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
|
|---|---|---|---|---|---|---|
P48367 | YCF17_CYAPA | ORF48 | Cyanophora | MQEERNIWNWGFTSGAENWNGRLAMLGFIAALLTESLTGQGTLHFLGIL | Possible role in chlorophyll and/or carotenoid binding. | P48367 |
O74863 | TRM82_SCHPO | Transfer RNA methyltransferase 82 | Schizosaccharomyces | MSEQRVFKHPCQFLTWNSKHNYIVCCSGPYLLGFSCSTGEKIFEHCYRDNINEKHREAAAYGEAIRQVAFSKDYSRMATVSEDKCLRLWDSTQPDKIELLYQKNIPKRCADLCFAGSNEIVFGDKFGDVYCVDENWFTTSEVTEEKKSNVVEGKQEPVNNDTLKDSKLQKLEPIMGHVSILTQLIVAQNPQNSKEEIIITSDKDEHIRISRFPNAFVIEGFCLGHEDFVSRMSLYDNRTLISGGGDNHVFVWDLENFKCLDAFDLRSAFSTYLSLNQPMVVSVILPIFKRQLVAFACEGMAGLIFAKVTPEKRLLFHSALKLSGPVLDAVLLDTDTDQILISLDSSFTFGACFECVKFDEGNAAVLTKPDVIKRIESDGLISTEKPFCPLAQIHTLRKNHSKFIRSVETGTSSPSVESKDN | Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit. | O74863 |
Q6PFM9 | WDR48_DANRE | USP1-associated factor 1 | Danio | MATLHRQNAAGRRKVQVSYVIRDEVEKYNRNGVNALQLDPALNRLFTAGRDSIIRIWSVNQHKQDPYIASMEHHTDWVNDIILCCNGKTLISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTASNNTVTTSSLSGNKDSIYSLAMNQTGTVIISGSTEKVLRVWDPRTCAKLMKLKGHTDNVKSLLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALQVNEAFTHIYSGGRDRKIYCTDLRNPDMRVLICEEKAPVLRMELDRSADPPQSIWVSTTKSFVNKWSLKAMHNFRASGDYDNDCSAPLTPLCTQPEQVIKGGTSIVQCHILNDKRHILTKDTNNSVAFWDVLKACKGEDLGKVDFDEEVKKRFKMVYVPNWFSVDLKTGMLTITLDESDCFAAWVAAKDAGFTSPDGSDPKLNLGGLLLQALLEFWPRTHINPMEEEENELNHVNGEQESRIQKGNGYFQVPPHTPVIFGEAGGRTLFRLLCRDSGGETESMLLNETVPQWVIDITVDKNMPKFNKIPFYLQPHSSSGAKTLKKDRLSASDMLQVRKVMEHVYEKIINLDTESQATSSSANDKPGEQEKEEDVSVMAEEKIELMCLDQVLDPNMDLRTVKHFIWKSGGDLTIHYRQKST | 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. 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. | Q6PFM9 |
Q971B6 | VATB_SULTO | V-ATPase subunit B | Sulfurisphaera | MSLLNVREYSNISMIKGPLIAVQGVSDAAYNELVEIEMPDGSKRRGLVVDSQMGVTFVQVFEGTTGISPTGSKVRFLGRGLEVKISEEMLGRIFNPLGEPLDNGPPVIGGEKRNINGDPINPATREYPEEFIQTGISAIDGLNSLLRGQKLPIFSGSGLPANTLAAQIAKQATVRGEESNFAVVFAAIGVRYDEALFFRKFFEETGAINRVAMFVTLANDPPSLKILTPKTALTLAEYLAFEKDMHVLAILIDMTNYCEALRELSASREEVPGRGGYPGYMYTDLATIYERAGKVIGKKGSITQMPILTMPNDDMTHPIPDLTGYITEGQIVLDRSLFNKGIYPPINVLMSLSRLMKDGIGEGKTRDDHKDLSNQLFAAYARAQDIRGLAAIIGEDSLSEVDRKYLLFAEAFERRFVAQGVNENRSIETTLDIGWEVLSILPESELSLIRSEYIKKYHPNYRGKK | Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory subunit. | Q971B6 |
B7I0F3 | TRPA_BACC7 | Tryptophan synthase alpha chain | Bacillus cereus group | MGVEKMKAAFENGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDGGVTLKGIFQALAEVRKEVQIPFVLMTYLNPVLAFGKEHFIERCLEAGVDGIIVPDLPYEEQDIIAPLLRTANIALIPLVTVTSPIERIEKITSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHTNLPVVAGFGISTKEHVEEMITICDGVVVGSKIIELLENEKREEICEFIQATKQKEEA | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | B7I0F3 |
B0UPF4 | TAM_METS4 | Trans-aconitate 2-methyltransferase | Methylobacterium | MADWNAAQYLKFADERTRPAADLLARVPLESPARVIDLGCGPGNSTALLCARFPRAAVTGLDSSPDMLATARERLPAVRFVEADLAGFTPAEPPDLLFANAVLQWLPDHAGLLARLARMLAPGGCLAVQMPDNLEEPSHRLMRRVAGEAPFAERLAQAAAARTRLGSFRDYDAWLSAAGCTVDLWRTTYVHPLAGHRGIVEWVRGTGLRPFLDPLDPADQAAFLARYEAALAEAYPPQADGRVLLPFPRLFLVARRR | Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate. | B0UPF4 |
A0R006 | WAG31_MYCS2 | Antigen 84 | Mycolicibacterium | MPLTPADVHNVAFSKPPIGKRGYNEDEVDAFLDLVENELTRLIEENADLRQRVAELDQELAAARSGAGASSQATSSIPLYEPEPEPAPAPPQPVYEAPAQPAAPQSEDTAVRAARVLSLAQDTADRLTSTAKAEADKLLSDARAQAEAMVSDARQTAETTVSEARQRADAMLADAQTRSEAQLRQAQEKADALQADAERKHSEIMGTINQQRTVLEGRLEQLRTFEREYRTRLKTYLESQLEELGQRGSAAPVDSSANSDASGFGQFNRGNN | Important for maintaining cell shape and cell wall integrity by localizing peptidoglycan synthesis to the cell poles. Protects PbpB (PBP3, FtsI) from oxidative stress-induced cleavage. | A0R006 |
A7TEN6 | TRM82_VANPO | Transfer RNA methyltransferase 82 | Vanderwaltozyma | MSLIHPIQAVVSNRSGELIFAVLKNVIIAYRYDQTNGKYLEMGKWEDQFSRDEMIKIAVVKEQARQLAENEEKGIKKSKTNEGNTIEKKHDAKIPVPGPGAPPIYSQIRNLMISNDETMLLACADSDKSVLVFKIETLNNDNCLKLIKRQPFPKRPNAITITEDDKTVIIADKFGDVYSMLIESPVIENIDEEFEPILGHVSMLTGVLSTTNNGMKFVMTSDRDEHIKISHFPQSYIVDKWLFGHKEFVSSICIPSWNSNILVSAGGDHGIFLWDWIKGEKLDEFDFTDLVLPYINENHLAPDRFQNEENDLKEFAVSKLVSLPNNPYFAFFVEATKLLIILEVDQSTYKMKLLQKIVLPYYITFISTFSDDKTMGFNISLDNRESGDKDFVKFIALDTTSNTFSIKEEQSDEFNTSIVNSFSKEDSIVKVELDEVYPLYNIISLKKHGEHYS | Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit. | A7TEN6 |
D5EY13 | XYFA_PRER2 | Ferulic acid esterase | Prevotella | MKKLLVALSLIAGSLTASAQWGRPVDYAAGPGLKDAYKDYFTVGVAVNKFNISDPAQTAIVKKQFNSVTAENAWKPGEIHPKEGVWNFGLADSIANFCRENGIKMRGHCLCWHSQFADWMFTDKKGKPVKKEVFYQRLREHIHTVVNRYKDVVYAWDVVNEAMADDGRPFEFVDGKMVPASPYRQSRHFKLCGDEFIAKAFEFAREADPTGVLMYNDYSCVDEGKRERIYNMVKKMKEAGVPIDGIGMQGHYNIYFPDEEKLEKAINRFSEIVNTIHITELDLRTNTESGGQLMFSRGEAKPQPGYMQTLQEDQYARLFKIFRKHKDVIKNVTFWNLSDKDSWLGVNNHPLPFDENFKAKRSLQIIRDFDAAMDNRKPKEDFVPNPMNQPGQEYPMVNSEGYARFRVEAPDAKSVIVSLGLGGRGGTVLRKDKNGVWTGTTEGPMDPGFHYYHLTIDGGVFNDPGTHNYFGSCRWESGIEIPAKDQDFYAYRKDINHGNIQQVTFWSESTGKMQTANVYLPYGYGKVVKGKQERYPVLYLQHGWGENETSWPVQGKAGLIMDNLIADGKIKPFIVVMAYGLTNDFKFGSIGKFTAEEFEKVLIDELIPTIDKNFLTKADKWNRAMAGLSMGGMETKLITLRRPEMFGYWGLLSGGTYMPEEIKDPKAVKYIFVGCGDKENPEGINKSVEALKAAGFKAEGLVSEGTAHEFLTWRRCLEKMAQSLFK | Involved in degradation of plant cell wall polysaccharides. Has endo-xylanase activity towards substrates such as oat spelt xylan (OSX), acetylated xylo-oligosaccharides and acetylated xylan, producing primarily xylobiose; cannot hydrolyze xylobiose to xylose. Also has feruloyl esterase activity, releasing ferulic acid from methylferulate, and from the more natural substrates wheat bran, corn fiber, and XOS(FA,Ac), a corn fiber-derived substrate enriched in O-acetyl and ferulic acid esters. Exhibits negligible acetyl esterase activity on sugar acetates. Acts synergistically with Xyl3A to increase the release of xylose from xylan. Does not possess endoglucanase or mannanase activities since it is not able to hydrolyze carboxymethyl cellulose and locust bean gum. | D5EY13 |
Q9Y2C2 | UST_HUMAN | Uronyl 2-sulfotransferase | Homo | MKKKQQHPGGGADPWPHGAPMGGAPPGLGSWKRRVPLLPFLRFSLRDYGFCMATLLVFCLGSLLYQLSGGPPRFLLDLRQYLGNSTYLDDHGPPPSKVLPFPSQVVYNRVGKCGSRTVVLLLRILSEKHGFNLVTSDIHNKTRLTKNEQMELIKNISTAEQPYLFTRHVHFLNFSRFGGDQPVYINIIRDPVNRFLSNYFFRRFGDWRGEQNHMIRTPSMRQEERYLDINECILENYPECSNPRLFYIIPYFCGQHPRCREPGEWALERAKLNVNENFLLVGILEELEDVLLLLERFLPHYFKGVLSIYKDPEHRKLGNMTVTVKKTVPSPEAVQILYQRMRYEYEFYHYVKEQFHLLKRKFGLKSHVSKPPLRPHFFIPTPLETEEPIDDEEQDDEKWLEDIYKR | Sulfotransferase that catalyzes the transfer of sulfate to the position 2 of uronyl residues. Has mainly activity toward iduronyl residues in dermatan sulfate, and weaker activity toward glucuronyl residues of chondroitin sulfate. Has no activity toward desulfated N-resulfated heparin. | Q9Y2C2 |
P54401 | TBG_ENTHI | Gamma-tubulin | Entamoeba | MPREIITLNVGQCGNQLGSEFFKKICSEHGILPDGSLSTNEFIDDRKDVFFYQADDQRYVPRSINIDLEPRVLDSIRTSEWRNFYNPENFIIPTNNGAGNSWANGYYTTEKMSEIEEIIDREVEHCDSLEGFFFCHSICGGTGSGLGSKIMEMISEKYPKNILTSFSVMVKENPDVVVSPYNSILTLRRLITECQSVVVFDNSALADITHTQFGVDEATVFDMNSIISSSMSAFTANLRFPSTLYNSLNSLMIHLCPSRFSHFLMTSYTPLRQVNQISSRTSAIDVMKRLIQPQNIMARTRLKEGKYISMCDFFQGDVSYDEINEALQRFTDRRLAEFVPWNKEAIKVVHTRVSPLVKRGNRMSGMLLANNTSIRYYFQDILKAFDQMFKKRVYLQTDRDNLRKFPEFEESKEIVKCVIEEYAKAESIEYSHYSYPIHKYLKGIAKEKIAE | Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly. | P54401 |
P53039 | YIP1_YEAST | YPT-interacting protein 1 | Saccharomyces | MSFYNTSNNANNGGGFYQPSAQFAVPQGSMSFQNTVGSSNTGNDNNLGVAPDPLPVGILHALSTKGYPHEPPLLEEIGINFDHIITKTKMVLIPIRFGSGVPQEILNDSDLAGPLIFFLLFGLFLLMAGKVHFGYIYGVALFGTISLHNLSKLMSNNDTSTQTNLQFFNTASILGYCFLPLCFLSLLGIFHGLNNTTGYVVSVLFVIWSTWTSSGFLNSLLQLQNARLLIAYPLLIFYSVFALMVIFV | Required for fusion of ER-derived vesicles with the Golgi during ER-to-Golgi protein transport, probably by mediating correct membrane localization of YPT1. | P53039 |
Q40284 | UFOG1_MANES | UDP-glucose flavonoid 3-O-glucosyltransferase 1 | Manihot | MGHLVSAVETAKLLLSRCHSLSITVLIFNNSVVTSKVHNYVDSQIASSSNRLRFIYLPRDETGISSFSSLIEKQKPHVKESVMKITEFGSSVESPRLVGFIVDMFCTAMIDVANEFGVPSYIFYTSGAAFLNFMLHVQKIHDEENFNPTEFNASDGELQVPGLVNSFPSKAMPTAILSKQWFPPLLENTRRYGEAKGVIINTFFELESHAIESFKDPPIYPVGPILDVRSNGRNTNQEIMQWLDDQPPSSVVFLCFGSNGSFSKDQVKEIACALEDSGHRFLWSLADHRAPGFLESPSDYEDLQEVLPEGFLERTSGIEKVIGWAPQVAVLAHPATGGLVSHSGWNSILESIWFGVPVATWPMYAEQQFNAFQMVIELGLAVEIKMDYRNDSGEIVKCDQIERGIRCLMKHDSDRRKKVKEMSEKSRGALMEGGSSYCWLDNLIKDMIK | In the presence of other necessary color factors, this glycosylation reaction allows the accumulation of anthocyanin pigments. | Q40284 |
Q8TAM2 | TTC8_HUMAN | Bardet-Biedl syndrome 8 protein | Homo | MSSEMEPLLLAWSYFRRRKFQLCADLCTQMLEKSPYDQEPDPELPVHQAAWILKARALTEMVYIDEIDVDQEGIAEMMLDENAIAQVPRPGTSLKLPGTNQTGGPSQAVRPITQAGRPITGFLRPSTQSGRPGTMEQAIRTPRTAYTARPITSSSGRFVRLGTASMLTSPDGPFINLSRLNLTKYSQKPKLAKALFEYIFHHENDVKTIHLEDVVLHLGIYPFLLRNKNHIEKNALDLAALSTEHSQYKDWWWKVQIGKCYYRLGMYREAEKQFKSALKQQEMVDTFLYLAKVYVSLDQPVTALNLFKQGLDKFPGEVTLLCGIARIYEEMNNMSSAAEYYKEVLKQDNTHVEAIACIGSNHFYSDQPEIALRFYRRLLQMGIYNGQLFNNLGLCCFYAQQYDMTLTSFERALSLAENEEEAADVWYNLGHVAVGIGDTNLAHQCFRLALVNNNNHAEAYNNLAVLEMRKGHVEQARALLQTASSLAPHMYEPHFNFATISDKIGDLQRSYVAAQKSEAAFPDHVDTQHLIKQLRQHFAML | The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization. | Q8TAM2 |
Q96K83 | ZN521_HUMAN | LYST-interacting protein 3 | Homo | MSRRKQAKPRSLKDPNCKLEDKTEDGEALDCKKRPEDGEELEDEAVHSCDSCLQVFESLSDITEHKINQCQLTDGVDVEDDPTCSWPASSPSSKDQTSPSHGEGCDFGEEEGGPGLPYPCQFCDKSFSRLSYLKHHEQSHSDKLPFKCTYCSRLFKHKRSRDRHIKLHTGDKKYHCSECDAAFSRSDHLKIHLKTHTSNKPYKCAICRRGFLSSSSLHGHMQVHERNKDGSQSGSRMEDWKMKDTQKCSQCEEGFDFPEDLQKHIAECHPECSPNEDRAALQCVYCHELFVEETSLMNHMEQVHSGEKKNSCSICSESFHTVEELYSHMDSHQQPESCNHSNSPSLVTVGYTSVSSTTPDSNLSVDSSTMVEAAPPIPKSRGRKRAAQQTPDMTGPSSKQAKVTYSCIYCNKQLFSSLAVLQIHLKTMHLDKPEQAHICQYCLEVLPSLYNLNEHLKQVHEAQDPGLIVSAMPAIVYQCNFCSEVVNDLNTLQEHIRCSHGFANPAAKDSNAFFCPHCYMGFLTDSSLEEHIRQVHCDLSGSRFGSPVLGTPKEPVVEVYSCSYCTNSPIFNSVLKLNKHIKENHKNIPLALNYIHNGKKSRALSPLSPVAIEQTSLKMMQAVGGAPARPTGEYICNQCGAKYTSLDSFQTHLKTHLDTVLPKLTCPQCNKEFPNQESLLKHVTIHFMITSTYYICESCDKQFTSVDDLQKHLLDMHTFVFFRCTLCQEVFDSKVSIQLHLAVKHSNEKKVYRCTSCNWDFRNETDLQLHVKHNHLENQGKVHKCIFCGESFGTEVELQCHITTHSKKYNCKFCSKAFHAIILLEKHLREKHCVFETKTPNCGTNGASEQVQKEEVELQTLLTNSQESHNSHDGSEEDVDTSEPMYGCDICGAAYTMETLLQNHQLRDHNIRPGESAIVKKKAELIKGNYKCNVCSRTFFSENGLREHMQTHLGPVKHYMCPICGERFPSLLTLTEHKVTHSKSLDTGNCRICKMPLQSEEEFLEHCQMHPDLRNSLTGFRCVVCMQTVTSTLELKIHGTFHMQKTGNGSAVQTTGRGQHVQKLYKCASCLKEFRSKQDLVKLDINGLPYGLCAGCVNLSKSASPGINVPPGTNRPGLGQNENLSAIEGKGKVGGLKTRCSSCNVKFESESELQNHIQTIHRELVPDSNSTQLKTPQVSPMPRISPSQSDEKKTYQCIKCQMVFYNEWDIQVHVANHMIDEGLNHECKLCSQTFDSPAKLQCHLIEHSFEGMGGTFKCPVCFTVFVQANKLQQHIFSAHGQEDKIYDCTQCPQKFFFQTELQNHTMTQHSS | Transcription factor that can both act as an activator or a repressor depending on the context. Involved in BMP signaling and in the regulation of the immature compartment of the hematopoietic system. Associates with SMADs in response to BMP2 leading to activate transcription of BMP target genes. Acts as a transcriptional repressor via its interaction with EBF1, a transcription factor involved specification of B-cell lineage; this interaction preventing EBF1 to bind DNA and activate target genes. | Q96K83 |
P02854 | VCLB_PEA | Type B | Pisum | MLLAIAFLASVCVSSRSDQENPFIFKSNRFQTLYENENGHIRLLQKFDKRSKIFENLQNYRLLEYKSKPHTLFLPQYTDADFILVVLSGKATLTVLKSNDRNSFNLERGDAIKLPAGSIAYFANRDDNEEPRVLDLAIPVNKPGQLQSFLLSGTQNQKSSLSGFSKNILEAAFNTNYEEIEKVLLEQQEQEPQHRRSLKDRRQEINEENVIVKVSRDQIEELSKNAKSSSKKSVSSESGPFNLRSRNPIYSNKFGKFFEITPEKNQQLQDLDIFVNSVDIKVGSLLLPNYNSRAIVIVTVTEGKGDFELVGQRNENQGKENDKEEEQEEETSKQVQLYRAKLSPGDVFVIPAGHPVAINASSDLNLIGLGINAENNERNFLAGEEDNVISQVERPVKELAFPGSSHEVDR | Seed storage protein. | P02854 |
Q9Y4E1 | WAC2C_HUMAN | Vaccinia virus penetration factor | Homo | MMNRTTPDQELVPASEPVWERPWSVEEIRRSSQSWSLAADAGLLQFLQEFSQQTISRTHEIKKQVDGLIRETKATDCRLHNVFNDFLMLSNTQFIENRVYDEEVEEPVLKAEAEKTEQEKTREQKEVDLIPKVQEAVNYGLQVLDSAFEQLDIKAGNSDSEEDDANGRVELILEPKDLYIDRPLPYLIGSKLFMEQEDVGLGELSSEEGSVGSDRGSIVDTEEEKEEEESDEDFAHHSDNEQNQHTTQMSDEEEDDDGCDLFADSEKEEEDIEDIEENTRPKRSRPTSFADELAARIKGDAMGRVDEEPTTLPSGEAKPRKTLKEKKERRTPSDDEEDNLFAPPKLTDEDFSPFGSGGGLFSGGKGLFDDEDEESDLFTEASQDRQAGASVKEESSSSKPGKKIPAGAVSVFLGDTDVFGAASVPSLKEPQKPEQPTPRKSPYGPPPTGLFDDDDGDDDDDFFSAPHSKPSKTRKVQSTADIFGDEEGDLFKEKAVASPEATVSQTDENKARAEKKVTLSYSKNLKPSSETKTQKGLFSDEEDSEDLFSSQSASNLKGASLLPGKLPTSVSLFDDEDEEDNLFGGTAAKKQTLSLQAQREEKAKASELSKKKASALLFSSDEEDQWNIPASQTHLASDSRSKGEPRDSGTLQSQEAKAVKKTSLFEEDKEDDLFAIAKDSQKKTQRVSLLFEDDVDSGGSLFGSPPTSVPPATKKKETVSEAPPLLFSDEEEKEAQLGVKSVDKKVESAKESLKFGRTDVAESEKEGLLTRSAQETVKHSDLFSSSSPWDKGTKPRTKTVLSLFDEEEDKMEDQNIIQAPQKEVGKGCDPDAHPKSTGVFQDEELLFSHKLQKDNDPDVDLFAGTKKTKLLEPSVGSLFGDDEDDDLFSSAKSQPLVQEKKRVVKKDHSVNSFKNQKHPESIQGSKEKGIWKPETPQANLAINPAALLPTAASQISEVKPVLPELAFPSSEHRRSHGLESVPVLPGSGEAGVSFDLPAQADTLHSANKSRVKMRGKRRPQTRAARRLAAQESSEAEDMSVPRGPIAQWADGAISPNGHRPQLRAASGEDSTEEALAAAAAPWEGGPVPGVDTSPFAKSLGHSRGEADLFDSGDIFSTGTGSQSVERTKPKAKIAENPANPPVGGKAKSPMFPALGEASSDDDLFQSAKPKPAKKTNPFPLLEDEDDLFTDQKVKKNETKSSSQQDVILTTQDIFEDDIFATEAIKPSQKTREKEKTLESNLFDDNIDIFADLTVKPKEKSKKKVEAKSIFDDDMDDIFSTGIQAKTTKPKSRSAQAAPEPRFEHKVSNIFDDPLNAFGGQ | (Microbial infection) Plays a role in fluid-phase endocytosis, a process exploited by vaccinia intracellular mature virus (IMV) to enter cells. As a result, may facilitate the penetration of IMV into cells. | Q9Y4E1 |
A6VM40 | TATA_ACTSZ | Sec-independent protein translocase protein TatA | Actinobacillus | MGGISIWQLLIIVAIVVLLFGTKKLRTLGSDLGESVKGFKKAMAEEPKDAEFKSLDKAENTAQTKKEEKEKEQA | 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. | A6VM40 |
Q5HRP5 | TILS_STAEQ | tRNA(Ile)-lysidine synthetase | Staphylococcus | MNIKTDGWSKKAHIVVAVSTGIDSMSLLYSLLNDYQHTYRKLTCVHVNHGLREQSYEEEAFLREYCHQHHIDIYIKRLDLSDIVADGNSIQQEARQRRYEWFGDIIAQLRADVLLTAHHLDDQFETIIYRLFTGRSTRNSLGMTYESYFNQYKVYRPMLNLKKTEILAYQYANQIPYYEDMSNQDRKYVRNDIRQRIIPAINENPHLNAHQLLKLKDWHDIELQSLKEQAETFINNEVSKSKYLTYSFSRTAFNELNVNIKSVVMDLLFEKLDCHLAMPQHAYDEWFEQIRNDKSQFNIHVTDEWIIQIAYDKLIIMAKSEMDQYILDRICIRKPGTYEFNDYQIDIHPDLPQQLYPLTVRVRQNGDVYKLNGQKGHKKVSRLFIDKKVTLAERQRIPLIINQENAVLAIGDLYVKENFKEFILISNNGDEL | 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. | Q5HRP5 |
Q39W52 | Y1286_GEOMG | Nucleotide-binding protein Gmet_1286 | Geobacter | MRVLVISGLSGSGKSTAVRVLEDEGFFCIDNLPVQLFPTIIDLVNKAQETVPGVALVMDIRGRDFLKGFEKIFQEIDDAGHTIEIIFFDATDEVLIRRFSETRRRHPALESGSVPEGIRYEREQLSGLRRLATLVIDTSELNVHQLKEMVLARVKGEAGARRMTIHLQSFGYRYGIPLESDLVMDVRFLSNPHFVPELKPLSGLDPGVRNFVLEKPETTQFLARFEGLLEYLLPAYQREGKSYLTISIGCTGGRHRSVALVEELRRFFDRAGIAVKVSHRDMEKG | Displays ATPase and GTPase activities. | Q39W52 |
Q4KLZ1 | TM186_RAT | Transmembrane protein 186 | Rattus | MAFLLRAVPRLQGPAAWRRPLQQLWCRAGQGDSIRWVGSRSPPSQEKPPGTETEKFHTIYRFNAIRALGFLSRLKLAQTAVTVVALPPGFYCYSQGLMTLSSLGLMSGIASFALVMLCWMSHFFRRLVGILYVNESGTLLRVAHLTFWGWRQDTYCAVSDMIPLSESEERVQDVFVRIQQYSGKQTFYLTLRYGRILDRDRFSQVFGTLATLKNSK | As part of the MCIA complex, required for efficient assembly of the mitochondrial complex I. | Q4KLZ1 |
P76498 | YFCO_ECOLI | Uncharacterized protein YfcO | Escherichia | MKILRWLFALVMLIATTEAMAAGHSVDVYYGYNGDSRNIATFNLKIMMPSAVYVGEYKSSQWLMTGEILQNVSWSGPPPAPSVKLIGYHQNINKASCPGLPSGWNCGYYTFEVIVSAEIESYFSCPWLVIMNDSEASPGGVTYQGPDSHDTICPSVSVQPYDVSWNENYVSKSKLLTLQSTGGVVEKTLSTYLMKDGKLCDSTQMNETGGYCRWVAQMITFTASGCDKAEVSVTPNRHPITDKQLHDMVVRVDTSSMQPIDSTCRFQYILNEL | Part of the yfcOPQRSUV fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes. | P76498 |
Q8Z322 | THIG_SALTI | Thiazole synthase | Salmonella | MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHNDAILAPLIEAGVTLLPNTSGAKTAEEAIFAAQLALEALGTHWLKLEIHPDARWLLPDPIETLKAAEALVKQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQGLETKAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVMMATAFRLAVEAGLLARQAVPGNRSTYASATSPLTGFLEALA | 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. | Q8Z322 |
Q39JF0 | UBIA_BURL3 | 4-HB polyprenyltransferase | Burkholderia cepacia complex | MLARFPLYLRLVRMDKPIGSLLLLWPTLNALWIASDGHPRWPLLVIFSLGTLLMRSAGCAMNDYADRDFDRHVKRTADRPLTSGKIRAWEAIAIAVGLAFVSFLLILPLNTLTKQLSVVALFVAGSYPFMKRFFAIPQAYLGIAFGFGIPMAFAAVQDTVPTIAWVMLIANIFWSVAYDTEYAMVDRDDDIKIGIRTSALTFGRFDVAAVMLCYAVTLGIYVWIGVTLGFGLAYWAGWAAAVGCALYHYTLIKDRERMPCFAAFRHNNWLGGVLFAGIAAHYLLAGS | 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. | Q39JF0 |
A4FVI0 | ZSWM7_DANRE | Zinc finger SWIM domain-containing protein 7 | Danio | MGSSLVSVAEQLLKDLQRTYSEIKQIPDDLLIALRFVFGPCALQALDLVDQHSVTCVSSPSGRKAFQVLGGSGRLYTCFTSCHYCPCPAFSFTVLRRNESLMCKHLLAVILSQAMGLCQQEQVSDQQMTHILSRQPEAST | Involved in early stages of the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. | A4FVI0 |
P27876 | TPIS_BACSU | Triose-phosphate isomerase | Bacillus | MRKPIIAGNWKMNKTLGEAVSFVEEVKSSIPAADKAEAVVCAPALFLEKLASAVKGTDLKVGAQNMHFEESGAFTGEISPVALKDLGVDYCVIGHSERREMFAETDETVNKKAHAAFKHGIVPIICVGETLEEREAGKTNDLVADQVKKGLAGLSEEQVAASVIAYEPIWAIGTGKSSTAKDANDVCAHIRKTVAESFSQEAADKLRIQYGGSVKPANIKEYMAESDIDGALVGGASLEPQSFVQLLEEGQYE | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | P27876 |
M0R7T9 | TBC12_RAT | TBC1 domain family member 12 | Rattus | MMGPEDAGACSGRNAELLPVPGPMGQDGKTVPATGGFSGGAVAAEPPGEAGEEEAPPPRQLLQRYLAAAAGPLQPGLGGVEAEAAAVPAARGSGMTNGDSGFLLLQDRRGPEEARRRRTCGRPCLAEPADEGVDGAGGLDDWAAPLEDPLRSCCLAAGDTDDPDPTATTSAGRDVGSAESSLGLPDARFGSRNTFEVSRRQSAGDLLPSAGQSAPLPAAEQGPGGTTVRARRSGGFADFFARNLFPKRTKELKSVVHSAPGWKLFGKVPPRENLQKTSKIIQQEYEARTGRTCKVPPQSSRRKNFEFEPLSTTALILEDRPSNLPAKSVEEALRHRQEYDEMVAEAKKREIKEAHKRKRIMKERFKQEESIASAMVIWINEILPNWEVMRSTRRVRELWWQGLPPSVRGKVWSLAVGNELNITPELYEIFLSRAKERWKSFSESSSDSDMEGLSVADREASLELIKLDISRTFPSLYIFQKGGPYHDVLHSILGAYTCYRPDVGYVQGMSFIAAVLILNLEEADAFIAFANLLNRPCQLAFFRVDHSMMLKYFATFEVFFEENLSKLFLHFKSYNLTPDIYLIDWIFTLYSKSLPLDLACRVWDVFCRDGEEFLFRTGLGILRLYEDILLQMDFIHIAQFLTKLPEDITSEKLFSCIAAIQMQNSTKKWTQVFASVTKDIKEGDKNNSPALKS | RAB11A-binding protein that plays a role in neurite outgrowth. | M0R7T9 |
C0HK73 | VKT2_HETMG | PI-stichotoxin-Hmg3b | Heteractis | GSICLEPKVVGPCKAGIRRFYFDSETGKCTLFLYGGCKGNGNNFETLHACRAICRA | Serine protease inhibitor. | C0HK73 |
Q3K093 | TARI_STRA1 | Ribitol-5-phosphate cytidylyltransferase | Streptococcus | MNIGVIFAGGVGRRMNTKGKPKQFLEVHGKPIIVHTIDIFQNTEAIDAVVVVCVSDWLDYMNNLVERFNLTKVKAVVAGGETGQMSIFKGLEAAEQLATDDAVVLIHDGVRPLINEEVINANIQSVKETGSAVTSVRAKETVVLVNDSSKISEVVDRTRSFIAKAPQSFYLSDILSIERDAISKGITDAIDSSTLMGMYNRELTIVEGPYENIKITTPDDFYMFKALYDARENEQIYGM | Catalyzes the transfer of the cytidylyl group of CTP to D-ribitol 5-phosphate. | Q3K093 |
A5W9G9 | THIE_PSEP1 | Thiamine-phosphate pyrophosphorylase | Pseudomonas | MKLRGLYAITDSQLLAGRFLSHVEAALEGGVCLLQYRDKSDDAARRLREAEGLMKLCERYGTQLLINDDAELAARLGVGVHLGQTDGPLTPARALLGRQAIIGSTCHASLELAAQAASEGASYVAFGRFFNSVTKPGAPAANVGLLEQARAQVKLPIAVIGGITLDNAAPLVAHGADLLAVIHGLFGADSAQEVTRRARAFNALFAS | Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). | A5W9G9 |
Q6DCE3 | ZNT9_XENLA | Solute carrier family 30 member 9 | Xenopus | MAGIYARSWPSLFRLYMRCAGTRCSGHGWQNALESKGLLYFLPSSYLPIQAHIRLYSSSDQKEDGGSKGTSAASSPEKSMAGLDPSKPEQKSTFPPDPIQVKVKAVLKKREYGTKYMKNNFITGVRALNEFCLKPSDLESLRKIRRRSPHDDTEAFTVYLRSDVEAKAYEVWGSPEAIFRERKMRKEEEIAYRENLFRNQKLLKEYKDFLGNTKPRLSTTNMFMKGPGKVVIVAICINGLNFFFKLLAWVYTGSASMFSEALHSLADTLNQALLALGISQSARTPDPGHPYGFTNMRYIASLISGVGIFMMGAGLSWYHGIIGLLHPQPIESLLWAYCILAGSLVSEGATLLVAINEIRKSSRAKGLSFYQYVMQSRDPSTNVVLMEDAAAVLGLVMAASCMGLTSLTGNPLYDSLGSLGVGTLLGAVSAFLIYTNTEALIGRSIQPDQVQRLTELLESDPAVRAIHDVKATDMGMSKVRFKAEVDFDGRVVTRSYLEKQDIDLVLNEIRQVKTAEDLEAFMLKHGENIIDTLGAEVDRLEKELKQRNPEVRHVDLEIL | May act as a zinc transporter involved in intracellular zinc homeostasis. May play a role as nuclear receptor coactivator. | Q6DCE3 |
B1LHA4 | TREA_ECOSM | Alpha,alpha-trehalose glucohydrolase | Escherichia | MKSPTPSRPQKMALIPACIFLCFAALSVQAEETSVTPQPPDILLGPLFNDVQNAKLFPDQKTFADAVPNSDPLMILADYRMQQNQSGFDLRHFVNVNFTLPKEGEKYVPPEGQSLREHIDGLWPVLTRATENTEKWDSLLPLPEPYVVPGGRFREVYYWDSYFTMLGLAESGHWDKVADMVANFAHEIDTYGHIPNGNRSYYLSRSQPPFFALMVELLAQHEGDAALKQYLPQMQKEYAYWMDGVENLQAGQQEKRVVKLQDGTLLNRYWDDRDTPRPESWVEDIATAKSNPNRPATEIYRDLRSAAASGWDFSSRWMDNPQQLNTLRTTSIVPVDLNSLMFKMEKILARASKAAGDNAMANQYETLANARQKGIEKYLWNDQQGWYADYDLKSHKVRNQLTAAALFPLYVNAAAKDRASKMATATKTHLLQPGGLNTTSVKSGQQWDAPNGWAPLQWVATEGLQNYGQKEVAMDISWHFLTNVQNTYDREKKLVEKYDVSATGTGGGGGEYPLQDGFGWTNGVTLKMLDLICPKEQPCDNVPATRPLSESTTQPLKQKEAEPTP | Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system. | B1LHA4 |
Q6YQT0 | TYSY_ONYPE | Thymidylate synthase | Candidatus Phytoplasma asteris | MNTYLDLCRFILQKGSFRNDRTNTGTKSVFGYQMRFNLEEGFPLLTTKKMNLRSIIHELLWFLKGDTNICYLVQNNVNIWNEWPYQKYQQSAFFQNETLKEFLEKIKNDPLFAIKHGNLGPVYGKQWRDFNGVDQIKFLISEIKTNPNSRRLILNSWNPPLLNQMALPPCHVLIQFYVHQGKLSLQLYQRSGDVFLGIPFNIASYSLLLMMVAQVTNLQPYEFIHTLGDAHIYSNHLAQVQTQIQRTPKKLPQMILNPDIKNIDDFKFSDFTLQNYQCDGILKGDIAV | 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. | Q6YQT0 |
Q8R9P1 | THIC_CALS4 | Thiamine biosynthesis protein ThiC | Caldanaerobacter | MTQLEYALSGIITKEMKIVADYEGVSEEFILEEVKKGEIVIPANVNHINLVPKGIGKGLSTKVNANIGTSDAFPEIGKEIEKLKVAIDAGADAVMDLSTGGDVNKSRREIIKNSSVPVGTVPMYQAAVESISRYGSIVAMPEEFIFKVIEEQAKDGVDFITVHCGLTLESLKRLKDNKRIMNVVSRGGAFTIAWMIHNEKENPLYQYFDRLLDIAKKYDVTLSLGDGLRPGCLEDATDAAQIQELIILGELVKKAREAGVQVMVEGPGHVPIDQIEANVKLQKSLCHNAPFYVLGPVVTDIAPGYDHITAAIGGAIAAFAGADFLCYVTPAEHLGLPDIQDVKEGVIAAKIAAHAADIAKGIKKAREKDLAMAKARANLDWNEQIQLSIDPEKAEKYRVTKNKPNVETCSMCGKFCAMQIVSEYLGTPTTSC | 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. | Q8R9P1 |
P42245 | YCBM_BACSU | Sensor histidine kinase YcbM | Bacillus | MTVLWVAAVIALACLNVIQFIMKKKRDGNLAYTADQLSYMLSRDSAGQILLPTDDHALKDLLVNINLIVENRQQISAQFAKTEQSMKRMLTNMSHDLKTPLTVILGYIEAIQSDPNMPDEERERLLGKLRQKTNELIQMINSFFDLAKLESEDKEIPITKVHMNDICKRNILHYYDAVQSKGFQAAIDIPDTPVYAQANEEALDRILQNLLSNAIQYGAAGKLIGLTLSYDERNIAITVWDRGKGISETDQQRVFERLYTLEESRNKAFQGSGLGLTITKRLTEKMGGIISVQSKPYERTAFTITLKRMTY | Member of the two-component regulatory system YcbM/YcbL. Probably activates YcbL by phosphorylation. | P42245 |
Q2SDQ0 | UREE_HAHCH | Urease accessory protein UreE | Hahella | MIRITERYIETEQTPVIAGVISLTYDERKRGRLRAKTQSGEDVGLFLERGKTLLDGDLLMAENGDIYTISAAPETVATAQANDPRQFAQICYHLGNRHTPLQIGELWVRFQPDHVLEDLCRLYGLDVVRESAPFNPENGAYGGHSGHSGHSGHSGHHHGHDHSHEQSRQDAKELSARYHFHAPDHEHPHGHVHLHAHPHEH | Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. | Q2SDQ0 |
Q4R5B4 | TMX2_MACFA | Thioredoxin domain-containing protein 14 | Macaca | MAVLAPLIALVYSVPRLSRWLAQPYYLLSALLSAAFLLVRKLPPLCHGLPTQREDGNPCDFDWREVEILMFLSAIVMMKNRRSITVEQHIGNIFMFSKVANAILFFRLDIRMGLLYITLCIVFLMTCKPPLYMGPEYIKYFNDKTIDEELERDKRVTWIVEFFANWANDCQSFAPIYADLSLKYNCTGLNFGKVDVGRYTDVSTRYKVSTSPLTKQLPTLILFQGGKEVMRRPQIDKKGRAVSWTFSEENVIREFNLNELYQRAKKLSKAGDNIPEEQPVAPTPTRVSDGESKKDK | Endoplasmic reticulum and mitochondria-associated protein that probably functions as a regulator of cellular redox state and thereby regulates protein post-translational modification, protein folding and mitochondrial activity. Indirectly regulates neuronal proliferation, migration, and organization in the developing brain. | Q4R5B4 |
B1I0X4 | Y300_DESAP | Nucleotide-binding protein Daud_0300 | Candidatus Desulforudis | MAGTRLLIVTGLSGAGKTQAVRCLEDLGFFCVDNLPPKLIPKFAELCAQTTGKIERIALVVDIRGGEFFATVLDVLKDLKNQGLRYEILYLEASNETLVRRFKESRRPHPLSTSGEIVEGIEAERLALRELRGLAHKIIDTSNFSVAQLKQEIANLYGGNEDRERLAITAVSFGYKYGIPLDADLVIDVRFLPNPHYEPQLQPLTGLDEPVREYVFEAPTTSEFLSHLVNLFDFLIPQYIREGKTTLTLAIGCTGGKHRSVVLADWLGEQLRERKHRIVVRHRDLGRDVSGTNY | Displays ATPase and GTPase activities. | B1I0X4 |
O25989 | YIDC_HELPY | Membrane protein YidC | Helicobacter | MDKNNNNLRLILAIALSFLFIALYSYFFQKPNKTTTQTTKQETTNNHTATSPNAPNAQHFSTTQTTPQENLLSTISFEHARIEIDSLGRIKQVYLKDKKYLTPKQKGFLEHVGHLFSSKENAQPPLKELPLLAADKLKPLEVRFLDPTLNNKAFNTPYSASKTTLGPNEQLVLTQDLGTLSIIKTLTFYDDLHYDLKIAFKSPNNLIPSYVITNGYRPVADLDSYTFSGVLLENSDKKIEKIEDKDAKEIKRFSNTLFLSSVDRYFTTLLFTKDPQGFEALIDSEIGTKNPLGFISLKNEANLHGYIGPKDYRSLKAISPMLTDVIEYGLITFFAKGVFVLLDYLYQFVGNWGWAIILLTIIVRIILYPLSYKGMVSMQKLKELAPKMKELQEKYKGEPQKLQAHMMQLYKKHGANPLGGCLPLILQIPVFFAIYRVLYNAVELKSSEWILWIHDLSIMDPYFILPLLMGASMYWHQSVTPNTMTDPMQAKIFKLLPLLFTIFLITFPAGLVLYWTTNNILSVLQQLIINKVLENKKRMHAQNKKEH | 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. | O25989 |
P9WL36 | Y2885_MYCTO | Putative RNA-guided DNA endonuclease MT2953 | Mycobacterium tuberculosis complex | MMARLKVPEGWCVQAFRFTLNPTQTQAASLARHFGARRKAFNWTVTALKADIKAWRADGTESAKPSLRVLRKRWNTVKDQVCVNAQTGQVWWPECSKEAYADGIAGAVDAYWNWQSCRAGKRAGKTVGVPRFKKKGRDADRVCFTTGAMRVEPDRRHLTLPVIGTIRTYENTRRVERLIAKGRARVLAITVRRNGTRLDASVRVLVQRPQQRRVALPDSRVGVDVGVRRLATVADAEGTVLEQVPNPRPLDAALRGLRRVSRARSRCTKGSRRYCERTTELSRLHRRVNDVRTHHLHVLTTRLAKTHGRIVVEGLDAAGMLRQKGLPGARARRRALSDAALATPRRHLSYKTGWYGSSLVVADRWFPSSKTCHACRHVQDIGWDEKWQCDGCSITHQRDDNAAINLARYEEPPSVVGPVGAAVKRGADRKTGPGPAGGREARKATGHPAGEQPRDGVQVK | An RNA-guided dsDNA endonuclease. When guided by an RNA derived from the right-end element of its insertion sequence element (IS), cleaves DNA downstream of the transposon-associated motif (TAM). Cleaves supercoiled and linear DNA in a staggered manner 15-21 bases from the TAM yielding 5'-overhangs. Binds reRNA, an approximately 150 nucleotide base sRNA derived from the 3' end of its own gene, the right end (RE) of the insertion sequence (IS) plus sequence downstream of the IS. | P9WL36 |
B1JAG3 | THIC_PSEPW | Thiamine biosynthesis protein ThiC | Pseudomonas | MSKQEKTINLSESAQVDQQSVQPFPRSRKIYVEGSRPDIRVPMREISLHDTPTDFGGEANAPVLVYDTSGPYTDPDVIIDVRKGLADVRSAWIDARGDTERLGGLSSNFGQQRLNDAELAKLRFNHVRNPRRAKAGANVSQMHYARQGIITAEMEYVAIRENMKLQEARAAGLLKQQHAGHSFGANIPKEITAEFVREEIARGRAIIPANINHTELEPMIIGRNFLVKINGNIGNSALGSSIEEEVAKLTWGIRWGSDTVMDLSTGKHIHETREWIIRNSPVPIGTVPIYQALEKVGGVAEDLTWELFRDTLIEQAEQGVDYFTIHAGVLLRYVPLTAKRVTGIVSRGGSIMAKWCLAHHQENFLYTHFDEICEIMKAYDVSFSLGDGLRPGSIADANDAAQFGELETLGELTKIAWKHDVQCMIEGPGHVPMQLIKENMDKQLECCDEAPFYTLGPLTTDIAPGYDHITSGIGAAMIGWFGCAMLCYVTPKEHLGLPNKDDVKTGIITYKIAAHAADLAKGHPGAQIRDNALSKARFEFRWEDQFNLGLDPDTARAFHDETLPKESAKVAHFCSMCGPKFCSMKITQEVREYAANLRIDAVDVSVEEGMREQAERFRQEGSQLYHKV | 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. | B1JAG3 |
Q6ZS27 | ZN662_HUMAN | Zinc finger protein 662 | Homo | MLENYGAVASLAAFPFPKPALISQLERGETPWCSVPRGALDGEAPRGISSGYPFLKPAGISHPEQVEEPLNLKLQGEGPSLICPEGVLKRKKEDFILKEEIIEEAQDLMVLSSGPQWCGSQELWFGKTCEEKSRLGRWPGYLNGGRMESSTNDIIEVIVKDEMISVEESSGNTDVNNLLGIHHKILNEQIFYICEECGKCFDQNEDFDQHQKTHNGEKVYGCKECGKAFSFRSHCIAHQRIHSGVKPYECQECAKAFVWKSNLIRHQRIHTGEKPFECKECGKGFSQNTSLTQHQRIHTGEKPYTCKECGKSFTRNPALLRHQRMHTGEKPYECKDCGKGFMWNSDLSQHQRVHTGDKPHECTDCGKSFFCKAHLIRHQRIHTGERPYKCNDCGKAFSQNSVLIKHQRRHARDKPYNCQISHLLEH | May be involved in transcriptional regulation. | Q6ZS27 |
Q5FJN8 | TRUB_LACAC | tRNA-uridine isomerase | Lactobacillus | MLNGIIVIDKDKGMTSADVVYHLRRALHIRKIGHAGTLDPEVTGVLPIAIGQATKLIELMHTRPKKYQGTGLFGYATDSYDIDGKVLKEKRLVMPFTVEEIQRGMNTFKGKIEQVPPIYSAVKVNGKHLYEYAREGIKVERPKRQVEIFQYDLLNDPSFDKEKGQESFDFEITCSKGTYVRSLVNDLGEKLDEPAVMTYLRRVASSGFDISQAVKLSEIEANPEKASELIQPIDAFFKDYETIDLPEGKWLKVKNGAGISLETNAKKVALRYNEKVKAIYEKKGKIYRPSLMLLQNE | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | Q5FJN8 |
B2V3W4 | YQGF_CLOBA | Putative pre-16S rRNA nuclease | Clostridium | MRILGLDLGKKTIGVAISDPLGFTAQGITTIRRANKEKDMEELRKICDEYKVETIVIGLPKNMNGTIGPSGEIAMEMGKLVEEALNIKVEFWDERLTTVAAHKAMLEADLSRSKRKKIVDKVASTYILQGYLDRISK | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | B2V3W4 |
A8AQN2 | TUSC_CITK8 | tRNA 2-thiouridine synthesizing protein C | Citrobacter | MKRIAFVFSTTPHGSASGREGLDALLATSALTEETGVFFIGDGVFQILSGQTPDVVLARDYIATFKLLGLYDIEQCWLCAASLRERGLETGASFIVDATPLEPEALRGELDNYDVILRF | Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. | A8AQN2 |
A4STJ3 | UBID_AERS4 | Polyprenyl p-hydroxybenzoate decarboxylase | Aeromonas | MKYKDLRDFIAQLEQNGQLKRITREIDPYLEMTEISDRTLRAGGPALLFENPKGYSMPVLTNLFGTPDRVAMGMGQPNVGALRQVGTWLSYLKEPEPPRGLKELMEKLPIFKQVLNMPTKRLSSAPCQQLVLEGEAVDLDQIPIQHCWPGDVAPLVTWGLTITRGPYKKRQNLGIYRQQKIGKNKLIMRWLDHRGGAIDFREWQEAHPGERFPVVVALGADPATILGAVTPVPDSLSEYAFAGLLRGSRTEVVKALSCDLEVPASAEIVLEGYLEPGELAPEGPYGDHTGYYNEVDEFPVFTITHMTMRRDAIYHSTYTGRPPDEPAVLGVALNEVFVPLLQKQFPEIVDFYLPPEGCSYRMAVVTIKKRYPGHAKRVMLGVWSFLRQFMYTKFVIVCDDDINARDWKDVIWAITTRMDPARDTTLIEHTPIDYLDFASPVSGLGSKMGLDATNKWPGETNREWGQPIVQDEAVKQKVDSIWAELNILG | Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis. | A4STJ3 |
Q2TB10 | ZN800_HUMAN | Zinc finger protein 800 | Homo | MPLRDKYCQTDHHHHGCCEPVYILEPGDPPLLQQPLQTSKSGIQQIIECFRSGTKQLKHILLKDVDTIFECKLCRSLFRGLPNLITHKKFYCPPSLQMDDNLPDVNDKQSQAINDLLEAIYPSVDKREYIIKLEPIETNQNAVFQYISRTDNPIEVTESSSTPEQTEVQIQETSTEQSKTVPVTDTEVETVEPPPVEIVTDEVAPTSDEQPQESQADLETSDNSDFGHQLICCLCRKEFNSRRGVRRHIRKVHKKKMEELKKYIETRKNPNQSSKGRSKNVLVPLSRSCPVCCKSFATKANVRRHFDEVHRGLRRDSITPDIATKPGQPLFLDSISPKKSFKTRKQKSSSKAEYNLTACKCLLCKRKYSSQIMLKRHMQIVHKITLSGTNSKREKGPNNTANSSEIKVKVEPADSVESSPPSITHSPQNELKGTNHSNEKKNTPAAQKNKVKQDSESPKSTSPSAAGGQQKTRKPKLSAGFDFKQLYCKLCKRQFTSKQNLTKHIELHTDGNNIYVKFYKCPLCTYETRRKRDVIRHITVVHKKSSRYLGKITASLEIRAIKKPIDFVLNKVAKRGPSRDEAKHSDSKHDGTSNSPSKKYEVADVGIEVKVTKNFSLHRCNKCGKAFAKKTYLEHHKKTHKANASNSPEGNKTKGRSTRSKALV | May be involved in transcriptional regulation. | Q2TB10 |
Q8N7M2 | ZN283_HUMAN | Zinc finger protein HZF19 | Homo | MESRSVAQAGVQWCDLGSLQAPPPGFTLFSCLSLLSSWDYSSGFSGFCASPIEESHGALISSCNSRTMTDGLVTFRDVAIDFSQEEWECLDPAQRDLYVDVMLENYSNLVSLDLESKTYETKKIFSENDIFEINFSQWEMKDKSKTLGLEASIFRNNWKCKSIFEGLKGHQEGYFSQMIISYEKIPSYRKSKSLTPHQRIHNTEKSYVCKECGKACSHGSKLVQHERTHTAEKHFECKECGKNYLSAYQLNVHQRFHTGEKPYECKECGKTFSWGSSLVKHERIHTGEKPYECKECGKAFSRGYHLTQHQKIHTGVKSYKCKECGKAFFWGSSLAKHEIIHTGEKPYKCKECGKAFSRGYQLTQHQKIHTGKKPYECKICGKAFCWGYQLTRHQIFHTGEKPYECKECGKAFNCGSSLIQHERIHTGEKPYECKECGKAFSRGYHLSQHQKIHTGEKPFECKECGKAFSWGSSLVKHERVHTGEKSHECKECGKTFCSGYQLTRHQVFHTGEKPYECKECGKAFNCGSSLVQHERIHTGEKPYECKECGKAFSRGYHLTQHQKIHTGEKPFKCKECGKAFSWGSSLVKHERVHTNEKSYECKDCGKAFGSGYQLSVHQRFHTGEKLYQRKEFGKTFTCGSKLVHERTHSNDKPYKYNECGEAFLWTTYSNEKIDTDETL | May be involved in transcriptional regulation. | Q8N7M2 |
Q47VH8 | Y4546_COLP3 | Nucleotide-binding protein CPS_4546 | Colwellia | MKLIIVSGRSGSGKSVALRVLEDLGYYCVDNIPINLLPALTHTVINDYENVAVSLDVRNLPKDPEDIPEIIAYLPKAVDVNTLFLDADDNDLIRRFSETRRLHPLIKENMALDQAIALEKSLLEPISTNADLYINTSQLSPHQLADLVRERILGKKTGSMVLVFESFGFKHGIPVDADYVFDARFLPNPFWEKSLKGQTGVDQEVKDFLASQAIVTKFIWQINSFMMTWLPHLERNNRSYVTIAIGCTGGKHRSVYIAEMLAKNFRKERDDIQTHHRDIDIKST | Displays ATPase and GTPase activities. | Q47VH8 |
Q609A8 | Y1327_METCA | Nucleoid-associated protein MCA1327 | Methylococcus | MKNPLANLMQQAQRFQETFQKTQEEIAATEIQAESGGGLVKIRMNGKREVLKVEIDPSLRQEEHEVLEDLIAAAFNDGVRRVAKLKQEKMAGLTGSLGIPPGFNLPF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | Q609A8 |
Q86L54 | Y2829_DICDI | TNF receptor-associated factor family protein DDB_G0272829 | Dictyostelium | MKLGRDIPIYKLIIIKNESIENNLKEISFSDNFKCQICEGLLISSLIPNRMKALQCINGHCFCLTCWESILEIKSECPTCRIQIQSMNTLSNNLFIIKSISESIKIHCPNYLNFDNSNNFNGCKEIITIDEIDRHESKCEFRFIKCSINNQCNEIIRFNERDKHESQCDFIIQKCTHCDESVQMKQMQGHILFECLKVLITCQHCSLQFTRLKLQNHIENHCKEIKIECPFKSLKIIYNNNNNDNDNNDSDENNSNQSLSSSSLSSSIIPLSPCNELMKRSELSKHFIRNHQYHNELVSIVLKKQENKIKKLETIIQQNNVNQNFEISIIKHSNSLTRDSFYKENKKKDKLIQDLMKRVLILEHQQQQNQIQNQIQNQIQKLSNKSIFTTTTTTTSTSDKNNNNNNNNNNNNNNNNEDEEDDDNIKNNDNQGNLKSLREMFNTISNFKDDENEQQQIQQQQQLPFTSFGPLSVQQQNNPTKQFNQLSQPQTQPQSQSQSQSLFGEWSPITINQNQNTPSNPFSIFSGTSL | Probable adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. | Q86L54 |
P04689 | TBA2_SCHPO | Tubulin alpha-2 chain | Schizosaccharomyces | MREIISIHVGQAGTQIGNACWELYCLEHGIQPNGYMNPETASQNSDGGFSTFFSETGQGKYVPRSIYVDLEPNVIDQVRTGPYRDLFHPEQLITGKEDASNNYARGHYTVGKELVDEVTDKIRRIADNCSGLQGFLVFHSFGGGTGSGFGALLLERLAMEYTKKSKLQFSVYPAPQVSTSVVEPYNSVLTTHATLDLADCTFMVDNESCYDICRRNLDIERPSYENLNRLIAQVVSSITASLRFEGSLNVDLAEFQTNLVPYPRIHFPLVTYAPIVSAAKAFHESNSVQEITNQCFEPYNQMVKCDPRAGRYMATCLLYRGDVIPRDVQAAVTTIKAKRTIQFVDWCPTGFKIGICDRPPQHIEGSEIAKVDRAVCMLSNTTSIAEAWSRLDHKFDLMYSKRAFVHWYVGEGMEEGEFSEAREDLAALERDYEEVGQDSMEVDYMEEEY | 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. | P04689 |
F6H9A9 | THI41_VITVI | Thiazole biosynthetic enzyme 1 | Vitis | MATLTSSICSKPKASVFDPHKSSFHGVPIATQARLSPVKSTPVNLAVTAAAMPYDLRSFKFEPIKESIVSREMTRRYMMDMITYADTDVVVVGAGSAGLSCAYELSKNPSVQVAIIEQSVSPGGGAWLGGQLFSSMVVRKPAHRFLDELGLEYDEQDNYVVIKHAALFTSTIMSKLLARPNVKLFNAVAAEDLIIKEGKVGGVVTNWALVSMNHDTQSCMDPNVMEAKVVVSSCGHDGPFGATGVKRLRSVGMIDSVPGMKALDMNTAEDEIVRLTREVVPGMIVTGMEVAEIDGSPRMGPTFGAMMISGQKAAHLALKSLGLPNALDGTYIGNLHPELVLAAAADAAEIAEA | Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance. | F6H9A9 |
C5D3Y4 | UPPP_GEOSW | Undecaprenyl pyrophosphate phosphatase | unclassified Geobacillus | MDIVEIIKAIILGMVEGLTEFAPVSSTGHMIIVDDMWLKSQEFLGKYAANTFKVVIQLGSILAVVVVFKDRFIDLLGLRGRHRDGKPRLKLMQVIVGLIPAGVLGVLFEDYIDEHLFSTATVLIGLVLGALLMIAADVFAKKAPKAQTVDQITYKQALIVGLVQCLSLWPGFSRSGSTISGGVLVGMSHRAAADFTFIMAVPIMMGASVLSLLKNWQYFTIDALPFFTAGFISAFLFALISIRFFLKLINQIRLVPFAVYRIVLALVIYIVYF | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | C5D3Y4 |
Q9Z9P4 | TATC_HALH5 | Sec-independent protein translocase protein TatC | Halalkalibacterium (ex Joshi et al. 2022) | MNERDMSLMDHIAELRRRILIIVVFFVIALVVGFFLATPMITYLQGAPTAQDLPMNAFKLTDPLRVYMTFAFTSAFILVFPIILYQLWAFVSPGLHENERKATLAYIPIAFFLFLGGLSFAYFILFPFLIQFIGGLAERLHINELYGINEYFTFLFQITMPFGVLFQLPVVVMFLTRLGIVTPEFLRSVRKYAFFVLLVVAGFITPPELISHLMVTVPLLLLYEFSIWVSHLTYRKVQKLEKLRQEEYRQEEG | 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. | Q9Z9P4 |
Q9Y5L0 | TNPO3_HUMAN | Transportin-SR | Homo | MEGAKPTLQLVYQAVQALYHDPDPSGKERASFWLGELQRSVHAWEISDQLLQIRQDVESCYFAAQTMKMKIQTSFYELPTDSHASLRDSLLTHIQNLKDLSPVIVTQLALAIADLALQMPSWKGCVQTLVEKYSNDVTSLPFLLEILTVLPEEVHSRSLRIGANRRTEIIEDLAFYSSTVVSLLMTCVEKAGTDEKMLMKVFRCLGSWFNLGVLDSNFMANNKLLALLFEVLQQDKTSSNLHEAASDCVCSALYAIENVETNLPLAMQLFQGVLTLETAYHMAVAREDLDKVLNYCRIFTELCETFLEKIVCTPGQGLGDLRTLELLLICAGHPQYEVVEISFNFWYRLGEHLYKTNDEVIHGIFKAYIQRLLHALARHCQLEPDHEGVPEETDDFGEFRMRVSDLVKDLIFLIGSMECFAQLYSTLKEGNPPWEVTEAVLFIMAAIAKSVDPENNPTLVEVLEGVVRLPETVHTAVRYTSIELVGEMSEVVDRNPQFLDPVLGYLMKGLCEKPLASAAAKAIHNICSVCRDHMAQHFNGLLEIARSLDSFLLSPEAAVGLLKGTALVLARLPLDKITECLSELCSVQVMALKKLLSQEPSNGISSDPTVFLDRLAVIFRHTNPIVENGQTHPCQKVIQEIWPVLSETLNKHRADNRIVERCCRCLRFAVRCVGKGSAALLQPLVTQMVNVYHVHQHSCFLYLGSILVDEYGMEEGCRQGLLDMLQALCIPTFQLLEQQNGLQNHPDTVDDLFRLATRFIQRSPVTLLRSQVVIPILQWAIASTTLDHRDANCSVMRFLRDLIHTGVANDHEEDFELRKELIGQVMNQLGQQLVSQLLHTCCFCLPPYTLPDVAEVLWEIMQVDRPTFCRWLENSLKGLPKETTVGAVTVTHKQLTDFHKQVTSAEECKQVCWALRDFTRLFR | (Microbial infection) Involved in immunodeficiency virus (HIV-1) infection by importing the pre-integration complex (PIC) into the nucleus . Required for a nuclear maturation step of HIV-1 prior to integration . | Q9Y5L0 |
A9WDJ3 | TRMD_CHLAA | tRNA [GM37] methyltransferase | Chloroflexus | MRFDILTLFPAMFQGPLTESILKRAQQAGRIEIHLHDIRQWTTDRHRTADDTPYGGGAGMVMKAEPLAAAIRAVRAADERPGVTILLTPDGELLTQQIVRELATLPRLLLVCGHYEGIDERVRETLIDRELSIGDYVLTGGELAAMVVVDAVARLVPGVIDSESIVEESHSDFLLEYPHYTRPAVWEGRAVPPVLLSGHHGEIARWRRAERLRRTLVRRPDLLARAAAAGVLTKADLALLAELGWRPETSNGA | Specifically methylates guanosine-37 in various tRNAs. | A9WDJ3 |
Q8QZZ7 | TPRKB_MOUSE | TP53RK-binding protein | Mus | MQLSQQLDLFPECRVTLLLFKDVKNAGDLRKKAMEGSIDGSLINPNVIVDPFQILVAANKAVHLHRLGKMKTRTLSTEIIFNLSPNNNISEALKKFGISETNTSVLIVYIEDGSKQVPQEHLVSQVEGQQVPLESLPEITRLSEVKKIYKLSSQEERIGTLLDAIICRMSTKDVL | 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. | Q8QZZ7 |
Q5ZJK8 | TCPH_CHICK | CCT-eta | Gallus | MMPTPVILLKEGTDTSQGIPQLVSNINACQVIAEAVRTTLGPRGMDKLIVDDRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKDIAVSVKKEDKDEQRSLLEKCAATALSSKLISQSKEFFSKMVVDAVMMLDDLLQLKMIGIKKVQGGALEDSQLVAGVAFKKTFSYAGFEMQPKKYQSPKIALLNVELELKAEKDNAEVRVNTVEDYQAIVDAEWNILYDKLDKIHKSGAKVVLSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALSDDVLGRCELFEEIQIGGDRYNFFTGCPKAKTCTIILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRAKHAQGGMWYGVDVNNEDIADNFEACVWEPAIVRINALTAASEAACLIVSVDETIKNPRSTVDAPPGGRGRGRGQTPQPLRPRSVALS | Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. | Q5ZJK8 |
O33017 | TRMD_MYCLE | tRNA [GM37] methyltransferase | Mycobacterium | MKIDIVTIFPAYLDPLRQSLPGKAIESGLVDVQVHDLRRWTHDVHHSVDDVPYGGGPGMVMKAPVWGEALDEICFDETLLVIPTPAGALFTQATAQCWSTERHLVFACGRYEGIDQRVVDDAVRRMRVEEVSIGDYVLPGGESAAVVMIEAVLRLVAGVLGNPASHRDDSHSPDLGRLLEGPSYTRPPTWRGLDVPPVLLSGDHARIAAWRREASLRRTRKRRPDLSGARFVWGLGLS | Specifically methylates guanosine-37 in various tRNAs. | O33017 |
P12460 | TBB2_SOYBN | Beta-2-tubulin | Glycine subgen. Soja | MRESLHIQGGQCGNQIGAKFWEVVCAEHGIDPTGRYGGDSELQLERINVYYNEASCGRFVRRAVLMDLEPGTMDSVRSGPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADESMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLASRGSQQYRALSVPELTQQMWDSKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMINVQNKNSSYFVEWIPHNVKSTVCDIPPTGLRMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEDEYEEEEEEEEFAQHDM | 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. | P12460 |
P75512 | THIO_MYCPN | Thioredoxin | Mycoplasma | MVTEIKSLKQLGELFASNNKVIIDFWAEWCGPCKITGPEFAKAASEVSTVAFAKVNVDEQTDIAAAYKITSLPTIVLFEKGQEKHRAIGFMPKAKIVQLVSQ | Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | P75512 |
Q9UJW2 | TINAG_HUMAN | Tubulointerstitial nephritis antigen | Homo | MWTGYKILIFSYLTTEIWMEKQYLSQREVDLEAYFTRNHTVLQGTRFKRAIFQGQYCRNFGCCEDRDDGCVTEFYAANALCYCDKFCDRENSDCCPDYKSFCREEKEWPPHTQPWYPEGCFKDGQHYEEGSVIKENCNSCTCSGQQWKCSQHVCLVRSELIEQVNKGDYGWTAQNYSQFWGMTLEDGFKFRLGTLPPSPMLLSMNEMTASLPATTDLPEFFVASYKWPGWTHGPLDQKNCAASWAFSTASVAADRIAIQSKGRYTANLSPQNLISCCAKNRHGCNSGSIDRAWWYLRKRGLVSHACYPLFKDQNATNNGCAMASRSDGRGKRHATKPCPNNVEKSNRIYQCSPPYRVSSNETEIMKEIMQNGPVQAIMQVREDFFHYKTGIYRHVTSTNKESEKYRKLQTHAVKLTGWGTLRGAQGQKEKFWIAANSWGKSWGENGYFRILRGVNESDIEKLIIAAWGQLTSSDEP | Mediates adhesion of proximal tubule epithelial cells via integrins alpha3-beta1 and alphaV-beta3. This is a non catalytic peptidase C1 family protein. | Q9UJW2 |
Q87VY6 | THIE_PSESM | Thiamine-phosphate pyrophosphorylase | Pseudomonas | MKLRGLYAITDSQLLTGKFLSYVEAALDGGVTLLQYRDKTGDDSRRLREATELLKLCERYKTRLIINDDAELAARLGVGVHLGQTDGSLPDARALLGHKAIVGATCHGQLELAEQAKADGATYVAFGRFFNSQTKPGAPAVPLDLIAQVRARVHLPIAVIGGITLENAPQLVEHGADLLAVVHGLFGAETPQEVTRRAKAFMALL | Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). | Q87VY6 |
P0DP46 | TP1B_HADIN | Double-knot toxin | Hadronyche | NECIRKWLSCVDRKNDCCEGLECYKRRHSFEVCVPIPGFCLVKWKQCDGRERDCCPGLECWKRSGNKSSVCAPIT | This toxin potently and selectively inhibits ASIC1a, an isoform of the gene ASIC1. It incompletely inhibits ASIC1a activation in a pH-independent and slowly reversible manner. This toxin acts by binding to and stabilizing the closed state of the channel, thereby impeding the transition into a conducting state. This toxin may bind to the acidic pocket of ASIC1a, since mutation of a key residue of this pocket (Arg-350) abolishes the ability of the toxin to inhibit ASIC1a. In vivo, this toxin protects the brain from neuronal injury when administered up to 8 hours after stroke onset. | P0DP46 |
Q1QUK4 | YEGS_CHRSD | Probable lipid kinase YegS-like | Chromohalobacter | MNETIQPCEHDGDTWLILNGKSAQLPEVREAVGRVREAGHHLAVRVTWEGGDGVRLAREASEAGIARVIAGGGDGTVNEIVGGLMQLASETRPALGILPLGSANDFAGGLGLPEEPYEALRVALETPPRRVDVGTLGDDYFINLASGGFGAQITNSTPAPLKRLLGGGAYSLMGMLKAWNYQPYQGRLRFPDGERNVPLFLLALGNGCQAGGGQQLAPLAKIDDGLLELLIVRHFTSLREMKQLIDELENLPESGDFVEYLQVPWVEFESEHALPLNLDGEPCFHENFRAALMPGALCLAAPEGSALLSHQ | Probably phosphorylates lipids; the in vivo substrate is unknown. | Q1QUK4 |
Q19AV6 | ZSWM7_HUMAN | SWIM-type zinc finger domain-containing protein 7 | Homo | MAVVLPAVVEELLSEMAAAVQESARIPDEYLLSLKFLFGSSATQALDLVDRQSITLISSPSGRRVYQVLGSSSKTYTCLASCHYCSCPAFAFSVLRKSDSILCKHLLAVYLSQVMRTCQQLSVSDKQLTDILLMEKKQEA | Involved in early stages of the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. | Q19AV6 |
Q8TLP5 | TRPD_METAC | Anthranilate phosphoribosyltransferase | Methanosarcina | MKGMKEYIKKLEEGSDLSSEEAEAAIGEILSTAEDEEIGAFLLALRAKGEKPQEIAGFVRGMKQAGNTIKPVTPFRVIDTCGTGGDGLNTINVSTAAAIVTAAAGVPVAKHGNRAATSMSGSSDVLEALGIKVDLTPGQVRKTIEKIGIGFMFAPVFHPAMKRVAGVRKKLGVRTVFNILGPLTNPAGAKGQVVGVFDKKLCEPIAYALAELGTEHALVVHGDGMDEISNTGETFVAELKDGEVSTYTITPEAMGMLRAKPEDIKGGTPKENARDLLCIFKGQKGPKRDLVILNAAAALYVSGIVGSIRQAIPIAEDAIDSGKVMVKFNQFRNFTAELSIQGKKEGSCPGEAFLASSDTSVLSPASGEKA | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | Q8TLP5 |
O28205 | THIE_ARCFU | Thiamine-phosphate pyrophosphorylase | Archaeoglobus | MSRLEDYLSVYFITDSEFGRTHEELAEMALRAGVRAIQFREKKLSTKRMYEIGKRLRALTRDYDALFFVNDRIDVALAVDADGVHIGQDDMPAFAAREIFPGYIGVSAGNVEEAKKDERFADYLGVGPVFPTKTKEDAGEAIGIEGLRRIVESVSVPVVAIGSINKQNAIEVLKTGVAGIAVISAIAAADDPERAARELVELVRRFKSGL | Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). | O28205 |
Q88RA3 | TAUD_PSEPK | Alpha-ketoglutarate-dependent taurine dioxygenase | Pseudomonas | MSLTITPLSPALGAQISGVDISRDISAEERDAIEQALLQHQVLFLRDQPINPEQQARFAARFGDLHIHPIYPNVPDTPQVLVLDTAVTDVRDNAVWHTDVTFLPTPALGAVLSAKQLPAYGGDTLWASGIAAFEALSAPLREMLDGLTATHDFTKSFPLERFGTTPQDLARWEATRRNNPPLSHPVVRTHPVSGRKALFVNEGFTTRINELSELESDALLRLLFAHATRPEFSIRWRWQENDVAFWDNRVTQHFAVDDYRPNRRVMHRATILGDAPF | Catalyzes the alpha-ketoglutarate-dependent hydroxylation of taurine yielding sulfite and aminoacetaldehyde after decomposition of an unstable intermediate. | Q88RA3 |
A8ALJ5 | ZAPD_CITK8 | Z ring-associated protein D | Citrobacter | MHTQVLFEHPLNEKMRTWLRIEFLIQQLSVNLPLADHADALHFFRNIGDLLDVFERGEVRTELLKELERQQRKLQAWVEVPGVDQSRIEALRQQLKTAGSILISAPRIGQQLREDRLIALVRQRLSIPGGCCSFDLPTLHIWLHLPQEQRDAQVETWIASLNPLNQALTLILDLIRNSSPFRKQTSLNGFYQDNGDDADLLRLQLALDSQLYPQISGHKSRFAIRFMPLDSENGLVPERLDFELACC | 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. | A8ALJ5 |
Q1BYZ6 | UBIA_BURCA | 4-HB polyprenyltransferase | Burkholderia cepacia complex | MLARFPLYLRLVRMDKPIGSLLLLWPTLNALWIASDGRPRWPLLVIFTLGTLLMRSAGCAMNDYADRDFDRHVKRTADRPLTSGKIRAWEAVAIAVGLSFIAFLLILPLNTLTKELSVVALFVAGSYPFMKRFFAIPQAYLGIAFGFGIPMAFAAVQDTVPMLAWVMLVANIFWSVAYDTEYAMVDRDDDIKIGIRTSALTFGRFDVAAVMACYAATLGIYVWIGVTLGFGLAYWVGWAAAVGCALYHYTLIKDRERMPCFAAFRHNNWLGGVLFAGIAAHYLLAGN | 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. | Q1BYZ6 |
X5M5N0 | WNK_CAEEL | Protein kinase with no lysine 1 | Caenorhabditis | MPDSITNGGRPPAPPSSVSSTTASTTGNFGTRRRLVNRIKKVDELHPAQENPTMGSHWLSEQERSRLEAVQQDWRRTRPMKFQWTSKKRPDDPTTSSPSTVSISNALENSTPSLNNVSSITNSSSPFSLSSAATSTASAIIPFTSNVATNHPHLNHHVSRIPQAIVTGGTNGSLPPLLISPTSAAAATPLISGKAGPMSPSTGSPINVAATVLQNAVSSPQHSIFDRSRLNKIPPNTSLASSSSPSDAANNDKPIQQRHSILSNVRTLTQAMVNDGPRTLTGDDMDKMVSEEERARKEQEKREEEEKAARRIDVEDDFDAQEKPIDKSKNGRFLKFDEELGRGSFKTVFRGLDTETGVAVAWCELQESKLNKTERQRFREEAEMLKDLQHPNIVRFYDYWESADLCGKRKYIVLVTELMTSGTLKMYLKRFKRINIKVLKSWCRQILKGLSFLHTRNPPVIHRDLKCDNIFITGTTGSVKIGDLGLATLKNKSFAKSVIGTPEFMAPEMYEEMYDESVDVYAFGMCLLEMVTGEYPYSECMNPATIYRKVISGVKPECFSRIPAQYPEIREIIDRCIRVRREERSTVKQLLVDDFFTPEDLIGIRVEIKNRDADLNDLNVEIQMQLRVYDEKKRKQYRFKENEGLQFAFDIENDSPDEVVQQMIEQQHIPDEDTRMITKLIKDKVDAFRRDRDHRLLEIKRAKEEEERIREEAEIKEELRLRAEAKEKEKERLEKERLEKKAAAAAAANPNPTPIPPTPATPHSSAQQQPIPPPLSTQTSAEIQQSAQQPSVPVTMIANIPAMSPTSAQPQPVLSPTSAAVPVPTTMIHVPKPSEIPVQNVATTAAPVAANNVPPSPAPFKTEDIQTPTLAQNTVPRTISTDASGLVINTPASIASPSPAPSATDVASTTAPVTPAPTPTTTTDGGAAAASTTTENKEEKRKSNKRKVVMEILGCDESRNFALVSCRLDTSHKSVTFQFAPGTDKPCTIATKLLAEDCLLKVHVHIVEAQLGEVIQLINSDGKKGVGTKLATVLDPNSTEPPTITAVMPKDSSAATASNTKPKIEIEKTPPTRDASQEPNNVQVTNVRKVSQESNAESVQSIPRPGGIIVMSPTNQTDSAPPPTGAAAKPSRFQVTKSADPIATPISSSISTATVIPIVAATPTNITSEPVIVQPITAQVITHLATPSPVSHSLSSNSSPSATTHSNMSSIQSTTSVPGRRFTVQPVSQAESGISSSISTPHPEPTPAITSCPPPVPSVPPVVSNGTLNLEVAPKQTPSATNQNVDTQHSSSTASTATLVSETPATVHVTPISVPAPVQEPLVIDHHSDVLTQLDSELRKCFQVSGVSHSASPSTVVESLTSMTPQTIPLACQTVPASIGQAPAVIAAAHAASLIPNASVPQSPSRLDAETGLAGLHEKLEALKMEQDRREDMGDDAIGTTTTDGKDEIPIDTLKGLAEALGKVIHADGRETTPMPPDHPDLTDASTQQLISPSNPDVLTTMSSAVEGSASSTMIEDIDASTSAVDASMMNSMPPGAQNSTDQIPAAMTLSMDQECAQSMTSSITRNTTGTKLATFENLETALSSTLGTHIRQPNAPSSRDETTAPMTPSFTNERIGGGGGGGATSFSIGTPPSHSPFPVSECDYDLKGQMDLESEDPEVIQMIVRHRMEQHKLLEKQRVEIERLRSKIRVPRATSVNPEMIGDDEADTTLTALQSALGNASLSLPASPPPNTEIPDNEGQHHCNSFRCIGDPNDNVSIVNQIKQRLGIIPSSRQSVRSATSSSPSTPPSSSSAPPKSLSSPTKSYVSHCSLSIGYGSTASSEQQQREPSPSATTSSFLSDPATGVIENV | Serine/threonine-protein kinase which phosphorylates gck-3 . Plays a role in osmotic stress responses during which it increases gpdh-1 translation, likely by phosphorylating gck-3 . Essential for larval development and the tubular formation of the excretory canals . | X5M5N0 |
B1LV84 | TIG_METRJ | PPIase | Methylobacterium | MQVTEINAQGLKREFQVLLAAQELEERLTNELSGMKDKVQLKGFRPGKVPVAHLRKVYGRSVMAEVVQNAVNEANRQIVTDNGLKLALEPQVEFPTDQAEVEKALDAKGDLAFKVALEVMPSFELADLSDVSLTKLVAKPSDAEVDEALDRMAGQSRPFTEREEGAEAQSGDRVTIDFVGRIDGEEFQGGKGEGIDLELGSGSFIPGFEDQLVGAKVGDKRLVKVTFPESYGAEHLAGKDAEFDVTVTKIQAAGEAKIDDEFAKSMGMESLEKLREAVSEAIGRDFEAASRRRLKKELLDALDGKYAFELPPSLVAQEFAAVWAQVEQDLKTRGKTFEDEDTTEEKAQAEYRKIAERRVRLGLVLAQVGESADIKVSDEEVNQALIARVRQFPGQEQQVWDFYRKNAQALAELRAPLFEEKVVDHVLGQVKLVEEPVSKEALFADEDGDDTTGGKPADKAEAKDESKTEAKAD | 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. | B1LV84 |
Q9H7R5 | ZN665_HUMAN | Zinc finger protein 160-like | Homo | MALPQGQLTFKDVAIEFSQEEWTCLDPAQKTLYRDVMLENYRNLVSLDISCKCVNTDLPPKGKNNMGEAFYTVKLERLESCDTVGLSFQEVQKNTYDFECQWKDDEGNYKTVLMLQKENLPGRRAQRDRRAAGNRHIENQLGVSFQSHLPELQQFQHEGKIYEYNQVEKSPNNRGKHYKCDECGKVFSQNSRLTSHKRIHTGEKPYQCNKCGKAFTVRSNLTIHQVIHTGEKPYKCNECGKVFSQPSNLAGHQRIHTGEKPYKCNECGKAFRAHSKLTTHQVIHTGEKPYKCKECGKCFTQNSHLASHRRIHTGEKPYKCNECGKAFSVRSSLTTHQTIHTGEKPYKCNECGKVFRHNSYLAKHRRIHTGEKPYKCNECGKAFSMHSNLTKHQIIHTGEKPFKCNECVKVFTQYSHLANHRRIHTGEKPYRCDECGKAFSVRSSLTTHQAIHTGEKPYKCNDCGKVFTQNSHLASHRGIHSGEKPYKCDECGKAFSQTSQLARHWRVHTGEKPYKCNECGKAFSVHSSLTIHQTIHTGQKPYKCNDCGKVFRHNSYLAIHQRIHTGEKPYKCNECGKAFSVHSNLATHQVIHTGEKPYKCNECGKVFTQNSHLANHRRIHTGEKPYRCNECGKAFSVRSTLTTHMAVHTGDKPYKCNQCGKVFTQNSNLAKHRRIHSG | May be involved in transcriptional regulation. | Q9H7R5 |
Q07163 | TY1AB_YEASX | p60 | Saccharomyces | MESQQLSQHSPNSHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQKLTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIQQCGMEEVRGWSCVFKNSQVTICLFVDDMVLFSKNLNSNKRIIEKLKMQYDTKIINLGESDEEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH | Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome. | Q07163 |
B7KNS9 | TIG_METC4 | PPIase | Methylorubrum | MQVTETTSEGLKREFQVLLPANELEDRLNTELSNIKGKVQIKGFRPGKVPVAHLRKVYGKSVMADVLQNAVNEANQQIVTDKGLRLALEPQIEFPKDEEQTIIERALDAKGDLAFKVKLEVLPSFELADLSDVSIKKLVLKPSDEEVNETLERMAKDSRSFEPREEGAEAQSGDRVTIDFVGRIDGTEFEGGKGEDVDLELGSNTFIPGFEDQLVGAKVGDSRLVKVAFPADYQAEQLAGKDAEFDVTVKAVAAPGETKIDDELAKRFGMDDLEKLKEAVSKAVGSDYEAQSRRKLKKELLDALDGKYAFDLPPSLVHQEFAAVWAQVEQDLKTRGKTFEDEGTTEEASQAEYRKIAERRVRLGLVLAQVGETADIKVSDDEVNQALFARIRQFPGQEKQVYDFYRNNPQALAELRAPLFEEKVVDHVLGQVQVVEEPVSKEALFAEDDEADAVTGGAATDEKPSESNNEAAADKAAG | 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. | B7KNS9 |
B4GYC7 | UBA5_DROPE | Ubiquitin-like modifier-activating enzyme 5 | Sophophora | MTNAIDELQAIIAELKTEVEEQRAVIRQSRDRIEHMSAEVRMNIVKNYERIRDKTVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNRLFFTPDQAGLSKVEAAARTLTFINPDVRIETHNYNITTIDNFDNFLNTITGDGTVAGEPVDLVLSCVDNFEARMAINAACNEKCLNWFESGVSENAVSGHIQFLRPGDTACFACAPPLVVAENIDEKTLKREGVCAASLPTTMGITAGFLVQNALKYLLNFGEVSDYLGYNALNDFFPKMTLKPNPQCDDRNCLLRQKEFQARPKPVVVQEEAPTDEPLHASNDWGIELVAEDAPSNAPTDLSQSTDVGQGLRLAYEAPEKSSAEATQAATAPVDDTSLEDLMAQMKSM | E1-like enzyme which activates UFM1. | B4GYC7 |
A0Q149 | YQGF_CLONN | Putative pre-16S rRNA nuclease | Clostridium | MRVLGLDVGDRTIGVAVSDPLGFTAQGITTVHRKSVKEDIDELKKICKEYAVELIISGLPKNMNGTVGEQGEKVIEFCELLKSELKMPIKMWDERLTTVAAHRAMLEANLSRAKRKKIVDKMAATYILQGYLDSI | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | A0Q149 |
C0R3B8 | TSAD_WOLWR | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | unclassified Wolbachia | MKTILAVETSCDETAVAIVNSDKQVLAHEILSQAEHKKRGGVIPEIASRAHMEHLSGLIKSAVEKSNLNFCDLNAIAATSGPGLIGGLIVGTMMAKAIAHVAQKPFIAVNHLEAHALVIRLLHEVKFPFLVLLISGGHCQFLIAQDVGKYIKLGETLDDSLGEAFDKVAKMLGLSYPGGPLIEKLAKKGNGARFKLPRAMIKRYGCNFSFSGIKTAVKNLVQELKMSEQDVCDVCASFQECISDILLDRVSNAIIMAESLNIKINDFVITGGVAANNFLREKLKQHINLNIFFPPNDLCTDNAIMVGWTGIERLQKNYIDPLNFAPRPKWELESY | 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. | C0R3B8 |
O28469 | TOP1_ARCFU | Untwisting enzyme | Archaeoglobus | MVMSWLIITEKDNTARRIASILFKDVKTLKKGRVSYYHSPSNDAYVVGLKGHIVELDFPKELNNWTKTPLEKLLQAELVKKVKERTISSILKEIAKKADRVTVATDYDREGELIGVEALEIVKSVNPTVKVDRVRYSAVTEKEIRSAFSKPVKVDFNLANAALARQKIDLIWGATLTRLISVHSGRMGKDFLSVGRVQTPTLRLIVDRELEIQNFKPEKYYEIFAEFEGFIAKHPKRYGSKEEAEKLFAKIGETAKVEEFTRRRMEENRPTPFNTTEFLREASKFMSPHKAMNIAETLYMNGYISYPRTDNTVYPPTINLIEIVSALSSVFPREAQIVLSQDKITPSRGRRETKDHPPIYPTGVAKRGELSKDEWTIYELVVRRFLATLAPKAVWDVRRVVLDSNGVKFVANGRQLVEAGWRDIYIYSKAEETELPLLKKGDVLRILKKRLEEKETKPPGRYSASSLIKMMEKLNLGTKSTRHEIIQKLVSRRYIHGNPFRPSETAFSVINVLKETAETITLPDMTAKLENEMDLIAEGKKREPEVVDESREMLLQILRAIDYRKLSKDLREGVKKDKIVGKCPECGGELVVRQSKAGKRFIGCSNYPDCTFTLPLPQNGTLYITAKQCKEHEIKEVKIRTKKGYWNLGCPYCNYLNWKKENS | Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. | O28469 |
P84195 | XYNA_GLOTR | Endo-1,4-beta-xylanase Xyn10A | Gloeophyllum | LYMGTATDNGATAMLNLVESLKYSWVPSTFSGQGAATPYDSNLVK | Has xylanase, avicelase and cellobiohydrolase activity. | P84195 |
Q58762 | WTPC_METJA | Molybdate/tungstate import ATP-binding protein WtpC | Methanocaldococcus | MLKVNNLSKIWKDFKLKNVSFEIDREYCVILGPSGAGKSVLIKCIAGILKPDSGRIILNGEDITNLPPEKRNVGYVPQNYALFPNKNVYKNIAYGLIIKKVNKLEIDRKVKEIAEFLNISHLLNRDVKTLSGGEQQRVALARALILNPSILLLDEPTSAVDIKIKESIISELKKIKHIPVLHITHDLAEARTLGEKVGIFMNGELIAFGDKSILKKPKNKKVAEFLGFNIIDDKAIAPEDVIIKDGNGGEVVNIIDYGKYKKVFVKYNGYIIKAFTERDLNIGDNVGLEFREQTKLT | Part of the ABC transporter complex WtpABC involved in molybdate/tungstate import. Responsible for energy coupling to the transport system. | Q58762 |
P05469 | YKP3_KLULA | Uncharacterized killer plasmid pGKl-2 protein 3 | Kluyveromyces | MSGSFRSNFSIASIHLRLYETIKSQSRIILLFCRGMFKRFAKYKSNLESAMVDVELEARIQIPKPTNIIFEDETVITYYRSTMYPSLIFRRINNGKLNSKETVEKIKYGEVTICLSIEQTYSNMDIKFPIIPANKRTISRKRICENPIVDITKCGDQYTLEIEFDYSNYMHIEKILKEWKNPYWPPVKPMEISSSNLAKKLANNEQWCISPKADGIHVLVYSDGENQFIVHTNGYTEGDTNIKVNRIFEGELMSNGEILYFDCLMWENKNITKLDYIARYKYLENMNKKEIILFNNIYAIKKYLDKKHDFETDGYIITNIKNRKKVYKSKFKNTVDLRYKNGYLLLENEEFSERSPKNVNEQLEEDKIYEFDMEMNLIRERKDKTIANYKMPYDDNPIYKIAHSIGVPTLRYYHNKIKRELLSMLPKTTLLDIGSAKGGDITKWTNLKFEKVYAVDPNLELRQRSKKVVEIRENIEDVYKMFDYESVSLFFVPWNDKFMDVINKAKYFVLICMDKPVTVKEDCFECKIENEKVILKIPDTQTSEYVEENLIKYTDVFKKLKNWKHMKINRTMNTGSAQEIELSRMYSYHFFSKK | The presence of the two linear plasmids, termed pGKL1 and pGKL2, in strains of Kluyveromyces lactis confers the killer phenotype to the host cell, by promoting the secretion of a toxin able to inhibit the growth of sensitive strains. | P05469 |
Q6HPD3 | TSAD_BACHK | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Bacillus cereus group | MGEYIMEKNTIILGIETSCDETAVAVVKNGTEIIANVVASQIESHKRFGGVVPEIASRHHVEEITVVLEEALKEANITFDDIDAIAVTEGPGLVGALLIGVNAAKAVAFAHDIPLVGVHHIAGHIYANRLVKEVQFPLLSLVVSGGHTELVYMKEHGSFEVIGETRDDAAGEAYDKVARTLSMPYPGGPHIDRLAHEGKPTIDLPRAWLEPDSYDFSFSGLKSAVINTVHNAKQRGIEIAPEDLAASFQESVIDVLVTKASRAADAYNVKQVLLAGGVAANKGLRARLEAEFAQKENVELIIPPLSLCTDNAAMIAAAGTIAYEQGKRATLALNANPGLDIES | 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. | Q6HPD3 |
Q72NR4 | TPX_LEPIC | Thioredoxin-dependent peroxiredoxin | Leptospira | MTKVTLKGNPVQLEGKIPSPGDKAPDFKAIKQDLSEFSLKDYAGKVKILVAVPSLDTSVCALETKAFNEKAAGISGVTTLVISGDLPFAMGRFCSTEGINSPNLVTGSQYRDFSFSKAYGTHIADGPLKGLSARAVFVLDKSDTVRYVEIVPEITTEPNYTAAIAAANAAL | 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. | Q72NR4 |
A4YZC4 | TYSY_BRASO | Thymidylate synthase | unclassified Bradyrhizobium | MHQYHDLLERILSDGAQKHDRTGTGTLSVFGHQMRFNLAAGFPMVTTKRLPLKAIVHELLWFLKGDTNIKYLHDHGVTIWDEWADANGDLGPVYGYQWRSWPTSDGGQIDQISNVVDMIRRNPDSRRLIVTAWNPADVEKMALPPCHCLFQFYVANGKLSCQLYQRSADVFLGVPFNIASYALLTMMVAQVTGLKLGEFVHSFGDVHLYSNHIEQARLQLSRTPRPLPTMTLNPDVKDIFAFRYEDFALAGYDPHPHIKAEVAV | 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. | A4YZC4 |
P91958 | TPM_MYTGA | Tropomyosin | Mytilus | MDAIKKKMVAMKMEKENALDRAEQLEQKLRETEEAKAKIEDDYNSLQKKSIQTENDLDNTQTQLQDVQAKYETTEKQIAEHEQEIQSLTRKISMLEEDIMKSEERYTTAASKLEEASKAADESERNRKVLENLNCGNDERIDQLEKQLTEAKWIAEEADKKYEEAARKLAITEVDLERAEARLEAAEAKVIDLEEQLTVVGANIKTLQVQNDQASQREDSYEETIRDLTNRLKDAENRATEAERTVSKLQKEVDRLEDELLTEKEKYKAISDELDATFAELAGY | Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction. | P91958 |
A4WVR7 | UBIE_CERS5 | Demethylmenaquinone methyltransferase | Cereibacter | MNDETSNTTHFGFRTVPEGEKAGMVHGVFTRVASKYDIMNDLMSGGIHRLWKDAMMDWLAPRPGQKLLDVAGGTGDISFRFLKRAPGAHATVCDMTESMLVEGRQRADAAQMADRLDWVVGDAMALPFASNTFDVYTISFGIRNVTRVQDALNEAFRVLKPGGRLMVLEFSQLPNPAMQWAYDRYSFNVIPVMGQIVANDRDSYQYLVESIRKFPDQETFAGMIRKAGFGLVKYRNLSMGIAALHSGWKI | 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). | A4WVR7 |
B2JGG3 | UBIA_PARP8 | 4-HB polyprenyltransferase | Paraburkholderia | MFARLPLYLRLVRMDKPIGSLLLLWPTLNALWIASDGHPSVSLLVIFALGTILMRSAGCAINDYADRDFDRYVKRTENRPITSGKIKAWEAVALAAGLSLVAFLLILPLNALTKELSVAALFVAGTYPFTKRFFAIPQAYLGIAFGFGIPMAFAAVQNQVPLLAWVMLIANVFWSVAYDTEYAMVDRDDDIKIGIRTSALTFGRFDVLAIMLCYAVTLGIYVGIGFTLGFGVLYWIGLAAAAGCAVYHYTLIKGRERMPCFAAFRHNNWLGGALFAGIAAHYAAQAF | 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. | B2JGG3 |
P21725 | TKTC_CUPNH | null | Cupriavidus | MNAPERIDSAARCANALRFLAADAVEQAKSGHPGAPMGMAEMAEVLWRRHLRHNPANPAWPDRDRFVLSNGHASMLQYALLHLTGYDLPMSQLRQFRQLHAATPGHPELGVTPGVETTTGPLGQGLANAVGMALAEKLLAATFNRPGFDIVDHHTYVFLGDGCLMEGLSHEACSLAGTLRLGKLICLYDDNGISIDGEVAGWFADDTPKRFAAYGWHVIADVDGHDAHALDAALHEAKAERDRPTLICCRTVIGKGAPAKAGGHDVHGAPLGAPEIAAMRTALGWEAEPFTVPADVADAWDARAQGAAREAEWEARFVSYCAAHPELAEEFVRRANGRLPEGFDAELMALLDAPSPLQGKIATRKASQLCLEALTPALPELLGGSADLTGSNLTNVKASVWVNHAGHGNYVSYGVREFGMAAAMNGIALHGGLIPYGGTFMTFSDYSRNAIRMAALMRLRVVHVLTHDSIGLGEDGPTHQPVEHAASLRLIPNNQVWRPCDGAETAYAWLAALRREDGPSCLVLSRQALMPFERNPAQRAEIARGGYVLRDVPAPRVVLIATGSEVEIAMRAALDLADAGIAARVVSMPCVELFYAQDVAYRDTVLPPGLPRVSVEAGGTWFWRGVVGEQGLALGIDTFGESAPAEALYQHFGLTPAHVAAAARVLLEEA | Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. | P21725 |
O76024 | WFS1_HUMAN | Wolframin | Homo | MDSNTAPLGPSCPQPPPAPQPQARSRLNATASLEQERSERPRAPGPQAGPGPGVRDAAAPAEPQAQHTRSRERADGTGPTKGDMEIPFEEVLERAKAGDPKAQTEVGKHYLQLAGDTDEELNSCTAVDWLVLAAKQGRREAVKLLRRCLADRRGITSENEREVRQLSSETDLERAVRKAALVMYWKLNPKKKKQVAVAELLENVGQVNEHDGGAQPGPVPKSLQKQRRMLERLVSSESKNYIALDDFVEITKKYAKGVIPSSLFLQDDEDDDELAGKSPEDLPLRLKVVKYPLHAIMEIKEYLIDMASRAGMHWLSTIIPTHHINALIFFFIVSNLTIDFFAFFIPLVIFYLSFISMVICTLKVFQDSKAWENFRTLTDLLLRFEPNLDVEQAEVNFGWNHLEPYAHFLLSVFFVIFSFPIASKDCIPCSELAVITGFFTVTSYLSLSTHAEPYTRRALATEVTAGLLSLLPSMPLNWPYLKVLGQTFITVPVGHLVVLNVSVPCLLYVYLLYLFFRMAQLRNFKGTYCYLVPYLVCFMWCELSVVILLESTGLGLLRASIGYFLFLFALPILVAGLALVGVLQFARWFTSLELTKIAVTVAVCSVPLLLRWWTKASFSVVGMVKSLTRSSMVKLILVWLTAIVLFCWFYVYRSEGMKVYNSTLTWQQYGALCGPRAWKETNMARTQILCSHLEGHRVTWTGRFKYVRVTDIDNSAESAINMLPFFIGDWMRCLYGEAYPACSPGNTSTAEEELCRLKLLAKHPCHIKKFDRYKFEITVGMPFSSGADGSRSREEDDVTKDIVLRASSEFKSVLLSLRQGSLIEFSTILEGRLGSKWPVFELKAISCLNCMAQLSPTRRHVKIEHDWRSTVHGAVKFAFDFFFFPFLSAA | Participates in the regulation of cellular Ca(2+) homeostasis, at least partly, by modulating the filling state of the endoplasmic reticulum Ca(2+) store . Negatively regulates the ER stress response and positively regulates the stability of V-ATPase subunits ATP6V1A and ATP1B1 by preventing their degradation through an unknown proteasome-independent mechanism . | O76024 |
Q9X525 | UREE_LIMFE | Urease accessory protein UreE | Limosilactobacillus | MVLTEVYRNVDDIPNIGSYHIETAMVKSDDLMKNILRVKTDHGNEYGIRLDNEDQILENGSAFKLGDKQLLVLSVIADEMIEITPRDINEMGLVAHFLGNLHKPVQIKDGKISLLLDKVVIKMLDKHDINYELKKVQLDQPLEYLDLTK | Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. | Q9X525 |
Q9V1J7 | TRMI_PYRAB | tRNA(m1A57/58)-methyltransferase | Pyrococcus | MIREGDKVVLVDPRGKRYLITVSKRDFHTDLGILKLEEIIGRNFGEAIKSHKGHEFKILRPRIVDYLDKMKRGPQIVHPKDAALIVAYAGISPGDFIVEAGVGSGALTLFLANIVGPEGRVVSYEIREDFAKLAWENIKWAGFDDRVTIKLKDIYEGIEEENVDHVILDLPQPERVVEHAAKALKPGGFFVAYTPCSNQVMRLHEKLREFKDYFMKPRTINVLVFDQEVKKECMRPRTTALVHTGYITFARRI | Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenosine at position(s) 57 (m1A57) and 58 (m1A58) in the T-loop of some tRNAs. Methylates the first adenine of an AA sequence. | Q9V1J7 |
C0QTH8 | YIDD_PERMH | Putative membrane protein insertion efficiency factor | Persephonella | MDRFLIKLIKIYKKFVSPALPNSCRYYPTCSSYAIQSIEKYGALKGSLKAVWRILRCNPFSKGGVDYP | Could be involved in insertion of integral membrane proteins into the membrane. | C0QTH8 |
C1DMY6 | THIE_AZOVD | Thiamine-phosphate pyrophosphorylase | Azotobacter | MKLRGLYAITDSRLLADGRLLPYVEAALRGGARLLQYRDKSDEDARRLREAEALRDLCLRYGAQLIVNDDLELAARLGVGLHLGQQDGSLSAARALLGPKAIIGATCHGQLELAEQAAADGASYLAFGRFFDSSTKPGAPPASLELLERARARFPQPLVAIGGVTLDNAPELIRRGAAMIAVINALFAAANAAEVEQRARAFGQLFADT | Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). | C1DMY6 |
A9VRA8 | TAGU_BACMK | Polyisoprenyl-teichoic acid--peptidoglycan teichoic acid transferase TagU | Bacillus cereus group | MKKKILFWILGIIGIMIIGGGVYAYNVYSSVSKTLDEVHKPLKRDKDSNGVETAKISKSEPVSILLLGADERGEDKGRSDSLMVITLNPKNNSMKTVSIPRDTYTEIVGKGKSDKINHAYAFGGVDMSVATVEKFLSVPINYYIEVNMEGFKDIVDAVGGVDVNNDLEFTANGHHFAKGNVHLTGDQALAFTRMRKEDPRGDFGRQMRQRQVMQAVIKKGASFSSLSSYGDVLTAIQKNVKTNLTQDQMFDMQKNYKNCLQNSEEIQIPGDGHKAADGIWYYYVPDAAKQDITNKLRAHLELTK | May catalyze the final step in cell wall teichoic acid biosynthesis, the transfer of the anionic cell wall polymers (APs) from their lipid-linked precursor to the cell wall peptidoglycan (PG). | A9VRA8 |
Q2YEM8 | TRIM5_HOOHO | TRIM5alpha | Hoolock | MASGILVNVKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKTSMPDEGERSCPVCRISYQHKNIRPNRHVANIVEKLREVKLSPEEGQKVDHCARHGEKLLLFCREDRKVICWLCERSQEHRGHHTFLTEEVAQEYQMKLQAALQMLRQKQQEAEELEADIREEKASWKTQIQYDKTNILADFEQLRHILDWVESNELQNLEKEKKDVLKRLMKSEIEMVQQTQSVRELISDLEHRLQGSVMELLQGVDGIIKRMKNVTLKKPETFPKNKRRVFRAADLKVMLEVLRELRDVRRYWVDVTVAPNNISYAVISEDMRQVSSPEPQIICEAQGTISQTFVNFNYCTGILGSQSITSGKHYWEVDVSKKSAWILGVCAGLQPDAMYNIEQNENYQPKCGYWVIGLEERVKCNAFQDGSFHTPSAPFIVPLSVNICPDRVGVFLDYEACTVSFFNITDHGFLIYKFSRCSFSQPVFPYLNPRKCTVPMTLCSPSS | Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. | Q2YEM8 |
A4XKB7 | TRUA_CALS8 | tRNA-uridine isomerase I | Caldicellulosiruptor | MRNILLTIEYDGTNYFGWQKQPNKKTVQGVIEDAIKKITGEDVNLVGSGRTDRGVHALGQKANFKTESKIPTEKFPLALNSVLPNDISIKDAAEVSLDFSARYSAKQKTYKYLIYNHKFRPAILCNYVYHFPYELDLVSMQKSCEYFIGEYDFSSFCSSGSETNSKVRRIFDCYLTFENDCIAIYITANGFLYNMARIIAGTILDVGVGRFKPTDIPLIIESKDRTKAGKTLPPWGLYLVDVVY | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | A4XKB7 |
A8GTI5 | YBEY_RICRS | Endoribonuclease YbeY | spotted fever group | MINVEIVRHYNKWREHKQINKSLIKKITQNILLRFDNFSKIKQFELSILLTNAAEILILNKQFRNIEKATNVLSFPSNELNWQDLYSKLEFLGDSDYMHLGDIAFCYEVIYNESCEQYKTFENHFIHLLIHSILHLIGFDHQNDTEANIMENLEIEILSYFGIFPPY | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | A8GTI5 |