ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
Q5U5Q3 | MPSGSSAALALAAAPAPLPQPPPPPPPPPPPLPPPSGGPELEGDGLLLRERLAALGLDDPSPAEPGAPALRAPAAAAQGQARRAAELSPEERAPPGRPGAPEAAELELEEDEEEGEEAELDGDLLEEEELEEAEEEDRSSLLLLSPPAATASQTQQIPGGSLGSVLLPAARFDAREAAAAAAAAGVLYGGDDAQGMMAAMLSHAYGPGGCGAAAAALNGEQAALLRRKSVNTTECVPVPSSEHVAEIVGRQGCKIKALRAKTNTYIKTPVRGEEPIFVVTGRKEDVAMAKREILSAAEHFSMIRASRNKNGPALGGLSCSPNLPGQTTVQVRVPYRVVGLVVGPKGATIKRIQQQTHTYIVTPSRDKEPVFEVTGMPENVDRAREEIEMHIAMRTGNYIELNEENDFHYNGTDVSFEGGTLGSAWLSSNPVPPSRARMISNYRNDSSSSLGSGSTDSYFGSNRLADFSPTSPFSTGNFWFGDTLPSVGSEDLAVDSPAFDSLPTSAQTIWTPFEPVNPLSGFGSDPSGNMKTQRRGSQPSTPRLSPTFPESIEHPLARRVRSDPPSTGNHVGLPIYIPAFSNGTNSYSSSNGGSTSSSPPESRRKHDCVICFENEVIAALVPCGHNLFCMECANKICEKRTPSCPVCQTAVTQAIQIHS | Function: E3 ubiquitin ligase responsible for the post-transcriptional regulation of common HLA-A allotypes. Binds to the 3' UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 69366
Sequence Length: 659
Domain: Binds RNA through its KH domains.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
|
Q86XN8 | MPSSLGQPDGGGGGGGGGGGVGAAGEDPGPGPAPPPEGAQEAAPAPRPPPEPDDAAAALRLALDQLSALGLGGAGDTDEEGAAGDGAAAAGGADGGAAPEPVPPDGPEAGAPPTLAPAVAPGSLPLLDPNASPPPPPPPRPSPPDVFAGFAPHPAALGPPTLLADQMSVIGSRKKSVNMTECVPVPSSEHVAEIVGRQGCKIKALRAKTNTYIKTPVRGEEPVFIVTGRKEDVEMAKREILSAAEHFSIIRATRSKAGGLPGAAQGPPNLPGQTTIQVRVPYRVVGLVVGPKGATIKRIQQRTHTYIVTPGRDKEPVFAVTGMPENVDRAREEIEAHITLRTGAFTDAGPDSDFHANGTDVCLDLLGAAASLWAKTPNQGRRPPTATAGLRGDTALGAPSAPEAFYAGSRGGPSVPDPGPASPYSGSGNGGFAFGAEGPGAPVGTAAPDDCDFGFDFDFLALDLTVPAAATIWAPFERAAPLPAFSGCSTVNGAPGPPAAGARRSSGAGTPRHSPTLPEPGGLRLELPLSRRGAPDPVGALSWRPPQGPVSFPGGAAFSTATSLPSSPAAAACAPLDSGASENSRKPPSASSAPALARECVVCAEGEVMAALVPCGHNLFCMDCAVRICGKSEPECPACRTPATQAIHIFS | Function: RNA binding protein, may be involved in post-transcriptional regulatory mechanisms.
PTM: Phosphorylated.
Sequence Mass (Da): 64883
Sequence Length: 651
Domain: Binds RNA through its KH domains.
Subcellular Location: Cytoplasm
|
Q3UE17 | MPGSTGQPDAGGAGTGTTAGDPGHPHPALAGAEDAAPRPPPEPDDAAAALRLALDQLSALGLGGARPGDEGMATRSADGATECGEDEPAPPDELEVAVAPPVTASVAPGGLPLLDPDVSPRPSPPDVFASFAPHPAALGPSTLLAEQLNVIGSRKKSVNMTECVPVPSSEHVAEIVGRQGCKIKALRAKTNTYIKTPVRGEEPVFIVTGRKEDVEMAKREILSAEHFSLIRATRSKAGGLSGATPGPPNLPGQTTIQVRVPYRVVGLVVGPKGATIKRIQQRTHTYIVTPGRDKEPVFAVTGMPENVDRAREEIEAHITLRTGAFTDSGPDSDFHANGTDVCLDLLGAAASLWAKAPHPGRRPPAATGGLRGDNALGAASTPEPFYVGSRGGPPLPDPSPSSPYGGSGNGGFTFGGDGPSAPTGTATPEDCDFGFDFLALDLTVPATATIWAPFERAAPLPAFSGCPAVNGAPAQPNTGTRRSSGGGAATTPRHSPTLPEPGGLSLELPLARRSVPDPVGAVPWRPPQSALPPFSGSTTFSTTPSLPSTTLASSTLDTVPSEGNHKPSTTAANSSASTAAPGPPSAALARECVVCSEGEAMAALVPCGHNLFCMDCAVRICGKSEPECPACRTPATQAIHIFS | Function: RNA binding protein, may be involved in post-transcriptional regulatory mechanisms.
Sequence Mass (Da): 65329
Sequence Length: 643
Domain: Binds RNA through its KH domains.
Subcellular Location: Cytoplasm
|
Q9XUB2 | MKAASNSVSSAGGSVSPTTTQPPLPPGQSSHPQIYDQQMQYYFAAAMPNQPMATYAAQNGSSQQYAPAAPYYQDANGQYVQVPANGSMAPQQHMMVSGQPYLYMAQPQQGAQQVMQSGQPQLIYYQQSMAPQAAPMYFHPMQAAPMLPEQMGVMPHTQPAIPPQQQPRQVGVEISSTRTAPLTSSTPLPTSLEYETVQRDNRNRNIQFRYHRVMEHDELPIDEISKITLDNHNDDTMSAEKENHFHEHRGEKFGRRGFPIPETDSQQPPNYKTRLCMMHASGIKPCDMGARCKFAHGLKELRATDAPARYPNNKYKTKLCKNFARGGTGFCPYGLRCEFVHPTDKEFQNIPPYQRMSHDDQDYDQDVIPEDYVVARHQPRFMRTGGRATTPTKVMLKHRNVAGSMMCLSNAGRDLQAGGDYNQPESNEDDLPPHLRRNRRENPPMNKRRTSLSTKWTSEENLGLRGHY | Function: Functions with mex-6 to affect embryonic viability, establish soma germline asymmetry in embryos and establish plk-1, pie-1, mex-1, and pos-1 asymmetry in embryos . Also affects formation of intestinal cells . Binds to mRNA in vitro, and inhibits pgl-3-mediated P-granule formation, probably by competing with pgl-3 for binding to mRNA . Required for neg-1 expression in anterior blastomeres during embryogenesis .
PTM: Phosphorylation on Ser-458 by par-1 promotes localization of the protein to the anterior cytoplasm of the zygote . Phosphorylation by mbk-1 appears to be required for subsequent phosphorylation by plk-1 .
Sequence Mass (Da): 52820
Sequence Length: 468
Subcellular Location: Cytoplasm
|
P84149 | MSYRGRGGGYNNNRGQFSSGPHQHQQNVDSFVAANQYPIEIMGWNGASSGECINFISRKCKVIVSNYSVDSNSGVLKGYVKNESQANTLLNWSGVKFAGQSLRFSKGVSNISNQMGGGASTGSQSTIETISQFLKARYQPEIKMLNLSNVKQDPTLTAQGFFGSLSVSSKFFPALMKVASDLKLDVDSIDLSNNELQDLQTLTSMAQTFPKLQNLSLQNNNFTKIKVFETWRHKLNFLRELILFNNPIVQTNDPAEIQTIKLELMKSFPRLVVLSGEILRNEQVLIANLSFPFESPETMFFQDEDSRNLATNFIANYLKLWDANRSELMILYQNESQFSMQVDSSHPHLIESGNSGYSGSTDFGYYLNNSRNLTRVSSIKARMAKLSIGQEQIYKSFQQLPKTRHDIIATPELFSMEVYKFPTLNGIMITLHGSFDEVAQPEVDGSASSAPSGPRGGSRYHSGPKHKRIPLSKKSFDRTFVVIPGPNGSMIVASDTLLIRPYTSDFPWKVQKLPSNPTAATPGVSATSTPSPLPPTTITTPQLAPPGTGPTTADLPADIKARLNQIQQELLVKILLETKLNINYGIMLCEQSNWDYQQASVNFKNSAASLPSDAFVQ | Function: Involved in the export of mRNA from the nucleus to the cytoplasm.
Sequence Mass (Da): 68257
Sequence Length: 617
Domain: The NTF2 domain heterodimerizes with MTR2. The formation of this heterodimer is essential for mRNA export and binds to all of the nucleoporin-FG-repeats.
Subcellular Location: Nucleus
|
Q9Y8G3 | MLRRKRERRNAVKENEMVIDTPLEKRRTPGKPRATREPPISVVITGHSKGSEDDLISFVWRKVKVRLMNISYSPASVTAVVKSQDFSRLNGLNGAAFAGDHLAIRRVDGASNVTQDYRKAKTKRSFRSVSAPSLSALATQAQRNVSKTLPQSTNETIEKLRQFLQTRYQPATKFLDLGNLQQDPLLKQMGILAEASTKSKMFPALMKVASLNFPDVISVSLSDNNLQSVTAVTTLAQTWPKLLNLSLANNRITSLSDLDPWSPKTKLPELQELVLVGNPIVTTFANRAMDYQREMVSRFPKLRLLDGNSINSEIIASQSTVPFPVYQSFFDKVETEQIVNSFLAAFFKGWDENRSALVNQLYSPNATFSISLNASNVRTNFSQKTDTKKWGAYKMKSRNLLYSQSQKESKSRLFNGHEEISNAVKSLPATAHDLSDRSQWVFDGWNLVLPSVGAAIKIVVHGQFEEPQNKRLLRSFDRTLLILPGGSTGILIINDLLVIRSFAGSLGWLPGQSSVRTSNNAMSASASKPSDIVQPRPEQAMLDTRQQIVLKIKAETGLNDYYAHMCCEQNNWDYNSALASFLELKSRNVIPAEAFS | Function: Involved in the export of mRNA from the nucleus to the cytoplasm.
Sequence Mass (Da): 66535
Sequence Length: 596
Domain: The leucine-rich repeats and the NTF2-domain are essential for the export of mRNA from the nucleus.
Subcellular Location: Nucleus
|
Q99257 | MSGFHNVGNINMMAQQQMQQNRIKISVRNWQNATMNDLINFISRNARVAVYDAHVEGPLVIGYVNSKAEAESLMKWNGVRFAGSNLKFELLDNNGASAGTSDTISFLRGVLLKRYDPQTKLLNLGALHSDPELIQKGVFSSISTQSKMFPAMMKLASTEKSLIVESVNLADNQLKDISAISTLAQTFPNLKNLCLANNQIFRFRSLEVWKNKFKDLRELLMTNNPITTDKLYRTEMLRLFPKLVVLDNVIVRDEQKLQTVYSLPMKIQQFFFENDALGQSSTDFATNFLNLWDNNREQLLNLYSPQSQFSVSVDSTIPPSTVTDSDQTPAFGYYMSSSRNISKVSSEKSIQQRLSIGQESINSIFKTLPKTKHHLQEQPNEYSMETISYPQINGFVITLHGFFEETGKPELESNKKTGKNNYQKNRRYNHGYNSTSNNKLSKKSFDRTWVIVPMNNSVIIASDLLTVRAYSTGAWKTASIAIAQPPQQQASVLPQVASMNPNITTPPQPQPSVVPGGMSIPGAPQGAMVMAPTLQLPPDVQSRLNPVQLELLNKLHLETKLNAEYTFMLAEQSNWNYEVAIKGFQSSMNGIPREAFVQF | Function: Involved in the export of mRNA from the nucleus to the cytoplasm.
Sequence Mass (Da): 67352
Sequence Length: 599
Domain: The leucine-rich repeats and the NTF2-domain are essential for the export of mRNA from the nucleus.
Subcellular Location: Nucleus
|
P52477 | MQRTPAMRVLVPALLVAISALSGCGKSEAPPPAQTPEVGIVTLEAQTVTLNTELPGRTNAFRIAEVRPQVNGIILKRLFKEGSDVKAGQQLYQIDPATYEADYQSAQANLASTQEQAQRYKLLVADQAVSKQQYADANAAYLQSKAAVEQARINLRYTKVLSPISGRIGRSAVTEGALVTNGQANAMATVQQLDPIYVDVTQPSTALLRLRRELASGQLERAGDNAAKVSLKLEDGSQYPLEGRLEFSEVSVDEGTGSVTIRAVFPNPNNELLPGMFVHAQLQEGVKQKAILAPQQGVTRDLKGQATALVVNAQNKVELRVIKADRVIGDKWLVTEGLNAGDKIITEGLQFVQPGVEVKTVPAKNVASAQKADAAPAKTDSKG | Function: The periplasmic linker component of the MexAB-OprM efflux system that confers multidrug resistance . Functions as the major efflux pump for n-hexane and p-xylene efflux . Has been shown in one study to be involved in the active efflux of the autoinducer N-(3-oxododecanoyl) homoserine lactone, thereby playing an indirect role in quorum-sensing; but has been shown in another study not to be involved in efflux of this autoinducer . Over-expression of the pump increases antibiotic and solvent efflux capacities . Implicated in the secretion of the siderophore pyoverdine .
Location Topology: Lipid-anchor
Sequence Mass (Da): 40970
Sequence Length: 383
Subcellular Location: Cell inner membrane
|
B8MYS7 | MKKIYNVYFLCGFATLGGGLFGFDISSMSGVLGTAAYTNYFQVGSGQYKQGSITCAMPFGSLVGALCSSFIADRYSRVRAIQFSSILWIIGSIFMCASNGIPLLVVGRVIAGGCVGIASAMVPVYQAEIAPKEIRGRVISLQQWAITWGILIQYFIQYGASNIDGGPNNPTQSTAAFRIPWGIQIVPGVILFFGMFLFPKSPRWLASKDRWEEALQVLSKLHGQGDVNHPKVLAEYKEIQEALALEREQSATGFQELIKPRIFKRVILGMSLQMWSQLCGMNVMMYYIVYIMQSTGAGSPLLTASIQYILNTALTLPAIIYLDKFGRRPAILIGFFLQAIFLYLEGGLQGGFGAPNPHTDPKLDAISWTVADHPAVGKAIIALSYLFVCSFATTIGPTSWTYPAEIYPAKVRAKAVSLATASNWIWNCLLALFVPPLLWSINWKMYMIFAAFNTAAFIHMFLTAPETKGYTLEEMDDVFDSGLPAWRKLERKSRMEELEKEIIEGNLKITPAHEATGVSATHVTPEKQV | Function: Probable MFS glucose transporter; part of the gene cluster 27 that mediates the biosynthesis of asparasone A, a sclerotium-specific anthraquinone pigment important for sclerotial survival .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58332
Sequence Length: 529
Subcellular Location: Membrane
|
Q6NUT3 | MGPGPPAAGAAPSPRPLSLVARLSYAVGHFLNDLCASMWFTYLLLYLHSVRAYSSRGAGLLLLLGQVADGLCTPLVGYEADRAASCCARYGPRKAWHLVGTVCVLLSFPFIFSPCLGCGAATPEWAALLYYGPFIVIFQFGWASTQISHLSLIPELVTNDHEKVELTALRYAFTVVANITVYGAAWLLLHLQGSSRVEPTQDISISDQLGGQDVPVFRNLSLLVVGVGAVFSLLFHLGTRERRRPHAEEPGEHTPLLAPATAQPLLLWKHWLREPAFYQVGILYMTTRLIVNLSQTYMAMYLTYSLHLPKKFIATIPLVMYLSGFLSSFLMKPINKCIGRNMTYFSGLLVILAFAAWVALAEGLGVAVYAAAVLLGAGCATILVTSLAMTADLIGPHTNSGAFVYGSMSFLDKVANGLAVMAIQSLHPCPSELCCRACVSFYHWAMVAVTGGVGVAAALCLCSLLLWPTRLRRWDRDARP | Function: Transporter that mediates the import of cysteine into melanosomes, thereby regulating skin pigmentation . In melanosomes, cysteine import is required both for normal levels of cystine, the oxidized dimer of cysteine, and provide cysteine for the production of the cysteinyldopas used in pheomelanin synthesis, thereby regulating skin pigmentation . Also catalyzes import of cysteine into lysosomes in non-pigmented cells .
Catalytic Activity: L-cysteine(in) = L-cysteine(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52075
Sequence Length: 480
Subcellular Location: Melanosome membrane
|
Q3U481 | MSPPSDDAGPGPPRTLSLAARLSFAVGHFLNDLCAGMWFTYLLLFLHSVRGYSSRGAGLLLLLGQVADGLCTPLVGYEADRASCVRCGPRKAWHLAGTVCVLLSFPFIFSPCLGCGEATPEWAALLYYGPFIVVFQFGWAATQIAHLSLIPELVTSDHEKVELTALRYAFTVVANITVYGAAWLLLHLQGSAHGEQDISVGDQLGVQDVPVFRNLALLVVGVGAIFSLLFHLGTKEGHRSQHWGNEPNEHTPLVAPAAQPLLLWKHWLREPAFYQVGMLYMTTRLIVNLSQTYIAMYLTYSLSLPKKFIATIPLVMYLSGFFSSFLMKPVNRRIGRNMTYFTGLLVILAFAAWVALADNLGVAVYGAAVLLGAGCATILVTSLAMTADLIGPHTHSGAFVYGAMSFSDKVANGLAVMAVQSLHPCPSELCCGACISFYHWVMTAVTGGVGVAAALALCSLLIWPIRIRNRDPRDRP | Function: Transporter that mediates the import of cysteine into melanosomes, thereby regulating skin/hair pigmentation . In melanosomes, cysteine import is required both for normal levels of cystine, the oxidized dimer of cysteine, and provide cysteine for the production of the cysteinyldopas used in pheomelanin synthesis, thereby regulating skin/hair pigmentation . Also catalyzes import of cysteine into lysosomes in non-pigmented cells (By similarity).
Catalytic Activity: L-cysteine(in) = L-cysteine(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51504
Sequence Length: 476
Subcellular Location: Melanosome membrane
|
A0A4Q4NJ90 | MAHSTAGDRDPEVGSEQHSSIAQLHTESMSDPWGDSNSPENPLNWPAPKKNFHVAIVSIFTLTANLAATMFAPGAPQLAKEFNITNSTVEAMTVSLYVLGFAFGPLLLAPLSELYGRLIIYNACNAVYIAFTVGCAFSTNVSMFLVFRFLCGCAASGPMSIGGGTVADITPQEERGKAMALFAMGPLLGPVLGPIIGGYVSQYTNWRWTFRIILIMSGIIGLATMFFMRETNAAVLLRRKAKRSPKDAEGMELELDKTKKETPSQVLVRAITRPFKMLLFSPIVLLISLYTGVLFGLIFLLFTTFPTVFQGVYGFDEGTSGLAYLGLGIGMFLGLVVFSILSDKLLGQKQGGTVSKPEQRLILMKWFGPITPLGCFMYGWSAYHHVHWIVPILGTSIIGFGSLFVVIPGQIYLVDSFGAEAAASALAANLLVRSPFGAFLGLVAAPLYDRLSLGWGNSVLGFITLAFTPVPWLFYRYGETLRTRFVVKL | Function: MFS-type efflux pump involved in the modulation susceptibility to various compounds including cumyl hydroperoxide, potassium superoxide, many singlet oxygen-generating compounds (eosin Y, rose Bengal, hematoporphyrin, methylene blue, and cercosporin), and the cell wall biosynthesis inhibitor Congo red . Involved in oxidative stress tolerance, colonization, and lesion formation .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53131
Sequence Length: 489
Subcellular Location: Cell membrane
|
G4MWA9 | MSNEGTNTVLKNPGSNQEEADPDSPSSLGDKSKLDELADSTSDGSQANSGRGIAFWAIFISLSVTGFLSSMEGGIMSTALPAVSRAVNAESDYVWIINVYFLTSAAFQPLYGQLADIWGRRWPMLSAVTIFAAGSAICGAANNSGTLIGGRAIQGLGAAGINTLVELILCDLLPLRERGQFMGLLFLFIVVGSVLGPMLGGIIVDKTSWRWIFFINLPICALCFGLLFFALNLKHRRDDNSTSLQKLKKIDFVGVLILCVAVTLLIYALTYGGGAKYAWSHPVIITTLVLGIFGHGLFIAFEASPWCSNPTTPLTLFQNRTSVAAYTLEAVQILVSWGALYFLPLYFQSVLALTPSRSGVLILAFSISYCLSAAIGGGLVTKLGKYRLVHIISFAIMTIMMGVFTILNRNSSLAVNVILGLIAGVGVGLPNASILTAVQASLPDSLNAASTALFAFIRSLATVFAVTIPAAIFNSRFDDLLSTSALDNDVKNSLDLGKAYQQASPDFLHSFPAPVQDQIVGLYELSLKLVWQVLIGIAAVGVIASLLEKDLECRTEQTTEEFGLKDRDEKAPKKSEV | Function: MFS-type efflux transporter; part of the gene cluster that mediates the biosynthesis of a tyrosine-derived cytochalasan acting as a fungal signal recognized by resistant rice plants and leads to avirulence in Pi33 resistant rice cultivars . MFS1 might be involved in the excretion of the signaling tyrosine-derived cytochalasan (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61724
Sequence Length: 577
Subcellular Location: Cell membrane
|
B2KWH5 | MVTLSNVGADVEKNIVPEVNDASKRDSDNASADFQPGVKRVRAVASVWSKKTLWLTFALLYLVAFVDMLLVSVQSTLNPFITSSFEKHGLLASVSIVATILSGCSTLTLAKIVDVWGRIEGFLFMLLVVVVALIMKATCKNMEAYVAAHTLYWTGHIGMIYCVDVMLADMTTLRNRMIMFSINNTPTIASTFAGPKIADLFFSNLNFRWAFGAFAIMLVGVSLPVIVIMLFMERKSVKAGFLVKEKSGRSAWESIKYHLIEFDVVGIVLITASFALILLPFSIVVYAPKGWATGYIIAMEVVGVVCGAIFLAWERFLAPVQFLPFKYLKNPTIIGSCLLYGVMFASALLTITTAGYVLNSFSLSSAILAPGIGLYTGNFKWAAYAGIPFMLLGTALLIPFRQPNTSIGAVTITQVLVGIGTSFFSVCGQLAVMSVVSHQEVAVVLAIWGMFGSIGASVGLAVAGAMWNNILPSQLYRRLPEESKAMAAQIFGDMQLQMSYLDGTPERDAIVGAYADVQRKMVIAGVCMMPLVMASIVIWRNVNIKKQEEEEGSQTTGNIF | Function: Major facilitator transporter involved in siderophore transport .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60879
Sequence Length: 560
Subcellular Location: Membrane
|
D4AXV8 | MTEKDTDGADGLTKAKSNAVSEDYETVNHVTGLKLAVIVTGLCLSVLLVALDNTIIATAIPKITDQFHALEDIGWYGSSYLLTICAFQLIFGKIYTFFPVKWVFLIAITIFEIGSAICGAAPNSTALIIGRAVAGIGSAGIFSGALIIIAYSIPLEKRPAYTGAIGGMYGIASVAGPLMGGAFTDHISWRWCFYINLPIGAVTILSILIFLKHPKQKLDNNQTWKARLLKLDPIGTAFFMPSIICLLLALQWGGTKYPWNNGRIIALFVVFAVLISGFIYFQIRGGDSATVPPRILKKRSIASGAFFLFTIGSAFFIMVYYLPIWFQAIKGASATSSGIMNIPMVLSLVVLSIASGITVTAIGYYAPLYYVSTVLTSIGAGLLTTFTTETSKGKWIGYQIIFGAGVGTGLQLSIIAAQAVLPLEDVAVGTVIMMFCQTLGGALFVSVGQNVFTNLLVKGVVNAAPGLDPQVVLRVGATQLKNMIPPQFLDGVQVAYNDALTKTWYVATALAALSVIGSVGMEWKSVKGKKIEPAAA | Function: MFS-type efflux pump involved in the modulation susceptibility to azoles, including fluconazole, itraconazole, miconazole and voriconazole (Ref.2). Confers also increased resistance chloramphenicol and thiamphenicol, suggesting that it acts as a pleiotropic drug transporter with a broad substrate spectrum (Ref.2). Finally, increases the tolerance to cycloheximide when expressed in S.cerevisiae, but not in dermatophyte species (Ref.2).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57066
Sequence Length: 536
Subcellular Location: Cell membrane
|
M2R8W9 | MDKTASLTSQDAEKHDPDALRKERATDPPDLFEHGALDPVYQAKAHLIASAIQEIGMGKYQWGLFVVAGFGWFSDSVWPLMGSLILSPVVNEFQFNSPFLSLALNAGLLAGAIFWAFGCDIWGRRWSFNLSLLIAGAFGLAAGGTQNFVALACLFAVVGFGVGGNMPVDSAVFLDFVPGSYQYLLTILSIWWSIGQLVASLIAWPLIANFSCPIGSTTCTRADNMGWRYLLFTLGGMTLLLWAIRFFVFPLMESPRFLVGRGRDAEAIAVIQRIAQFNGRPSSLTLEELAMVAEKAAPKDAVATQRRQVLSQSSDFSTDHVKGLFATPKLAWSTSLLIALWGIIGLASTLYNSFLPFLLANRGAEFGDSSYFITYRNQVIIAVLGVPGAFLAGWAVEQPYLGRKGTLAISAGLTGVFLFATTTARSSNALLGWNCGYAFHSNIMYGVLYAISPEVFPAKDRGTGNGLTATATRVFGLIAPVIALYANLSTAVPVYVSGALIIASGAMALLLPYEPRGRASL | Function: Major facilitator transporter probably involved in siderophore basidioferrin transmembrane transport .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56014
Sequence Length: 521
Subcellular Location: Membrane
|
G4N2A8 | MTALAAVPDLQDAAGPSTTTVHSPNYSGSPADISSSPTTRAVSRNTARQTASAPPNHAESSPPGNASPTGPPSPSGNNVSPHGRHQGMSKLRACLVIATLSGVSFLNTMGSGILTVSLPTMARDVRLDDSLLLWPASVYSLAAGCTLLVFGAVGHIIGPKRVWITGACLYAAFTLGVGRSATGSQLIAFRSVLGVSIAMCLPTAVSLTTNGFGAGRWRNMAFAFQGMGQPLGYSTGLILGGIFTDTVGWRFGFYISGGINAVLAICALVVLPSPPRHDEGDGEQREVEEEATDATVAAAAVNRSSRSRPLISRLAHDVDWTGTLAISASMGFLSYVFSVVSKDYDRMAAPQNIALLVAAALLLPTFTLWVGRQERLDRPALIPNSLWRKAAFSSTCAAVFFTWAVFNAFQYFSALYFERIEHITALQTSLRFLPMVLVGAATNIVTGYLVETVEVRWLVVVSAIFSLFSPLIMALVRPGWGYWKGAFFAMLLSPLHPDVLFTVSNLIISRVYDGRSQSLAGAVFNAVSQVGNSVGLGLTAVVSSAVARSYHGSGGVGNAMDPPTGRPQHLPSSPTVEATLAGYHAAFWLMFGAAALVTVITFLGLRRGGKVGAVE | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of pyriculol and pyriculariol, two heptaketides that induce lesion formation upon application on rice leaves but are dispensable for pathogenicity . With the ABC transporter ABC7, is most likely responsible for pyriculol and pyriculariol secretion and thereby may contribute to intrinsic resistance (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64730
Sequence Length: 615
Subcellular Location: Membrane
|
A0A0C4VYV1 | MTHSSSNEHEKEDDRRASDDMMDRDDQNAKEEQDVSKDAPPVNPWDPSQFPDGGFKAWSVVAGGFCSLFCSFGWINCIGIFQQYYQSDYLRGYSSSTISWIASLELFILFAGGLVVGRVYDRYGPRYILLFGTFMHVFGLMMASLSTEYYQILLSQGICSPIGISCLFTPAVNCIATWFRKKRGLANGIVAAGSSLGGVIFPIMFDRLIPRVGFPWAMRIGAFLILFLLIIANLTVVSRIPPMPKPITAKQYLAPFQERTYLLTTIAAMIFVLGLFLPINYIQAQAVEFGMDPSLANYLIPILNAASLFGRTVPGFVADKIGPYNVHTFMCFFSSVVAFALWLPAASNAPIIVFAALYGFGSGAFVAILPTLIAQISDIKEIGLRIGMEFGVLSLPALVSNPIGGAFVAHDNGGYRSCQIWTGCITMLGAILFVVARISLGGPSLMKKV | Function: MFS-type transporter that mediates the secretion of the 4 major naphthoquinone derivatives produced, erythrostominone (NQ1), deoxyerythrostominone (NQ2), epierythrostominol (NQ4), and deoxyerythrostominol (NQ5), as well as of 3 newly identified naphthoquinone derivatives termed NQ7, NQ8 and NQ9.
Catalytic Activity: erythrostominone(in) = erythrostominone(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49084
Sequence Length: 449
Subcellular Location: Cell membrane
|
Q3T9M1 | MSVPHGPTPAPVAEPHTQEPGSDKRDGRLSVCTKVCYGIGGVPNQVASSASAFYLQLFLLDVAQIPAAQVSLALFGGKVSGAVADPVAGFFINKSRRTGSGRLMPWALGCMPLIALAYFFLWFLPPFTSLRGLWYTSFYCLFQALATFFQVPYTALTMILTPSPRERDSATAYRMTMEMAGTLMGATVHGLIVSSAHGSQRCEDTVHPRSPAVSPDVARLYCIAAAVVALTYPVCGSLLCLGVKEQPDTSAPASGQGLNFFTGLAITSQHPPYLSLVVSFLFISAAVQVEQSYLVLFCTHASKLQDHVQNLVLIILVSAVLSTPLWEWVLQRFGKKTSAFGICVMVPFSILLAAVPSAPVAYVVAFVSGVSIAVSLLLPWSMLPDVVDDFQLQHRCGPGVETIFYSSYVFFTKLSGAGALGISTLSLEFAGCEAGACQQAEEVVVTLKVLIGAVPTCMILIGLCILLVGPTPKMPRQDTSSQLSLRRRTSYSLA | Function: Lipid transporter that specifically mediates export of sphingosine-1-phosphate in red blood cells and platelets . Sphingosine-1-phosphate is a signaling sphingolipid and its export from red blood cells into in the plasma is required for red blood cell morphology . Sphingosine-1-phosphate export from platelets is required for platelet aggregation and thrombus formation . Mediates the export of different sphingosine-1-phosphate (S1P) species, including S1P(d18:0) (sphinganine 1-phosphate), S1P (d18:1) (sphing-4-enine 1-phosphate) and S1P (d18:2) (sphinga-4E,14Z-dienine-1-phosphate) . Release of sphingosine-1-phosphate is facilitated by a proton gradient . In contrast, cations, such as sodium, are not required to drive sphingosine-1-phosphate transport . In addition to export, also able to mediate S1P import . Does not transport lysophosphatidylcholine (LPC) .
Catalytic Activity: sphing-4-enine 1-phosphate(in) = sphing-4-enine 1-phosphate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52797
Sequence Length: 494
Subcellular Location: Cell membrane
|
A4IH46 | MAETSRELPLSTLTASTRRALRIRARQAREAKLSVLSKVCYAIGGAPNQVSGSASAFFLQIYLLDVALISPYQASLVLSLGKTWGGITDPIVGYCISKSKWTRIGRLMPWMLGCTPFLVVSYFLLWFVPTFETGRVLWYLAFFSCFQALSTAYHVPYTTLTMFLSTDQMERDSATAYRMTVEVLGTLIGAAVQGQIVASAHTGSHCNVTNMTGNLTADFLYEPTEYITSARQVYMIAAGIIGCLYLLCISVLFLGVKERDDPYALVAGKVIPFFKGFRETMQFGPYLNLISSFLLISAAVQIQQSNFVLFCTHAADLQDHFQNLVLTILIAAVLSIPFWQWFLQKFGKKMAAFGISLMIPFSIMLVTISSLVVAYVVAVASGLSIAASLLLPWSMLPDVVDNFRLTNPQGKGLEAIFYSSFVFFTKLSAGIALGISTLSLQFADYNTSLCKQSYSVVLTLKLLIGAAPALMIIIGLTILAFYPITEDTRKETELALDVIRMRTRRSTLIVI | Function: Lipid transporter that specifically mediates export of sphingosine-1-phosphate in red blood cells and platelets. Sphingosine-1-phosphate is a signaling sphingolipid and its export from red blood cells into in the plasma is required for red blood cell morphology. Sphingosine-1-phosphate export from platelets is required for platelet aggregation and thrombus formation. In addition to export, also able to mediate S1P import.
Catalytic Activity: sphing-4-enine 1-phosphate(in) = sphing-4-enine 1-phosphate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56318
Sequence Length: 511
Subcellular Location: Cell membrane
|
B2KWH6 | MRSAFLSKLQTHAPVAQPQVISSGLAKEAGDLPQEQEVDAEDQLSADAQDGVRKIQATTQVWSKGHLIFAYVMIWVITFVDTMQQGMSNSLLPYVTSSFRLHSLTASTMIMSNIIGGLIKLPLAKVLDIWGRPQGFLIMVGALTIGLVMMAACNNVKTYAAAQVFYWVGYNGMSYTISIFIADTSALKNRALMFAFVSSPYIATVWVGGPLATVFLNGPGFRWGYGAFAIITPAITCPLYAVFAWNYKKAKDAGLLPEKTHSRTFTQSLKHYFFEFDIIGIILLASGLALFLLPFSLYSYQKDQWRSSLVISMIIVGGLLLIAFALYEKYRAPVCFIPFELLFDRTVLGACILAASLFVSFYIWDSYFSSFLQIVNDLSITQASYIVNIYSIGACFWSIIVGILVRWSGRFKWLALYFGVPLTILGVGLMITFRQPDVNIGYIIMCQIFIAFAGGTCVITEQMAVMAATSHQYVAVVLAVESMFANIGGAIGQTVAAAIWTGVFPQRLAEYLPDEAKANATLIYGDLTVQKSYPVGSLERIAINRAYGDGQKYMLIGGTAILAVGLGATMMWRDIKVKDFKQVKGLVV | Function: Major facilitator transporter involved in siderophore transport .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64631
Sequence Length: 588
Subcellular Location: Membrane
|
A9BJC1 | MKRFLGILVFVVMVLSVFAGPNHLVIFHMNDTHGHVWGTEDGGGFARAATLINQAREEVAKEGGAVLFLHAGDVNTGIPESDQLDAVPDFLALHYMGLDAMSLGNHEFDKPFEVLEKQYEVAQFPFLGANFVNEKRGGPVFEPYIIKDYGDFSVGIIGLVTEQTKVLEPIYLGENTIVDAEETLNMYLPIVQEKADVVIVLAHLGYHADGGRPNLSVEFTTSDELAENVSGVDIIIDGHSHTLLETPVVINNVIVAQAGDNAENIGRIDLWIDDGRIVDWRGEVIPLTSDIPEDPFIKMFTDAFYQLGSEALNEVVGVTKVYLDGERAHVRSDETNLSNLIADGMIWKTGADVALMNGGGIRASIEAGEITYRDILTVLPFGNTLYVLELTGKDIMDVLNYAATIPDGQGAKLHVAGLTAEIKGGKATNVKINGKPIDLNKTYKVVTNNYVAAGGDGYTMLAGKPGYDTYFRDADSLREYIAHLGTIEDYTSQERLIELDQVK | Function: Involved in the biosynthesis of the compatible solute mannosylglucosylglycerate through a phosphorylating pathway. Catalyzes the dephosphorylation of mannosylglucosyl-3-phosphoglycerate (MGPG) to mannosylglucosylglycerate (MGG). Can also dephosphorylate UDP-glucose, ADP-glucose, GDP-mannose, glucosyl-3-phosphoglycerate (GPG), mannosyl-3-phosphoglycerate (MPG), ADP, GDP and UDP.
Catalytic Activity: (2R)-2-O-[alpha-D-mannopyranosyl-(1->2)-alpha-D-glucopyranosyl]-3-phospho-glycerate + H2O = (2R)-2-O-[alpha-D-mannopyranosyl-(1->2)-alpha-D-glucopyranosyl]-glycerate + phosphate
Sequence Mass (Da): 54892
Sequence Length: 503
EC: 3.1.3.-
|
A9BFS6 | MEIGLVHYRVGETDGVSLEMVKWKQALRNMHLKTYLIAGDMGTSPGFKIPYIAYTDKRSNILKQKSFVNLDEWDENYFKKEMNKYIEDIYNQLYEMMDLDVMIVNNIFSLAHNPAAAVAIYRFCKDNGIKMIGHHHDFYWERDFYKNPTNDYIKEILEEYFPPKDITHVVINSLAQEELKNKKGLDSIVIPNVFDFNQKRWEIDDYNIKIYDKLNISQKDLIFLQATRIVRRKAIELAIDTVAEVKKDLKKYIGKTTFNGKKITQDTNVFLVLPGLSEESDYVEVLKEYASQKDVELKLAFSISDDIRHEEEEIFSLWDFYAIADFITYPSILEGFGNQFLEAIFAKTPVLMFEYPVYKKDIAPLGFEVVSLGSKAEYERGMYRVNQNEIIKAKEEIFQILFDPQGLHRLSRRILNLGKNIFPMKLWRKS | Function: Involved in the biosynthesis of the compatible solute mannosylglucosylglycerate through a nonphosphorylating pathway. Catalyzes the synthesis of mannosylglucosylglycerate (MGG) from glucosylglycerate (GG) and GDP-mannose.
Catalytic Activity: (2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + GDP-alpha-D-mannose = (2R)-2-O-[alpha-D-mannopyranosyl-(1->2)-alpha-D-glucopyranosyl]-glycerate + GDP + H(+)
Sequence Mass (Da): 50510
Sequence Length: 430
EC: 2.4.1.-
|
Q9X0V7 | MKIALIHYRGGLMDGVSLEMEKWKKVLTKMGHEVHIVAENKKEGVDLTLKEIGFENPDFERVNRNFFGGIKDFLSEKEFLDFLKEKEEELFHILNEALKDYDLIVPNNIWSLGLFPSLGLALSRLEKNFVAHHHDFWWERKHLIPENRRFREILDKHFPPDLPNVKHVVINTIAQRELKRRRNIDSVVVPNVMDFSSPITSEEMYHRVREELQIAPGTIVALQATRIDRRKTIELSIDVVSLLKETLTSKKEADLYNGERYSGEVILLFSGICEDEEYLKELKEYASSKGVSLLVLSEEVRKNTSLFWKLYNAADFVTYPSILEGWGNQLLEAIAAKKPVVLFEYEVFKSDIKPAGLKYVSLGDRCFRENGLVKVDERILKKAVEEISRLLFDPSLYRETVEHNFEVGKRHFSLERLEDILSREVLP | Function: Catalyzes the synthesis of mannosylglucosylglycerate (MGG) from glucosylglycerate (GG) and GDP-mannose.
Catalytic Activity: (2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + GDP-alpha-D-mannose = (2R)-2-O-[alpha-D-mannopyranosyl-(1->2)-alpha-D-glucopyranosyl]-glycerate + GDP + H(+)
Sequence Mass (Da): 49702
Sequence Length: 427
EC: 2.4.1.-
|
D8QTR2 | MAGPVRCLPPVVEATSIPHAPPVISKEVSEIVNNMLSVAIPAAAAASAQDQRFASQFRCGPEFTTMKAQALEACRKILAENDQGGYTIPAKGLYPYQWNWDSALVSLGLAEMEEERAWEELDRLMSAQWEDGMVPHIVFHKPSSTYFPGPEIWGSPDKPRNTTGITQPPVAAISVRRLLEEAKDKALALAMARKLFPKLLAWHRWFYRARDPEGTGLVATIHPWETGMDNSPAWDEALARVPIDDIPPYVRRDLGHVDAKMRPQKAEYDRYLTLLYRFRALDYDEAKLYYETPFRVTDLCTNCILHKANEDLLWLAGATGACTDESEIRGWTARANVAFDTLFDVEAGLYRCKDQLTGQFLPAATSAGFLPLFAGVASGEKASAVARTLGRWLDDVAYGIPSCDPRDPQFEALRYWRGPVWLIVNWMVSEGLKRYGYGELAQRVERDSYELVKNGGIFEYYCPLTGMGAGGGCFSWTAAMCLAWLFKT | Function: Catalyzes the hydrolysis of alpha-D-mannosyl-glycerate (MG) to D-glycerate and D-mannose . Can also hydrolyze alpha-D-glucopyranosyl-glycerate (GG)with lower efficiency .
Catalytic Activity: (2R)-2-O-(alpha-D-mannosyl)-glycerate + H2O = (R)-glycerate + D-mannose
Sequence Mass (Da): 54528
Sequence Length: 488
EC: 3.2.1.170
|
Q03649 | MRLKELLPNFLIVHQEVPEDPIAFKSTDKRENENKEITIPELIDTKVPELADGATDTLYGLLVNGHLQTAYGSFRHFDNIYKVQYKRMIIKYPHGGEGTVDFAVNGRSTKRRKVEKEYVPTSQPVFNGNLKRRYSYYSPDDPKLNSDDAKPMLIILHGLTGGSRESYVRAIVHEITTKYDFEACVFNARGCCYSAITTPLLYNGGWTNDIRYCVNDLRKRFPNRKFYMMGFSLGASIMTNYLGEESDRTKIECAISVSNPFDLYNSAYFINSTPMGSRFYSPALGHNLLRMVRNHLSTLEENPDFKDVIEKHLKKIRTVRQFDNLLTGPMFGYKNAEEYYKNASSYKRIPGIRTPFIALHAQDDPIVGGDLPIDQIKSNPYTLLLETSTGGHVGWFKDRSGRRWYAEPLCRFLKIFHDEITVKGLKPDLENVQLPDPNCEPIATTFRAN | Function: Converts monoacylglycerides (MAG) to free fatty acids and glycerol. Has a preference for palmitoyl-MAG . Does not play a significant role in ethyl ester biosynthesis . Also possesses ester hydrolase and low but persistent TAG lipase activity .
Catalytic Activity: Hydrolyzes glycerol monoesters of long-chain fatty acids.
Sequence Mass (Da): 51438
Sequence Length: 449
EC: 3.1.1.23
|
Q6LK34 | MNQVLLEMRGITKTFPGVKALDNVQLTLKKGRVMALMGENGAGKSTLMKVLFGIYQRDCGTIRYQGEQVNYSGAKEALEAGVSMIHQELSPILHRSIAENIWLGREPLKGPLRLIDHAKMYRDTTELLKKLDLHLDPRTPMSELTVATMQMIEISKAISYNSKIIIMDEPTSALTGKEVDHLFEIIEKLKKQGVSIVYISHKMDEIFRICDDITVFRDGCYIGEREAQNTNHDELVQMMVGRDLGDVFPPPTAKPGKVRLEVKNLSVEGVFDNISFKLHEGEILGIAGLVGAGRTELIETLFGVRKHDVGEIWINGENVEIKTPQDAISHKMAFLTEDRRQSGLYLMLDIFANTSIAHLDAYRNKVVNVLDVRSMQKDCASQCTKLKVKTPGMAEKIDNLSGGNQQKVLLARWMLTKPDILFLDEPTRGIDIGAKSEIYKLMRLLTGMGKSLVMISSELPEVIGMSDRILVMHGGKLKGELDGKDASQQQVMSMAFN | Function: Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-galactose(out) + H2O = ADP + D-galactose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55487
Sequence Length: 497
Subcellular Location: Cell inner membrane
EC: 7.5.2.11
|
Q896Y2 | MVENNIILEMNGISKNFPGVKALDGVDLKVKKGTVHALMGENGAGKSTLMKCLFGIYRSDDGEIVLGGKKVQFKNAKDALENGISMIHQELHPVPHRSVMENVWLGRFPVKKVFGLGIVDHKKMYEDTKDLLGKLKMNIDPNTLVSKLSVSQVQGLEIAKAVSYNSKIIVMDEPTSSLTENEVTHLFNIISDLKNQGVAIIYISHKMEEILKIADEVTIMRDGKYIGTWEAEGLTTDLIISKMVGRDLTNRFPPKENTPGEVIMKVENLTSANNKSFKDISFELRKGEILGIGGLVGAQRTELVESIFGLRKIETGKIYINGQEVKIKSPINSKKYGIALLTEERRSTGIFPVLTVGDNTIIAGLDKYIDLKFVVNQKRGMKDIKNSIEKLNIRTPSHATQIKNLSGGNQQKVIFSRWLLTEPDVLIMDEPTRGIDVGAKYEIYSIISDLSKMGKSIIMISSEMPELIGMSDRIMIMCDGRLSGIIEGEEATQEEIMKYATRFI | Function: Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-galactose(out) + H2O = ADP + D-galactose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56052
Sequence Length: 504
Subcellular Location: Cell membrane
EC: 7.5.2.11
|
P0AAG8 | MVSSTTPSSGEYLLEMSGINKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGTILFQGKEIDFHSAKEALENGISMVHQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRETKAIFDELDIDIDPRARVGTLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEVTVLRDGQWIATEPLAGLTMDKIIAMMVGRSLNQRFPDKENKPGEVILEVRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKQINNHNANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKGKGIIIISSEMPELLGITDRILVMSNGLVSGIVDTKTTTQNEILRLASLHL | Function: Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import. Responsible for energy coupling to the transport system (Probable).
Catalytic Activity: ATP + D-galactose(out) + H2O = ADP + D-galactose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56415
Sequence Length: 506
Subcellular Location: Cell inner membrane
EC: 7.5.2.11
|
Q8REE1 | MENLKYVLEMENISKEFPGVKALDDVQLKLKPGTVHALMGENGAGKSTLMKCLFGIYEKNSGKILLDGVEVNFKSTKEALENGVSMVHQELNQVLQRNVLDNIWLGRYPMKGFFVDEKKMYNDTINIFKDLDIKVDPRKKVADLPIAERQMIEIAKAVSYKSKVIVMDEPTSSLTEKEVDHLFRIIKKLKESGVGIIYISHKMEEIKMISDEITILRDGKWISTNDVSKISTEQIISMMVGRDLTERFPKKDNKAKEMILEVKNLTALNQPSIQDVSFELYKGEILGIAGLVGSKRTEIVETIFGMRPKKHGEIILNGKTVKNKSPEDAIKNGFALVTEERRSTGIFSMLDVAFNSVISNLDRYKNKFRLLKNKDIEKDTKWIVDSMRVKTPSYSTKIGSLSGGNQQKVIIGRWLLTEPEVLMLDEPTRGIDVLAKYEIYQLMIDLAKKDKGIIMISSEMPELLGVTDRILVMSNGRVAGIVKTSETNQEEIMELSAKYL | Function: Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + D-galactose(out) + H2O = ADP + D-galactose(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56581
Sequence Length: 500
Subcellular Location: Cell inner membrane
EC: 7.5.2.11
|
Q8UIV6 | MEGQRCIALIAHDEKKDDMADFARHHQKVLASFRIVATGTTGGRVQEACPGLEVIRLKSGPLGGDQQIGAMIATGEVDMLIFFTDPLTAMPHDVDVKALTRLATVYDIPMALNRATAENLIDFNSAD | Function: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Catalytic Activity: dihydroxyacetone phosphate = methylglyoxal + phosphate
Sequence Mass (Da): 13753
Sequence Length: 127
EC: 4.2.3.3
|
Q5WGQ3 | MKIALIAHDKKKQELVDFCVAYEPILKEHELYATGTTGTRIMEATELVVTRFKSGPLGGDQQIGALVAENQFDLILFMRDPLTAQPHEPDVTALIRLCDVQSVPLATNMGTAEILIKGLERGDFAFRDIIHEQEKANPLKEG | Function: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Catalytic Activity: dihydroxyacetone phosphate = methylglyoxal + phosphate
Sequence Mass (Da): 15759
Sequence Length: 142
EC: 4.2.3.3
|
A7GN71 | MKIALIAHDKKKDDMVSFAYAYKPIFEQHELFATGTTGLRVMEATGLAVTRYQSGPLGGDQEIGAMIAKNALDMVIFFRDPLTAQPHEPDVNALLRLCDVYAIPLATNMASAEMLMHALNRGDLDYRKFRK | Function: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Catalytic Activity: dihydroxyacetone phosphate = methylglyoxal + phosphate
Sequence Mass (Da): 14619
Sequence Length: 131
EC: 4.2.3.3
|
Q72NU6 | MKEVSVPAIKRIVLIAHDNRKEDLVNWVKTHREILSKHQLYGTGTTGKLISEETELPVYRFLSGPLGGDQQIGAKIAEGDLDIVIFFWDPLTAQPHDPDVKALLRIAVLYNVPMACNRSTADYMISSPQFTKTYKKILLSYNTKVKKD | Function: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Catalytic Activity: dihydroxyacetone phosphate = methylglyoxal + phosphate
Sequence Mass (Da): 16727
Sequence Length: 148
EC: 4.2.3.3
|
C6BZQ4 | MSKVKNIAVVAHDNCKKELLDFVDCNHNILSRHNLVATGTTGGLVEKMIMERVEQKADEGYEFKPVNRMKSGPLGGDQQLGAMISEGKIDVLIFFWDPMQPQPHDVDVKALLRLAVLYNIPTASNRSTAEFLISSPFFEGEFQRKETDFSSYTQRKL | Function: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Catalytic Activity: dihydroxyacetone phosphate = methylglyoxal + phosphate
Sequence Mass (Da): 17720
Sequence Length: 157
EC: 4.2.3.3
|
B2A7A5 | MRIALIAHDNKKDELLHFIKRYEHVLATHTLCATNSTGRLIAENTNLMVHRYQSGPLGGDQQIGSEIATGNVDFVFFLRDPLTAQPHEPDITALLRICDVHNIPVATNFATAEILVESVL | Function: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Catalytic Activity: dihydroxyacetone phosphate = methylglyoxal + phosphate
Sequence Mass (Da): 13329
Sequence Length: 120
EC: 4.2.3.3
|
Q30ZX0 | MKGQRNIGMVAHDERKEDLLDWVQHNLQALIPHRIFATGTTGGLLRQRFGDLTITPMKSGPLGGDQQLGSMIAEGRLDMLFFLIDPMAPHPHDVDIKALLRLAVLYNIPAAYNRSTADFLITSPFMTGEYIPEIKDYTPYVKRLGAK | Function: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Catalytic Activity: dihydroxyacetone phosphate = methylglyoxal + phosphate
Sequence Mass (Da): 16477
Sequence Length: 147
EC: 4.2.3.3
|
Q6D6C8 | MEFTTRTIPAQKHIALVAHDHCKQSLLDWVGTNKQQLTEHTLYATGTTGNLIQSNTGLPVKSMLSGPMGGDQQVGALISEGKIDLMIFFWDPLNAVPHDPDVKALLRLATVWNIPVATNRATADFLINSALFKEPVQIAIPDYQRYLQDRLK | Function: Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Catalytic Activity: dihydroxyacetone phosphate = methylglyoxal + phosphate
Sequence Mass (Da): 16878
Sequence Length: 152
EC: 4.2.3.3
|
A0R1T4 | MNSPGAVDVVIVGAGPVGLTLANILGGQGVRTLIIEERETLIDYPRGVGLDDESLRTFQSIGLVDAILPHTVPNQILRFYDANRRLLAEMAPPDARFGWPKRNGFVQPMVDAELLAGLDRFDHVEVMWGRRMQTIAEDADGVTVEVSGPDGPASVHAQYVVGCDGGRSATRHLMGVSFDGTTSSTRWVVIDLANDPLGHPNSEVGADPQRPYASISIAHGIRRFEFMIHADETDEQAEDPEFVAELLRPFVPHPDRVDVIRRRVYTHHSRIAGSFRKGRMLLAGDAAHLMPVWQGQGYNSGIRDAFNLGWKLAAVVRGQAGDALLDTYDAERRKHARAMIDLSTMVGRVISPTNRKVAALRDKLIRGASIVPTLKRYVLEMRFKPMPRYHEGAVYHAKPPTPASPVGTLFIQPRVDTREQDNVLLDDVLGTGFAVLCWNNNPRTLLGEAAFTRWKALGATFIAARPSTQLHWTKDDDPDVVIVGDRTGALKAFFDAHTESVLVLRPDRCIAGADIAQRAPELSTALFGILHLRQGGENGATGPVLYVPQPTAESSGTVGRAS | Function: Catalyzes the insertion of one atom of molecular oxygen into position 2 of the phenyl ring of 3-(3-hydroxyphenyl)propionate (3-HPP) and hydroxycinnamic acid (3HCI).
Catalytic Activity: 3-(3-hydroxyphenyl)propanoate + H(+) + NADH + O2 = 3-(2,3-dihydroxyphenyl)propanoate + H2O + NAD(+)
Sequence Mass (Da): 61387
Sequence Length: 562
Pathway: Aromatic compound metabolism; 3-phenylpropanoate degradation.
EC: 1.14.13.127
|
Q4P8D2 | MLSSKLVACSAGRSVQRISRTFLPAMRGVATKAAAGPSRQSALSSYSIAAVTAIGVGASFYALQSRSSAIQCEPRQAWHDRLKPKEAKGDATLHKDAHTRHAPAEVQDERVEPVEETPVAIEVAVEESEEQTGQQSAYDPETGEINWDCPCLGGMAHGPCGEQFKLAFSCFVYSEAEPKGIDCVDKFKAMQDCFREHPDVYKDEIEDDEAANAQFEKEEANAKSNGLNDAAQEAVEESSGGKEGASA | Cofactor: Cu(2+) or Zn(2+).
Function: Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Forms a redox cycle with ERV1 that involves a disulfide relay system. Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondria. The oxidized form of MIA40 forms a transient intermolecular disulfide bridge with the reduced precursor protein, resulting in oxidation of the precursor protein that now contains an intramolecular disulfide bond and is able to undergo folding in the IMS (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 26545
Sequence Length: 247
Domain: The CHCH domain contains a conserved twin Cys-X(9)-Cys motif which is required for import and stability of MIA40 in mitochondria.
Subcellular Location: Mitochondrion inner membrane
|
Q6PBC3 | MSYCRQEGKDKIIFVTKEDHETPSSAELIADDPNDPYEDHGLILPNGDINWNCPCLGGMASGPCGEQFKSAFSCFHYSQEEIKGSDCLDQFRAMQECMQKYPDIYPQEDDEDEAEKEKQNKEAEAFSTETSDTKEESSS | Function: Central component of a redox-sensitive mitochondrial intermembrane space import machinery which is required for the biogenesis of respiratory chain complexes (By similarity). Functions as chaperone and catalyzes the formation of disulfide bonds in substrate proteins, such as COX17 or MICU1. Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondria.
Sequence Mass (Da): 15712
Sequence Length: 139
Domain: The CHCH domain contains a conserved twin Cys-X(9)-Cys motif which is required for import and stability of MIA40 in mitochondria.
Subcellular Location: Mitochondrion intermembrane space
|
P36046 | MLRNLVVRNACRNRPSIQVARGLCRHQTRRLMASSPQFGRNSNQEKTAGFIMGILSMAGALYFIAPNRKPLFASRKVESDKTAEEELSSGGEQSPENEDDNNSKSDENGDDNDSKNDETEAGPQLGGDKIGASKVAEDGELVVLAEEDNKSSEDKDTDESKVSTKDDEQSNEDNATANNQKDENISSENSEENTSDKTLDNNAGSSEKKDPEHSDDEKSQQGQSDDKTTTEDNNGEEESSKKTVSDSENSAKQSESSDEEKEELRKQEEKQMGPTEEEVQHEGAYNPDTGEINWDCPCLGGMAHGPCGEEFKSAFSCFVYSEAEPKGIDCVEKFQHMQDCFRKYPEHYAEQLKETSDDEEPQDKVKVNTIESAPNVSSAKENAAKKAEQSDVKKEPLNEESKP | Cofactor: Cu(2+) or Zn(2+).
Function: Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Forms a redox cycle with ERV1 that involves a disulfide relay system. Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondria. The oxidized form of MIA40 forms a transient intermolecular disulfide bridge with the reduced precursor protein, resulting in oxidation of the precursor protein that now contains an intramolecular disulfide bond and is able to undergo folding in the IMS. Reduced MIA40 is reoxidized by FAD-linked sulfhydryl oxidase ERV1.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 44536
Sequence Length: 403
Domain: The CHCH domain contains a conserved twin Cys-X(9)-Cys motif which is required for import and stability of MIA40 in mitochondria.
Subcellular Location: Mitochondrion inner membrane
|
Q8A018 | MPTLIVLIGPTGVGKTELSLRLAENFHTSIVSADSRQLYAELKIGTAAPTPDQLKRVPHYLVGTLHLTDYYSAAQYEQEAMEILHQLFTEHEVVVLTGGSMMYVDAICKGIDDIPTVDAETRQVMLQKYEEEGLEQLCAELRLLDPDYYRIVDLKNPKRVIHALEICYMTGKTYTSFRTQQKKERPFRILKIGLTRDREELYDRINRRVDQMMEEGLLDEVRSVLSYRHLNSLNTVGYKELFKYLDGEWELPFAIEKIKQNSRIYSRKQMTWFKRDEEIRWFHPEQETEILEYLRLQNLTHLPSLDTF | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 36187
Sequence Length: 308
EC: 2.5.1.75
|
A5GE43 | MSCNLLVILGPTASGKTQLGVELARRLSGEIISADSRQVYRGMDIGTGKDLAEYGDIPYHIIDIVDPGFEFNVFEFQRCFQRAFAHIVNRGRLPVMVGGTGMYLEAVLNRYRFVEVPENADLRRELSTFSDEELAERLKGANPRLHNTTDLLERGRLVRAIEIAEYEDSREPLPLPELAPLIFGIRWERPVLRQRITDRLKARLEQGMIDEIEQLHRSGIPYETLEFYGLEYRFVAKYLKGELNRNDMFQKLNSAIHDFAKRQDNWFRRMERHGTVIHWLEGDGDPLKEAQEILRLNAIPR | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 34870
Sequence Length: 301
EC: 2.5.1.75
|
Q2SJX0 | MSIANDNPNARPVVVLGPTACGKTRLAVALARAFAGEVVSADSRQVFRGMDIGTGKDLQDYGDTPYHLIDIVDPGAPFSLFDYLGAMQRTLDDLDAREKRPIIAGGSGLYLDAILRGYRLVEAPVDPLLRERLKHHDQERLNALLASLRPLHNTTDTQDRERTLRAIEIAYAELNEDSPSVQISIDPVVIGLHCDNDRLRARIRERLETRLDEGLIEEVESLRAEGLSWRQLDELGLEYRYVALYLQEQLNRNDMMQKLASAIYLFARQQVKWFRRMERQGVAIHWLEADDAPLDNALALLRR | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 34367
Sequence Length: 303
EC: 2.5.1.75
|
A6L8Q7 | MKSYELITILGPTASGKTTFAAALAAQLDTEIISADSRQIYRSMDIGTGKDLADYNVNGKQIPYHLIDICEPGYKYNVFEYQHDFFRVYEDMKRRGKLPILCGGTGMYIEAVLKGYKLLDVPQNPELRESLRNKTLEELETILASYKILHNKTDVDTAQRAIRAIEIEEYYKTQAPDVNEYNPINSLIIGIHIDRELRREKISRRLRTRLDEGMVDEVRTILATGVKPEDLIYYGLEYKFLTLYIIGELSFEEMVSQLEIAIHQFAKRQMTWFRGMERRGCEIHWIDATLPTEEKIATTMRILNNQL | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 35576
Sequence Length: 307
EC: 2.5.1.75
|
B2RKS4 | MITILGPTACGKTRLAVSLAYRLGTEIISADSRQIYRGMDIGTGKDLADYQVGGTTIPCHLIDIRPAGDKYNLFAYQHDFHQAYASILARGMDPILCGGTGMYIEAVLKGYHLPDVPPNPTLRDRLQGKSLTELTLILAAYGPLHNKTDVDSAQRAIRAIEIAEYIKNNPAESTEFPPIDSLIIGLDLDRDTRRKRITDRLHARMHEGMIEEVKGLLDSGIPADDLIYYGLEYKFVTLYLTGQTDYESMFTGLETAIHQFAKRQMTWFRGMERRGFLIHWIDALLPADEQCEAVMKLYTANG | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 33847
Sequence Length: 302
EC: 2.5.1.75
|
Q2LTI8 | MMKNLVVILGPTASGKTRLAVRLARDLKSEIVSADSRQVYRGMDIGTGKDLDEYRIDGEEIPCHLIDIVDPDYDFNVFEYQSRFYRCFEEILSRGIVPILVGGTGLYLSAVLENYRMVQVPENLDLRESLKAEPLERLQQILLEITPRIHNTTDLLDRGRLLRAIEIAQHSGRRGLRESPEHPRIEPLVFGVRWNRDLLRKRIALRLKERLSAGLIDEVKELHQSGISWDRLEFFGLEYRYVGLYLQSRMSYREMAEKLTIHICRFAKRQETWFRRMERHGIEIIWIEGDDYEALKEQLKGNLRS | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 35757
Sequence Length: 305
EC: 2.5.1.75
|
Q056X7 | MNKKKFLFFLMGPTAIGKSSLALEIKKKFPLIELISVDSKLVYKGLNIGTDKPNKSDLKNFSYKLVNIVKPKNIYTVINFYNDVLKEIKNILKSGKIPLLVGGTMLYFKILLNGFANLPPSNSIIRKYIFKNICLKKKKNLFNLLKKIDPISSKKIHINDVQRVLRAVEVFFVSGGFPLSELIKFFHNKLPYKVFQFGLIPDNKEHLYKKIEKRFFFMLKSGFKKEVQNLYNQKFLDPKLPSMNSIGYKQMLLYLKNKYTYFQMIKETIKSTHKLVKHQLTWLKKWPNIIFIKDNKKDLLITKIYKILNRNL | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 36686
Sequence Length: 312
EC: 2.5.1.75
|
A3NYW4 | MSERNAASARTVACLLGPTASGKTAAALALAARRPIEIVSVDSALVYRGMDIGTAKPTRDERAAVPHHLIDIVDPADAYSAAEFRADALRLVAQIAARGRTPLLAGGTMLYYRALTQGLNDLPAADPDVRATLDADAARDGWPALHARLAGIDPATAARLAPNDSQRIQRALEVYLLTGQPMSALLAAPPRDDDAAAGLRFVPVALEPSERAVLHARIAARFDAMLEAGFIDEVERLRRRDDLHLGLPSMRCVGYRQAWEYLDGCTDYRTMRDKGIFATRQLCKRQLTWLRAMPERIVVDCCAPDATVRAVDALERVLDGRAPA | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 35096
Sequence Length: 324
EC: 2.5.1.75
|
B9MJT8 | MEKIPLIVIAGLTATGKTDVAVELAQLVNGEIVSADSMCVYKLMDIGTAKPTKEQREAVRHHVIDVVFPDEDYNVAMFQKDATNAILDIYKRGKVPLLVGGTGFYIKSVVDDIEFPEMGDSKQVRKKLFDELNNKGNMYLYELLKEIDKDAANSVHPNNVKRVIRYLEIYFLTGKKPTEFLDKVRRKGSERYNVLPLCFIMEREALWQRIDQRVEKMFDMGLADEVKMLLDMGYSKDLKSMQGLGYKQVIPYVEGKISLQEAKEELKIRTRQFAKRQRIWFKYQGEFVFLDVTGMRFEEVVKKCFELCKSVV | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 36056
Sequence Length: 312
EC: 2.5.1.75
|
Q7U323 | MKIIAVLGSSGSGKSALAHRIAMEQNCKIFSLDSLSIYKYLDIASAKPTLLEQSQVCYYALNILEPHQKSNVMIFKDLLLQSIEDIKNNSPHTPLLIVGGSSFFLKSIMEGLSPMPPLEEHEEWVKSLGNISMQYAQLTQIDKTYAQSLSPTDTYRICKALALFKATNTPPSIYFATHKKESLGYDIEIFCLECERDELRERIAKRTKAMIQKGIVEEVQNVLEAYGAQAPALNAIGAKECVNFLQGKVATLQQLEEQIFFHTCQLAKRQRTFNRTQFAQITHLKEKALEAQLIQQIHNNIL | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 34054
Sequence Length: 302
EC: 2.5.1.75
|
O25961 | MIKEGFLIKTPKKLIALLGPSGSGKSALSIELAQELDAEIFSLDSLSIYKDINIASAKPSLKERKNIKHYALDHLNIDEKNNAPLFKTLLEDAMRVSSKEILLIVGGSSFYLKSILEGLSRMPKLSGEEVVKIEREIATLSNPYIFLKSIDPNMAFKIHPNDTYRTHKALEIFYATCTPPSEYFKANPKKPFEHAISLFALSIEKSALHNNIKRRTKNMLHSGLVEEIKALYTQYPKDSQPFKAIGVKESVLFLEKRLTLKELEEAITSNTMKLAKRQNTFNKTQFNNLYVGSAEEVRHAILKHSKSGIKG | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 35037
Sequence Length: 311
EC: 2.5.1.75
|
A9AY15 | MQAPQPLIIAIVGPTAVGKTAFSLDLAQALNGEIVSVDSRLVYRGMDIGTAKPTPAEQALVKHHLIDVVNPDQEYSLATYQAAAYAAIAQIQQQAKQPILVGGTGQYMAALLEGWSIPEVAPNYELRARYEQQAASEGHAALHQQLQTIDPEAAKAIDPTNVRRVIRALEVFHETGQPISQLQQRNPPHYRILTLDLERPRDELYARIDQRVDLMMREGLIAEVWALIRQGYGWELPSMSGLGYAEFRPLWQGQQSAGACISQLKFNTHRFARKQGAWFRRLPKRVSLDARHTDLLAQVQELLAMPEHAPIHTDH | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 35194
Sequence Length: 315
EC: 2.5.1.75
|
Q31GP3 | MQSMNVAQLIEQKICLAIMGPTASGKSGLTMALAKHLPIEIISVDSALIYRGMDIGTAKPTLDEQVAVPHHLIDILDPTESYSAADFVEDVHELVKEIFARGNLPVLAGGTMMYFNALQQGMAKLPSADEAIRAKIHQAWQANPAAVHAQLKQVDPEAAERIHQNDPQRLIRALEVYEMTGKPLTQLQREGQQEGLTEFKLAKVALIPEDRKKLHEQIAVRFHEMLNNGFLKEAEKVFSLDGLSADLPAIRSVGYRQAWLFFAQEYDYDTFVEKSIVATRQLAKRQITWLRKEQDLLVLDPFKTNVDDRVEAVLDYLSALTKNA | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 36299
Sequence Length: 324
EC: 2.5.1.75
|
B4U6P0 | MSIDAIIIGGPTASGKTEIAHELAKLLNTEIISADSMCVYKFMNIGTAKPSLEKRKEIKYHMIDVVLPNEYFDTYIYVEKAKSIIKQIKEKGKIPIIVGGTYLYIQALLYGLPETSEPDFRLRKKLESIANKKGLHFLYEKLKVIDKVYAEKIGKNDKKRIIRALEIFINTGKPFSSFHKWHEPTMKVLGFYTNLTQEELNKNIEKRTYYMIEQGLEVECINLLCLGYKEAMTSSQAIGYKEMIPYIEGKSSLKEAIENIIKNTKEYASRQRRWFQKTTFTPIRTIEDIKHHLQSLVL | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 34473
Sequence Length: 298
EC: 2.5.1.75
|
Q0C511 | MHPAILIHGPTASGKSALAIELARKLGGEVINADSMQVYSDLQVISARPTEEEMAGVPHHLFGYVDAGRRYSTGEWLESARSVLKRLQRQNKHAVIVGGTGLYLLALTQGLSDIPPVPEDIRAEVKAISESEGADGLRLRLAPHDPELAERLGTGDRQRLARAYEVWLATGRQLSEFQNERQPPVLKEGEWVGFALTPPRAALYKKIDRRFEGMLMQGAVAEARALVSRNLDPELPAMKALGMPSIAAFVRGEISAEEAAESAKRESRRYAKRQFTWIGRQFPFWPRIPSPEVSDRMRVIFALYREIDTADTEDYA | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 35169
Sequence Length: 316
EC: 2.5.1.75
|
A6W849 | MGQPNVPLVAVVGPTASGKSDVGVALAHLLEREHGRPGEVVNADAMQLYRGMDVGTAKLTPAEREGVPHHLLDVLDVTETAEVARFQADARAAVEDVTARGGLPLLVGGSGLYVRAAVDDLRFPGTDPEVRARWEAELAVLGPHALHARLAERDPAAAAKILPGNGRRIVRALEVGELTGRPFAASLPEQTYLRPTVQVGLAVPREQLDARIDARVERMWAAGLVAEVRDLEARGLREGRTASRALGYAQVLDAFDGTTTEDEARELTARLTRRFARKQESWFRRDPRVHWLPAPDGSDPLDLARRVLELLPVASAA | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 34276
Sequence Length: 317
EC: 2.5.1.75
|
Q92HW4 | MLACNDDTSLYLLVKQVTKKEIYSNDLENGNVKRGASMQSLYLIGDPKCCRNNSSKQKSIIILCGPTASGKSYLGHELAKAYNGEIINIDSMQVYKEIPIITASPPKSYKTEILYHLYNFLSMTEDFSVIKYLKLATEKIKEITDRGKLPILIGGTGLYINSLVFGYNNIPDISEDLQEQVRNLHVKIGNIELWSKLEKFDPLAASKINQNDTQRLIRAYEVFMQTGKSIFSFQTLPKEQILSDFNFKIIFLNPERKFLYKTCDERLDKIFKEGAIDEIALIKKQFAPKDYTNLKAVGIKEILAYLNGNLTLDEALNAAQIRTRQYAKRQVTWFKNQIQDKITLEYANQEEFTQTLKNPFKII | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 41636
Sequence Length: 363
EC: 2.5.1.75
|
A5UYJ2 | MIPLIAIVGPTAVGKTALSIRLAQQFNGEIVSVDSRQVYRGMDIGTAKPTPAERAAVPHHLIDIVDPDEAFSLAVYQDLATAAIADIAARGRLPFLVGGTGQYLAAVLQGWQLPRVAPRPDIRAALERQAAELGAAALYARLAEIDPAAAASIPPNNIRRIIRALEVYEATGKPISEQRSVQPPPYHTVTIWLTLPTPALYARIDARVEAMIAAGLLDEVHRLLERGYHWDLPSMSGLGYREFRPYFEGRITLDEAIARLKYDTHAFARRQPAWFRRLPNVLTLPADASDLQQQAATIVRQWIDA | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 33530
Sequence Length: 305
EC: 2.5.1.75
|
Q1AW38 | MRSARVVAVCGPTASGKSEVADELSALLTEAEGVWVPTVVVDSMQVYREIPEITNQARSRPAELVGVVPVTREWTVAEHRRRARAAIEGSGAGAAVLDAGTGMYLNATVLDIPLAPKVPREIRALAQRAAAGAANPRREARRLELELYGAPERGSIWEGEPAYELALIYLRPERASLDEAIARRSSRIARRGLADARRLQDLLEAGARVNPSVLGSIGVRELLSHLRGEISLPEAEETISVRTRHLARRQMRWFDKLARTLSGRARLVVSPSPEDPALRKALHSMHDIIGA | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 31753
Sequence Length: 291
EC: 2.5.1.75
|
Q5LSV5 | MAVGAALPPIPEGAPVLIAGPTASGKSALALEIAERFGGVIVNADASQVYDCWRAISARPSPEEEARAPHLLYGHLPYDAPYSAGHWLREVTPLLDGTARPIIVGGTGLYFTALTEGMADIPATPPDVRAEADTLPLDRLLAGIDPATAAGLDRNNRARVQRAWEVERATGRALHLWQADTPPPPLPLARTVPLVLEVDKLWLWDRIARRFDQMLDQGALDEVAAMAARYDPALPAFKAIGVPELMAHLRGEITLDAARERASIATRQYAKRQRSWFRARMGDWHRLPVGG | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 31627
Sequence Length: 291
EC: 2.5.1.75
|
B8GNC6 | MPQPMSPPAIFLMGPTASGKTDLAVELVRRLPCEIISVDSALVYRGMDIGTAKPGPEILAEAPHRLIDILDPAEAYSAARFREDALAAMAEIAAAGRVPLLVGGTMLYFRALEFGLDRLPEADPEVRAQIEAEAAASGWEAIHARLAAVDPPSAARIHPNDPQRLQRALEVYLLTGRPLSAFHGGADASTLPYRLLRLALIPADRAALRERIARRFDQMLELGLIHEVETLYRREDLNPSLPAIRAVGYRQAWAYLAGEMDFETMRSKAIIATGQLAKRQLTWLRSYPGIEVLEMEQLDPAAVVARVRAHLEAARAGAGP | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 34930
Sequence Length: 320
EC: 2.5.1.75
|
O83644 | MRLETQALVPYPVRFDRSHHDALVVLGATATGKTALAVALAQKYQGEIISADSRQVYRGLDVGTGKDLALYGSVPYHLIDVCDPYEEYNVFRFQQAVYGIVPSILRAHKVPIIVGGTGLYLDAVLRQYALVPVERNQALRASLRGASLSHMRAVYFSLKDSHAVHNKTDLEDPARLMRAIEIAVFHATHPELLQQARETRPMMRAKVYGIQYPRSMLRARIRARLEQRIRGGLIEEVAALHKGGVSWQRLEYFGLEYRFTAQYLQGIIATRDEYVDLLFRAISRFAKRQETWFRRMQRLGVKIHWLVHTENGFVLR | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 36174
Sequence Length: 316
EC: 2.5.1.75
|
Q820X9 | MLAVAFVGATGTGKSLLSLDAARDFNGHIVNADSMQLYRDMDIGTAKLSHSARQGIPHHQIDVIDPSSEASVARYKLSAQTCIKHIHALNSIPFLVGGSGLYVSSVVHNLQFPPTDGRVRKLLEDEADKSGIGVLHDRLLKLHPGFTVSRGNRRRIIRALEVAYITGRSPNPVLPLQNRANNFIVINLICDKGTLDIRLQKRVESFYDNGLIDEVRLLQEKYVLGRTAAKAIGYKQAIMYLAGEISCADAKDSTLQETIRLANKQIKWFRRYSGQHIVDTTDMSVAYEQIRSILNKSFRIS | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 33453
Sequence Length: 301
EC: 2.5.1.75
|
A1WQM5 | MAAPDSRLPNIALAGPTAAGKTAAALALAAALGRRQAVEIISVDSALVYRGMDIGSAKPTPAERAAVPHHLIDIRDPLQAYSAAEFVQDARRLIGEIRARGALPLLVGGTMLYFKALFDGLDAMPAADPAVRARLNARAAEQGWPALHTELARVDPVTAARLAPGDSQRIQRALEVWQISGQPLSSFHAIEKGAAGAYGACACALFSLEPQDRAWLHERIARRFDAMLAAGFIAEVQALRARGDLHPDLPAMRCVGYRQVWEALDWQARHAGGPPLHGAPLHARGMDAVRERGVAATRQLAKRQITWLRSMPQRHTTACDQPQAVAQLVQAVLQRLEQHAP | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 36691
Sequence Length: 341
EC: 2.5.1.75
|
A5CW57 | MPIQINKTVIFLMGPTASGKTNLAIKLSQQFKTRLISVDSALIYKGMNIGTAKPDKATLKKYPHYLINICSPESSYSVFDFIRDANKQIKTAFAKNELPILVGGTSFYFHVLEHGLSNLPESSTKSKEKFNQLLRNKGTIKLHQDLKKIDPQAANKIHPNDSQRIIRALEVFNLSGKTISELQGNKKPIIDYPIKKIILMPKRNELHTKIETRFLLMMKNGFLNEVQHLKQNPNLHQNLSSIRCVGYRQAWQYLNGKIDKTEMIEKIIIATRQLCKRQITWLKSEKYALVLNNSNLAKAVTFINS | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 34821
Sequence Length: 305
EC: 2.5.1.75
|
Q8D318 | MNENKCTDKINNLPKAIFIMGQTAVGKTKIAEILKKKLPVEIISVDSGCIYKGMNIGTDKPNVKKSSSDKYHLIDICEPNDYYSVENFRLDALKIMEKISKKGLIPLLVGGSMFYFKSLLHGLSNLPSYNIENKNLLKKKINEIGWYKSYIFLKKIDPIFASNIHPNDHYRLTRALEIYFSSGNIPTNLFKAKTKKLEYNIRQFSIMISDKKILYKKIKDRFFNMLKNGFKKEVEFLKNKKQINKNMPSMRCIGYKQMLAYLSGEINYKEMILFTISATNKLAKKQSTWLKKWKNINYIYNKDVYISSEEIFNILKKDNFID | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 37598
Sequence Length: 322
EC: 2.5.1.75
|
Q97I18 | MDKNKLFFIETWGCQMNAEDSEKLAGMLKEMKYEATDNREDADLIIFNTCCVRENAELKVYGNLGTLKKLKDKKPNLIITVCGCMMQQRDMAEHIKKRFPFVDIVMGTHNTQMFPQYLKKVENERTSVVEIWDKEEGIVEGMPIYRSYDMKAFVTIMYGCNNFCTYCIVPYVRGRERSRKPEDIENEIKELVKKGYKEITLLGQNVNSYGKSLDEEMNFALLLRRLNNIEGLLRIRFMTSHPKDLTDDVIAAIADCDKVCEHIHLPVQSGSTTILNKMNRNYTREDYINLVNKIKSGIKNVAITTDIIVGFPGETEEDFEDTLSLVKEVEYDSAFTFLYSIREGTPAAKYENQIPDEVKHKRFNKLLEAVNLISEKKNKEYEGKIVEILVEGKSKNDGSKLMGRTRTGKLVNFEGLESSIGKLINVKITKAQAFSLVGEEV | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 50575
Sequence Length: 441
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
Q895H1 | MLNNIVNTIHSDKNQKGTFFIETWGCQMNEEDSEKLSGMLKNIGYKNAEDKNQADIIIFNTCCVRENAELKVYGNLGALKGLKSKNPNLIIAVCGCMMQQEGMAEAIIKKYPFVDIIFGTHNSYKFPEYLNRAKQEGKSIIEVWDKEEEIVEGIPVDRKSSTKAFVTIMYGCNNFCTYCIVPYVRGRERSREVSDIEKEIKELVKSGYKEITLLGQNVNSYGKDLEPKVSFAELLRHVNEIEGIERVRFMTSHPKDLTEDVIYAIKECDKLCNHIHLPVQSGSSRILKKMNRYYNREDYLNLVNKIKEEIPNVAITTDIIVGFPGETEEDFNETLELVKEVEYDSAFTFLYSKRKGTPAYDIEEQVPEDVKHDRFKKLVEVVNKSCEKNNKKYQDRIVKVLVEGESKNDKNKLSGRTDTAKLVNFIGNKDNIGKIVDVKITKTLSFSLEGEEV | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 51894
Sequence Length: 453
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
B5Y8R7 | MKYYIFTYGCQMNKNDSEMVSGILKSSGWEEAKNVVDSDLVVINTCSVRLHAEERAIGTISALKKLGKKVVVMGCMSEVRGNEIMSRFPHVQAVLGPSYEAHILDVLNGERRILVGDEKVDFEKYSSANRKEKHSVYVSIMKGCDDFCTYCIVPFTRGRVQSRDPESILEEVRVCVDNGAVEITLLGQNVNDYGKDLSGWDFVSLVERVATIDGVRRIRFMSPHPANFKKDDITRLANLPQVAPYYHLPLQSGDDEILRRMNRKYTTGEFAELVGFIRESVPNVAIGTDLIVGFPGESDEHFQNTFKFLEKMQFDVVYMAIYSPRPGTAAARQETSFVPAEVAKARYDELLRLQEKISYSINQRYVGTLQEVLIDREDKTTGKFIGRTPTNKTVVFTSIRHVSPGEFVDVRINEAKSWVLYGEAAD | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 48122
Sequence Length: 426
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
Q2G9P6 | MSSSAPSSASPKTFRVKSFGCQMNVYDGERMAELLAAQGMSAAGDGDDADLVVLNTCHIREKATEKVYSDIGRLRRADGSAPLIAVAGCVAQAEGEEIMARAPSVKVVVGPQSYHRLPEMVADAAAGKRSTETDMPAEAKFAALPKRRKSAPTAFLTVQEGCDKFCTYCVVPYTRGAEISRPFSDLVEEAKLLVAGGAREITLLGQNVNAWAGEDDKGRPIGLDGLARALAAEPDLKRIRYTTSHPNDMTDGLIAAHGELEKLMPFLHLPVQAGNDRVLKAMNRSHTADSYMALLERIRAARPDIALSGDFIVGFPGETDAEFEDTLRLVDAVGYAQAFSFKYSARPGTPAATMENHVPVAVMDERLQRLQAALNRDQLAFNKASVGKTCEVLVERRGKHPGQWLGKSPWLQSVHFSGEAEIGDMVTVELIEAGPNSISGRLA | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 47685
Sequence Length: 443
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
Q30YS1 | MHERTFHIMTFGCQMNVNDSDWLARALEARGFTQVPEHEAAIYIINTCSVRDKPEQKVYSLLGRIRRETKNRRNVTVCVGGCVAQQIGKGFFKRFSQVRLVFGTDGAASAPQAIERLVQEPHARISLLDFSEEFPERDAGWENGEVPVSAYVNIMQGCNNFCAYCIVPYTRGRQKSRSSAAVLDECRTLVGNGAREITLLGQNVNSYGLDPHGDGTTFARLLHDVAAIPGLERLRFMTPHPKDIAGEVIEAFGALKNLCPRVHLPLQSGSDRVLKAMGRKYDMARYMDIVTRLKAVRPDIQITSDLIVGFPGETEADFEQTLEAMRTVPFVQSFSFIYSDRPGTRAEMLPGKLSREEKTARLVRLQEVQNEYSEAALQAMVGKTVMVLFESPSPKSAAGSGTDAQNAAEESGRTASSWQGRDEHGFILNVHLPAPADLYGKIMPVTVTAARKHSLTGEPAGESC | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 51243
Sequence Length: 464
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
B1ZVI7 | MNRVHIKTYGCQMNERDSEAVAAMLRARGYRIVADENDCDILLLNTCSVRDAAEQKAIGKAGYLQQRKKKQPDFVLGILGCMAQNRGASLLDQLPDVDLIVGTQKFHQVPGYLDNLRAARDAGVPIGETIVDIGEEAGSQNTIKDHLLPQDSDSDSQPSTLNSQLRGAAAPPPQITAFVSIQQGCNMDCAFCIVPKTRGDERSRPMDDIVRECEQLAARGVREVTLLGQIVTSYGRRDYTHTNGISPFVQLLERVHALDGIERIRFTSPHPRGFKDDLVAAYGRLPKLCGYVHLPLQSGSNRILRAMNRPYTRERYREIVDALRAVRSDMYFSTDVIVGFPGETDEDFEQTRELFEACNYDMAYVFKYSVRTGTPAAERGDQVPEDVKEQRNQLLLELLRQNSERRNALLLDTVEEVLVEGPDKTGQRFTGRTRGNRVCIFEATPDLVGRLVSLRITRASVSTLYGELMLAGVGRERNRK | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 53739
Sequence Length: 480
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
B3CV38 | MNKMLYIKTYGCQMNVYDSNRMVDLLETQGYNIVANMADASVIILNTCHIREKASEKMYSELGRIKKLQQSRLKAGKSKAKIIVAGCVGQAEGEEIFIREPAVNIIVGPQSYYNLPTMLEKLDSGTENHLIDLDFVEAAKFNKLPEVLKSPTVSGLVSVQEGCDKFCTFCVVPYTRGAEFSRPLEQVYREVLNIAQQGAKEVVLVGQNVSAYHGKDENGKECSLADLIKYVAKIDKIKRIRYITSHPNDMTDQLLSLHATEEKLMPFLHLPVQSGSNKILKLMNRRHSRERYLEIIQQLRELRPDIVISSDIIVGFPGEDDEDFEATLSLAKEARFGQCYSFKYSQRPGTPAAVKQQISEEVKQHRLSILQAQLMQQQLECNQKLIGKVVPVLFDRDGKYDGQIIGKTPYMQSVCIMNEKDNNLYGKIVNVKILTASASSLFGEVYADS | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 50580
Sequence Length: 449
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
Q0AYB7 | MGDKEKKPLKYRILTYGCQMNVRDSETIAGLLEGSGFNQAEDLSEADLIVFNTCSVRHSAENKVYGKLGEIASLKKKRPELLIAFGGCMAQLPEVRQKLKKRGVDVVFGTHNIHELPYLIARAKEKRSPVFEVWEKEGSIVEPLPSCRKPGLSAFVNIMFGCNNFCSYCIVPYTRGRERSRKADDIIRELEELAAAGYKEVTLLGQNVNSYGRGLGEKIEFADLLYRANSVAGIERIRFTTSHPKDVSDRLLQAIAECEKLCEHIHAPLQAGSNRILQRMNRNYSREHYLKLVERMRHYVPGVSITSDLIVGFPGETEEDFLETLDMVERVRFDAAFTFLYSQRSGTRAAELAEQIPLEEKKQRLERLNRRQYQIATEINQELQGSIQEVLVEGPSKTNPQKLTSRTRSNRIVIFSGGKDLIGRLINVKITEAKTFSLFGEIFNE | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 50501
Sequence Length: 445
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
Q9WZC1 | MRFYIKTFGCQMNENDSEAMAGLLVKEGFTPASSPEEADVVIINTCAVRRKSEEKAYSELGQVLKLKKKKKIVVGVAGCVAEKEREKFLEKGADFVLGTRAVPRVTEAVKKALEGEKVALFEDHLDEYTHELPRIRTSRHHAWVTIIHGCDRFCTYCIVPYTRGRERSRPMADILEEVKKLAEQGYREVTFLGQNVDAYGKDLKDGSSLAKLLEEASKIEGIERIWFLTSYPTDFSDELIEVIAKNPKVAKSVHLPVQSGSNRILKLMNRRYTKEEYLALLEKIRSKVPEVAISSDIIVGFPTETEEDFMETVDLVEKAQFERLNLAIYSPREGTVAWKYYKDDVPYEEKVRRMQFLMNLQKRINRKLNERYRGKTVRIIVEAQAKNGLFYGRDIRNKIIAFEGEDWMIGRFADVKVEKITAGPLYGKVVWVEKTPSPVSSSE | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 50742
Sequence Length: 443
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
B5YKW2 | MKGRAVYIKTFGCQMNEHDSERMLGILGTKGFIEVDEPKKADIVIFNTCAIRHKAEQKFFSSLGRVKHLKKKNPQLKIIVAGCSAQLQGEKLLNKLPYIDYIIGPDNLHVIENIIENQVSHRIFTDENPEVANINLPVKRKDCVKAWVNIIYGCNNYCTYCVVPYTRGKERSRPVDDIIKEISLLAEQGYKEVTLLGQNVNSYKDGNTNFPLLLEKVEKIEGIKRIRFITSHPKDLSKELVDVMKDYKKICEHIHLPLQAGSNKILKLMNRKYTYEEYFEKICWLREAIPDIAITSDIIVGFPQEQHEDFEKTINALKEIRFDGIFAFKFSPRLGTAAAKLDGHISEEVKAARLIEVLKLQDEITERKNKRLEGKIQEVLVEGKDEEGFTTGKTRTNKVVKIYSDIKAGEIVNVKIAKTHRHSLEGDIIST | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49301
Sequence Length: 431
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
Q73MD3 | MTYFFETYGCQMNQAESSSMEQILLEKGWTNSSDAEHCDLLIINTCSVRITAENRVLGRLGHFSGLKKKRKFFVLLIGCMAERLYTEIQKEFPLIDYVVGMFERNLLPQIFDEIKARLKNDNYMAEFTHDNIEEKPVSGYYFAPLSHSPKSFQSYVPIMNGCNNFCTYCIVPYVRGREVSRPVNEILQEITELSSRGVREITLLGQNVNSYKGEDGEGRLIDFPKLLTLIAREADKTDMIRWIRFMSSHPKDMSDALIDTIAAEKRLCKLVHLPVQHGSDTILKRMNRVYTIEHYKNRIKRLKETIPDIALSTDILMGFPGETEDDVKATLDLMQEIEFDSAFMYHYNPREGTKAFNYPDRIPEEVKIERLGRVIDLQLKITAKKMKAKLGKKVDILVESHSRNERSELFGHTEQGEMTVIQGNPPESLIGNFAHAELKELKGKTFRANLN | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 51918
Sequence Length: 451
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
O83735 | MTYFFETYGCQMNVAESASVEQLLLARGWTKAVDAQTCDVLIINTCSVRITAETRVFGRLGLFSSLKKKRAFFIILMGCMAQRLHDKIQQQFPRIDYVVGTFAHARFESIFQEIEQKLTQKDYRFEFISERYREHPVSGYRFFASSYSEGSFQSFIPIMNGCNNFCSFCIVPYVRGREISRDLDAILQEVDVLSEKGVREITLLGQNVNSYRGRDREGNIVTFPQLLRHLVRRCEVKDQIKWIRFVSSHPKDLSDDLIATIAQESRLCRLVHLPVQHGANGVLKRMRRSYTREQYLSLVGKLKASVPNVALSTDILIGFPGETEEDFEQTLDLMREVEFDSAFMYHYNPREGTPAYDFPDRIPDATRIARLQRVIALQMSTTLKKMRARVGKTLPVLVESRSRNNPEELFGHTELGEMTVLEGKVDPTYIGRFVDVQVKEVRGRTLRAHLVQERAK | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 52572
Sequence Length: 456
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
B3E424 | MNHKKLYIDTVGCQMNVNDSERIVTMLQPLGYTQTSRRHEAALILFNTCTVRAGAEECLLQNIANLKNLKRKKPGTLIGVAGCVAQQMGAELLQKFPWVDLVFGTHNLHLVPEMVKDAEAGRRRAETDFLDSSERLDLFPPIEGRKRVSAFVTVMQGCDNFCSYCIVPYVRGREISRRFAEILQEVQDLAAQGLREVVLLGQNVNSYGLKGEEQPSFAELVRAVAAVSGIDRVRFVTSHPKDMSDDLIACFADLAKLCGSLHLPAQAGNNRILKAMNRGYSREHYLETIYKLRQARPEIKITGDMIVGFPGETEAEFEETLSLMEEVRYFDLFSFVYSPRPGTKAAELSDELAKEVKLARLDRLQKLQAVHSRIHNETYVGSTQQVLVEGLAKRHGQVSGRCDSGRIVNLAGSPALIGKLVDVKILEGYANSLLGELL | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 48768
Sequence Length: 438
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
Q8YT18 | MNLFKPRILVLFAATALISGIAIVAQTSVADSGDKITATSSLKTPIVNRAITESEVLAAQKAWGEALVAISTTYDAKGKASAKALAEKVIDDAYGYQFGPVLFKPTLAISPRTFRTTRAGALAYFVGDDKAFPEDKGFALSSWRKVEIKNAAIFITGNTATTMGNVIITDKQGKATTVDKTWQFLKDDHGKLRIITHHSSLPYEQ | Cofactor: Does not require a metal cofactor.
Function: Catalyzes the hydration of carbon dioxide (CO2) to bicarbonate (HCO3(-)) . Has only very low bicarbonate dehydration activity . May function even in metal-poor environments .
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 22111
Sequence Length: 205
EC: 4.2.1.1
|
Q09T02 | MNDILETETPVMVSPRWDMLLDAGEDTSPSVQTQIDAEFRRVVSPYMSSSGWLCTLTIECGTIICACR | Function: Lanthionine-containing peptide antibiotic (lantibiotic) active against S.michiganensis subspecies sepedonicus strain 2136 (MIC=30 pmol/ml). The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.
PTM: Maturation of lantibiotics involves the enzymatic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. The 62-67 beta-methyllanthionine thioether bond is oxidized to a sulfoxide. This is followed by membrane translocation and cleavage of the modified precursor.
Sequence Mass (Da): 7572
Sequence Length: 68
Subcellular Location: Secreted
|
Q5B7T4 | MVGSVVEAHRQSVGCLRNLSQLLAWASNTSGGLIFYSREDDVLTSTRISYAELLADAGEKARLIGQITGLSSESIILLHFDTQREVIEWFWAATLAGYLPAISTPFVDDTARRKAHLLHLHAQLNQPVVLTSKRLVPEFLGLEELRLHDVESLLSSAAKDGLIQYLGVQKLAEDVAVLMLTSGSTGSAKAVPLRHGQLLTAIQGKSTHHGTLPGDVFYNWVGLDHVASLTEIHLHALILGSDQVHTAASELLRNSLQFVRLLDTHKVAYTFAPNFFLTKVLDSLRENPTFTADLSSLKALISGGESNVVVTCDKLTRELRRRGVQAEVIRPGFGMTETCAGSIYSRACPSYDIRQSLEFASLGSCIPGMHMRIMSITEPGKLAAPGESGELQVAGPVVFDHYYNDETATRNAFTPDGWFITGDLGWIDDAGNLNLAGRTKDTIIVNGVKWSSTELEAAIEEEAVSGLVRSFTVVVPTRPPGSATEEIAVVYSPAYAPEDYHARYETAQVISKTVSLLTGTKPARLIPLPQSLLEKSSLGKISHSKVRAALESGEYASIERADQLILAQYRQFKWRPAKSDSERAVQKALVEFLQVPAEGINMDDSIYDLGVSSLNLILLRSTLQRMLDPKIDIPLSIILNNPTPGAIARSIDSSRSSLAGYNAIVPLQQHRHGGTPLFCIHPGSGEVLVFVALAAHFPTRPVYALRTRGYGSNEQLFGSIEETVETYATQIRQVQPHGPYAIAGYSLGSTLAFEVAKVLEAQGEEVKFLASIDYPPHIAHYVRDLNWTDVLLHIAFFLELIDEKTMVEVTPYLHTLDRQTALTHILNIGDAERARALAIDTKHLGLISDIAENFRVNVKTYKPQGKVQHLDVFVADPPTYAARDRKDWRENKLGRWVDFCETKVEFHDCPGIHAKMLNREHIAGFAKVFKAAMRRRGV | Function: Microperfuranone synthase is the only protein required for the biosynthesis of the secondary metabolite microperfuranone from phenylpyruvic acid (PPA) . Several steps for the microperfuranione biosynthesis have been proposed . These steps include the activation of PPA, by the micA adenylation (A) domain to AMP-phenylpyruvic acid followed by loading of the PPA unit to the thiolation and peptide carrier (T) domain and eventually transferring to the thioesterase (TE) domain . After loading another PPA unit onto the T domain, aldol condensation establishes the carbon-carbon bond between the alpha- and beta-carbon of the two PPA units . Sulfur-assisted furan ring formation, TE domain mediated hydrolysis, decarboxylation, and keto-enol tautomerization would generate microperfuranone attached to the T domain . Finally, microperfuranone is released by the TE domain .
Sequence Mass (Da): 103240
Sequence Length: 938
Pathway: Secondary metabolite biosynthesis.
EC: 2.3.1.-
|
Q29983 | MGLGPVFLLLAGIFPFAPPGAAAEPHSLRYNLTVLSWDGSVQSGFLTEVHLDGQPFLRCDRQKCRAKPQGQWAEDVLGNKTWDRETRDLTGNGKDLRMTLAHIKDQKEGLHSLQEIRVCEIHEDNSTRSSQHFYYDGELFLSQNLETKEWTMPQSSRAQTLAMNVRNFLKEDAMKTKTHYHAMHADCLQELRRYLKSGVVLRRTVPPMVNVTRSEASEGNITVTCRASGFYPWNITLSWRQDGVSLSHDTQQWGDVLPDGNGTYQTWVATRICQGEEQRFTCYMEHSGNHSTHPVPSGKVLVLQSHWQTFHVSAVAAAAIFVIIIFYVRCCKKKTSAAEGPELVSLQVLDQHPVGTSDHRDATQLGFQPLMSDLGSTGSTEGA | Function: Seems to have no role in antigen presentation. Acts as a stress-induced self-antigen that is recognized by gamma delta T-cells. Ligand for the KLRK1/NKG2D receptor. Binding to KLRK1 leads to cell lysis.
PTM: N-glycosylated. Glycosylation is not essential for interaction with KLRK1/NKG2D but enhances complex formation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 42915
Sequence Length: 383
Subcellular Location: Cell membrane
|
Q22638 | MMVSPPQEDTVFNTDSDPVYEQATDDMTFNDTTTDGNGQESVPLEALTVVEIEKTSKGFGFNIVGGTDNPHFVGDIGIYVSSVNSESKSYGVVRTGDKILSFDGIDMTYKTHDEAVEVFRSVKIGHVAKMLIDREYLHLQEDRTQTPTASVSITPQVTPQTRSTQNNTDTPKSMSHSESKSRLTSHGLSAVIERIRGKVYEEEDAQSVTSYAPSTHSIIDDVPRTPRKPLSLLDPRNNSWLTEALYVSIGLGALTISGYLAYRFIRGRR | Function: Plays a role in the regulation of lifespan in a partially daf-16-mediated manner, and may be involved in regulating the levels of reactive oxygen species production in response to heat stress.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 29730
Sequence Length: 269
Subcellular Location: Membrane
|
Q95PZ2 | MLHCSFLRVIPIKNASKRLIIVRSLTSAPAKTSEAEKQQDSLKNIDAGEKYTALGNIRQKKDVFHYTDRASGVGYSHYSSSVYQHRPYIWPPLRKLYHWNYALVIAGMVILMSDFEWLKDQIKSASLPFRPEASQKEEVTESNGEVEEVKEKPKKKKLGFRERRIIEYEDRLRLYSTPDKIFRYFATLKIIDPNEDSGRFEVFMTPEDFLRSFTPGVMQPRRWGLDSFKNYNPEKHKRHKFSDPDSIFYKLGENGLINFSDYLFLMTLLSTSHADFALAFKIFDVDGNGALDKEEFTKVQQLIMSQTTVGQRHRDHITPNQSFRVETNSALETYFFGKDGKGSLSSEKFIEFQERLQHDILKMEFERRDALDNPDGLINEDSFAQLLLLHAQINEKKQKHMLKRVKRRFKGENLKGISFGETKAFFEFLYHIDDVDIALHFHKMAGMSIDAKLLQRVAVKVTGIPLSDHVVDVVITLFDDNLDGKLSHEEMVAVMRRRMRRGLERPRDTGLFRLFDAVLECGKRAYHASPLPFY | Function: Key regulator of mitochondrial calcium uniporter (MCU). Modulates the activity of the mitochondrial calcium uniporter protein mcu-1 depending on the level of intracellular calcium in PLM touch receptor neurons following axonal injury .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 62120
Sequence Length: 534
Subcellular Location: Mitochondrion inner membrane
|
P0AEZ5 | MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYDFVNVIQGDATLNQALIKDKRTENLYILPASQTRDKDALTREGVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSDRILGILASKSRRAENGEEPIKEHLLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLRASNQGEPVILDINADAGKAYADTVERLLGEERPFRFIEEEKKGFLKRLFGG | Function: ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29614
Sequence Length: 270
Subcellular Location: Cell inner membrane
|
O25098 | MAIVVTITSGKGGVGKSTTTANLAIGLAESGKKVVAVDFDIGLRNLDMILGLENRIVYDVVDVMEKNCNLSQALITDKKTKNLSFLAASQSKDKNILDKEKVAILINALRADFDYILIDSPAGIESGFEHAILHADMALVVVTPEVSSLRDSDRVVGIIDAKSNRAKKGMEVHKHLIINRLKPELVANGEMISIEEVLKILCLPLIGIIPEDHHIISATNKGEPVIRTDCESAKAYQRITRRILGEEVEYVEFKAKRGFFSALKGIFS | Function: ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29294
Sequence Length: 268
Subcellular Location: Cell membrane
|
Q7DDS7 | MAKIIVVTSGKGGVGKTTTSASIATGLALRGYKTAVIDFDVGLRNLDLIMGCERRVVYDLINVIQGEATLNQALIKDKNCENLFILPASQTRDKDALTREGVEKVMQELSGKKMGFEYIICDSPAGIEQGALMALYFADEAIVTTNPEVSSVRDSDRILGILQSKSHKAEQGGSVKEHLLITRYSPERVAKGEMLSVQDICDILHIPLLGVIPESQNVLQASNSGEPVIHQDSVAASEAYKDVIARLLGENREMRFLEAEKKSFFKRLFGG | Function: ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29559
Sequence Length: 271
Subcellular Location: Cell inner membrane
|
Q55900 | MNRIIVVTSGKGGVGKTTTTANLGAALARLGKKVVLIDADFGLRNLDLLLGLEQRIVYTAIDVLADECTIDKALVKDKRLPNLVLLPAAQNRSKDAINAEQMQSLVEQLKDKFDYIIIDCPAGIEAGFRNAVAPAQEAIIVTTPEMSAVRDADRVIGLLEAEDIGKISLIVNRLRPEMVQLNQMISVEDILDLLAVPLIGILPDDQKIIISTNKGEPLVMEEKLSVPGLAFQNIARRLEGQDIPFLDFMAAHNTLLNRIRRRLLGG | Function: ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29047
Sequence Length: 266
Subcellular Location: Cell membrane
|
Q9X2I3 | MGNVIVVTSGKGGVGKTTITANLGCALAKLGEKVCLIDADIGLKNLDIVLGLENRIVYTMIDVVNGKVSPQEALVKHKMLKNLYLLPASQIATKEMISPNDMKAIVKELIPHFDYIIIDSPAGIERGFRNAVAPAERVLVVTTPELPAISDADRVIGLLENFGFSDEKINVIINRFKPHMVKKGEMLTTDDIKHTLSLEIIAVIPDSEDIIVASNTGIPVSLNGNSRISKNFENLARRIRGEGVPLENDFVTVSKGLIDTLKDFFSKLKRG | Function: ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29483
Sequence Length: 271
Subcellular Location: Cell membrane
|
Q8L799 | MTILIDRHSDQNDAGDEIVEKNQGNGKEEETELVLDAGFEAPHTNSFGRTFRDYDAESERRRGVEEFYRVNHIGQTVDFVRKMREEYEKLNRTEMSIWECCELLNEFIDESDPDLDEPQIEHLLQTAEAIRKDYPDEDWLHLTGLIHDLGKVLLHSSFGELPQWAVVGDTFPVGCAFDESIVHHKYFKENPDYDNPSYNSKYGIYTEGCGLDNVLMSWGHDDYMYLVAKENQTTLPSAGLFIIRYHSFYALHKSEAYKHLMNNEDRENMKWLKVFNKYDLYSKSKVRVNVEEVKPYYLSLTNKYFPSKLKW | Cofactor: Binds 2 iron ions per subunit.
Function: Catalyzes the oxygenative cleavage of myo-inositol to D-glucuronate. Involved in the biosynthesis of UDP-glucuronic acid (UDP-GlcA), providing nucleotide sugars for cell-wall polymers. May be also involved in plant ascorbate biosynthesis.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
Sequence Mass (Da): 36574
Sequence Length: 311
Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.13.99.1
|
O82200 | MTILVEHFVPDSRVDEKKVIEERDNELVLDGGFVVPKSKETDAFDAPDMNFLGHSFRDYENGESERQQGVEEFYRMQHIHQTYDFVKKMRKEYGKLNKMEMSIWECCELLNNVVDESDPDLDEPQIQHLLQTAEAIRRDYPDEDWLHLTALIHDLGKVLLLPEFGGLPQWAVVGDTFPVGCTFDSANIHHKYFKGNHDINNPKYNTKNGVYTEGCGLDNVLMSWGHDDYMYLVAKKNGTTLPHAGLFIIRYHSFYPLHKAGAYTHLMNDEDRDDLKWLHVFNKYDLYSKSKVLVDVEQVKPYYISLINKYFPAKLKW | Cofactor: Binds 2 iron ions per subunit.
Function: Involved in the biosynthesis of UDP-glucuronic acid (UDP-GlcA), providing nucleotide sugars for cell-wall polymers. May be also involved in plant ascorbate biosynthesis.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
Sequence Mass (Da): 37048
Sequence Length: 317
Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.13.99.1
|
Q8H1S0 | MTISVEKPIFEEVSAFEKSGDNIGELKLDGGFSMPKMDTNDDEAFLAPEMNAFGRQFRDYDVESERQKGVEEFYRLQHINQTVDFVKKMRAEYGKLDKMVMSIWECCELLNEVVDESDPDLDEPQIQHLLQSAEAIRKDYPNEDWLHLTALIHDLGKVITLPQFGGLPQWAVVGDTFPVGCAFDESNVHHKYFVENPDFHNETYNTKNGIYSEGCGLNNVMMSWGHDDYMYLVAKENGSTLPSAGQFIIRYHSFYPLHTAGEYTHLMNEEDKENLKWLHVFNKYDLYSKSKVHVDVEKVKPYYMSLIKKYFPENLRW | Cofactor: Binds 2 iron ions per subunit.
Function: Catalyzes the oxygenative cleavage of myo-inositol to D-glucuronate. Involved in the biosynthesis of UDP-glucuronic acid (UDP-GlcA), providing nucleotide sugars for cell-wall polymers. May be also involved in plant ascorbate biosynthesis.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
Sequence Mass (Da): 36904
Sequence Length: 317
Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.13.99.1
|
Q9FJU4 | MNISVENPVFVHEDSTTQKTGELRLDSDIPMSKISSDDEVFLAPEMNAFGRQFRDYTDTNSERQKSVEHFYATQHTNQTLDFVQKMRSEYGKLDKMVMNIWECCELSKEVVDESDPDLDEPQIQHLLQSAEAIRKDYPNEDWLHLTALIHDLGKVLTLPQFGGLPQWAVVGDTFPVGCAFDESNVHHKYFMENPDFNNPKYNTKAGIYSEGCGLENVLMSWGHDDYMYLVAKENGSTLPSPGLFIIRYHSFYPLHKAGAYTHLMNEEDKENLKWLHVFNKYDLYSKSKVHVNVEKVKPYYMSLIKKYFPENLRW | Cofactor: Binds 2 iron ions per subunit.
Function: Involved in the biosynthesis of UDP-glucuronic acid (UDP-GlcA), providing nucleotide sugars for cell-wall polymers. May be also involved in plant ascorbate biosynthesis.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
Sequence Mass (Da): 36544
Sequence Length: 314
Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.13.99.1
|
Q4V8T0 | MGPDPSLAYRPECHEKDKTEFRNFENGDLFDRVFNTYKLMHTHQTLDFVKQKHQVWSNCSHFSLSMMDSIDSLDELVDESDPDVDFPNSFHAFQTAEGIRREHPDKDWFQLVGLIHDVGKVMALYSEPQWAVVGDTYPVGCKFQNSIVFRNSTFEGNPDGKNPAPNTEFGIYEPQCGLDKVLMSWGHDEYLYRVMKFNKCTIPEEGLYMIRFHSFYPWHSNGDYMHLCNEKDQQMLPWVKEFNKFDLYTKSTELPDVERLKPYYQSLIDKYCPGVLQW | Cofactor: Binds 2 iron ions per subunit.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
Sequence Mass (Da): 32735
Sequence Length: 278
Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.13.99.1
|
Q54GH4 | MIETRTTTSTSEIKHDNSLKTGFEITKEVEEFRNYENSEDRVSEAYRNSHTYQTYDYATEKKKQYSQLDTSIKMGLWEAAELLNTIIDESDPDSNIPQINHCLQTAEAIRKVYPDSKYDWFHLTGFIHDLGKVLLSKKFKEQPQWATVGDTFPLGCKFDESNIFYEFFKMNPDYNDSKYNSECGIYKKNIGLENVTMSWGHDEYFYLVCVGNKCLLPKESLYMIRFHSFYPWHRHNKYTHLTNEEDEKMLNWVKEFNKFDLYSKDSEPVDVESLKPYYQSLISKYFPNELHW | Cofactor: Binds 2 iron ions per subunit.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
Sequence Mass (Da): 34801
Sequence Length: 292
Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.13.99.1
|
Q9UGB7 | MKVTVGPDPSLVYRPDVDPEVAKDKASFRNYTSGPLLDRVFTTYKLMHTHQTVDFVRSKHAQFGGFSYKKMTVMEAVDLLDGLVDESDPDVDFPNSFHAFQTAEGIRKAHPDKDWFHLVGLLHDLGKVLALFGEPQWAVVGDTFPVGCRPQASVVFCDSTFQDNPDLQDPRYSTELGMYQPHCGLDRVLMSWGHDEYMYQVMKFNKFSLPPEAFYMIRFHSFYPWHTGRDYQQLCSQQDLAMLPWVREFNKFDLYTKCPDLPDVDKLRPYYQGLIDKYCPGILSW | Cofactor: Binds 2 iron ions per subunit.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
Sequence Mass (Da): 33010
Sequence Length: 285
Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.13.99.1
|
Q9QXN5 | MKVDVGPDPSLVYRPDVDPEMAKSKDSFRNYTSGPLLDRVFTTYKLMHTHQTVDFVSRKRIQYGSFSYKKMTIMEAVGMLDDLVDESDPDVDFPNSFHAFQTAEGIRKAHPDKDWFHLVGLLHDLGKIMALWGEPQWAVVGDTFPVGCRPQASVVFCDSTFQDNPDLQDPRYSTELGMYQPHCGLENVLMSWGHDEYLYQMMKFNKFSLPSEAFYMIRFHSFYPWHTGGDYRQLCSQQDLDMLPWVQEFNKFDLYTKCPDLPDVESLRPYYQGLIDKYCPGTLSW | Cofactor: Binds 2 iron ions per subunit.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
Sequence Mass (Da): 33164
Sequence Length: 285
Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.13.99.1
|
Subsets and Splits
No saved queries yet
Save your SQL queries to embed, download, and access them later. Queries will appear here once saved.