ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
D3EBC1 | MERNIIVLDTTLRDGEQVPGAKLNVQQKIEFAQQLKRLNVDIIEAGFPASSAGDFQAVQEIARTVGDSVSITALARAVKGDIDAVYESIKLAQNPLIHIVLGTSNIHVEKKFNRSKDAVLQMGVDAVKYAKTLLPQVQYSTEDASRSDFEYLWKTIEAVVKAGATMINVPDTVGYAVPDEFGELIRKINERLKNLNDQVILSVHCHNDLGLATANTLSAVRNGAEKVECTINGLGERAGNTSLEEVVMGLKVRENHFKASTNVRLKELIRTSRLLTHLTGLDVQVNKAITGENAFAHSSGIHQDGLLKDKQVYEIMSPEEVGADSMELILTARSGRHAFKNAVEKLGFETGEGDDFEALFEKFLLLADAKKEVYDHDVFYLVTQHRTHEEVSSHLYELDSFQVVTNDMYPTATVKLKKGSETFRDSMVGDGPIDALYSAIKALVGLDVQLKDYKINSLSRGKEAIGRVNIRIEYQGKIYSGRAMDTDIIKASALAFLNGINAVLLDAGHDSQAPVSAR | 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): 56944
Sequence Length: 518
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
|
Q7NI93 | MFQDRLIIFDTTLRDGEQSPGATLNADEKVEIARQLARLGVDVIEAGFAYASPGDFEAVERVARTVGTEDGPVICSLARAIRSDIQAAAEAIRPAARGRIHTFISTSDIHLEHQLRKSRAEVLAIAAEMVAFAKGFVDDVEFSPMDAGRSAPEYLYRVLEAAIAAGATTVNIPDTVGYLTPAEFGGLIRGITQNVRGIERAVISVHCHNDLGLAVANSLAAIENGARQIECTVNGIGERAGNCSLEEIVMALHVRRQFFNPIFGRPADSTVPLSTIDTRQIYKSSRLVSHLTGMLVQPNKAIVGANAFAHESGIHQDGVLKNRLTYEIMDAETVGVNENRIVLGKHSGRNAFRTRLVELGYELGDADLNRAFLRFKELADKKKTVSDWDIEAVISDEIRLIPEAYRLEQVQVSCGEPGLPTATVRLTGPDGVERVDAAVGTGPVDAVYKAINRLIELPNELIEFSVQSVTAGIDAMGEVTIRVRQDGRTFSGHAANTDIIVASARAYLNALNKLHFALAHPTHSGGALAHPDAAAQKL | 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): 58035
Sequence Length: 538
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
|
P43861 | MTDRVIIFDTTLRDGEQALKASLTVKEKLQIALALERLGVDVMEVGFPVSSQGDFESVQTIARHIKNARVAALSRAVDKDIDAAYEALKVAEAFRIHTFIASSALHVEAKLKRSFDDVVGMAVAAVKRARNYTDDVEFSCEDAGRTGIDNICRIVEAAINAGATTVNIPDTVGFCLPNEYGNIIAQVRNCVPNIDKAVISVHCHNDLGMATANSLTAVQNGARQIECTINGIGERAGNTSLEEVVMAMKVRQDFMGVDTHINTQEIHRVSQMVSQLCNMPIQPNKAIVGSNAFAHSSGIHQDGMLKNKNTYEILSPETIGLKKEKLNLTARSGRAAVKGHMADMGYNEQDYDLDKLYDEFLKLADKKGQVFDYDLEALAFIDMQQGDEDRLVLDKLSAHSTKEYPATAFVQLKLDGEKLSTSSIGGNGPVDAVYNAILNLTGLEIKMSHYNLTAKGEGAEALGQVDIVVEHKGRKFHGVGLATDIVESSALALVHAINAIYRAHKVADIKNHKHH | 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): 56081
Sequence Length: 515
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
|
C4XPA8 | MSDDNRVYIFDTTLRDGEQSPGATMTREEKVRMARQLETLGVDIIEAGFPAASEGDFQAVSAIAAAVKTPVVAALCRALASDIDRGFEAIKGAQRRRIHTFLATSELHMQHKLNKTPTQVLDMIEAAVSHAASKGVEVQFSAEDASRSEPAFLVAACERAINAGATILNIPDTVGYAQPAEFAELIRHLMTTVRGAGGVTFAVHCHNDLGLAVANTLAALHAGARQAEVTLSGIGERAGNASLEQVVMGLNTRPNYYNLTTGIVTEELFPSCRRLSGIIGQPIPPYAPIMGRNAFAHESGIHQHGVLKDRRTYEIMTAESIGRKGAVVVLGKHSGRHALDAKVKELGYALNDEELLVVFVAVKQLADRKQRILDEDIEALILEKVLRRPDRYALQFLSVHCGNVELAPFAVVEMQVEGQTVRHYSAGSGPVDAVFNAVCQAVGRKPDLEEYQINAITGGTDAQGEVTVRIKDGTATTVGRGVHDDVIMASTLAFINALNRLAKKEEERTCPQL | 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): 55331
Sequence Length: 513
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
|
Q39891 | MPTKTSTPSSQSPKLSHLRPQYIPNHIPDSSYVRILDTTLRDGEQSPGATMTAKEKLDIARQLVKLGVDIIQPGFPSASNSDFMAVKMIAQEVGNAVDDDGYVPVIAGFCRCVEKDISTAWEAVKYAKRPRLCTSIATSPIHMEHKLRKSKDQVIQIARDMVKFARSLGCNDIQFGAEDATRSDREFLYEILGVVIEAGATTVNIADTVGIVMPLELGKLIVDIKDNTPGIANVIISTHCHNDLGLATANTIEGARTGARQLEVTINGIGERAGNASLEEVVMALASKGDHALNGLYTRINTRHILETSKMVEEYSGMHLQPHKPLVGANAFVHASGIHQDGMLKHKGTYETISPEEIGHKRTTRIGIVLGKLSGSQALRKRLEELGYDLKEDEVDSVFWQFKAMAEKKKVVTDVDLKALVSYKAFHAESIWKLGDLQVTCGTIGLSTATVKLVNIDGSTHVACSIGIGAVDSTYKAINLIVKEPTKLLDYSLNSVTEGIGVNVTARVVICRENNHTSTYAFTEDANYPTFSGIAAEMDVVVSTVKAYLVALNKLLRWKESFRCA | 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) (By similarity). May play an important role in symbiotic nitrogen fixation (Probable).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 61580
Sequence Length: 565
EC: 2.3.3.13
|
Q7VC80 | MASHKITLLTGDGIGPEISIVAKKILAALSEKHSITFTIEEKPFGGQAIELTGKPLPEDTLNSCKASDAVLLAAIGDPKYDDLPRDLRPETGLLNLRAGLNLFANIRPIKIRQALISSSSLKSEIIKDVDLVVVRELTGGIYFGQPKGRISTEEAGERAFNTMTYSDYEIDRIAKIAFDLSETRRKKICSIDKANVLEVSQLWRERVIKAQEQYPNIELTHQYVDNAAMQLVREPAQFDVILTSNLFGDIISDEAAMLTGSIGMLPSASLGEDGPGVFEPVHGSAPDIAHKNLANPIAMILSTAMMLRTGLMEYKAATDLENAIDKVLGKGFRTIDLNRDQSNTKLGCREMGDQIIKAINGI | 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-oxopentanoate + CO2 + NADH
Sequence Mass (Da): 39521
Sequence Length: 362
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
Subcellular Location: Cytoplasm
EC: 1.1.1.85
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Q4FRV0 | MATILTLAGDGIGPEIMTQAIDVLNAVNNKFALGLTLESGLIGGVAVDATGEPLPEETLQRARAADAVLLGAVGGPKWDGIERSKRPERGLLKIRSELGLFANLRVAKLYPQLVNASSIKPEIISGLDLLIVRELTGGIYFGEPRGIRTLENGEQQGYNTMVYSTSEINRIGKVAFELAQTRAQAAGTPAKVCSIDKANVLEVTELWKQTMIELQQAEYSDVALSHMYADNACMQLIKDPKQFDVMVTGNLFGDILSDEAAMLTGSIGMLPSASLDEAGKGMYEPCHGSAPDIAGQDIANPLATILSVAMMLRYTFKQEVAAQAIEQAVSDVLDDGLRTVDILDRNEAGLIQVGCQQMGQAVLAKLL | 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-oxopentanoate + CO2 + NADH
Sequence Mass (Da): 39205
Sequence Length: 367
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
Subcellular Location: Cytoplasm
EC: 1.1.1.85
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Q8XXX5 | MTKIAVLPGDGIGTEIVAEAVKVLKTLGETFEMETAPVGGAGYEAKGHPLPEDTLKLAKEADAILFGAVGDWKYDTLPRELRPEQAILGLRKHLQLFANFRPAICYPELAGASSMKPEIVAGLDILIVRELTGDIYFGQPRGVRAAPDGLFAGAREGFDTMRYSEPEIRRIAHVAFQAAAKRGKKLCSVDKANVLETFQFWKDIVTDVHKEYPEVELSHMYVDNAAMQLVKAPKNFDVVVTGNMFGDILSDEAAMLTGSIGMLPSASLDANNKGLYEPSHGSAPDIAGKGIANPLATILSAAMMLRYTLGKAEQADRIENAVKKVLAQGYRTGDILTPGCKQVGTVEMGDAVVAAL | 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-oxopentanoate + CO2 + NADH
Sequence Mass (Da): 38218
Sequence Length: 356
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
Subcellular Location: Cytoplasm
EC: 1.1.1.85
|
P80858 | MMPRTIIEKIWDQHIVKHGEGKPDLLYIDLHLIHEVTSPQAFEGLRQKGRKVRRPQNTFATMDHNIPTVNRFEIKDEVAKRQVTALERNCEEFGVRLADLHSVDQGIVHVVGPELGLTLPGKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLSTQTLWQQRPKTLEVRVDGTLQKGVTAKDVILAVIGKYGVKFGTGYVIEYTGEVFRNMTMDERMTVCNMSIEAGARAGLIAPDEVTFEYCKNRKYTPKGEEFDKAVEEWKALRTDPGAVYDKSIVLDGNKISPMVTWGINPGMVLPVDSEVPAPESFSAEDDKKEAIRAYEYMGLTPHQKIEDIKVEHVFIGSCTNSRMTDLRQAADMIKGKKVADSVRAIVVPGSQSVKLQAEKEGLDQIFLEAGFEWRESGCSMCLSMNNDVVPEGERCASTSNRNFEGRQGKGARTHLVSPAMAAMAAIHGHFVDVRKFYQEKTVV | 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): 52392
Sequence Length: 472
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
|
Q8A6L7 | MNTLFDKIWDAHVVTTVEDGPTQLYIDRLYCHEVTSPQAFAGLRERGIKVLRPEKVFCMPDHNTPTHDQDKPIEDPISKTQVDTLTKNAKDFGLTHFGMMHPKNGIIHVVGPERALTLPGMTIVCGDSHTSTHGAMGAIAFGIGTSEVEMVLASQCILQSRPKTMRITVDGELGKGVTAKDVALYMMSKMTTSGATGYFVEYAGSAIRNLTMEGRLTLCNLSIEMGARGGMVAPDEVTFEYIKGRENAPQGEAWDQAMEYWKTLKSDDDAVFDQEVRFDAADIEPMITYGTNPGMGMGITQNIPTTEGMGEAAQVSFKKSMEYMGFQPGESLLGKKIDYVFLGACTNGRIEDFRAFASLVKGRRKADNVIAWLVPGSWMVDAQIRKEGIDKILTEAGFAIRQPGCSACLAMNDDKIPAGKYSVSTSNRNFEGRQGPGARTLLASPLVAAAAAVTGVITDPRELM | 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): 50491
Sequence Length: 464
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
|
Q938C9 | MGMTIIEKILARKAGVAEVHAGEIVTVEVDMTVLIDLQFATMWMQPLMINDASKVAIVMDHAVPAPTIKDAAGGPNARKFANDYGIERFYDVGRHGICHQVIAENGLARPGEILACTDSHTCAGGAFNTAARGLGPAEVYSILCTGQTWFQASPTIRYELIGSMPAGVSGKDVFLYIADAFGDATNSNLEYGGPGLASIPLNDRRTIATQGAEISADFSTFAYDDVLAEHFDDLGITSYEPAHADPDAAYAAVREIDLSALAPYVARPGTVSRNGVSVDEVEPRKIDQAFIGSCANGQLDDLRIAAEILRGRRVAPGVRLIVTPASQQVYRDAMRLGYLQDIADAGAVITNSTCGACFGYHMGVVGPGEVCLTSSTRNFTGRMGSTEAEIYMASPATVAASAVAGHITDARKVVAQWLQVSL | 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): 44668
Sequence Length: 422
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
|
Q18AJ1 | MIANGSVFKFGDNIDTDVIIPARYLNIADYKELATHCMEDIDDKFISKVKKGDIIVATKNFGCGSSREHAPIVIKESGVSCVIASTFARIFFRNSINIGLPILECEEAANNIDEGDNIEVDFSTGVIKNITKGKEYKAEPFPEFMQNIILNEGLINSIKANRG | 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): 17965
Sequence Length: 163
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
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P31960 | HAPIALKAAGVSCVIAKSFARIFYRNSINIGFPILECEEAVNDAKNNHELEVDFTTGIIKNITLGKEYKAQAYPQFMIDIMKNEGLINCVKNGALNSFMR | 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): 11108
Sequence Length: 100
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
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C3PFZ5 | MEKFVTHTGVGVPLRVSNVDTDQIIPARYLKSVKRTGFADGLFSNWRSDENFILNQEPFKEGSVLFAGPDFGTGSSREHAVWALAEYGFKAVFSSRFADIFRGNSGKAGLLTGLMEQEDIELIWKQLESGETETTVDLEARTVTVGGNSYTFEIDDYTRWRLMEGLDDIGLTLRNEGDIEAFESTRPGFKPRVVAS | 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): 21860
Sequence Length: 196
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
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Q8NQV7 | MEKFTTYTGVGVPLQRSNVDTDQIIPAVYLKRVTRTGFEDGLFSNWRQNDPNFVLNTDTYKNGSVLVAGPDFGTGSSREHAVWALMDYGFRAVFSSRFADIFRGNSGKAGMLTGIMEQSDIELLWKLMEQTPGLELTVNLEKQIVTAGDVVISFEVDPYIRWRLMEGLDDAGLTLRKLDEIEDYEAKRPAFKPRTNA | 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): 22199
Sequence Length: 197
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
|
Q4JUX3 | MEKFNTHTGVAAPLNRSNVDTDQIIPAVYLKRVTRTGFEDGLFAGWRKDPEFILNQEPYKNASVLVAGPDFGTGSSREHAVWALMDYGFRVVLSSRFADIFRGNSGKAGLLAAQMEQSDIELIWKLLEQQPGAEITVNLEDRTVTLGTHTFGFDVDDYTRWRLMEGLDDIGLTLRNEEAIEAFESQRASFKPRTIPAS | 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): 22189
Sequence Length: 198
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
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Q44022 | MEPFTMHRGVAAPLLRINIDTDAIIPSREMKRVSRHGLAEGLFAGWRYLAGTDRSPDPLFVLNQPEYTGASILLAGSNFGCGSSREHAVWALKEFGIRAIVAPGFGAIFHNNCVRNGLLPVVLPMATVQALADDCAAAPATRQVTVDLRQLEVVSPAGARYGFTLGSEQRQMLLEGLDPIALTLKLASSIDAFQGADRLRRPWIHFDG | 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): 22550
Sequence Length: 208
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
|
Q11NN7 | MEKFITIKSTVVPLPIEDVDTDQIIPARFLKATTKEGFGKSLFCDWRYNQDGTPKADFVMNNPLYSGQILVAGKNFGCGSSREHAAWAIGDAGFRVVVSSFFADIFRGNALNNGILPVQVSDAFLKSIFDAVAANAKQELVVDLANQVISIAGTDLKESFVINEYKKTCLINGYDDIDYVLSIKDKIEAYEKTSKYLSLLA | 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): 22138
Sequence Length: 201
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
|
C1CVE0 | MPRVHVFARDHINTDEIIPARHLTTDIEAELAPYAMEDYDRDFAKRVQPGDIIVAGADFGCGSSREHAVWALRGAGVGAVIAPNFARIYYRNSINNGFLALECDGIVEAFQDGDEANLDLKGGTITNLRTGQTLTFVPVPQFALDVQKAGGWLEYMRAQVPAEADDSSSAQPHPGKENAHA | 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): 19665
Sequence Length: 181
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
|
C0QDY4 | MKPFTTHTGVIATLNRSNVDTDAIIPKQFLKSIKRTGYGPSAFYDWRYTADGRPDPNFELNHPRFEGRSILVTRNNFGCGSSREHAVWALVQDGYRVIIAPWKEIGEKRLPAFADIFLSNTTKNGMLCIELSETIIDAIFEQTASQPGLQATVDLTVQQLTIHGRIPATYPFQIEEGVREQLINGLDEIALSLKHEADIAAFEARRPTWMDGRD | 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): 24078
Sequence Length: 214
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
|
Q726X3 | MRYAGTAHKVGDHIDTDAIIPARFLVTTDAQKLGENCMEGLEHGWVARVKSGDIMVGGRNFGCGSSREHAPIAILGAGMPVVVAHSFARIFYRNGFNMGLLLLEVGDDVDKIADGDDIEVDAASGVITNRTTGATITCAPVPQSMRELLDTGGLVPYVRARLERENG | 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): 17810
Sequence Length: 167
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
|
Q9A724 | MLTRKQHELLMFIHERIKETGVSPSFDEMKEALDLASKSGIHRLITALEERGFIRRLAHRARALEVVKLPQQATAAAPPKGRGAFRPQVFEGGGAPPPAASPAAAANDSRELPILGRIAAGTPIDAIQHERERLPVPEAMLGAGEHYVLEVQGDSMIEAGILDGDYVIIKKGDTATSGEIVVALVGEEATLKRLRKKGGSIALEAANPKYETRIFGPDQVEVQGKLVGLIRRYH | 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 DNA repair.
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 25329
Sequence Length: 234
EC: 3.4.21.88
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Q9ZFA4 | MLTRKQMELLDFIKTRMDRDGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLAHRARAIEIVKLPEAMERAGFSARAAKAAAAPLPKGAVTVETAGALDLPLMGRIAAGLPIEAINGGPQSVTVPGMMLSGRGQHYALEVKGDSMIAAGINDGDIVVIREQQTADNGDIVVALVADHEATLKRYRRRGGMIALEPANDSYETQVYPEQMVKVQGRLVGLIRSY | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Has been shown to bind to the direct repeat sequence 5'-GTT-N(7)-GTTC-3'. 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 DNA repair.
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 24800
Sequence Length: 228
EC: 3.4.21.88
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Q97I23 | MATDKITRDVQSEIYEFIRQEVLDKGYPPSVREICAKVGLSSTSTVHGHLSRLEKKGLIRRDPTKPRAIELIKDPISKREMIDIPIVGKVQAGQPILAVENIDDYLTIPLNFVRNTNDLFILKISGNSMIEAGIYDGDLAIIEKTNYAQNGDIVVALIENDATIKRFFKEKDKIRLQPENHTMDPIIVDNCEVIGKLAGIYRRY | 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 DNA repair.
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 23066
Sequence Length: 204
EC: 3.4.21.88
|
Q187P1 | MYLDLTEKQVLILEFIKSQIILKGYPPAVREICTAVGLRSTSTVHSHLNKLEKLGYIRKDPTKPRAIEVLERSKVNDVSGANQEIIELPLVGQITAGEPILAQQNIEEYIPFPASLVKGSNNFVLRVKGESMINAGILDEDYVVVDKKNTALNSQIVVALINGESATVKRFFKEGNLIRLQPENDFMEPIMLNDSEVEIVGIVTGVFRVIK | 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 DNA repair.
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 23473
Sequence Length: 211
EC: 3.4.21.88
|
Q129C4 | MSILNDFSHLSSEGPKLTARQQQILELIQSAITRTGAPPTRAEIANELGFKSANAAEEHLQALARKGVIELVSGTSRGIRLRSDTLRSIHESRVKQFSLPLQSLAQLALPLVGRVAAGSPILAQEHIEQTYYFESSLFQRQPDYLLKVRGMSMRDAGIIDGDLLAVKQAKEARNGQIVVARIGDEVTVKRFRRTKHLIELLPENPDFKTIVVEPGEPFELEGLAVGLIRNTMLI | 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 DNA repair.
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 25883
Sequence Length: 234
EC: 3.4.21.88
|
A8F429 | MKKELTDRQKKILDFVLSYIDSHGYPPSIRDIARAFRITPRGAIVHLNALEKKGYLTRGKRARSIKVLNRSEAIRLPVVGTIAAGNAIEAIENPTEIIEVPKAMIKIGFDHFLLRVRGESMIEEHILDKDYVVIRKQNTANNGDIVAVLTNSNEATLKKIYIEPEKIILKPANSKMQPIELKPENVKILGKMVGVIRIYG | 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 DNA repair.
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 22519
Sequence Length: 200
EC: 3.4.21.88
|
Q2K8X2 | MLTRKQQELLLFIHERMKESGVPPSFDEMKDALDLASKSGIHRLITALEERGFIRRLPNRARALEVIKLPEAYNPSLQPRRGFSPSVIEGSLGKPQPVAAPAAPKPVADNGNSISVPVMGRIAAGVPISAIQNNTHDIVVPADMLGSGEHYALEVKGDSMIDAGIFDGDTVIIRNGSTASPGDIVVALVDDEEATLKRFRRKGASIALEAANPAYETRIFGPDRVKVQGKLVGLIRRYH | 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 DNA repair.
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 25874
Sequence Length: 239
EC: 3.4.21.88
|
Q98MD2 | MLTRKQHELLMFIHERLKESGIPPSFDEMKEALDLASKSGIHRLITALEERGFIRRLPNRARALEVLRLPDSIAPGLNAAKKFSPSVIQGSLGQGGLGRQIKPAPSRLPAAGNDDDAVSAVSIPVMGRIAAGVPIDAIQHQTHSISVPPDMIMGGEHYALEVKGDSMIDAGIFDGDTVIIRNADTASPGEIVVALVDEEEATLKRFRRKGASIALEAANPAYETRIFGPDRVKVQGKLVGLIRRY | 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 DNA repair.
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 26496
Sequence Length: 245
EC: 3.4.21.88
|
Q7Z429 | MSHEKSFLVSGDNYPPPNPGYPGGPQPPMPPYAQPPYPGAPYPQPPFQPSPYGQPGYPHGPSPYPQGGYPQGPYPQGGYPQGPYPQEGYPQGPYPQGGYPQGPYPQSPFPPNPYGQPQVFPGQDPDSPQHGNYQEEGPPSYYDNQDFPATNWDDKSIRQAFIRKVFLVLTLQLSVTLSTVSVFTFVAEVKGFVRENVWTYYVSYAVFFISLIVLSCCGDFRRKHPWNLVALSVLTASLSYMVGMIASFYNTEAVIMAVGITTAVCFTVVIFSMQTRYDFTSCMGVLLVSMVVLFIFAILCIFIRNRILEIVYASLGALLFTCFLAVDTQLLLGNKQLSLSPEEYVFAALNLYTDIINIFLYILTIIGRAKE | Function: Potential apoptotic regulator.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41203
Sequence Length: 371
Subcellular Location: Membrane
|
Q9ESF4 | MSHEKSFLVSGDSYPPQNIVGPQAPMPPYVQAPYPGAPYPQAPFQPSPYGQPGYPHGPSPYPQGGYPQGPYPQGGYPQGPYPQSPFPPNPYGQPPPFQDPGSPQHGNYQEEGPPSYYDNQDFPAVNWDKNIRQAFIRKVFLVLTLQLSVTLSTVAIFTFVGEVKGFVRENVWTYYVSYAIFFISLIVLSCCGDFRRKHPWNLVALSILTVSLSYMVGMIASFYNTEAVIMAVGITTAVCFTVVIFSMQTRYDFTSCMGVLLVSVVVLFIFAILCIFIRNRILEIVYASLGALLFTCFLAVDTQLLLGNKQLSLSPEEYVFAALNLYTDIINIFLYILTIIGRAKE | Function: Potential apoptotic regulator.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38408
Sequence Length: 345
Subcellular Location: Membrane
|
Q9M1V9 | MWNQKHDLESAQTPLYPMMSESPELRWSFIRKVYSIISIQLLVTIAVAATVVKVHSISVFFTTTTAGFALYILLILTPLIVMCPLYYYHQKHPVNYLLLGIFTVALAFAVGLTCAFTSGKVILESVILTAVVVISLTLYTFWAAKRGHDFNFLGPFLFGAVIVLMVFSFIQILFPLGKISVMIYGCLASIIFCGYIVYDTDNLIKRHSYDEYIWAAVSLYLDVINLFLSLLTLLRAVDS | Function: Regulates the brassinosteroid (BR) signaling pathway that mediates cell elongation and organ morphogenesis .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26908
Sequence Length: 239
Subcellular Location: Membrane
|
Q9BWQ8 | MTQGKLSVANKAPGTEGQQQVHGEKKEAPAVPSAPPSYEEATSGEGMKAGAFPPAPTAVPLHPSWAYVDPSSSSSYDNGFPTGDHELFTTFSWDDQKVRRVFVRKVYTILLIQLLVTLAVVALFTFCDPVKDYVQANPGWYWASYAVFFATYLTLACCSGPRRHFPWNLILLTVFTLSMAYLTGMLSSYYNTTSVLLCLGITALVCLSVTVFSFQTKFDFTSCQGVLFVLLMTLFFSGLILAILLPFQYVPWLHAVYAALGAGVFTLFLALDTQLLMGNRRHSLSPEEYIFGALNIYLDIIYIFTFFLQLFGTNRE | Function: Antiapoptotic protein which protects cells uniquely from Fas-induced apoptosis. Regulates Fas-mediated apoptosis in neurons by interfering with caspase-8 activation. May play a role in cerebellar development by affecting cerebellar size, internal granular layer (IGL) thickness, and Purkinje cell (PC) development.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35110
Sequence Length: 316
Subcellular Location: Cell membrane
|
Q8K097 | MTQGKLSVANKAPGTEGQQHQANGEKKDAPAVPSAPPSYEEATSGEGLKAGTFPQGPTAVPLHPSWAYVDPSGSSGYEGGFPAGHHEHFTTFSWDDQKVRRLFIRKVYTILLVQLLVTLAVVALFTFCDVVKDYVQANPGWYWASYAVFFATYLTLACCSGPRRHFPWNLILLTIFTLSMAYLTGMLSSYYNTTSVLLCLVITALVCLSVTIFSFQTKFDFTSCQGVLFVLLMTLFFSGLLLAVLLPFQYVPWLHAVYAVLGAGVFTLFLAFDTQLLMGNRRHSLSPEEYIFGALNIYLDIIYIFTFFLQLFGTNRE | Function: Antiapoptotic protein which protects cells uniquely from Fas-induced apoptosis. Regulates Fas-mediated apoptosis in neurons by interfering with caspase-8 activation. Plays a role in cerebellar development by affecting cerebellar size, internal granular layer (IGL) thickness, and Purkinje cell (PC) development.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35258
Sequence Length: 317
Subcellular Location: Cell membrane
|
Q969X1 | MSNPSAPPPYEDRNPLYPGPPPPGGYGQPSVLPGGYPAYPGYPQPGYGHPAGYPQPMPPTHPMPMNYGPGHGYDGEERAVSDSFGPGEWDDRKVRHTFIRKVYSIISVQLLITVAIIAIFTFVEPVSAFVRRNVAVYYVSYAVFVVTYLILACCQGPRRRFPWNIILLTLFTFAMGFMTGTISSMYQTKAVIIAMIITAVVSISVTIFCFQTKVDFTSCTGLFCVLGIVLLVTGIVTSIVLYFQYVYWLHMLYAALGAICFTLFLAYDTQLVLGNRKHTISPEDYITGALQIYTDIIYIFTFVLQLMGDRN | Function: Negatively regulates aortic matrix metalloproteinase-9 (MMP9) production and may play a protective role in vascular remodeling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34607
Sequence Length: 311
Subcellular Location: Membrane
|
Q8BJZ3 | MSNPSAPPPYEDHNPLYPGSPPPGGYGQPSVLPGGYPAYPAYPQPGYGHPAGYPQPVPPVHPMPMNYGHDYNEEERAGSDSFRPGEWDDRKVRHSFIQKVYCIISVQLLITVAIIAIFTFVEPVGKYVRNNVAVYYVSYAVFLVTYLTLACCQGPRRRFPWDIILLTIFTLALGFVTGTISSMYENKAVIIAMIITAVVSISVTIFCFQTKVDFTSCTGLFCVLGIVLMVTGIVTSIVLIFKYIYWLHMVYAALGAICFTLFLAYDTQLVLGNRKHTISPEDYITGALQIYTDIVYIFTFVLQLVGSRD | Function: Negatively regulates aortic matrix metalloproteinase-9 (MMP9) production and may play a protective role in vascular remodeling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34393
Sequence Length: 309
Subcellular Location: Membrane
|
Q9HC24 | MADPDPRYPRSSIEDDFNYGSSVASATVHIRMAFLRKVYSILSLQVLLTTVTSTVFLYFESVRTFVHESPALILLFALGSLGLIFALILNRHKYPLNLYLLFGFTLLEALTVAVVVTFYDVYIILQAFILTTTVFFGLTVYTLQSKKDFSKFGAGLFALLWILCLSGFLKFFFYSEIMELVLAAAGALLFCGFIIYDTHSLMHKLSPEEYVLAAISLYLDIINLFLHLLRFLEAVNKK | Function: Anti-apoptotic protein which can inhibit apoptosis induced by intrinsic and extrinsic apoptotic stimuli. Can modulate both capacitative Ca2+ entry and inositol 1,4,5-trisphosphate (IP3)-mediated Ca2+ release.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26971
Sequence Length: 238
Subcellular Location: Golgi apparatus membrane
|
Q9DA39 | MADTDPGYPRSSIEDDFNYGSCVASASVHIRMAFLRKVYSILSLQVLLTTVTSALFLYFQALRTFVHESPALIVVFALGSLGLIFALTLHRHTHPLNLYLLFAFTLSESLAVAAVVTFYDVYLVLQAFIMTTAVFLGLTAYTLQSKRDFTKFGAGLFAGLWILCLAGFLKLFFYSETMELVLASLGALLFCGFIIYDTHSLMHRLSPEEYVIAAISLYMDIINLFLHLLKFLEAVNKK | Function: Anti-apoptotic protein which can inhibit apoptosis induced by intrinsic and extrinsic apoptotic stimuli. Can modulate both capacitative Ca2+ entry and inositol 1,4,5-trisphosphate (IP3)-mediated Ca2+ release (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26647
Sequence Length: 238
Subcellular Location: Golgi apparatus membrane
|
A8WGA3 | MEWLIFSLLLLAVSASGQLCPKRCMCQNLSPSLAILCAKTGLLFVPTVIDRRTVELRLTENFITAVKRRDFANMTSLLHLTLSRNTISQIMPYTFADLKRLRALHLDSNRLSVITDDHFRGLTNLRHLILANNQLHNISPHAFDDFLGTLEDLDLSYNNLVDIPWDTIGRLTNVNTLNMDHNLIEHVPLGIFSNLHKLARLDMTSNKLKKIPPDPLFLRIPVYAKSKGSPLSSLVLSFGGNPLHCNCELLWLRRLTREDDLETCASPPDLTAKYFWTIPEEEFICDPPVITRKSPKTFAMEGQPTSLKCKANGDPDPDVHWISPEGRLIANTSRTLSFSNGSLEINITSLKDTGIFTCIASNAAGESTGTVELVVSPLPHLANSTNRIREPDPGPSDILTSAKSTSSVSNETRSQERKVVLAELSANSALIRWPSQQHFPGIRMYQIQYNSSVDDTLVYRMIPSTSFDFLVRDLVSGREYDLCVLAVYDDGVTSLTATRQVGCVTFVTETEFSQCQSLRSHFLGGTMIIIIGGIIVASVLVFIIILMIRYKVYSQHGADSGKGTAMTNVRSQTNGGQAAGQVPRSSSKIVEGQEASGGSLGGAANIKDSTALVLVTDSETAVQISEISSEDIVSPTQRHHPRTCIELKRRPSLSCKEGTSSDTQEDTASPQVSDEKKAQRDWSDFKI | Function: May be involved in the regulation of excitatory synapses.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 75776
Sequence Length: 687
Subcellular Location: Membrane
|
Q2P2R2 | MTPFRRPIVLATSASAPFPPAEAALTDPDGLLAVGGDLSPQRLLNAYAHGIFPWYSDGRPILWWSPDPRMVFRTDGVRLSSRFKRQLRASTWTVRADTAFEQVIDACAASPRPGQDGTWITAEMQQAYIALHRLGHAHSIEVFDGARLVGGIYGVAVGRMFFGESMFSGESGGSKVALAALAADLHGRGWPLIDAQVENPHLLSMGAERLPRAEFLHDVQRQVALAEQPGSWSQRYGEHAASDLCETHLT | 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-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 27273
Sequence Length: 250
Subcellular Location: Cytoplasm
EC: 2.3.2.6
|
Q5NP09 | MTNMIDPHLLLSAYATGIFPMSDSRETDEVYWVEPKKRGILPPDHFHLSRSLAKIIRSDRFLVTADRDFEAVIDLCAEPTEDRPDSWINPPIRAAYCQLHNLGYAHSIECWLDNRLVGGLYGVNLGYAFFGESMFSRVSNASKVALAWLVARLKVGNFSLLDCQFITDHLASMGAIEITREDYLKRLKSAVSSYFTDKETGNWNTLDRLSPLLHNKHSKTKENQFADADLPFTEGIALETDGTAPGEASFSLACPNGARIVQLLGQIS | 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-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 29930
Sequence Length: 268
Subcellular Location: Cytoplasm
EC: 2.3.2.6
|
Q64280 | MPFLWLCWALWALSLVSLREALTGEQILGSLLQQLQLDQPPVLDKADVEGMVIPSHVRTQYVALLQHSHASRSRGKRFSQNLREVAGRFLVSETSTHLLVFGMEQRLPPNSELVQAVLRLFQEPVPRTALRRQKRLSPHSARARVTIEWLRFRDDGSNRTALIDSRLVSIHESGWKAFDVTEAVNFWQQLSRPRQPLLLQVSVQREHLGPGTWSSHKLVRFAAQGTPDGKGQGEPQLELHTLDLKDYGAQGNCDPEAPVTEGTRCCRQEMYLDLQGMKWAENWILEPPGFLTYECVGSCLQLPESLTSRWPFLGPRQCVASEMTSLPMIVSVKEGGRTRPQVVSLPNMRVQTCSCASDGALIPRRLQP | Function: Required for left-right axis determination as a regulator of LEFTY2 and NODAL.
PTM: The processing of the protein may also occur at the second R-X-X-R site located at AA 132-135. Processing appears to be regulated in a cell-type specific manner.
Sequence Mass (Da): 41498
Sequence Length: 368
Subcellular Location: Secreted
|
O00292 | MWPLWLCWALWVLPLAGPGAALTEEQLLGSLLRQLQLSEVPVLDRADMEKLVIPAHVRAQYVVLLRRSHGDRSRGKRFSQSFREVAGRFLASEASTHLLVFGMEQRLPPNSELVQAVLRLFQEPVPKAALHRHGRLSPRSAQARVTVEWLRVRDDGSNRTSLIDSRLVSVHESGWKAFDVTEAVNFWQQLSRPRQPLLLQVSVQREHLGPLASGAHKLVRFASQGAPAGLGEPQLELHTLDLRDYGAQGDCDPEAPMTEGTRCCRQEMYIDLQGMKWAKNWVLEPPGFLAYECVGTCQQPPEALAFNWPFLGPRQCIASETASLPMIVSIKEGGRTRPQVVSLPNMRVQKCSCASDGALVPRRLQP | Function: Required for left-right (L-R) asymmetry determination of organ systems in mammals. May play a role in endometrial bleeding.
PTM: The processing of the protein may also occur at the second R-X-X-R site located at AA 132-135. Processing appears to be regulated in a cell-type specific manner.
Sequence Mass (Da): 40920
Sequence Length: 366
Subcellular Location: Secreted
|
Q89AC7 | MYIHFPQFSPIIFSIFSIPIRWYGLMYFLAFIFALWRGKTRAEYYNLTQIEVENLLYSCFIGLFIGGRIGYIIFYNPVFFFENMSHILKIWEGGMSFHGGLLGVIIVLLFFSKKLNKHILEISDFIVPLVPFGLGAGRLGNFINGELWGRIAPDFKFSVLFPNSREIDLNVAANNLELKSLIEKFGVLPRHPSQIYEFVLEGLVLFFVLNYFSKKSMPFGFVSSIFLILYGCFRIFLEIFRQPDRQIGLFLNTFSMGQLLSMPMIVLGILIAINIYVKVL | 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(+) + S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32365
Sequence Length: 280
Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Subcellular Location: Cell membrane
EC: 2.5.1.145
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Q8R6A3 | MNPVFLKIGPIELHYYGLMYAIAFFVGISLGKKIAKERNFDLDLVENYAFVAIISGLIGGRLYYILFNLPYYLQNPFEILAVWHGGMAIHGGILGGIAGTLIFAKIKKINPLILGDFAAGPFILGQAIGRIGNFMNGEVHGVPTFTPFSVIFNVKPKFYEWYTYYQSLSISDKANYPDLVPWGVVFPTSSPAGSEFPNLALHPAMLYELILNLIGFFIIWFILRKKENKASGYMWWWYIIIYSINRIIVSFFRVEDLMFFNFRAPHVISIILIAVSIFFLKKDNKKVF | 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(+) + S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32859
Sequence Length: 288
Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Subcellular Location: Cell inner membrane
EC: 2.5.1.145
|
Q5KVC0 | MESTIQPLDRVFLHLGPITIYWYGVIIGTGVLIGLWLATREAVRRGLPKETFVDLVLFAVPIAIVCARAYYVLFEWHYYSKHLSEIPKVWQGGLAIHGGLIGAVATGAVFARARGLSFWKLADIAAPSIILGQAIGRWGNFMNQEAHGGPVSRQFLENLHLPDWIINQMYIDGRYWHPTFLYESLWNLVGFFLLLWLRRVNLRRGELFLSYLIWYSVGRFWIEGMRTDSLMLAGSLRAAQVVSVTLIVLSIALWIVRRAKGWAKARYQDE | 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(+) + S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30850
Sequence Length: 270
Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Subcellular Location: Cell membrane
EC: 2.5.1.145
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P60970 | MQFPHIDPVFFRLGHLEFRWYGLMYILGFIAAYFIVRRAAGRRGLALTQDDVADVIFSLAIGVILGGRLGYILFYNLSYYLSHPLKLFAVWEGGMSFHGGLLGVILAGVYVARQKKIGFPVLADICAPAAPVGLGLGRLGNFINGELYGRVTDVPWGIIFPGGGGVPRHPSQLYEAVLEGPVLFLILMAVGRRERPAGVVFWTFIAFYGLFRFLVEFFREPDAQLGLLAGPFSMGQLLSFPMFLLGLTMAVLVSRRKVGP | 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(+) + S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28663
Sequence Length: 260
Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Subcellular Location: Cell inner membrane
EC: 2.5.1.145
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Q7ND43 | MPMETGFTSPGPLIVQIGGFAVRWYSLLILAGIIAGTLLSQKLAPERKVAPEVLSDLVVWLVVGAIPMARLYYVLFEWQRFAGEPWWKVFAIWEGGIAIHGAILGGLLAGWLFCRRNGYSLLTMIDLAAPGLILGQAIGRWGNFFNSEAYGAPTNLPWKLFIPEANRPPGMAAFAYYHPTFLYESLWNLGVLALLLFVFFRFKNLRPGSIACLYALAYSVGRFWIEGLRLDSLMVGPLRTAQLVSLAGIVLGAVGLWWLNRRSARQEAP | 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(+) + S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29832
Sequence Length: 269
Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Subcellular Location: Cell inner membrane
EC: 2.5.1.145
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P44930 | MNSNYLLLPHFDPSIFTLGDSNIGLRWYGLMYLLGFVFARWLAVRRANRPNSGWTVDQVDSLLFNGFMGVFIGGRVGDVFFYNLDHFLQEPLYLFRVWEGGMSFHGGLIGVIVAMIWTSYSQKRNFWQTADFVAPLIPFGLGLGRIGNFINLELWGRETNVPWAMIFPNDPLLLPRHPSQLYEAFLEGLVLFTILNIFIKKPRPMASVAGLFLIGYGVFRFIVEYVREPEVENFFGIITRGQALCLPMIIGGAFIMAWAYSRKSAVIK | 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(+) + S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30570
Sequence Length: 268
Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Subcellular Location: Cell inner membrane
EC: 2.5.1.145
|
Q9K6Y5 | MEEMIEPLDRVFLQLGPFTIYWYGVLIGLGVIIGYVMASRESVRRGMPKDTFSDFVMYVIPVAIIFARLYYVIFRWEQYADDPIRVFYIWEGGLAIHGALIGGVLTAYILTKKRQLSFWQLMDVAAPSILIGQAIGRWGNFMNQEVYGGPVTREFLEGLMLPEFIINQMYINGTYYHPTFLYESIWNFIGVVVLLLLRRVNLRRGELFFSYLIWYSIGRFFIEGMRLDNLMIGDSLRTAQIVSILLIVGALLLWWYRRAKGLATERYLDPHQPARTNGNKKKTKKKKKK | 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(+) + S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33670
Sequence Length: 289
Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Subcellular Location: Cell membrane
EC: 2.5.1.145
|
Q7VIU4 | METYSVWNRIYDYINPIAFKIFDISVHWYGIMYVSAMLIALLIAKAFITYRNERFPITQELLDSFFIWVEIGVILGGRIGYVLIYSPNRWEYLMQPWQMFNPYTNGVFVGISGFSYHGAMAGFVLAAIIFCYVKKQSFWIFMDLSAISIPLGYVFGRIGNFFNHELFGRVIESDSSLRDIGILVNGELRYPSQLFEAFAEGIIVFILLICLLRYAKKPGTLLVAYGVFYALARFVCEYFREADSQMGYFVFGLSMGQILSLVMLVISIFLGLFVFVQKPISSQKIKHQRKKK | 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(+) + S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33710
Sequence Length: 292
Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Subcellular Location: Cell inner membrane
EC: 2.5.1.145
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Q2FIN2 | MGIVFNYIDPVAFNLGPLSVRWYGIIIAVGILLGYFVAQRALVKAGLHKDTLVDIIFYSALFGFIAARIYFVIFQWPYYAENPSEIIKIWHGGIAIHGGLIGGFIAGVIVCKVKNLNPFQIGDIVAPSIILAQGIGRWGNFMNHEAHGGSVSRAFLEQLHLPNFIIENMYINGQYYHPTFLYESIWDVAGFIILVNIRKHLKLGETFFLYLTWYSIGRFFIEGLRTDSLMLTSNIRVAQLVSILLILISISLIVYRRIKYNPPLYSKVGALPWPTKKVK | 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(+) + S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31572
Sequence Length: 279
Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Subcellular Location: Cell membrane
EC: 2.5.1.145
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Q49VV9 | MMTLSYIDPIAFELGPISVRWYGIIIAMGILLGYFIAQASVKRIGFHQDTLVDIIFWSAIFGFIIARIYFVIFQWPYYVQHPIEIPMIWQGGIAIHGGLIGGFVTGIIICKQKNINPFQIGDVIAPSMILGQGIGRWGNFMNHEAHGGTVSKSFLENLHIPDFIINNMYIDGKYYQPTFLYESIWDVLGFVILILLRKHLRIGDTFCLYLIWYSIGRFFVEGMRTDSLMLAGDIRIAQLMSIILIIIGVVIMIVRRVKYDAPRYKAVGPLSWPSKEVK | 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(+) + S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31703
Sequence Length: 278
Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Subcellular Location: Cell membrane
EC: 2.5.1.145
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P04124 | MADLKPSLTGLTEEEAKEFHGIFVTSTVLYLATAVIVHYLVWTARPWIAPIPKGWVNLEGVQSALSYLV | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 7643
Sequence Length: 69
Subcellular Location: Cell inner membrane
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P09927 | MRDDDDLVPPKWRPLFNNQDWLLHDIVVKSFYGFGVIAAIAHLLVYLWKPWLP | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 6320
Sequence Length: 53
Subcellular Location: Cell membrane
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Q2RQ23 | MAEVKQESLSGITEGEAKEFHKIFTSSILVFFGVAAFAHLLVWIWRPWVPGPNGYSALETLTQTLTYLS | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 7716
Sequence Length: 69
Subcellular Location: Cell inner membrane
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P80587 | ADANKVWPTGLTVAEAEELHTYVTNGFRVFVGIAVVAHVLVFAAHPWGRGGALVA | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 5787
Sequence Length: 55
Subcellular Location: Cell inner membrane
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P26274 | MADNTDLSFTGLTDEQAQELHSVYMSGLFLFAAVAVVAHLATYIWRPWFG | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 5592
Sequence Length: 50
Subcellular Location: Cell inner membrane
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Q9SYW8 | MASSLCASSAIAAISSPSFLGGKKLRLKKKLTVPAVSRPDASVRAVAADPDRPIWFPGSTPPEWLDGSLPGDFGFDPLGLSSDPDSLKWNVQAEIVHCRWAMLGAAGIFIPEFLTKIGILNTPSWYTAGEQEYFTDKTTLFVVELILIGWAEGRRWADIIKPGSVNTDPVFPNNKLTGTDVGYPGGLWFDPLGWGSGSPAKLKELRTKEIKNGRLAMLAVMGAWFQHIYTGTGPIDNLFAHLADPGHATIFAAFTPK | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated, here photosystem I.
PTM: Photoregulated by reversible phosphorylation of its threonine residues.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27755
Sequence Length: 257
Domain: The N-terminus of the protein extends into the stroma where it is involved with adhesion of granal membranes and post-translational modifications; both are believed to mediate the distribution of excitation energy between photosystems I and II.
Subcellular Location: Plastid
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Q9SY97 | MAAQALVSSSLTSSVQTARQIFGSKPVASASQKKSSFVVKAAATPPVKQGANRPLWFASSQSLSYLDGSLPGDYGFDPLGLSDPEGTGGFIEPRWLAYGEIINGRFAMLGAAGAIAPEILGKAGLIPAETALPWFQTGVIPPAGTYTYWADNYTLFVLEMALMGFAEHRRLQDWYNPGSMGKQYFLGLEKGLAGSGNPAYPGGPFFNPLGFGKDEKSLKELKLKEVKNGRLAMLAILGYFIQGLVTGVGPYQNLLDHLADPVNNNVLTSLKFH | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated, here photosystem I.
PTM: Photoregulated by reversible phosphorylation of its threonine residues.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29181
Sequence Length: 273
Domain: The N-terminus of the protein extends into the stroma where it is involved with adhesion of granal membranes and post-translational modifications; both are believed to mediate the distribution of excitation energy between photosystems I and II.
Subcellular Location: Plastid
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Q9C639 | MAVVLRGGITGGFLHHRRDASSVITRRISSVKAAGGGINPTVAVERATWLPGLNPPPYLDGNLAGDYGFDPLGLGEDPESLKWYVQAELVHSRFAMLGVAGILFTDLLRTTGIRNLPVWYEAGAVKFDFASTKTLIVVQFLLMGFAETKRYMDFVSPGSQAKEGSFFFGLEAALEGLEPGYPGGPLLNPLGLAKDVQNAHDWKLKEIKNGRLAMMAMLGFFVQASVTHTGPIDNLVEHLSNPWHKTIIQTLFTSTS | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated . Seems involved in the function of the photosystem I in low light conditions, when other LHCA proteins are less abundant . Required, together with LHCA6, for the formation of a full-size NAD(P)H dehydrogenase-photosystem I supercomplex (NDH-PSI) that triggers cyclic and chlororespiratory electron transport in chloroplast thylakoids, especially under stress conditions (e.g. increased light intensity) (Probable) .
PTM: Photoregulated by reversible phosphorylation of its threonine residues.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27802
Sequence Length: 256
Domain: The N-terminus of the protein extends into the stroma where it is involved with adhesion of granal membranes and post-translational modifications; both are believed to mediate the distribution of excitation energy between photosystems I and II.
Subcellular Location: Plastid
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Q8LCQ4 | MAFAIASALTSTLTLSTSRVQNPTQRRPHVASTSSTGGRLMRERLVVVRAGKEVSSVCEPLPPDRPLWFPGSSPPEWLDGSLPGDFGFDPLGLGSDPDTLKWFAQAELIHSRWAMLAVTGIIIPECLERLGFIENFSWYDAGSREYFADSTTLFVAQMVLMGWAEGRRWADLIKPGSVDIEPKYPHKVNPKPDVGYPGGLWFDFMMWGRGSPEPVMVLRTKEIKNGRLAMLAFLGFCFQATYTSQDPIENLMAHLADPGHCNVFSAFTSH | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. Seems involved in the function of the photosystem I in low light conditions, when other LHCA proteins are less abundant. Required, together with LHCA5, for the formation of a full-size NAD(P)H dehydrogenase-photosystem I supercomplex (NDH-PSI) that triggers cyclic and chlororespiratory electron transport in chloroplast thylakoids, especially under stress conditions (e.g. increased light intensity).
PTM: Photoregulated by reversible phosphorylation of its threonine residues.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29939
Sequence Length: 270
Domain: The N-terminus of the protein extends into the stroma where it is involved with adhesion of granal membranes and post-translational modifications; both are believed to mediate the distribution of excitation energy between photosystems I and II.
Subcellular Location: Plastid
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P29996 | MSRPEGRKNRGGREEVLEQWVSGRKKLEELERDLRKVKKKIKKLEDEHPWLGNIKGILGKKDKDGEGAPPAKRARTDQMEVDSGPRKRPSRGGFTDKERQDHRRRKALENKRKQLSAGGKNLSKEEEEELRRLTEEDERRERRIAGPQVGGVNPLEGGTRGAPGGGFVPSMQGVPESPFTRTGEGLDIRGSQGFPWDILFPADPPSSPQSCRPQ | Function: Following virus entry into host cell, provides nuclear import of HDV RNPs thanks to its nuclear localization signal. Needs co-infection with hepatitis B virus to provide surface proteins, otherwise there is no packaging or budding. Packages the HDV ribonucleoprotein in hepatitis B virus empty particles. Interacts with both HDV genomic RNA and cytoplasmic tail of HBsAg. May inhibit viral RNA replication.
PTM: Prenylated by host farnesyl-transferase in the cytoplasm prior to nucleus translocation.
Sequence Mass (Da): 24060
Sequence Length: 214
Subcellular Location: Virion
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P06181 | MAFKQLFAAISLALLLSAANAAAVIEKRATCSNGKTVGDASCCAWFDVLDDIQQNLFHGGQCGAEAHESIRLVFHDSIAISPAMEAQGKFGGGGADGSIMIFDDIETAFHPNIGLDEIVKLQKPFVQKHGVTPGDFIAFAGRVALSNCPGAPQMNFFTGRAPATQPAPDGLVPEPFHTVDQIINRVNDAGEFDELELVWMLSAHSVAAVNDVDPTVQGLPFDSTPGIFDSQFFVETQLRGTAFPGSGGNQGEVESPLPGEIRIQSDHTIARDSRTACEWQSFVNNQSKLVDDFQFIFLALTQLGQDPNAMTDCSDVIPQSKPIPGNLPFSFFPAGKTIKDVEQACAETPFPTLTTLPGPETSVQRIPPPPGA | Cofactor: Binds 2 calcium ions per subunit.
Function: Depolymerization of lignin. Catalyzes the C(alpha)-C(beta) cleavage of the propyl side chains of lignin.
Catalytic Activity: 1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + glycolaldehyde + guaiacol + H2O
Sequence Mass (Da): 39686
Sequence Length: 372
Pathway: Secondary metabolite metabolism; lignin degradation.
EC: 1.11.1.14
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P20011 | VTXPDGKNTATNA | Function: Depolymerization of lignin. Catalyzes the C(alpha)-C(beta) cleavage of the propyl side chains of lignin.
Catalytic Activity: 1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + glycolaldehyde + guaiacol + H2O
Sequence Mass (Da): 1300
Sequence Length: 13
Pathway: Secondary metabolite metabolism; lignin degradation.
EC: 1.11.1.14
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C1DIC2 | MQRRIAFSLLLLLPFASPALADSACPDWTAQRAAAELAALAERLRQWDVAYHRDGRSPVADELYDQARARLADWNRCFPGQADASPEPLAGSAGPLLHPVPHTGLAKLDEAAVRDWMATREDLWTQPKVDGVAVTLEYADGRLRRAISRGDGRHGQDWTARVRRLPALPRQLAERRRLILQGELYWRLPGHVQAEAGGRSARARVAGLLARDTLDDGDAAGIGLFVWDWPNGPADMRARLDGLERLGFAEARRYSRPVADFATARQWRERWYREPLPFASDGVVLRQGRRPPGERWRAEPPHWAVAWKYPLAQALAEVRAVRFRIGRSGRITPQLELQPVRLDDRQIRRVALGSLRRWRELDVRPGDQVAIRLAGQSIPQVDAVVWRAAERPALPSPDPAAHHALSCWRPLPGCEEQFLARLDWLGGRRGLDLRGVGRGTWEALLENGRLDDLLGWLELDEARLAELPGFGERSASLLAERFRAARRRPFPMWLRALGLPPAGEATLPPSWDELAGRGPEQWQREPGIGPGRARQLQAFFAHPEVQALRQRLRAAGVEGF | 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+m + AMP + beta-nicotinamide D-nucleotide.
Sequence Mass (Da): 62867
Sequence Length: 560
EC: 6.5.1.2
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Q1QXD7 | MSRRPVWIDGSDMRPAPLRTAAWLRACLLVGLSTLAMPGWASAPPCPQMTPEAMQNDYQALDARIARWDRAYYRQGQRLVDDGTYDSAKRRLAHWAECFPLLAKPSVNTHEPTGAKHHPVAQTGIAKLPDRDAVAGWVARQGDHPLWVQPKVDGVAVTLVYRHGRLAAAISRGDGVSGQDWYTKALHIAAIPSHLPADAPPLVILQGELYARRTAHRQSRDGTDGARARIAGLMARDTLTDREGSTIGLFVWAWPNGPDTMPERLETLAGWGFGDVAEMTHGVATAEDIAAWRQRWYRHALPFATDGVVVKRGDRPPGSDWQASPPDWAMAWKYPAREALARVDALEFSVGRTGRIAVVAELEPVLLGDKRVTRVSLGSLAHWRRTDVRPGDQVRLRLAGLTIPQLQEVVVRTRPRPQVDAPEADQYDRLSCLRFTPACRDQFLARLEWLGSDEGLDFPGIGPATWNQLVDAGLVKGLLDWRTLDTAALEALPGVGKKTARAWQRHFALADTRSAVRWLRALGVPAVPRQALTDALERYGMAGLGTLAPPDWRDYSGIGETRAMQLTRFFRDTDIRHWLASLESTRALQKQHGTNTRNEQKGDVRRVDVKQDNGTTWLPEQDSNLRPND | 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+m + AMP + beta-nicotinamide D-nucleotide.
Sequence Mass (Da): 69898
Sequence Length: 629
EC: 6.5.1.2
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Q8XD89 | MKVWMAILISILCWQSSVWAVCPAWSPARAQEEIFRLQQQIKQWDDDYWKEGKSEVEDGVYDQLSARLTQWQRCFVSEPRDVMMPPLNGAVMHPVAHTGVRKMADKNALSLWMRERSDLWVQPKVDGVAVTLVYRDGKLNKAISRGNGLKGEDWTQKVSLISAVPQTVSGPLANSTLQGEIFLQREGHIQQQMGGINARAKVAGLMMRQDDSDTLNSLGVFVWAWPDGPQLMTDRLKELATAGFTLTQRYTRAVKNADEVARVRNEWWKAKLPFVTDGVVVRGAKEPESRHWLPGQAEWLVAWKYQPVAQVAKVKAIQFAVGKSGKISVVASLAPVMLDDKKVQRVNIGSVRRWQEWDIAPGDQILVSLAGQGIPRIDDVVWRGAERTKPTPPENRFNSLTCYFASDVCQEQFISRLVWLGSKQVLGLDGIGEAGWRALHQTHRFEHIFSWLLLTPEQLQNTPGIAKSKSAQLWHRFNLARKQPFTRWVMAMGIPLTRAALNASDERSWSQLLFSTEQFWQQLPGTGSGRARQVIEWKENAQIKKLGSWLAAQQITGFEP | 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+m + AMP + beta-nicotinamide D-nucleotide.
Sequence Mass (Da): 63381
Sequence Length: 560
EC: 6.5.1.2
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P92186 | MSTVVSEGRNDGNNRYSPQDEVEDRLPDVVDNRLTENMRVPSFERLPSPTPRYFGSCKWFNVSKGYGFVIDDITGEDLFVHQSNLNMQGFRSLDEGERVSYYIQERSNGKGREAYAVSGEVEGQGLKGSRIHPLGRKKAVSLRCFRCGKFATHKAKSCPNVKTDAKVCYTCGSEEHVSSICPERRRKHRPEQVAAEEAEAARMAAEKSSPTTSDDDIREKNSNSSDE | Function: Heterochronic protein which controls the choice of stage specific cell fates . Regulates the timing of the second larval stage events (L2 events) in the hypodermis . May negatively regulate the larval to adult transition via the suppression of the microRNA (miRNA) let-7 during L3 . Through this regulatory role, controls the timing of the sexual maturation of the nervous system . Also has a role in the fox-1-sex-1-mediated determination of sexual fate . Plays a role in governing the developmental timing of male tail tip morphogenesis . Plays a role in controlling the seam cell number during larval stages . Plays a role in vulval development .
PTM: Cleavage by caspase ced-3 during larval development probably induces lin-28 degradation.
Sequence Mass (Da): 25465
Sequence Length: 227
Subcellular Location: Cytoplasm
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G5EDT1 | MPKRAADEPGTSTTDPFHEQSPFDAVLAGTETTDTICEEPPAKRIDLDIKQEFNGGVQSGGLIKNESELTQMTIKQETEGNINEARREEEDEEQDEDSRTSMPPALGEDDDYEEDDADSFIDKTNTPPPSQSFLEGCRAANLPNDIVTGAWETYNHAVQRVSLEGSESAWQLSAIYYYLLSKGIKRRGKTIRILIQPFPVSILTIANSFDISVAEMLDKTARFVEIIHSRKIRRYQEYIRRIQEGLAVSCVIFKKFCRIFCKIFEEIKVGSENCPSSHELFTVLWTSFLVMKSRMTVDDLISNYQLLFSILDQVYTEMCSMKEGIVHHLNQKFVEDLLENDCTIIRALCTQFGGSVLDARHFSDHTFKKMEKTGIPSTWNFQEFRDLIMNVPKTAYENYLLQRGSIDERIFIPSVEDFSKIFQSPDTYSVADILKVSYSGRRFRDAEFLTKISNNHCLEKLALGGKVASEKLVTQSKEQPRVPCVEYNLELGNYPDDLESNNQSLYNRLTKIIGSWKLENSKLEEVCGTMSDSPMATILLKSDEMTNKFERTLSAELGETINENIPKYHYNVRKELELVFLIFMEKIIVAELKKKVREEDLLNVIRREEFLDSVFCFCVELILVSNGYDRPFPWSAELCGVHPFMFHKVIDLMITHEKQLSRQMVQHFSRIEETVIEYFSWKSDSPLWPMVVRCPFAHFQEFGEDWADKLNSYSPIKFTPIKKPDDLRDELGRPIVPQNQTSRTLRIFLKRTYFTAARRLQDLTDRVSMGARAKSQCWSLFDYLLRNDTLIFMDRHLDQILLCCVFVIMKINESSMLFTEIMAQYRRQSANSLLVYRSVTVFQEQLNPENPQAVNTKETILERLEGPQKEKTTVDIIKYYNIEFRDRIKYIIGQIDSASDEDLMEMPVATESGLMPVRVYLTHKLSIQTLPKTKHGESKQERAIANLEKSGITIAMERSGD | Function: Key regulator of cell division which acts as a transcriptional repressor and negatively regulates cell cycle progression in its active unphosphorylated form, but allows cell cycle progression when phosphorylated . When unphosphorylated and in its active form, interacts with E2F transcription factors such as efl-1 to repress their transcriptional activity and negatively regulate the progression through the G1 phase of the cell cycle during postembryonic development . May furthermore act with cell cycle regulator cki-1 to negatively regulate cell cycle progression . Acts redundantly with lin-53, fzr-1 and lin-23 to control cell cycle progression by regulating the expression of G1 phase cyclins . In particular, negatively regulates the expression of the cyclin E homolog cye-1, which is essential for the G1/S phase transition . Regulates cell division in the intestinal lineage, repressing the expression of genes such as cdc-25.2, which are required for intestinal cells to transition from the karyokinesis cell cycle (also known as nuclear division) to endoreplication, a specific growth pathway in the intestinal epithelium required for feeding and gut development in growing larvae during the L1 stage molt . Its role as a transcriptional repressor in the regulation of intestinal cell division during postembryonic development is most likely in complex with an E2F cell cycle regulatory transcription factor efl-1 and its binding partner the synthetic multivulva class B protein dpl-1 . Synthetic multivulva (synMuv) class B protein . SynMuv proteins are required to repress the induction of vulval development by Ras signaling and probably act by forming the multiprotein DRM complex that represses transcription . Together with synMuv class B protein lin-53, and redundantly with synMuv class A protein lin-15A, represses transcription to control vulval development, most likely through antagonization of the Ras-signaling pathway in the major hypodermal syncytium hyp7 . Acts redundantly with the transcriptional corepressor spr-1 and the zinc finger protein zfp-2 to play a role in vulval morphogenesis, promote germline proliferation and somatic gonad development . Acts redundantly with ubc-18 in the regulation of pharyngeal morphogenesis during embryonic develpment by negatively regulating the expression of proteins such as sup-35 . Functions with the SWI/SNF complex and proteins such as pha-1 to regulate larval development . Functions redundantly with xnp-1 to regulate somatic gonad development . Acts redundantly with slr-2 to regulate the expression of intestinal genes required for nutrient utilization . Regulates transcription in response to starvation . Furthermore, in response to starvation, promotes germ cell programmed cell death by negatively regulating the expression of the anti-apoptotic protein ced-9 . Conversely, in conjunction with mcd-1, efl-1 and the synthetic multivulva class B proteins dpl-1, lin-37 and lin-52, may also regulate transcription to promote programmed cell death independently of ced-1, ced-8 and ced-9 cell death pathways . Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation . In particular, negatively regulates the expression of mes-4, a histone methyltransferase that controls the expression of germline specific genes . May play a role in double strand break formation during meiosis . May suppress sensitivity to RNAi . May play a role in the response to endoplasmic reticulum (ER) stress .
PTM: Phosphorylated by the cyclin dependent kinase cdk-4. Phosphorylation inhibits the transcriptional repressor activity of lin-35 and allows for progression through the G1 phase of the cell cycle during postembryonic development.
Sequence Mass (Da): 110903
Sequence Length: 961
Subcellular Location: Nucleus
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Q03345 | MRKMLLFCILLLFMPQFTVSESCLPSWFRQERSAPEQLQSAENAAENSGSVPPDTSRNSLETNEIGDAPSSTSTPETPTETTISEAGDDEKRTEEVAKELIEKEAEYEGEYEDEKVDEEVEEALKYNEDATQDATSTLKPAVRKEIEKLKEAKCKDYCHHNATCHVEVIFREDRVSAVVPSCHCPQGWEGTRCDRHYVQAFYAPINGRYNVRLSTMSSTAQLLVQQSSTSAIPAFAFLIVMLIMFITIVVYAYRRMSKRSDDMTYTMSHMCPPEAFNVLKTPNGRHIPVHQIPSCSYTIPTPGTVPPNISSTPGSRIPTRQQAIRNNEQARNNFFSILRSQGTIPSRSINDDDTPKHYKSVPRVEVSAINYSGHIDFSTVSYQSTESEVSKASVTCPPPAHTVINIELDSADTNFRSPSRSSGEQGSPATCEPMIRHT | Function: Probable ligand for tyrosine kinase receptor let-23. Essential for vulval induction, where it acts downstream of the synthetic multivulva (synMuv) class genes . Probably by activating let-23, phospholipase plc-3 and inositol 1,4,5-trisphosphate receptor itr-1 signaling cascade, plays a role in ovulation by promoting gonadal sheath cell contractions and spermatheca dilatation during ovulation . Probably by regulating neuronal transmission in ALA neurons, mediates the decrease in pharyngeal pumping and locomotion during the quiescent state that precedes each larval molt, by activating receptor lin-23-mediated signaling cascade .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 48924
Sequence Length: 438
Subcellular Location: Membrane
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Q1II13 | MAPELIQIDLEPRKPAPKPSWLRAKAPMGENYHDLKKLARGMNLHTVCESAQCPNIGECWNHKTATFMLLGNLCTRRCGFCAVPKGRPEPIDFDEPRRVAEAVATLGLNFAVVTSVNRDDDNVGAAQVFAQTIEQIREQKPGCRVEVLIPDFQGNDESLRIVLAAKPEILNHNTETVPRLYRAVRSGARYERTLNLLRRAKEINPAQVTKTGVMVGLGETTEELLHVYRDLARQNVDILTIGQYLRPSKDHAPMTRYYTPEEFLFMKEEAMKMGFRHVESGPLVRSSYHAHEQANSTKQPLVTI | 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, thereby converting the octanoylated domains into lipoylated derivatives.
Catalytic Activity: [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 34312
Sequence Length: 304
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.8.1.8
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B0CQH8 | MPTLLRILRPPRSPFTRCLATFATPSSSGSSSRSKFTESLETGPGLDDFISEEVPDRVVLGNTKGPRLPSYLKTSIPSGASFNKIKKDLRGLGLHTVCEEARCPNIGDCWGGKPGATEAEGRSAATATIMLMGDTCTRGCRFCSVKTSRTPPPLDPHEPENTAEAISRWGLGYIVLTSVDRDDLLDGGAHHFAETIRKIKYKAPQILVEALTGDFAGSLDHVSIVAQSGLDVYAHNIETVEELTPFVRDRRATFRQSLKVLEHAKKSGVRITKTSIMLGVGETKEQVLAALKELRKIDVDVVTFGQYMRPTKRHMKVDRYVEPAEFDNWKEVAENLGFLYVASGPLVRSSYKAGEFYIENVLRGKNKAIGGLGISQLEGSEKGSMTGIDR | 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, thereby converting the octanoylated domains into lipoylated derivatives.
Catalytic Activity: [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 42676
Sequence Length: 390
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.
Subcellular Location: Mitochondrion
EC: 2.8.1.8
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Q1AT13 | MRHRWEDRPVAPPPDGRPTEYLPFRQERGRHGRPGWLKARVPDGPGYREIKETMRGLSLHTVCEEARCPNIGECWNNRTATFMILGNVCTRSCGFCAVLTGRPQELDLEEPYRVADAVKKMGLRHAVITSVNRDELPDGGASVFAATIRAIRREVPGCAVEVLTPDFKGDRDAIKTVIDARPDTFNHNIETVPRLYPAVRPQAKYGRSLEVLRYAKELDPGVLTKSGFMVGLGEVEEEIVRTMRDLREHGVDILTIGQYLRPTENHLPMARYYTPQEFARYKKLGLEMGFSHVESGPLVRSSYHAHEQTEDARRGALGARG | 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, thereby converting the octanoylated domains into lipoylated derivatives.
Catalytic Activity: [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 36215
Sequence Length: 321
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.8.1.8
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Q1GGW2 | MRDLKIPEQRHPEKAHRPDNAQPKKPSWIRVKAPGGKGYAETHKIMRENNLVTVCEEAGCPNVGECWSQGHATMMIMGEICTRGCTFCNIATGRPDTLDAFEPGRVAHAVQKLGLNHVVITSVDRDDLEDGGADHFAQTIRAVRHRSPQTTIEILTPDFLKCAPEVLETVVEAKPDVFNHNLETVPGLYPEVRPGARYFHSLRLLQRVKELDPSIFTKSGIMVGLGEQAPQVKQVMDDMRAADVDFLTIGQYLQPTPKHHAVDRFVTPEEFESYEKAAYGKGFLMVSATPLTRSSYHAGDDFAKLRAARNAKLGLA | 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, thereby converting the octanoylated domains into lipoylated derivatives.
Catalytic Activity: [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 35106
Sequence Length: 316
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.8.1.8
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A4XHV1 | MKLNVCYLEMVEYEDALHLQERLHKLRVANELEDTLLLLQHPPVITIGRRGKWENILISKEKLLQMGVKVFEVTRGGDVTYHGPGQIVGYPIFDLGTVGKDIKRFVWLLEEVFINLLKDEYGIEAYRDEKQYTGVWVGGEKIVAIGIAVKKWITMHGFAFNVNTNLEHFSWIIPCGLKDRGVTSLEKLLGHKVEFDDVVYKVAKYFGKVFGAKFRFISKEDLEEIIKIKVEDSER | 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] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 27131
Sequence Length: 235
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
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Q9A6B8 | MRRDDAAPVGWAVSTQPVPYPAAVAAMEARAAAIADGTAGELIWLLEHPPLYTAGVSAKAGDLIQPDRFPVFESGRGGQFTYHGPGQRVAYVMLDLTQRGRDVRAFVAALEAWIIDALAAFNVTGELREGRVGVWVERKGAGWSREDKIAAIGVKLRRWVSFHGISLNVEPDLSHFSGIVPCGQTEHGVTSLVDLGLPVTLDDADAALRASFSKVFGPVEDAEAPV | 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] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 24156
Sequence Length: 226
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
|
B3PKN9 | MALLPLLDVINLGRQPYEQSWQAMTAFTNQRTPDTPDQLWLVEHPPVFTQGQAGKAEHLLFPGDIPVVQTDRGGQVTYHGPGQLVAYPLLDLRRLKMGVRDLVTAIEQTIVATLAEYGIESYPKPDAPGVYVENHKIASLGLRVRRGCSFHGLALNVDMDLSPFLRINPCGYQGLAMTQMRDLMPETPSLVQVQEQLVCQFARKLGYETCTMRAN | 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] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 23976
Sequence Length: 215
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
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A9WKF8 | MRTLTVHYLGQIAYTAAWDIQRQLAAERSRGQIGDTLLLLEHPPTITLGNKARPDHVLASPAELAARGVAVVQSDRGGEVTYHAPGQLVAYPIFKLSQHGSDVGRYVRGLEESVIRVLAGYGLVGERVAGLTGVWVRNGAAKICAIGVKLSASGVTTHGLALNVDPDLSGFDLIVPCGITDRSVTSLAFELGQAPALAEVAERLIAQIGEVFALEPRVEALAM | 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] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 23581
Sequence Length: 223
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
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B8G783 | MRTLTVYHLGHIDYTAAWEMQRRLARQRSSGQIGDTLLLLEHPPTITLGNKARPEHIVATPAELAARGVVVVQSDRGGEVTYHAPGQLVAYPIFKLSQHGSDVGRYVRGLEESVIRVLAGYGITGERVNGLTGVWVRGGAAKICAIGVKLSASGVTTHGLALNVDPDLSGFELIVPCGISDRGVTSLAVELGKAPPMAEVADRLIASLCAIFDLRPVNALS | 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] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 23451
Sequence Length: 221
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
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Q7NTG0 | MPRIIKHLGRVDYEPTWRAMQAFTDSRGAETRDELWVVEHPPVFTQGLAGKPEHLLQQNDVPVVKTDRGGQITYHGPGQLVVYLLVDFKRMHVGVRELVRRIEQAIIDMLAEQGIAANGDVDAPGVYVDGAKIASLGLRIKNGATYHGLSLNVDMDLTPFSWINPCGYANLKVTQMKNLGVNLTVAEAADKLLPHLERHLSTSKETA | 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] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 22913
Sequence Length: 207
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
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A5MZJ0 | MRKCYVKEFHKLISYSEGIEIQQKAFDFVIRNNIDGILLLLQHKPVITIGKSGGKNNILASKYELDKYSIDLCHTSRGGNVTYHGPGQLVGYPILNLNNFQKDIHLYLRQLELILINTVREYGIKAGIKPKYTGVWVGDRKIAAIGVGIRKWITRHGFAINISVNKEHFKLIVPCGIKEFGVCSLEDFTANVDYNDVVQKIENNFKMIFETDLIKEETVDNLFERSNLNLRIT | 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] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 26660
Sequence Length: 233
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
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C3PHK5 | MTAPREPFFPVDRSIRASDEPLEIRRLGRMGYQEAWDLQAEIAAARAAGTQGDVILVVEHPNVYTAGKRTQPEDMPDNGLPVIDVDRGGRITWHGEGQLVVYPIIKLAEPVDVVDYVRRLEEAIIQAVRELGVSTAGRIDGRSGVWVPSTTQAADPAAPKRDRKLGALGIRVTRGVTMHGLALNCTNTLEYYEHIVACGIDDADVSTLSLELGREVTMEEAEAPLLDALLKALSGELTVADHTFASAPDPIKVANEKARQARKAAQEK | 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] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 29135
Sequence Length: 268
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
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Q73YJ7 | MIDSIRSSRALIDVRRLGTVDYRAAWQQQRDLADARVAGGPDTLLLLQHPAVYTAGRRTEPHERPLDGTPVVDTDRGGKITWHGPGQLVGYPIIGLAEPLDVVDYVRRLEEALIKVCADLGLDTVRVPGRSGVWVPGDAGRPDRKVAAIGVRVSRATTLHGFALNCDCELGAFNAIVPCGISDAGVTSLTAELRRPVAVDDVVTSVADAVCDALDGVLPVREHSPGARVASAM | 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] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 24767
Sequence Length: 233
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
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Q9X6X4 | MNTITVYRLGRVEYEDGLALMHLFSESRRQGLSGDVLLLLEHPPILTLGRAAKRENIVASDAQLAKEGAEVFETNRGGDVTYHGPGQLVGYPIFLLPEDRRDVRRYVRDVERSVMQVLAQWGITAGPIPKWPGVWIGAEGAPDARKIAAIGVHLSRWLTTHGFALNVNTNLDHFQLIVPCGIREAGVTSMQRELGRALPMAEVEEAIANSFCTVFDSERVDAPPPMRTVSIAVVKGRGPEARVLLVRRRPERGGFWQVLTGRLEAGESPAQAAARELEEETGLRVPLVDLDYRHAFALGEALPPQLVEENGFAVHVPPDADVRLGAEHDAFEWVDVPTALERLPFQGLRETVKRATA | 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 (By similarity).
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 39373
Sequence Length: 357
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
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Q9JUC7 | MKIIHKGLVEYLPTFEAMKTFNAGRNADTEDELWVVEHPPVFTQGLVGKPEHLLIRDDIPVVQIDRGGQITYHGPGQLVVYTMIDFKRRKTSVRNIVSALENSIIATLAEYGIEAAADPKRPGVYVGERKIASLGLRIKNGSVYHGLALNVNMDLSPFTHINPCGYAGMEMTQIADFVQPCPTPDEVAAKLTAHLETQFTPKADNNE | 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] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 22869
Sequence Length: 207
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
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Q2GEU6 | MEWKIDKDCVDYQMSLMFMQERVKQVINGSGDELVWMLQYEALYTGGTSADPQDLLNSDLFPVFNVGRGGKYTYHGPGQRVIYPILNLRSRNICDLHKYIYLLEEVVIVTLDNFGINGCRKEGHIGVWVGTGCQPPKKIAAIGVRVSKWVSYHGIAVNLYPDLSHYDAIIPCGIKNFGVTSAKEMGIEIRSFNAFDRYFKKSFVKIFGE | 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] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 23718
Sequence Length: 209
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
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Q8D326 | MNKVNFRILGLQKYQDIYYIMQKFITCLKKNNINEIWLLEHYPVFTQGNSDNFNKKYIFNIPVVKTDRGGHMTFHGPGQKIIYFLLNIKNLNIKISKLIFYLENIIISTLSYFKINSYSIKNSPGVYVDKKKICSIGLRIKDGYSLHGLALNVDMDLYPFSHIHPCGDKNIKMTQIRDLISNINLEKLNTQIINNCKKFLMMNNFEINFLNSIKIF | 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] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 25348
Sequence Length: 216
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.181
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Q06005 | MSRCIRQSVCTNFNVCRRQCFSTYASALKEMTHPIKPSAQTLRHLQFTQRIPFQKGLEIQETLVRANLDIKDIQSKIERKLIQLDEEYKGTATINDNEKRILDKVMAMKPNPIILTFEFEPTYTGGKRIKKTMTPDQIAAYESFIPETQKDNPRPKFVQVERGGQVTFHGPGQIVIYIILDLKTFQSFPAKCLVSCIEQATIRTLKNTKMCDDTDKPLNLDAMTTKDTGVWVENGKKKVASVGIHVRRSITSHGVAINVNTDLSYMNSFEMCGLKNTLTTSIMEQRPDAVVNVQSVAISFVKEMTKLLGIKTLERMQIDDVNILKKNP | 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 (By similarity).
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Mass (Da): 37237
Sequence Length: 328
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Subcellular Location: Mitochondrion
EC: 2.3.1.181
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A6NI73 | MAPWSHPSAQLQPVGGDAVSPALMVLLCLGLSLGPRTHVQAGNLSKATLWAEPGSVISRGNSVTIRCQGTLEAQEYRLVKEGSPEPWDTQNPLEPKNKARFSIPSMTEHHAGRYRCYYYSPAGWSEPSDPLELVVTGFYNKPTLSALPSPVVTSGENVTLQCGSRLRFDRFILTEEGDHKLSWTLDSQLTPSGQFQALFPVGPVTPSHRWMLRCYGSRRHILQVWSEPSDLLEIPVSGAADNLSPSQNKSDSGTASHLQDYAVENLIRMGMAGLILVVLGILIFQDWHSQRSPQAAAGR | Function: May play a role in triggering innate immune responses. Does not seem to play a role for any class I MHC antigen recognition.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 32755
Sequence Length: 299
Subcellular Location: Cell membrane
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Q8NHL6 | MTPILTVLICLGLSLGPRTHVQAGHLPKPTLWAEPGSVITQGSPVTLRCQGGQETQEYRLYREKKTALWITRIPQELVKKGQFPIPSITWEHAGRYRCYYGSDTAGRSESSDPLELVVTGAYIKPTLSAQPSPVVNSGGNVILQCDSQVAFDGFSLCKEGEDEHPQCLNSQPHARGSSRAIFSVGPVSPSRRWWYRCYAYDSNSPYEWSLPSDLLELLVLGVSKKPSLSVQPGPIVAPEETLTLQCGSDAGYNRFVLYKDGERDFLQLAGAQPQAGLSQANFTLGPVSRSYGGQYRCYGAHNLSSEWSAPSDPLDILIAGQFYDRVSLSVQPGPTVASGENVTLLCQSQGWMQTFLLTKEGAADDPWRLRSTYQSQKYQAEFPMGPVTSAHAGTYRCYGSQSSKPYLLTHPSDPLELVVSGPSGGPSSPTTGPTSTSGPEDQPLTPTGSDPQSGLGRHLGVVIGILVAVILLLLLLLLLFLILRHRRQGKHWTSTQRKADFQHPAGAVGPEPTDRGLQWRSSPAADAQEENLYAAVKHTQPEDGVEMDTRSPHDEDPQAVTYAEVKHSRPRREMASPPSPLSGEFLDTKDRQAEEDRQMDTEAAASEAPQDVTYAQLHSLTLRREATEPPPSQEGPSPAVPSIYATLAIH | Function: Receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C, HLA-G and HLA-F alleles . Receptor for H301/UL18, a human cytomegalovirus class I MHC homolog. Ligand binding results in inhibitory signals and down-regulation of the immune response. Engagement of LILRB1 present on natural killer cells or T-cells by class I MHC molecules protects the target cells from lysis. Interaction with HLA-B or HLA-E leads to inhibition of FCER1A signaling and serotonin release. Inhibits FCGR1A-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions . Recognizes HLA-G in complex with B2M/beta-2 microglobulin and a nonamer self-peptide . Upon interaction with peptide-bound HLA-G-B2M complex, triggers secretion of growth-promoting factors by decidual NK cells . Reprograms B cells toward an immune suppressive phenotype .
PTM: Phosphorylated on tyrosine residues. Dephosphorylated by PTPN6.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 70819
Sequence Length: 650
Domain: Contains 4 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases.
Subcellular Location: Cell membrane
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Q8N423 | MTPIVTVLICLGLSLGPRTRVQTGTIPKPTLWAEPDSVITQGSPVTLSCQGSLEAQEYRLYREKKSASWITRIRPELVKNGQFHIPSITWEHTGRYGCQYYSRARWSELSDPLVLVMTGAYPKPTLSAQPSPVVTSGGRVTLQCESQVAFGGFILCKEGEDEHPQCLNSQPHARGSSRAIFSVGPVSPNRRWSHRCYGYDLNSPYVWSSPSDLLELLVPGVSKKPSLSVQPGPVMAPGESLTLQCVSDVGYDRFVLYKEGERDLRQLPGRQPQAGLSQANFTLGPVSRSYGGQYRCYGAHNLSSECSAPSDPLDILITGQIRGTPFISVQPGPTVASGENVTLLCQSWRQFHTFLLTKAGAADAPLRLRSIHEYPKYQAEFPMSPVTSAHAGTYRCYGSLNSDPYLLSHPSEPLELVVSGPSMGSSPPPTGPISTPGPEDQPLTPTGSDPQSGLGRHLGVVIGILVAVVLLLLLLLLLFLILRHRRQGKHWTSTQRKADFQHPAGAVGPEPTDRGLQWRSSPAADAQEENLYAAVKDTQPEDGVEMDTRAAASEAPQDVTYAQLHSLTLRRKATEPPPSQEREPPAEPSIYATLAIH | Function: Receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C, HLA-G and HLA-F alleles . Involved in the down-regulation of the immune response and the development of tolerance. Recognizes HLA-G in complex with B2M/beta-2 microglobulin and a nonamer self-peptide (peptide-bound HLA-G-B2M) triggering differentiation of type 1 regulatory T cells and myeloid-derived suppressor cells, both of which actively maintain maternal-fetal tolerance . Competes with CD8A for binding to class I MHC antigens. Inhibits FCGR1A-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions .
PTM: Phosphorylated on tyrosine residues. Dephosphorylated by PTPN6.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 65005
Sequence Length: 597
Domain: Contains 3 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases.
Subcellular Location: Cell membrane
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P97484 | MSCTFTALLRLGLTLSLWIPVLTGSLPKPILRVQPDSVVSRRTKVTFLCEETIGANEYRLYKDGKLYKTVTKNKQKPENKAEFSFSNVDLSNAGQYRCSYSTQYKSSGYSDLLELVVTGHYWTPSLLAQASPVVTSGGYVTLQCESWHNDHKFILTVEGPQKLSWTQDSQYNYSTRKYHALFSVGPVTPNQRWICRCYSYDRNRPYVWSPPSESVELLVSGNLQKPTIKAEPGSVITSKRAMTIWCQGNLDAEVYFLHNEKSQKTQSTQTLQEPGNKGKFFIPSVTLQHAGQYRCYCYGSAGWSQPSDTLELVVTGIYEYYEPRLSVLPSPVVTAGGNMTLHCASDFPYDKFILTKEDKKFGNSLDTEHISSSGQYRALFIIGPTTPTHTGAFRCYGYYKNAPQLWSVPSALQQILISGLSKKPSLLTHQGHILDPGMTLTLQCFSDINYDRFALHKVGGADIMQHSSQQTDTGFSVANFTLGYVSSSTGGQYRCYGAHNLSSEWSASSEPLDILITGQLPLTPSLSVQPNHTVHSGETVSLLCWSMDSVDTFILSKEGSAQQPLRLKSKSHDQQSQAEFSMSAVTSHLSGTYRCYGAQDSSFYLLSSASAPVELTVSGPIETSTPPPTMSMPLGGLHMYLKALIGVSVAFILFLFIFIFILLRRRHRGKFRKDVQKEKDLQLSSGAEEPITRKGELQKRPNPAAATQEESLYASVEDMQTEDGVELNSWTPPEEDPQGETYAQVKPSRLRKAGHVSPSVMSREQLNTEYEQAEEGQGANNQAAESGESQDVTYAQLCSRTLRQGAAASPLSQAGEAPEEPSVYATLAAARPEAVPKDMEQ | Function: May act as receptor for class I MHC antigens. Becomes activated upon coligation of LILRB3 and immune receptors, such as FCGR2B and the B-cell receptor. Down-regulates antigen-induced B-cell activation by recruiting phosphatases to its immunoreceptor tyrosine-based inhibitor motifs (ITIM).
PTM: Phosphorylated on tyrosine residues by LYN. Phosphorylation at Tyr-794 and Tyr-824 is important for interaction with PTPN6/SHP-1 and PTPN11/SHP-2.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 93054
Sequence Length: 841
Domain: Contains 3 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases, including PTPN6/SHP-1, resulting in the dephosphorylation of the downstream protein kinases SYK and BTK.
Subcellular Location: Cell membrane
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Q8NHJ6 | MIPTFTALLCLGLSLGPRTHMQAGPLPKPTLWAEPGSVISWGNSVTIWCQGTLEAREYRLDKEESPAPWDRQNPLEPKNKARFSIPSMTEDYAGRYRCYYRSPVGWSQPSDPLELVMTGAYSKPTLSALPSPLVTSGKSVTLLCQSRSPMDTFLLIKERAAHPLLHLRSEHGAQQHQAEFPMSPVTSVHGGTYRCFSSHGFSHYLLSHPSDPLELIVSGSLEDPRPSPTRSVSTAAGPEDQPLMPTGSVPHSGLRRHWEVLIGVLVVSILLLSLLLFLLLQHWRQGKHRTLAQRQADFQRPPGAAEPEPKDGGLQRRSSPAADVQGENFCAAVKNTQPEDGVEMDTRQSPHDEDPQAVTYAKVKHSRPRREMASPPSPLSGEFLDTKDRQAEEDRQMDTEAAASEAPQDVTYAQLHSFTLRQKATEPPPSQEGASPAEPSVYATLAIH | Function: Inhibitory receptor involved in the down-regulation of the immune response and the development of immune tolerance . Receptor for FN1 . Receptor for apolipoprotein APOE . Receptor for ALCAM/CD166 . Inhibits receptor-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions . Inhibits FCGR1A/CD64-mediated monocyte activation by inducing phosphatase-mediated down-regulation of the phosphorylation of multiple proteins including LCK, SYK, LAT and ERK, leading to a reduction in TNF production . This inhibition of monocyte activation occurs at least in part via binding to FN1 . Inhibits T cell proliferation, inducing anergy, suppressing the differentiation of IFNG-producing CD8+ cytoxic T cells and enhancing the generation of CD8+ T suppressor cells . Induces up-regulation of CD86 on dendritic cells . Interferes with TNFRSF5-signaling and NF-kappa-B up-regulation .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 49356
Sequence Length: 448
Domain: Contains 3 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases.
Subcellular Location: Cell membrane
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Q96500 | MQGALFIKPTILLPLPSSVSSPKLTFLLPHATKASRLSSLRSNNSSSSSSLTSDPNTVDYNSSILSVFPAEACEVISGYACSADIYPEVKLDTKPVSRPVASEPVDREYEEYNSPKTVFREEACDDLGGEFCEPDFQKDAN | Function: Thylakoid-determinant subunit of high molecular weight LFNRs-containing protein complexes.
PTM: May form interchain disulfide bonds with LFNR1 and LFNR2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15314
Sequence Length: 141
Subcellular Location: Plastid
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Q03200 | MQTAASSVVGLSAVLPAAVKGRSLQIQAPRRVALRVRAAAAAVAVEAAEVDYSSNISVFPMEACDLIGGEACNVQMYPEAKLSSSAAVAVSRAAAEEVDRDYLSYDEPTTVFPEEACDDLGGEFCKAT | Function: Thylakoid-determinant subunit of high molecular weight LFNRs-containing protein complexes.
PTM: May form interchain disulfide bonds with LFNR1 and LFNR2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13317
Sequence Length: 128
Subcellular Location: Plastid
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Q7RY30 | MSQILTSRQADELHRALIAYLTAANLPNTAAALREELNLSEEVFDPATAKKYEGLLEKKWTSVVRLQKKIMDLESRNHILQSELDNATPTSRQNKDPVAWLPRAPPRHTLQSHRDPITCVAFHPVFSSLASGSEDQTIKIWDWELGELERTIKGHTKAVLDVDYGGPRGNTLLASCSSDLTIKLWDPLDSYKNIRTLPGHDHSVSAVRFIPGSGNLLVSASRDKTLRIWDVSTGYCVKTLRGHAEWVRDVCPSLDGKYILSTSDDYTSRLWDVTITNPEPKVTLIGHEHVVLCCAIAPPAAYQNLAAMAGIKKPPATSSAEFMATGSRDKSIRLWDARGTCIKTLVGHDNWVRGLVFHPGGKYLLSVSDDKTLRCWDLTQEGKCVKTIGDAHGHFVQCIKWAPSVIKDASVNGDNGEPNGTPKKGGAAATPEAQIRCVIATGSVDLNVRIFAN | Function: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for nuclear migration during vegetative growth as well as development. Required for retrograde early endosome (EE) transport from the hyphal tip. Required for localization of dynein to the mitotic spindle poles. Recruits additional proteins to the dynein complex at SPBs.
Sequence Mass (Da): 49757
Sequence Length: 453
Domain: Dimerization mediated by the LisH domain may be required to activate dynein.
Subcellular Location: Cytoplasm
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C3K053 | MIISSASDYRAAAQRKLPRFLFDYIDGGAYAEHTMRANSSDLAEISLRQRILRNVDNLSLKTTVFGQELDMPVILSPVGLTGMYARRGEVQAAKAAANKGVPFCLSTVSVCPIEEVASQSARAIWFQLYVLKDRGFMRNALERAQAAGVTTLVFTVDMPTPGARYRDAHSGMSGPFAAQRRMLQAMTKPQWAFDVGLMGRPHDLGNISKYLGKPTHLEDYIGWLANNFDPSISWKDLEWIREFWKGPMIIKGILDPQDAKDAVSFGADGIVVSNHGGRQLDGVLSTAKALPPIADAVGDDLTVLVDSGIRSGLDVVRMLALGAKACLLGRASAYALAADGQNGVENLLDIFAKEMRVAMTLTGVTSIEQIDHTTLVGQRQ | Function: Catalyzes the conversion of L-lactate to pyruvate. Is coupled to the respiratory chain.
Catalytic Activity: (S)-lactate + A = AH2 + pyruvate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 41302
Sequence Length: 380
Subcellular Location: Cell inner membrane
EC: 1.1.-.-
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Q68DH5 | MSGAALGLEIVFVFFLALFLLHRYGDFKKQHRLVIIGTLLAWYLCFLIVFILPLDVSTTIYNRCKHAAANSSPPENSNITGLYATANPVPSQHPCFKPWSYIPDGIMPIFWRVVYWTSQFLTWILLPFMQSYARSGGFSITGKIKTALIENAIYYGTYLLIFGAFLIYVAVNPHLHLEWNQLQTIGIAAANTWGLFLLVLLLGYGLVEIPRSYWNGAKRGYLLMKTYFKAAKLMTEKADAEENLEDAMEEVRKVNESIKYNHPLRKCVDTILKKCPTEYQEKMGRNMDDYEDFDEKHSIYPSEKSLVKLHKQVIYSVQRHRRTQVQWQILLEQAFYLEDVAKNETSATHQFVHTFQSPEPENRFIQYFYNPTFEWYWECLLRPWFYKILAVVLSIFSVIVVWSECTFFSTTPVLSLFAVFIQLAEKTYNYIYIEIACFLSIFFLSICVYSTVFRIRVFNYYYLASHHQTDAYSLLFSGMLFCRLTPPLCLNFLGLTHMDSSISHKNTQPTAYTSIMGSMKVLSFIADGFYIYYPMLVVILCIATYFSLGTRCLNLLGFQQFMGDDDMTSDLVNEGKELIRKEKRKRQRQEEGENRRREWKERYGHNREDSTRNRNIHTDPKESNFSDVNTNRSAFKYTRANNRTERDRIELLQDAEPLDFNAETFTDDPLESESGRYQPGGRYLSMSRSDIFNDV | Function: Recruited to ligand-activated beta-2 adrenergic receptor/ADRB2, it negatively regulates the adrenergic receptor signaling pathway . May also regulate other G-protein coupled receptors including type-1 angiotensin II receptor/AGTR1 (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81172
Sequence Length: 695
Subcellular Location: Cell membrane
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Q9Y468 | MHLVAGDSPGSGPHLPATAFIIPASSATLGLPSSALDVSCFPREPIHVGAPEQVAGCEPVSATVLPQLSAGPASSSTSTVRLLEWTEAAAPPPGGGLRFRISEYKPLNMAGVEQPPSPELRQEGVTEYEDGGAPAGDGEAGPQQAEDHPQNPPEDPNQDPPEDDSTCQCQACGPHQAAGPDLGSSNDGCPQLFQERSVIVENSSGSTSASELLKPMKKRKRREYQSPSEEESEPEAMEKQEEGKDPEGQPTASTPESEEWSSSQPATGEKKECWSWESYLEEQKAITAPVSLFQDSQAVTHNKNGFKLGMKLEGIDPQHPSMYFILTVAEVCGYRLRLHFDGYSECHDFWVNANSPDIHPAGWFEKTGHKLQPPKGYKEEEFSWSQYLRSTRAQAAPKHLFVSQSHSPPPLGFQVGMKLEAVDRMNPSLVCVASVTDVVDSRFLVHFDNWDDTYDYWCDPSSPYIHPVGWCQKQGKPLTPPQDYPDPDNFCWEKYLEETGASAVPTWAFKVRPPHSFLVNMKLEAVDRRNPALIRVASVEDVEDHRIKIHFDGWSHGYDFWIDADHPDIHPAGWCSKTGHPLQPPLGPREPSSASPGGCPPLSYRSLPHTRTSKYSFHHRKCPTPGCDGSGHVTGKFTAHHCLSGCPLAERNQSRLKAELSDSEASARKKNLSGFSPRKKPRHHGRIGRPPKYRKIPQEDFQTLTPDVVHQSLFMSALSAHPDRSLSVCWEQHCKLLPGVAGISASTVAKWTIDEVFGFVQTLTGCEDQARLFKDEARIVRVTHVSGKTLVWTVAQLGDLVCSDHLQEGKGILETGVHSLLCSLPTHLLAKLSFASDSQY | Function: Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor by recognizing and binding mono- and dimethylated histone H1b/H1-4 at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condense chromatin and repress transcription. Recognizes and binds p53/TP53 monomethylated at 'Lys-382', leading to repress p53/TP53-target genes. Also recognizes and binds RB1/RB monomethylated at 'Lys-860'. Participates in the ETV6-mediated repression. Probably plays a role in cell proliferation. Overexpression induces multinucleated cells, suggesting that it is required to accomplish normal mitosis.
PTM: Ubiquitinated in a VCP/p97-dependent way following DNA damage, leading to its removal from DNA damage sites, promoting accessibility of H4K20me2 mark for DNA repair protein TP53BP1, which is then recruited to DNA damage sites.
Sequence Mass (Da): 92297
Sequence Length: 840
Domain: The MBT repeat 2 specifically recognizes and binds monomethylated and dimethylated proteins. In contrast, it does not bind trimethylated proteins. The MBT repeat 1 does not bind methylated peptides but inserts a proline ring in a Pro-Ser-Ser/Thr sequence context.
Subcellular Location: Nucleus
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