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
|
|---|---|---|---|---|---|---|
B0XPZ9 | YPI1_ASPFC | Type 1 phosphatases regulator ypi1 | Aspergillus subgen. Fumigati | MSRTRQVPSNTASSSHIQLLSPAVPQENHSTVRISGTLRLRAENDSIATDHIEGARPGRHIRWTEDVVDNEGLGKKSSKVCCIYHKPRPVGESSSESDDSTSSSSEPESDNDVDCRDSTGRAESHEQNAQDASQSPSNRSLNRGRTPSYTKRHAKRNGKRKPSPNAYEKMPKVKGQPRKTGM | Regulator of type 1 phosphatases which maintains protein phosphatase activity under strict control. | B0XPZ9 |
F1QZ15 | TPRKB_DANRE | TP53RK-binding protein | Danio | MYLTQDLELFHEYTVTQLLFKDVKNATELRKMAVNGEIKGALINPSMVVDAFQILVATNKAVHLHKIGKMKTRSLYSEIIFNLSPTNNISEAFKRFGISDSDTAVHIVLVHNKEETLNIDDIISKVDGQQIDVGQVSEMTDTAKIKKLYKITPQEDKCGTLLDAVVCRMAIKDVA | 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. | F1QZ15 |
Q3MIF4 | XYLB_RAT | Xylulose kinase | Rattus | MAERAGRRCCLGWDFSTQQVKVVAVDAELNVFYEDSVHFDRDLPEFGTQGGVHVHKDRLTVTSPVLMWVQALDLILEKMKASGFDFSQVLALSGAGQQHGSVYWKTGASLALSSLSPALLLHQQLQACFSVSDCPIWMDSSTTAQCHQLEAAVGGAQALSCLTGSRAYERFTGNQISKIFQKNPEAYSNSERISLVSSFAASLFLGRYSPIDYSDGSGMNLLQIQEKVWSQACLDACAPHLKEKLGSPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMRLEEGDVAVSLGTSDTLFLWLQKPMPALEGHIFCNPVDARQYMALLCFKNGSLMREKIRDESASCSWNKFSKALQSTEMGNNGNLGFYFDVMEITPEIIGCHRFNADNMEVSAFPGDVEIRALVEGQFMAKRIHAEGLGYRIMPKTKILATGGASHNKDILQVLADVFGAPVYVIDTTSSACVGSAYRAFHGLAGGTGVAFSEVVKSAPQPSLAATPNPGASQVYAALLPRYAELEQRILSKARGPLE | Phosphorylates D-xylulose to produce D-xylulose 5-phosphate, a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. | Q3MIF4 |
Q15696 | U2AFM_HUMAN | U2AF35-related protein | Homo | MAAPEKMTFPEKPSHKKYRAALKKEKRKKRRQELARLRDSGLSQKEEEEDTFIEEQQLEEEKLLERERQRLHEEWLLREQKAQEEFRIKKEKEEAAKKRQEEQERKLKEQWEEQQRKEREEEEQKRQEKKEKEEALQKMLDQAENELENGTTWQNPEPPVDFRVMEKDRANCPFYSKTGACRFGDRCSRKHNFPTSSPTLLIKSMFTTFGMEQCRRDDYDPDASLEYSEEETYQQFLDFYEDVLPEFKNVGKVIQFKVSCNLEPHLRGNVYVQYQSEEECQAALSLFNGRWYAGRQLQCEFCPVTRWKMAICGLFEIQQCPRGKHCNFLHVFRNPNNEFWEANRDIYLSPDRTGSSFGKNSERRERMGHHDDYYSRLRGRRNPSPDHSYKRNGESERKSSRHRGKKSHKRTSKSRERHNSRSRGRNRDRSRDRSRGRGSRSRSRSRSRRSRRSRSQSSSRSRSRGRRRSGNRDRTVQSPKSK | Pre-mRNA-binding protein required for splicing of both U2- and U12-type introns. Selectively interacts with the 3'-splice site of U2- and U12-type pre-mRNAs and promotes different steps in U2 and U12 intron splicing. Recruited to U12 pre-mRNAs in an ATP-dependent manner and is required for assembly of the prespliceosome, a precursor to other spliceosomal complexes. For U2-type introns, it is selectively and specifically required for the second step of splicing. | Q15696 |
Q5ZY91 | TRMB_LEGPH | tRNA(m7G46)-methyltransferase | Legionella | MMQRKIKSYVLRAGRISNRQQQGLDLWLEDYELKFDSPTPWNFAKEFGRHDADTIVEIGFGMGTSLFAMAMNNPQCNYLGIEVHKAGVGSLVADLHEYQISNVRVVVHDAVEVLQTKIPENSLAGVQIFFPDPWHKKRHHKRRLIQSEFIQMLVKKIRPSGFIHCATDWEDYAEHILNVLSSESALFNQQKEGGYSPRPDSRPLTKFELRGERLGHGVWDLVFIKK | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | Q5ZY91 |
B0R686 | TRUB_HALS3 | tRNA-uridine isomerase | Halobacterium | MGIRPPPGERSPAAVLSFGVVNLDKPPGPSAHQVSAWIRDLVGVEKAAHAGTLDPKVTGCLPVLTGTATRIAPALLEGFKEYVAVLELHDDPPRILPDVIEAFTGEIYQKPPKKSAVARRLRTRTVYDLDVLDVDGRQVLLRIRCESGTYIRKLCHDIGRALGTNAHMGHLRRSATTPFDDTDLVTLHDLADAVAWLRDTDDTEPPDAPADALRAAVQPAERALTHLPRLTIADSAAHEVATGAPVYAPGVIDTTALPTPPADGALVACYTAGGTAVCLGRLVGDPDADAGVVVALERVLV | Could be responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | B0R686 |
A6LSF8 | YQGF_CLOB8 | Putative pre-16S rRNA nuclease | Clostridium | MRILGLDLGSKTIGVAVSDPLGFTAQGLTTVRRTNKEKDIAEIKKFCDEYDAKVIVIGLPKNMNGTIGPSGEIAMAFGKVIEEELNVEVKFWDERLTTVAAHKAMLEADLSRNKRKKIVDKVASTYILQGYLDMISRK | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | A6LSF8 |
P44039 | TRUD_HAEIN | tRNA-uridine isomerase D | Haemophilus | MLEQLPYLALKTPPKTTALLKAECADFIVKEHLGYEMSGDGEFVALYVRKTDCNTLFVGEKLAKFAGVSERNMGYAGLKDRRAVTEQWFCLQMPGMETPDFSQFELDGVEILTVTRHNRKIRTGSLEGNYFDILLRGAEESDELKARLDFVANFGFPNYFTEQRFGRDGHNLTQALRWAQGEIKVKDRKKRSFYLSAARSEIFNLVVAARIEKSTINQVLPNDIVQLAGSHSWFKADEKEDLTALQVRLENQDILLTAPLIGEDILAASEIENEIVNQHSAFDPLMKQERMKAARRPLLMKAKGFSWAFEPEGLRLKFYLPAGSYATALVRELVNYTEE | Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. | P44039 |
Q8PBH3 | UVRA_XANCP | Excinuclease ABC subunit A | Xanthomonas | MAMDFIRIRGARTHNLKNIDLDLPRDKLIVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLSVMEKPDLDHIEGLSPAISIEQKSTSHNPRSTVGTITEIYDYLRLLYARVGQPRCPDHGFPLEAQTVSQMVDHMLTLDPEQRYMLLAPVIRDRKGEHAQVFEQLRAQGFVRVRVDGELYEIDAVPPLALRQKHTIEAVIDRFRPREDIKQRLAESFETALKLGEGMVAVQSLDDATAAPHLFSSKYSCPVCDYSLPELEPRLFSFNAPVGACPSCDGLGVAEFFDPDRVVVHPELSLSAGAVRGWDRRNAYYFQLIASLAKHYKFDVDAVWNTLPAKVRQAVLFGSGDEVISFTYFTDAGGRTTRKHRFEGILPNLERRYRETESPAVREELTKYVSQQPCPACNGTRLNRAARNVFVADRPLPELVVLPVNEALNFFRGLSLPGWRGEIASKIVKEIGERLGFLVDVGLDYLTLERKADTLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLTRLRDLGNTVIVVEHDEDAIRLADHVLDIGPGAGVHGGEICAQGTLQDILESPRSLTGQYLSGKRRIEIPKQRHKPNPKMMLHLRGATGNNLKNVDLEIPAGLLTCITGVSGSGKSTLINDTLFTLAANEINGASHTVAPHREVENLDLFDKVVDIDQSPIGRTPRSNPATYTGMFTPLRELFAQVPESRARGYSPGRFSFNVRGGRCEACQGDGMIKVEMHFLPDVYVPCDVCHGKRYNRETLEIRYKGFNISDVLQMTVEDALRLFEPVPSIARKLETLVDVGLSYIKLGQSATTLSGGEAQRVKLSKELSRRDTGRTLYILDEPTTGLHFHDIEALLGVLHKLRDEGNTVVVIEHNLDVIKTADWIVDLGPEGGHRGGTILVSGTPEDVAAHKASYTGQFLAKMLPSVKARETRPAAMANKPDARPPRKVKPEKVAKATKTATKKTAKKKAS | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. | Q8PBH3 |
A6V3U3 | TAL_PSEA7 | Transaldolase | Pseudomonas | MTSKLEQLKQYTTVVADTGDFDAIARLKPVDATTNPSLLLKAAALPRYAEHLRRATAGSGGDAGLACDRFAVAVGKDILGVIPGRISTEVDARLSFDSEATLARAHRLVELYEEQGVGRERVLIKIASTWEGIRAAEILEREGIQTNLTLLFSFAQAAACADAGVFLISPFVGRIYDWYRKSENRDYVGAEDPGVRSVSRIYRYYKANGYKTVVMGASFRNLGQIEQLAGCDRLTISPDLLQQLADSQGELPRLLLPGDGEPRQVLDESAFRWQMNEDAMATEKLAEGIRLFARDQEKLEYQLATRH | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | A6V3U3 |
B8H7N3 | TAL_PSECP | Transaldolase | Pseudarthrobacter | MTTPTQQLSEAGVSIWLDDLSRGRLETGTLRKLIEEKNVVGVTTNPSIFHAAITAGTDYDATVAAQAAAGASVEETIFEITTTDVADACDLFAPVAAATKGVDGRVSIEVDPRLAWDTNGTIAEAKHLYKKVNKDNVLIKIPATIEGLEAITATLAEGISVNVTLIFSLERYRAVINAFQAGLEQAKENGHDLSKIHSVASFFVSRVDSEIDKRLDKIGTDEAKALKGKAGLANARLAYQVYEELFATERWALLAEAGALPQRPLWASTGVKDPAYPDTLYVTELVAPGVVNTMPEKTLDATFDHGVVTGDTVSGTYADANATLDALEKLGVSYNEVVALLESEGLDKFVASWKELLADVEGALASARKAS | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | B8H7N3 |
Q9XIG1 | U80B1_ARATH | UDP-glucose:sterol glucosyltransferase 80B1 | Arabidopsis | MASNVFDHPLQELEGEDNGVKSEKASLLETSGSVDTTPEDSGHRSSDGHRGLDHCETAPVGLYGDMLINDSEIQYSRSLTEKGSPAIHNLKLDRLSEQEKQKLIVELVRIQNDGTVEVIDNGTPVSELWEFEPTKGQSTITYEKSLTESFRSIPRLKIAILVVGTRGDVQPFLAMAKRLQEFGHRVRLATHANFRSFVRAAGVEFYPLGGDPRELAAYMARNKGLIPSGPSEISKQRKQLKAIIESLLPACIEPDLETATSFRAQAIIANPPAYGHVHVAEALGVPIHIFFTMPWTPTNEFPHPLARVPQSAAYWLSYIVVDLMVWWSIRTYINDFRKRKLNLAPIAYFSTYHGSISHLPTGYMWSPHVVPKPSDWGPLVDVVGYCFLNLGSKYQPREEFLHWIERGSPPVYIGFGSMPLDDPKQTMDIILETLKDTEQRGIVDRGWGGLGNLATEVPENVFLVEDCPHDWLFPQCSAVVHHGGAGTTATGLKAGCPTTIVPFFGDQFFWGDRIYEKGLGPAPIPIAQLSVENLSSSIRFMLQPEVKSQVMELAKVLENEDGVAAAVDAFHRHLPPELPLPESSSEKKDEDDRPDLLQWFFIQIGKKCCLPCGGV | Involved in the biosynthesis of sterol glucosides. Catalyzes the synthesis of steryl glycosides (SGs) and acyl steryl glycosides (ASGs) which are the most abundant sterol derivatives in higher plants. Can act on several sterols like sitosterol, campesterol and stigmasterol. Is required for embryonic development, seed suberin accumulation, cutin formation and flavanoid accumulation in the seed coat. Both UGT80A2 and UGT80B1 are required for the normal production of SGs and ASGs in seeds. | Q9XIG1 |
P58452 | VARG_VIOAR | Varv peptide G | Viola | GVPVCGETCFGGTCNTPGCSCDPWPVCSRN | Probably participates in a plant defense mechanism. | P58452 |
A0A348G5V9 | TX13A_ODOMO | Poneratoxin | Odontomachus | MKPSGLALAFLVVFMMAIMYNSVQAAAIADADAEAEAIAKIKWGKIFKKGGKLIGKTALEAAANAAASEAISAMASQNEK | Cationic amphipathic alpha-helical peptide with antimicrobial activities against E.coli (MIC=3.1 uM), S.aureus (MIC=25 uM), and S.cerevisiae (MIC=50 uM). Also shows histamine-releasing activity (37.5% at 10 uM). Does not show hemolytic activity, even at 50 uM. | A0A348G5V9 |
A5UD72 | YIDC_HAEIE | Membrane protein YidC | Haemophilus | MDSRRSLLVLALIFISFLVYQQWQLDKNPPVQTEQTTSITATSDVPASSPSNSQAIADSQTRGRIITLENDVFRLKIDTLGGDVISSELLKYDAELDSKTPFELLKDTKEHIYIAQSGLIGKNGIDTRSGRAQYQIEGDNFKLAEGQESLSVPLLFEKDGVTYQKIFVLKRGSYDLGVDYKIDNQSGQAIEVEPYGQLKHSIVESSGNVAMPTYTGGAYSSSETNYKKYSFADMQDNNLSIDTKAGWVAVLQHYFVSAWIPNQDVNNQLYTITDSKNNVASIGYRGPVVTIPAGSQETITSSLWTGPKLQNQMATVANNLDLTVDYGWAWFIAKPLFWLLTFIQGIVSNWGLAIICVTIVVKAILYPLTKAQYTSMAKMRILQPKMQEMRERFGDDRQRMSQEMMKLYKEEKVNPLGGCLPILLQMPIFIALYWTFLEAVELRHAPFFGWIQDLSAQDPYYILPILMGISMFLLQKMSPTPVTDPTQQKVMNFMPLIFMVFFLWFPSGLVLYWLVSNLITIAQQQLIYRGLEKKGLHSRKK | Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins. | A5UD72 |
C3SBS8 | TNMT_ESCCA | (S)-tetrahydroprotoberberine N-methyltransferase | Eschscholzia | MGSSAGEIMGRLMKGEIEDEELKKLIRHQWDRRIEWGYKPTHEKQLAFNLDFIKGLKEMVMSGEIDTMNKETYELPTAFLEAVFGKTVKQSCCYFKDENSTIDEAEEAAHELYCERAQIKDGQTVLDIGCGQGGLVLYIAEKYKNCHVTGLTNSKAQANYIEQQAEKLELTNVDVIFADVTKFDTDKTYDRILVVETIEHMKNIQLFMKKLSTWMTEDSLLFVDHISHKTFNHNFEALDEDDWYSGFIFPKGCVTILSSSTLLYFQDDVSALDHWVVNGMHMARSVEAWRKKLDETIEAAREILEPGLGSKEAVNQVITHIRTFCIGGYEQFSYNNGEEWMITQILFKKK | N-methyltransferase with a broad substrate range, accepting protoberberine alkaloids (R,S)-stylopine and (R,S)-tetrahydropalmatine, and to a lesser extent (R,S)-canadine and (S)-scoulerine. | C3SBS8 |
Q7ZVN4 | ZD18B_DANRE | Zinc finger DHHC domain-containing protein 18-B | Danio | MKNREYQQIDPQALATPTPTPPPRSLPEHKPRRARRKWEVFPGKNRFYCDGRIIVARQSGVLPLTLGLILLTSGLFFIFDCPFLVKHLTSCIPAIGGVLFVFVIISLLQTSFTDPGILPRATPEEAADIEKQIDNPTGSSSSYRPPPRTKEVVINQQVVKLKYCFTCKIFRPPRTSHCSLCDNCVERFDHHCPWVGNCVGKRNYRFFYTFIVSLSFLTAFIFGCVTTHLALRSQGGNGLVNALQSSPASALELVVCFFSVWSILGLSGFHTYLVAANLTTNEDIKGSWSGKSGNEDVGNPYSYNSMIKNCCSVLCGPMPPSLIDRRGFVPSDDSVQTSPVEIELPAAKNDINMVGRAVTSGRPPPPPPPPLVVTLQQPAISMQNHSTA | Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates, such as CGAS, HRAS and LCK. | Q7ZVN4 |
Q299E7 | TOTZ_DROPS | Protein Turandot Z | Sophophora | MSRLIHLSFVLALLACLTGPISANPIDDDRERLNQLLSNPEPADDAELLRNTQEAIALYKKHASRTLPGHQVELDLDRDIRAFETEHLTVDGLPIQGGVWDLIKRGADKVPDEVKDQAKELAKTTAKVLFNKLTEYLKKKISGEDAEKKDT | A humoral factor that may play a role in stress tolerance. | Q299E7 |
A0A2K9RFZ2 | TPS2_VITAC | Viteagnusin D synthase | Vitex | MSLRFNLIVTPFSNHRIRNRRETFPAQEFPVATSKSAVKVKCNLITSTDLVGKVREKINGKVDNSLEVPAIHPVDIPSNLCMIDTLERLGVDRYFQSEIDGVLEETYRLWQQKEKDIFADVTCRAMAFRLLRVKGYEVSSDELAPYADQAHVNLQISDVTAVIELYRASQERIYEEESTLEKLHAWTSTYLKQQLVSGTISDKKLHKQVEYYLKNYHGILDLVGIRRSLDLYDIDHYQILKAADRFRTICKDLLAFSRQDFNNCQAQYQRELQLLQRWYEDCRLDKLNYGRDVLRISYFVSSAIIGDPELSDARLAFAKYCVLTTCIDDFFDHAGSREESYRILELVKEWKEKPAEDYGSKEVEFLFTAVYNTVNELAEMAYVEQGRCVKSLLIKLWVELLTSFKKELDSWTDDTALSLDEYLSSSWVSITSRINILTSIQFLGLKLSEEMLSSQECTDLCRHGSLVVRLLNDMQTFEKERRENTKNSVSILLEAPKHEGAITEEEVISKIKEIVEQNRRKLMQMVYQRGTIFPRKCKDVFLKSCRGGYYLYSNGDEFTSPVQIMEDMKLCYEPLTFHPLEANNGGNKN | Involved in the biosynthesis of labdane-type diterpenoid including cleroda-dienols, and peregrinol lactones and furan derivatives, dopaminergic diterpenoids that can bind to dopamine receptors in the human pituitary gland, have probably ability to lower prolactin levels, and are used to treat menstrual cycle disorders (e.g. premenstrual syndrome and mastodynia) (Probable). Terpene synthase the catalyzes the conversion of peregrinol diphosphate to viteagnusin D and 9,13(R)-epoxy-labd-14-ene, and of syn-copalyl diphosophate to vitexifolin A . | A0A2K9RFZ2 |
A7MIG0 | ZAPD_CROS8 | Z ring-associated protein D | Cronobacter | MQTHVLFEHPLNEKMRTWLRIEFLIQQMKALLPVSDHASALHFFRNVGDLLDVFERGDTRTELLKELERQQRKLQSWAEVPGVDNERIESLRHELKARSSMLMAAPRLGQTLREDRLIALVRQRLSIPGGCCSFDLPLLHVWLCSPQEERDVQVNSWLATLQPLTYTLDMILDLIRQSAPFRKQTSLNGFYQDNGDDADLLRLQLPLQEALYPQISGHKSRFAIRFMPLDSEHGRVPERFDFELACC | Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity. | A7MIG0 |
A4WDV0 | TRUD_ENT38 | tRNA-uridine isomerase D | Enterobacter | MTAFENLTWLHGKPQGNGLLKANPEDFVVVEDLGFEPDGEGEHILVRILKNGCNTRFVADALAKFLKIHAREVSFAGQKDKHAVTEQWLCARVPGNAMPDLSQFELEGCKVLEYARHKRKLRLGALQGNAFTLILRDVTDRDDVEKRLAAIAEQGVPNYFGAQRFGIGGSNLLGALRWAQSDAPVRDRNKRSFWLSAARSALFNQIVSERLKKPDANQVVVGDALQLAGRGSWFVATAEEITDVQTRVDNKTLMITAAMPGSGEWGTQADALAAEQAAIADAPELQSLLMREKVEAARRAMLLYPQKLSWNWWDDVTVELRFWLPAGSFATSVVRELINTSGDYANIAE | Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. | A4WDV0 |
P36537 | UDB10_HUMAN | UDP-glucuronosyltransferase 2B10 | Homo | MALKWTTVLLIQLSFYFSSGSCGKVLVWAAEYSLWMNMKTILKELVQRGHEVTVLASSASILFDPNDSSTLKLEVYPTSLTKTEFENIIMQLVKRLSEIQKDTFWLPFSQEQEILWAINDIIRNFCKDVVSNKKLMKKLQESRFDIVFADAYLPCGELLAELFNIPFVYSHSFSPGYSFERHSGGFIFPPSYVPVVMSKLSDQMTFMERVKNMLYVLYFDFWFQIFNMKKWDQFYSEVLGRPTTLSETMRKADIWLMRNSWNFKFPHPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSSGENGVVVFSLGSMVSNMTEERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQNDLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFFDQPDNIAHMKAKGAAVRVDFNTMSSTDLLNALKTVINDPSYKENIMKLSRIQHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHNLTWFQYHSLDVIGFLLACVATVLFIITKCCLFCFWKFARKGKKGKRD | UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. | P36537 |
A8M4E3 | THIG_SALAI | Thiazole synthase | Salinispora | MSGVSFELGGVSISSRLVLGTGGAANLHVLEQAIRAAGTGLVTVALRRVDSTPGGSGGLLDLIDRCGVRLLPNTAGCYTAGEAVKVAHLAREAFDTDWVKLEVIGDERTLLPDGVELLRAAEELVAEGFTVLPYTSDDPILARRLADVGCAAVMPAGSPIGSGLGVSNPHHIRLIRQCVDVPVILDAGIGTASDAALAMELGCDAVLLASAVTRAADPVAMATAMRYAVEAGRLAYRAGRIPRRFHALASTPDDGRPEL | 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. | A8M4E3 |
P47825 | TAF4_DROME | Transcription initiation factor TFIID 110 kDa subunit | Sophophora | MNTSQTAAGNRITFTSQPLPNGTISIAGNPGAVISTAQLPNTTTIKTIQAGIGGQHQGLQQVHHVQQQQQSQQQQQQQQQTQSAGQPLLNSMLPAGVVVGMRQQAPSQQQQKNVPTNPLSRVVINSHMAGVRPQSPSITLSTLNTGQTPALLVKTDNGFQLLRVGTTTGPPTVTQTITNTSNNSNTTSTTNHPTTTQIRLQTVPAAASMTNTTATSNIIVNSVASSGYANSSQPPHLTQLNAQAPQLPQITQIQTIPAQQSQQQQVNNVSSAGGTATAVSSTTAATTTQQGNTKEKCRKFLANLIELSTREPKPVEKNVRTLIQELVNANVEPEEFCDRLERLLNASPQPCLIGFLKKSLPLLRQALYTKELVIEGIKPPPQHVLGLAGLSQQLPKIQAQIRPIGPSQTTTIGQTQVRMITPNALGTPRPTIGHTTISKQPPNIRLPTAPRLVNTGGIRTQIPSLQVPGQANIVQIRGPQHAQLQRTGSVQIRATTRPPNSVPTANKLTAVKVGQTQIKAITPSLHPPSLAAISGGPPPTPTLSVLSTLNSASTTTLPIPSLPTVHLPPEALRAREQMQNSLNHNSNHFDAKLVEIKAPSLHPPHMERINASLTPIGAKTMARPPPAINKAIGKKKRDAMEMDAKLNTSSGGAASAANSFFQQSSMSSMYGDDDINDVAAMGGVNLAEESQRILGCTENIGTQIRSCKDEVFLNLPSLQARIRAITSEAGLDEPSQDVAVLISHACQERLKNIVEKLAVIAEHRIDVIKLDPRYEPAKDVRGQIKFLEELDKAEQKRHEELEREMLLRAAKSRSRVEDPEQAKMKARAKEMQRAEMEELRQRDANLTALQAIGPRKKLKLDGETVSSGAGSSGGGVLSSSGSAPTTLRPRIKRVNLRDMLFYMEQEREFCRSSMLFKTYLK | TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. May function as a coactivator by serving as a site of protein-protein contact between activators like Sp1 (or btd) and TFIID complex. | P47825 |
Q57686 | TRPD_METJA | Anthranilate phosphoribosyltransferase | Methanocaldococcus | MITEALKKVIEFKDLDEKEAEAVMKDIMSGNAKPTQIAAILTALRMKGETIEEITAFAKIMREFSLKINPNVPKLLDTCGTGGDNLNTFNISTATAFVVSAYVPVAKHGNKAVSSKSGSADVLEALGVNLNVPIERVKESIEKIGIGFLFAPHFHPAMKFATPVRKELGIRTVFNVLGPLTNPANANYQLMGVYDEKLTEKLANVLKNLGLKGALVVHGSGMDEITTIGKTKISELRNGEIKSYYIEPEDFGIKKAKLEDIRGGDAEENAKIIGEIFEGEEVGAKRDIVVLNAAFALYIAEEAKDVEEGIKLAEKSIDEGKALKKLEDLIEFYREG | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | Q57686 |
B3PP83 | UBIG_RHIE6 | 3-demethylubiquinone 3-O-methyltransferase | Rhizobium | MTEGARSTIDQGEVDRFSAMAAEWWSPTGKFKPLHKFNPVRLAYIRDKACANFGRDQKSPRPLEGLRVLDIGCGGGLLSEPVARMGASVVGADPSDKNIGIASTHAKASGVPVDYRAVTAEELAEAGETFDIVLNMEVVEHVADVEFFMTTCAKMVRPGGLIFVATINRTMKAAALAIFAAENILRWLPRGTHQYEKLVRPEELEKPLAASGLEITDRTGVFFNPLSNQWNLSRDMDVNYMLLGKRPA | O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. | B3PP83 |
C1DNG2 | UREF_AZOVD | Urease accessory protein UreF | Azotobacter | MNGMWALLRLASPQLPIGGYSYSQGLELAIERGLVCDPPTARRWLEDQLLLNLARFEAPLLLAQCRAAADGDWTALEALAERHRASRETRELHLESRQMGFSLRQLLEDLPELDEPSRAVFARLVEPGLAPAWALAARAWGIAPEDALAAWLWSWLENQLAVLMKSLPLGQQAAQRLTSALLPALGQAQRTACAHAPDDWGTVAFGLTLASMAHERQYSRLFRS | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | C1DNG2 |
P18727 | ZG52_XENLA | Gastrula zinc finger protein XlCGF52.1 | Xenopus | TAENPFTCPECGKRFSQKSNCWHTEDHTGEKPFTCMECSKSFTVKSSLLSHQRVHTGEKPYTCTQCNKQFSHSAQLRAHISTHTGVGPFPCTECSKTFSLKHKLYKHQRIHTGEKPFQCLECGKSFSVKHGLLKHQRSHTGEKPYACSECQKTFAHKTTLMVHERIHTGERPYECNDCGKRFIHSTNLNCHQKIHSGEKPFTCTECGKSFSLKNKLVRHQKIH | May be involved in transcriptional regulation. | P18727 |
Q9UUB6 | UBLH2_SCHPO | Ubiquitin carboxyl-terminal hydrolase 2 | Schizosaccharomyces | MSWTTIESDAGVFTDLIENLGVKDVEVDELYSLDVDSLRQFPDIYGIIFLFKWNSKVDKPDGTMDYDSMDNIFFAKQVINNACATQALLSVLLNHSDEIDLGTTLSEFKDFSKTLPPELKGEALGNSEHIRCCHNSFARSDPFISEEVRAATDEDEVYHFIAYTNINNVFYELDGLQAAPINHGSCTKEEFAEKAVSVIQARIANYDPAEIRFNLMVICKDKKASLLTREDLTDEEKAASIAVEDEKRLRWKRENQLRRHNFVGLFVELSKLLVKDRIDKNTWNSTLETAKAKYASQKRP | Ubiquitin-protein hydrolase is involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. | Q9UUB6 |
Q5HIG6 | TILS_STAAC | tRNA(Ile)-lysidine synthetase | Staphylococcus | MQLNSNGWHVDDHIVVAVSTGIDSMCLLYQLLNDYKDSYRKLTCLHVNHGVRSASIEEARFLEAYCERHHIDLHIKKLDLSHSLDRNNSIQNEARIKRYEWFDEMMNVLEADVLLTAHHLDDQLETIMYRIFNGKSTRNKLGFDELSKRKGYQIYRPLLAVSKKEIKQFQERYHIPYFEDESNKDNKYVRNDIRNRIIPAIDENNQLKVSHLLKLKQWHDEQYDILQYSAKQFIQEFVKFDEQSKYLEVSRQAFNNLPNSLKMVVLDCLLSKYYELFNISAKTYEEWFKQFSSKKAQFSINLTDKWIIQIAYGKLIIMAKNNGDTYFRVQTIKKPGNYIFNKYRLEIHSNLPKCLFPLTVRTRQSGDTFKLNGRDGYKKVNRLFIDCKVPQWVRDQMPIVLDKQQRIIAVGDLYQQQTIKKWIIISKNGDE | 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. | Q5HIG6 |
Q94AB5 | U7E12_ARATH | UDP-glycosyltransferase 76E12 | Arabidopsis | MQVLGMEEKPARRSVVLVPFPAQGHISPMMQLAKTLHLKGFSITVVQTKFNYFSPSDDFTHDFQFVTIPESLPESDFKNLGPIQFLFKLNKECKVSFKDCLGQLVLQQSNEISCVIYDEFMYFAEAAAKECKLPNIIFSTTSATAFACRSVFDKLYANNVQAPLKETKGQQEELVPEFYPLRYKDFPVSRFASLESIMEVYRNTVDKRTASSVIINTASCLESSSLSFLQQQQLQIPVYPIGPLHMVASAPTSLLEENKSCIEWLNKQKVNSVIYISMGSIALMEINEIMEVASGLAASNQHFLWVIRPGSIPGSEWIESMPEEFSKMVLDRGYIVKWAPQKEVLSHPAVGGFWSHCGWNSTLESIGQGVPMICRPFSGDQKVNARYLECVWKIGIQVEGELDRGVVERAVKRLMVDEEGEEMRKRAFSLKEQLRASVKSGGSSHNSLEEFVHFIRTL | Possesses quercetin 3-O-glucosyltransferase and 7-O-glucosyltransferase activities in vitro. | Q94AB5 |
O30143 | WTPB_ARCFU | Molybdate/tungstate transport system permease protein WtpB | Archaeoglobus | MRLLFSALLALLSSIILLFVLLPVAATVTLQLFNFDEFLKAASDPAVWKVVLTTYYAALISTLIAVIFGTPLAYILARKSFPGKSVVEGIVDLPVVIPHTVAGIALLVVFGSSGLIGSFSPLKFVDALPGIVVAMLFVSVPIYINQAKEGFASVDVRLEHVARTLGSSPLRVFFTVSLPLSVRHIVAGAIMSWARGISEFGAVVVIAYYPMIAPTLIYERYLSEGLSAAMPVAAILILLSLAVFVALRIIVGREDVSEGQG | Part of the ABC transporter complex WtpABC involved in molybdate/tungstate import. Probably responsible for the translocation of the substrate across the membrane (Probable). | O30143 |
Q5KVD5 | Y3066_GEOKA | Nucleotide-binding protein GK3066 | Geobacillus thermoleovorans group | MGQNGALQPIQLVIITGMSGAGKTVAIQSFEDLGFFCIDNLPPTLLPKFLELVKESGNKMNKVALVMDLRSRDFFDHLFAALDELAEQAWVIPQVLFLDAQDSTLVARYKETRRTHPLAPNEPPLEGIRLERKLLEELKGRAQIIYDTTGLKPRELREKIIRQFSSHAQSGFTINVMSFGFKYGIPIDADLVFDVRFLPNPHYIEHMRPKTGLDDDVSSYVLKWGETQKFLEKLIDLLSFMLPYYQREGKSQLVIAIGCTGGQHRSVALAEYIARHFSDDYKTVVSHRDMERRKDIHR | Displays ATPase and GTPase activities. | Q5KVD5 |
Q8CXC4 | TGT_OCEIH | tRNA-guanine transglycosylase | Oceanobacillus | MNPITYELIKTDKQTGARLGRVHTPHGSFDTPTFMPVGTLATVKTMSPEDLQSMQANIILSNTYHLWLRPGEDIIREAGGLHKFMNWDGAILTDSGGFQVFSLSDMREIKEEGVHFRNHLNGEKLFLSPEKAMDIQNALGSDIMMAFDECPPYPAEYDYMKASVERTSRWAERCLQAHNRPHDQGLFGIVQGGEYEALRKQSAEDLVSLDFPGYAIGGLSVGEPKHVMNKVLEFTTPFLPSNKPRYLMGVGSPDALIDGAIRGVDMFDCVLPTRIARNGTCMTSNGRLVVRNAKYARDFNPIDEHCSCHVCKNYSRAYIRHLIKCNETFGFRLTTYHNLHFLLKLMEQVRTAIKEDRLGDFKESFFEQYGLNKANPKNF | Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). | Q8CXC4 |
A9MHE0 | THIG_SALAR | Thiazole synthase | Salmonella | MLRIADKTFDSHLFTGTGKFASAQLMVDAIRASGSQLVTLAMKRVDLRKPNDAILSPLLEAGVTLLPNTSGAKTAEEAIFAAQLAREALGTHWLKLEIHPDARWLLPDPIETLKAAGELVKQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQGLETRAMLEIIIQQATVPVVVDAGIGVPSHATQALEMGADAVLVNTAIAVANDPVMMANAFRLAVEAGVLARQAVPGNRSVYASATSPLTGFLEVSA | 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. | A9MHE0 |
P29289 | TNNC1_HOMAM | Troponin C, isoform 1 | Homarus | MDTLDEDQVQALQKAFNSFDTDDKGFITPDTVGVILRMMGVKISDRHLQEVISETDEDGSGEIEFEEFAALAAKFLSEEDEEALKKELKEAFRIYDRGGNGYITVHTLKEILRELDNKLTEDNLDSIIEEVDEDGSGTIDFNEFMKMMNG | Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. | P29289 |
B9MM32 | TRMFO_CALBD | Folate-dependent tRNA(M-5-U54)-methyltransferase | Caldicellulosiruptor | MEIVVIGAGLAGVEAANVISKFGIKVKLFEMKPKKFSPAHKIDNFAELVCSNSLKSKLLTNASGLLKEEMKVFGSLVMEAAEATSVEAGQALAVDRYKFSEYITQRIKHNGLISIIHEEVTEVPRDKVVVVSTGPLTTESLLSDISKLCNSKNLYFFDAAAPIVLKDSIDFSKAFFASRYNKGSNDYINCPMTKEEYERFYWELVNAEVIEVKDFEKDLLFEGCMPIEEMARRGIDTMRYGPLKPVGIIDPRTGKMPYAVVQLRKDTQDGKLYNMVGFQTRLKWSEQKRVFRLIPGLENAEFVRYGVMHKNSYINSPEVLTKYLFLKKYPNIFFAGQITGVEGYLESASTGIIAGINAARQILGKEPISLPPNTCIGALIEYITTPKKDFQPMNANYGIISIDDEISKIKDKEKRKLLIAQKSLNICRELANKIFE | Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. | B9MM32 |
Q7V6B8 | TAL_PROMM | Transaldolase | Prochlorococcus | MATLLEQLSTMTVVVADTGDLDAIRKFTPRDATTNPSLILAAAQIPAYQSLIDEALHSSRQLLGNSAAVEEVVHEALDEICVIFGKEILKIVPGRVSTEVDARLSFNTEATIAKAHKLIGLYNDAGITNDRVLIKIASTWEGIKAAEVLEKDGIHCNLTLLFGFSQAVACAEAGVTLISPFVGRILDWYKASTGRDSYAGPEDPGVISVTKIFNYFKTYDYKTEIMGASFRNLDEIIELAGCDLLTISPKLLDQLGSTEAPLKRKLDAVNPVAAESQIHVDKESFESMMRADRMAFEKLDEGIRGFSKAIETLEAQLAHRLAVLEGGAAFCHVVQEIFMLNDLDGDGCITREEWLGSDAVFDALDHDHDGRLLQEDVRSGLGAALALTTA | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | Q7V6B8 |
P32732 | TRUB_BACSU | tRNA-uridine isomerase | Bacillus | MVNGVLLLHKPVGMTSHDCVMKIRKLLKTKKVGHTGTLDPEVSGVLPICVGRATKIVEYLTEKSKTYDAEITLGFSTTTEDQTGETVETKPVNHDIDKADVEKVLNSLKGKQEQIPPMYSAVKVNGKKLYEYARAGIEVERPKRMITIEDIALTTEIKHHGETASFRFTVTCSKGTYVRTLAVMIGEKLGYPAHMSHLIRTASGDFSLDECFTFDELEAQAQSGTVEEHTVPIERALNHLPKWIISDTLAKKVENGALLETPEQFSEMTSGDRIAVFTESGTCLAIYFPHPAKKGLLKPAKVLMQKSEQ | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | P32732 |
F4I700 | UBN2_ARATH | Ubiquitously expressed nuclear protein 2 | Arabidopsis | MEDEPKLPTDDGPTFNESCKISSEILTAGDRKLLKVELLKEETTLVSWKKLMDEASKENGGLFVSAPERLLNANPNLEFRLAPGAQTENEMVNQPHPNRLNSVIAKIERLYMGKDGSDGEELDGAPDDDDYDTEDSFIDDAELDEYFEVDNSPIKHDGFFVNRGKLERIEPSATSNQQQPKKRRRKESAKPCGDVVDVSRKRAKMAKTAGGKDQSASPGPSSKKISNDSKTVQDSFSPLKAQNGNDSLVLENVKHTDKANHQPMNATSPKSKAAGSSGPLHPKCSSKSVHEQSNSPPGKSRPNVSAKSAVVRQQVNNGMPDLDIATESKTSIQISKKSGSNGRPKYSTLEKAIRNLEKLVAESRPPAATENQDADISSQAVKRGLPGDVKLHLAKVARIAYASQGEISGELINRLMGIVGHLIQIRSLKRNLKIMIDSIVTANREKDTRFQRIKSEITEMLKTQVPLVESQETNQEAGTSDDFQDVGSLGKSPVKKFVMDVALEEKLCDLYDVFVEGMDEHSGSQIRKLYSDLAQLWPNSLVDNHEIRRAICREKERRRALEGNIGKEMDQTKITKKKQTQLVPKSEGITYPDKTSGVEVKASVVLTATTTSLVDCQPAADSSFERSKQQHEKLKRTSSLSNPAAEGKKVRRKTEPALEETHLPAEKPLVLALKRQTHLKSKTHKQVQVHPQSKAHKQAQVHPKAKTQTPPDLNLPS | May be required for replication-independent chromatin assembly. | F4I700 |
O94348 | YIP1_SCHPO | Protein transport protein yip1 | Schizosaccharomyces | MAYYNNPANLQYYDYSYTADNSFNTQSRAAGFYDEPLHEPLSQGWLAAFSTSGYPGEPSLLEELEINFGHIKQKTTHVLNPFKHVDVHIMDDTDMAGPILFCLLFSTFLSLHGRSHFGYIYGIALLGSLSLHFVLRLMSAKNLFFTRTVSVLGYSLLPLVVIAFFKNIFTFNGIAGYALAALACIWCTYAASAMFVGILQVNNMRFLVAYPIALFYGVFAVITVFSK | Required for fusion of ER-derived vesicles with the Golgi during ER-to-Golgi protein transport, probably by mediating correct membrane localization of ypt1. | O94348 |
A0LDT5 | TIG_MAGMM | PPIase | Magnetococcus | MEVNVVENGLFDRDITITVAAEKVDALLSQEMTKTAAQVRLPGFRAGKVPTKMIEQRFGASIRAEVAEQLFRDSYPTALMEKGLRPVGQPELDLVELEKGKPFTYTAKIQIFPVIEPKDYTGMSLTKPVVTIQDSDVETVITRVREANAEYRTQEGVAAASGDRMTFDFEGFVDGEAFEGGKAEDYVLELGSNRFIPGFEDQLIGAKGGDALEVKVTFPEDYHGTQLAGKEAIFKCVVKAIESRELPEVDEELAKKAGVQEGGVEAMKQEIHERLVKEADKVAKQEMKQQVFKLLLENNPNELPSQMVDHEIEQMVATAKEEYSRQGVDPEQLGFTDETWRNQYAEKAKERIILGLLMGSIVSKENLEIDDQAVEAHIDALVQQFAAGDYAEQLKAQLKKDKARLEEFRGAALEEKTVAWLIEQGTVTEEEKSFEELVAQRG | 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. | A0LDT5 |
Q12132 | USV1_YEAST | Up in starvation protein 1 | Saccharomyces | MENTTNRNTAGVLTSSNGNFATNSVAASTPKRSKSARRKTFKCTGYDGCTMSFTRAEHLARHIRKHTGEKPFQCPACLKFFSRVDNLKQHRESVHAHKNHHSTSSHQRKPSSSSLSSSSSASSSSSASSSTSYSDPYRKTNINSGNMPMMAENEKAPQIIHSSPEFITSTRSIPPISPRSIYNTQRQQQHQQQQHQQAPYYFPSHPITDSYYQYPLPSNNNTINYLPSVDVQYPLNVSPSSTSHPASEVIISSFPPRSMPSTSFKYKDSADFQARTTMNKYNIRPSNINVNTSNINNHLDSFSPPFSPSTTVAEAKPIILPQYQQAFSQPPNGNKNNNMSSSKNGGKGGENFKNTDDRNDNNNKKRSETLSESDISVNTNKKRLSVDYILT | Transcription factor that participates in the transcriptional activation of glucose-repressed genes during exponential growth in non-fermentable carbon conditions. Also involved in salt-stress response. | Q12132 |
O84072 | Y069_CHLTR | Probable metal transport system membrane protein CT_069 | Chlamydia | MLSCIFQDTIFLSSFLAVSLICMTTALWGTILLVERQPLLSESLSHACYPGLLIGALLSYKVPAFSDSLWVIIFFGCLASVLGCLGISFLEKKLAMHKDSALCLVLVSFFGVGVILVSYVKDCCPLLYNKINAYLYGQAATLGYTEAKLALIIFCLSAVVLWWWYRQISVAIFDREFAYSCGLRTRTAELVVLVFISLVIVSGVRSVGILLISAMFVAPPLSARQLSDRLSTILILSSIFGGICGALGCYFSVAFTCQTVVEGKPISIILPTGPLVVFFAGVLVFLCLIFSWKTGWITRYFRRKWFLFSRDEEHLLKIFWYLREQNTYQVGMRDFVRSRKYQEYFGDKVFPRFRMFLLCKKGLVSCSEHQWSLTDKGLARAAKLVRAHRLWESYLVSQLDFNKNEVHHFAEEMEHVLTDELDSTLSQMLQDPDYDPHQREIPKRTRKSDGC | Part of an ATP-driven transport system CT_067/CT_068/CT_069/CT_070 for a metal. | O84072 |
Q601G9 | TIG_MESH2 | PPIase | Mesomycoplasma | MIKREFLPESAELKIKLTADSKKWAEFYQKAEQKQAAKVSLRGFRKGKVPLEKARAYLNPQAVFELALRMFLPELEKQAATNIIDSDNVIESPIFNIVNMDKNNLEIEFLYPVYPEIKLPDYKNLKTKFAIKKITKEDIELQKQKLLEAKGRFIEVNRPVKIGDVINFNFKGFIDDEPFDGGEGENFDLRIGSNSFIAGFEEQLVGLEIKKEADIYVTFPENYQVHTYANKKARFRVKINKIKENQPAKLTNEFVASLKIQNVETISQLEVYLENLTERENIERAKIDFQKNALTEIGEQVEVPLAKKLINLEIERLNEVFHSTLKQQEIPLKEYLKITKFTEKDIYDQFEVEAKKLLKNSFIFAEIAKLEGLVPTQQEYESHVEKLAKFTGKSVQEISETVSYNEIQINITNQKVIDKLIEFNHETKDEEIVNKNQNDNEIEQDKEQKDNNEEKIKQENNLENK | 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. | Q601G9 |
Q21FH2 | YBEY_SACD2 | Endoribonuclease YbeY | Saccharophagus | MLTIDIQQASTADASQLPSDKQFEIWVEAALQQRMNEAELSIRIVDEDESQALNLQYRGKDKSTNVLSFPCELPDGVELPLLGDLVICAQVVAKEALEQGKLLHAHWAHMVVHGTLHLLGYDHIEDGEAEEMEAIEIQVLLELGYPNPY | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | Q21FH2 |
A0RN29 | THIC_CAMFF | Thiamine biosynthesis protein ThiC | Campylobacter | MRKDWCEARKNDPTPTQMYYAKNGVITPEMEYVAKVEMLKPEYIRQLVAEGKLIIPANINHTNQIPMAIGRAVKCKINANIGSSALASDINEEIEKLKVCLKYGADTVMDLSTGGDLDEIRRAIIANSTVPIGTVPIYQIIHDIKDLDNLTPQIMLECIEKQAKQGVSYFTIHAGFLLKFMPLVAKRKMGIVSRGGSLMASWMMKHHKENPFYEAFDEICDICAKYDASLSLGDSLRPGCLHDASDEAQMSELAVLGELTKRAWEKNVQVMVEGPGHVPFNQIEFNMKEEKRLCHDAPFYILGPLPTDIGAGYDHITSAIGGTMAAFHGASMLCYVTPKEHLGLPNAKDVRDGIISHKIAAHAADIALGRVGAIERDHAMSDARYKFDWNKQFELALDPDKARELHDESLPQDVFKEAEFCSMCGPKFCAYKISQEIAKIECSDYPKEKK | 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. | A0RN29 |
A1K4B0 | TRPA_AZOSB | Tryptophan synthase alpha chain | Azoarcus | MSKIQTTFQRLQAQGRKALIPFITAGDPDPTLTVPLMHALVAGGADIIELGVPFSDPMADGPTIQRASERALAQGMTLRKVLQAVREFRSGDADTPVVLMGYANPIEAMGQQAFVAAAREAGVDGALVVDYPPEECVEFAAASKAAGLDPIFLLAPTSSEQRFADVARAGSGYIYYVSLKGVTGAGTLDLDEVARRIPQIRAAVGMPVGVGFGIRDAESARRIGAVADAVVIGSRIIEEIERSPREQACSNVTHFVKGIREALDTLPGVKQ | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | A1K4B0 |
B3R789 | TATA_CUPTR | Sec-independent protein translocase protein TatA | Cupriavidus | MGSFSIWHWLIVLVIVMLVFGTKKLRNIGQDLGGAVKGFKDGMKDGEDKGAQPAASKELRDSTTIDVDAKEKSRQQ | 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. | B3R789 |
Q6NQ64 | TRM52_ARATH | tRNA methyltransferase 5 homolog 2 | Arabidopsis | MVSKLSLFRANSLPFPVISSYSARFILKPYPKPKTLIFCVFSSNLSSTTFPYGPSLLKGKKPVLDDIRLASIGRDRDAHRGKIGEFDESIEKDVLLNEDEFTRVFEISAIRVPAKDCFALENRLRGHLLNWPRIRNIARVPGDEIEEDVVKLLGRETDEEEEDEDSVVDSVNRRIRGKAEGDGERLSSVLHRDKLARTFNSTGYLKFRNLAKISRPKRKRKTERTREGKEKEIASRRNEMAVVEVVETRGGEEDFEGLLGEGYGSRGRWRGSTRLLLLDEKYSGEEVQDLPEAIKVLFAEAKMADASLSFELVKCRLTLFYDYWPMIEILEAVLPKGMIVPSAFEMVGHIAHLNLRDEHLPYKRLIAKVVLDKNQPKIQTVVNKIDPIHNDFRTMQLEVLAGNHSLVTLVVENGLRFHVDLARVYWNSKLGTERQRLLLGFDQNDVVCDVFAGVGPIALAAARIVKRVYANDLNPHAVEFMEQNSVVNKLEKRIEIFNMDGRRFIKAMFSSEKGQKVTQVVMNLPKDAAESLDAFRGVYNDRHRDEGLSFPTIHVYGFSKASDPEFDFHERIRIALSEVAVDVKMRKVRLVAPGKWMLCASFILPKNVAFSRKNLSYVD | Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding. | Q6NQ64 |
A4X4H8 | TRMD_SALTO | tRNA [GM37] methyltransferase | Salinispora | MRVDVVSIFPEYFAPLDLSLIGRARASGTLQLAVHDLRTWTHDVHRTVDDTPYGGGPGMVMRPEPWGEALEALAPPGGNPPRLLVPTPAGAPFTQALAHELAAEPHLLFACGRYEGIDQRVLEHAASRMPVTEVSLGDYVLFGGEVAVLVILEAVTRLLPGVLGNVGSLDDESHAHGLLEAPMYTKPAVWRGQEVPTVLRSGDHGKIARWRRDEALARTVARRPDMIAALPPECLDPRDRAALERAGFPDPPEGVAK | Specifically methylates guanosine-37 in various tRNAs. | A4X4H8 |
O07577 | YHDH_BACSU | Uncharacterized sodium-dependent transporter YhdH | Bacillus | MSEQKPVQWASKIGFVMAAAGSAIGLGAIWKFPYVAGTNGGGAFFLIFVLFTILLGYPLLVGEFIFGRRNQTNAIDAYKKEAPRSAWFLTGWIGVAACFLVLSFYSVIGGWILLYIVKTASGSLSGLSQAQYGALFASIIQNPVQTLAAQLVFMALTVLVVARGVQKGIERVSAVMMPILFLLFILLVLRSLTLNGAMEGVKFLLVPHFGDLTPESILFALGQAFFTLTLGVSVMVTYSSYLPKTQNIPRSAASIVLMNIIVTLLAGLAIFPAVFSFGFQPNEGPTLLFTVLPAVFEQLPFGTLFFIGFLVAFLFAALTSAFSMVEIIVATIGKGDEKKRKKLSWTSGLLIFLVGIPCCLSYGVLSDVHLFGKTFFDIADFTVSNVLMPSGALLISLFIPLKISKSELLAEMRNGSNAGKAFFYTWFYLLRFIVPLAIIIVFLNLIGILSF | Putative sodium-dependent transporter. | O07577 |
Q4R3I5 | ZN668_MACFA | Zinc finger protein 668 | Macaca | MEVEAAEARSPAPGYKRSGRRYKCLSCTKTFPNAPRAARHAATHGPADCSEEVAEVKPKPETEAKAEEASGDKVAGSAAKPRPYACPLCPKAYKTAPELRSHGRSHTGEKPFPCPECGRRFMQPVCLRVHLASHAGELPFRCAHCPKAYGALSKLKIHQRGHTGERPYACADCGKSFADPSVFRKHRRTHAGLRPYSCERCGKAYAELKDLRNHERSHTGERPFLCSECGKSFSRSSSLTCHQRIHAAQKPYRCPACGKGFTQLSSYQSHERTHSGEKPFLCPRCGRMFSDPSSFRRHQRAHEGVKPYHCEKCGKDFRQPADLAMHRRVHTGDRPFKCLQCDKTFVASWDLKRHALVHSGQRPFRCEECGRAFAERASLTKHSRVHSGERPFHCNACGKSFVVSSSLRKHERTHRSSEAAGAPPAQELVVGLALPVGVAGEGSATPAAGAGLGDPPAGLLGLPPESGGVMATQWQVVGMTVEHVECQDAGVREAPGPLEGAGEVGGEEADEKPPQFVCRECKETSSTMTLLRRHERSHPELRPFPCTQCGKSFSDRAGLRKHSRTHSSVRPYTCPHCPKAFLSASDLRKHERTHPVPMGTPTPLEPLAALLGIPEEGPA | May be involved in transcriptional regulation. | Q4R3I5 |
Q5E207 | UBIA_ALIF1 | 4-HB polyprenyltransferase | Aliivibrio | MNMSKAEAFWQLTRMNRPIGSLLLLWPTLWALFLAADGLPDWHVLIVFVLGVVFMRSAGCVINDFADRKVDGHVKRTANRPLPSGLISSKEALSLFAVLVVCSFLLVLTMNTLTIMLSGIGIVLAIAYPFMKRVTYLPQFVLGLAFSWAIPMAYAAESNQVPPEAWLLFVINALWTIAYDTQYAMVDRDDDVKIGIKSTAILFGRYDKTIIGLLQLSVLALLIVLGSQLALSGIYYWGILAAAGFFVYQQWLIKGREREACFKAFLNNNYVGGLIFIAISASVLI | Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate. | Q5E207 |
Q5E2K6 | UPPP_ALIF1 | Undecaprenyl pyrophosphate phosphatase | Aliivibrio | MTYFEAFFLALLQGFTEFLPISSSAHLILPSAILGWSDQGLAFDVAVHVGTLAAVVIYFRKEVVTLLTAWVGSIVKKEHNKESNLAWLIVLATIPAALFGLLFKDFIEIYLRSAWVIAATTIVFGLLLWWVDKNATLAKDEYQMTWKKALFLGIAQAMAMIPGTSRSGITITAALYLGFTREAAARFSFLMSIPIITLAGSYLGLKLAMSDISIHLGLLSTGVIVSFISAYICIHFFLKLISSMGMMPFVIYRILLGSSLLVWLALH | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | Q5E2K6 |
P66969 | TRMD_MYCBO | tRNA [GM37] methyltransferase | Mycobacterium tuberculosis complex | MRIDIVTIFPACLDPLRQSLPGKAIESGLVDLNVHDLRRWTHDVHHSVDDAPYGGGPGMVMKAPVWGEALDEICSSETLLIVPTPAGVLFTQATAQRWTTESHLVFACGRYEGIDQRVVQDAARRMRVEEVSIGDYVLPGGESAAVVMVEAVLRLLAGVLGNPASHQDDSHSTGLDGLLEGPSYTRPASWRGLDVPEVLLSGDHARIAAWRREVSLQRTRERRPDLSHPD | Specifically methylates guanosine-37 in various tRNAs. | P66969 |
P44973 | YIDC_HAEIN | Membrane protein YidC | Haemophilus | MDSRRSLLVLALIFISFLVYQQWQLDKNPPVQTEQTTSITATSDVPASSPSNSQAIADSQTRGRIITLENDVFRLKIDTLGGDVISSELLKYDAELDSKTPFELLKDTKEHIYIAQSGLIGKNGIDTRSGRAQYQIEGDNFKLAEGQESLSVPLLFEKDGVTYQKIFVLKRGSYDLGVDYKIDNQSGQAIEVEPYGQLKHSIVESSGNVAMPTYTGGAYSSSETNYKKYSFSDMQDNNLSIDTKAGWVAVLQHYFVSAWIPNQDVNNQLYTITDSKNNVASIGYRGSVVTIPAGSQETITSSLWTGPKLQNQMATVANNLDLTVDYGWAWFIAKPLFWLLTFIQGIVSNWGLAIICVTIVVKAILYPLTKAQYTSMAKMRILQPKMQEMRERFGDDRQRMSQEMMKLYKEEKVNPLGGCLPILLQMPIFIALYWTFLEAVELRHAPFFGWIQDLSAQDPYYILPILMGISMFLLQKMSPTPVTDPTQQKVMNFMPLVFMFFFLWFPSGLVLYWLVSNLITIAQQQLIYRGLEKKGLHSRKK | Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins. | P44973 |
A9N730 | TRUB_SALPB | tRNA-uridine isomerase | Salmonella | MSRPRRRGRDIHGVLLLDKPQGMSSNDVLQKVKRIYNANRAGHTGALDPLATGMLPICLGEATKFSQYLLDSDKRYRVIARLGQRTDTSDADGQIVQERPVTFSAEQLASALETFRGDIEQIPSMYSALKYQGKKLYEYARQGIEVPREARPITVYELLFIRHEGNELELEVHCSKGTYIRTIIDDLGEKLGCGAHVTYLRRLTVSKYPVDRMVTLEHLQTLVAQAEQQGVPAAQLLDPLLMPMDSPASDYPVVNLPLTSSVYFKNGNPVRTTGAPLKGLVRVTEGEDDKFIGMGEIDDEGRVAPRRLVVDYPA | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | A9N730 |
P36244 | TRMD_SERMA | tRNA [GM37] methyltransferase | Serratia | MFIGIVSLFPEMFRAITDYGVTGRAVKNGLLSVQCWSPRDFTYDRHRTVDDRPYGGGPGMLMMVQPLREAIHAAKAAAGEGAKVIYLSPQGRKLDHTGVCELAANQKMILVCGRYEGIDERVIQTEIDEEWSIGDYVLSGGELPAMTLIDSVARFIPGVLGHQASAEEDSFADGLLDCPHYTRPEVLEGMEVPPVLLSGNHAEIRRWRLKQSLGRTWLRRPELLESLALTDEQAVLLAEFQREHQARQQDYEGNV | Specifically methylates guanosine-37 in various tRNAs. | P36244 |
Q5LBZ2 | TRPA_BACFN | Tryptophan synthase alpha chain | Bacteroides | MNRINQLFDSNPRDLLSIYFCAGYPTLEGTTEVIRTLEKHGVNMIEIGIPFSDPMADGMVIQNAATQALRNGMSLRLLFEQLHDIRRDVKIPLILMGYLNPIMQFGFDNFCRQCAECGIDGVIIPDLPFKDYQEHFRTIAERYDVKVIMLITPETSEERVREIDEHTDGFIYMVSSAATTGAQQDFDGQKRAYFKKIEKMNLRNPRMVGFGISNEATFRAACENASGAIIGSRFVTLLHEEKNPEKAITRLKAILNLSSNDLR | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | Q5LBZ2 |
Q9F7B2 | WZB_SALTY | Low molecular weight protein-tyrosine-phosphatase Wzb | Salmonella | MFNKILVVCVGNVCRSPTAERLLKRFHPSLTVASAGLGALVGKGADPAAASVASAHDLSLENHCARQISARLCREYDLILTMEKRHIAALCDIAPEMRGKVMLFGHWDSEREIPDPYRKSRDAFEAVYTLLERSARQWAQALNAEQGKP | Dephosphorylates Wzc. Required for the extracellular polysaccharide colanic acid synthesis. Probably involved in the export of colanic acid from the cell to medium. Involved in protection of cells against contact-dependent growth inhibition (CDI). | Q9F7B2 |
Q92956 | TNR14_HUMAN | Tumor necrosis factor receptor-like 2 | Homo | MEPPGDWGPPPWRSTPKTDVLRLVLYLTFLGAPCYAPALPSCKEDEYPVGSECCPKCSPGYRVKEACGELTGTVCEPCPPGTYIAHLNGLSKCLQCQMCDPAMGLRASRNCSRTENAVCGCSPGHFCIVQDGDHCAACRAYATSSPGQRVQKGGTESQDTLCQNCPPGTFSPNGTLEECQHQTKCSWLVTKAGAGTSSSHWVWWFLSGSLVIVIVCSTVGLIICVKRRKPRGDVVKVIVSVQRKRQEAEGEATVIEALQAPPDVTTVAVEETIPSFTGRSPNH | (Microbial infection) Acts as a receptor for Herpes simplex virus 2/HHV-2. | Q92956 |
B2IP44 | VATB_STRPS | V-ATPase subunit B | Streptococcus | MSVIKEYRTASEVVGPLMIVEQVNNVSYNELVEIQLHNGEIRRGQVLEIHEDKAMVQLFEGSSGINLEKSKIRFAGHALELAVSEDMVGRIFNGMGKPIDGGPDLIPEKYLDIDGQAINPVSRDYPDEFIQTGISSIDHLNTLVRGQKLPVFSGSGLPHNELAAQIARQATVLNSDENFAVVFAAMGITFEEAEFFMEELRKTGAIDRSVLFMNLANDPAIERIATPRIALTAAEYLAFEKDMHVLVIMTDMTNYCEALREVSAARREVPGRRGYPGYLYTNLSTLYERAGRLVGKKGSVTQIPILTMPEDDITHPIPDLTGYITEGQIILSHELYNQGYRPPINVLSSLSRLKDKGSGEGKTRGDHAPTMNQLFAAYAQGKKVEELAVVLGESALSDVDKLYVRFTKRFEEEYINQGFYKNRNIEDTLNLGWELLSILPRTELKRIKDDLLDKYLPLVEV | Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit. | B2IP44 |
A9BWD4 | UPP_DELAS | UPRTase | Delftia | MSTLHLIDHPLVQHKLTLMRRKEASTNSFRRMLGELSTLMAYEITRDMPLQDIEIETPLETMTGKVIDGKKLVLVSILRAGNGFLDGMLNVVPGARIGHIGLYRDPETLQPVEYYFKMPSEMEERDVLVVDPMLATGNSAAAAVARLKQLNPKSIKFMCLLAAPEGVATMQKAHPDVDIYTAAVDRQLDAHGYILPGLGDAGDRIFGTK | Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. | A9BWD4 |
Q9VMK1 | UCP4C_DROME | Mitochondrial uncoupling protein 4C | Sophophora | MDKAERDYWHLRSLEIEEEPRFPPTNVADPLTARNLFQLYVNTFIGANLAESCVFPLDVAKTRMQVDGEQAKKTGKAMPTFRATLTNMIRVEGFKSLYAGFSAMVTRNFIFNSLRVVLYDVFRRPFLYQNERNEEVLKIYMALGCSFTAGCIAQALANPFDIVKVRMQTEGRRRQLGYDVRVNSMVQAFVDIYRRGGLPSMWKGVGPSCMRACLMTTGDVGSYDISKRTFKRLLDLEEGLPLRFVSSMCAGLTASVLSTPADVIKSRMMNQPVDESGKNLYYKNSLDCVRKLVREEGVLTLYKGLMPTWFRLGPFSVLFWLSVEQLRQWEGQSGF | Mitochondrial protein that is likely to be responsible for thermogenic respiration. Likely to function in mitochondrial uncoupling i.e. creating mitochondrial proton leaks across the inner mitochondrial membrane and can therefore dissipate the mitochondrial proton gradient and convert the energy of substrate oxidation into heat instead of ATP. Involved in cold tolerance, it is required for development to the adult stage at low temperatures. | Q9VMK1 |
E9Q6P5 | TTC7B_MOUSE | Tetratricopeptide repeat protein 7B | Mus | MATRKAGSRLETEIERCRSECQWERIPELVKQLSAKLIANDDMAELLLGESKLEQHLKEKPLRQGASPRGPRPQLTEVRKHLTAALDRGNLKSEFLQESNLVMAKLTYVEGDYKEALNIYARVGLDDLPLTAVPPYRLRMIAEAYATKGLCLEKLPVSSSTSNLHVDREQDVITCYEKAGDIALLYLQEIERVMLTNIQNRSPKPGPAPHDQELGFFLETGLQRAHVLYFKNGNLTRGVGRFRELLRAVETRTTQNLRMTIARQLAEILLRGMCEQSYWSPLEEPPYQSPLDDPLRKGANTKAYTLPRRARVYSGENIFCPQENTEEALLLLLISESMANRDAVLSRIPEHKSDRLISLQSASVVYDLLTIALGRRGQYEMLSECLERAMKFAFEEFHLWYQFALSLMAAGKSARAVKVLKECIRLKPDDATIPLLAAKLCVGSLHWLEEAEKFAKTVVDVGEKTSEFKAKGYLALGLTYSLQATDASLRGMQEGLQRKALLAFQRAHSLSPTDHQAAFYLALQLAISRQIPEALGYVRQALQLQGDDANSLHLLALLLSAQKHYHDALNIIDMALSEYPENFILLFSKVKLESLCRGPDEALLTCKHMLQIWKSCYNLTNPSDSGRGSSLLDRTIADRRQLNTITLPDFSDPETGSVHATSVAASRVEQALSEVASSLQSSAPKQGPLHPWMTLAQIWLHAAEVYIGIGKPAEATACTQEAANLFPMSHNVLYMRGQVAELRGHFDEARRWYEEALSISPTHVKSMQRLALVLHQLGRYSLAEKILRDAVQVNSTAHEVWNGLGEVLQAQGNDAAATECFLTALELEASSPAVPFTVIPRVL | Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis. In the complex, plays a central role in bridging PI4KA to EFR3B and FAM126A, via direct interactions. | E9Q6P5 |
P38627 | URA8_YEAST | UTP--ammonia ligase 2 | Saccharomyces | MKYVVVSGGVISGIGKGVLASSTGMLLKTLGLKVTSIKIDPYMNIDAGTMSPLEHGECFVLDDGGETDLDLGNYERYLGITLSRDHNITTGKIYSHVISRERRGDYLGKTVQIVPHLTNAIQDWIQRVSKIPVDDTGLEPDVCIIELGGTVGDIESAPFVEALRQFQFEVGRENFALIHVSLVPVIHGEQKTKPTQAAIKDLRSLGLIPDMIACRCSEELNRSTIDKIAMFCHVGPEQVVNVHDVNSTYHVPLLLLKQHMIDYLHSRLKLGEVPLTLEDKERGSQLLTNWENMTKNLDDSDDVVKIALVGKYTNLKDSYLSVTKSLEHASMKCRRQLEILWVEASNLEPETQEVDKNKFHDSWNKLSSADGILVPGGFGTRGIEGMILAAKWARESGVPFLGVCLGLQVAAIEFARNVIGRPNSSSTEFLDETLLAPEDQVVIYMPEIDKEHMGGTMRLGLRPTIFQPNSEWSNIRKLYGEVNEVHERHRHRYEINPKIVNDMESRGFIFVGKDETGQRCEIFELKGHPYYVGTQYHPEYTSKVLEPSRPFWGLVAAASGTLGEVIKDINLSEGNENE | Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Plays an important role in the regulation of phospholipid synthesis. | P38627 |
Q6NME7 | TEN1_ARATH | Protein telomeric pathways with STN1 homolog | Arabidopsis | MAKSQIEPGVPITLQELYPSSLFYKEGVSLRVTAMLRGYSVETAIGVIEDGGRSLKINTQNIRDVSFRVGSIYQFIGELHIEQPNNEAILQARTGRNVDGIDMNLYRKTIELLRQFLKEEDNSNMVE | Required for the maintenance of meristems and stem cells through the reduction of DNA damage . Promotes telomere integrity by maintaining telomere length and proper architecture of the chromosome terminus . Negatively regulates telomerase repeat addition processivity . Hampers contacts between enzymatically active telomerase and CST complex . | Q6NME7 |
Q8U4K3 | WTPC_PYRFU | Molybdate/tungstate import ATP-binding protein WtpC | Pyrococcus | MLEVQGISKKWKDFHLKDISFSVMDGEYFIVLGPSGAGKTVLLEIIAGIIPPDGGKVLLDGKDITLLPPEKRGIAYVPQNYALFPNMSVFDNIAFGLKVRRVPRSEIEKRVLEISEVLGIRHLLHRKPRTLSGGEQQRVAVARALVIEPEIILLDEPFANLDVQIRSRLINEMKRWRRELGFTAIHVTHSFEEALALGDRVGIMLNGKLVQVGEIREVFSRPNSEEVAKFLGFENIIEGIADGRVLHVGKLRIELPLEAKGRVRIGIRPEDILISTERIKTSARNVFKAKVEAIEDVGPLVKLTLNVCDITLRAFITRSSLVELGIEEGKEVYASFKASAIHVF | Part of the ABC transporter complex WtpABC involved in molybdate/tungstate import. Probably responsible for energy coupling to the transport system. | Q8U4K3 |
A6VT87 | TSAC_MARMS | tRNA threonylcarbamoyladenosine biosynthesis protein TsaC | Marinomonas | MHLVTSVEELADIIRQGGVIAYPTEAVWGLGCDPFNESAVRRILTLKSRPESKGLILVAGAQEELSPWLNLLDDKAAQRLISLNETPTSWVVPDTTITPSWVRGEHQSVAIRLSQHQPVQRLCAAFQGVIVSTSANPAGLEPAMSAKEVHQYFGCNIDAIFDAPLGDASQPSQVRDILTDNLFRA | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. | A6VT87 |
B6ELG6 | YACG_ALISL | DNA gyrase inhibitor YacG | Aliivibrio | MSQPNSQQPTIVKCPTCQNKVVWNTESEFRPFCSKKCQMIDFGEWADEEKSIAGAPDMSDSDGWSSEPY | 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. | B6ELG6 |
C3YZ51 | UBA5_BRAFL | Ubiquitin-like modifier-activating enzyme 5 | Branchiostoma | MATVEELQTRVKQLEEELERERTRNRGGTDGGGGRKKIDQMSSEVVDSNPYSRLMALKRMGIVDNYERIRDFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEITLRDINPDVEFETHNYNITTVDNFQHFMDRISHGHLKGDRPVDLVLSCVDNFEARMAINTACNEQGQVWIESGVSENAVSGHIQVIKPGETACFACAPPLVVASGIDEKTLKREGVCAASLPTTMGIVAGFLVQNTLKYLLEFGSVTYYLGYNAMQDFFPSMAMKPNPNCDDSFCTKLQTEYQEKLLAQPKEEAKEETVEEVVHDANDWGIELVAETTEEELKAASHGHVPELVEGVHVAYVRPMTQEDEEGAAGLTVDDQESLEDLMAKMKSI | E1-like enzyme which activates UFM1. | C3YZ51 |
B6DCT5 | TX403_LYCSI | Toxin-like structure LSTX-C3 | Lycosa | MKVLVLFSVLFLTLFSYSSTEAIDEFDSDAEDDMLSLMANEQVRAKACTPRLHDCSHDRHSCCRGELFKDVCYCFYPEGEDITEVCSCQQPKSHKYIEKVVDKAKTVVG | Enhances the high-affinity desensitization of human P2RX3 purinoceptors. | B6DCT5 |
Q4A6N9 | TMCAL_MYCS5 | tRNA(Met) cytidine acetate ligase | Mycoplasmopsis | MLINKNLKIGIVVEYNPFHNGHIYQLNWIKNNYPNSKIIIVMSHKYSQRGEIICMPFWKRKLWAKKYDVSKVLKLSTRKTIQAAHIFAQNAIQKLNKEKIDILVFGSESTNDSLMLKIATFIKENKEIYNQTLKKNLKGGNSFPKANFLTLKELTNEDFSLPNDILGFEYIKQIVENNYKIQPIAIKRSVGFHSEEPSDEFASASLIRKMLKDGRDVSKYTPVDLKQIPTKLLIENTFLKFKKYILKTPASKLKKYLLVDEGIENLFKKNILLFDNYHDFIDACVSRRYTRSKIMRTYLCILLKIKK | Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34. | Q4A6N9 |
A5VJH6 | YBEY_LIMRD | Endoribonuclease YbeY | Limosilactobacillus | MDLEIFDQTTAQLPNEQLEMVRDLLQYAAKELSLSENTEMSLTFVNNPEIKKLNAQYRNVDRATDVLSFAAEEAGDETPIIMDPEMAAEIPVNLGDLFISIDKVAEQAKFLGHSVDRELGFLAVHGFLHLNGYDHEEPADEEKMFKLQREILDGYGLTR | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | A5VJH6 |
Q2NKZ1 | TCPH_BOVIN | CCT-eta | Bos | MMPTPVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKEDKVEQRKLLEKCAMTALSSKLISQQKAFFAKMVVDAVMMLDDLLQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAGFEMQPKKYHNPMIALLNVELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALSSDVLGRCQVFEETQIGGERYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMWYGVDINTEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIKNPRSTVDASPAAGRGRGRGRLH | Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. The TRiC complex plays a role in the folding of actin and tubulin. | Q2NKZ1 |
Q7X222 | TPIS_KLEPN | Triose-phosphate isomerase | Klebsiella | MRHPLVMGNWKLNGSRHMVNELVANLRTELAGVSGCAVAIAPPEMYLDLAKRAAEGSHIHLGAQNVDVNLSGAFTGETSAEMLKDIGAQYIIIGHSERRTYHKESDELIAKKFAVLKEQGLTPVLCIGETEAENEAGKTEEVCARQIDAVLKTQGAAVFEGVVIAYEPVWAIGTGKSATPAQAQAVHKFIRDHIAKADAKIAEQVIIQYGGSVNAGNAAELFTQPDIDGALVGGASLKADAFAVIVKAAEAAKKA | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | Q7X222 |
Q96TU8 | TBB_UROFA | Beta-tubulin | Uromyces | MREIVHLQTGQCGNQIGAKFWEVVSDEHGIATDGQYKGNTDLQLERISVYYNEVAANKYVPRAVLIDLEPGTMDSVRSGAFGSLFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSPKVSDTVVEPYNATLSVHQLVENSDETFCIDNEALYDICFRTLKLATPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHFFMVGFAPLTARGSQQYRAITVPELTSQMFDAKNMMAASDPRHGRYLTVAAYFRGKVSMKEVEENMLSVQNKNSNYFVEWIPNNVQTAHCDIAPRAHKMSVTFIGNSTAIQDLFKRVADQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMQDLVAEYQQYQEAHMDDEEAEEAYEDEAPPEE | 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. | Q96TU8 |
Q6MQH6 | TRUA_BDEBA | tRNA-uridine isomerase I | Bdellovibrio | MTTKVRFTVAYDGTGFCGWQKQKPEDQISVAQVIEEALSKVFNEKITLFASGRTDAGVHALNQVCHFSTHRKIDPNKKWDLCWALNSHLPPSIVAKKAWIAPDDFHATLSATHKTYRYLIVNKPRPSAHLNRYADWVRLPIDIEHLQESSKYLLGNQDFKSFQSVGTPVPDTVREIYKADWEWRKPGVMQFTITGSGFLKQMVRNIVGTSLFLERKGLDPSKMQEIIAAQDRMKAGPPAPAQGLYLMKVYYPQDLDNRCLEL | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | Q6MQH6 |
Q1LIP2 | ZAPD_CUPMC | Z ring-associated protein D | Cupriavidus | MILYEYPFNERIRTLLRLEDLFDRLDYFLGQEHPLQHHVAITTIFEIIDVAGRADLKTDLIKELERQRQALAPLRSNPQIDQDALVAVITEIEQGIAALSQTVGKAGQLLADNEWLTSIRSRAIIPGGTCEFDLPAYYAWQHRDADDRRADILKWARPLASLRMGAGIVLRLLRESGQSGKVIATGGSYQQMLSGRSYQLMQVYLDESLLAFIPEMSANKYMLWVRFTQQDGDMRPRSVDADIPFLLKLCNF | Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity. | Q1LIP2 |
Q8ZRN5 | TILS_SALTY | tRNA(Ile)-lysidine synthetase | Salmonella | MTTLTLNTSLLSSRRILAAFSGGLDSTVLLHQLVLWRERHPDVTLRAIHIHHGLSPHADSWVRHCETVCERWQVPLVVERVTLADNGLGIEAHAREARYRAFAQTLLPGEVLATAQHLDDQCETFLLALKRGSGPAGLSAMGERSPFAGTLLLRPLLRETRKTLEQWAVRHGLCWIEDESNQDDAYDRNFLRLRALPLLQQRWPHFPAAVARSATLCAEQERLLDELLASDLTDCITAEGTLRLSPLMSMSDVRRAAILRRWLAMRNAPMPSRDALERIWQEVALARDDASPCLRFGDHEIRRYQSQLWWIKSVAGQHETTVAWPVWQTPLALPAGLGTVQLVPGGELRRPREEESVSIRFKAPGVLHIVGRNGGRKLKKIWQEQGIPPWRRDTTPLLFYGETLIAAAGVFVTREGAAEDKEGVSLVWHA | 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. | Q8ZRN5 |
Q9Y5Q8 | TF3C5_HUMAN | Transcription factor IIIC subunit epsilon | Homo | MAAEAADLGLGAAVPVELRRERRMVCVEYPGVVRDVAKMLPTLGGEEGVSRIYADPTKRLELYFRPKDPYCHPVCANRFSTSSLLLRIRKRTRRQKGVLGTEAHSEVTFDMEILGIISTIYKFQGMSDFQYLAVHTEAGGKHTSMYDKVLMLRPEKEAFFHQELPLYIPPPIFSRLDAPVDYFYRPETQHREGYNNPPISGENLIGLSRARRPHNAIFVNFEDEEVPKQPLEAAAQTWRRVCTNPVDRKVEEELRKLFDIRPIWSRNAVKANISVHPDKLKVLLPFIAYYMITGPWRSLWIRFGYDPRKNPDAKIYQVLDFRIRCGMKHGYAPSDLPVKAKRSTYNYSLPITVKKTSSQLVTMHDLKQGLGPSGTSGARKPASSKYKLKDSVYIFREGALPPYRQMFYQLCDLNVEELQKIIHRNDGAENSCTERDGWCLPKTSDELRDTMSLMIRQTIRSKRPALFSSSAKADGGKEQLTYESGEDEEDEEEEEEEEEDFKPSDGSENEMETEILDYV | 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. | Q9Y5Q8 |
Q9SMJ3 | ZDS_CAPAN | Carotene 7,8-desaturase | Capsicum | MATCSAYLCCPATSASLKKRVFPDGSAGFLFFGGRRLSNRLVTPKSVIRADLNSMVSDMSTNAPKGLFPPEPEHYRGPKLKVAIIGAGLAGMSTAVELLDQGHEVDIYESRTFIGGKVGSFVDKRGNHIEMGLHVFFGCYNNLFRLMKKVGAEKNLLVKEHTHTFVNKGGEIGELDFRFPVGAPLHGINAFLSTNQLKTYDKARNAVALALSPVVRALVDPDGALQQIRDLDSVSFSDWFMSKGGTRASIQRMWDPVAYALGFIDCDNISARCMLTIFALFATKTEASLLRMLKGSPDVYLSGPIKKYIIDKGGRFHLRWGCREVLYETSSDGSMYVSGLAMSKATQKKIVKADAYVAACVVPGIKRLVPQKWRELEFFGNIYKLIGVPVVTVQLRYNGWVTELQDLERSRQSKRATGLDNLLYTPDADFSCFADLALASPEDYYIEGQGSLLQCVLTPGDPYMPLPNEEIIRRVSKQVLALFPSSQGLEVTWSSVVKIGQSLYREGPGKDPFRPDQKTPVENFFLAGSYTKQDYIDSMEGATLSGRQASAYICDAGEQLLALRKKIAAAELNEISKGVSLSDELSLV | Catalyzes the conversion of zeta-carotene to lycopene via the intermediary of neurosporene. It carries out two consecutive desaturations (introduction of double bonds) at positions C-7 and C-7'. Shows stereoselectivity toward trans C15-C15'zeta-carotene double bond. The zeta-carotene produced by the phytoene desaturase PDS has a C15-C15' double bond in the cis configuration and it requires isomerization before being recognized as substrate by ZDS. No activity with all-trans-zeta-carotene. The main product is 7,9,7',9'-tetra-cis-lycopene (pro-lycopene). | Q9SMJ3 |
Q8XX97 | TSAD_RALSO | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Ralstonia | MLVLGIESSCDETGVALYDTDAGLRAHALYSQIAMHRDYGGVVPELASRDHIRRVIPLLEDVLAEAGVGRADIDAIAYTKGPGLAGALLVGASVANALGFALGKPLVGVHHLEGHLLSPLLEADRPAFPFLALLVSGGHTQLMRVDAVGQYTLLGETLDDAAGEAFDKTAKLLGLGYPGGPAVSRLAEFGNPGAFELPRPMLHSGNFDFSFAGLKTAVLTQVRKLNLDGGEACEQPRADLARAFVDAIVDVLVAKTLRAAREHGLKRIVVAGGVGANRQLRERLNAEGGKRGLRVYYPDLQFCTDNGAMIAFAGAMRLQADPGQVQSGYGYGVTPRWDLEDIRIRQA | 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. | Q8XX97 |
Q39QX7 | UPPP_GEOMG | Undecaprenyl pyrophosphate phosphatase | Geobacter | MNPLHATVLGAIQGLTEVLPVSSSAHLILIPWLFGWPESGITFDVALHLGTLIALALYFRRDIAELVVNALSGLTGGAHSSATRLPWYIIAGCVPAAIVGKTLEEPIEAIFRANPAIIAAFLIGFGLLLALADTLGSKKSRMDQIDLKNAMMIGLAQCLALLPGVSRSGITITAALFLGFSRETAARFSFLLSLPIVAGAALLKVGHLVRHGVPEGELQPLLIGVGVSAVFGYVSVALLLKLVQRYSLYPFVWYRLLAGAGVLLFIFNQ | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | Q39QX7 |
B8EBP1 | TRMD_SHEB2 | tRNA [GM37] methyltransferase | Shewanella | MWLGVITLFPEMFRAVTDFGVTGRAVKNGLLELHTWNPRDFTHDRHNTVDDRPYGGGPGMLMMVQPLRDAIHAAKAAAGEGAKVIYLSPQGRKLDQQGVTELAQSSRLILVCGRYEGIDERIIQTEVDEEWSIGDYVLSGGELPAMTLIDSVSRLVPGVLGKQASAEQDSFSDGLLDCPHYTRPESLDGVDVPAVLLSGNHEQIRLWRLQQSLGRTLLRRPELLQNLALTDEQTTLLAQFVEAMNKHA | Specifically methylates guanosine-37 in various tRNAs. | B8EBP1 |
Q54YZ0 | UGPA2_DICDI | UDP-glucose pyrophosphorylase 2 | Dictyostelium | MMKPDLNSPLPQSPQLQAFGSRSSDLATEDLFLKKLEAISQTAPNETVKNEFLNKEIPSINKLFTRFLKNRKKVIDWDKINPPPADMVLNYKDLPAITEQRTSELASKLAVLKLNGGLGTTMGCTGPKSVIEVRSEKTFLDLSVQQIKEMNERYNIKVPLVLMNSFNTHQETGKIIQKYKYSDVKIHSFNQSRFPRILKDNLMPVPDKLFGSDSEWYPPGHGDVFFALQNSGLLETLINEGKEYLFISNVDNLGAVVDFNILEAMDKNKVEYIMEVTNKTRADVKGGTLIQYEGKAKLLEIAQVPSSKVEEFKSIKKFKIFNTNNIWVNLKAMDRILKQNLLDDMDIIINPKVADGKNIIQLEIAAGAAIEFFNNARGVNVPRSRFLPVKSTSDLFIVQSNLYSLEKGVLVMNKNRPFTTVPLVKLGDNFKKVSDYQARIKGIPDILELDQLTVSGDITFGPNMVLKGTVIIVANHGSRIDIPEGSEFENKVVSGNLHCGAL | Plays a central role as a glucosyl donor in cellular metabolic pathways. | Q54YZ0 |
Q2V6K0 | UFOG6_FRAAN | Flavonol 3-O-glucosyltransferase 6 | Fragaria | MKKASELIFIPIPGIGHIVSTVEIAKLLLCRDDNLFITILIMKFPFTADGSDVYIKSLAVDPSLKTQRIRFVNLPQEHFQGTGATGFFTFIDSHKSHVKDAVTRLMETKSETTRIAGFVIDMFCTGMIDLANEFGLPSYVFYTSGAADLGLMFHLQALRDEENKDCTEFKDSDAELVVSSFVNPLPAARVLPSVVFEKEGGNFFLNFAKRYRETKGILVNTFLELEPHAIQSLSSDGKILPVYPVGPILNVKSEGNQVSSEKSKQKSDILEWLDDQPPSSVVFLCFGSMGCFGEDQVKEIAHALEQGGIRFLWSLRQPSKEKIGFPSDYTDYKAVLPEGFLDRTTDLGKVIGWAPQLAILAHPAVGGFVSHCGWNSTLESIWYGVPIATWPFYAEQQVNAFELVKELKLAVEIDMGYRKDSGVIVSRENIEKGIKEVMEQESELRKRVKEMSQMSRKALEEDGSSYSSLGRFLDQIQTS | Broad spectrum multifunctional glucosyltransferase. Catalyzes the formation of flavonol 3-O-glucosides during fruit ripening. Accepted substrates include several flavonoids, hydroxycoumarins and beta-naphthols. Uses UDP-Glc as a sugar donor, but not UDP-Gal or UDP-GlcUA. May also be involved in detoxification of xenobiotics. | Q2V6K0 |
Q5R6F3 | ZN512_PONAB | Zinc finger protein 512 | Pongo | MSSRLGAVPATSGPTTFKQQRSTRIVGAKNSRTQCSIKDNSFQYTIPHDDSLSGSSSASSCEPVSDFPASFRKSAYWMKMRRIKPAATSHVEGSGGVSAKGKRKPRQEEDEDYREFPQKKHKLYGRKQRPKTQPNPKSQARRIRKEPPVYAAGSLEEQWYLEIVDKGSVSCPTCQAVGRKTIEGLKKHMENCKQEMFTCHHCGKQLRSLAGMKYHVMANHNSLPILKAGDEIDEPSERERLRTVLKRLGKLRCMRESCSSSFTSIMGYLYHVRKCGKGAAELEKMTLKCHHCGKPYRSKAGLAYHLRSEHGPISFFPESGQPECLKEMNLESKSGGRVQRRSAKIAVYHLQELASAELAKEWPKRKVLQDLVPDDRKLKYTRPGLPTFSQEVLHKWKTDIKKYHRIQCPNQGCEAVYSSVSGLKAHLGSCTLGNFVAGKYKCLLCQKEFVSESGVKYHINSVHAEDWFVVNPTTTKSFEKLMKIKQRQQEEEKRRQQHRSRRSLRRRQQPGIELPETELSLRVGKDQRRNNEELVVSASCKEPEQEPVPAQFQKVKPPKTNHKRGRK | May be involved in transcriptional regulation. | Q5R6F3 |
P21733 | YCR2_BACTK | ORF2 | Bacillus cereus group | MLKYHFPNVCEDELINIYSYGDFKGQGKYICLFKIENQSFLFWRNDKGNKIYTNLESISVEIINTNNTYNQSQNVCPQDLVDTYNQSQNVCPQDLVDTYNQSQNVCPQDLVDTYNQSQNVCPQDLVDTYNQSQNVCPQDLVDTYNQSQNVCPQDLVDTYNQSQNVYTQDLIDTYNQSQNVCPQDLVDTYNQSQNVCPQDLVDTYNQSQNVCPQDLVDTYNQSQNVCPQDLNVYTQDLIDTYNQSQNCDCGCK | A protein probably derived from this gene is found in cuboidal crystalline inclusions, but is not toxic even when coexpressed with upstream ORF1. The protein runs anomalously as a 50 kDa band in gels. | P21733 |
C3N6D4 | VATB_SULIA | V-ATPase subunit B | Sulfolobus | MLSVREFSNISMIKGPLIYVQGVTDASYNELVEIEMPNGEKRRGLVIDSQMGIAIVQVFEGTTGVSPTGTKIRMLGRGLEVKISEEMLGRIFNPLGDSLDNGPPVIKGEKRDINGSPLNPAAREYPEEFIQTGISAIDGLNALLRGQKLPIFSGSGLPANMLAAQIAKQATVRGEESNFAVVFAAIGARYDDALFFRKFFEETGAINRVAMIVSLANEPPVMKTLTPKTALTLAEYLAFEQDMHVLAILIDMTNYCEALREISAAREEVPGRGGYPGYMYTDLATIYERAGKVLGKKGSITQMPILTMPNDDITHPIPDLTGYITEGQIVLDRALYNKGIYPPINVLMSLSRLAKDGIGEGKTRDDHKDVSNQLFASYARAVDTRGLAAIIGEDSLSEVDRKYLLFGELFERKFVSQGFNENRDIETTLDIGWEILSVLPESELTNIKTQYIKKYHPNYRGKK | Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory subunit. | C3N6D4 |
P75992 | YMGA_ECOLI | Probable two-component-system connector protein YmgA | Escherichia | MKTSDNERIKYEITGQAVLQILRMKINFSLQTLIKQLLVMKSAEEDAFRRDLIDSIIRDFSNSDSGGPNRRTATADNKSMFNGKKINRIH | Probably a connector protein for RcsB/C regulation of biofilm formation, providing additional signal input into the two-component signaling pathway. May serve to stimulate biofilm maturation, probably via the Rcs phosphorelay. Mild overexpression at 16 degrees Celsius increases the production of colanic acid, an exopolysaccharide and matrix component, and reduces adhesive curli fimbriae expression. Both of these effects require RcsB. | P75992 |
Q5T0D9 | TPRGL_HUMAN | Protein FAM79A | Homo | MLQLRDSVDSAGTSPTAVLAAGEEVGAGGGPGGGRPGAGTPLRQTLWPLSIHDPTRRARVKEYFVFRPGSIEQAVEEIRVVVRPVEDGEIQGVWLLTEVDHWNNEKERLVLVTEQSLLICKYDFISLQCQQVVRIALNAVDTISYGEFQFPPKSLNKREGFGIRIQWDKQSRPSFINRWNPWSTNVPYATFTEHPMAGADEKTASLCQLESFKALLIQAVKKAQKESPLPGQANGVLILERPLLIETYVGLMSFINNEAKLGYSMTRGKIGF | Presynaptic protein involved in the synaptic transmission tuning. Regulates synaptic release probability by decreasing the calcium sensitivity of release. | Q5T0D9 |
B2GI05 | UREE_KOCRD | Urease accessory protein UreE | Kocuria | MIVTEILGNIHEDSGRELVAGRHVEKVVLPSAELVKRIQRLRTDHDRQIGLRLPAGAPDLRDGDVVAVEDAAPSGAGHGDGEQDGTGAPGRGNAVVIQVLPTDVLVIGARSVVEMAFVAHSLGNRHLQAQFFDADSEYGAEVMVVQYDHTVQDFLDHHGVPYSRQERVMPVPFRHAEHTH | Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. | B2GI05 |
Q3KMZ5 | TRMD_CHLTA | tRNA [GM37] methyltransferase | Chlamydia | MEIDILSLFPDYFASPLQATILGRAIKQGALSVRSRDIREFGLGKWKQVDDSPYNGEGMLLMAEPVVQAIRSIRRKKSKVIYLSPQGQLLSAKKSRELASCSHLVLLCGHYEGIDERALTAEVDEEISIGDYVLTNGCAAALVLVDALARFIPGVLGNQESAEYDSLENGLLEGPQYTRPRVFEGESVPEVLLCGDHQKIADWRKQVSLERTRERRPDLYLQYFYGNSACLSTQEDLPRIEVVSPKTFSVVLEVQDLRKAKKFYSRMFGKECWDGDKLFLLGKTSLYLQQTKETRGPTTVFIELETDHDFVRFLKRWEMLGGELGEQGTGGFPLRQVFDLDGHIWVVSCVQK | Specifically methylates guanosine-37 in various tRNAs. | Q3KMZ5 |
Q9Z0W1 | TNR16_MOUSE | Low-affinity nerve growth factor receptor | Mus | MRRAGAACSAMDRLRLLLLLLLLLGVSFGGAKETCSTGMYTHSGECCKACNLGEGVAQPCGANQTVCEPCLDSVTFSDVVSATEPCKPCTECLGLQSMSAPCVEADDAVCRCSYGYYQDEETGRCEACSVCGVGSGLVFSCQDKQNTVCEECPEGTYSDEANHVDPCLPCTVCEDTERQLRECTPWADAECEEIPGRWITRSTPPEGSDVTTPSTQEPEAPPERDLIASTVADTVTTVMGSSQPVVTRGTADNLIPVYCSILAAVVVGLVAYIAFKRWNSCKQNKQGANSRPVNQTPPPEGEKLHSDSGISVDSQSLHDQQTHTQTASGQALKGDGNLYSSLPLTKREEVEKLLNGDTWRHLAGELGYQPEHIDSFTHEACPVRALLASWGAQDSATLDALLAALRRIQRADIVESLCSESTATSPV | Does not bind NGF, BDNF, NTF3, and NTF4. | Q9Z0W1 |
C0HLF5 | TOP1B_OXYTA | Oxyopinin-1b | Oxyopes | FRGLAKLLKIGLKSFARVLKKVLPKAAKAGKALAKSLADENAIRQQNQ | Disrupts cell membranes, particularly those rich in phosphocholine, through formation of pores. Has antimicrobial activity, hemolytic activity and insecticidal activity. | C0HLF5 |
P78811 | UGPA1_SCHPO | UDP-glucose pyrophosphorylase | Schizosaccharomyces | MDLAPRPLGRQHSKSQSAFAFDNTATSIAASTMKNELNHLASTVKDPLAKKAFQKEMDNFFSLFSRYLQEDARGSEINWDLVESPKPEQVVEYDTITEAGGLSRDYLNKLAVLKLNGGLGTTMGCVGPKSIIEVRDGNSFLDLSVRQIEHLNRKYNVNVPFVLMNSFNTDEATAKVIKKYEAHKIDILTFNQSRYPRVHKETLLPVPHTADSAIDEWYPPGHGDVFEALTNSGIIDTLIAQGKEYLFVSNIDNLGAVVDLNILNHMVETNAEYLMELTNKTKADVKGGTLIDYDGNVRLLEIAQVPPQHVEEFKSIKKFKYFNTNNLWFHLPSVKRVVNNHELSMEIIPNKKTIKHKGENINIIQLETAAGAAIRHFKNAHGVNVPRRRFLPVKTCSDLLLVKSDLYSINHGQVEMNPRRFGGTAPLVKLGAHFKKVADFSAHIPSIPKILELDHLTITGDVNIGRNVTLKGTVIIVASDANRIDIPNGSVLENCVITGNLNILEH | Plays a central role as a glucosyl donor in cellular metabolic pathways. | P78811 |
A2T7D2 | ZKSC5_PANTR | Zinc finger protein 95 homolog | Pan | MIMTESREVIDLDPPAETSQEQEDLFIVKVEEEDCTWMQEYNPPTFETFYQRFRHFQYHEASGPREALSQLRVLCCEWLRPELHTKEQILELLVLEQFLTILPEEFQPWVREHHPESGEEAVAVIENIQRELEERRQQIVACPDVLPRKMAPPGAVQESCSPQPLTVDTQPEQAPQKPRLLEENALPVLQVPSLPLKDSQELTASLLSTGSQKLVKIEEVADVAVSFILEEWGHLDQSQKSLYRDDRKENYGSITSMGYESRDNMELIVKQISDDSESRWVAPEHTERSVPQDPDFAEVSDLKGMVQRWQVNPTVGKSRQNPSQKRDLDAITDISPKQSTHGERGHRCSDCGKFFLQASNFIQHRRIHTGEKPFKCGECGKSYNQRVHLTQHQRVHTGEKPYKCQVCGKAFRVSSHLVQHHSVHSGERPYGCNECGKNFGRHSHLIEHLKRHFREKSQRCSDKRSKNTKLSVKKKISEYSEADMELSGKTQRNVSQVQDFGEGCEFQGKLDRKQGIPMKEILGQPSSKRMNYSEVPYVHKKSSTGERPHKCNECGKSFIQSAHLIQHQRIHTGEKPFRCEECGKSYNQRVHLTQHQRVHTGEKPYTCPLCGKAFRVRSHLVQHQSVHSGERPFKCNECGKGFGRRSHLAGHLRLHSREKSHQCRECGEIFFQYVSLIEHQVLHMGQKNEKNGICEEAYSWNLTVIEDKKIELQEQPYQCDICGKAFGYSSDLIQHYRTHTAEKPYQCDICRENVGQCSHTKQHQKIYSSTKSHQCHECGRGFTLKSHLNQHQRIHTGEKPFQCKECGMNFSWSCSLFKHLRSHERTDPINTLSVEGSLL | May be involved in transcriptional regulation. | A2T7D2 |
Q9H3N1 | TMX1_HUMAN | Transmembrane Trx-related protein | Homo | MAPSGSLAVPLAVLVLLLWGAPWTHGRRSNVRVITDENWRELLEGDWMIEFYAPWCPACQNLQPEWESFAEWGEDLEVNIAKVDVTEQPGLSGRFIITALPTIYHCKDGEFRRYQGPRTKKDFINFISDKEWKSIEPVSSWFGPGSVLMSSMSALFQLSMWIRTCHNYFIEDLGLPVWGSYTVFALATLFSGLLLGLCMIFVADCLCPSKRRRPQPYPYPSKKLLSESAQPLKKVEEEQEADEEDVSEEEAESKEGTNKDFPQNAIRQRSLGPSLATDKS | May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. | Q9H3N1 |