TRUB_BARBK

tRNA-uridine isomerase

Bartonella

MSRQSKKKGRSISGWVILDKPKAMKSTEAVSKIKRLFNAQKAGHAGTLDPLASGLLPIALGEATKTVPYVMEGTKTYHFHVAWGEERSTDDLEGVVTKTSSKRPTQEEIFALLPKYTGVILQTPPQFSAIKIAGNRAYDLAREGEIFEIPPRQVKIDSLELIGTTDQGYSIFEMTCGKGTYVRSLARDMGHDLGCYGYIADLRRTAVAPFCENDLITWDALKAAIPHENTTDENCIPLKQNFSTLDGLLIETDVALKCLAHYTLNQIQAQRVRMGNSILLCDQNMPTSNIDICVTYKAQLLAIGTIDQNQFKPKRIFTTL

Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.

A1UU52

Q2SUP3

THIC_BURTA

Thiamine biosynthesis protein ThiC

pseudomallei group

MNANPKFLSADARVDAAAVAPLPNSRKVYVTGSQPDIRVPMREITQADTPTSFGGEKNPPIYVYDTSGPYTDPDAKIDIRAGLPALRQRWIDARGDTETLAGLTSEYGRERAADPATAELRFPDLHRHPRRAKAGRNVTQMHYARQGIITPEMEFIAIRENQRRAEYLESLKASGPNGAKLAAMMGRQHAGQAFGAAAFGANEAGTNMLTEITPEFVRSEVACGRAIIPANINHPETEPMIIGRNFLVKINANIGNSAVTSSIGEEVDKMTWAIRWGGDTVMDLSTGKHIHETREWIIRNSPVPIGTVPIYQALEKVNGKAEDLTWEIFRDTLIEQAEQGVDYFTIHAGVRLQYVPLTANRMTGIVSRGGSIMAKWCLAHHKESFLYEHFEEICEIMKAYDVSFSLGDGLRPGSIYDANDEAQLGELKTLGELTQIAWKHDVQVMIEGPGHVPMQLIKENMDLQLDWCKEAPFYTLGPLTTDIAPGYDHITSGIGAAMIGWFGTAMLCYVTPKEHLGLPNKDDVKEGIITYKLAAHAADLAKGHPGAQVRDNALSKARFEFRWEDQFNLGLDPDKAREFHDETLPKDSAKVAHFCSMCGPHFCSMKITQDVREFAAQQGMSEDDALKKGMEVKAVEFVKTGSEIYHRQ

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.

Q2SUP3

A3PBC8

YIDD_PROM0

Putative membrane protein insertion efficiency factor

Prochlorococcus

MFKTINKSITSILLLLISFYQKWFSPFFGPRCRFIPSCSSYGYEAITRHGPWKGGWLTLKRLSRCHPLTPCGCDPVPD

Could be involved in insertion of integral membrane proteins into the membrane.

A3PBC8

Q6AQH2

UPP_DESPS

UPRTase

Desulfotalea

MSLHIADHPLVKHKLGLMRQNDISTKDFRALASEIARLLTYEAVKDLPTEKHIVDGWAGPVEVDRLKGKKITIVPILRAGLGMMDGVIDLIPSAKVTVVGFYRDEETLEPVEYYVKTASEMSERVALIIDPMLATGGTLIATIDTLKKAGSKKIKGLFLVAAPEGIKKVQDAHPDVEIYVAAVDERLNEAGYILPGLGDAGDKIFGTR

Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.

Q6AQH2

C3L3F6

YBEY_CLOB6

Endoribonuclease YbeY

Clostridium

MIYIDNRQNKIKVNEEFENKIKEIIDYALKEEKVNIDYEISVVFIDNNSIKEINKDYRNIDKATDVLSFPMLDYEEGKVFKDVYLNYEFDESDLDEGNLILGDIALSLEKAEEQSKEFGHSFLRETCYLTIHSVLHLLGYDHMEEEEKAIMRQREEEILKSFNLRR

Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.

C3L3F6

Q8BH57

WDR48_MOUSE

USP1-associated factor 1

Mus

MAAHHRQNTAGRRKVQVSYVIRDEVEKYNRNGVNALQLDPALNRLFTAGRDSIIRIWSVNQHKQDPYIASMEHHTDWVNDVVLCCNGKTLISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTASNNTVTTSSLSGNKDSIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLHRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALQVNDAFTHVYSGGRDRKIYCTDLRNPDIRVLICEEKAPVLKMELDRSADPPPAIWVATTKSTVNKWTLKGIHNFRASGDYDNDCTNPITPLCTQPDQVIKGGASIIQCHILNDKRHILTKDTNNNVAYWDVLKACKVEDLGKVDFEDEIKKRFKMVYVPNWFSVDLKTGMLTITLDESDCFAAWVSAKDAGFSSPDGSDPKLNLGGLLLQALLEYWPRTHVTPMDEEENEVNHVSGGQESRVQKGNGYFQVPPHTPVIFGEAGGRTLFRLLCRDSGGETEAMLLNETVPQWVIDITVDKNMPKFNKIPFYLQPHASSGAKTLKKDRLSASDMLQVRKVMEHVYEKIINLDNESQTTSSSNNEKPEQEKEEDIAVLAEEKIELLCQDQVLDPNMDLRTVKHFIWKSGGDLTLHYRQKST

Regulator of deubiquitinating complexes, which acts as a strong activator of USP1, USP12 and USP46. Enhances the USP1-mediated deubiquitination of FANCD2; USP1 being almost inactive by itself. Activates deubiquitination by increasing the catalytic turnover without increasing the affinity of deubiquitinating enzymes for the substrate. Also activates deubiquitinating activity of complexes containing USP12. Docks at the distal end of the USP12 fingers domain and induces a cascade of structural changes leading to the activation of the enzyme. Together with RAD51AP1, promotes DNA repair by stimulating RAD51-mediated homologous recombination. Binds single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA). DNA-binding is required both for USP1-mediated deubiquitination of FANCD2 and stimulation of RAD51-mediated homologous recombination: both WDR48/UAF1 and RAD51AP1 have coordinated role in DNA-binding during these processes.Together with ATAD5 and by regulating USP1 activity, has a role in PCNA-mediated translesion synthesis (TLS) by deubiquitinating monoubiquitinated PCNA. Together with ATAD5, has a role in recruiting RAD51 to stalled forks during replication stress.

Q8BH57

A6LTL5

THIG_CLOB8

Thiazole synthase

Clostridium

MKKDVLTLGGHEFSSRFILGSGKYNLNLIKAAVENAGAQMITLALRRANTSGGENILDFIPEGVTLLPNTSGARNAEEAVRIARLARAMNCGDFVKVEIIHDSKYLLPDNYETIKATEILAKEGFIVMPYMHADLNVARDLVNAGAACIMPLASPIGSNKGLATKEFIKILVDEIDLPIIVDAGIGRPSQACEAMEMGVAAVMANTAIATAGDIPAMAGAFKQAIEAGRAAYLSGLGRVLDKGASASSPLTGFLED

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.

A6LTL5

Q21UL3

UBIG_ALBFT

3-demethylubiquinone 3-O-methyltransferase

Rhodoferax

MSHQPYFADNHPMTSTLNADPAELAKFSDLAHRWWDLEGEFRPLHQINPLRLEWINHLCPVAGQQVLDVGCGGGILADSMARLGAQVTGIDLASKALRVAQLHALEAQTPNLQYQEISVEALAAQQPGSFDVVTCMEMLEHVPDPASVVRACATLVKPGGWVFFSTLNRSPKSFVLAIVGAEYVLNLLPRGTHEYAKMIRPSELASYCRSVELDLRHTRGMQYNPLTRRYWMSDDTSVNYLFATQKSNAAIL

O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.

Q21UL3

Q0IHY4

TBC12_XENTR

TBC1 domain family member 12

Silurana

MVGPEDAGQGAVYRCGEERHGLTDAADEEEGEGEAGDRQTDILQLYISRPAIKMTNGDLNYLPQGGAGEGDMPSAGDMHSLSTHKEDIKQPNGGLLVADSTRPQGCACHRQCCSLSEAVPSPGTPPGSSPISSSSSSPVSARTVAGYFVSEEADRFRFLDVSRQSCRNTFEGSRRQSAPDHLADGLSLPAESPGTAEQDGDRPWKVGIAEFFSRNFFSKRTKDPKSSSSVPGWKLFGKVPPRETAQKDSKIIQQDDSSGSLSSVSTPNLLNTGEYEARTGRSCKAPSQSTRKKKFEFEPLSTTALILEDRPSNLPAKSVHETLRHRQEYDEMVAEAKKREVKEAQRRKKLMKERIRQEENIASAMVIWNTEILPNWDVMRSTRRVRDLWWQGLPPSIRGKVWSLAIGNELNITPELYEIFLSRAKERWKSFSETNSENENEDAGASLADREASLELIKLDISRTFPSLYIFQKGGPYHDLLHSILGAYTCYRPDVGYVQGMSFIAAVLILNLEEADAFIAFANLLNKPCQLAFFRVDHSMMLKYFAAFEVFFEENLPKLFFHFNAYSLTPDLYLIDWIFTLYSKSLPLDLACRVWDVFCRDGEEFLFRTALGILRLYEDILLQMDFIHIAQFLTKLPEDITSEKLFGCIAAIQMQNSNKKWTQVFTSLMKDYKEGDKMSQASKT

May act as a GTPase-activating protein for Rab family protein(s).

Q0IHY4

Q0TNU2

YBEY_CLOP1

Endoribonuclease YbeY

Clostridium

MIFIDNRQNKFEVTEELTKKLEEVISFVLKEEKVKEDCEVSLVFVDNEEIRGINNETRGIDRATDVLSFPMIDYPEDKVYKDVYLEHEFDKCYFDGDELILGDIVLSLERTKEQSIEFNHSFEREACYLVTHSVLHLLGYDHMEEEEKARMRGREEELLGKLNITRES

Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.

Q0TNU2

A9WLN5

UPP_RENSM

UPRTase

Renibacterium

MRVLVVDHPLVAHKLTVLRDKNTPSPVFRQLTEELVTLLAYEATREVRVEEVSIETPVTKTVGTGLVKPTPLVVPILRAGLGMLEGMTRLLPTAEVGFLGMARNEETLEAITYAERLPEDLTGRQVYVLDPMLATGATLREAIKFLFARRALDITCICLLGAPEGIEALREQHEGANVTIVLASIDEGLNEKAYIVPGLGDAGDRLYGVVG

Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.

A9WLN5

Q7JR49

VAS1_DROME

Vacuolar H(+) ATPase AC45 accessory subunit

Sophophora

MLWKSLIALCVIGAAVAEQTPVFLWGANSVAKPSLKTVSQVEFAEQLAALLEDHMVVAFEENGLSSKDFLCSNSQAQSCYAQLQGVSPKTYYTSVENPSEALRSVAAKREHNSIDASGKLTTPAKCAVGTALFVTFEDAAESREASLESHDAAIAAISKQFECKVAYLYLAAPSTAPVVQRRTRRDTAATTGGIMWKSTNQFQIFYTALLYNGNPITVTDLKLTNSSSTKLSVVMDTSVADKPITFDVVYNGGYFSLSNLVYDNNNFRSSGVNAPTTFSYSCGNLTLESAAVNNMYNTLSFKSLQLQAPFDGTYKEDFPFGDSWDCVGFVTPGILMGLFVVALLLVIMFVGVCWMMDINTMDRFDDPKGKTITINAAAE

Accessory subunit of the proton-transporting vacuolar (V)-ATPase protein pump, which is required for luminal acidification of secretory vesicles.

Q7JR49

A9HI81

UPPP_GLUDA

Undecaprenyl pyrophosphate phosphatase

Gluconacetobacter

MDSRTMTLIQAIVIAILQGATELFPVSSLGHAVIVPALLGWAFDPHGEIFLPFLVMLHLGTAIALLVYFRNDWAAIFQGLRGRDGSQRQAESIHILALLVVATIPAVIIGGLLEHWLRALFGTARYAAIFLFLNGLLLLLTERMKSRQPVQGGYAIASLTYADAAIIGLWQCLAFLPGISRSGATIIGALFRGLNHEGAARFSFLMAQPVIIAATVREALHMRHVAIPPGQMQVATIGAMVAAVTALASTAFLMRYFHNHERWALSPFGYYCVLAGAVSFFILGH

Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.

A9HI81

Q5M8X5

TPC2L_XENTR

Trafficking protein particle complex subunit 2-like protein

Silurana

MAVCVAVIAKENYPLYIRSTPTENQLKFHYTVHTSLDVVDEKISAMGKAVMDQRELYLGLLYPTEDYKVYGYVTNSKVKFVMVVDSSNTSLRDNEIRSMFRKLHNSYTDVMCNPFYNPGDPIQSRAFDNTVTSMMVPAC

May play a role in vesicular transport from endoplasmic reticulum to Golgi.

Q5M8X5

Q83RF3

YDEP_SHIFL

Protein YdeP

Shigella

MKKKIESYQGAAGGWGAVKSVANAVRKQMDIRHDVIAMFDMNKPEGFDCPGCAWPDPKNSASFDICENGAKAIAWEVTDKQVNASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAAFLYQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGITEKPSAEFLARLGERYGFPPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAALPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNSKLVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRSSRRMDRLKVVIYPMADRSLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEPSN

Probably involved in acid resistance.

Q83RF3

Q55031

TBP_SACSH

TATA-box factor

Saccharolobus

MSNSAVSYKPIVNIENIVATVTLEQSLDLYAMERSIPNIEYDPDQFPGLIFRLEQPKVTALIFKSGKMVVTGAKSTEELIKAVKRIIKTLKKYGIKIMGKPKIQIQNIVASANLHVNVNLDKAAFLLENNMYEPEQFPGLIFRMDDPRVVLLIFSSGKMVITGAKREDEVSKAVKRIFDKLAELDCVKPIEEEEELEL

General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation.

Q55031

B3GZ49

TORD_ACTP7

Chaperone protein TorD

Actinobacillus

MAHSQLLSSEERLFCYRWFHSLLAKELSEPQLQALQAGQFASFFALLAELGFQPQVTDLQNELAKLTAYDSPRLELAADFAQCFLLEGKLSALPYASYYLDERDLSENLAVMDQWLTKFQLKINRLHNEPSDHLCIYLEVLIKLIETEQPVQVQQQFIRQQLLGWLPQWAEKTAQIHSSTAFYQIISNLLLGFLQQDIA

Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor.

B3GZ49

P18734

ZG67_XENLA

Gastrula zinc finger protein XlCGF67.1

Xenopus

SDRKTVSCPECGKCFTSRTYLNVHKKVHTGQTYSCSECGKSFLSRSHLNTHLRTHTGEKPYSCSECGKCFTSSAILITHKRIHTGERPFSCQECGKSFSYRSVFMEHQKIHTGEKPFSCSDCGKCFRYRSHLKVHSRIH

May be involved in transcriptional regulation.

P18734

Q6INE8

VMP1_XENLA

Vacuole membrane protein 1

Xenopus

MAENGTDCEQRRVGMPKEQNNGSFQDPSFMCNRKRRDREERQSIVLWRKPLITLQYFILEVLINLKEWSVRLWHRRMMVVSVLLLLAVLSVAYYIEGEHQQCVQYIEKKCLWCAYWVGLGILSSVGLGTGLHTFLLYLGPHIASVTIAAYECNSVNFPEPPYPDEIICPDEEGTEGAISLWTIISKVRLEACMWGAGTAIGELPPYFMARAARLSGVETDDEEYAEFEEMLEHAQTAQDFATRAKLTVQNLVQKVGFLGILACASIPNPLFDLAGITCGHFLVPFWTFFGATLIGKAIIKMHIQKLFVIITFSKHIVEQMVSLIGVIPSIGPSLQKPFQEYLEAQRKKLHHKGDSGTPQSENWLSWAFEKLVIIMVFYFILSIINSMAQSYAKRVQQKKLSVEKTK

Phospholipid scramblase involved in lipid homeostasis and membrane dynamics processes. Has phospholipid scramblase activity toward cholesterol and phosphatidylserine, as well as phosphatidylethanolamine and phosphatidylcholine. Required for autophagosome formation: participates in early stages of autophagosome biogenesis at the endoplasmic reticulum (ER) membrane by reequilibrating the leaflets of the ER as lipids are extracted by atg2 (atg2a or atg2b) to mediate autophagosome assembly. In addition to autophagy, involved in other processes in which phospholipid scramblase activity is required. Modulates ER contacts with lipid droplets, mitochondria and endosomes.

Q6INE8

Q9Y5Q9

TF3C3_HUMAN

Transcription factor IIIC subunit gamma

Homo

MSGFSPELIDYLEGKISFEEFERRREERKTREKKSLQEKGKLSAEENPDDSEVPSSSGINSTKSQDKDVNEGETSDGVRKSVHKVFASMLGENEDDEEEEEEEEEEEEEEETPEQPTAGDVFVLEMVLNRETKKMMKEKRPRSKLPRALRGLMGEANIRFARGEREEAILMCMEIIRQAPLAYEPFSTLAMIYEDQGDMEKSLQFELIAAHLNPSDTEEWVRLAEMSLEQDNIKQAIFCYTKALKYEPTNVRYLWERSSLYEQMGDHKMAMDGYRRILNLLSPSDGERFMQLARDMAKSYYEANDVTSAINIIDEAFSKHQGLVSMEDVNIAAELYISNKQYDKALEIITDFSGIVLEKKTSEEGTSEENKAPENVTCTIPDGVPIDITVKLMVCLVHLNILEPLNPLLTTLVEQNPEDMGDLYLDVAEAFLDVGEYNSALPLLSALVCSERYNLAVVWLRHAECLKALGYMERAAESYGKVVDLAPLHLDARISLSTLQQQLGQPEKALEALEPMYDPDTLAQDANAAQQELKLLLHRSTLLFSQGKMYGYVDTLLTMLAMLLKVAMNRAQVCLISSSKSGERHLYLIKVSRDKISDSNDQESANCDAKAIFAVLTSVLTKDDWWNLLLKAIYSLCDLSRFQEAELLVDSSLEYYSFYDDRQKRKELEYFGLSAAILDKNFRKAYNYIRIMVMENVNKPQLWNIFNQVTMHSQDVRHHRFCLRLMLKNPENHALCVLNGHNAFVSGSFKHALGQYVQAFRTHPDEPLYSFCIGLTFIHMASQKYVLRRHALIVQGFSFLNRYLSLRGPCQESFYNLGRGLHQLGLIHLAIHYYQKALELPPLVVEGIELDQLDLRRDIAYNLSLIYQSSGNTGMAQTLLYTYCSI

Involved in RNA polymerase III-mediated transcription. Integral, tightly associated component of the DNA-binding TFIIIC2 subcomplex that directly binds tRNA and virus-associated RNA promoters.

Q9Y5Q9

P68424

TXH10_CYRSC

Huwentoxin-X

Cyriopagopus

MNMKILVLVAVLCLVVSTHAERHSKTDMEDMEDSPMIQERKCLPPGKPCYGATQKIPCCGVCSHNKCT

Reversibly blocks N-type calcium channels (Cav2.2/CACNA1B) in rat dorsal root ganglion cells (IC(50)=40 nM). Elicits no toxic symptoms in either vertebrates or invertebrates during a period of 48 hours post-injection, when it was assayed in vivo by direct injection into mice and cockroaches.

P68424

P58453

VARH_VIOAR

Varv peptide H

Viola

GLPVCGETCFGGTCNTPGCSCETWPVCSRN

Probably participates in a plant defense mechanism.

P58453

Q96NC0

ZMAT2_HUMAN

Zinc finger matrin-type protein 2

Homo

MASGSGTKNLDFRRKWDKDEYEKLAEKRLTEEREKKDGKPVQPVKRELLRHRDYKVDLESKLGKTIVITKTTPQSEMGGYYCNVCDCVVKDSINFLDHINGKKHQRNLGMSMRVERSTLDQVKKRFEVNKKKMEEKQKDYDFEERMKELREEEEKAKAYKKEKQKEKKRRAEEDLTFEEDDEMAAVMGFSGFGSTKKSY

Involved in pre-mRNA splicing as a component of the spliceosome.

Q96NC0

C5BCI2

THII_EDWI9

tRNA 4-thiouridine synthase

Edwardsiella

MKFIIKLFPEITIKSQSVRLRFIKILTGNIRNVLKPLVEDVAVTRHWDHIEVRAKEESRRDLVRDALTRIPGIHHILEVEDHPYTDMHDIFEQTLAMYREQLEEKTFCVRVKRRGKHTFTSIEVERYVGGGLNQNIPSARVRLNHPEVTVNLEIEDDRLLLVRGRFEGQGGYPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGSAHEIGVKQVAHYLWNRFGSSHRVRFVAIDFAPVVGEILEKVDDGQMGVVLKRMMVRAASRVAERYGIQALVTGEALGQVSSQTLTNLRLIDGVSDTLVLRPLIAHDKEHIIRLARNIGTEDFAKTMPEFCGVISKSPTVKAVKARIEAEEEHFDFAILDRVVDEAQTMDIRDIARQSEADVVEVETIESLAEGDVVLDIRAPDEQEAKPLQLADSEVICLPFYKLANAFGDLDQVRRYVLYCDRGVMSRLQALYLREQGYDNVRVYRP

Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.

C5BCI2

Q60493

ZN664_CAVPO

Zinc finger protein from organ of Corti

Cavia

MIYKCPMCREFFSERADLFMHQKVHTAEKPHKCDKCDKGFFHISELHIHWRDHTGEKVYKCDDCGKDFSTTTKLNRHKKIHTVEKPYKCYECGKAFNWSPHLQIHMRVHTGEKPYVCSECGRGFSNSSNLCMHQRVHTGEKPFKCEECGKAFRHTSSLCMHQRVHTGEKPYKCYECGKAFSQSSSLCIHQRVHTGEKPYRCCGCGKAFSQSSSLCIHQRVHTGEKPFKCDECGKAFSQSTSLCIHQRVHTKERNHLKISVI

May be involved in transcriptional regulation.

Q60493

P53061

ZIP2_YEAST

Zipping up meiotic chromosomes protein 2

Saccharomyces

MIIERWEVKLSKCNQNVGGYSVLSGNLKENIKLGRRAQKYLKELRNLQLKPLKIGGYENCGTINGEEYFLEVIHITSGRQKIDVAVGKTWNVTNIENDNKEELQYELFKEKLKVGKQDMLFFSWMKSLSVQLNAPLHQKMTEHGLADDNTRLEWFNIPLLRRSQYRKKVPYPSLRQMSSVLEVQCSTLTEEKLNFCVGFSDKPLSEWKPQIFEQTYNRYRLQRISPEKSFKYKSRCSKYNFKTSSQSWVVKVPEHDQQLNTFEKRYDELFDAQFNKLEFFKIRMKKLKKNKPIEKKNYKIWCLEKEDLKDLVWDPLKRICNHSRYAIFEHVTINREAYSIKPLRLTFQKLDSGSLDLIDNQKKTFGSIKLAMSMPDVKKTENQSIEESERHDETAIETQEFDENDCLSSKADINTSLAPQKRSFIDNELMSMLVTKKKIKKDKDVSDTGISSTSYLINSGTYANSHIEIPTSNSVYNGKEDCSFNNYSVKHSILEEDIENKCIAVNENKVIENQKVIQSLCKNSHLDLIEQSYFGECDFIINHSTCVYKIQASRFMQLRNNGSLHYDKAVNDLLTEFQRVIIIVEFSEIIQDVDPDLFWKIKLYLLNSRVDVFFIHETTDFFIDWMKYFIARWAFSYNDEKEKNIANADILLDLGFNILLVRKIFQTYSLEEFFMAIIKEESKAVKMLTVSQMTRLKKLLTLEW

Required for initiation of meiotic chromosome synapsis. Involved in synaptonemal complex formation, a structure that tethers a pair of homologous chromosomes along their lengths and plays a central role in recombination and homolog segregation during meiosis. Required for the normal localization of MSH4 to chromosomes.

P53061

A7E305

ZSWM8_BOVIN

Zinc finger SWIM domain-containing protein 8

Bos

MELMFAEWEDGERFSFEDSDRFEEDSLCSFISEAESLCQNWRGWRKQSAGPNSPTGGGGGGGSGGTRMRDGLVIPLVELSAKQVAFHIPFEVVEKVYPPVPEQLQLRIAFWSFPENEEDIRLYSCLANGSADEFQRGDQLFRMRAVKDPLQIGFHLSATVVPPQMVPPKGAYNVAVMFDRCRVTSCSCTCGAGAKWCTHVVALCLFRIHNASAVCLRAPVSESLSRLQRDQLQKFAQYLISELPQQILPTAQRLLDELLSSQSTAINTVCGAPDPTAGPSASDQSTWYLDESTLTDNIKKTLHKFCGPSPVVFSDVNSMYLSSTEPPAAAEWACLLRPLRGREPEGVWNLLSIVREMFKRRDSNAAPLLEILTVELAQDLLANPPDLKVEPPPAKGKKNKVSTSRQTWVATNTLTKAAFLLTVLSERPEHHNLAFRVGMFALELQRPPASTKALEVKLAYQESEVATLLKKIPLGPSEMSTVRCRAEELREGTLCDYRPVLPLMLASFIFDVLCAPVVSPTGSRPPSRNWNNEMPGDEELGFEAAVAALGMKTTVSEAEHPLLCEGTRREKGDLALALMITYKDDQARLKKILDKLLDRESQTHKPQTLSSFYSSSRPATASQRSPSKHGGPSAPGALQPLTSGSAGPAQPGSVAGAGPGPTEGFTEKNVPESSPHSPCEGLPPEAALTPRPEGKVPSRLALGSRGGYNGRGWGSPGRPKKKHTGMASIDSSAPETTSDSSPTLSRRPLRGGWAPTSWGRGQDSDSISSSSSDSLGSSSSSGSRRASASGGARAKTVEVGRYKGRRPESHAPHVPNQPSEAAAHFYFELAKTVLIKAGGNSSTSIFTHPSSSGGHQGPHRNLHLCAFEIGLYALGLHNFVSPNWLSRTYSSHVSWITGQAMEIGSAALTILVECWDGHLTPPEVASLADRASRARDSNMVRAAAELALSCLPHAHALNPNEIQRALVQCKEQDNLMLEKACMAVEEAAKGGGVYPEVLFEVAHQWFWLYEQTAGGSSTAREGATSCSASGIRAAGEAGRGLPEGRGGPGTEPVTVAAAAVTAATVVPVISVGSSLYPGPGLGHGHSPGLHPYTALQPHLPCSPQYLTHPAHPAHPMPHMPRPAVFPVASSAYPQGVHPAFLGAQYPYSVTPPSLAATAVSFPVPSMAPITVHPYHTEPGLPLPTSVALSSVHPASTFPAIQGASLPALTTQPSPLVSGGFPPPEEETHSQPVNPHSLHHLHAAYRVGMLALEMLGRRAHNDHPNNFSRSPPYTDDVKWLLGLAAKLGVNYVHQFCVGAAKGVLSPFVLQEIVMETLQRLSPAHAHNHLRAPAFHQLVQRCQQAYMQYIHHRLIHLTPADYDDFVNAIRSARSAFCLTPMGMMQFNDILQNLKRSKQTKELWQRVSLEMTTFSP

Substrate recognition component of a SCF-like E3 ubiquitin-protein ligase complex that promotes target-directed microRNA degradation (TDMD), a process that mediates degradation of microRNAs (miRNAs). The SCF-like E3 ubiquitin-protein ligase complex acts by catalyzing ubiquitination and subsequent degradation of AGO proteins (AGO1, AGO2, AGO3 and/or AGO4), thereby exposing miRNAs for degradation. Specifically recognizes and binds AGO proteins when they are engaged with a TDMD target. May also act as a regulator of axon guidance: specifically recognizes misfolded ROBO3 and promotes its ubiquitination and subsequent degradation.

A7E305

O32583

THIS_ECOLI

Thiamine biosynthesis protein ThiS

Escherichia

MQILFNDQAMQCAAGQTVHELLEQLDQRQAGAALAINQQIVPREQWAQHIVQDGDQILLFQVIAGG

Is the sulfur donor in the synthesis of the thiazole phosphate moiety of thiamine phosphate.

O32583

Q8A7D1

TILS_BACTN

tRNA(Ile)-lysidine synthetase

Bacteroides

MIQQRVIRYIEKEHLFLPDDKLLVALSGGADSVALLRVLHTAGYQCEAAHCNFHLRGEESNRDERFVRQLCQKYGIRLHITDFNTTQYATEKRISIEMAARELRYNWFEKIKEECGAHVIAVAHHQDDSVETMLFNLIRGTGITGLLGIRPRNGAIVRPLLCINREEIIRYLQQIGQDFVTDSTNLEDEYTRNKIRLNLLPLMQEINPSVKNSLIETSNHLNDVATIYNKVIDEAKTRIITPEGIRIDALLDEPAPEAFLFETLHPLGFNSAQIKDIANSLHGQPGKQFVSKEWRVIKDRNLLLLETIRPEDESTLPYQLIKEEREFTPDFRIPREKETACFDADKLNEEIHCRKWQAGDTFIPFGMTGKKKISDYLTDRKFSISQKERQWVLCCGERIAWLIGERTDNRFRIDETTKRVIIYKIV

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.

Q8A7D1

Q9KJF6

XERC_STAAU

Tyrosine recombinase XerC

Staphylococcus

MNHIQEAFLNTLKVERNFSEHTLKSYQDDLIQFNQFLEQEHLQLNTFEYRDARNYLSYLYLNHLKRTSVSRKISTLRTLYEYWMTLDENIINPFVHLVHPKKEKYLPQFSLEEEMEALFTTVEKDTSKNLRDRVILELLYATGIRVSELVNIKKQDIDFYANGVTVLGKGSKERFVPFGAYCRQSIENYLEHFKPIQSCNHDFLILNMKGEAITERGVRYVLNDIVKRTAGVSEIHPHKLRHTFATHLLNQGADLRTVQSLLGHVNLSTTGKYTHVSNQQLRKVYLNAHPRAKKENET

Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.

Q9KJF6

Q4A0A8

TARI_STAS1

Ribitol-5-phosphate cytidylyltransferase

Staphylococcus

MIYAGILAGGIGSRMGNVPLPKQFLDLDGKPILVHTVEKFLLTSEFDKIFIATPQKWISHTKDTLRKHHITDDRIEVVQGGSDRNETIMNIISAAEKENGISDDDVIITHDAVRPFLTRRIIKENIESVLKYGAVDTVITATDTIITSADGDSIQSIPVRSEMYQGQTPQSFNVNLLRNSYNDLSDEDKQIMTDACKILVVAGKQVKLVMGELYNIKITTPYDLKVANSIIKGGMLSD

Catalyzes the transfer of the cytidylyl group of CTP to D-ribitol 5-phosphate.

Q4A0A8

Q9P7B4

YI13_SCHPO

L-allo-threonine dehydrogenase

Schizosaccharomyces

MSRLDGKTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPKEFADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVYKNSEPLTPEDIAEVILFALTRRENVVIADTLVFPSHQGGANHVYRKQA

NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L-allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate.

Q9P7B4

P15120

UROK_CHICK

Urokinase-type plasminogen activator chain B

Gallus

MKLIIFLTVTLCTLVTGLDSVYIRQYYKLSHKHRPQHRECQCLNGGTCITYRFFSQIKRCLCPEGYGGLHCEIDTNSICYSGNGEDYRGMAEDPGCLYWDHPSVIRWGDYHADLKNALQLGLGKHNYCRNPNGRSRPWCYTKRRYSIQETPCSTIEKCERTCGQRSFSKYFKIVGGSQAEVETQPWIAGIFQNIMGTDQFLCGGSLIDPCWVLTAAHCFYNPTKKQPNKSVYKVFLGKSILNTNDEHEQVFMVDEIISHPDFTDHTGGNDNDIALIRIRTASGQCAVESNYVRTVCLPEKNLNLYDNTWCEIAGYGKQNSYDIYYAQRLMSATVNLISQDDCKNKYYDSTRVTDNMVCAGDPLWETDACKGDSGGPMVCEHNGRMTLYGIVSWGDGCAKKNKPGVYTRVTRYLNWIDSNMNAVFTKSRSFREPK

Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.

P15120

B5EFL1

UBIE_CITBB

Demethylmenaquinone methyltransferase

Citrifermentans

MYALSEKGERIRAMFGSIAPRYDLLNRLLSLGIDRRWRRFAVKKIGLNGSGRVLDVATGTGDVALEIASQTPASVSIVGIDFTPEMIELGRVKVKDSRHCGRITLQVAPCEEIPFDDGSFDAATISFGIRNVVDRIKGLAEMHRVLKNDGKIVILEFSTPTLPVFKDLYHFYFLKVLPKIGGAFSRFSAYQYLPDSVLEFPSREVFKGMMTQVGFKDVRHFDLTGGIATVYVGTK

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).

B5EFL1

Q89UF8

UREF_BRADU

Urease accessory protein UreF

Bradyrhizobium

MLMTTNEPVNAGDLAAREAAALYRLMTWLSPAFPVGGFSYSSGIEWAVEAGDITDTATLADWLDTMLGDGSGFCDATFLVQAYRATEAGEETSLRDIAELASAFVPSRERQLETTSQGRAFIDIARAAWDAEGLDAMVAACRTPLVYPVAVGVVAAMHGVPLAPTLHAFLHAVVSNWISAASRLIPLGQTDSQRVLVRLEAAVAATATRALSATLDDLGSATFRADLASLRHETQYTRLFRS

Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.

Q89UF8

Q5E2R0

YACG_ALIF1

DNA gyrase inhibitor YacG

Aliivibrio

MTKPTTEQPTTVKCPTCQSAVIWNAESPFRPFCSKKCQMIDFGEWADEEKSIPGAPDMSDSDGWSEDQY

Inhibits all the catalytic activities of DNA gyrase by preventing its interaction with DNA. Acts by binding directly to the C-terminal domain of GyrB, which probably disrupts DNA binding by the gyrase.

Q5E2R0

C5BHG1

TSAD_EDWI9

tRNA threonylcarbamoyladenosine biosynthesis protein TsaD

Edwardsiella

MRILGIETSCDETGIAIYDDEKGILANQLYSQIKLHADYGGVVPELASRDHVRKTVPLIQAALREADLTPADLDGVAYTAGPGLVGALLVGATVGRSLAFAWGVPAVPVHHMEGHLLAPMLEENPPAFPFVALLVSGGHTQLISVTGIGEYRLLGESIDDAAGEAFDKTAKLLGLDYPGGPVLSRMAQQGVPGRFVFPRPMTDRPGLDLSFSGLKTFAANTIHANGDDAQTRADIARAFEDAVVDTLAIKCRRALDQTGFQRLVMAGGVSANRALRGRLAQMMQQRGGAVFYARPEFCTDNGAMIAYAGMVRLKSGVDADLSISVRPRWPLAELPPVAARS

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.

C5BHG1

Q9A6Q5

THIC_CAUVC

Thiamine biosynthesis protein ThiC

Caulobacter

MNIQSTIKAVAETISTGPIPGSRKVYQAGELFPELRVPFREVAVHPSANEPPVTIYDPSGPYSDPAIQIDIEKGLPRTREALVVARGDVEEVADPRQVKPEDNGFAQGKHLAPEFPDTGRKIYRAKPGKLVTQLEYARAGIITAEMEYVAIRENLRREQDRPCVRDGEDFGASIPDFVTPEFVRQEIARGRAIIPANINHGELEPMAIGRNFLVKINANIGNSAVLSTVADEVDKLVWATRWGADTVMDLSTGRNIHNIRDWIIRNSSVPIGTVPIYQALEKVNGVAEDLNWEVFRDTLIEQCEQGVDYFTIHAGVRLPFIPMTAKRVTGIVSRGGSIMAKWCLAHHKENFLYERFDEICEIMRAYDVSFSLGDGLRPGSTADANDEAQFSELRTLGELTKVAWKHGVQVMIEGPGHVAMHKIKANMDEQLKHCHEAPFYTLGPLTTDIAPGYDHITSAIGAAMIGWFGTAMLCYVTPKEHLGLPDRDDVKTGVITYKLAAHAADLAKGHPGAAMWDDAISRARFEFRWEDQFNLGLDPETARKFHDETLPKEAHKTAHFCSMCGPKFCSMKISQEVRDFAAGKAPNSAELGMAEMSEKFREQGSEIYLKTE

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.

Q9A6Q5

Q91507

VSP1_PROMU

Tm-VIG

Protobothrops

MVLIRVLANLLILQLSYAQKSSELVIGGDECNINEHPFLVLVYYDDYQCGGTLLNEEWVLTAAHCNGKDMEIYLGVHSKKVPNKDVQRRVPKEKFFCDSSKTYTKWNKDIMLIRLDRPVRKSAHIAPLSLPSSPPSVGSVCRVMGWGTITSPQETYPDVPHCANINLLDYEVCRAAYAGLPATSRTLCAGILEGGKDSCVGDSGGPLICNGQFQGIVSWGGDPCAQPREPGVCTNVFDHLDWIKGIIAGNTDVTCPL

Snake venom serine protease with strong beta-fibrinogenolytic activities, angiotensin I (AGT)-degrading activities and strong kallikrein-like activities in vitro, releasing bradykinin from kininogen (KNG1). Intravenous injection strongly lowers blood pressure in experimental rats, which may be explained by the action on angiotensin I and kininogen.

Q91507

A3N0Y0

YCIB_ACTP2

Inner membrane-spanning protein YciB

Actinobacillus

MKQLLEFIPLILFFTVYKLYGVQQAAITLVIATVIQLIVLKVLYKKIEKSQWIMGIFAVFFGILTAYFNDLNFLKWKVTIINGLFAAVLLVSQFVFKKPIIQMLLGKELKLPTNVWNRLNLGWAGFFIICMLLNIVISYYFSDDVWATFKTFGFTGLSLIAAIATGVYLYPHLKNVENTNEQA

Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.

A3N0Y0

A4VGU2

XPT_PSEU5

Xanthine phosphoribosyltransferase

Pseudomonas

MEQLKDKIRSHGIVLSDRVLKVDAFLNHQIDPVLMQAIGREFARRFRDDGITKIVTIEASGIAPAVMAGLELGVPVIFARKHQSLTLHDNLLTATVYSFTKQVESTIAVSTQHLSANDRVLIIDDFLANGKAAKGLISIINQAGASIAGLGIVIEKSFQTGRKELEEAGYRVESLARVASLADGAVQFID

Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis.

A4VGU2

Q9BZM4

ULBP3_HUMAN

Retinoic acid early transcript 1N

Homo

MAAAASPAILPRLAILPYLLFDWSGTGRADAHSLWYNFTIIHLPRHGQQWCEVQSQVDQKNFLSYDCGSDKVLSMGHLEEQLYATDAWGKQLEMLREVGQRLRLELADTELEDFTPSGPLTLQVRMSCECEADGYIRGSWQFSFDGRKFLLFDSNNRKWTVVHAGARRMKEKWEKDSGLTTFFKMVSMRDCKSWLRDFLMHRKKRLEPTAPPTMAPGLAQPKAIATTLSPWSFLIILCFILPGI

Binds and activates the KLRK1/NKG2D receptor, mediating natural killer cell cytotoxicity.

Q9BZM4

Q9Y3C4

TPRKB_HUMAN

TP53RK-binding protein

Homo

MQLTHQLDLFPECRVTLLLFKDVKNAGDLRRKAMEGTIDGSLINPTVIVDPFQILVAANKAVHLYKLGKMKTRTLSTEIIFNLSPNNNISEALKKFGISANDTSILIVYIEEGEKQINQEYLISQVEGHQVSLKNLPEIMNITEVKKIYKLSSQEESIGTLLDAIICRMSTKDVL

Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine . The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37 . TPRKB acts as an allosteric effector that regulates the t(6)A activity of the complex. TPRKB is not required for tRNA modification .

Q9Y3C4

Q0VQH0

UPPP_ALCBS

Undecaprenyl pyrophosphate phosphatase

Alcanivorax

MDWFQALVLALIQGLTEFLPISSSAHLILPSQILGWPDQGLAFDVAVHLGTLLAVMMYYRRDLIAMVGGAGLAVQQRRMNDDLKLGLLVALATIPAVVFGFLGDDFIERELRSALVIAITTLVFGALLWASDAFGKREFSLARLGVAGAIFIGLAQALALIPGTSRSGITITAALALGYRREDAARFSFLLSIPVILGAGLLKTKDLIEQQVVVDWGMMALGVIVSAVTAYLTIVFFIRLLERVGMLPFVVYRLILGVALLFWLA

Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.

Q0VQH0

Q9I068

TSI4_PSEAE

Immune protein Tsi4

Pseudomonas

MTTSSGSRIGGLLHASLFSLLGLGLLLAGGFKTVERYHFLRTAQEAQGTVSALNAGGSHPQIDFTSVSGERISYPQGGFIFGYQVGEPVRVLYEAGRPAASAIVDDAGALWGTGAFLCGFGALFGIVGFRGLLGLRSSQPTSKGH

Immunity protein that plays a role in preventing early activation of toxin Tse4.

Q9I068

B1ICC8

VATB_STRPI

V-ATPase subunit B

Streptococcus

MSVIKEYRTASEVVGPLMIVEQVNNVSYNELVEIQLHNGEIRRGQVLEIHEDKAMVQLFEGSSGINLEKSKIRFAGHALELAVSEDMVGRIFNGMGKPIDGGPDLIPEKYLDIDGQAINPVSRDYPDEFIQTGISSIDHLNTLVRGQKLPVFSGSGLPHNELAAQIARQATVLNSDENFAVVFAAMGITFEEAEFFMEELRKTGAIDRSVLFMNLANDPAIERIATPRIALTAAEYLAFEKDMHVLVIMTDMTNYCEALREVSAARREVPGRRGYPGYLYTNLSTLYERAGRLVGKKGSVTQIPILTMPEDDITHPIPDLTGYITEGQIILSHELYNQGYRPPINVLPSLSRLKDKGSGEGKTRGDHAPTMNQLFAAYAQGKKVEELAVVLGESALSDVDKLYVKFTKRFEEEYINQGFYKNRNIEDTLNLGWELLSILPRTELKRIKDDLLDKYLPLVEV

Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit.

B1ICC8

Q05741

TRXB_STRCL

Thioredoxin reductase

Streptomyces

MSDVRNVIIIGSGPAGYTAALYTARASLQPLVFEGAVTAGGALMNTTDVENFPGFRDGIMGPDLMDNMRAQAERFGAELIPDDVVSVDLTGDIKTVTDSAGTVHRAKAVIVTTGSQHRKLGLPREDALSGRGVSWCATCDGFFFKDQDIVVVGGGDTAMEEATFLSRFAKSVTIVHRRDSLRASKAMQDRAFADPKISFAWNSEVATIHGEQKLTGLTLRDTKTGETRELAATGLFIAVGHDPRTELFKGQLDLDDEGYLKVASPSTRTNLTGVFAAGDVVDHTYRQAITAAGTGCSAALDAERYLAALADSEQIAEPAPAV

Component of the thioredoxin-thioredoxin reductase system which may be involved in biosynthesis of penicillins and cephalosporins and may be important in determining the thiol-disulfide redox balance.

Q05741

Q4XFJ8

TCTP_PLACH

Translationally-controlled tumor protein homolog

Plasmodium (Vinckeia)

MKVYKDIFTNDEVCSDSYAQEDPFGNPEFREIAFEVKSNKRIKGNDDYGIADNSEDAVEGMGADVEHVIDIVDSFQLTSTSLSKKEYSAYVKNFMQRILKHLEEKKPDRVEIFKTKAQPLIKHILTNFDDFEFYMGESLDMEAGLIYSYYKGEEITPRFVYISDGLFEEKY

Involved in calcium binding and microtubule stabilization.

Q4XFJ8

P62722

VIRG_AGRT9

Regulatory protein VirG

Agrobacterium tumefaciens complex

MIVHPSRENFSSAVNKGSDFRLKGEPLKHVLLVDDDVAMRHLIIEYLTIHAFKVTAVADSTQFTRVLSSATVDVVVVDLNLGREDGLEIVRNLAAKSDIPIIIISGDRLEETDKVVALELGASDFIAKPFSIREFLARIRVALRVRPNVVRSKDRRSFCFTDWTLNLRQRRLMSEAGGEVKLTAGEFNLLLAFLEKPRDVLSREQLLIASRVRDEEVYDRSIDVLILRLRRKLEADPSSPQLIKTARGAGYFFDADVQVSHGGTMAA

VirG is required for the positive regulation of at least two vir loci encoded by the Ti plasmid of A.tumefaciens.

P62722

A5W1B2

UVRC_PSEP1

Excinuclease ABC subunit C

Pseudomonas

MSQVFDASAFLATCSGRPGVYRMFDGEARLLYVGKAKNLKKRLASYFRKAGLAPKTAALVARIAQVETTITANETEALLLEQNLIKEWRPPYNILLRDDKSYPYVFLSDGEFPRLGIHRGAKKAKGRYFGPYPSAGAIRESLSLLQKAFSVRQCEDSYYANRTRPCLQYQIKRCKGPCTDLVTAEEYAEDVRHSVMFLEGRSQQLGNELNAEMEKAAMALDFEKAAELRDQIALLRRVQDQQYIEGGSGDVDVIAAFVNPGGACVHLISVRGGRVLGSKNFFPQVGIEEEVAEVMAAFLSQYYLGNAERELPGELIVNVVHEDFNAITEALHTLRGRELTISHRVRGTRARWQQLAVTNAEQALNARLANRQHMAARFEALAEVLGLDEVPQRLECYDISHSSGEATVASCVVFGPEGPIKSDYRRFNIEGVTAGDDYAAMHQALTRRYGRIKDGEGKLPDVLLVDGGKGQLNMARDVMQALGFTDLTLLGVAKGVTRKAGFETLYLNDVHHEFTLKGDSSALHLIQQIRDEAHRFAITGHRARRGKARRVSSLEDVAGVGPKRRRDLLKHFGGLQELNRASIDEIAKAPGISKKLAESIYASLHSE

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.

A5W1B2

C5BB99

TDH_EDWI9

L-threonine 3-dehydrogenase

Edwardsiella

MKALSKLKAEEGIWMTDVPLPALGHNDIMIKIRKAAICGTDVHIYNWDTWSQKTIPVPMVVGHEYVGEVVAVGQEVRGFRIGDRVSGEGHITCGHCRNCRAGRTHLCRNTIGVGVNRQGAFAEYLVIPAFNAFKIPDNIPDALAAIFDPFGNAVHTALSFDLVGEDVLVSGAGPIGIMAAAVCRHVGARHVVITDVNDYRLDLARKMGVTRAVNVSRESLPEVMQALGMSEGFDVGLEMSGAPPAFHTMLDTMNHGGKIAMLGIPPGDMAIDWNQVIFKGLLIKGIYGREMFETWYKMAALIQSGLDLTPIITHQYAIDDFQKGFDVMRSGHSGKVILNWS

Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.

C5BB99

Q5KWH6

UVRC_GEOKA

Excinuclease ABC subunit C

Geobacillus thermoleovorans group

MNERLKEKLAVLPEQPGCYLMKDKHGTVIYVGKAKSLKARVRSYFTGTHDGKTQRLVEEIADFEYIVTSSNAEALILEMNLIKKHDPKYNVMLKDDKSYPFIKITAEKHPRLLITRKVKKDGGKYFGPYPNVQAANETKKLLDRLYPLRKCSTLPSRACLYYHMGQCLAPCVHPVSDEQNKAMVEQIVRFLNGGYEDVKRELAEKMHEAAETLEFERAKEYRDQIAAIEMTMEKQKMMLNDFIDRDVFGYAYDKGWMCVQVFFLRQGKLIERDVSIFPLYQDPDEEMLTFLGQFYAKAHHLKPKEVVLPSDIDGELARELLGVAVVQPKKGKKKELVELASKNAAIALKEKFYFIERDEERTIKAVERLGERLGIPAPRRIEAFDNSNIYGADPVSALVVFLDGKPAKKEYRKYKVKTVAGPNDYETMREVVRRRYTRVLKEGLPLPDLIIIDGGKGHLSAVRDVLENELGLDVPLAGLAKDEKHRTSELLAGDPPDVVPLDRQSQEFYLLQRIQDEVHRFAVMFHRKTRQKTMFHSVLDDIPGVGEKRKKALLNYFGSVKKMKEATVEELQRANIPRAVAEKIYEKLHE

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.

Q5KWH6

Q6UXN9

WDR82_HUMAN

WD repeat-containing protein 82

Homo

MKLTDSVLRSFRVAKVFRENSDKINCFDFSPNGETVISSSDDDSIVLYDCQEGKPKRTLYSKKYGVDLIRYTHAANTVVYSSNKIDDTIRYLSLHDNKYIRYFPGHSKRVVALSMSPVDDTFISGSLDKTIRLWDLRSPNCQGLMHLQGKPVCSFDPEGLIFAAGVNSEMVKLYDLRSFDKGPFATFKMQYDRTCEWTGLKFSNDGKLILISTNGSFIRLIDAFKGVVMHTFGGYANSKAVTLEASFTPDSQFIMIGSEDGKIHVWNGESGIKVAVLDGKHTGPITCLQFNPKFMTFASACSNMAFWLPTIDD

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) . Component of PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase . Together with ZC3H4, but independently of the SET1 complex, part of a transcription termination checkpoint that promotes transcription termination of long non-coding RNAs (lncRNAs) . The transcription termination checkpoint is activated by the inefficiently spliced first exon of lncRNAs and promotes transcription termination of lncRNAs and their subsequent degradation by the exosome .

Q6UXN9

Q31ZU8

YCIB_SHIBS

Inner membrane-spanning protein YciB

Shigella

MKQFLDFLPLVVFFAFYKIYDIYAATAALIVATAIVLIYSWVRFRKVEKMALITFVLVVVFGGLTLFFHNDEFIKWKVTVIYALFAGALLVSQWVMKKPLIQRMLSKELTLPQPVWSKLNLAWAVFFILCGLANIYIAFWLPQNIWVNFKVFGLTALTLIFTLLSGIYIYRHMPQEDKS

Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.

Q31ZU8

A3MM33

UVRC_BURM7

Excinuclease ABC subunit C

pseudomallei group

MTSPDAPESRFEPKPILAQLPHLPGVYRYYDVQDAVLYVGKARDLKKRVSSYFTKTQLSPRIAMMITRIARIETTVTRSEAEALLLENNLIKALAPRYNILFRDDKSYPYLKLTGHRFPRMAYYRGAVDKKNQYFGPFPSAWAVRESIQILQRVFQLRTCEDSVFNNRTRPCLLHQIGRCSAPCVGAIGEEDYARDVDNASRFLLGRQGEVMGELERKMHAFAAELKFEQAAAVRNQMSSLAKVLHQQAIDVGGDSDVDILAVVAQGGRVCVNLAMVRGGRHLGDKAYFPAHVETALALAGDIEALAGEGAGDGVQAAAQPAQAPLATDADATDAAATEAKTVTAAAAARAGARTAQAAGARAAASAEGDVERRAEGETHARADAREAAALPDGAAAAQEADADVDAAPLETEVLEAFIAQHYLGNRVPPVLVVSHAPANRELIDLLVEQAGHKVAVVRQPQGQKRAWLTMAEQNARLALARLLSEQGSQQARTRSLADVLGYESDDLAQLRIECFDISHTMGEATQASCVVYHHHRMQSSEYRRYNIAGITPGDDYAAMRQVLTRRYEKMVEEAAAEASADEAAGIDGNAVHAAASAGRLPNVVLIDGGRGQVEIARQVFSELGLDISMLVGVAKGEGRKVGLETLIFADGRAPLELGKESAALMLVAQIRDEAHRFAITGMRAKRAKTRQTSRLEELEGVGAKRRQRLLARFGGLRGVVAASVDELASVEGISRALAEQIYRQLH

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.

A3MM33

Q9WZ09

TRPB2_THEMA

Tryptophan synthase beta chain 2

Thermotoga

MRIVVNLKPEEIPKHWYNVLADLPFKLDPPLDPETKQPISPEKLSVIFPMSLIEQEVSEERFIEIPEPVLKEYAVYRPTPLIRATFLEEYLQTPARIYYKYEGVSPTGSHKPNTAIAQAYYNKIEGVKRLVTETGAGQWGSALSYAGAKFGLEVKVFMVKVSYQQKPMRKYMMNLFGGKVTPSPSEETNFGRKILSEDPDNPGSLGIAISEALEVAVSDPNTKYSLGSVLNHVLLHQTVIGLEIKKQLELIGEKPDILLGCHGGGSNFGGTILPFVPDKLSGRDIRFVACEPAACPSLTKGNYDYDFGDTAGLTPLLKMYTLGKDFIPPKIHAGGLRYHGSAPIIARLVKEGLVEAQAFDQDETFEAAKIFAKLEGIIPAPESAHAIAGAIREAKKAKEEGKERVIVFTLSGHGLLDLTAYV

The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.

Q9WZ09

E2AIS8

TACHY_CAMFO

Tachykinin-related peptide 4

Camponotus

MQCDFRVHQDARLARVYYFTEVWWMFIFKFLEPKMLINSVLFLAIWSSSFAEESSSSDATSNKRAAMGFQDMRGNKNLIPTSLEHNKLSKRTLMDFQDNKDSNAPDIEDNLSHEFEKRAPMGFQGMRGKKGYLTPDFEDSYFRDEKRAPMGFQGMRGKKVVSDDDYYKRAPMGFQGMRGKKSLEEVLGEIEKKAAMDYYDTRDKKTYVFEYPEDYEKRLLASIRGKLKEFPMEWEKRAPMGFQGMRGKKSLLDEIEELEKRTIMGFQGMRGKKNALENYIDYYLDPDMDFDKRAPMGFQGMRGKKDSDKRAPMGFQGMRGKRNTGQRFDTGINFNIRSSNEYQGTNNRRNALASCQLEKRSPFRYFEMRGKKNPRWELRGMFVGVRGKKWATAPYEDDSPFISVFDNTERIGVDGDSPAILGNSIS

Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles.

E2AIS8

E0ZS45

URED_ORYSI

Urease accessory protein D

Oryza sativa

MEAEAAMAAAAAATGAVRVEKVRGRSAVTRCFAKYPLKLIAPSKAGRASSGAAWLYAITYGGGIVSGDIISCTVAVGDGCAAAMTTQASTKVYKAVDSKCSEQVLEARVGEDALFALIPDPVTCFSMARYHQKQVFHVFPNSNLVVVDWFTSGRYESGEKWNFSFYKSINHILLEDQPLFIDSVLLEQSSNFSIADRMQEYNVVAMVILLGPKLKHIQDQMQDEVKKMMSVQLRPPTSAGGRYSTRSQPLHPQRPPIIASCSPFGRMGTGMVARITAVSTESVYSFLRHHLAALEPFLGACPYPAS

Required for the maturation and activation of urease via the functional incorporation of the urease nickel metallocenter.

E0ZS45