ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
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 (ae... |
Q60E70 | MAVGGAGSSRSVAPCCCCAVLLAAALLFSAPATTEAYDALDPNGNITIKWDVMSWTPDGYVAVVTMFNYQQFRHIQAPGWQLGWTWAKKEVIWSMVGAQTTEQGDCSKFKGGTPHCCKKDPTVVDLLPGTPYNMQIANCCKAGVINTFNQDPSNAASSFQISVGLAGTTNKTVKLPKNFTLKAPGPGYTCGRAMIVRPTKFFTGDGRRATQALMTWNVTCTYSQFLAQKTPSCCVSLSSFYNDTIVNCPTCSCGCQNNGTSPGSCVNENSPYLQSAIDGPGKWTGQPLVQCTSHMCPIRIHWHVKLNYKEYWRVKITITN... | 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:... |
A2XHZ9 | MELHRCSLLALLLAVTCSVAVAYDPLDPKGNITIKWDVISWTPDGYVAMVTMSNYQMYRQILAPGWTVGWSWAKKEVIWSIVGAQATEQGDCSKFKGGIPHSCKRTPAIVDLLPGVPYNQQIANCCKAGVVSAYGQDPAGSVSAFQVSVGLAGTTNKTVKLPTNFTLAGPGPGYTCGPATIVPSTVYLTPDRRRRTQALMTWTVTCTYSQQLASRYPTCCVSFSSFYNSTIVPCARCACGCGHDGYRGNGGGGKNARAGDGRSRRNSGGGGGHSGGTECIMGDSKRALSAGVNTPRKDGAPLLQCTSHMCPIRVHWHVKL... | 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... |
Q7XR91 | MDVDQLILFVFVCCLSSRFADAYDPVDPNGNIIINWDFQSIENVYTVMVSVHNHQLYRHIEQPGWRLSWRWAGNEIIWGMTGAEATEQGDCHRIRGATRPHCCEKQPVIVDLPPGTPYNNQVSSCCRGGVLSSLTQNNRTSTAAFQMVVGGFRRATYHDGDRGPALPSRFGVGVPGYSCSNATKVNATSSERFLLPRARAPCAVTWQVTCTYSQFMEAASPTCCVSLSSFYNSTIVPCPRCSCGCPRSPTAPQCISEGEKPELPAGDGEAVAPVFRCTDHMCPVRVHWHVKISYREYWRVKVTITNYNQVKNYSDWNLVV... | 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:... |
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(+)
Loc... |
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(+)
Loc... |
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(+)
Loc... |
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(+)
Loc... |
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(+)
Loc... |
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(+)
Loc... |
B4SH92 | MPEKLQLLLDRIKPASRSLSDAARAHLDDLTKPQGSLGRLEEIALKYVLATGNLSPLLSKKKICCFAADHGVAAEGVSAFPAEVTPQMVYNMLGGGAAINVLTRHAGVDLDVVDMGVNHDFPDLAGLVKRKVQPGSANMATGPAMSEEDALQALLCGAELAAEAQEAGYHLLGTGEMGIANTTPATALYAVLLDVSVESITGRGTGIDDERLLHKIAVIKQAIAVNGSRCTTPFATLAALGGYEIAAIAGFILGAAAARTPVVVDGFISSAGAVVALKLCPAVEDYLFFSHLSNEQGHRAVMEKLGARPILDLDLRLGEG... | 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
Pa... |
B2RIR0 | MKTFNIKSPDQAIRQALIDRIDNLAKPEGSLGMLEELALQIGLIQQTLSPRLRNPHNIIFAADHGIADEGVSFSPKEVTWQVINNFLGGGAGINFLCRQHGFELVLVDGGIDFDFPEGLDIIDRKVRKGTRNYLYEAALTGEEMEQAVTAGAEVVSDCHHRGCNVVSFGEMGVANTSTSSMWMSFLTGIDLKDCVGAGSGLDSEGVRHKYNILKQAKENYKGNGSTEDVITYFGGLEMLMAVGGMLQAAELGMLIIVDGFIMTNCLLAASQFYPEVCDYAVFGHCGDESGHARLLEYMKAKPLLNLGLRLGEGSGAVCSY... | 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
Pa... |
Q9I465 | MSLQWWRDTCREADPQMRRRAAERQDRLTKPRGSLGRLEQVAIDLAALQGRERPSLERIWVTVFAGDHGVVAEGISAYPQAVTGEMLRNFVRGGAAISVLARELGAGLEVVDLGTAFPLEALPGVRHLRLAAGTANFVEAPAMGAEECLLALEAGRESVRRAEQAGSQLFIGGEMGIGNTTAAAAMACALLDAPASALVGPGTGLDASGVAHKAAVIERALALHGAHRADPFETLRRLGGLEIAALAGAYLACAQKGMVALVDGYICSVAALCAVRLNPACRDWLLFAHSGAEPGHRHVLEALAAQPLLDLGLRLGEGSG... | 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
Pa... |
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... |
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... |
Q3IRY6 | MVTFLAGGTGTPKLRYGAETVFDTADTPVVCNTGDDVELGGLVVCPDVDTVLFAAADRLDRETWWGIDGDTTETHEELRALADAADLDTGPRYLPDKKQTAGRDIARWRRFSGVAEFMEIGDTDRAVHITRTSLLDEGKRLTEATATLADALGVDHPVLPMSDDPVATLIDTDEGLVHFQEFWVHRRAEPTINGVEFRGADAAEPTPEVREALADPVVIGPSNPITSIGPMVALDGIRKALAETPVVAVSPFVEDRVFSGPADDLMAADGYAPSTAGVAEAYPFADAFVVDEADETPLERPTVRTDTELGSPADGERVCR... | 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... |
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), wit... |
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-gl... |
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-gl... |
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-gl... |
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), wit... |
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-gl... |
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... |
F4HQ84 | MATKAASSSSLPKSGAISKGYNFASTWEQSAPLTEQQQAAIVSLSHAVAERPFPANLVHEHVHRPENGLSVSVEDTHLGDSGAIEAVLVNTNQFYKWFTDLESAMKSETEEKYRHYVSTLTERIQTCDNILHQVDETLDLFNELQLQHQGVTTKTKTLHDACDRLLMEKQKLMEFAEALRSKLNYFDELENVSSNFYSPNMNVSNSNFLPLLKRLDECISYIEDNPQYAESSVYLLKFRQLQSRALGMIRTYILAVLKTAASQVQAAFRGTGGNKTSVSEGVEASVIYVRFKAAANELKPVLEEIESRSARKEYVQILAE... | 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 ... |
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 ... |
Q54TT4 | MNNQTNQQSQTQSQSQQRINFDITGWEKKSKLSTQQYLLINNLNKSTQEKPLPQKYLEDKINNDIKKEENQQLQQQQQQQQQQQQQQQSPIIENFMDNFNPKTDIDNLSDFYQWYSIIDKNNPHLHQYEWFLETIVNYSKGSNQLLSMVENCDKLVESIQTDYSNLTKKTNQLNEDCEKFFNEELKLRYIAQSIHDKLKFYNQLEIQTKKFNTTNFNVTDSTFLTSLENLENSINFMKSNSTFMESNKYLTQYGFIFSRALGLIKDYISSNLKILSRDIINAQKQLKTSVSTPTSPQLQSSSGGSPLINDFSNSTDFNDL... | 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 | MDDVERIQSENENLRKIRNRLMQWESKTDPLAALSIQQEEHLDVLTNLWRDSGPSAPAPTTPTQVGPTDSSAAATSQSGDDIRLPAEGLQNTNEFLLWFADVSAEIEQRGDADYHKYLQQLEQRKAECSHMLDQIAGAMERLGALCDEYDFVSQKTSALNTASEQLIEEQERLQELSHEIQRRLHYFSQVELLNQRLQSPTLSVASEAFRECLNKIDECLNYIEENPKFKDAAAYNVKYRQCLAKASGLVRNYVTSVINQATEATLHPKNNMPDASAALKAPDAAFALYYGKYQTAAAKVKRVAQLIESRSEHSLDYAQL... | 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 | MAEAALLLLPEAAAERDAREKLALWDRRPDTTAPLTDRQTDSVLELKAAAENLPVPAELPIEDLCSLTSQSLPIELTSVVPESTEDILLKGFTSLGMEEERIETAQQFFSWFAKLQTQMDQDEGTKYRQMRDYLSGFQEQCDAILNDVNSALQHLESLQKQYLFVSNKTGTLHEACEQLLKEQSELVDLAENIQQKLSYFNELETINTKLNSPTLSVNSDGFIPMLAKLDDCITYISSHPNFKDYPIYLLKFKQCLSKALHLMKTYTVNTLQTLTSQLLKRDPSSVPNADNAFTLFYVKFRAAAPKVRTLIEQIELRSEK... | 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 | MFDQLEFYPAVNYEDNETQNDIKLPEVAKLENIETVHSISKERRDSLTEILNDSSSLPARPFSLPNPNNSTVEKQSLFPFEEKMNPIWIISRPTFSIEQDAEKKINELQTFTNIIDQILGQTNNIESTLLSMKEKFESSEKKLSEFSEMCENLSTDEMRFSEIADGIRKGLTIFAPLKELTRVFRHPPPDFAGKVSFKEHITQLNTCIMFLEENLDFQESPHYLGQYKKLLSQAMDIFKPYFIRIIKQTTDQVLKDSKKMDVHKQLHSSLFYARFSAVGHNLCPTITELCKLCSKESLDAFLPAFYDVYFQCRTRLLKPV... | 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 m... |
P40094 | MARSRKNSLVRDIASHPTIPESQTIVGLLDDSYLFDKLKKLSLAVENSDSLQRTDVSEGCSEVNGSEATTSADVKKTNKYLYYTTYLDQLNIKIDEYKVVLDQTRQVNDQLDSSIKKFRKISQDTGAFIEETKTIYEKQSKLSNLTESIPKALHYFEVLDPIMRRLNHATSPAIVKKSSFTTMLATIDESLRFLDENSDLKDAAAYRIKFKQCLIRACELISHFLTNLLKQTNQEILDKTKNKNSLTGLPSTTRDAFLYSKFYTIADTFKIQVSEIVKRSNEKAYNKYHDELNSILYECFNHYFQTRLRLLTPVIWSHID... | 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 org... |
Q8L838 | MPEIEQDDAAAETVDSSTVKFGTPEALEYVRSLTDVGAMTRLLHECIAYQRSLDSDLDTLLSQRTELDRNLVQLQRSAEILDIVKADADHMLGNVRSTCDLADQVSGKVRELDLAQSRVNVTLSRIDAIVERGNCIEGVKTALESEDYESAAKFVQRFLQIDLQYKDSGSDQSEQLHASKEQLEGIAKKKLLAAIDQRDHPTILRFVRLYSPLGMETEGLQLYVGYLKKVIALRGRMEYENVVELMEQGLGQVNFVGCLTNLFKDIVMAIEENDEILRGLCGEDGVAYAICELQEECDLRGSLILKKYMDFRKLAILASD... | 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 | MPEPILHSKFLSGLPAGRKNGVRHGEKPEKVGEKQFDFTRKIRELRLELEIKKREEERIEKDIAIILEENTIDGGEQNRSFGLAVTRLNNHMLVVENSAKQLTSALKNISVLADTISGRVSALDVAKTRVVGCLQLAGDMRDLGVCAEGIDDAIRSEDFETASQHIHRFLTLDQAVFQIREFKQKDATDSIRHSYEVLSSAKERLSKILKSRLTESVQKGDVAEMQRFIKMFPLIHEPDEGLQRYSVFLNQKIDKLAEDNLAIMKAGGTDDNRRNVLYADTLFMFFEGVAEIIESNLPVLEHSYGLEKLLDFMFILQARI... | 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.... |
Q29RB1 | MEEAASPARRRGGPAGVSAVQTDTIEALTELEDLERVYAQLCAEEAEVQVELDALVGQQNNIETKMLSLQRMGPNLQLIEGDAVQLSGMINFTCSLAENVSSKVRQLDLTKKRLYQAIQRADDILDLKFCTDGVQTALRNQDYEQAAAHIHRYLSLDQSVIELSKQGGEGSAVEASLALLQEAERNLKTLVTTRLEEAVATGDLPQVERFFKILPLLGLHEQGLARFAQYLCSQLASKAEENLILAVGSDLGERRAPVIFADTLTLLLEGIARIVETHQPIVETYYGPGRLHTLLAHLQKECDKQAQKIVDKFIQQRDYN... | 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 | MDELIVDFNNLDSNLSIDDAKKYLQNLISRDKAIEINLKQHIKLKDDLEIQMESFDNEIPEYLTLSLKKSNELNNRISSTCQLAENLSSKVKKLDNIRERIKDTLKKVDDIIDLKNCIEGVQISIEKEDYEGAAFHINRYLSIDKSVLEDNSSEKLSIAEKKLLSMIESKYQQSLQDNDQKQVLRFCILYVPLEKPLEGIDKYCNYLKNQSKKLDAMITHYRNYIQSPKTIKPISAVSVITKIFEHFAAIIEDDLPIIKSEFGVLHCPHFILNITQQCDYYSSKVYDSFNDQFQTNKNVNDILVYKQQLEKSQQSIQDSG... | 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 | MSVLEQLGALDIGTNEQVDETLQRIADEEAKVNEKLESLLAKQCQIEAKMSGIGRSLSLLHTVDSDSNKLNDQIVNTAQLAESVSAKVRRLDLARCRASECQQRVHDLIDLHLCSQGVVKAIGEEDYEKSATHIARFLAMDQQLLRRTADDVQGSITSVSDAVKTLEDATEKTRVLIAKRFDEAVKADDLASVERFFKIFPLVGCHRTGIEKFSLYICQKLANKAQKELRNAQDIAKAESRLQLAYADRLTAILENFARVVEVNQPIIEAFYGQASSSLIDMVSILQHECDTEVKNLLMEFNKNRQIQYRSKQVNESTQR... | 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 | MADLDSPPKLSGVQQPSEGVGGGRCSEISAELIRSLTELQELEAVYERLCGEEKVVERELDALLEQQNTIESKMVTLHRMGPNLQLIEGDAKQLAGMITFTCNLAENVSSKVRQLDLAKNRLYQAIQRADDILDLKFCMDGVQTALRSEDYEQAAAHTHRYLCLDKSVIELSRQGKEGSMIDANLKLLQEAEQRLKAIVAEKFAIATKEGDLPQVERFFKIFPLLGLHEEGLRKFSEYLCKQVASKAEENLLMVLGTDMSDRRAAVIFADTLTLLFEGIARIVETHQPIVETYYGPGRLYTLIKYLQVECDRQVEKVVDK... | 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... |
P46946 | MVTGEENVYLKSSLSILKELSLDELLNVQYDVTTLIAKRVQALQNRNKCVLEEPNSKLAEILCHEKNAPQQSSQTSAGPGEQDSEDFILTQFDEDIKKESAEVHYRNENKHTVQLPLVTMPPNRHKRKISEFSSPLNGLNNLSDLEDCSDTVIHEKDNDKENKTRKLLGIELENPESTSPNLYKNVKDNFLFDFNTNPLTKRAWILEDFRPNEDIAPVKRGRRKLERFYAQVGKPEDSKHRSLSVVIESQNSDYEFAFDNLRNRSKSPPGFGRLDFPSTQEGNEDKKKSQEIIRRKTKYRFLMASNNKIPPYEREYVFKR... | 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 ... |
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:... |
P51973 | MLCVLAGAAYGVFRTEAALSSQWRAEAVSGVPLTVEVTDMPRSDGRRVQFAAKAVDSGGRTFDLLLSDYKRREWAVGSRWRITARVHPVVGELNLRGLNREAWALSNGVGGVGTVGADRVLLHGGSGWGIAVWRSRISRNWRQADADGGLSDGIGLMRALSVGEQSALRPGLWQAFRPLGLTHLVSISGLHVTMVAVLFAWLAKRLLACSPRLPARPRAWVLAAGCAGALFYALLAGFSVPTQRSVLMLAAFAWAWRRGRLSAWATWWQALAAVLLFDPLAVLGVGTWLSFGLVAALIWACAGRLYEGKRQTAVRGQWAA... | 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 | MKFGKRHYRPQVDQMDCGVASLAMVFGYYGSYYFLAHLRELAKTTMDGTTALGLVKVAEEIGFETRAIKADMTLFDLPDLTFPFVAHVLKEGKLLHYYVVTGQDKDSIHIADPDPGVKLTKLPRERFEEEWTGVTLFMAPSPDYKPHKEQKNGLLSFIPILVKQRGLIANIVLATLLVTVINIVGSYYLQSIIDTYVPDQMRSTLGIISIGLVIVYIFQQILSYAQEYLLLVLGQRLSIDVILSYIKHVFHLPMSFFATRRTGEIVSRFTDANSIIDALASTILSIFLDVSTVVIISLVLFSQNTNLFFMTLLALPIYTV... | 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 memb... |
Q99027 | MKNLIKKFTIAVIVLSILYISYTTYISMNGIIIGTKIHKNDKSQFMIEEISESSYGQFVGLRQGDIILKINKEKPSDKHLKWGYLSHINSLDILRSGKKIHLKDFDLVTLNRPYSFFLFVLPLFFYFLSIICIFYILKVNKKRRSFAAYILILLLLDISIAYISAGGPFRGHIINRYINLFTFISSPILYLQFIQRYLGEIGKTFLNRISFLYIIPIFNLGIEFFQDYLQVDIDFLATLNLVSFATLTLFSFSAIYLHLNKYKYAEHSFILKLLILTNTLSFAPFLIFFVLPIIFTGNYIFPALASASLLVLIPFGLVYQ... | 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 h... |
P35445 | MVLAAARVLLLTLAALGASGQGQMPLGGDLGPQMLRELQETNAALQDVRDLLRQQVKEITFLKNTVMECDACGMQPARTPKLTVRPLSQCSPGFCFPGVACTETANGARCGPCPEGFTGNGSHCADVNECTAHPCFPRVRCINTSPGFRCEACPPGFSGPTHEGVGLAFAKANKQVCTDINECETGQHNCVPNSVCVNTVGSFQCGPCQPGFVGDQASGCRRRPQRFCPDGTPSPCHEKADCVLERDGSRSCVCAVGWAGNGLICGRDTDLDGFPDEKLRCSERQCRKDNCVTVPNSGQEDVDQDGIGDACDPDADGDGV... | 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... |
P49747 | MVPDTACVLLLTLAALGASGQGQSPLGSDLGPQMLRELQETNAALQDVRELLRQQVREITFLKNTVMECDACGMQQSVRTGLPSVRPLLHCAPGFCFPGVACIQTESGARCGPCPAGFTGNGSHCTDVNECNAHPCFPRVRCINTSPGFRCEACPPGYSGPTHQGVGLAFAKANKQVCTDINECETGQHNCVPNSVCINTRGSFQCGPCQPGFVGDQASGCQRRAQRFCPDGSPSECHEHADCVLERDGSRSCVCAVGWAGNGILCGRDTDLDGFPDEKLRCPERQCRKDNCVTVPNSGQEDVDRDGIGDACDPDADGDG... | 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... |
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 simila... |
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 farn... |
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 wit... |
Q949P2 | MASEDTLSSNPLLQNFDFPPFDSVDAHHVRPGIRALLQQLEAELEQLEKAVEPSWPKLVEPLEKIIDRLSVVWGMINHLKAVKDTPELRAAIEEVQPEKVKFQLRLGQSKPIYNAFKAIRESPDWNSLSEARQRLVEAQIKEAVLSGIALEDDKREEFNKIEQELEKLSHKFSENVLDATKKFEKLITDKKEIEGLPPSALGLFAQAAVSKGHETATADTGPWLITLDAPSYLPVMQHAKNRALREEVYRAYLSRASSGDLDNTAIIDQILKLRLEKAKLLGYRNYAEVSMATKMATVEKADELLEKLRSASWDPAVQDI... | 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 als... |
Q93Y22 | MVVLAAAIVVKSGKVIVSRHYVDMSRIRIEGLLAAFPKLVGMGKQHTYIETENVRYVYQPIEALFLLLVTTKQSNILEDLATLTLLSKLVPEYSMSLDEEGISRASFELIFAFDEVISLGHKESVTVAQVKQYCEMESHEEKLHKLVMQSKINDTKDVMKRKANEIDKSKIEKNKPGGFSSMGSMGSGRLESGFNELSISSGGGGGYGSGSGFGMISDVDPINTKPKDRSRSSVTAPPKSSGMKLGKSGKNQLMESLKAEGEDVIEDVKPTGQSKAAAPPPTDPFTLTVEEKLNVALRRDGGLSSFDMQGTLSLQILNQE... | 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 membra... |
Q09236 | MVLIAACILSKTGKLLVARQFVNDMMRSRLEGLVDAFPKLIGNEKEAATRQHTFVETDSVRYVYHPLDNIYLVLVTTKNSNILEDLETLRLFVRVIPEYCRSNEEKEILAHDFDLIFAFDEVVTLGYRESVNLAQIRTFTEMDSHEERVFMQIKEAQEKAAKQAMAEKAKELKRAQKEALSRGLKPSYQSSTGISSSSTPNAAAVSEPAAPRPSAPKGPIGGGKALKLGGKTNNEDDFLDTLRQQGQSIAPVQKASLSGGVSSLAAPISTAPRVKREVVHVRTEEKINTRVSRDGGLESGEVQATVTLSIGSPEFIPISI... | 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 membra... |
Q55EZ6 | MVVLAAAICTKNGKALLSRQFSEMTKSRVEGLLAAFPKLIGLGRQHTFIETENIRYVYQPLESLYIVLITNKNSNILEDLETLHLLAKLVPEYSNFDEYDISKNAFELIFTFDEVIAMGYKERVTLQQIKHFISMESHEEERFRMEEKIKQKEAQILASSKAKEIERMRHEEMLRGKRSGGYTGISGGGGMGSGGMGSNQYRDNDRDNYHSNNNNNNNNNNNNNNNNNNNRDRDRGDSPNTSRPSAASSGSQGGMILGGKSGTNKNSAIAQVLKEEKIVEKVEDVEQLLDSQISQIPETPTVPQEGVHITVEESFTSFVE... | 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 membra... |
P48444 | MVLLAAAVCTKAGKAIVSRQFVEMTRTRIEGLLAAFPKLMNTGKQHTFVETESVRYVYQPMEKLYMVLITTKNSNILEDLETLRLFSRVIPEYCRALEENEISEHCFDLIFAFDEIVALGYRENVNLAQIRTFTEMDSHEEKVFRAVRETQEREAKAEMRRKAKELQQARRDAERQGKKAPGFGGFGSSAVSGGSTAAMITETIIETDKPKVAPAPARPSGPSKALKLGAKGKEVDNFVDKLKSEGETIMSSSMGKRTSEATKMHAPPINMESVHMKIEEKITLTCGRDGGLQNMELHGMIMLRISDDKYGRIRLHVENE... | 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 fr... |
Q5XJY5 | MVLLAAAVCTKAGKAIVSRQFVEMTRTRIEGLLAAFPKLMNTGKQHTFVETESVRYVYQPMEKLYMVLITTKNSNILEDLETLRLFSRVIPEYCRALEENEISEHCFDLIFAFDEIVALGYRENVNLAQIRTFTEMDSHEEKVFRAVRETQEREAKAEMRRKAKELQQARRDAERQGKKAPGFGGFGSSAVSGGSTAAMITETIIETDKPKVAPAPARPSGPSKALKLGAKGKEVDNFVDKLKSEGETIMSSNMGKRTSEATKVHAPPINMESVHMKIEEKITLTCGRDGGLQNMELHGMIMLRISDDKFGRIRLHVENE... | 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 membra... |
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 | MVVLAASITTRQGKPLLSRQFKDLSKDRVLELLSNFQNLVSEISSDHTFVEDKHVRYVYRPFDNYYIILITNRQSNIIKDLATLNLFSQTINSYLSSFQDQEIFHNAFEILSSFDEIVSMGGYKENLSFTQVQTYLSMESHEERIQEIIERNKEIEATEERKRRAKEIARKEHERKHGFMSSNGDYDGANRFMGSKDPNVTNAINSYYSHASPAAQQSYLQSSHAAAAEVAPVASPMATSQRAGHSATGGMKLGGGAGRRAGAAPRPSAISSASSGTPPPPEEDVPENNGILISIKEVINAEFSRDGTIHSSELKGVLEL... | 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 membra... |
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 me... |
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 me... |
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
Pat... |
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
Pat... |
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
Pat... |
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
Pat... |
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
Pat... |
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 mem... |
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 mem... |
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-p... |
Q5RGU1 | MAGDMLLLMRGLARLSQAVIETQANSLRSGGVQTMQMTAEQAMGVAMQKIQEFTGSQQSVSDFSADMDSKYDFTASEQNFESAAHGGLDSDSVFRDANTGAANTYSQAQGKSKLFDGYKDPTSQFTGHTRSYHQDHSSVGGITAEDIEKAREAKQNGSKPHKQMLSERARERKVPVTRLGRLANFGGLAVGLGIGALAEVAKKSLRSEDKNGNKKAVLDSSPFLSEANAERIVRTLCKVRGAALKLGQMLSIQDDAFINPQLAKIFERVRQSADFMPIKQMTKALSNDLGPNWRDKLEMFEERPFAAASIGQVHLARMKD... | 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 kinas... |
Q8NI60 | MAAILGDTIMVAKGLVKLTQAAVETHLQHLGIGGELIMAARALQSTAVEQIGMFLGKVQGQDKHEEYFAENFGGPEGEFHFSVPHAAGASTDFSSASAPDQSAPPSLGHAHSEGPAPAYVASGPFREAGFPGQASSPLGRANGRLFANPRDSFSAMGFQRRFFHQDQSPVGGLTAEDIEKARQAKARPENKQHKQTLSEHARERKVPVTRIGRLANFGGLAVGLGFGALAEVAKKSLRSEDPSGKKAVLGSSPFLSEANAERIVRTLCKVRGAALKLGQMLSIQDDAFINPHLAKIFERVRQSADFMPLKQMMKTLNNDL... | 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 kin... |
A3QJU3 | MLLSEVLQVLRGAGKVGAAFTSTQGEQLRLMACNSTFGAGMKAAAEAVEGVMGTVMGGGDMTSKTDEFAGIEKWEEMDLDEAAKWSVASEMPPDFSSKDGRGETSETPVGAATGTIKGAGWPAQNTRFLHVSASQHHFRFVHDSIVARLSPEDIQRAREAKQNIARPVRQKLNERAKERKVPATRISRLANFGGLAVGLGIGAIAEVAKQSFGGKRSEVGALLDSPLLSEANAERIVNTLCKVRGAALKIGQMLSIQDNSFINPQLQKIFERVRQSADFMPAWQMHKVLEEELGSGWREKLSSIEEKPFAAASIGQVHHG... | 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 kinas... |
Q96D53 | MWLKVGGLLRGTGGQLGQTVGWPCGALGPGPHRWGPCGGSWAQKFYQDGPGRGLGEEDIRRAREARPRKTPRPQLSDRSRERKVPASRISRLANFGGLAVGLGLGVLAEMAKKSMPGGRLQSEGGSGLDSSPFLSEANAERIVQTLCTVRGAALKVGQMLSIQDNSFISPQLQHIFERVRQSADFMPRWQMLRVLEEELGRDWQAKVASLEEVPFAAASIGQVHQGLLRDGTEVAVKIQYPGIAQSIQSDVQNLLAVLKMSAALPAGLFAEQSLQALQQELAWECDYRREAACAQNFRQLLANDPFFRVPAVVKELCTTR... | 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 kina... |
Q566J8 | MWLELGAMLRRTCGPLGRAVRLPCGGALGPRPHWWGPCRSCLAQSVHQDQPGRGLSEDDIRRAREARLRKAPRPQLSDRSRERKVPASRISRLASFGGLAVGLGLGALAEVTKKSLPGGSLQHEGVSGLGSSPFLSEANAERIVQTLCTVRGAALKIGQMLSIQDNSFISPQLQRIFERVRQSADFMPRWQMMRVLEEELGKDWQDKVASLEEVPFAAASIGQVHQGLLKDGTEVAVKIQYPGVAQSIQSDVENLLALLKMSVGLPEGLFAEQSLQTLQQELAWECDYRREAACAQTFRKLLADDPFFRVPAVVQELCTT... | 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 kinas... |
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
|
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, comple... |
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, comple... |
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, comple... |
P98005 | MAITAKPKAGVWAVLWDLLTTVDHKKIGLMYTATAFFAFALAGVFSLLIRTQLAVPNNQFLTGEQYNQILTLHGATMLFFFIIQAGLTGFGNFVVPLMLGARDVALPRVNAFSYWAFLGAIVLALMSYFFPGGAPSVGWTFYYPFSAQSESGVDFYLAAILLLGFSSLLGNANFVATIYNLRAQGMSLWKMPIYVWSVFAASVLNLFSLAGLTAATLLVLLERKIGLSWFNPAVGGDPVLFQQFFWFYSHPTVYVMLLPYLGILAEVASTFARKPLFGYRQMVWAQMGIVVLGTMVWAHHMFTVGESTLFQIAFAFFTAL... | 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 transf... |
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, comple... |
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
|
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... |
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... |
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
|
Q9FKT8 | MFRAVGSALKRNKEAFNGIARGFTTSSHRVFTSNITAASVTSASSSPLAGNSFYGLRSLLKGQNASMFRRMSTVASISSESKEGLKLLVTGGPQAQKWVGIWLFGSAAWVFSMVVLGGVTRLTRSGLSMTDWKFTGEFPPLSDEAWAKEFEKYKQSPEYKRVNKGMNLEDFKFIYWMEYAHRMWGRGLGIMFALPFSYFLRKGYITLRLGVQLSGLFALGAGQGFIGWWMVKSGLEEPPSEYSQPRVSPYRLAAHLTSAFAIYCGLFWTALSVVMPEPPAESLAWVRGAAKVKKLALPVSLIVGITAISGAFVAGNDAGR... | 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
|
Q08DG6 | MQRLLFTPLTAFLGSPCLRLLVPRVAPRTQCGCSCGIRRPLRPGQYSTISDVALQPGRSTVSLPSKAAERVVGRWLLVCSGTVAGAVILGGVTRLTESGLSMVDWHLIKEMKPPTSKEEWEAEFQKYQQFPEFKILNHDMTLAEFKFIWYMEYSHRMWGRLVGLAYILPAAYFWKKGWLTRGLKGRVLALCGLVCFQGLLGWYMVKSGLEEKPDSHDIPRVSQYRLAAHLGSALVLYCASLWTSLSLLLPQHKLTETRQLLRLRRFAHGTAGLVFLTALSGAFVAGLDAGLVYNSFPKMGESWIPEDLFTFSPLLRNVFE... | 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
|
Q7KZN9 | MQRLLFPPLRALKGRQYLPLLAPRAAPRAQCDCIRRPLRPGQYSTISEVALQSGRGTVSLPSKAAERVVGRWLLVCSGTVAGAVILGGVTRLTESGLSMVDWHLIKEMKPPTSQEEWEAEFQRYQQFPEFKILNHDMTLTEFKFIWYMEYSHRMWGRLVGLVYILPAAYFWRKGWLSRGMKGRVLALCGLVCFQGLLGWYMVKSGLEEKSDSHDIPRVSQYRLAAHLGSALVLYCASLWTSLSLLLPPHKLPETHQLLQLRRFAHGTAGLVFLTALSGAFVAGLDAGLVYNSFPKMGESWIPEDLFTFSPILRNVFENPT... | 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
|
P40086 | MLFRNIEVGRQAAKLLTRTSSRLAWQSIGASRNISTIRQQIRKTQLYNFKKTVSIRPFSLSSPVFKPHVASESNPIESRLKTSKNVAYWLIGTSGLVFGIVVLGGLTRLTESGLSITEWKPVTGTLPPMNQKEWEEEFIKYKESPEFKLLNSHIDLDEFKFIFFMEWIHRLWGRAIGAVFILPAVYFAVSKKTSGHVNKRLFGLAGLLGLQGFVGWWMVKSGLDQEQLDARKSKPTVSQYRLTTHLGTAFFLYMGMLWTGLEILRECKWIKNPVQAISLFKKLDNPAIGPMRKISLALLAVSFLTAMSGGMVAGLDAGWV... | 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:... |
Q02766 | MVLNRYSLITNCNHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIIAQENVNLYNMIFTIHGIIMIFFNIMPGLFGGFGNYFLPILCGSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLSTSLMSLSPVAVDVIIFGLLVSGVASIMSSLNFITTVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGVISHVISTNYCRNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIP... | 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-... |
P20681 | MSGGVSLWIERWMLSTNAKDIGNLYLIFALFSGLLGTAFSVLIRMELSGPSVQYIADNQLYNSIITAHALLMIFFMVMPALIGGFGNFLLPLLVGGPDMAFPRLNNISFWLLPPSLILLVFSACIEGGAGTGWTIYPPLSGVQSHSGPSVDLAIFALHLSGVSSLLGAMNFITTIMNMRTPSIRLHKLALFGWAVIITAVLLLLSLPVLAGAITMLLTDRNFNTSFFETAGGGDPILFQHLFWFFGHPEVYILIIPAFGIISTTISAYSNKSVFGYIGMVYAMMSIGILGFIVWSHHMYTVGLDVDTRAYFTAATLIIAV... | 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-... |
O03546 | MTFITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTIEAGAGTGWTVYPPLAGNLAHAGASVDLPIFSLHLAGVSSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIK... | 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-... |
Q08855 | MATSAAAHGEHAEDHGHDEHAHPTGWRRSTNHKDIGTLYLIFAIIAGVIGAAMSLAIRAELMYPGVEYFHNTHLYNVFVTSHGVIMIFFMVMPAMIGGFGNWFLPLMIGAPDMAFPRMNNISFWLLPASFGLLLMSTFVEGEPGANGAGAGWTMYVPLSSSGHPGPAVDLAIFSLHIAGASSILGAINFITTILNMRAPGMTLHKMPLFAWSVLITAFLLLLSLPVLAGAITMLLTDRNFGTTFFAPEGGGDPLLYQHLFWFFGHPEVYILILPGFGMISHIISTFSRKPVFGYIGMVYAMAAIGGLGFVVWAHHMYIVG... | 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 a... |
O99818 | MLPRWMYSTNHKDIGTMYLIFGAWSGMLGLSMSMLIRMELGQPGTLIGNDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFPRMNNMSFWLLPPSLFLLINSSLIESGAGTGWTVYPPLSSNLSHYGPSVDLAIFSLHLAGASSILGAINFITTIVNMRSIGMTMERMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIICYNTGKKEPFGNLGMIYAMAAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIF... | 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-... |
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-cyt... |
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-cyt... |
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-cyt... |
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
Locat... |
P98054 | MEQIPASIWTLTAGVVVTLISFWVGHHHGLLPEQASEQAPLVDNFFDIMLTIGTALFLVVQGAIILFVIRYRRRAGEEGDGLPVEGNLPLEAFWTAIPALIVIFLGIYSVDIFQRMGGLNPGDHAMHSMHAPKSGMAVVAQAPSKTTSDATALLAAAQPPEIGIGASPDVQGKAPDLVVDVAGMQYAWIFTYPDSGIVSGELHIPVGKDVQLNLSARDVIHSFWVPQFRLKQDAIPGVPTTRFKATKVGTYPVVCAELCGGYHGAMRTQVIVHTPEDFETWRRQNQAIATAPVIPSLRDRHIHEMGVTAELVAQVEAIAH... | 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)-[cytoch... |
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-cyt... |
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-cyt... |
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, comple... |
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