ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q6PDU4 | MAGIKALISLSFGGAIGLMFLMLGCALPIYNQYWPLFVLFFYILSPIPYCIARRLVDDTDAMSNACKELAIFLTTGVVVSAFGLPVVFARAHLIEWGACALVLTGNTVIFATILGFFLVFGSNDDFSWQQW | Function: Negatively regulates growth hormone (GH) receptor cell surface expression in liver. May play a role in liver resistance to GH during periods of reduced nutrient availability (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14400
Sequence Length: 131
Subcellular Location: Mem... |
Q93373 | MRLLLCLLLFSTLLINSTNACPGVITQACFCSEVHSGIVLDCSNSSASGILQIIRTNQAQVGLIQSLTMNQAELVELPPNFFSGLFIRRLDLSQNKIKKIDDAAFAGINPVLEEVVLNHNLIEKVPAAALAGLPNLLRLDLSNNSIVEIQEQEIFPNLNKLYDINLGSNKIFSIHTSTFQNVKNSIQTINLGHNNMTAVPSSAIRGLKQLQSLHLHKNRIEQLDALNFLNLPVLNLLNLAGNQIHELNRQAFLNVPSLRYLYLSGNKITKLTAYQFQTFEQLEMLDLTNNEIGAIPANSLSGLKQLRQLYLAHNKISNIS... | Function: Required for apical extracellular matrix organization and epithelial junction maintenance.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 85297
Sequence Length: 773
Subcellular Location: Apical cell membrane
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P22981 | MTEYKLVVVGDGGVGKSALTIQLIQNHFVEEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLLVFAVNEAKSFENVANYREQIRRVKDSDDVPMVLVGNKCDLSSRSVDFRTVSETAKGYGIPNVDTSAKTRMGVDEAFYTLVREIRKHRERHDNNKPQKKKKCQIM | Function: The level of let-60 controls the switch between vulval and hypodermal cell fates during C.elegans vulval induction . May stimulate the guanine nucleotide exchange factor (GEF) activity of rap-1 . May induce nuclear condensation .
Location Topology: Lipid-anchor
Sequence Mass (Da): 20983
Sequence Length: 184
S... |
Q8Y5R9 | MKKIQFFDTTLRDGEQTPGVNFDVKEKIQIALQLEKLGIDVIEAGFPISSPGDFECVKAIAKAIKHCSVTGLARCVEGDIDRAEEALKDAVSPQIHIFLATSDVHMEYKLKMSRAEVLASIKHHISYARQKFEVVQFSPEDATRSDRAFLIEAVQTAIDAGATVINIPDTVGYTNPTEFGQLFQDLRREIKQFDDITFASHCHDDLGMATANALAAIENGARRVEGTINGIGERAGNTALEEVAVALHIRKDFYQAETNIVLNQFKNSSDLISRLSGMPVPRNKAVIGGNAYAHESGIHQDGVLKNPDTYEIITPALVGV... | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 56096
Seque... |
A0LBW3 | MNGSMPFHKYSPYPPVALANRQWPNRTLTKAPLWCSVDLRDGNQALANPMGPQAKRRMFDLLVEIGFKEIEVGFPSASRDDFQFLRDLIEQKAIPDDVTVQMLVQSRAHLIERTFEALQGAKRAIVHLYTPTSSLQRRVVFGKSQQEIIDVAVEGTQMIKEHAQRSPETEIVLEFSPESFTGTELPFALAISEAVQQVWQPTPAQPMILNLPATVEMSTPNIYADQIEWMLSHLSDPQSIIISLHAHNDRGTAVAATELAMLAGAGRVEGTLFGNGERTGNTDVVAVAMNLHSQGIDAGLNFSEMPRIIATSEACTGMSV... | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 61808
Seque... |
Q8THA5 | MYTLKEGIDFYIEPMQNKKVTVFDTTLRDGEQTPGVSLTSSQKLEISRQLDKLGVDIIEAGFPISSEGDKESVKSISNAGLETTVCGLARVLKKDIDACFESDVGLVHTFVPTSDVQRIYTIKKSQEEVIQLAVEAVQYIKDHGLKCMFSAMDATRTDPAYLIEVFKAVQEAGCDIINVPDTVGVMVPSAMYRQIKDIAAEITIPIDVHCHNDFGLAVANSLMAVEAGASQVQVTINGIGERAGNADLAQTVMSLASIYGIKTNIRTEYLVETSKMIENYTGIRLPPNTPVVGQNAFSHESGIHSQGVLEKSDTFEPGIM... | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 55693
Sequen... |
B3DX88 | MEMTANRLIVFDTTLRDGEQCPGASMTSRQKLEVAKQLARLGVDVIEAGFPVISQGDFESVSEIAAQVKGPKICGLARCLPKDIEAAAEALKAAADAARIHVFLATSQIHRRFKLAKDEEEIVRIAVEGVRLAKRYVQDVEFSAEDASRTEPEFLAKIIQKVIEAGATTVNIPDTVGYAVPEEFASLIRYLFDHVQDIDKVVVSVHCHNDLGLAVSNSLAAIKAGARQVEGTINGIGERAGNAALEEIIMALHTRPDAFGKIETGIQLKEILRTSRLVSRMSGLAVQRNKAVVGENAFAHAAGIHQDGILKKRETYEIID... | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 55078
Seque... |
Q58595 | MIIYREENEIIKKALENLNIPDRVYIFDTTLRDGEQTPGVSLTPEEKIDIAIKLDDLGVDVIEAGFPVSSLGEQEAIKKICSLNLDAEICGLARAVKKDIDVAIDCGVDRIHTFIATSPLHRKYKLKKSKEEIIDIAVDAIEYIKEHGIRVEFSAEDATRTEIDYLIEVYKKAVDAGADIINVPDTVGVMIPRAMYYLINELKKEIKVPISVHCHNDFGLAVANSLAAVEAGAEQVHCTINGLGERGGNAALEEVVMSLMSIYGVKTNIKTQKLYEISQLVSKYTEIKVQPNKAIVGENAFAHESGIHAHGVLAHALTYE... | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 56620
Sequen... |
Q8TYB1 | MPDRVRIFDTTLRDGEQTPGVSLTVEEKVEIARKLDEFGVDTIEAGFPVASEGEFEAVRAIAGEELDAEICGLARCVKGDIDAAIDADVDCVHVFIATSDIHLRYKLEMSREEALERAIEGVEYASDHGVTVEFSAEDATRTDRDYLLEVYKATVEAGADRVNVPDTVGVMTPPEMYRLTAEVVDAVDVPVSVHCHNDFGMAVANSLAAVEAGAEQVHVTVNGIGERAGNASLEQVVMALKALYDIELDVRTEMLVELSRLVERLTGVVVPPNTPIVGENAFAHESGIHSHGVIKKAETYEPIRPEDVGHRRRIVLGKHA... | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 54339
Sequen... |
B0JGK2 | MNTSPDRVIIFDTTLRDGEQSPGAALNVDEKLTIARALARLGVDVIEAGFPHASPGDFDAVQKIAASVGSEADSPIICGLARTTQKDIKSAADALRPAAKPRIHTFLATSDIHLQYKLKKTRQEVLEIVPEMVAYAKSFVDDVEFSPEDAGRSDPDFLYQVLERAIAAGATTVNIPDTVGYTTPSEFGALIRGIKENVPNIDQAIISVHGHDDLGLAVANFLEAVKNGARQLECTINGIGERAGNASLEELVMALHVRRSYFNPFLGRPAESTEPLTKINTKEIYRTSRLVSNLTGMIVQPNKAIVGANAFAHESGIHQD... | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 58027
Seque... |
Q7TVV6 | MTTSESPDAYTESFGAHTIVKPAGPPRVGQPSWNPQRASSMPVNRYRPFAEEVEPIRLRNRTWPDRVIDRAPLWCAVDLRDGNQALIDPMSPARKRRMFDLLVRMGYKEIEVGFPSASQTDFDFVREIIEQGAIPDDVTIQVLTQCRPELIERTFQACSGAHRAIVHFYNSTSILQRRVVFRANRAEVQAIATDGARKCVEQAAKYPGTQWRFEYSPESYTGTELEYAKQVCDAVGEVIAPTPERPIIFNLPATVEMTTPNVYADSIEWMSRNLANRESVILSLHPHNDRGTAVAAAELGFAAGADRIEGCLFGNGERTG... | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 75683
Seque... |
Q9CB76 | MASFSESLSQDPADAYKSAPSITKPMGPPSPGQPQWNPQRATSMPVFRYRPFAKEVEPIRLVDRTWPDRVIDCAPLWCAVDLRDGNQALIDPMSPICKRRMFDLLVRMGYKEIEVGFPSASQTDFDFVREIITDGTIPDDVTIQVLTQCRPELIERTFEACENASRVIVHFYNSTSILQRRVVFRADQATVKAIATDGARKCVEEAFKYPGTHWRFEYSPESYTGTELEYAKQVCDAVGEVIQPTPDNPIIFNLPATVEMATPNVYADSIEWMSRNLANRESVILSLHPHNDRGTAVAAAELGYHAGADRIEGCLFGNGE... | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 66898
Seque... |
P9WQB2 | MTTSESPDAYTESFGAHTIVKPAGPPRVGQPSWNPQRASSMPVNRYRPFAEEVEPIRLRNRTWPDRVIDRAPLWCAVDLRDGNQALIDPMSPARKRRMFDLLVRMGYKEIEVGFPSASQTDFDFVREIIEQGAIPDDVTIQVLTQCRPELIERTFQACSGAPRAIVHFYNSTSILQRRVVFRANRAEVQAIATDGARKCVEQAAKYPGTQWRFEYSPESYTGTELEYAKQVCDAVGEVIAPTPERPIIFNLPATVEMTTPNVYADSIEWMSRNLANRESVILSLHPHNDRGTAVAAAELGFAAGADRIEGCLFGNGERTG... | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 70114
Seque... |
Q2LWJ3 | MDSPEKRIYIFDTTLRDGEQSPGSSMNPAEKLRIARQLEKMGVDIIEAGFPIASEGDFLSVQQIAQEIRGAQIAGLARANNADIDRAWEAIRDAANPRIHTFISSSDIHLKYQLRKSREQVLKEAVAAVERARSYTPNVEFSPMDATRTDRGYLCEMVEAVIAAGASTVNIPDTVGYAIPQEFGELIAYLRANVPNISQAIISVHCHNDLGLAVANSLSAILNGARQVECTINGIGERAGNTAMEEVVMALRTRKDLFGFYTGIKTESIYQSSRLLTQITGVAVQPNKAIVGANAFAHESGIHQDGLIKEKITYEIMTPQ... | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 56596
Seque... |
Q58130 | MHKICVIEGDGIGKEVVPATIQVLEATGLPFEFVYAEAGDEVYKRTGKALPEETIETALDCDAVLFGAAGETAADVIVKLRHILDTYANIRPVKAYKGVKCLRPDIDYVIVRENTEGLYKGIEAEIDEGITIATRVITEKACERIFRFAFNLARERKKMGKEGKVTCAHKANVLKLTDGLFKKIFYKVAEEYDDIKAEDYYIDAMNMYIITKPQVFDVVVTSNLFGDILSDGAAGTVGGLGLAPSANIGDEHGLFEPVHGSAPDIAGKKIANPTATILSAVLMLRYLGEYEAADKVEKALEEVLALGLTTPDLGGNLNTF... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate, which decarboxylates to 4-methyl-2-oxopentanoate (2-oxoisocaproate). Also catalyzes the oxidative decarboxylation of 3-methylmalate t... |
O27441 | MKSMKIAVIPGDGIGVEVMEAALHILNTLDLDLEFIHADAGDACLKRTGTALPEETLEAVGEARATLFGAAGESAADVIVRLRREFDLFANLRPVKSLPGVPCLYPDLDFVIVRENTEDLYVGDEEYTPEGAVAKRIITRTASRRISQFAFQYAQKEGMQKVTAVHKANVLKKTDGIFRDEFYKVASEYPQMEATDYYVDATAMYLITQPQEFQTIVTTNLFGDILSDEAAGLIGGLGLAPSANIGEKNALFEPVHGSAPQIAGKNIANPTAMILTTTLMLKHLNKKQEAQKIEKALQKTLAEGLVTPDLGGKLGTMEMA... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate (By similarity).
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-me... |
Q73VI1 | MKLAVIGGDGIGPEVTAEALKVLDAVLPGVDKTEYDLGARRYHATGELLPDSVIDELRAHDAILLGAIGDPSVPSGVLERGLLLRLRFELDHHINLRPGRLYPGVSSPLAGNPDIDFVVVREGTEGPYTGTGGAIRVGTPNEVATEVSQNTAFGVRRVVVDAFERARRRRKHLTLVHKTNVLTFAGKLWSRIVAEVGRDYPDVEVAYQHIDAATIFMVTDPGRFDVIVTDNLFGDIITDLSAAVCGGIGLAASGNIDGTRTNPSMFEPVHGSAPDIAGQGIADPTAAIMSVALLLAHLGEDAAATRVDRAVERYLATRGN... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentan... |
Q94AR8 | MASVISSSPFLCKSSSKSDLGISSFPKSSQISIHRCQKKSISRKIVSVMAPQKDRSPGTTGSVKTGMTMTEKILARASEKSLVVPGDNIWVNVDVLMTHDVCGPGAFGIFKREFGEKAKVWDPEKIVVIPDHYIFTADKRANRNVDIMREHCREQNIKYFYDITDLGNFKANPDYKGVCHVALAQEGHCRPGEVLLGTDSHTCTAGAFGQFATGIGNTDAGFVLGTGKILLKVPPTMRFILDGEMPSYLQAKDLILQIIGEISVAGATYKTMEFSGTTIESLSMEERMTLCNMVVEAGGKNGVIPPDATTLNYVENRTSV... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate . Functions in both the biosynthesis of leucine and in the methionine chain elongation pathway of aliphatic glucosinolate formation .
Catalytic A... |
P96195 | MAGKTLYDKLWDMHEVKRRDDGSSLIYIDRQILHEVTSPQVRGAAPGRANVARGCQHRHPGPQRADHPGSPVGGRRHRRRNLAHPGADPGRELRRVRHRRVQDERPAPGHRPCGRPGAGRHLPGMTVVCGDSHTSTHWCGALAHGIGTSEVEHVLATQCLVAKKMKNMQVRVEGELPLGVSAKDIVLAVIGRIGTAGGTGHALEFAGSAIRGLSMEGRMTLCNMAIEAGARVGMVAVDEKTIDYVKGRPYAPQGADWDKAVAQWRELVSDADAGFDTVVELKAEEIRPQVTWGTSPEMVLPVDERVPDPASESDPVKRDS... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 50894
Sequence Length: 470
Pathway: Amino-acid biosyn... |
Q2VZV4 | MAKLRTLFDKIWDAHLVDVQDDGTCLIYIDRHMVHEVTSPQAFEGLEMSGRKVRHPELTLAVADHNVPTTDRSKGIENEESRIQVETLEANAKKFGVEYLRMDDIRQGVVHIVGPEQGFTLPGTTIVCGDSHTATHGAFGSLAFGIGTSEVEHVLATQTLVQKPAKNMRITVTGKPGPGVTAKDIVLAIIGKIGTAGGTGYVVEFAGEAIRDLSMEGRMTVCNMTIEAGARAGLVAPDEKTFAYIAGKPRSPKGAAFEAAVSYWKTLFTDEGAHFDAEVTLDASTLVPQITWGTSPEDVIAITGTVPNPADIKDEAKRKA... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 49880
Sequence Length: 467
Pathway: Amino-acid biosyn... |
Q0AT09 | MSPETETGATSSVPRSLFDKVWDAHQVRAETAETPGLLYIDLHLVHEVTSPQAFSVLAERGLKVRRPDRTLATIDHATPTLDFAAGETPPYATAAAQNQVETLQSNTAQHGITLHGWGSGHRGVVHVIGPELGATQPGMTIVCGDSHTATHGAFGALAFGIGTTEVGHVLASQCLLQRKPKSMRVTVDGETAAGISAKDIILAIIAEIGVDGGTGCVIEYAGSAIEALDMEGRMTVCNMSIEAGARAGMIAPDETTFAWLEGREQVPTGSEWDAAIDRWRALRSDAGARFDHEVMIDAASIRPMVTWGTAPDTGIAVNAP... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 50379
Sequence Length: 481
Pathway: Amino-acid biosyn... |
Q82JR8 | MGRTLAEKVWDDHVVRRAEGEPDLLFIDLHLLHEVTSPQAFDGLRQAGRPVRRLDLTIATEDHNTPTLDIDKPIADPVSRAQLETLRKNCAEFGVRLHSLGDVEQGVVHVVGPQLGLTQPGTTVVCGDSHTSTHGAFGALAFGIGTSQVEHVLATQTLPLARPKTMAITVDGELPDGVTAKDLILAIIARIGTGGGQGYILEYRGSAIEKLSMEARMTICNMSIEAGARAGMIAPDETTFAYLKGRAHAPEGEEWDAAVAYWKTLKSDEDAEFDAEVVIAAAALSPFVTWGTNPGQGAPLSASVPDPASYEDASERFAAE... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 50346
Sequence Length: 477
Pathway: Amino-acid biosyn... |
Q5M406 | MSGKSIFDKLWDRHVITGDEGQPQLMYVDQHYIHEVTSPQAFQGLRDAGRKVRRPDLTFGTFDHNVPTVNIFDIRDAISKAQIDKLAENVIEFGIDNASHGSDKQGIVHMVGPETGRTQPGKFIVCGDSHTATHGAFGTIAFGIGTSEVEHVFATQTLWQVKPKKMLVEFTGNPQKGIYSKDYILALIAKYGVACGVGYVVEYRGEAIDRLTMEERMTICNMSIEFGSKMGIMNPDQTTYDYMRGRECVPEDFDAAVADWKTLVSDDDAEYDKVIRMDVSELAPMVTWGTNPSMGVDFDTPFPEVRDMNDERAYHYMGLR... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 50911
Sequence Length: 460
Pathway: Amino-acid biosyn... |
A1W1W9 | MQKFIIHKGIACPLEYANIDTDQIIPKQFLLAVSKQGFGKHLFHDLRYLDDKESVLNMDFNLNKKEYQNSSILVSFENFGSGSSREHAPWALVDYGIRAIIAPSFADIFKNNALGNGLLTIELAKDEVLGIVDELKKSQDKNIEISLLEKRVFFKDKIFSFDLDDFHRICLLEGLDNIALTLKHEAQIKAYEKNSKSFLV | Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 22827
Sequence Length: 200
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3... |
Q4FP16 | MQKFNSLTSIPAYLPIVNIDTDMIIPKQFLKTIKRTGLGKNLFFEMRYDDNGNEIKDFILNQKPHNQSKILIAGKNFGCGSSREHAPWALLDFGITCVISSSYADIFYSNCFKNGILPITLPEEKIKELSEYSKRKEEISIDLNEEKIIFGNSEIKFDIDPFKKKCLLEGLDDIALSLAKKEKIITFEENLKNNKPWIFNDKN | Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 23350
Sequence Length: 203
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3... |
B4RCC0 | MEAFTRLDAKAAPLPLANIDTDQIIPKQFLKTVERAGLAKGLFYDLRFDEQGREKPNFVLNRPEYKGAGVLVAGDNFGCGSSREHAPWALMDFGIRCVISTSFADIFYGNCFQNGLLPVVLKAEEVQQLMDEARGGNHVVSVDLEAQTVTSPSGAVFRFEIDPQRKDKMLRGLDAIGETLQSQKDIDVYEMKRALAQPWLEGA | Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 22512
Sequence Length: 203
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3... |
Q321T8 | MVPGPNTLFVLKNSVSSGMKGGYLAACGVFIGDAVLMFLAWAGVATLIKTTPILFNIVRYLGAFYLLYLESKILYATLKGKNNEAKSDEPQYGAIFKRALILSLTNPKAILFYVSFFVQFIDVNAPHTGISFFILATTLELVSFCYLSFLIISGAFVTQYIRTKKKLAKVGNSLIGLMFVGFAARLATLQS | Function: Exporter of leucine.
Catalytic Activity: H(+)(out) + L-leucine(in) = H(+)(in) + L-leucine(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20896
Sequence Length: 191
Subcellular Location: Cell inner membrane
|
P16150 | MATLLLLLGVLVVSPDALGSTTAVQTPTSGEPLVSTSEPLSSKMYTTSITSDPKADSTGDQTSALPPSTSINEGSPLWTSIGASTGSPLPEPTTYQEVSIKMSSVPQETPHATSHPAVPITANSLGSHTVTGGTITTNSPETSSRTSGAPVTTAASSLETSRGTSGPPLTMATVSLETSKGTSGPPVTMATDSLETSTGTTGPPVTMTTGSLEPSSGASGPQVSSVKLSTMMSPTTSTNASTVPFRNPDENSRGMLPVAVLVALLAVIVLVALLLLWRRRQKRRTGALVLSRGGKRNGVVDAWAGPAQVPEEGAVTVTVG... | Function: Predominant cell surface sialoprotein of leukocytes which regulates multiple T-cell functions, including T-cell activation, proliferation, differentiation, trafficking and migration. Positively regulates T-cell trafficking to lymph-nodes via its association with ERM proteins (EZR, RDX and MSN) (By similarity)... |
P15702 | MALHLLLLFGACWVQVASPDSLQRTTMLPSTPHITAPSTSEAQNASPSVSVGSGTVDSKETISPWGQTTIPVSLTPLETTELSSLETSAGASMSTPVPEPTASQEVSSKTSALLPEPSNVASDPPVTAANPVTDGPAANPVTDGTAASTSISKGTSAPPTTVTTSSNETSGPSVATTVSSKTSGPPVTTATGSLGPSSEMHGLPATTATSSVESSSVARGTSVSSRKTSTTSTQDPITTRSPSQESSGMLLVPMLIALVVVLALVALLLLWRQRQKRRTGALTLSGGGKRNGVVDAWAGPARVPDEEATTTSGAGGNKGS... | Function: Predominant cell surface sialoprotein of leukocytes which regulates multiple T-cell functions, including T-cell activation, proliferation, differentiation, trafficking and migration. Positively regulates T-cell trafficking to lymph-nodes via its association with ERM proteins (EZR, RDX and MSN) . Negatively re... |
P13838 | WAQVVSQENLPNTMTMLPFTPNSESPSTSEALSTYSSIATVPVTEDPKESISPWGQTTAPASSIPLGTPELSSFFFTSAGASGNTPVPELTTSQEVSTEASLVLFPKSSGVASDPPVTITNPATSSAVASTSLETFKGTSAPPVTVTSSTMTSGPFVATTVSSETSGPPVTMATGSLGPSKETHGLSATIATSSGESSSVAGGTPVFSTKISTTSTPNPITTVPPRPGSSGMLLVSMLIALTVVLVLVALLLLWRQRQKRRTGALTLSRGGKRNGTVDAWAGPARVPDEEATTASGSGGNKSSGAPETDGSGQRPTLTTF... | Function: Predominant cell surface sialoprotein of leukocytes which regulates multiple T-cell functions, including T-cell activation, proliferation, differentiation, trafficking and migration. Positively regulates T-cell trafficking to lymph-nodes via its association with ERM proteins (EZR, RDX and MSN). Negatively reg... |
P08638 | MEGRSDFVATSQSGSEMSHSETRNRTGMNARKRKFACVECRQQKSKCDAHERAPEPCTKCAKKNVPCILKRDFRRTYKRARNEAIEKRFKELTRTLTNLTSDEILKKIEEEQEIVLDNSNFTKEKVKQLRKSAFETTEIEPRSYKTLRGEPISYSTNRRHTDSSPLTLLSSSTNFDPVHSTNVMTDDQLKCLPKSLGDVYLSSSDIAELFQEFATKYHQFLPVVDLSKGAERIYHLSPCLFWVILLIGLRRKFGATDLMTRLSVLVKSVLSEITISPIIRYTPSDKDEPVLNVASVYSVQAFLLYTFWPPLTSSLSADTS... | Function: Factor for control of RNA levels of a group of leucine-specific genes.
Sequence Mass (Da): 100153
Sequence Length: 886
Domain: the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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A8MZ59 | MFEGPRRYRRPRTRFLSKQLTALRELLEKTMHPSLATMGKLASKLQLDLSVVKIWFKNQRAKWKRQQRQQMQTRPSLGPANQTTSVKKEETPSAITTANIRPVSPGISDANDHDLREPSGIKNPGGASASARVSSWDSQSYDIEQICLGASNPPWASTLFEIDEFVKIYDLPGEDDTSSLNQYLFPVCLEYDQLQSSV | Function: Paired-like homeobox transcription factor involved in embryogenesis . May act as a regulator of embryo genome activation . Binds to a 36 bp DNA elements containing a 5'-TAATCC-3' sequence motif, referred to as EEA motif (EGA-enriched Alu-motif), present in the promoters of target genes activated in early embr... |
Q314F2 | MGRNREDDITPLQQETLDEICRYVSAKGYPPTVKEMSETFGISHASVHDRINQLVRKGYLKREEGKARGLTVTKHPQTNAVALVAVPIVGTVAAGHPIFAHENITGEVLVEASVVGSGKCFALYTQGDSMIDAGINDGDLIIVRRQPIAEDGDIVIALLDDEATVKRLKIDNELIELVPENPRLKPIRVKPEDELRILGKVVGRKRI | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
B1ZZZ4 | MLTEKQEAILDYIRSVQAQRGVPPSTREIQRHFGYESQNAAMNHLRALARKGQLHQVDGATWGLKVSEVQGHFELPIYGTIPAGVPSMQEQQPKETITFDPAVFRLRRPERLWGLEVHGDSMIDAHILDGDIAVLERREAKPGDIVAALVDETTTTLKRLAYVKGKPVLKPENARYALIVPKDRLEIQGVFVGLIGRAKR | Function: Binds a consensus sequence 5'-TGTTC-N(4)-GAACA-3'; some genes have a tandem consensus sequence and their binding is cooperative . Binds to the promoters of a number of genes, including lexA and splB . Represses a number of genes involved in the response to DNA damage (SOS response).
Catalytic Activity: Hydrol... |
A1R556 | MAAKATGGGAPLRSQQPQKSPKSLTVRQKKILETIQRSVNDNGYPPSMREIGDTVGLASLSSVTHQLSQLEKLGYLRRDPKRPRAMEVLMPLTLDGGAIPGVEAPTTLRSAGGLAVTELASASDTAMVPLVGRIAAGGPILADQTVEDVLALPRQLVGHGELFMLKVAGDSMIDAAICDGDWVVVRRQNDAINGDIVAALLDDEATVKTFRQRDGHTWLLPQNTQYEPILGDQATIMGKVVSVLRSL | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
A1B3Z0 | MLTRKQIQLLEFIQARMARDGVPPSFDEMKLALDLRSKSGIHRLVTALEERGFIRRLPHRARALEIVRLPESLSKGPGFQPRVIEGTMPDRPAPLPRGAMEVSVSAIELPVMGRIAAGVPIEAISEISHHIAVPTTMLSGQDRHYALEVRGDSMIEAGINDGDVVVIREQNAAESGDIVVALVDGYEATLKRYRRKGNMIALEAANPAYETRVLPEDKVRIQGRLVGLIRSY | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
Q6D9I5 | MKVLTARQQQVYDLIRDHIAHSGMPPTRAEIAQQLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLMEEETGIPLVGRVAAGEPLLAQEHIECRYQVDPAMFKPSADFLLRVSGMSMKNIGIMDGDLLAVHKTEDVRNGQIVVARIDDEVTVKRLKKQGNTVHLLAENEEFAPIVVDLRQQSFSIEGLAVGVIRNSDWS | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
A9BGA3 | MEELTKRQSQVLDFIKSYMEKNGFAPSIRDIMKHFNFKSPRAAHKHLIILEKKGYIERKNVSRGIKMMPKSGEIFATETLAPVSGKIAAGDAIEAIQTISDYIPIPTNFFPKNYEYFSLRVEGNSMIEAQIKSGDFVLIRKQDYAMDGDIVVALIDGNDATLKRYKRLNEDEVLLIPENKSMKEIKVKADHLKIQGKMVGLIRVL | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
Q9PNI5 | MKSSNLYSKLLNAPKNAPVFLSQNLEADFIVKAYTFGLFPWTSKPVTWWCPDPRCILIPNQIHIQKNMKKFINLYQIKLDYDFLKLITLCRDTRSQSWIDDEFITTYYKLFTQGYAHSLELYENNELIGGIYGLILGKVFFGESMVSIKKNASKVAMIKLCDLLKPYDFIIDCQVYNQHLEFMGAHNISRKEFLNILKEKCNQESGFKNFKDLIT | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
B9KCU7 | MQKSNLYSKLLKSPDDAPVFISEKLELDFISHAYSLGLFPWTSNPVTWWCPSPRMVLFPDEIHIQKSIKKALKTYEIRLDYDFALLIKHCSLRKKTWINQEFIETYTKLFEQNLAHSVEVYENDEFIGGLYGLIIGKVFFGESMISLKKDASKIALIKLCEILKPYDFLIDCQVPNEHLKFMGAKEMIKKDFLKILEKKVSLESGFENFQNLL | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
A4WSI3 | MTPPALTPRLLLRAYALGIFPMAESRDDPEIHWVDPRRRGIFPLDGFHISRSLARRIRRMDWTVTVNEDFAGTVRACADRDDTWINPTIFRLYVGLHALGHAHSLEVREGDALVGGVYGVTLGRAFFGESMFSRRTDASKVALAFLIDRLRAGGFTLFDTQFLTPHLASLGAIEIPRADYHRRLGEALAGKAEFAPPGYSPDPASVVQRSSQTS | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
Q8KFI0 | MIKVEDILRAYRHGFFPMADSREGTVSWCQPYQRAVVPLDSFRPSRSLRRVIGKKRFTIKINSVFEQVIRACSQPRSTGQETWLSEEIIKVFLKLHRLGVAHSVESWQDGELAGGLYGLSMGGAFFGESMFFFRSDASKVAFAWLVGYLKRKGYLLLDAQIMNPHLESLGAIEIPHEEYMVQLERALGKKISFV | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
Q3IH36 | MKKQLYQLSNTDIAFPPIECALDSPDGLLAIGGDLSLARLSNAYNNGIFPWFSEDEPIMWWSPSERGIVELDNFHISKSLRKHLKKHPVTVTINNAFIEVIEACCEQRIDTDGTWITSDMLTAYINAHNAGIAHSVEVWREGELAGGLYGIMQNGVFCGESMFHHQTNCSKLAMWALVNWLKRHNAHFIDCQLENPYLMSLGATVIPRPAFLAKLHAAQNYKVDPAMWIPQELNAIYE | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
Q4FUQ3 | MNNINDSSAIHITPETFVKQIRSLGRYNFPEPALVDPDGIGIVGIGGNLAPETLISAYAQGLFPWFNDDEPIAWWCPEPRCVMQPTDYQPSKSLRKQANNARWQLTLNQAFNEVIHACSLPRSNGLPEGEHTWIHDDMIEAYNELHAQGFAHSVEVWDDQGQLVGGLYGLKIGSIYFGESMFHIASNASKLAFWGLMRLCTQSNVTLVDCQLPNEHLMSLGAITLSRTEFLTQLDTLISNGSDAWHKNSHRPLAVSLLGNLQPWQLNP | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
A1SWY4 | MTLYIPELPINNTIFPDTSLALSDPDGLLAMGGDLSPQRIIKAYQQGIFPWFSDGQPILWWSPSQRAIIQPNLVHISSSMKKIISKNNFSLSINHAFHDVIDACAAPRGNQNETWITFDMIAAYQKLHQQGIAHSIEVWRDNKLVGGLYGVCIGSVFCGESMFSKEDNTSKIAFIALCQHFDKFKGQLIDCQILTKHLQSFGVQNESRDNFINYLNQYKNININKKCWDKQTIFIKNR | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
Q92QK2 | MKETRSKQPDITPDMLLRAYSIGLFPMADSADDPELFWVEPEIRGIIPLDRFHVSRSLAKAIRRRPFDIRFDTAFAEVMEGCAQPAPDRPTTWINDTIRSLYAALHNMGHAHSVEAWEGDALVGGLYGVSLGAAFFGESMFSRRTGASKICLVHLVERLRSKGFQLLDTQFTTEHLKSFGAVDVPKAQYEVLLAKAIASPNLEF | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
A5V9E5 | MKAIDPDLLLRAYSIGVFPMADSRAADDVYWVEPKKRGILPLDHFRLSRSLAKTIRSDRFAVTADRAFGEVVAECAAVTSQRPDTWINPAIEAAYADLHRRGHAHSIECWREGRLVGGLYGVRLGGAFFGESMFSRESNASKVALAWLVARLRAGGFRLLDCQFITDHLQSLGAIEVSRDDYVALLDVALGVVAGAGAAGGVAVAGAAAGWSAPDFFALDGGATDPDTRTVSGPISGCTIVQLLGQTS | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
Q6N734 | MASRDSSAASEITPDVLLRAYACGIFPMAESVDDPSLFWVEPDLRGIIPLGGFRVSSRLARTVRSDAFTVTVNRDFKAVIDGCAAPQPGRDDTWINRRIRELYIGLHDIGRCHSVEVWQDGDLAGGLYGVSLGRAFFGESMFHRARDASKVALVHLVARLLAGGYTLLDTQFVTDHLKSFGAIEVPRLRYRSLLDDALEGEASFAALPLDRPVTGTEALAIITRT | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L... |
B3VI55 | MPIATSTGDNVLDFTVLGLNSGTSMDGIDCALCHFYQKTPDAPMEFELLEYGEVPLAQPIKQRVMRMILEDTTSPSELSEVNVILGEHFADAVRQFAAERNVDLSTIDAIASHGQTIWLLSMPEEGQVKSALTMAEGAILASRTGITSITDFRISDQAAGRQGAPLIAFFDALLLHHPTKLRACQNIGGIANVCFIPPDVDGRRTDEYYDFDTGPGNVFIDAVVRHFTNGEQEYDKDGAMGKRGKVDQELVDDFLKMPYFQLDPPKTTGREVFRDTLAHDLIRRAEAKGLSPDDIVATTTRITAQAIVDHYRRYAPSQEI... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Levoglucosan kinase that catalyzes the transfer of a phosphate group from ATP to levoglucosan (1,6-anhydro-beta-D-glucopyranose, LG) to yield glucose 6-phosphate in the presence of magnesium ion and ATP . In addition to the canonical kinase phosphotransfer reaction, ... |
Q03077 | MIILVLLISYSFGKTQDGKDQLSPNYPYGKMNKDVNFNKPFTSAVDSYQIQQYAENGVFSANQENYVRAKCKTCCRVIFASDYNYKTNTQFTDEDDKKGDERYVMDMEFDDKRSVRFRNGGYEQNILLRPLKQGNELQFFEFAPYRMYTSYAIPKRVHDIRGGANEGATLIIWPKNPPLSDAPGTRNQRFVYVHPYPTEWYPEYNSTTKYTQNGKTVIKTLKWPTYKRHFYLPYRLDVDLCYQARKATDGRSTWTGNKNLNTTSKSYQIIASRCSATEARQIFIPVFA | Function: Light subunit of a heterodimeric lectin; the heavy subunit binds galactose and N-acetyl-D-galactosamine of host glycoproteins and thus mediates adhesion to host cells.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33595
Sequence Length: 288
Subcellular Location: Cell membrane
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Q95M12 | MIWEFTVLLSLVLGTGAVPLEDPEDGGKHWVVIVAGSNGWYNYRHQADACHAYQIVHRNGIPDEQIIVMMYDDIANSEDNPTPGIVINRPNGSDVYQGVLKDYTGEDVTPKNFLAVLRGDAEAVKGVGSGKVLKSGPRDHVFVYFTDHGATGILVFPNEDLHVKDLNETIRYMYEHKMYQKMVFYIEACESGSMMNHLPPDINVYATTAANPRESSYACYYDEQRSTFLGDWYSVNWMEDSDVEDLTKETLHKQYQLVKSHTNTSHVMQYGNKSISAMKLMQFQGLKHQASSPISLPAVSRLDLTPSPEVPLSIMKRKLM... | Function: Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. Required for normal degradation of internalized EGFR. Plays a role in the regulation of cell proliferation via its role in EGFR degradation (By similarity). Required for nor... |
Q99538 | MVWKVAVFLSVALGIGAVPIDDPEDGGKHWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIVVMMYDDIAYSEDNPTPGIVINRPNGTDVYQGVPKDYTGEDVTPQNFLAVLRGDAEAVKGIGSGKVLKSGPQDHVFIYFTDHGSTGILVFPNEDLHVKDLNETIHYMYKHKMYRKMVFYIEACESGSMMNHLPDNINVYATTAANPRESSYACYYDEKRSTYLGDWYSVNWMEDSDVEDLTKETLHKQYHLVKSHTNTSHVMQYGNKTISTMKVMQFQGMKRKASSPVPLPPVTHLDLTPSPDVPLTIMKRKLM... | Function: Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. Required for normal lysosomal protein degradation in renal proximal tubules. Required for normal degradation of internalized EGFR. Plays a role in the regulation of cell pro... |
O89017 | MTWRVAVLLSLVLGAGAVPVGVDDPEDGGKHWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIIVMMYDDIANSEENPTPGVVINRPNGTDVYKGVLKDYTGEDVTPENFLAVLRGDAEAVKGKGSGKVLKSGPRDHVFIYFTDHGATGILVFPNDDLHVKDLNKTIRYMYEHKMYQKMVFYIEACESGSMMNHLPDDINVYATTAANPKESSYACYYDEERGTYLGDWYSVNWMEDSDVEDLTKETLHKQYHLVKSHTNTSHVMQYGNKSISTMKVMQFQGMKHRASSPISLPPVTHLDLTPSPDVPLTILKRK... | Function: Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system. Required for normal lysosomal protein degradation in r... |
P39400 | MSTMNVLICQQPKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIADLKNGQQVAVIPYVACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANILPADGIDPQAAALIEPFAISAHAVRRAAIAPGEQVLVVGAGPIGLGAAAIAKADGAQVVVADTSPARREHVATRLELPLLDPSAEDFDAQLRAQFGGSLAQKVIDATGNQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKITADMMLTHRYPFATLA... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the oxidation of L-galactonate to D-tagaturonate. Required for growth on L-galactonate as the sole carbon source. In vitro, can also use L-gulonate.
Catalytic Activity: L-galactonate + NAD(+) = H(+) + keto-D-tagaturonate + NADH
Sequence Mass (Da): 36448
Seq... |
P39398 | MEKENITIDPRSSFTPSSSADIPVPPDGLVQRSTRIKRIQTTAMLLLFFAAVINYLDRSSLSVANLTIREELGLSATEIGALLSVFSLAYGIAQLPCGPLLDRKGPRLMLGLGMFFWSLFQAMSGMVHNFTQFVLVRIGMGIGEAPMNPCGVKVINDWFNIKERGRPMGFFNAASTIGVAVSPPILAAMMLVMGWRGMFITIGVLGIFLAIGWYMLYRNREHVELTAVEQAYLNAGSVNARRDPLSFAEWRSLFRNRTMWGMMLGFSGINYTAWLYLAWLPGYLQTAYNLDLKSTGLMAAIPFLFGAAGMLVNGYVTDWL... | Function: Probably responsible for the transport of L-galactonate from the periplasm across the inner membrane. Is essential for growth on L-galactonate as the sole carbon source.
Catalytic Activity: H(+)(in) + L-galactonate(in) = H(+)(out) + L-galactonate(out)
Location Topology: Multi-pass membrane protein
Sequence Ma... |
Q8L3C7 | MTTDTARRHTGAERANEMTYEQLARELLLVGPAPTNEDLKLRYLDVLIDNGLNPPGPPKRILIVGAGIAGLVAGDLLTRAGHDVTILEANANRVGGRIKTFHAKKGEPSPFADPAQYAEAGAMRLPSFHPLTLALIDKLGLKRRLFFNVDIDPQTGNQDAPVPPVFYKSFKDGKTWTNGAPSPEFKEPDKRNHTWIRTNREQVRRAQYATDPSSINEGFHLTGCETRLTVSDMVNQALEPVRDYYSVKQDDGTRVNKPFKEWLAGWADVVRDFDGYSMGRFLREYAEFSDEAVEAIGTIENMTSRLHLAFFHSFLGRSDI... | Function: Catalyzes the oxidative deamination of L-glutamate to 2-ketoglutarate along with the production of ammonia and hydrogen peroxide . Shows strict substrate specificity for L-glutamate, and exhibits only very weak activity with L-aspartate (Ref.2).
PTM: The precursor form is proteolytically cleaved by an endopep... |
D6A5I3 | MTEDHAVVRSDGGLSRRSFAAVAGTATVATALTSGVAAALPAPAASGDSRGADFDRCLAVARALLVLDSDDRPLVPRYQSVLQKGLPAQRRTRPKNVLVIGAGPAGLVAAWLLKRAGHRVTVLEANGNRAGGRVKTFRSGGHERAEQPFADPRQYAEAGAMRIPGSHPLVMELIDQFELKKRRFHYVDVDSEGRPANRTWIHVNGIRVRRADYARAPRRVNRSFGVPRAHWDTPAAAILRSVLDPVRDEFSRVGRDGKRVDKPLPERLQGWARVVQRFGDWSMFRFLTEHAGLDERTIDLIGTLENLTSRLPLSFIHSFI... | Function: Catalyzes the oxidative deamination of L-glutamate to 2-ketoglutarate along with the production of ammonia and hydrogen peroxide.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Catalytic Activity: H2O + L-glutamate + O2 = 2-oxog... |
E7FE13 | MALLAVRMLVLGLCVGGQAAAAGEGQSTPATCSPLCRCDEDGGADCSGRGLTSVPTGLSAFTYYLDISMNNITELPANVFRNLPYLEELRLAGNDLAFIHPEALSGLHQLKVLMLQNNQLKTVPSAALKNLNALQSLRLDANHITSVPEDSFEGLQQLRHLWLDDNSLTEVPISPLQHQSNLQALTLALNRITHIPDNAFANLSSLVVLHLHNNRIQEIGKNCFNGLDNLETLDLNFNNLKIFPEAIQMLPKLKELGFHSNNIASIPEGAFCRNSLLRTIHLFDNPLSFVGTTAFQNLSDLHSLMLRGASMMQDFPSLTG... | Function: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and is involved in the formation of various organs. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering t... |
A2ARI4 | MPGPLRLLCFFALGLLGSAGPSGAAPPLCAAPCSCDGDRRVDCSGKGLTAVPEGLSAFTQALDISMNNITQLPEDAFKNFPFLEELQLAGNDLSFIHPKALSGLKELKVLTLQNNQLKTVPSEAIRGLSALQSLRLDANHITSVPEDSFEGLVQLRHLWLDDNILTEVPVRPLSNLPTLQALTLALNNISSIPDFAFTNLSSLVVLHLHNNKIKSLSQHCFDGLDNLETLDLNYNNLDEFPQAIKALPSLKELGFHSNSISVIPDGAFAGNPLLRTIHLYDNPLSFVGNSAFHNLSDLHSLVIRGASLVQWFPNLAGTVH... | Function: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and is involved in the formation of various organs. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering t... |
Q9FDM1 | MPFAFIEQMKSVIHFDALGLSPIAFDLGVWHLFGLTLHPLIHWYALAYITGILLAWRYVLFLLKQPGTPMKPEQTDDLVFWSTLGILVGGRLAYVLFYQPAILENPLEIFKLWEGGMSYHGGMIGVFLAIWWVKTTNHLSWLRIADYIGCAAPIGLFLGRLANFVNGELWGRPSTMPWAVIFPQAGALPRHPSQLYEAGLEGILLFAFLNYQFFATKARLHPGKLAGFFLVGYGLSRFIVEWFREPDVQLGTLSWGLTMGQTLTIPMVIAGLWLIITSKKREISL | Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+... |
Q8W593 | MVRIIPMAASSIRPSLACFSDSPRFPISLLSRNLSRTLHVPQSQLFGLTSHKLLRRSVNCLGVAESGKAAQATTQDDLLTWVKNDKRRMLHVVYRVGDMDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYGPEDSHFVIELTYNYGVDKYDIGAGFGHFGIAVDDVAKTVELVKAKGGKVSREPGPVKGGKTVIAFIEDPDGYKFELLERGPTPEPLCQVMLRVGDLDRAIKFYEKAFGMELLRTRDNPEYKYTIAMMGYGPEDKFPVLELTYNYGVTEYDKGNAYAQIAIGTDDVYKTAEAIKLFGGKITREPGPLP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Sequence Mass (Da): 39167
Sequence Length: 350
Pathway: Secondary metabolite metabol... |
Q8H0V3 | MASEARESPANNPGLSTNRDEATKGYIMQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFSEMKFSLYFLGYEDTTTAPTDPTERTVWTFGQPATIELTHNWGTESDPEFKGYHNGNSEPRGFGHIGVTVDDVHKACERFEELGVEFAKKPNDGKMKNIAFIKDPDGYWIEIFDLKTIGTTTVNAA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Sequence Mass (Da): 20848
Sequence Length: 185
Pathway: Secondary metabolite metabol... |
P0AC82 | MRLLHTMLRVGDLQRSIDFYTKVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEACEKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEKDAGRGLGN | Cofactor: Binds 1 nickel ion per subunit. In the homodimer, two nickel ions are bound between subunits.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Sequence Mass (Da): ... |
P44638 | MQILHTMLRVGDLDRSIKFYQDVLGMRLLRTSENPEYKYTLAFLGYEDGESAAEIELTYNWGVDKYEHGTAYGHIAIGVDDIYATCEAVRASGGNVTREAGPVKGGSTVIAFVEDPDGYKIEFIENKSTKSGLGN | Cofactor: Binds 1 nickel ion per subunit. In the homodimer, two nickel ions are bound between subunits.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Sequence Mass (Da): ... |
Q04760 | MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM | Cofactor: Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are bound between subunits.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione . Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B . Required for no... |
P0A0T2 | MRLLHTMLRVGNLEKSLDFYQNVLGMKLLRRKDYPEGRFTLAFVGYGDETDSTVLELTHNWDTERYDLGNAYGHIAVEVDDAYEACERVKRQGGNVVREAGPMKHGTTVIAFVEDPDGYKIEFIQKKSGDDSVAYQTA | Cofactor: Binds 1 nickel ion per subunit.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Sequence Mass (Da): 15669
Sequence Length: 138
Pathway: Secondary metabolite metab... |
Q948T6 | MASGSEAEKSPEVVLEWPKKDKKRLLHAVYRVGDLDRTIKCYTECFGMKLLRKRDVPEEKYTNAFLGFGPEDTNFALELTYNYGVDKYDIGAGFGHFAIATEDVYKLAEKIKSSCCCKITREPGPVKGGSTVIAFAQDPDGYMFELIQRGPTPEPLCQVMLRVGDLDRSIKFYEKALGMKLLRKKDVPDYKYTIAMLGYADEDKTTVIELTYNYGVTEYTKGNAYAQVAIGTEDVYKSAEAVELVTKELGGKILRQPGPLPGLNTKIASFLDPDGWKVVLVDNADFLKELQ | Cofactor: Binds 1 nickel ion per subunit.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione (By similarity). Involved in the detoxifiation of methylglyoxal. Can functionally complement growth defect of a yeast mutant lacking GLY I. Involved in abioti... |
P84719 | ITACLDPDGWKEPGPLPGISTK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Sequence Mass (Da): 2296
Sequence Length: 22
Pathway: Secondary metabolite metabolis... |
Q9HU72 | MSFNTEVQPGICMEPDAITQEYVFNHTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFLAMTRGEEVPDAVDERQRYTFGRQSVLELTHNWGSESDDSQYHNGNQDPRGFGHICFSVPDLVAACERFETLGVNFVKPLDRGMKNVAFISDPDGYWVEIVQASLNGEMGRG | Cofactor: Binds 1 nickel or zinc ion per subunit.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Sequence Mass (Da): 20215
Sequence Length: 176
Pathway: Secondary metaboli... |
P16635 | MSLNDLNTLPGVTAQADPATAQFVFNHTMLRVKDIEKSLDFYTRVLGFKLVDKRDFVEAKFSLYFLALVDPATIPADDDARHQWMKSIPGVLELTHNHGTERDADFAYHHGNTDPRGFGHICVSVPDVVAACERFEALQVPFQKRLSDGRMNHLAFIKDPDGYWVEVIQPTPL | Cofactor: Binds 1 nickel or zinc ion per subunit.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Sequence Mass (Da): 19540
Sequence Length: 173
Pathway: Secondary metaboli... |
P0A1Q3 | MRLLHTMLRVGDLQRSIAFYTNVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVESYDMGNAYGHIALSVDNAAEACERIRQNGGNVTREAGPVKGGSTIIAFVEDPDGYKIELIEAKDAGRGLGN | Cofactor: Binds 1 nickel ion per subunit. In the homodimer, two nickel ions are bound between subunits.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
Sequence Mass (Da): ... |
Q810M6 | MAGRGGTGAAEYGEEGEEEEEEEAREGGAEGSPGSKLPPIVGTASELAKRKVKKKKKKKKTKGSGKGDADKHHSRGRKNQPLSSSFHDILNPHKDHGLRAEPRDKEENRQTLPYSYSINHPCFAEIEDTLSSQINESLRWDGILTDPEAEKERIRIYKLNRRKRYRLMALKCFHSDPCVEESVENLPYLSDKDCSPCSKQPSSKGDHAHSYFEASKLLHPELATTVAE | Function: Participates in nucleolar liquid-liquid phase separation (LLPS) through its N-terminal intrinsically disordered region (IDR) . May be involved in ATE1-mediated N-terminal arginylation .
PTM: Post-translationally modified by JMJD6 lysyl-hydroxylase activity at its Lys-rich domain, which inhibits its self-assoc... |
Q03974 | MSAIENIVISMENATERRKHITKQFESKKLSFSFFNAYTYQSINQSINQSINQSINQSINQSINQSINQSNSILHNIEESRILTKGEKGCLISHFLLWNKCVNENFEYLKIFEDDVILGENAEVFLNQNEWLKTRFDFNDIFIIRLETFLQPVKLEKQTKIPPFNSRNFDILKSTHWGTAGYIISQGAAKYVIEYLKNIPSDEIVAVDELIFNKLVDVDNYIVYQLNPAICIQELQANQSKSVLTSGLEKERQKRSKIRKKKTLKQRLTRIKENIIRALNRKKWKEQQRIKEMQGKEIVRFM | Function: Involved in extracellular lipooligosaccharide (LOS) biosynthesis and virulence expression. Involved in the synthesis of the oligosaccharide moiety of the LOS molecule by adding GalNAc.
Sequence Mass (Da): 35490
Sequence Length: 302
Domain: Between 2 and 7 copies of the SINQ repeats are to be found in differen... |
P46320 | MTKGLKIVTIGGGSSYTPELVEGFIKRYDELPVRELWLVDIPEGEEKLNIVGTLAKRMVEKAGVPIDIHLTLDRRKALKDADFVTTQFRVGLLQARAKDERIPLKYGVIGQETNGPGGLFKGLRTIPVILEIAKDIEELCPNAWLVNFTNPAGMVTEALLRYSNLKKVVGLCNVPIGIKMGVAKALDVDVDRVEVQFAGLNHMVFGLDVFLDGVSVKEQVIEAMGDPKNAMTMKNISGAEWEPDFLKALNVIPCGYHRYYFKTKEMLEHELEASQTEGTRAEVVQKVEKELFELYKDPNLAIKPPQLEKRGGAYYSDAAC... | Function: Hydrolyzes phospho-beta-glucosides.
Catalytic Activity: 6-phospho-beta-D-glucosyl-(1->4)-D-glucose + H2O = D-glucose + D-glucose 6-phosphate
Sequence Mass (Da): 48711
Sequence Length: 442
EC: 3.2.1.86
|
J3SDX8 | MWRLIIIAILFQGLVNSAMLERRKRGVDPETAMNISEIILFRGYPSEEYEVVTGDGYILCLNRIPYGKISQKTKEPKPAVFLQHGLLADGSNWVTNLDYNSLGFALADAGFDVWLGNSRGNTWSQKHINYTIKQKEFWMFSFNEMAMYDIPASVNFVLNKTGQEQLFYVGHSQGTTIGFIAFSVLPELAKKIKMFFGLAPVMTVKFSSGGLVKLGELPEFLLKEIFGTKQIFPQNAVIKWLATHVCGQVLIDELCGNFFFLLCGFNEKNLNMSRVEIYSTHCPAGTSVQNMLHWSQAVKSGEVRAFDWGSRKENMAHYKQ... | Function: In physiological conditions, is crucial for intracellular hydrolysis of cholesteryl esters and triglycerides that have been internalized via receptor-mediated endocytosis of lipoprotein particles. In venom, the biological contribution is unknown.
Catalytic Activity: a sterol ester + H2O = a fatty acid + a ste... |
Q6DB58 | MWLRNSVFLIIIVVGGIGGFPAVAAVCPDWDNTRASKEIDALRQQLEQWDDVYYTEGKSPIEDDVYDQLREQLNQWSQCFQPQNVIPARLPDNGKQPHPVAHTGLKKLSDRVQLVQWIVQREDLWVQPKVDGVAVTLVYQHGKLVSAVSRGNGLQGEDWTEKARLIPDIPHLLSGAPSSFVLQGELFLKMTDHRQYAQGGVNARSIVAGEMRRHQPSPVLSQIGLFVWEWPDGPKAMPERLDKLKEMGFAMTADYTHAIESFADVEKWRDHWYHSPLPFVTDGVVIRQTKEPQGRYWRNTSADWAIAWKYPPVHQVAEVV... | Function: Catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction.
Catalytic Activity: NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n... |
Q7N9N4 | MLNLLILILFIVFSSPIVAAEIFVSNTEKNCPEWSQDKLQRETNSLMQQMAHWDQLYRQKGISEIDDEVYDQLMSELTHWQFCLKQAPHSDFPVEVFPDNKLVHPVAHTGLSKLKDKQEINRWLHGRLPVWLQPKIDGVAVTLVYQNGKLVSLISRGNGAEGVNWTAKSRYIPDIPQNIENAPPDLVLQGELFLHKEEHRQQLLGSDGARNRVAGLMMRKDHSSELKQIGLFIWSWPDGPAEMESKLRKLADMGFPLALRYSHKIEEPEQVQKLRMHYFEQPMLFATDGIVLKQEIEPKGNQWRSGSNSWAVAWKHPLRH... | Function: Catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction.
Catalytic Activity: NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n... |
Q2Q1W2 | MASFPETDFQICLLCKEMCGSPAPLSSNSSASSSSSQTSTSSGGGGGGPGAAARRLHVLPCLHAFCRPCLEAHRLPAAGGGAAGEPLKLRCPVCDQKVVLAEAAGMDALPSSAFLLSNLLDAVVATADEPPPKNGRAGAPAGAGGHSNHRHHAHHAHPRASASAPPLPQAPQPPAPSRSAPGGPAASPSALLLRRPHGCSSCDEGNAASSRCLDCQEHLCDNCVRAHQRVRLTKDHYIERGPPGPGAAAAAQQLGLGPPFPGPPFSILSVFPERLGFCQHHDDEVLHLYCDTCSVPICRECTMGRHGGHSFIYLQEALQD... | Function: E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance (Probable). Binds to miRNAs and associates with AGO2, participating in post-transcriptional repression of transcripts such as CDKN1A (By similarity). In addition, p... |
Q1PSW8 | MASFPETDFQICLLCKEMCGSPAPLSSNSSASSSSSQTSTSSAGGGGPGAAARRLHVLPCLHAFCRPCLEAHRLPAPGGAGPAEALKLRCPVCDQKVVLAEAAGMDALPSSAFLLSNLLDAVVATAEEPPPKNGRAGGGPGGAGGHSNHRHHAHHPAQRAAAPAPQPPPGPAASPGSLLMRRPHGCSSCDEGNAASSRCLDCQEHLCDNCVRAHQRVRLTKDHYIERGPPGPAAASAAQQLGLGPPFAGAPFSILSVFPERLGFCQHHDDEVLHLYCDTCSVPICRECTLGRHGGHSFAYLQDALQDSRALTIQLLADAQ... | Function: E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance . Binds to miRNAs and associates with AGO2, participating in post-transcriptional repression of transcripts such as CDKN1A. Facilitates the G1-S transition to promo... |
Q27886 | MRAAPFDFFFQSTALSTFFILCSLATNEIPTISGAPAGKIVQPPKPNILKQGCPSDLLHSRALRSIQLACRTHPATVISAFEGVQEGLQNCANRLRFQQWDCSEAGNIMHDPPLLRQGFRESSLIWALSSASAAWGVATACAQGWIDDCACNNQMGQNEYEFGGCTHGVQHGITASRKLLTKVGAVNTLLRKVEKHNLKAGRLAIKKTLISSCKCHGVSGSCQQKTCWKRTATLEHITDYLVEKYARAKLYTDDSVVKTTDLIYLEASPDVCKAKSVAGRVCAWRNETHTQGDCDRLCCGNGFSIRHEVVRVKCDCEFVW... | Function: Ligand for members of the frizzled family of seven transmembrane receptors (By similarity). Affects male tail development, vulval precursor cell specification and egg laying. Involved in morphogenesis by influencing polarity of asymmetric cell divisions of the B, U, and F cells in the male, and the T cell in ... |
Q95QD7 | MNQGEIVYQDDDDYYDESEIYDNYEEGAEFIEVNGQLVPHNPNLQAQQNRPGTSSMIQQHNRSMEVNQGLVKDEPIDTSSHRVYVPPPRPVQRKLFQPGPSTPGSSQYTVRNLSNLSGSPSMYDRQPASLPRTVQPMGLEMGNSEQRKVYIDMKDHVSHIRLKTKKKVFAPGQRKPCNCTKSQCLKLYCDCFANGEFCRDCNCKDCHNNIEYDSQRSKAIRQSLERNPNAFKPKIGIARGGITDIERLHQKGCHCKKSGCLKNYCECYEAKVPCTDRCKCKGCQNTETYRMTRYKNSGGAVSNTNALMSLTNASSTATPD... | Function: Synthetic multivulva class B (synMuvB) protein. SynMuvB proteins are required to repress the induction of vulval development by Ras signaling and probably act by forming the multiprotein DRM complex that repress transcription.
Sequence Mass (Da): 49109
Sequence Length: 435
Domain: The CRC domain mediates DNA-... |
Q0BSW6 | MVTRVLIDHRQGGRHEAGVRHPEKQHRPDNPSQPKPSWIRVKAPNHPVYHQTQALMRENRLTTVCEEAACPNIGECWSQRHATMMIMGDTCTRACSFCNVKTGLPHALDGDEPARVADAVARLGLRHVVITSVDRDDLNDGGAAHIAAVIKAVRLAAPETTIEVLTPDFLRKPGAAETVAEARPDVFNHNLETVPRLYPAIRPGARYFQSLRLLDQVKRLDPSIFTKSGLMVGLGEDRAEIAQVMDDLRIAEVDFITLGQYLQPTPKHAAVDRFVTPDEFSDYASMARSKGFLMVSSSPLTRSSYHADADFAALRAARME... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
B9LR22 | MQRGRRKPDWLKSRPPSGSRFTEIKERLRERDLHTVCEEANCPNMGECWSGRDGPGTATFMLMGDRCSRGCNFCDVETGGMKSLDSDEPENVADAVAEIGLDYVVLTSVDRDDLADGGSEHFAETIREIQRRDPEILVETLIPDFQGDPEAIDRIIDAGPDVIAHNVETVERLQWPVRDRRADYEQSLAVLDRVGRESDIHTKTSLMLGVGEYDHEVYRTLGDLSEVGVDVVTFGQYLQPSRSHLDVFEYVHPDVFETWRAVAEREFDFLYCASGPMVRSSYKAGELFVEALLREGRSPEDARRHARAAGGD | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
Q31F42 | MKARNESMSKGEYKTKSLKNRPDPTQPKLKKPSWIKAKLPSAKHIGRVKELKQVLREQGLNSVCEEASCPNLGECFGHGTATFMIMGHICTRKCPFCDVTHGRPNPLNQDEPRHLAKTIHAMNLNYVVITSVDRDDLRDGGATHFKNCTQAIRDKMPDIQIETLVPDFRGRLTVALDILAQQAPDVLNHNLETVPRLYEEARPGADYQASLDLLKRFKQMVPETKTKSGLMVGLGETFDEILQVMRDLRAHDVEMLTVGQYLQPSDFHLAVQRYWTPEEFKQLEQAGMEMGFTHVASGPMVRSSYHADLQAQGQFS | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
Q97U63 | MEKKVQIAVYENENFKRVAEIVKKKSIATVCEEALCPNIMECWGSGTATFMIMGSICTRGCRFCYVLKGKPSPLDDEEPKRVAEAVKEMELDYVVITSVDRDDLSDGGAQHFANVVKTVKELNPGIIVEVLTPDFRGNIDAVKKVIDAGVDVFAHNVETVRRLTPIVRDPRASYEQSLNVLKYAENVIKKSSILLGLGETWDEIVETMRDLRSVGVSILVLSQYMRPSRKQLEVKKRYTLEEFKELEEIAYSMGFSAVISLPLARTSYKAKEAYFRAIENAKNHS | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes,... |
Q6MPS6 | MADLIFQDWGLINYDEALKKQNDLVEKVHTEDLPGFLVFCTHPPVVTVGRATQAGDVFSWNGPVVEVTRGGRATYHGPSQLVVYPILNLAHVRKGRKDREINPYLKVFEDAIVDVLKTYGLTGIEGRSSAKSSFNRADADDTGVWVNDLKIASVGVGVRKWVAFHGAAINLTFDEKAFLGLRPCGFPSEVMVSLEQLTGAKVDVGEFKEKLKRRLLEVL | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q2L1E2 | MSMNVAWLSPGAAYADVWEAMKAFTASRGPATPDEIWLCEHAPVYTLGQAGLPQHVLNPADIAVVRSDRGGQVTYHGPGQIVVYCLFDLRRAGMYVRDYVALLEETAIAVLGRAGIVAQRKPGAPGVYVEQPGQTLAKIAALGIKIRKGCAYHGLSLNVAMDLTPFHGINPCGYEGLQTTDMASCGLSCSVHEVGQALADELVRRLSAYQGSLSSGE | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
A9IH67 | MIKWLTRPADYAPVWQDMRAFTAGRGAATPDEVWLCEHAPVYTLGQAGKPEHLLNPGAIPVVMCDRGGQVTYHGPGQVVAYTLFDLRRAGLFVREYVRLLEDAAIGTLDDFGVPGACRKPGAPGVYVPLGPAGELAKIAALGIKIRNGYAYHGVALNVDMDLSPFLGINPCGYEGLVTVDMAACGVRRDLVDVGQRLAERLLAAMPEPAGATR | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q89JM6 | MVNSPQNPRQDQRQDLDLTSFSATGGEPVEWRISDAPVPYPEAVAAMEARVAAIAAGEAPELVWLLEHPPLYTSGTSGKDSDLLDPRFPTFATGRGGQLTYHGPGQRVAYIMLDLKRRRPDVRAYVASLEELILKTLAAFNVRGERREDRVGVWVKRPDKGDGYEDKIAAIGVRLKRWVSFHGIAINVEPELSHFAGIVPCGVADPRYGVTSLVDLGQLVTMADVDVALRQAFEELFGPTRALVPEAAA | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q2YKK8 | MPTGKLRQKPPYAAIMTNSPVTPSTETQQPKRDALYARFLPQEADAPPVEWLIAEGLTDYEEALAFMEARVQATREGTASELVWLVEHPPLYTAGTSANAEDLLTPDRFPVFNTGRGGEYTYHGPGQRVAYVMLDLKRRREDVRAFVASLEQWIIETLAAFNIKGERREDRVGVWVVRPEKPRLADGSMCEDKIAAIGIRLRRWVSFHGIAINVEPDLSHYGGIVPCGISEHGVTSLVDLGLPVTMGDVDVALGKAFESVFGPRQTK | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
P57356 | MKKKIIFLRNLGIEHWLTTFNKMNNFIISRNPCTYDEIWFVEHYPIFTQGQSNEQKNLIVSNDIPVVQTNRGGQITYHGPGQQILYFLIDLKRRKMNIRQLINIMEQTVIETLNNFSIQAYTKKKMPGVYINEKKICSLGLRIKKGFTLHGLALNVNMNLTPFNYIHPCGDKNMKMTQIKDFNSNVKLKDVRFILIKELSKFLEIFIINSN | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q8K9Q3 | MNNRIILFQNFGLKHWIDMFNKMHAFTEVRNINTYDEIWFLEHYPIFTQGLLQKINTITYNNDILHDIPIVSTDRGGQITYHGPGQQILYFLIDLKRRKITIRDLINIMQNLIIETLNYFSIKSHIKKNSPGVYVNNKKISSLGLRVKKGFTLHGLSLNVDMDLTPFNYIYPCGDINIKMTQVKEFNSFLTLNDIRVILIKKLSQLLNVSIIEKFSIK | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q89AL8 | MYKKNIKIRNLGLRRIQDVCSSMNDFTITRKISTPDEIWLVQHYPVFTIGVSGTKHDVLVSNNIPIIFSNRGGKITYHAPGQLIIYVLINLFRRKLTVRRLILLMQNIIISTLKSFSIDSYILNNFPGVYVNNKKICSLGLRIRNGCSFHGMALNINMDLLPFEYINPCGNSFKMTQVIDIKPNLCFKIIKLMLMHKIREIFS | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q4FLP4 | MNIEIKKSIKPIKYEDAIKLLEERLLEINNGQKEDLIWILEHEEVYSAGTSYKEKEILNKDISLVKTNRGGKITYHGPGQLICYFVIDLKKRKKDIRKFITLIEETIIDSLSKFNIKTFGDPKNIGIWTDHKGKINKVAAIGVRVSKWIAYHGFAININNDLSKYKNIIPCGISDKGVINLKEIKDQDYKNLDEIIIETFSKNLEI | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
C0QQ61 | MLKIIDLGKTEYQEALEIQNRIFERKLTGEDQDNYFFITEHHPVYTAGKTTKPEHILNTEDIPVYYIDRGGSVTFHGEGQIVVYPVLSLKNRISVKRYVFTLEEIVIKTVKEIGINAYRKDRLRGVFTDKGKIASVGVKVSKGVTKHGISLNVNIEKRYFRRIIPCGIWDIPVCNITDFVEADIDKIKLKLIKHIIKEGRKLV | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q7N766 | MKFQLQHKTIFLRQLGIQPYEPISDAMHLFTEQRDTNTPDEIWLVQHPKVFTQGQAGKAEHLLSLGDIPVIQSDRGGQVTYHGPGQQVMYVMIDIKRARIGVRQLVTAIEDTVIKTLAHFGVKAYARPDAPGVYVNEAKICSLGLRIRKGCSFHGLALNIAMDLEPFQRINPCGYAGMKMIQLSDLVPGITVEQVQPVLVEKFCQQLGFKLNS | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q6LN88 | MQNSLIIRNLGRQDYEPTLQAMHEFTDQRTPETTDEVWLVEHNPVFTQGQAGKTEHLLNTGDIPVIQSDRGGQVTFHGPGQLVAYVLIDLRRNKLGVRDLVTHIENTVINTLSQFGVESNARPDAPGVYVDNKKICSLGLRIRRGCSFHGLALNINMDLTPFLRINPCGYAGMEMTQLALLSGPSELNKVQPVLVEELTKLLAYQSIEWITESN | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
A4T0B0 | MTVLVKHLGVVDYVSTYEVMRAFTKERNSTTPDEIWILEHPPVFTLGLAGDAGNLHSPSNQIPLVQVDRGGEITYHGPGQIVVYLLLDLKRLGIFVKELVSRIEQALINTLADFGLVAERRSGAPGIYVSLQPGISPEWIGAKVAALGLKVSKSCSYHGLALNVATDLEAFGRIHPCGYEGLKTVDMQTLGIKDNIDTISQRLLEHLQKQLMPT | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q12GR3 | MNMEIRHLGRVDYLPTYEAMQAFTLERTAATPNSLWICEHPPVYTQGLAGKIEHVLNPGDIPVVQTNRGGQVTYHGPGQVVAYPLIDLKQAGYYVKEYVYRIEEAVIRTLSHFGVTGHRVPGAPGIYVRLDDPFSHARLRPSPQPSPKGRGSSTPVLLPPLPGEGGGGGGPDPDPFHSLGKIAALGIKVSRHCTYHGVALNVAMDLEPFSRINPCGYAGLKTVDLRTIGVSVTWQEAADVLGQKLSSYLAP | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
Q7MUY1 | MRCILLGSGTSTGVPEVGCHCRVCRSEDRHDKRTRTSLLIITDAGKRILIDCSPDFRQQALFAGIDSLDAVLLTHEHFDHVGGLDDLRTICWHRELAVYAEQNVLDSIRDRLHYVFRKNPYPGTPLLKLCEVKPDMPFQVADLTVEPLRIMHGRLPILGYKIGEMAFLTDMKDIAAEEIECLKSCRLLFINGLRYRKEHPSHQTIEQAIDTIGQIGNPESVLIHLSHHAPLHQEHLEILPPHIHSGYDGLEAIIDEKGIRIKDFEPHVSRSEYHYQDCGRIGYESALTLQRKLFHDAVADKLENRKPQNTLLFCEHEPVL... | Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP... |
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