ids
stringlengths 6
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stringlengths 11
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stringlengths 108
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P21920 | MAGSLFDTSAMEKPRILILGGTTEARELARRLAEDVRYDTAISLAGRTADPRPQPVKTRIGGFGGADGLAHFVHDENIALLVDATHPFAARISHNAADAAQRTGVALIALRRPEWVPLPGDRWTAVDSVVEAVSALGDRRRRVFLAIGRQEAFHFEVAPQHSYVIRSVDPVTPPLNLPDQEAILATGPFAEADEAALLRSRQIDVIVAKNSGGSATYGKIAAARRLGIEVIMVERRKPADVPTVGSCDEALNRIAHWLAPA | Function: Catalyzes the reduction of the macrocycle of precorrin-6X into precorrin-6Y.
Catalytic Activity: NADP(+) + precorrin-6B = 2 H(+) + NADPH + precorrin-6A
Sequence Mass (Da): 28096
Sequence Length: 261
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 6/10.
EC: 1.3.1.54
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Q60E70 | MAVGGAGSSRSVAPCCCCAVLLAAALLFSAPATTEAYDALDPNGNITIKWDVMSWTPDGYVAVVTMFNYQQFRHIQAPGWQLGWTWAKKEVIWSMVGAQTTEQGDCSKFKGGTPHCCKKDPTVVDLLPGTPYNMQIANCCKAGVINTFNQDPSNAASSFQISVGLAGTTNKTVKLPKNFTLKAPGPGYTCGRAMIVRPTKFFTGDGRRATQALMTWNVTCTYSQFLAQKTPSCCVSLSSFYNDTIVNCPTCSCGCQNNGTSPGSCVNENSPYLQSAIDGPGKWTGQPLVQCTSHMCPIRIHWHVKLNYKEYWRVKITITNFNYRMNYTQWNLVAQHPNFNNITQLFSFNYKPLTPYGSKINDTAMFWGVKFYNDLLMQAGPLGNAQSELLLRKDSKDFTFDKGWAFPHRVYFNGDNCVMPPPDAYPWLPNASPLTKQPLTLSVLVFSIVLATLLAYA | Function: Involved in determining the orientation of cell expansion, probably by playing an important role in cellulose deposition. May act by recruiting cellulose synthesizing complexes to discrete positions on the cell surface (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 50443
Sequence Length: 457
Subcellular Location: Cell membrane
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A2XHZ9 | MELHRCSLLALLLAVTCSVAVAYDPLDPKGNITIKWDVISWTPDGYVAMVTMSNYQMYRQILAPGWTVGWSWAKKEVIWSIVGAQATEQGDCSKFKGGIPHSCKRTPAIVDLLPGVPYNQQIANCCKAGVVSAYGQDPAGSVSAFQVSVGLAGTTNKTVKLPTNFTLAGPGPGYTCGPATIVPSTVYLTPDRRRRTQALMTWTVTCTYSQQLASRYPTCCVSFSSFYNSTIVPCARCACGCGHDGYRGNGGGGKNARAGDGRSRRNSGGGGGHSGGTECIMGDSKRALSAGVNTPRKDGAPLLQCTSHMCPIRVHWHVKLNYKDYWRAKIAITNFNYRMNYTQWTLVAQHPNLNNVTEVFSFQYKPLLPYGNINDTGMFYGLKFYNDLLMEAGPFGNVQSEVLMRKDYNTFTFSQGWAFPRKIYFNGDECKMPPPDSYPYLPNSAPIGPPRSVAAAASAILVVLLLVA | Function: Involved in determining the orientation of cell expansion, probably by playing an important role in cellulose deposition. May act by recruiting cellulose synthesizing complexes to discrete positions on the cell surface.
Location Topology: Lipid-anchor
Sequence Mass (Da): 50960
Sequence Length: 468
Subcellular Location: Cell membrane
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Q7XR91 | MDVDQLILFVFVCCLSSRFADAYDPVDPNGNIIINWDFQSIENVYTVMVSVHNHQLYRHIEQPGWRLSWRWAGNEIIWGMTGAEATEQGDCHRIRGATRPHCCEKQPVIVDLPPGTPYNNQVSSCCRGGVLSSLTQNNRTSTAAFQMVVGGFRRATYHDGDRGPALPSRFGVGVPGYSCSNATKVNATSSERFLLPRARAPCAVTWQVTCTYSQFMEAASPTCCVSLSSFYNSTIVPCPRCSCGCPRSPTAPQCISEGEKPELPAGDGEAVAPVFRCTDHMCPVRVHWHVKISYREYWRVKVTITNYNQVKNYSDWNLVVQHPNLRSLTQLFSFNYQPLIEYGTLNDTGMFWGIQYYNEMMLQDGNVQTEMILKKDKSDFTFSGGWAFPRRVYFDGHECVMPPPDQYPLLPNGGPDSRVSAAQLIASSCLLLPFIFLIM | Function: Involved in determining the orientation of cell expansion, probably by playing an important role in cellulose deposition. May act by recruiting cellulose synthesizing complexes to discrete positions on the cell surface (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 49305
Sequence Length: 439
Subcellular Location: Cell membrane
|
A4XT57 | MIAPRIALQFLTRLPVSLPGMPTPEQIGRSLLWYPAVGLLLGLLLWLAHLLLGQTPDVLQAAIILALWVGLSGGLHLDGLADTADAWVGGFGDPGRTLAIMKDPRSGPIAVVVLVLLLLLKFAALLSLLQAGQGIYLVLLPWLGRSLLPLLLATTPYVRAGGLGQALVDHLPRRQLPWVLGGHVAAMLLLGWGALIALATALALFVWLRRALMQRLGGTTGDTAGALLELAECAALLALALSL | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25581
Sequence Length: 243
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell inner membrane
EC: 2.7.8.26
|
Q88M93 | MLPFWIALQFLSSLPVSLPGMPAPREVGRSLLYYPLVGLLFGLLLWLASHLLQGTPSPLHAALLLTLWVLLSGALHLDGLADSADAWLGGFGDRERTLRIMKDPRSGPIAVVTLVLVLLLKFCALWVLVGQGIGAQLLLAPLIGRAAMLGLFLCTPYVRPGGLGQALAEHMPRRAAGWVLLVCVLFCLFLGGWSVLLALAVFAWLRHLMCRRLGGTTGDTAGALLELLELAVVLGLALGL | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25651
Sequence Length: 240
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell inner membrane
EC: 2.7.8.26
|
Q885W4 | MLPFWIALQFLGSLPIRLPGMPRPAELGRSLLFYPLVGVVFGTLLLGFNALLSGAPLLLHAALLLSAWVLLSGGLHLDGLADSADAWLGGFGDRERTLNIMKDPRSGPIAVVTLVVVLLLKFAAIVALIESHNSIGLLLAPLIGRSAMLALFLGTPYVRSGGLGQALADHLPRSLGRKVLLVSTVACVVLAGWSGIAALLVCAVCFYWLRHMMMRRLGGSTGDTAGALLELLELAVVLTLALL | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25630
Sequence Length: 243
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell inner membrane
EC: 2.7.8.26
|
A1RUA0 | MRCLKAVVAFFTALPVGGAELDFSCIWATPYLAGLMVGGAGGAVYFLTHSPAAAYAALLLATGLHHLDGLADVGDALMVRDRERARRVLEDPRRGVGGIFAVVALFVLAASARPESWLDYIVTDLYSKALALVVAAYSKPFKEGLGSLFIVSAKRQWPAALPALAVAAWLHPAAFLAATVLSLFFYVAAYKHLGGANGDLLGALLEVTRALYLATVDLSTSLINGLF | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23939
Sequence Length: 227
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell membrane
EC: 2.7.8.26
|
Q8XWS4 | MMAALREACRSLWIAIGYFTRIPVPASVGFSQDGLNRAARFFPLVGWLVGAAGALAYWLASRTVPAPGVAVAASMAATLLLTGAFHEDGLADCADGFGGGYTAEDRLRIMRDSRIGAFGAIAVCMALLLKWQLLMAMAAQHAAAAMAAMVAAHAASRGMAVSYLLTHDYARMEGKAKPVAQPMGRRDAAWAALFGGLPLLGFGMACAAIAVAVLLAARWALGRYFTRRLGGITGDCLGLAQQVFELLVLWVLLAWTSS | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27124
Sequence Length: 258
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell inner membrane
EC: 2.7.8.26
|
Q98KP0 | MKLPNLTLSPRQILDDVALCLVFFTRLPLPDLDFRGRGLAAAIWAAPVAGLLVGLIGAIVFATAERFGLAMGPAAALALVATVIATGCLHEDGLSDVADGFGGGKSRGRKLDIMRDSRIGAYGAMALALSLLIRWNVLSELVDPTQALFALVAAHAASRGVLGAFMHLLPPARSDGLSAGAGAVSLETAIAGAVLGAIPLLLLGAGGAIAALILLGLLFAAFHALCLNQIGGQTGDTIGALQQVSEIAVLLVASVALSS | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26130
Sequence Length: 259
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Subcellular Location: Cell inner membrane
EC: 2.7.8.26
|
B4SH92 | MPEKLQLLLDRIKPASRSLSDAARAHLDDLTKPQGSLGRLEEIALKYVLATGNLSPLLSKKKICCFAADHGVAAEGVSAFPAEVTPQMVYNMLGGGAAINVLTRHAGVDLDVVDMGVNHDFPDLAGLVKRKVQPGSANMATGPAMSEEDALQALLCGAELAAEAQEAGYHLLGTGEMGIANTTPATALYAVLLDVSVESITGRGTGIDDERLLHKIAVIKQAIAVNGSRCTTPFATLAALGGYEIAAIAGFILGAAAARTPVVVDGFISSAGAVVALKLCPAVEDYLFFSHLSNEQGHRAVMEKLGARPILDLDLRLGEGTGAAIAMQLIEGAVKIYNEMATFSAARVSEKSGE | Function: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
Catalytic Activity: 5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate
Sequence Mass (Da): 36801
Sequence Length: 354
Pathway: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-ribazole from 5,6-dimethylbenzimidazole: step 1/2.
EC: 2.4.2.21
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B2RIR0 | MKTFNIKSPDQAIRQALIDRIDNLAKPEGSLGMLEELALQIGLIQQTLSPRLRNPHNIIFAADHGIADEGVSFSPKEVTWQVINNFLGGGAGINFLCRQHGFELVLVDGGIDFDFPEGLDIIDRKVRKGTRNYLYEAALTGEEMEQAVTAGAEVVSDCHHRGCNVVSFGEMGVANTSTSSMWMSFLTGIDLKDCVGAGSGLDSEGVRHKYNILKQAKENYKGNGSTEDVITYFGGLEMLMAVGGMLQAAELGMLIIVDGFIMTNCLLAASQFYPEVCDYAVFGHCGDESGHARLLEYMKAKPLLNLGLRLGEGSGAVCSYPIIVSAVSMINEMHTFAQAAVTKYF | Function: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
Catalytic Activity: 5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate
Sequence Mass (Da): 37394
Sequence Length: 345
Pathway: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-ribazole from 5,6-dimethylbenzimidazole: step 1/2.
EC: 2.4.2.21
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Q9I465 | MSLQWWRDTCREADPQMRRRAAERQDRLTKPRGSLGRLEQVAIDLAALQGRERPSLERIWVTVFAGDHGVVAEGISAYPQAVTGEMLRNFVRGGAAISVLARELGAGLEVVDLGTAFPLEALPGVRHLRLAAGTANFVEAPAMGAEECLLALEAGRESVRRAEQAGSQLFIGGEMGIGNTTAAAAMACALLDAPASALVGPGTGLDASGVAHKAAVIERALALHGAHRADPFETLRRLGGLEIAALAGAYLACAQKGMVALVDGYICSVAALCAVRLNPACRDWLLFAHSGAEPGHRHVLEALAAQPLLDLGLRLGEGSGAALAVPLLRQACALHAGMATFAEAAVSDRPA | Function: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
Catalytic Activity: 5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate
Sequence Mass (Da): 36531
Sequence Length: 351
Pathway: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-ribazole from 5,6-dimethylbenzimidazole: step 1/2.
EC: 2.4.2.21
|
Q8PVT6 | MIIFSGGTGTPKLLDGLKEILPEEELTVVVNTAEDLWVSGNLISPDLDTVLYLFSDQIDRKRWWGIENDTFGTYERMKELGIEEGLKLGDRDRATHIIRSNIIRDGASLTDSTVKLSSLFGIKANILPMSDDPVSTYIETAEGIMHFQDFWIGKRGEPDVRGVDIRGVSEASISPKVLEAFEKEENILIGPSNPITSIGPIISLPGMRELLKKKKVVAVSPIIGNAPVSGPAGKLMPACGIEVSSMGVAEYYQDFLDVFVFDERDRADEFAFERLGCHASRADTLMTSTEKSKELAEIVVQAF | Function: Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.
Catalytic Activity: (2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0
Sequence Mass (Da): 33357
Sequence Length: 303
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 2.7.8.28
|
O27097 | MWRQSMITVLSGGTGTPKLLQGLVRVVDPEEITVIVNTVENGYLSGVYVAPDVDTVLYTLAGIINEETWYGVEGDTFITHETLRELGCPELLRIGDRDRAFKIQKTLLLGEMPLHRAVEIQSRALGVESRVLPMSNEDSDIVIVTDEGDMEFHEFLVERRSEPGVLDVRFSRVKPAPGVLDAIESADMVILGPSNPVTSIGPIINMEGVTDSLRKVNVSAVSPFTGGRPFSGPAGKFMEAKGYDASSLGVAEIYADFLDRLVIDETDSDLKGEIEKLIKEVTITKTNMENIGDKIMLARILLGEIL | Function: Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.
Catalytic Activity: (2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0
Sequence Mass (Da): 33492
Sequence Length: 306
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 2.7.8.28
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Q3IRY6 | MVTFLAGGTGTPKLRYGAETVFDTADTPVVCNTGDDVELGGLVVCPDVDTVLFAAADRLDRETWWGIDGDTTETHEELRALADAADLDTGPRYLPDKKQTAGRDIARWRRFSGVAEFMEIGDTDRAVHITRTSLLDEGKRLTEATATLADALGVDHPVLPMSDDPVATLIDTDEGLVHFQEFWVHRRAEPTINGVEFRGADAAEPTPEVREALADPVVIGPSNPITSIGPMVALDGIRKALAETPVVAVSPFVEDRVFSGPADDLMAADGYAPSTAGVAEAYPFADAFVVDEADETPLERPTVRTDTELGSPADGERVCRAVREAFDRLGVEVA | Function: Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.
Catalytic Activity: (2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0
Sequence Mass (Da): 35792
Sequence Length: 334
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 2.7.8.28
|
O28028 | MRVEVFPVEGLPLIKEGDDLAELISSRVRFEDGDVLVVCSTVISKAEGRIRRLEEFNPSERAKEIAARIGKPAEFVQAVLEESEEVLLDFPFLLVKAKFGNVCVNAGIDASNVEEGSLLLPPLDPDGSAEKLRRRILELTGKRVGVIITDTNGRCFRRGVVGFAIGISGVKAMKDWIGRKDLYGRELEVTVECVADEIAAFANLLMGEGGDGIPAVVVRGLNVAGEGSMEEIYRSEEEDVIRRCLKRCL | Cofactor: Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.
Function: Catalyzes the GTP-dependent successive addition of two L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2), with a gamma-linkage between the two glutamates. May be able to add up to four gamma-linked glutamates, since F420-4 is a species that was isolated from A.fulgidus.
Catalytic Activity: GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate
Sequence Mass (Da): 27261
Sequence Length: 249
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 6.3.2.31
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B9LPH6 | MELFAVPGLPEIRDGDDLAAMIDERVDLREGDVVVVASTVVSKAEGRTFDLSDFPASERAEAVADRLAEIAGEEKDPRFAQAVIEESTELIMEAPFLLTATRFGHIGVNAGIDQSNVPDGDLLLLPERPSESAARIREGIAADRVVVSDTCGRPFRHGQRGVAIGWAGLPASRDWRGERDRDGREMGVTVQNVIDELASAANLVAGEGDGGTPVVVVRDWEFGDHDGSDNHFREVEGDFVRQALRQWTFDD | Cofactor: Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.
Function: Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.
Catalytic Activity: GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate
Sequence Mass (Da): 27294
Sequence Length: 251
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 6.3.2.31
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Q5UZQ7 | MEVFAVEGVPEVRPGDDVAELLVEQADLQDDDVVCVASTIVSKANGRGRSLSSYEPSGRAERIAATIEDIADEEKDPRMAQAILDECEEVLVEAPFILGVTKFGHITVNAGIDRSNVPGADLLLLPEDPTAEAEAIRDGIREHAGVEPSVIVTDTSGRPFRLGQRGVALGWAGLSASRDWRGEHDRDGRELEATVQAVVDELAAAANLVTGEGDGGTPAAVVRDFDFGDHAGSEQLFRDPEKDVVRQALREWSHVRD | Cofactor: Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.
Function: Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.
Catalytic Activity: GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate
Sequence Mass (Da): 27600
Sequence Length: 257
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 6.3.2.31
|
Q8TUD3 | MKFEAIAVEKIPLIRKGDDLPYIICERIELQDRDIIVIASTIVAKAEGETFRLEDITPGEEALAIASRTGKDARFIQAVLSRSREVFVEAPFMLVTTLAGHTCVNAGVDESNIEHGFLLYPPKNPDSSASKLGERLESISGKKLSVIITDTNGRAFKIGQTGVAIGIYKIKPIKRWIGEKDLFDKVLEITEEAVADELAGAANLLMGEGAGGIPVAVIRGLDYYCEEEISMSENYRPEDMDVIKKGLRCLQKKN | Cofactor: Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.
Function: Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.
Catalytic Activity: GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate
Sequence Mass (Da): 27899
Sequence Length: 254
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 6.3.2.31
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Q58178 | MIKEKRKVEVIGLELPIFKGGEQINLSELIAQYPIEDGDIIVIAETLISKLEGGVIDRDKIIPSKEAIELAKKTGKDPKVVQVILDEAKEIVKVGKNFIITETKHGFVCANSGVDESNIYKGIKILPKNPDESAEKIRKEIEKLTGKRVGVIISDSVGRPFRKGAVGIAIGVSGILALWDRKGEKDLFGRELKTTEVAIADELASMANVVMGEADEGIPVVIIRGANVPFGNGKGRDLIRPKEEDVFRN | Cofactor: Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.
Function: Catalyzes the GTP-dependent successive addition of two L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2), with a gamma-linkage between the two glutamates. Cannot use F420-2 as substrate to add more glutamates. Exhibits maximum activity with GTP, compared with UTP (66%) and dGTP (25%); with ATP, only F420-1 is observed as the product; CTP and TTP support no activity.
Catalytic Activity: GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate
Sequence Mass (Da): 27148
Sequence Length: 249
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 6.3.2.31
|
Q8TWR1 | MGGLPTLRIEPVPLERKVRPGDDLAELIAESAELEEGDVLAIAHTVVSKAEGALISLDEIEPSPFAKTLAERTGKDPRVVEVILREAESIVRVGPDFIITEVRGGMVCANAGVDESNAPPGYVIVLPEDPDRSARELRRRLRELVGVDVGVIITDTQGRPFREGVVGVAIGASGVPVLADRRGDRDLYGRELKITIVALGDLLASAAELVMGQADEGTPAVIFRGLKPELERFEGPRKARAIIRSPSRDIFR | Cofactor: Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.
Function: Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.
Catalytic Activity: GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate
Sequence Mass (Da): 27135
Sequence Length: 252
Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 6.3.2.31
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O59705 | MTEKDADSGSDLVDAFLSDAYLNTEELRKDGPFSPDEFLVSKRFLGLDGLVNELSRLFEQVNNELMLLVKDNYQDFVHLGSRMKSGNTKVSTLISSIHRSEEQLKNSKQSLIGHSTEIQNNLKHKQDVENEKLIASNLLLLDQILKFLKSNDSSHPLWLESLNNAQRLCDTYKDHPWVQSISPTLINYIKH | Function: Required for normal Golgi morphology and function.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21829
Sequence Length: 191
Subcellular Location: Golgi apparatus membrane
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P53271 | MDFLNDDELDLDLPVTAEISKELFATEIEKYRESETNGTDVDNFDVDRFLVQKNFHYLPLDSLIRDLSGLSQKMVQTLLEQIRSNYDDYLTFSNTYTDEENETLINLEKTQSDLQKFMTQLDHLIKDDISNTQEIIKDVLEYLKKLDEIYGSLRNHSQLTEALSLGKRLSKSLHEMCGIEPLEEEICSGLIEQLYKLITASRRILESCADSNSPYIHHLRNDYQDLLQEFQISLKILTEKCLENPSSLQNLSLTLVSIIKTA | Function: Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events. COG2 is required for ER to Golgi vesicle docking. Not essential for viability.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30325
Sequence Length: 262
Subcellular Location: Golgi apparatus membrane
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F4HQ84 | MATKAASSSSLPKSGAISKGYNFASTWEQSAPLTEQQQAAIVSLSHAVAERPFPANLVHEHVHRPENGLSVSVEDTHLGDSGAIEAVLVNTNQFYKWFTDLESAMKSETEEKYRHYVSTLTERIQTCDNILHQVDETLDLFNELQLQHQGVTTKTKTLHDACDRLLMEKQKLMEFAEALRSKLNYFDELENVSSNFYSPNMNVSNSNFLPLLKRLDECISYIEDNPQYAESSVYLLKFRQLQSRALGMIRTYILAVLKTAASQVQAAFRGTGGNKTSVSEGVEASVIYVRFKAAANELKPVLEEIESRSARKEYVQILAECHRLYCEQRLSLVKGIVHQRVSDFAKKEALPSLTRSGCAYLMQVCHMEHQLFTHFFPASSEEVSSLAPLVDPLSTYLYDILRPKLIHEANIDLLCELVHILKVEVLGDQSARQSEPLAGLRPTLQRILADVNERLTFRARTYIRDEIANYTPSDEDLDYPAKLEGSPNTTSETDLRDDENADVFKTWYPPLEKTLSCLSKLYRCLEQAVFTGLAQEAVEVCSLSIQKASKLIIKRSTTMDGQLFLIKHLLILREQIAPFDIEFSVTHKELDFSHLLEHLRRILRGQASLFDWSRSTSLARTLSPRVLESQIDAKKELEKCLKTTCEEFIMSVTKLVVDPMLSFVTKVTAIKVALSSGTQNHKVDSVMAKPLKEQAFATPDKVVELVQKVYAAIQQELLPILAKMKLYLQNPSTRTILFKPIKTNIVEAHTQVESLLKAEYSAEEQANINMISIQDLQTQLDNFL | Function: Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking . Involved in pollen tube growth by modulating Golgi morphology and vesicle trafficking homeostasis leading to the deposition of cell wall components and proteins at the pollen tube tip . Required for sporophytic development .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 88609
Sequence Length: 784
Subcellular Location: Golgi apparatus membrane
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P34155 | IVGGTEVTPGEIPYQLSLQD | Function: This enzyme is a serine protease capable of degrading the native triple helix of collagen.
Catalytic Activity: Hydrolysis of proteins, with broad specificity for peptide bonds. Native collagen is cleaved about 75% of the length of the molecule from the N-terminus. Low activity on small molecule substrates of both trypsin and chymotrypsin.
Sequence Mass (Da): 2116
Sequence Length: 20
EC: 3.4.21.32
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Q54TT4 | MNNQTNQQSQTQSQSQQRINFDITGWEKKSKLSTQQYLLINNLNKSTQEKPLPQKYLEDKINNDIKKEENQQLQQQQQQQQQQQQQQQSPIIENFMDNFNPKTDIDNLSDFYQWYSIIDKNNPHLHQYEWFLETIVNYSKGSNQLLSMVENCDKLVESIQTDYSNLTKKTNQLNEDCEKFFNEELKLRYIAQSIHDKLKFYNQLEIQTKKFNTTNFNVTDSTFLTSLENLENSINFMKSNSTFMESNKYLTQYGFIFSRALGLIKDYISSNLKILSRDIINAQKQLKTSVSTPTSPQLQSSSGGSPLINDFSNSTDFNDLFQHSNIRFRAFAPKLRPLCLELEKRAIGPYLSYLYDTQNIYFNNRRSILSLIMFEKLQSLSKMTDISSMIRSSSLFMIQFYENEYQIYSNFFSPPDLNNNNNNNNNNNNNDNINNSTNINNSNNTNNNNQDIINNCPAFSNILDEYSQQLYDTIRPIYIHIHSFETLCNLAHLIRNELIDDLVQKSMKYSNGFKMTIERMLQDIQERLIFIIQTYIRDEIRSYHPNSDDLDYPNKLKIYVTAESTAVDGDGNGSGNSSPTLSYKSIYSTWYPTLEKSLTCLSKLYLVLETRIFEGLAQEVVEACTFTLIQASRLLLIQQKNDPYIILDSQLFLIKNLLTLREQIAPFDINFVIIEKIVDFPNLKHSLSTLYNVGSFLTLSTNNPILSLLSPRVTNTSIDSKKDLEKELKQSIESFILSNANTIIDPLLSLLTKISVFLNQSNKNQTDPMLLSQQSFADPQRIKEIIEQVKEKASNYLPQVIDRMKLYLSISTQILLMKPIRTNIIDSFDQINQYTKKYYTEDQIKIIDLQSLKLILDKILTPSKQSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNKNENNENENENNSNVNSPSPQQL | Function: Required for normal Golgi function.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 107427
Sequence Length: 925
Subcellular Location: Golgi apparatus membrane
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Q961G1 | MDDVERIQSENENLRKIRNRLMQWESKTDPLAALSIQQEEHLDVLTNLWRDSGPSAPAPTTPTQVGPTDSSAAATSQSGDDIRLPAEGLQNTNEFLLWFADVSAEIEQRGDADYHKYLQQLEQRKAECSHMLDQIAGAMERLGALCDEYDFVSQKTSALNTASEQLIEEQERLQELSHEIQRRLHYFSQVELLNQRLQSPTLSVASEAFRECLNKIDECLNYIEENPKFKDAAAYNVKYRQCLAKASGLVRNYVTSVINQATEATLHPKNNMPDASAALKAPDAAFALYYGKYQTAAAKVKRVAQLIESRSEHSLDYAQLMADLQQHYLAQRASVMSPAVNLSIQNVKVAHKGDHCSLTRSACAFLVHVCQDEQRLFYQFFSTGAPHLTVYLEGLCTILYDTMRPFIIHINHLETLAEICSILRIEMLEEHVQQNPVALEAFATIAHQLLQDVQERLVFRAHLYLQSDIQNFNPSSGDLAYPEKLEMMESIALSLQEPAPLRRSDSRNSMVSSVSSAVETESVATAYTVKQMNSPADLHGMWYPTVRRTLVCLSRLYRCVDRPIFQGLSQEALKLCIQSVSHAAGKISANKTPIDGELFEIKHLLILREQIAPFRVDFTVKETSLDFSKVKTAAFGLLQKRKQLFSMGSNNALLEFLLEGTPQIKEHLLDSRKEVDRQLKSVCEKYIKDAVQMLVGPLITFLEKAQSLLAQSTPATPQSPESTKASYVLRQSPWASPQQISSIIQETQRLIKAKLAVLQRSMQLYLSNRDTEFIIFRPIRNNIIQSFVKLEQLLTTNGYSTDDMIITSCPSAEQVSILLSSASILAAEGVASFAAAARKISTSSSVEGSTVGRKLSAMSNKSELVEEPKVEEVAGQIEVVPAEVQPPAKIEEEEVTETQTQANSE | Function: Involved in ER-Golgi transport.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 101240
Sequence Length: 905
Subcellular Location: Golgi apparatus membrane
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Q96JB2 | MAEAALLLLPEAAAERDAREKLALWDRRPDTTAPLTDRQTDSVLELKAAAENLPVPAELPIEDLCSLTSQSLPIELTSVVPESTEDILLKGFTSLGMEEERIETAQQFFSWFAKLQTQMDQDEGTKYRQMRDYLSGFQEQCDAILNDVNSALQHLESLQKQYLFVSNKTGTLHEACEQLLKEQSELVDLAENIQQKLSYFNELETINTKLNSPTLSVNSDGFIPMLAKLDDCITYISSHPNFKDYPIYLLKFKQCLSKALHLMKTYTVNTLQTLTSQLLKRDPSSVPNADNAFTLFYVKFRAAAPKVRTLIEQIELRSEKIPEYQQLLNDIHQCYLDQRELLLGPSIACTVAELTSQNNRDHCALVRSGCAFMVHVCQDEHQLYNEFFTKPTSKLDELLEKLCVSLYDVFRPLIIHVIHLETLSELCGILKNEVLEDHVQNNAEQLGAFAAGVKQMLEDVQERLVYRTHIYIQTDITGYKPAPGDLAYPDKLVMMEQIAQSLKDEQKKVPSEASFSDVHLEEGESNSLTKSGSTESLNPRPQTTISPADLHGMWYPTVRRTLVCLSKLYRCIDRAVFQGLSQEALSACIQSLLGASESISKNKTQIDGQLFLIKHLLILREQIAPFHTEFTIKEISLDLKKTRDAAFKILNPMTVPRFFRLNSNNALIEFLLEGTPEIREHYLDSKKDVDRHLKSACEQFIQQQTKLFVEQLEEFMTKVSALKTMASQGGPKYTLSQQPWAQPAKVNDLAATAYKTIKTKLPVTLRSMSLYLSNKDTEFILFKPVRNNIQQVFQKFHALLKEEFSPEDIQIIACPSMEQLSLLLLVSK | Function: Involved in ER-Golgi transport.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 94096
Sequence Length: 828
Subcellular Location: Golgi apparatus
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Q9Y7Z4 | MFDQLEFYPAVNYEDNETQNDIKLPEVAKLENIETVHSISKERRDSLTEILNDSSSLPARPFSLPNPNNSTVEKQSLFPFEEKMNPIWIISRPTFSIEQDAEKKINELQTFTNIIDQILGQTNNIESTLLSMKEKFESSEKKLSEFSEMCENLSTDEMRFSEIADGIRKGLTIFAPLKELTRVFRHPPPDFAGKVSFKEHITQLNTCIMFLEENLDFQESPHYLGQYKKLLSQAMDIFKPYFIRIIKQTTDQVLKDSKKMDVHKQLHSSLFYARFSAVGHNLCPTITELCKLCSKESLDAFLPAFYDVYFQCRTRLLKPVLDYHLKSFFMEKSISSYIQKSLALLQLTFFDENKLFREILIMDDFRFMHYWNNLCQSFFENSRSLILHEKNLTELCEVCSYIQSFQNAILEGEREDVDKKVVEFLNPLVLELQERLLFVVQTAIETDIQRYSPTEEDLNPIADDKSLLFDLEKLRLNNDEEKLDPDVPQKLAMAQGWYPVVQKSLIILSKIYRLVNSQVFDEIALELVHSCIRSLVDAYRYFSRNNDKQLARLFLIKNFLVLKDQLNSFDIHYACIEAGVDLRKVWDSVREWRSNLRGVLQLVYETFPKFITNAVDTRQELNQQLRVAVNGYIETAVIHYTECLSIGNLESITEFQNRIQKFPELRQQISLYLSETWIIELFLQAIREEVVSKFQNFYESIVANEDITGSDHNKSGTTSLKHLNEYVEDIYSVMS | Function: Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis- Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 85999
Sequence Length: 735
Subcellular Location: Golgi apparatus membrane
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P40094 | MARSRKNSLVRDIASHPTIPESQTIVGLLDDSYLFDKLKKLSLAVENSDSLQRTDVSEGCSEVNGSEATTSADVKKTNKYLYYTTYLDQLNIKIDEYKVVLDQTRQVNDQLDSSIKKFRKISQDTGAFIEETKTIYEKQSKLSNLTESIPKALHYFEVLDPIMRRLNHATSPAIVKKSSFTTMLATIDESLRFLDENSDLKDAAAYRIKFKQCLIRACELISHFLTNLLKQTNQEILDKTKNKNSLTGLPSTTRDAFLYSKFYTIADTFKIQVSEIVKRSNEKAYNKYHDELNSILYECFNHYFQTRLRLLTPVIWSHIDEIVVKDKDQGLVKFIQDGKVYFQQLCADEYKLFVEFFPEKECRFKINQWFLQLCEPLYDSIRVRVLKETDICTLCDSVTLFAPYYEFEEGSEEYVKQFTDIQYDKLFEPIVQKVQARLILRVQIYVQQNILSYRPTRDVFMISNRRRKSKTSLQGGNEDATTSDDNPDPLLESYLSSFKNRSILPISPNDADDKSIDSEESTDKISQLQTYYPPLLKTLALLSKIYEMINSVVFDDLAHHVVHDCIVSLRNAYDMVIKSSAGKSDFNNLDISLAYLKNLLMLRDSIQNFNIQYTVNETYLDFSGVEGFFKSLKENGRNVLKKTKSSSILTLARELVPKVVNNMVDARTELISELRNVIKDFTESTSLELIDDTLDINSDEDLLSKNVKLRENIKARLPRIYEQILNYIDDQEIVTNLLDAVQELITQSYSKYYETITELAENGKFAKDQVADVMYLDVFTDFFAKEVADLLRNGDIDTITK | Function: Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis- Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events. COG3 is also involved in actin cytoskeleton organization.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 92544
Sequence Length: 801
Subcellular Location: Golgi apparatus membrane
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Q8L838 | MPEIEQDDAAAETVDSSTVKFGTPEALEYVRSLTDVGAMTRLLHECIAYQRSLDSDLDTLLSQRTELDRNLVQLQRSAEILDIVKADADHMLGNVRSTCDLADQVSGKVRELDLAQSRVNVTLSRIDAIVERGNCIEGVKTALESEDYESAAKFVQRFLQIDLQYKDSGSDQSEQLHASKEQLEGIAKKKLLAAIDQRDHPTILRFVRLYSPLGMETEGLQLYVGYLKKVIALRGRMEYENVVELMEQGLGQVNFVGCLTNLFKDIVMAIEENDEILRGLCGEDGVAYAICELQEECDLRGSLILKKYMDFRKLAILASDINNSPNLNILPGGASEGPDPREVELYVEEILSLMQLGEDYTEFMVSKIKSLTSVDPELLPTATKAFRNKSFSKAIQDVTRYYVILEGFFMVENVRKAIRIDEHVPDSLTTSMVDDVFYVLQSCLRRAISTSNISSVIAVLSYAGSLLGNDYHEALQQKIREPNLGARLFLGGIGVENTGTEIATALNNMDVSCEYILKLKHEIEEQCTEVFPAPADRERIKSCLSELGELSSTFKQLLNSGMEQLVATVTPRIRPVLDTVATISYELTETEYAENEVNDPWVQRLLHSVETNAAWLQPLMTSNNYDSFLHLIIDFIVKRLEVIMMQKRFSQLGGLQLDRDTRALVSHFSGMTQRTVRDKFARLTQMATILNLEKVSEILDFWGENSGPMTWRLTPAEVRRVLGLRVEFKPESIAALKL | Function: Required for normal Golgi function.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 82978
Sequence Length: 738
Subcellular Location: Golgi apparatus membrane
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Q95XZ0 | MPEPILHSKFLSGLPAGRKNGVRHGEKPEKVGEKQFDFTRKIRELRLELEIKKREEERIEKDIAIILEENTIDGGEQNRSFGLAVTRLNNHMLVVENSAKQLTSALKNISVLADTISGRVSALDVAKTRVVGCLQLAGDMRDLGVCAEGIDDAIRSEDFETASQHIHRFLTLDQAVFQIREFKQKDATDSIRHSYEVLSSAKERLSKILKSRLTESVQKGDVAEMQRFIKMFPLIHEPDEGLQRYSVFLNQKIDKLAEDNLAIMKAGGTDDNRRNVLYADTLFMFFEGVAEIIESNLPVLEHSYGLEKLLDFMFILQARIDEFFRRLHEEFDTRRRLSHFNRLVDDVIHQKKAAEAVEDAPDPMEIDAIASEICMMNTSAEMYWRFVSRRIGKNEVIRSPSGDGDDEENEEARQERHRLRKEAKEQKMDQLLNRSRVGTKMQELIGNYCLLEHFYMLKSVQKAIKSDVKEDAGGLTSSIVDDVVFIIRKSIRRAAGSGNVDSVCATINNATALIDTVVHGHLRQSIQQGYVTSSNFASEAFTAYQQGKPVKEAADAQKEQFLLALNNSAKLSELLIELQKGLITEWAGVKRPDVEKNKLEHSTTQIEESAKKLASLAKHGVEELFKSAFKNKIKQGADPYQEIDRQMTMQDVEYYEAHDPFMEQFLAQIDRLLVENEPLLFADNYQTLLLLTSSEIARQIEQSLAKCQFNRYGALQLDREYRQICAYLTNVAGWSAREKVGRLGQIVSLLNVETIDEAMEVWHNSKAMTSSATIRTLTLPEVRKVLALRADFPTVAIKSIE | Function: Required for normal Golgi function.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 91020
Sequence Length: 801
Subcellular Location: Golgi apparatus membrane
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P34156 | AAILQDEYLXSGGVVPYVFG | Cofactor: Binds 1 zinc ion per subunit.
Function: This enzyme is a metal protease capable of degrading the native triple helix of collagen.
Catalytic Activity: Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.
Sequence Mass (Da): 2110
Sequence Length: 20
EC: 3.4.24.7
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Q29RB1 | MEEAASPARRRGGPAGVSAVQTDTIEALTELEDLERVYAQLCAEEAEVQVELDALVGQQNNIETKMLSLQRMGPNLQLIEGDAVQLSGMINFTCSLAENVSSKVRQLDLTKKRLYQAIQRADDILDLKFCTDGVQTALRNQDYEQAAAHIHRYLSLDQSVIELSKQGGEGSAVEASLALLQEAERNLKTLVTTRLEEAVATGDLPQVERFFKILPLLGLHEQGLARFAQYLCSQLASKAEENLILAVGSDLGERRAPVIFADTLTLLLEGIARIVETHQPIVETYYGPGRLHTLLAHLQKECDKQAQKIVDKFIQQRDYNNKFQVVQSNMMRGMTTDKIEPRDLDPVLCEVTLMNSRAELYFRFLRRRIVADFEVADAMADEAVIQEHQQSLEQLLKNCQLSRTMQELIGYYIPMEEYYMRESVNKAVAMDTAEVGQLSSSVVDDVFYIVKKCISRALTSSSSDCVCAMINHATSVLETDFREVLVCKLRAGYPVSALQDLQRGVSSAVSLMQSSLQQGKITNLTQTLGIESQEQAKSAYLVTLNNVEVCSENISTLKKNLESDCAKLFSQGASSDHAKEKIDSCLSDLVNTSSKFKDLLQEGLQELNNTAIRPQVKPWISSFLSVSHNIEEEEFSEYEANDPFVQQLIVQLEQLMAEFKVGLSPVIYDTLTSLMTSLIAMEMEKTVFKCTFSRLGGLQFDKELRALVAYLSSVTSWTIRDKFARLTQMATILNLERVSEILDYWGPNSGPLTWRLTPAEVRQVLALRVDFRSEDIKRLRL | Function: Required for normal Golgi function . Plays a role in the vesicular trafficking between the endoplasmic reticulum and the Golgi apparatus (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 87587
Sequence Length: 781
Subcellular Location: Cytoplasm
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Q55FT5 | MDELIVDFNNLDSNLSIDDAKKYLQNLISRDKAIEINLKQHIKLKDDLEIQMESFDNEIPEYLTLSLKKSNELNNRISSTCQLAENLSSKVKKLDNIRERIKDTLKKVDDIIDLKNCIEGVQISIEKEDYEGAAFHINRYLSIDKSVLEDNSSEKLSIAEKKLLSMIESKYQQSLQDNDQKQVLRFCILYVPLEKPLEGIDKYCNYLKNQSKKLDAMITHYRNYIQSPKTIKPISAVSVITKIFEHFAAIIEDDLPIIKSEFGVLHCPHFILNITQQCDYYSSKVYDSFNDQFQTNKNVNDILVYKQQLEKSQQSIQDSGSGSGGGGGKVSEKIDPRNFAQFLDETSMISKATKFYEKYLIRKEHLIKSDIYQYYSKLEKEKIEKLNSIKSLIITNSRNQQLQQLPQPQQLQQQQQYQQQLQTQENKENELLKKLTQEKDKQMKQTIYSNVTKQKMNQLLGNYILLEEYFMVESVNKAIQMDSLQSLDFENNINSSNSNSSSVSGSGIGGSNTLSSSNSQQSQQSTDNTMIDFIFFVLQKSLQRAIDSHSIQTLNVICNRLCRILSQTRDNLKRIFREYIIRSSSKSVMDYQSSLQVLNNLETSSEYIIRLKKEFDSKCLKIYPIYKLDEKSKDLESSSTSSTSIEQQQQQQQQQQQQQQQQQQQQQQQQQQQEQQQENEFESNLKDDIIIIRNLLNLELKKKQENDRDQVNILSNEFLNCSKSFNKILQEEIESLFKSVQPRLKNVLNQFTLVNYEINQLEYDNNDINDPFVLQFTLEISHFFKPFQEHLSNTNYDYLVHQTIQFILKKIEGITIQQKKFTLLGGLQFGKDLRAISTYFTKISQSTIRDKFSKLNQISSFLILESISEVEDHWNENRNSPTWKLSSSEVQKILMTRIDFNHDQILKLKFN | Function: Required for normal Golgi function.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 106365
Sequence Length: 911
Subcellular Location: Golgi apparatus membrane
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Q95TN4 | MSVLEQLGALDIGTNEQVDETLQRIADEEAKVNEKLESLLAKQCQIEAKMSGIGRSLSLLHTVDSDSNKLNDQIVNTAQLAESVSAKVRRLDLARCRASECQQRVHDLIDLHLCSQGVVKAIGEEDYEKSATHIARFLAMDQQLLRRTADDVQGSITSVSDAVKTLEDATEKTRVLIAKRFDEAVKADDLASVERFFKIFPLVGCHRTGIEKFSLYICQKLANKAQKELRNAQDIAKAESRLQLAYADRLTAILENFARVVEVNQPIIEAFYGQASSSLIDMVSILQHECDTEVKNLLMEFNKNRQIQYRSKQVNESTQRSAGGGNLGSNSIQALGHYRKPSGGSVDKLNPKEIDAIIAEITVMHARVELYFRFMRRRLQVHVETCVPEKEQFDIMERYEKIMKNSDLRRQMQEILSTYLLLERYFMEESVLKAIGLDTYESGQQCSSMVDDVFFILRKSIRRALTTQSINGTCAVINNVAACLDGDFVNALKAPLKSGYPSGYIDLAQAYNAIQTSLQQGKLHSSDADRGRANFLVQLNNADISTEYIETLCQTMEQEIAGTFPQTTQVERQMLDSCLTELKAVRDALKATVDFGMQQLRSSVIKPRLNPWINQFLNYSHNLNEEELAAYEAGETFVQFFIVQLDGLLNSFKNSLSPRNYDALVSILATEVTIQLERAIKKISFNRLGGLVLDQEVRALGSYLTGATSWSVRDKMTRISQIATLLNLDKITELSEYWNPENNKEMSSWHLTPNEVRTFLTLRNDFRIEDIKRLQL | Function: Required for normal Golgi function.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 87715
Sequence Length: 776
Subcellular Location: Golgi apparatus membrane
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Q9H9E3 | MADLDSPPKLSGVQQPSEGVGGGRCSEISAELIRSLTELQELEAVYERLCGEEKVVERELDALLEQQNTIESKMVTLHRMGPNLQLIEGDAKQLAGMITFTCNLAENVSSKVRQLDLAKNRLYQAIQRADDILDLKFCMDGVQTALRSEDYEQAAAHTHRYLCLDKSVIELSRQGKEGSMIDANLKLLQEAEQRLKAIVAEKFAIATKEGDLPQVERFFKIFPLLGLHEEGLRKFSEYLCKQVASKAEENLLMVLGTDMSDRRAAVIFADTLTLLFEGIARIVETHQPIVETYYGPGRLYTLIKYLQVECDRQVEKVVDKFIKQRDYHQQFRHVQNNLMRNSTTEKIEPRELDPILTEVTLMNARSELYLRFLKKRISSDFEVGDSMASEEVKQEHQKCLDKLLNNCLLSCTMQELIGLYVTMEEYFMRETVNKAVALDTYEKGQLTSSMVDDVFYIVKKCIGRALSSSSIDCLCAMINLATTELESDFRDVLCNKLRMGFPATTFQDIQRGVTSAVNIMHSSLQQGKFDTKGIESTDEAKMSFLVTLNNVEVCSENISTLKKTLESDCTKLFSQGIGGEQAQAKFDSCLSDLAAVSNKFRDLLQEGLTELNSTAIKPQVQPWINSFFSVSHNIEEEEFNDYEANDPWVQQFILNLEQQMAEFKASLSPVIYDSLTGLMTSLVAVELEKVVLKSTFNRLGGLQFDKELRSLIAYLTTVTTWTIRDKFARLSQMATILNLERVTEILDYWGPNSGPLTWRLTPAEVRQVLALRIDFRSEDIKRLRL | Function: Required for normal Golgi function . Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with SCFD1 .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 89083
Sequence Length: 785
Subcellular Location: Cytoplasm
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O74986 | MNEEEHNKSVHWSIVYRQLGNLLEQYEVEIARLKSQLVLEKKLRIQVEKELESVKTKQISSSASSKVSSNTIQELDSTTDEDEIPGSDTVDEEDPSLNAPFSEKNQSVKIPPHSPTLPVQNASAFVKPISVPLGNVKEEKFLDTNPIGAESFESSDGEMHLRARSPEDMILLRETQPLAPLDINTLGVSDNRQKKGTEKKRPFEPEFLNDDVIRGNKRKALPAYECPDCQKFYELHGPVKESSVAPTWNDENRLGGGSLPNCKHQPLVQKVGRHRKLNIPKPIPNGFWESDFVD | Function: Endonuclease that cooperates with the MRN complex in processing meiotic and mitotic double-strand breaks by allowing the endonucleolytic removal of rec12 from the break sites and ensuring both resection and intrachromosomal association of the broken ends. Required for the formation of RPA-coated single strand DNA adjacent to the DSBs where it functions together with the MRN complex in 5'- 3' resection. Required for the repair of programmed meiotic DSBs. Involved also in an rhp51 recombinase-dependent recombinational repair pathway.
PTM: Phosphorylated by tel1 in response to DNA damage.
Sequence Mass (Da): 33101
Sequence Length: 294
Subcellular Location: Nucleus
EC: 3.1.-.-
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P46946 | MVTGEENVYLKSSLSILKELSLDELLNVQYDVTTLIAKRVQALQNRNKCVLEEPNSKLAEILCHEKNAPQQSSQTSAGPGEQDSEDFILTQFDEDIKKESAEVHYRNENKHTVQLPLVTMPPNRHKRKISEFSSPLNGLNNLSDLEDCSDTVIHEKDNDKENKTRKLLGIELENPESTSPNLYKNVKDNFLFDFNTNPLTKRAWILEDFRPNEDIAPVKRGRRKLERFYAQVGKPEDSKHRSLSVVIESQNSDYEFAFDNLRNRSKSPPGFGRLDFPSTQEGNEDKKKSQEIIRRKTKYRFLMASNNKIPPYEREYVFKREQLNQIVDDGCFFWSDKLLQIYARC | Function: Endonuclease that cooperates with the MRX complex in processing meiotic and mitotic double-strand breaks by allowing the endonucleolytic removal of SPO11 from the break sites and ensuring both resection and intrachromosomal association of the broken ends. Required for proper recovery from checkpoint-mediated cell cycle arrest after DNA damage. MRX complex and SAE2 remove a small oligonucleotide(s) from the DNA ends to form an early intermediate which is rapidly processed by EXO1 and/or SGS1 to generate extensive tracts of single-stranded DNA that serve as substrate for RAD51. Plays a transitional role in the dissociation of MRE11 from, and the recruitment of RAD52 to, repair foci. Ensures that both ends of a DSB participate in a recombination event and impairs the formation of palindromic structures in the genome. With TEL1, promotes microhomology-mediated end joining (MMEJ) but inhibits non-homologous end joining (NHEJ), likely by regulating MRE11-dependent ssDNA accumulation at DNA break. SAE2 and MRX are particularly important for removal of hairpins, bulky adducts and other irregular end structures. Facilitates telomere length reequilibration and subsequent checkpoint switch off. Involved in homing efficiency of VMA1 intein VDE and in repair of transposon excision sites.
PTM: Phosphorylated forms accumulate periodically during the unperturbed cell cycle and in response to DNA damage in G2. Phosphorylated by MEC1 and TEL1. Mutagenesis experiments showed that several of the 5 residues located in canonical (S/T)Q motifs, which are favored for phosphorylation by ATM/ATR kinases (Ser-73, Thr-90, Ser-249, Thr-279 and Ser-289) may be phosphorylated. Phosphorylated at Ser-267 by CDC28 which is required to initiate meiotic DSB resection by allowing SPO11 removal from DSB ends.
Sequence Mass (Da): 40097
Sequence Length: 345
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q9TWL9 | QXPSTAELCKINSNACSVPFSXIPCQKXFLAACDRHDTCYHCGKHFGFKQDDCDDAFFRDMTALCAHGTDDEGXCPX | Function: Heterodimer: conodipine-M catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. This activity may be supported by the alpha chain. Conodipine-M inhibits the binding of isradipine (a ligand specific for L-type calcium channel) to L-type calcium channels.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Sequence Mass (Da): 8492
Sequence Length: 77
Subcellular Location: Secreted
EC: 3.1.1.4
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P51973 | MLCVLAGAAYGVFRTEAALSSQWRAEAVSGVPLTVEVTDMPRSDGRRVQFAAKAVDSGGRTFDLLLSDYKRREWAVGSRWRITARVHPVVGELNLRGLNREAWALSNGVGGVGTVGADRVLLHGGSGWGIAVWRSRISRNWRQADADGGLSDGIGLMRALSVGEQSALRPGLWQAFRPLGLTHLVSISGLHVTMVAVLFAWLAKRLLACSPRLPARPRAWVLAAGCAGALFYALLAGFSVPTQRSVLMLAAFAWAWRRGRLSAWATWWQALAAVLLFDPLAVLGVGTWLSFGLVAALIWACAGRLYEGKRQTAVRGQWAASVLSLVLLGYLFASLPLVSPLVNAVSIPWFSWVLTPLALLGSVVPFAPLQQAGAFLAEYTLRFLVWLADVSPEFAVAAAPLPLLVLAVCAALLLLLPRGLGLRPWAVLLLAGFVSYRPEAVPENEAAVTVWDAGQGLSVLVRTANRHLLFDTGTVAAAQTGIVPSLNAAGVRRLDKLVLSHHDSDHDGGFQAVGKIPNGGIYAGQPEFYEGARHCAEQRWQWDGVDFEFLRPSERKNIDDNGKSCVLRVVAGGAALLVTGDLDTKGEESLVGKYGGNLYSQVLVLGHHGSNTSSSGVFLNAVSPEYAVASSGYANAYKHPTEAVQNRVRAHGIKLLRTDLSGALQFGLGRGGVKAQRLRVYKFYWQKKPFE | Function: Essential for natural transformation. Could be a transporter involved in DNA uptake.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74358
Sequence Length: 691
Subcellular Location: Cell inner membrane
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Q03727 | MKFGKRHYRPQVDQMDCGVASLAMVFGYYGSYYFLAHLRELAKTTMDGTTALGLVKVAEEIGFETRAIKADMTLFDLPDLTFPFVAHVLKEGKLLHYYVVTGQDKDSIHIADPDPGVKLTKLPRERFEEEWTGVTLFMAPSPDYKPHKEQKNGLLSFIPILVKQRGLIANIVLATLLVTVINIVGSYYLQSIIDTYVPDQMRSTLGIISIGLVIVYIFQQILSYAQEYLLLVLGQRLSIDVILSYIKHVFHLPMSFFATRRTGEIVSRFTDANSIIDALASTILSIFLDVSTVVIISLVLFSQNTNLFFMTLLALPIYTVIIFAFMKPFEKMNRDTMEANAVLSSSIIEDINGIETIKSLTSESQRYQKIDKEFVDYLKKSFTYSRAESQQKALKKVAHLLLNVGILWMGAVLVMDGKMSLGQLITYNTLLVYFTNPLENIINLQTKLQTAQVANNRLNEVYLVASEFEEKKTVEDLSLMKGDMTFKQVHYKYGYGRDVLSDINLTVPQGSKVAFVGISGSGKTTLAKMMVNFYDPSQGEISLGSVNLNQIDKKALRQYINYLSQQPYVFNGTILENLLLGAKEGTTQEDILRAVELAEIREDIERMPLNYQTELTSDGAGISGGQRQRIALARALLTDAPVLILDEATSSLDILTEKRIVDNLIALDKTLIFIAHRLTIAERTEKVVVLDQGKIVEEGKHADLLAQGGFYAHLVNS | Function: Required for induction of competence. Seems to transport the competence-stimulating peptide (CSP).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80404
Sequence Length: 717
Subcellular Location: Cell membrane
EC: 3.4.22.-
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O30583 | MNAQKGFTLIELMIVIAIIGILAAIAIPAYTDYTVRARVSEGLTAASSMKTTVSENILNAGALVAGTPSTAGSSCVGVQEISASNATTNVATATCGASSAGQIIVTMDTTKAKGANITLTPTYASGAVTWKCTTTSDKKYVPSECRG | Function: Pilin-like competence factor, which is essential for natural transformation of the Gram-negative soil bacterium A.baylyi ADP1. Is not a subunit of the pilus structures. Likely functions as a major subunit of an oligomeric structure acting as a channel or pore mediating DNA translocation through the outer membrane and periplasm.
PTM: Glycosylated by PglL2 . The 20-kDa form is glycosylated; a 23-kDa form also exists, that might be due to a further modification. The glycosylation of ComP is not required for its function in DNA binding and uptake .
Sequence Mass (Da): 14872
Sequence Length: 147
Subcellular Location: Cell inner membrane
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Q99027 | MKNLIKKFTIAVIVLSILYISYTTYISMNGIIIGTKIHKNDKSQFMIEEISESSYGQFVGLRQGDIILKINKEKPSDKHLKWGYLSHINSLDILRSGKKIHLKDFDLVTLNRPYSFFLFVLPLFFYFLSIICIFYILKVNKKRRSFAAYILILLLLDISIAYISAGGPFRGHIINRYINLFTFISSPILYLQFIQRYLGEIGKTFLNRISFLYIIPIFNLGIEFFQDYLQVDIDFLATLNLVSFATLTLFSFSAIYLHLNKYKYAEHSFILKLLILTNTLSFAPFLIFFVLPIIFTGNYIFPALASASLLVLIPFGLVYQFVANKMFDIEFILGRMRYYALLAMIPTLLIVGALVLFDVMDIQMNPVRQTVFFFVVMFAVFYFKEVMDFKFRLKRFSEKFNYQDSIFKYTQLMRGVTSLQQVFKELKNTILDVLLVSKAYTFEVTPDHKVIFLDKHEVGPDWNFYQEEFENVTSEIGKIIEVNQGFLMKVGERGGSSYVLLCLSNINTPRLTRDEISWLKTLSFYTSVSMENVLHIEELMEHLKDLKQEGTNPIWLKKLMFAIEEKQRSGLARDLHDSVLQDLISLKRQCELFLGDFKKDDNPCREEVQDKLVQMNEQMSDVISMTRETCHELRPQLLYDLGLVKALSKLVAQQQERVPFHIRLNTGRFTASLDLDSQLNLYRIIQEFLSNAVKHSQATDVLIMLISIQNKIVLHYEDDGVGFDQEKNTEHSMSMGLSGIKERVRALDGRLRIETSEGKGFKADIEIEL | Function: Sensor in the two-component regulatory system ComP/ComA involved in a major quorum response pathway that regulates the development of genetic competence. Plays a role in sporulation, at least partly interchangeable with that of SpoIIJ. Probably activates ComA by phosphorylation.
PTM: Autophosphorylates on a histidine and transfers the phosphate group onto an aspartate in ComA, thus activating it.
Location Topology: Multi-pass membrane protein
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 89309
Sequence Length: 769
Subcellular Location: Cell membrane
EC: 2.7.13.3
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P35445 | MVLAAARVLLLTLAALGASGQGQMPLGGDLGPQMLRELQETNAALQDVRDLLRQQVKEITFLKNTVMECDACGMQPARTPKLTVRPLSQCSPGFCFPGVACTETANGARCGPCPEGFTGNGSHCADVNECTAHPCFPRVRCINTSPGFRCEACPPGFSGPTHEGVGLAFAKANKQVCTDINECETGQHNCVPNSVCVNTVGSFQCGPCQPGFVGDQASGCRRRPQRFCPDGTPSPCHEKADCVLERDGSRSCVCAVGWAGNGLICGRDTDLDGFPDEKLRCSERQCRKDNCVTVPNSGQEDVDQDGIGDACDPDADGDGVLNEKDNCPLVRNPDQRNTDGDKWGDACDNCRSQKNDDQKDTDKDGRGDACDDDIDGDRIRNPVDNCPKVPNSDQKDTDGDGVGDACDNCPQKSNADQRDVDHDFVGDACDSDQDQDGDGHQDSKDNCPTVPNSAQQDSDHDGQGDACDDDDDNDGVPDSRDNCRLVPNPGQEDMDRDGVGDACQGDFDADKVVDKIDVCPENAEVTLTDFRAFQTVVLDPEGDAQIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTATDDDYAGFIFGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDTASQVRLLWKDPRNVGWKDKTSYRWFLQHRPQVGYIRVRFYEGPELVADSNVILDTTMRGGRLGVFCFSQENIIWANLRYRCNDTIPEDYEAQRLLQA | Cofactor: Binds 11-14 calcium ions per subunit.
Function: Plays a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors. Could play a role in the pathogenesis of osteoarthritis. Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and XIAP) (By similarity). Essential for maintaining a vascular smooth muscle cells (VSMCs) contractile/differentiated phenotype under physiological and pathological stimuli. Maintains this phenotype of VSMCs by interacting with ITGA7 (By similarity).
Sequence Mass (Da): 82362
Sequence Length: 756
Domain: The cell attachment motif mediates the attachment to chondrocytes. It mediates the induction of both the IAP family of survival proteins and the antiapoptotic response.
Subcellular Location: Secreted
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P49747 | MVPDTACVLLLTLAALGASGQGQSPLGSDLGPQMLRELQETNAALQDVRELLRQQVREITFLKNTVMECDACGMQQSVRTGLPSVRPLLHCAPGFCFPGVACIQTESGARCGPCPAGFTGNGSHCTDVNECNAHPCFPRVRCINTSPGFRCEACPPGYSGPTHQGVGLAFAKANKQVCTDINECETGQHNCVPNSVCINTRGSFQCGPCQPGFVGDQASGCQRRAQRFCPDGSPSECHEHADCVLERDGSRSCVCAVGWAGNGILCGRDTDLDGFPDEKLRCPERQCRKDNCVTVPNSGQEDVDRDGIGDACDPDADGDGVPNEKDNCPLVRNPDQRNTDEDKWGDACDNCRSQKNDDQKDTDQDGRGDACDDDIDGDRIRNQADNCPRVPNSDQKDSDGDGIGDACDNCPQKSNPDQADVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQEDSDHDGQGDACDDDDDNDGVPDSRDNCRLVPNPGQEDADRDGVGDVCQDDFDADKVVDKIDVCPENAEVTLTDFRAFQTVVLDPEGDAQIDPNWVVLNQGREIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTVTDDDYAGFIFGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDTESQVRLLWKDPRNVGWKDKKSYRWFLQHRPQVGYIRVRFYEGPELVADSNVVLDTTMRGGRLGVFCFSQENIIWANLRYRCNDTIPEDYETHQLRQA | Cofactor: Binds 11-14 calcium ions per subunit.
Function: Plays a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors . Could play a role in the pathogenesis of osteoarthritis . Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and XIAP) . Essential for maintaining a vascular smooth muscle cells (VSMCs) contractile/differentiated phenotype under physiological and pathological stimuli. Maintains this phenotype of VSMCs by interacting with ITGA7 (By similarity).
Sequence Mass (Da): 82860
Sequence Length: 757
Domain: The cell attachment motif mediates the attachment to chondrocytes. It mediates the induction of both the IAP family of survival proteins and the antiapoptotic response.
Subcellular Location: Secreted
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P0DV08 | MKEIVHEKIQNLDLKEYLINFIDEKNHFSFGILSFKHYVALSGNRSSHILTLAGGIELLILAFDIFDDLEDEDNIEIKWMKIDPSLALNAATTLYTLGLETICSISNSAEFHRLTLKYALNAMQGQHEDLRNSPETEEECIQMMKQKAGSLTAMSAVLAAMLANGEFNQTIEDYAYKIGIIKQLENDYYGLVNDQRSDIRKKRKTLIYLFLNRKFNEASEKILKLINSHTSYHSFISDSSKFDELLFEAGLNQYVSMLIKLYEEEITASMNQLNINIKL | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Part of a major quorum-sensing system that regulates the development of genetic competence (By similarity). Involved in the maturation of the competence pheromone ComX (By similarity). Acts by catalyzing the transfer of a prenyl group on the ComX pheromone (By similarity).
Sequence Mass (Da): 32015
Sequence Length: 279
Subcellular Location: Cell membrane
EC: 2.5.1.-
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D4G0R4 | MSHLVKWNGRGEVVIEQICLDSVRIKEKMKEIVDENILNEDLKVKLISFIKEKKQFSFAELAYYHYIAFDGKNDKAIELLASGIELLILSADIFDDIEDKDNLQASWMKLDPSIATNAATALYTLSLQVIGSVSNHPKLLSLTLQYSLQSLQGQHVDLNLTASSESEYIEMIKLKSGSLVTLPSILGVYLATGEYNETVEEYSRYLGIVEQIANDHYGLYYPNYNDFKTRHTLAFNYLKNKFNQSSIDLLNFYAQENHMINNLEDLKGKLRESGVIQYLNVIKNLAVENFKESFKKLRLDEQRKNKLLIQLLRGI | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Part of a major quorum-sensing system that regulates the development of genetic competence . Involved in the maturation of the competence pheromone ComX . Acts by catalyzing the transfer of a farnesyl group on the ComX pheromone . In vitro, can also catalyze the farnesylation of single tryptophan and tryptophan derivatives .
Catalytic Activity: (2E,6E)-farnesyl diphosphate + L-tryptophyl-[protein] = (2S,3R)-3-farnesyl-2,3-dihydro-2,N(alpha)-cyclo-L-tryptophyl-[protein] + diphosphate
Sequence Mass (Da): 36132
Sequence Length: 315
Subcellular Location: Cell membrane
EC: 2.5.1.-
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P33690 | MKEIVEQNIFNEDLSQLLYSFIDSKETFSFAESTILHYVVFGGENLDVATRLGAGIEILILSSDIMDDLEDEDNHHALWMKINRSESLNAALSLYTVGLTSIYSLNNNPLIFKYVLKYVNEAMQGQHDDITNKSKTEDESLEVIRLKCGSLIALANVAGVLLATGEYNETVERYSYYKGIIAQISGDYYVLLSGNRSDIEKNKHTLIYLYLKRLFNDASEDLLYLISHKDLYYKSLLDKEKFQEKLIKAGVTQYISVLLEIYKQKCISAIEQLNLDKEKKELIKECLLSYTKGDTRCKT | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Part of a major quorum-sensing system that regulates the development of genetic competence . Involved in the maturation of the competence pheromone ComX . Acts by catalyzing the transfer of a farnesyl group on the ComX pheromone . Shows weak geranylation activity with geranyl diphosphate (GPP) .
Catalytic Activity: (2E,6E)-farnesyl diphosphate + L-tryptophyl-[protein] = (2S,3R)-3-farnesyl-2,3-dihydro-2,N(alpha)-cyclo-L-tryptophyl-[protein] + diphosphate
Sequence Mass (Da): 34218
Sequence Length: 299
Subcellular Location: Cell membrane
EC: 2.5.1.-
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Q949P2 | MASEDTLSSNPLLQNFDFPPFDSVDAHHVRPGIRALLQQLEAELEQLEKAVEPSWPKLVEPLEKIIDRLSVVWGMINHLKAVKDTPELRAAIEEVQPEKVKFQLRLGQSKPIYNAFKAIRESPDWNSLSEARQRLVEAQIKEAVLSGIALEDDKREEFNKIEQELEKLSHKFSENVLDATKKFEKLITDKKEIEGLPPSALGLFAQAAVSKGHETATADTGPWLITLDAPSYLPVMQHAKNRALREEVYRAYLSRASSGDLDNTAIIDQILKLRLEKAKLLGYRNYAEVSMATKMATVEKADELLEKLRSASWDPAVQDIEDLKSFAKNQGAAEADSLTHWDITFWSERLRESKYDINEEELRPYFSLPKVMDALFGLAKTLFGIDVVPADGVAPVWNSDVRFYCVKDSSGNPTAYFYFDPYSRPSEKRDGAWMDEVFSRSRVMAQKGSSVRLPVAQMVCNQTPPVGDKPSLMTFREVETVFHEFGHALQHMLTKEDEGLVAGIRNIEWDAVELPSQFMENWCYHRDTLMSIAKHYQTGETLPENVYKKLLAARTFRAGSLSLRQLKFATVDLELHTKYMPGGAETIYEVDQRVSIKTQVIPPLPEDRFLCSFSHIFAGGYAAGYYSYKWAEVLSADAFSAFEDAGLDDIKAVKETGQRFRNTILALGGGKAPLKVFVEFRGREPSPEPLLRHNGLLAASA | Cofactor: Binds 1 zinc ion.
Function: Oligopeptidase that may be involved in the degradation of proteasome-generated peptides (By similarity). Binds salicylic acid.
Catalytic Activity: Hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-Pro-Ala is cleaved, but not Z-(Gly)(5).
Sequence Mass (Da): 79044
Sequence Length: 701
Subcellular Location: Cytoplasm
EC: 3.4.24.70
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Q93Y22 | MVVLAAAIVVKSGKVIVSRHYVDMSRIRIEGLLAAFPKLVGMGKQHTYIETENVRYVYQPIEALFLLLVTTKQSNILEDLATLTLLSKLVPEYSMSLDEEGISRASFELIFAFDEVISLGHKESVTVAQVKQYCEMESHEEKLHKLVMQSKINDTKDVMKRKANEIDKSKIEKNKPGGFSSMGSMGSGRLESGFNELSISSGGGGGYGSGSGFGMISDVDPINTKPKDRSRSSVTAPPKSSGMKLGKSGKNQLMESLKAEGEDVIEDVKPTGQSKAAAPPPTDPFTLTVEEKLNVALRRDGGLSSFDMQGTLSLQILNQEDGFVQVQIATGENPEILFKTHPNINRDMFNNENILGLKRPDQPFPTGQGGDGVGLLRWRMQRADESMVPLTINCWPSVSGNETYVSLEYEASSMFDLTNVIISVPLPALREAPSVRQCDGEWRYDPRNSVLEWSILLIDNSNRSGSMEFVVPPVDSSVFFPISVQFAATSTYSGLKVTGMIPLRGGGGATPRFVQRTQLIAQNYQVI | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 57719
Sequence Length: 527
Subcellular Location: Cytoplasm
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Q09236 | MVLIAACILSKTGKLLVARQFVNDMMRSRLEGLVDAFPKLIGNEKEAATRQHTFVETDSVRYVYHPLDNIYLVLVTTKNSNILEDLETLRLFVRVIPEYCRSNEEKEILAHDFDLIFAFDEVVTLGYRESVNLAQIRTFTEMDSHEERVFMQIKEAQEKAAKQAMAEKAKELKRAQKEALSRGLKPSYQSSTGISSSSTPNAAAVSEPAAPRPSAPKGPIGGGKALKLGGKTNNEDDFLDTLRQQGQSIAPVQKASLSGGVSSLAAPISTAPRVKREVVHVRTEEKINTRVSRDGGLESGEVQATVTLSIGSPEFIPISIKMNNGSAAGTQLQVHPNLDKKEWQSSSTLKIKPNGKPYPVNSDVGILKWKMALSEEEQLPISFNCWPQESSDGVQVNIEYTLQREDITLNNVRIIVPLPTATAPSVGECDGEYEYHKTKNVIVWSLAVIDSSNSSGTLEFSVPNGHCDHFFPVSVGFTSENLFVPITVQKVVKNDGSPVTYSVETTFNSENFEIV | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56646
Sequence Length: 515
Subcellular Location: Cytoplasm
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Q55EZ6 | MVVLAAAICTKNGKALLSRQFSEMTKSRVEGLLAAFPKLIGLGRQHTFIETENIRYVYQPLESLYIVLITNKNSNILEDLETLHLLAKLVPEYSNFDEYDISKNAFELIFTFDEVIAMGYKERVTLQQIKHFISMESHEEERFRMEEKIKQKEAQILASSKAKEIERMRHEEMLRGKRSGGYTGISGGGGMGSGGMGSNQYRDNDRDNYHSNNNNNNNNNNNNNNNNNNNRDRDRGDSPNTSRPSAASSGSQGGMILGGKSGTNKNSAIAQVLKEEKIVEKVEDVEQLLDSQISQIPETPTVPQEGVHITVEESFTSFVESDGTVESIDIKGGLSVQINDQSLGKVKVNLKQGKLSKQFQFITHPNIDKALFGEQSVLRLRDGGKGFPSGGILKWRCKTNQESMMPIRVNCWPSPGRDSTTVNLEYDSLVGYELKSVFIVIPNPTSNAPIINQFDGLYEYDNKQKCVIWKIPLIDDSNRQGSMEFSVKGNTQSFFPVKIQFTASQTICDTTVGSVFVEDSNQSTNFSTETTLSVDTYEIK | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 60335
Sequence Length: 540
Subcellular Location: Cytoplasm
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P48444 | MVLLAAAVCTKAGKAIVSRQFVEMTRTRIEGLLAAFPKLMNTGKQHTFVETESVRYVYQPMEKLYMVLITTKNSNILEDLETLRLFSRVIPEYCRALEENEISEHCFDLIFAFDEIVALGYRENVNLAQIRTFTEMDSHEEKVFRAVRETQEREAKAEMRRKAKELQQARRDAERQGKKAPGFGGFGSSAVSGGSTAAMITETIIETDKPKVAPAPARPSGPSKALKLGAKGKEVDNFVDKLKSEGETIMSSSMGKRTSEATKMHAPPINMESVHMKIEEKITLTCGRDGGLQNMELHGMIMLRISDDKYGRIRLHVENEDKKGVQLQTHPNVDKKLFTAESLIGLKNPEKSFPVNSDVGVLKWRLQTTEESFIPLTINCWPSESGNGCDVNIEYELQEDNLELNDVVITIPLPSGVGAPVIGEIDGEYRHDSRRNTLEWCLPVIDAKNKSGSLEFSIAGQPNDFFPVQVSFVSKKNYCNIQVTKVTQVDGNSPVRFSTETTFLVDKYEIL | Function: Component of the coatomer, a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 57210
Sequence Length: 511
Subcellular Location: Cytoplasm
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Q5XJY5 | MVLLAAAVCTKAGKAIVSRQFVEMTRTRIEGLLAAFPKLMNTGKQHTFVETESVRYVYQPMEKLYMVLITTKNSNILEDLETLRLFSRVIPEYCRALEENEISEHCFDLIFAFDEIVALGYRENVNLAQIRTFTEMDSHEEKVFRAVRETQEREAKAEMRRKAKELQQARRDAERQGKKAPGFGGFGSSAVSGGSTAAMITETIIETDKPKVAPAPARPSGPSKALKLGAKGKEVDNFVDKLKSEGETIMSSNMGKRTSEATKVHAPPINMESVHMKIEEKITLTCGRDGGLQNMELHGMIMLRISDDKFGRIRLHVENEDKKGVQLQTHPNVDKKLFTAESLIGLKNPEKSFPVNSDVGVLKWRLQTTEESFIPLTINCWPSESGNGCDVNIEYELQEDNLELNDVVITIPLPSGVGAPVIGEIDGEYRHDSRRNTLEWCLPVIDAKNKSGSLEFSIPGQPNDFFPVQVSFISKKNYCNIQVTKVTQVDGNSPVRFSTETTFLVDKYEIL | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 57229
Sequence Length: 511
Subcellular Location: Cytoplasm
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P12377 | MEDPLSIAVRFALYTDLMMLFGLALFGLYSLRGAERRSGAVLPFRPLLSATALIGLLLSVVSIVLMAKAMSGASEWLEAVPHAEMMVTQTELGTAWLIRMAALVGAAVTIAFNLRVPMASLLMVSLLGGVALATLAWTGHGAMDEGSRRFWHFSADILHLWSSGGWFGALVAFALMLRPNKVETLQSVQVLSRTLSGFERAGAVIVAFIVLSGVVNYLFIVGPQVSGVVESTYGVLLLGKLALFGLMVGLASANRFVLSPAFERAVHRGEYARAARSIRYSMALELGAAVLVLGLIAWLGTLSPEMEAGM | Function: Exact function not known. Involved in copper resistance. Appears to be involved in copper uptake in conjunction with CopC.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33089
Sequence Length: 310
Subcellular Location: Cell inner membrane
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P43621 | MVVLAASITTRQGKPLLSRQFKDLSKDRVLELLSNFQNLVSEISSDHTFVEDKHVRYVYRPFDNYYIILITNRQSNIIKDLATLNLFSQTINSYLSSFQDQEIFHNAFEILSSFDEIVSMGGYKENLSFTQVQTYLSMESHEERIQEIIERNKEIEATEERKRRAKEIARKEHERKHGFMSSNGDYDGANRFMGSKDPNVTNAINSYYSHASPAAQQSYLQSSHAAAAEVAPVASPMATSQRAGHSATGGMKLGGGAGRRAGAAPRPSAISSASSGTPPPPEEDVPENNGILISIKEVINAEFSRDGTIHSSELKGVLELRINDHDLSHSNLKLADSIDVRDKSFQFKTHPNIDKQSFLSTKLISLRDKSKAFPANDQSLGVLRWRKVAPAEDDSLIPLTLTTWVSPSESQQGFDVIIEYESVLETELADVIFTIPVFPQEPVDINTESSTCSDAEVVNMDQEMGTSIKISKIAANDAGALAFTIEAPYEDALYPMTVSFQESTRDKLAKSFTGMAIQSVVMANDHDQELPYDVITSLKSDEYLVQ | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 60628
Sequence Length: 546
Subcellular Location: Cytoplasm
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Q9SA78 | MASMAGPDHLFNLRNHFYLGAYQAAINNSEIPNLSQEDIVERDCLVHRAYIALGSYQLVISEIDEAAATPLQAVKLLAMYLSSPENKESTISSLREWLADPTVGNNAIIRLIAGTIFMHEEDYNEALKHTHSGGTMDLHALNVQIFIKMHRSDFAEKQLRVMQQIDEDHTLTQLASAWLNLAVGGSKIQEAYLIFQDFSEKYPMTSLILNGKAVCCMHMGNFEEAETLLLEALNKDAKDPETLANLVVCSLHVGKSSSRYLNQLKLSHPEHVLVKRAASAEDNFERALQSFA | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32602
Sequence Length: 292
Subcellular Location: Cytoplasm
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Q9MAX6 | MASPDLLFNLRNLFYLGAYQAAINNSDVPGLDADAAAERDAIVFRSYVALGSYQLVISEIDSSAATSLQAVKLLALYLSGDKESAIVSLKEWLSDSAVGSNPVLRLIAGIIFMHEQDYTEALKHTHSGGTLDLHALNVQIFIKMHRSDYAEKQLKIMQQIDEDHTLTQLANAWLDIAVGGSKIREAYLIFQDFAEKYPMTGMVLNGKAVCCMHMGSFDEAETLLLEALNKDAKDPETLANLIVCNLHLGKPSSRYLSQLKLSHPDHVLVKRAVSAEDNFERALQAVA | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31581
Sequence Length: 287
Subcellular Location: Cytoplasm
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Q5CT19 | MNKFTNLLIKRTASSLKGGDFRELFRKNYIPITQFEKVLLSVTSCVEGLKNPTDSNSVACITELTSNRALRRLQILMNSTPDGRRIIKNRPLIDSSKYSIKDLMAFPDDSLGRRYGEFLTTYNLEINRDPVRYVNSEDLAYVLTRFRQIHDILHTAFELNITVESEVTLKLFEFLHAGIPFGAIGAFMGLFITPILKVRPKEIFENHNKTHVYPSKPIQIHQDCDKYLNSLEITKKEILYPKRIVIKELIPWIYKAEKKMRHNIYTIMVEDWFPRPIADFQNYLNISPPPKQLQKYTRIKPMPFC | Function: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 35648
Sequence Length: 305
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Mitochondrion inner membrane
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Q54CZ2 | MNSSSNIIYKSFKNSKIFLNKQCIINNGLKLNKKYFTTTSTKENNNNNNNKNPKFIENNLFQKGLLTIGSAFVAFINPGRGDMVATLGEMTGGCAIKSMKQKMMLDPIGRQLLKEKPRIKESTYPLNIHLLPSTTFGGAYYRWMKEHGYSPDERTEVTLIQDEDDAYVMQRYREVHDFWHVLAGVRPDFQGEVAIKWFEFLQTGLPMNAIGSIIGPLRCSWNERNELINHMIPWAIKSSKSCVYLMNVKYEDHWEDDLNEFRAKLNFIPYKYLSDINQNKTTTINM | Function: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33136
Sequence Length: 286
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Mitochondrion inner membrane
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Q9VVG6 | MMQRCLRLQKPLALRRGLRLAQANSQAVATEAPEAEPLDAFERQYLKERIEISPFQRLFLGAGSSIAALLNPRRHDMIACLGETTGEDALWTILDTMQASEEGQRIMADKPRIHTSTIDFKYLETLPPDTFGAAYVKFLKDNQVTPDSRMAVRFLEDPKLAYLMTRYRECHDLIHTVLDMPTNMLGEVAVKWVEALNTGLPMCYGGAVFGAVRLRPKQRRAYLKHYLPWALENGKRTKPLMPVYWEKRWEQNIHELRSELGITVLNKA | Function: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30743
Sequence Length: 268
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Mitochondrion inner membrane
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Q2LZH7 | MMQRCWRLPVPLGKRGLAVVTHTRQAVVSDNPEAENLDGFEQQYLKERIEITTFQRMLLGAGSSIAAILDPRRHDMIACLGETTGEDALWNIMDTMHESEEGQRIMVEKPRIHTSTIDFKRLESLPADTFGAAYVKFLKDNKVTPDSRMAVRFLEDPKLAYLMTRYRECHDLIHTVLDMPTNMLGEVAVKWVEALNTGLPMCYGGAVFGAVRLRPKQRRAYLKHYLPWALENGKQMKPLMPVYWEERWEQNVNELRAELGIKLLNKF | Function: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30806
Sequence Length: 267
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Mitochondrion inner membrane
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Q9Y3A0 | MATLLRPVLRRLCGLPGLQRPAAEMPLRARSDGAGPLYSHHLPTSPLQKGLLAAGSAAMALYNPYRHDMVAVLGETTGHRTLKVLRDQMRRDPEGAQILQERPRISTSTLDLGKLQSLPEGSLGREYLRFLDVNRVSPDTRAPTRFVDDEELAYVIQRYREVHDMLHTLLGMPTNILGEIVVKWFEAVQTGLPMCILGAFFGPIRLGAQSLQVLVSELIPWAVQNGRRAPCVLNLYYERRWEQSLRALREELGITAPPMHVQGLA | Function: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29657
Sequence Length: 265
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Mitochondrion inner membrane
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Q3BYB0 | MTQISPTRLHSPLDRLLVEAQRALDTVFGNPPAERPNPAADTPDVVLDPEQRRHAAGLMRINHVGEVCAQGLYFGQAAVARDAHTQHHLLEAAQEETDHLAWCADRLHELDSRPSLFNPVWYAGSYALGALAGLRGDDWSLGFVVETERQVEAHLDEHLETLPQNDQRSRAILRVMKIDEARHADQAEQAGARPLPAPIPSAMALASKLMKTVAYRL | Cofactor: Binds 2 iron ions per subunit.
Function: Catalyzes the hydroxylation of 2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol during ubiquinone biosynthesis.
Catalytic Activity: a 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol + AH2 + O2 = A + a 3-demethylubiquinol + H2O
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24005
Sequence Length: 217
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Cell membrane
EC: 1.14.99.60
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Q9PD41 | MDVILSTRHHSHLDSLLIETQRVLEVVFGHPVAQRPSPANAFPNPLLSPKDRRHAAGLMRINHVGEICAQGLYFGQVAVARKEELRRHLLKAAQEETDHLSWCSDRLHELESRPSLFNPLWYSSSYMLGVFAGLLGDPWSLGFVVETERQVEAHLEKHLQVLPESDARSREILRVMKVEEARHADQADHAGARLLPSPIPGAMAWAARLMKVVAYRI | Cofactor: Binds 2 iron ions per subunit.
Function: Catalyzes the hydroxylation of 2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol during ubiquinone biosynthesis.
Catalytic Activity: a 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol + AH2 + O2 = A + a 3-demethylubiquinol + H2O
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24492
Sequence Length: 217
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Cell membrane
EC: 1.14.99.60
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P41735 | MLSRVSVFKPASRGFSVLSSLKITEHTSAKHTEKPEHAPKCQNLSDAQAAFLDRVIRVDQAGELGADYIYAGQYFVLAHRYPHLKPVLKHIWDQEIHHHNTFNNLQLKRRVRPSLLTPLWKAGAFAMGAGTALISPEAAMACTEAVETVIGGHYNGQLRNLANQFNLERTDGTKGPSEEIKSLTSTIQQFRDDELEHLDTAIKHDSYMAVPYTVITEGIKTICRVAIWSAERI | Cofactor: Binds 2 iron ions per subunit.
Function: Catalyzes the hydroxylation of 2-hexaprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis . Has also a structural role in the COQ enzyme complex, stabilizing COQ3 and COQ4 polypeptides .
Catalytic Activity: a 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol + AH2 + O2 = A + a 3-demethylubiquinol + H2O
PTM: Phosphorylated . Dephosphorylated by PTC7; dephosphorylation is essential for enzyme activation .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26060
Sequence Length: 233
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Mitochondrion inner membrane
EC: 1.14.99.60
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Q5RGU1 | MAGDMLLLMRGLARLSQAVIETQANSLRSGGVQTMQMTAEQAMGVAMQKIQEFTGSQQSVSDFSADMDSKYDFTASEQNFESAAHGGLDSDSVFRDANTGAANTYSQAQGKSKLFDGYKDPTSQFTGHTRSYHQDHSSVGGITAEDIEKAREAKQNGSKPHKQMLSERARERKVPVTRLGRLANFGGLAVGLGIGALAEVAKKSLRSEDKNGNKKAVLDSSPFLSEANAERIVRTLCKVRGAALKLGQMLSIQDDAFINPQLAKIFERVRQSADFMPIKQMTKALSNDLGPNWRDKLEMFEERPFAAASIGQVHLARMKDGREVAMKIQYPGVAQSINSDVNNLMTVLSMSNALPEGLFPEHLIDVMRRELALECDYIREAKCARKFKELLKDHPFFYVPDVISELSSQHVLTTELVPGFPLDQAEALTQELKNEICKNILNLCLRELFEFRYMQTDPNWSNFFYDPQTHRVALLDFGATRGFDESFTDVYIEIIKAAADGNREGVLKQSIDMKFLTGYESKAMVNAHVDAVMILGEAFASEEPFDFGAQSTTERIHNLIPVMLKQRLIPPPEETYSLHRKMGGSFLICSRLNAKISCKDMFEAAYSNYWSGRKKGPSQ | Function: Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. Its substrate specificity is unclear: does not show any protein kinase activity. Probably acts as a small molecule kinase, possibly a lipid kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway, as suggested by its ability to bind coenzyme Q lipid intermediates. Shows an unusual selectivity for binding ADP over ATP.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 68951
Sequence Length: 619
Domain: Adopts an atypical protein kinase-like fold: while it adopts a core fold similar to that of well-characterized protein kinase-like domains. The KxGQ motif completely occludes the typical substrate binding pocket. Nucleotide-binding opens the substrate binding pocket and flips the active site from inside the hydrophobic core into a catalytically competent, solvent-exposed posture.
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Mitochondrion
EC: 2.7.-.-
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Q8NI60 | MAAILGDTIMVAKGLVKLTQAAVETHLQHLGIGGELIMAARALQSTAVEQIGMFLGKVQGQDKHEEYFAENFGGPEGEFHFSVPHAAGASTDFSSASAPDQSAPPSLGHAHSEGPAPAYVASGPFREAGFPGQASSPLGRANGRLFANPRDSFSAMGFQRRFFHQDQSPVGGLTAEDIEKARQAKARPENKQHKQTLSEHARERKVPVTRIGRLANFGGLAVGLGFGALAEVAKKSLRSEDPSGKKAVLGSSPFLSEANAERIVRTLCKVRGAALKLGQMLSIQDDAFINPHLAKIFERVRQSADFMPLKQMMKTLNNDLGPNWRDKLEYFEERPFAAASIGQVHLARMKGGREVAMKIQYPGVAQSINSDVNNLMAVLNMSNMLPEGLFPEHLIDVLRRELALECDYQREAACARKFRDLLKGHPFFYVPEIVDELCSPHVLTTELVSGFPLDQAEGLSQEIRNEICYNILVLCLRELFEFHFMQTDPNWSNFFYDPQQHKVALLDFGATREYDRSFTDLYIQIIRAAADRDRETVRAKSIEMKFLTGYEVKVMEDAHLDAILILGEAFASDEPFDFGTQSTTEKIHNLIPVMLRHRLVPPPEETYSLHRKMGGSFLICSKLKARFPCKAMFEEAYSNYCKRQAQQ | Function: Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration . Its substrate specificity is unclear: does not show any protein kinase activity . Probably acts as a small molecule kinase, possibly a lipid kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway, as suggested by its ability to bind coenzyme Q lipid intermediates . Shows an unusual selectivity for binding ADP over ATP .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 71950
Sequence Length: 647
Domain: Adopts an atypical protein kinase-like fold: while it adopts a core fold similar to that of well-characterized protein kinase-like domains, a number of features are positioned to inhibit the kinase activity: (1) an atypical AAAS motif in an alanine-rich (A-rich) loop that replaces the canonical glycine-rich (G-rich) nucleotide-binding loop and limits ATP binding by establishing an unusual selectivity for ADP and (2) an N-terminal domain, containing the KxGQ motif, that completely occludes the typical substrate binding pocket . Nucleotide-binding opens the substrate binding pocket and flips the active site from inside the hydrophobic core into a catalytically competent, solvent-exposed posture .
Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Subcellular Location: Mitochondrion
EC: 2.7.-.-
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A3QJU3 | MLLSEVLQVLRGAGKVGAAFTSTQGEQLRLMACNSTFGAGMKAAAEAVEGVMGTVMGGGDMTSKTDEFAGIEKWEEMDLDEAAKWSVASEMPPDFSSKDGRGETSETPVGAATGTIKGAGWPAQNTRFLHVSASQHHFRFVHDSIVARLSPEDIQRAREAKQNIARPVRQKLNERAKERKVPATRISRLANFGGLAVGLGIGAIAEVAKQSFGGKRSEVGALLDSPLLSEANAERIVNTLCKVRGAALKIGQMLSIQDNSFINPQLQKIFERVRQSADFMPAWQMHKVLEEELGSGWREKLSSIEEKPFAAASIGQVHHGVLPGGKEIAMKIQYPGVAESIHSDINNLMSVLKMSVVLPDGLFADSSLEVLQRELAWECDYEREAKCAKRFRNLLKGDPVFVVPEVFDELSARRVITMELVNGVPLDRCVDLDQETRNEICFNILQLCLRELFEFRFMQTDPNWSNFFYNSEQNKIFLLDFGACRDYPELFTDHYIEVVHAASVGDRATVLKKSKDLKFLTGFEAKAFEDAHVEAVMILGEAFASAEAFDFGTQSTTQRIQSLIPVMLRHRLTPPPEESYSLHRKMAGSFLICSKLKARFSCRNMFLDVYNAYKRQQQERRSQV | Function: Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. Its substrate specificity is unclear: does not show any protein kinase activity. Probably acts as a small molecule kinase, possibly a lipid kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway. Required for podocyte migration.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 69460
Sequence Length: 624
Domain: Adopts an atypical protein kinase-like fold: while it adopts a core fold similar to that of well-characterized protein kinase-like domains. The KxGQ motif completely occludes the typical substrate binding pocket. Nucleotide-binding opens the substrate binding pocket and flips the active site from inside the hydrophobic core into a catalytically competent, solvent-exposed posture.
Subcellular Location: Mitochondrion membrane
EC: 2.7.-.-
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Q96D53 | MWLKVGGLLRGTGGQLGQTVGWPCGALGPGPHRWGPCGGSWAQKFYQDGPGRGLGEEDIRRAREARPRKTPRPQLSDRSRERKVPASRISRLANFGGLAVGLGLGVLAEMAKKSMPGGRLQSEGGSGLDSSPFLSEANAERIVQTLCTVRGAALKVGQMLSIQDNSFISPQLQHIFERVRQSADFMPRWQMLRVLEEELGRDWQAKVASLEEVPFAAASIGQVHQGLLRDGTEVAVKIQYPGIAQSIQSDVQNLLAVLKMSAALPAGLFAEQSLQALQQELAWECDYRREAACAQNFRQLLANDPFFRVPAVVKELCTTRVLGMELAGGVPLDQCQGLSQDLRNQICFQLLTLCLRELFEFRFMQTDPNWANFLYDASSHQVTLLDFGASREFGTEFTDHYIEVVKAAADGDRDCVLQKSRDLKFLTGFETKAFSDAHVEAVMILGEPFATQGPYDFGSGETARRIQDLIPVLLRHRLCPPPEETYALHRKLAGAFLACAHLRAHIACRDLFQDTYHRYWASRQPDAATAGSLPTKGDSWVDPS | Function: Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration . Its substrate specificity is unclear: does not show any protein kinase activity. Probably acts as a small molecule kinase, possibly a lipid kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway. Required for podocyte migration .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 60069
Sequence Length: 544
Domain: Adopts an atypical protein kinase-like fold: while it adopts a core fold similar to that of well-characterized protein kinase-like domains. The KxGQ motif completely occludes the typical substrate binding pocket. Nucleotide-binding opens the substrate binding pocket and flips the active site from inside the hydrophobic core into a catalytically competent, solvent-exposed posture.
Subcellular Location: Mitochondrion membrane
EC: 2.7.-.-
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Q566J8 | MWLELGAMLRRTCGPLGRAVRLPCGGALGPRPHWWGPCRSCLAQSVHQDQPGRGLSEDDIRRAREARLRKAPRPQLSDRSRERKVPASRISRLASFGGLAVGLGLGALAEVTKKSLPGGSLQHEGVSGLGSSPFLSEANAERIVQTLCTVRGAALKIGQMLSIQDNSFISPQLQRIFERVRQSADFMPRWQMMRVLEEELGKDWQDKVASLEEVPFAAASIGQVHQGLLKDGTEVAVKIQYPGVAQSIQSDVENLLALLKMSVGLPEGLFAEQSLQTLQQELAWECDYRREAACAQTFRKLLADDPFFRVPAVVQELCTTRVLGMELAGGIPLDQCQGLSQDIRNQICFQLLRLCLRELFEFRFMQTDPNWANFLYDASSHQVTLLDFGASRAFGTEFTDHYIEVVKAAADGDRDRVLQKSQDLKFLTGFETKAFSDAHVEAVMILGEPFAASGPYDFGAGETARRIQGLIPVLLRHRLRPPPEETYALHRKLAGAFLACARLHAHIACRDLFQDTYHRYWASRQTLPLPAAS | Function: Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. Its substrate specificity is unclear: does not show any protein kinase activity. Probably acts as a small molecule kinase, possibly a lipid kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway. Required for podocyte migration.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59232
Sequence Length: 533
Domain: Adopts an atypical protein kinase-like fold: while it adopts a core fold similar to that of well-characterized protein kinase-like domains. The KxGQ motif completely occludes the typical substrate binding pocket. Nucleotide-binding opens the substrate binding pocket and flips the active site from inside the hydrophobic core into a catalytically competent, solvent-exposed posture.
Subcellular Location: Mitochondrion membrane
EC: 2.7.-.-
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P0DP16 | QVMVQGDGDQPAARNAVPKDDNPGGEAGKFMNVLRRSGCPWEPWCG | Function: Its target is unknown, but this toxin may modulate voltage-activated calcium channels (Cav) or calcium-dependent potassium channels (KCa).
Sequence Mass (Da): 4943
Sequence Length: 46
Domain: The cysteine framework is C-C.
Subcellular Location: Secreted
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Q01519 | MADQENSPLHTVGFDARFPQQNQTKHCWQSYVDYHKCVNMKGEDFAPCKVFWKTYNALCPLDWIEKWDDQREKGIFAGDINSD | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 9788
Sequence Length: 83
Domain: The Cx9C/Cx10C motifs are involved in the recognition by the mitochondrial MIA40-ERV1 disulfide relay system and the subsequent transfer of disulfide bonds by dithiol/disulfide exchange reactions to the newly imported protein.
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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V5IRD7 | MFAQRQMFFARLAANLRAPAVRQTVQRRFASTPANESGKNAFVREREAVKQHAAETTELWRKISLYGIPPALALAGYNAYTLYNEHWEHWSHLPPLEERTEYPYQNIRTRNYPWGDGDKTLFWNESVNYHNRDKVT | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of Cox2 and heme A of Cox1 to the active site in Cox1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16043
Sequence Length: 136
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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O74471 | MSMMNRNIGFLSRTLKTSVPKRAGLLSFRAYSNEAKVNWLEEVQAEEEHAKRSSEFWKKVTYYIGGPALILASANAYYIYCKHQEHAKHVEDTDPGYSFENLRFKKYPWGDGSKTLFWNDKVNHLKKDDE | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15199
Sequence Length: 130
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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P98005 | MAITAKPKAGVWAVLWDLLTTVDHKKIGLMYTATAFFAFALAGVFSLLIRTQLAVPNNQFLTGEQYNQILTLHGATMLFFFIIQAGLTGFGNFVVPLMLGARDVALPRVNAFSYWAFLGAIVLALMSYFFPGGAPSVGWTFYYPFSAQSESGVDFYLAAILLLGFSSLLGNANFVATIYNLRAQGMSLWKMPIYVWSVFAASVLNLFSLAGLTAATLLVLLERKIGLSWFNPAVGGDPVLFQQFFWFYSHPTVYVMLLPYLGILAEVASTFARKPLFGYRQMVWAQMGIVVLGTMVWAHHMFTVGESTLFQIAFAFFTALIAVPTGVKLFNIIGTLWGGKLQMKTPLYWVLGFIFNFLLGGITGVMLSMTPLDYQFHDSYFVVAHFHNVLMAGSGFGAFAGLYYWWPKMTGRMYDERLGRLHFWLFLVGYLLTFLPQYALGYLGMPRRYYTYNADIAGWPELNLLSTIGAYILGLGGLVWIYTMWKSLRSGPKAPDNPWGGYTLEWLTASPPKAHNFDVKLPTEFPSERPLYDWKKKGVELKPEDPAHIHLPNSSFWPFYSAATLFAFFVAVAALPVPNVWMWVFLALFAYGLVRWALEDEYSHPVEHHTVTGKSNAWMGMAWFIVSEVGLFAILIAGYLYLRLSGAATPPEERPALWLALLNTFLLVSSSFTVHFAHHDLRRGRFNPFRFGLLVTIILGVLFFLVQSWEFYQFYHHSSWQENLWTAAFFTIVGLHGLHVVIGGFGLILAYLQALRGKITLHNHGTLEAASMYWHLVDAVWLVIVTIFYVW | Cofactor: Binds 1 copper B ion per subunit.
Function: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme a of subunit 1 to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 89214
Sequence Length: 791
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Cell membrane
EC: 7.1.1.9
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P32799 | MFRQCAKRYASSLPPNALKPAFGPPDKVAAQKFKESLMATEKHAKDTSNMWVKISVWVALPAIALTAVNTYFVEKEHAEHREHLKHVPDSEWPRDYEFMNIRSKPFFWGDGDKTLFWNPVVNRHIEHDD | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15021
Sequence Length: 129
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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A8E7D3 | MVSGKRIADVGYRLFSGSMMLLTVYGGYLCVVRAQRYMQRKKQLELAAQSENTASEIIKE | Function: Plays a role in the assembly or stability of the cytochrome c oxidase complex (COX).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6790
Sequence Length: 60
Subcellular Location: Mitochondrion membrane
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Q96I36 | MPTGKQLADIGYKTFSTSMMLLTVYGGYLCSVRVYHYFQWRRAQRQAAEEQKTSGIM | Function: Core component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly. Requires for coordination of the early steps of cytochrome c oxidase assembly with the synthesis of MT-CO1.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6600
Sequence Length: 57
Subcellular Location: Mitochondrion outer membrane
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Q8BH51 | MPSAKQLADIGYKTFSASMMLLTVYGGYLCSVRAYRYLQLRSARRQAAEEQKTSGVL | Function: Core component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly. Requires for coordination of the early steps of cytochrome c oxidase assembly with the synthesis of MT-CO1.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6380
Sequence Length: 57
Subcellular Location: Mitochondrion outer membrane
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P39103 | MSKYAWYTRVTDTLHRLTVLTLVGGTLYMSGGLAYTLYMNGKKYEQQVTQQKALEEDNQQLQSPTAPPTE | Function: Required for the synthesis of yeast cytochrome oxidase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7959
Sequence Length: 70
Subcellular Location: Mitochondrion membrane
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Q9FKT8 | MFRAVGSALKRNKEAFNGIARGFTTSSHRVFTSNITAASVTSASSSPLAGNSFYGLRSLLKGQNASMFRRMSTVASISSESKEGLKLLVTGGPQAQKWVGIWLFGSAAWVFSMVVLGGVTRLTRSGLSMTDWKFTGEFPPLSDEAWAKEFEKYKQSPEYKRVNKGMNLEDFKFIYWMEYAHRMWGRGLGIMFALPFSYFLRKGYITLRLGVQLSGLFALGAGQGFIGWWMVKSGLEEPPSEYSQPRVSPYRLAAHLTSAFAIYCGLFWTALSVVMPEPPAESLAWVRGAAKVKKLALPVSLIVGITAISGAFVAGNDAGRAFNTFPKMGDTWIPDNIFEMKPLLRNFFENTATVQLDHRLLATTTLIAIGTMWWFTRKLDIHPAVKALIGSTVGMTAVQVTLGVSTLLSYVPVSLGSAHQAGALTLLTLMLLLNHTLRRPSPSLLKSLPQVAKSNFS | Function: May be involved in the biosynthesis of heme A.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50127
Sequence Length: 457
Subcellular Location: Mitochondrion inner membrane
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Q08DG6 | MQRLLFTPLTAFLGSPCLRLLVPRVAPRTQCGCSCGIRRPLRPGQYSTISDVALQPGRSTVSLPSKAAERVVGRWLLVCSGTVAGAVILGGVTRLTESGLSMVDWHLIKEMKPPTSKEEWEAEFQKYQQFPEFKILNHDMTLAEFKFIWYMEYSHRMWGRLVGLAYILPAAYFWKKGWLTRGLKGRVLALCGLVCFQGLLGWYMVKSGLEEKPDSHDIPRVSQYRLAAHLGSALVLYCASLWTSLSLLLPQHKLTETRQLLRLRRFAHGTAGLVFLTALSGAFVAGLDAGLVYNSFPKMGESWIPEDLFTFSPLLRNVFENPTMVQFDHRVLGIASVTAVTVLYFLSRRIPLPRRTKIAATTLLALAYTQVGLGISTLLMYVPTPLAATHQSGSLALLSVALWLMNELRRVPK | Function: May be involved in the biosynthesis of heme A.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46126
Sequence Length: 413
Subcellular Location: Mitochondrion membrane
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Q7KZN9 | MQRLLFPPLRALKGRQYLPLLAPRAAPRAQCDCIRRPLRPGQYSTISEVALQSGRGTVSLPSKAAERVVGRWLLVCSGTVAGAVILGGVTRLTESGLSMVDWHLIKEMKPPTSQEEWEAEFQRYQQFPEFKILNHDMTLTEFKFIWYMEYSHRMWGRLVGLVYILPAAYFWRKGWLSRGMKGRVLALCGLVCFQGLLGWYMVKSGLEEKSDSHDIPRVSQYRLAAHLGSALVLYCASLWTSLSLLLPPHKLPETHQLLQLRRFAHGTAGLVFLTALSGAFVAGLDAGLVYNSFPKMGESWIPEDLFTFSPILRNVFENPTMVQFDHRILGITSVTAITVLYFLSRRIPLPRRTKMAAVTLLALAYTQVGLGISTLLMYVPTPLAATHQSGSLALLTGALWLMNELRRVPK | Function: May be involved in the biosynthesis of heme A.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46030
Sequence Length: 410
Pathway: Porphyrin-containing compound metabolism; heme A biosynthesis; heme A from heme O: step 1/1.
Subcellular Location: Mitochondrion membrane
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P40086 | MLFRNIEVGRQAAKLLTRTSSRLAWQSIGASRNISTIRQQIRKTQLYNFKKTVSIRPFSLSSPVFKPHVASESNPIESRLKTSKNVAYWLIGTSGLVFGIVVLGGLTRLTESGLSITEWKPVTGTLPPMNQKEWEEEFIKYKESPEFKLLNSHIDLDEFKFIFFMEWIHRLWGRAIGAVFILPAVYFAVSKKTSGHVNKRLFGLAGLLGLQGFVGWWMVKSGLDQEQLDARKSKPTVSQYRLTTHLGTAFFLYMGMLWTGLEILRECKWIKNPVQAISLFKKLDNPAIGPMRKISLALLAVSFLTAMSGGMVAGLDAGWVYNTWPKMGERWFPSSRELMDENFCRREDKKDLWWRNLLENPVTVQLVHRTCAYVAFTSVLAAHMYAIKKKAVIPRNAMTSLHVMMGVVTLQATLGILTILYLVPISLASIHQAGALALLTSSLVFASQLRKPRAPMRNVIITLPHSSKVTSGKILSEASKLASKPL | Function: Required for the assembly of yeast cytochrome oxidase. Involved in the biosynthesis of heme A and the initial step in this pathway, the hydroxylation of heme O, is thought to be catalyzed by a three-component mono-oxygenase consisting of COX15, ferredoxin YAH1 and ferredoxin reductase ARH1.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54658
Sequence Length: 486
Subcellular Location: Mitochondrion inner membrane
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Q02766 | MVLNRYSLITNCNHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIIAQENVNLYNMIFTIHGIIMIFFNIMPGLFGGFGNYFLPILCGSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLSTSLMSLSPVAVDVIIFGLLVSGVASIMSSLNFITTVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGVISHVISTNYCRNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWICTYMSSNFGMIHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGKNLRENSIVILWSMLFFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIFK | Cofactor: Binds 2 heme A groups non-covalently per subunit.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52729
Sequence Length: 476
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.9
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P20681 | MSGGVSLWIERWMLSTNAKDIGNLYLIFALFSGLLGTAFSVLIRMELSGPSVQYIADNQLYNSIITAHALLMIFFMVMPALIGGFGNFLLPLLVGGPDMAFPRLNNISFWLLPPSLILLVFSACIEGGAGTGWTIYPPLSGVQSHSGPSVDLAIFALHLSGVSSLLGAMNFITTIMNMRTPSIRLHKLALFGWAVIITAVLLLLSLPVLAGAITMLLTDRNFNTSFFETAGGGDPILFQHLFWFFGHPEVYILIIPAFGIISTTISAYSNKSVFGYIGMVYAMMSIGILGFIVWSHHMYTVGLDVDTRAYFTAATLIIAVPTGIKIFSWLATCYGGSIRLTPSMLFALGFVFMFTIGGLSGVVLANASLDIAFHDTYYVVAHFHYVLSMGAVFAMFSGWYFWIPKMLGLNYNMTLSKVQFWILFIGVNVTFFPQHFLGLQGMPRRISDYPDAFAGWNLISSFGSIISVVAAWLFLYIVYLQLVEGEYAGRFPWLNPQFYTDTLQALLNRSYPSLEWALSSPPKPHAFVSLPLQSNILRSLF | Cofactor: Binds 2 heme A groups non-covalently per subunit.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59737
Sequence Length: 541
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.9
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O03546 | MTFITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTIEAGAGTGWTVYPPLAGNLAHAGASVDLPIFSLHLAGVSSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDP | Cofactor: Binds 2 heme A groups non-covalently per subunit.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36792
Sequence Length: 337
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.9
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Q08855 | MATSAAAHGEHAEDHGHDEHAHPTGWRRSTNHKDIGTLYLIFAIIAGVIGAAMSLAIRAELMYPGVEYFHNTHLYNVFVTSHGVIMIFFMVMPAMIGGFGNWFLPLMIGAPDMAFPRMNNISFWLLPASFGLLLMSTFVEGEPGANGAGAGWTMYVPLSSSGHPGPAVDLAIFSLHIAGASSILGAINFITTILNMRAPGMTLHKMPLFAWSVLITAFLLLLSLPVLAGAITMLLTDRNFGTTFFAPEGGGDPLLYQHLFWFFGHPEVYILILPGFGMISHIISTFSRKPVFGYIGMVYAMAAIGGLGFVVWAHHMYIVGMDLDTEAYFVSATMIIAVPTGIKIFSWIATMWGGSIEFATPMLWALAFIFLFTVGGVTGVVLANASLDRVLHDTYYVVAHFHYVLSLGAIFAIFAGWYYWFPKMSGYMYNETLAEAHFWLIFIGVNLIFFPEHFLGISGMPRRYIDYPDAFAGWNLVSSIGSYISGFSVLLFIYCVYDAFAKNVPVGDNPWGAGATTLEWTLPSPPPVHEFEVLPRVE | Function: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59133
Sequence Length: 538
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Cell membrane
EC: 7.1.1.9
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O99818 | MLPRWMYSTNHKDIGTMYLIFGAWSGMLGLSMSMLIRMELGQPGTLIGNDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFPRMNNMSFWLLPPSLFLLINSSLIESGAGTGWTVYPPLSSNLSHYGPSVDLAIFSLHLAGASSILGAINFITTIVNMRSIGMTMERMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIICYNTGKKEPFGNLGMIYAMAAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSHIKFNTSILWALGFVFLFTVGGLTGIMLANSSIDIVLHDTYYVVAHFHYVLSMGAVFGIMGAIIHWFPMFLGLNLNSMLTKVQFMITFIGVNLTFFPQHFLGLAGMPRRYSDYPDFFTKWNFISSLGSLISLMGVIMLIIIIWTSIIEKKMINFSSFTNSSIEWMLNFPPSEHSFNQNNIILK | Cofactor: Binds 2 heme A groups non-covalently per subunit.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57126
Sequence Length: 512
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.9
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P13588 | MFLIMLKGHILMDAPTPWGIFFQDSASPQMEGIMELHNNIMFYLAIILFTVTWMMITIIRNFVAKKSPIAHKYMNHGTLIELIWTITPAFILILIAFPSFKLLYLMDEVMDPSLVVYAEGHQWYWSYQYPDFTNEDNEFIEFDSYIVPESDLEEGQFRMLEVDNRVIIPELTHTAFVISADVIHSYACPSLGIKADAYPGRLNQASVYINGPGTFFGQCSEICGILHSSMNIAIQSVSIKDFLLWLRDQMEG | Cofactor: Binds a dinuclear copper A center per subunit.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28931
Sequence Length: 252
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.9
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P34189 | MAHPTQLGFQDAASPVMEELLHFHDHALMIVFLISALVLYVIITTVSTKLTNMYILDSQEIEIVWTVLPALILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYENLSFDSYMIPTQDLTPGQFRLLETDHRMVVPMESPIRILVSAEDVLHSWALPAMGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLSHFENWSTLMLKDA | Cofactor: Binds a dinuclear copper A center per subunit.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26093
Sequence Length: 230
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.9
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P29658 | MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYXLDSQEIEVIWTXLPAVI | Cofactor: Binds a dinuclear copper A center per subunit.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 8117
Sequence Length: 72
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.9
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Q5SJ80 | MVDEHKAHKAILAYEKGWLAFSLAMLFVFIALIAYTLATHTAGVIPAGKLERVDPTTVRQEGPWADPAQAVVQTGPNQYTVYVLAFAFGYQPNPIEVPQGAEIVFKITSPDVIHGFHVEGTNINVEVLPGEVSTVRYTFKRPGEYRIICNQYCGLGHQNMFGTIVVKE | Function: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18563
Sequence Length: 168
Subcellular Location: Cell membrane
EC: 7.1.1.9
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P98054 | MEQIPASIWTLTAGVVVTLISFWVGHHHGLLPEQASEQAPLVDNFFDIMLTIGTALFLVVQGAIILFVIRYRRRAGEEGDGLPVEGNLPLEAFWTAIPALIVIFLGIYSVDIFQRMGGLNPGDHAMHSMHAPKSGMAVVAQAPSKTTSDATALLAAAQPPEIGIGASPDVQGKAPDLVVDVAGMQYAWIFTYPDSGIVSGELHIPVGKDVQLNLSARDVIHSFWVPQFRLKQDAIPGVPTTRFKATKVGTYPVVCAELCGGYHGAMRTQVIVHTPEDFETWRRQNQAIATAPVIPSLRDRHIHEMGVTAELVAQVEAIAHDPSAEKL | Cofactor: Binds a copper A center.
Function: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35356
Sequence Length: 327
Subcellular Location: Cell membrane
EC: 7.1.1.9
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Q01556 | MNLVAPTPWGLFFQDSATPQMEGIEELHNNIMFYLTIILFSVTWMMITIIKSFVNTKSPISHKYMNHGTLIELIWTITPAVILILIAFPSFKLLYLMDEVMDPSLVIYGEGHQWYWSYQYPDFTNADGEFVEFDSYIVPESDLEEGTLRMLEVDNRVIIPELTHTRFVISAADVIHSFACPSLGIKCDAYPGRLNQSSVYLNRQGTYFGQCSEICGILHSSMPIVIQSVSLKNFYYD | Cofactor: Binds a dinuclear copper A center per subunit.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27154
Sequence Length: 237
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.9
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P98023 | MSFILSFWMIFLIDSVIVLLSFVCFVCVWICVLLLSTVLFVTKINNIYCTWDFVSSKFVDTYWFVIGVMFIMCLLLRLCLLLYFGCLNFVSFDLCKVVGFQWYWVYFLFGETTIFSNLILESDYLVGDMRLLQCNHVLTLLSLVIYKLWVSAVDVIHSFTLASLGIKVDCIPGRCNEIILFASNNATIYGQCSELCGVLHGFMPIVICFI | Cofactor: Binds a dinuclear copper A center per subunit.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24145
Sequence Length: 210
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.9
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P00420 | MTHLERSRHQQHPFHMVMPSPWPIVVSFALLSLALSTALTMHGYIGNMNMVYLALFVLLTSSILWFRDIVAEATYLGDHTMAVRKGINLGFLMFVLSEVLIFAGLFWAYFHSAMSPDVTLGACWPPVGIEAVQPTELPLLNTIILLSSGATVTYSHHALIAGNRNKALSGLLITFWLIVIFVTCQYIEYTNAAFTISDGVYGSVFYAGTGLHFLHMVMLAAMLGVNYWRMRNYHLTAGHHVGYETTIIYTHVLDVIWLFLYVVFYWWGV | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix (Probable). COX3 is a catalytic core subunit .
PTM: The N-terminus is blocked.
Location Topology: Multi-pass membrane protein
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Sequence Mass (Da): 30360
Sequence Length: 269
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.9
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Subsets and Splits