ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9CR35 | MAFLWLVSCFALVGATFGCGVPAIQPVLTGLSRIVNGEDAIPGSWPWQVSLQDRTGFHFCGGSLISENWVVTAAHCGVKTTDVVVAGEFDQGSDEENVQVLKIAQVFKNPKFNSFTVRNDITLLKLATPAQFSETVSAVCLPTVDDDFPAGTLCATTGWGKTKYNALKTPDKLQQAALPIVSEAKCKESWGSKITDVMICAGASGVSSCMGDSGGPLVCQKDGVWTLAGIVSWGSGFCSTSTPAVYARVTALMPWVQEILEAN | Catalytic Activity: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Sequence Mass (Da): 27822
Sequence Length: 263
Subcellular Location: Secreted
EC: 3.4.21.1
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Q00871 | MIGKLSLLLVCVAVASGNPAAGKPWHWKSPKPLVDPRIHVNATPRIVGGVEATPHSWPHQAALFIDDMYFCGGSLISSEWVLTAAHCMDGAGFVEVVLGAHNIRQNEASQVSITSTDFFTHENWNSWLLTNDIALIRLPSPVSLNSNIKTVKLPSSDVSVGTTVTPTGWGRPSDSASGISDVLRQVNVPVMTNADCDSVYGIVGDGVVCIDGTGGKSTCNGDSGGPLNLNGMTYGITSFGSSAGCEKGYPAAFTRVYYYLDWIQQKTGVTP | Function: Serine protease with chymotryptic and collagenolytic activities.
Catalytic Activity: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Sequence Mass (Da): 28685
Sequence Length: 271
Subcellular Location: Secreted
EC: 3.4.21.1
|
P07338 | MAFLWLVSCFALVGATFGCGVPTIQPVLTGLSRIVNGEDAIPGSWPWQVSLQDKTGFHFCGGSLISEDWVVTAAHCGVKTSDVVVAGEFDQGSDEENIQVLKIAQVFKNPKFNMFTVRNDITLLKLATPAQFSETVSAVCLPNVDDDFPPGTVCATTGWGKTKYNALKTPEKLQQAALPIVSEADCKKSWGSKITDVMTCAGASGVSSCMGDSGGPLVCQKDGVWTLAGIVSWGSGVCSTSTPAVYSRVTALMPWVQQILEAN | Catalytic Activity: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Sequence Mass (Da): 27849
Sequence Length: 263
Subcellular Location: Secreted
EC: 3.4.21.1
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P0DJB7 | DDETTFPCNSGRCACLPEDSHSYTCQSP | PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 3064
Sequence Length: 28
Domain: The cysteine framework is IX (C-C-C-C-C-C).
Subcellular Location: Secreted
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Q08977 | MFASAGQQHPQIVPKEEESILNYLLEVRSSLAKLKQNRTQYLNSKDVQTTYQHVLTKVRELDDIRKNSHETPAKSAATLIHSTELHNRVDSVLDDVFQLLSLCFLTVGLKNSAPATYASLSTVESLLEHLNESNVFTHHDLSPIKERLEEISKIVEQKNSSPAYDEDGNDDRLREIDNERKKNKIEEDLLLRAKLKHCKDEYDILEGKLEEIDPSLSTVMEKLFRIRRGLLSLVASAKKTMSKSDINTNSLLQEQNDLQTNNESLTDDKHLVSQEYVHEKLSVLKNELSELESNRDDSGKFKSLESHQVAEKGQSVLNGL... | Function: Involved in bleomycin tolerance with links to DNA repair and/or proteasome function.
PTM: Phosphorylated by PKA in vitro.
Sequence Mass (Da): 62780
Sequence Length: 551
Subcellular Location: Cytoplasm
|
Q6D9J5 | MSDRPLCDAVVILCTAPDDACAQRLANSLLETRLAACVTLLPGARSLYYWEGKLEQQSEVQMLIKSDTSHQQALLTHLKQQHPYDTPELLVLPVSGGDSDYLTWLNASLR | Cofactor: Binds 1 copper ion per subunit.
Function: Involved in resistance toward heavy metals.
Sequence Mass (Da): 12212
Sequence Length: 110
Subcellular Location: Cytoplasm
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O58720 | MIIVYTTFPDWESAEKVVKTLLKERLIACANLREHRAFYWWEGKIEEDKEVGAILKTREDLWEELKERIKELHPYDVPAIIRIDVDDVNEDYLKWLIEETKK | Cofactor: Binds 1 copper ion in the interface between two trimers.
Function: Involved in resistance toward heavy metals.
Sequence Mass (Da): 12348
Sequence Length: 102
Subcellular Location: Cytoplasm
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Q5AVY9 | MHFKLLSLAALAGLSVASPLNLDERQLGSSSGNDLRDGDCKPVTFIFARASTEPGLLGMSTGPAVCNDLKADASLGGVACQGVGPKYTAGLAENALPQGTSSAAINEAKELFELAASKCPDTRIVAGGYSQGTAVMHGAIPDLSDEIKDKIAGVVLFGDTRNKQDGGQIKNFPKDKIKIYCATGDLVCDGTLVVTAAHFTYVANTGEASKWLEQQLASMPASTSTSSSSSSSSSAPASQTSQSSGLSSWFSGLGN | Function: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants . Degrades cutin, a macromolecule that forms the structure of the plant cuticle . Also degrades suberin, a specialized macromolecule found in the cell wall of various plant tissues (By similarity).
Catalytic Activity: c... |
G4MZV6 | MQFSLSIATAILAATASAMPVLETRQTVGTTANEFTSGGCKDVVLLYARGTTQAGNMGQEPGPELGNALKARLGAARVAVQGVAYSASLLGNLNPGGAPANEATSFRTLIGQVASQCPNARIVVSGYSQGAALVHRAVEGATAAVRARIAAGVTFGDTQKQQDGGRIPGLDASKTLIICNTGDRVCEGTLIITAAHSGYGARAGEAVDFIAARV | Function: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants . Degrades cutin, a macromolecule that forms the structure of the plant cuticle . Required for efficient penetration of the host plant cuticle by the appressorium during the initial stage of fungal infection .
PTM: The ... |
Q5AX00 | MRFHTILLAALASLVIATPLPSDTDVSLERRQSMNSNDLEKGDCKSVAFIFARGSTEIGNMGFVVGPGVCSNLKSTLGSDKVACQGVGGAYTAGLIQNALPANTDSGSIKEAVKMFDLAAKCPDTQIVAGGYSQGSAVIDNAIQKLDDSTRDRVKGVVLFGFTRNLQDKGQIPGYPKDQTKVYCAVGDLVCSGTLIITASHMTYGLNAGDAAKFLASQVSV | Function: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants . Degrades cutin, a macromolecule that forms the structure of the plant cuticle (By similarity). Also degrades suberin, a specialized macromolecule found in the cell wall of various plant tissues (By similarity).
Cataly... |
C8VJF5 | MPLPLLPPLLLPLEALLDLALHLVDSTGVAYSARQVTPTAPLPRLRGSSTSNDVTDNSGCKELTFIFARGTTEIGNMGTVVGPKVGEALKSLTGNKAAIQGVDYPADAAGNAALGGSGGPKMASLVETALKQCPDTKIVLGGYSQGAMVVHNAASKLSSGQVVGAVTFGDPFKSQKPDNIDQFKTFCASGDPVCLNGANVMAHLSYGNDAQTAAQFLVSAAGL | Function: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (By similarity). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (By similarity). Also degrades suberin, a specialized macromolecule found in the cell wall of various plant tissues (By simi... |
P07470 | MRALRVSQALVRSFSSTARNRFENRVAEKQKLFQEDNGLPVHLKGGATDNILYRVTMTLCLGGTLYSLYCLGWASFPHKK | 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... |
Q9TRZ8 | FENKVAEKQKLFQADNGLPVXLK | 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... |
P24310 | MQALRVSQALIRSFSSTARNRFQNRVREKQKLFQEDNDIPLYLKGGIVDNILYRVTMTLCLGGTVYSLYSLGWASFPRN | 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... |
P80333 | VDNMVPEKQKLFQAXNGIPVHLF | 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... |
Q9TR28 | LENRVAEKQKLFQEDNGLPVHLKGGATDN | 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... |
Q9TR29 | FENKVPEKQKLFQEDNGIPVVLKGGVADA | 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... |
P14406 | MLRNLLALRQIGQRTISTASRRHFKNKVPEKQKLFQEDDEIPLYLKGGVADALLYRATMILTVGGTAYAIYELAVASFPKKQE | 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... |
P35171 | MLRNVLALRQIAQRTISTTSRRHFENKVPEKQKLFQEDNGMPVHLKGGTSDALLYRATMLLTVGGTAYAIYMLAMAAFPKKQN | 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... |
Q8TF08 | MMFPLARNALSSLKIQSILQSMARHSHVKHSPDFHDKYGNAVLASGTAFCVATWVFTATQIGIEWNLSPVGRVTPKEWKHQ | 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... |
B0L0Y6 | MKLFMFAAIIFTMASTTVRAEQCANNRKVCTWDGQGDTNCDCIGTACHEDDAHKVSVAGSAFYTCQPISAFRVCDGSEDVMDAGFSELYCRCSGGSYTISNGEVVCD | Function: Acts as a neurotoxin.
PTM: Contains 5 disulfide bonds.
Sequence Mass (Da): 11509
Sequence Length: 107
Domain: The cysteine framework is VIII (C-C-C-C-C-C-C-C-C-C).
Subcellular Location: Secreted
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G8FZS4 | ADNHARVAGPRAVASGRYATEKAFLQMMTRGSCGLPCHENRRCGWACYCDDGICKPLRV | Function: Crassispirid snail peptide that induces sleep-like symptoms in young mice (12 and 14 days) and hyperactivity in older mice (16 days), when intracranially injected.
PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 6471
Sequence Length: 59
Domain: The cysteine framework is IX (C-C-C-C-C-C).
Subcellular Loca... |
O00574 | MAEHDYHEDYGFSSFNDSSQEEHQDFLQFSKVFLPCMYLVVFVCGLVGNSLVLVISIFYHKLQSLTDVFLVNLPLADLVFVCTLPFWAYAGIHEWVFGQVMCKSLLGIYTINFYTSMLILTCITVDRFIVVVKATKAYNQQAKRMTWGKVTSLLIWVISLLVSLPQIIYGNVFNLDKLICGYHDEAISTVVLATQMTLGFFLPLLTMIVCYSVIIKTLLHAGGFQKHRSLKIIFLVMAVFLLTQMPFNLMKFIRSTHWEYYAMTSFHYTIMVTEAIAYLRACLNPVLYAFVSLKFRKNFWKLVKDIGCLPYLGVSHQWKS... | Function: Receptor for the C-X-C chemokine CXCL16. Used as a coreceptor by SIVs and by strains of HIV-2 and m-tropic HIV-1.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39280
Sequence Length: 342
Subcellular Location: Cell membrane
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Q9EQ16 | MDDGHQESALYDGHYEGDFWLFNNSSDNSQENKRFLKFKEVFLPCVYLVVFVFGLLGNSLVLIIYIFYQKLRTLTDVFLLNLPLADLVFVCTLPFWAYAGTYEWVFGTVMCKTLRGMYTMNFYVSMLTLTCITVDRFIVVVQATKAFNRQAKWKIWGQVICLLIWVVSLLVSLPQIIYGHVQDIDKLICQYHSEEISTMVLVIQMTLGFFLPLLTMILCYSGIIKTLLHARNFQKHKSLKIIFLVVAVFLLTQTPFNLAMLIQSTSWEYYTITSFKYAIVVTEAIAYFRACLNPVLYAFVGLKFRKNVWKLMKDIGCLSH... | Function: Receptor for the C-X-C chemokine CXCL16.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40468
Sequence Length: 351
Subcellular Location: Cell membrane
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P69998 | MGEWTILERLLEAAVQQHSTMIGRILLTVVVIFRILVVAIVGETVYDDEQTMFVCNTLQPGCNQACYDKAFPISHIRYWVFQIIMVCTPSLCFITYSVHQSSKQRERQYSTVFITLDKDKKREDNKIKNTTVNGVLQNSEFFTKEMQSDFLEVKEMQNSAARNSKMSKIRRQEGISRFYIIQVVFRNALEIGFLMGQYFLYGFKVPSMYECNRYPCVKMVECYVSRPTEKTVFLVFMFAVSGLCVILNLAELNHLGWRKIKTAVRGAQERRKSIYEIRNKDSPHRIGVPNFGRTQSSDSAYV | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35044
Sequence Length: 302
Subcellular Location: Cell membr... |
O54851 | MGEWTILERLLEAAVQQHSTMIGRILLTVVVIFRILIVAIVGETVYDDEQTMFVCNTLQPGCNQACYDRAFPISHIRYWVFQIIMVCTPSLCFITYSVHQSAKQRERRYSTVFLALDRDPAESIGGPGGTGGGGSGGSKREDKKLQNAIVNGVLQNTETTSKETEPDCLEVKELTPHPSGLRTAARSKLRRQEGISRFYIIQVVFRNALEIGFLVGQYFLYGFSVPGLYECNRYPCIKEVECYVSRPTEKTVFLVFMFAVSGICVVLNLAELNHLGWRKIKLAVRGAQAKRKSVYEIRNKDLPRVSVPNFGRTQSSDSAY... | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36082
Sequence Length: 321
Subcellular Location: Cell membr... |
Q8N144 | MGEWAFLGSLLDAVQLQSPLVGRLWLVVMLIFRILVLATVGGAVFEDEQEEFVCNTLQPGCRQTCYDRAFPVSHYRFWLFHILLLSAPPVLFVVYSMHRAGKEAGGAEAAAQCAPGLPEAQCAPCALRARRARRCYLLSVALRLLAELTFLGGQALLYGFRVAPHFACAGPPCPHTVDCFVSRPTEKTVFVLFYFAVGLLSALLSVAELGHLLWKGRPRAGERDNRCNRAHEEAQKLLPPPPPPPPPPALPSRRPGPEPCAPPAYAHPAPASLRECGSGRGKASPATGRRDLAI | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31933
Sequence Length: 294
Subcellular Location: Cell membr... |
Q96KN9 | MEGVDLLGFLIITLNCNVTMVGKLWFVLTMLLRMLVIVLAGRPVYQDEQERFVCNTLQPGCANVCYDVFSPVSHLRFWLIQGVCVLLPSAVFSVYVLHRGATLAALGPRRCPDPREPASGQRRCPRPFGERGGLQVPDFSAGYIIHLLLRTLLEAAFGALHYFLFGFLAPKKFPCTRPPCTGVVDCYVSRPTEKSLLMLFLWAVSALSFLLGLADLVCSLRRRMRRRPGPPTSPSIRKQSGASGHAEGRRTDEEGGREEEGAPAPPGARAGGEGAGSPRRTSRVSGHTKIPDEDESEVTSSASEKLGRQPRGRPHREAAQ... | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40140
Sequence Length: 370
Subcellular Location: Cell membr... |
Q8BSD4 | MEKLNLLGFLIITLNCNVTIMGMIWLIVEVLLRMLVVVLAGSPIYEDEQERFICNTLQPGCANVCYDLFSPVSPLRFWLVQSLALLLPSVVFGTYTLHRGAKLAAVGGACRPQVPDLSTAYLVHLLLRMLLEAGLAFLHYFLFGFSVPARVSCSHVPCSGAVDCYVSRPTEKSLLILFFWAVSALSFLLSLADLLWILPRRKTLRTTQWVNGEARPVCEVPAPPPCLLQNPQGYLSQGQVDQEDRQEEQVVPEFPCMWTAGQSDNSNVGQACVSGLLEHSDQDASEATSSAGDRLTVAHTAHELRFHRETSLDLGGKNTQ... | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40042
Sequence Length: 364
Subcellular Location: Cell membr... |
P0DQZ1 | MNCLQLLLVLLLISTIAALHGDGRVPQRRGRNIRTMSNLLNFQTRDCPSSCPAVCPNQNECCDGDVCNYSNTLNKYFCIGCGSGGGE | Function: May interact and inhibit Cav3.1/CACNA1G calcium channels. In a ex vivo model, shows ability to block nerve signal transduction.
PTM: Contains 4 disulfide bonds.
Sequence Mass (Da): 9426
Sequence Length: 87
Domain: The cysteine framework is XIII (C-C-C-CC-C-C-C).
Subcellular Location: Secreted
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B4YSU8 | MQKATVLLLALLLLLPLSTAQDAEGSQEDAAQREVDIATRCGGTGDSCNEPAGELCCRRLKCVNSRCCPTTDGC | PTM: Contains disulfide bonds.
Sequence Mass (Da): 7786
Sequence Length: 74
Domain: The cysteine framework is XVII (C-C-CC-C-CC-C).
Subcellular Location: Secreted
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F1SY52 | MHSVLAQAASGALSFELRLGQSSVLTICILALLTFVLREIVLYFTRHSMPPGPFRWPLIGNALQLPQDHPWVKYTEWAKMYGPLMQLDVLGQHMLVITSAQTARDLMEKRSSIYSDRPHLVMAGDLAGFGDTLILQNYGEEFRYQRKLVSHSFSPSVIHRYYDLQEAAARRLVLAIIEDPDSLENSTRLHIASIILRMTYGYTVKGVDDPLFTTGIAVINGFSEATRPGAWPVDFVPILQYVPHWVPGFVFTRKAREWRGVLERAMWAPYHWCKENYARDAAHGLCLCGSILAAEGSQLSSDQEWLFVNAAVTVMGGGLD... | Function: Cytochrome P450 monooxygenase that is able to use trans-stilbene as a substrate for oxidation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58964
Sequence Length: 529
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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F1SY62 | MPASFLASLRAWIASSTIGQRILLALALGLLLITARVISKSKGTMPPGPRGLPLLGNIFQLPKLPWYRFTEWKEEFGPIFSLNFAGTPVVVLNSHEVVGDLLERKSTIYSDRPRFIMAGEILTGGMLIVFTGYGKVWRKLRRAGQEGLNVRASEKYQPLQESEARLLTTNMLREPAEWDAHLQRAAASSIASAVYAWPPLTKSDDGLVHRIDELMRRLVMAGLPGRYLVEIFPIMKHLPTWMAKWKREGLEWHRRDTEMFEGFYDNVARFMASGKYKPSLTAGLIERQEKNGLSKKEVSWLAGTMIGAGAETTAASLSVF... | Function: Cytochrome P450 monooxygenase that is able to use delta(6)-protoilludene as a substrate to produce delta(6)-protoilludene-8-ol.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58894
Sequence Length: 526
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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F1SY73 | MRDSLARNILLPTAPSLGAIACLLLAIAIGLLLLPRSQPHCFPPGPPVKPIVGSILQVSPQGAWYKFSEYQKVYGDLLFFRGLGSHVLVLNSMKAINDLLDKRSSVYSNRPTFTVVGELMGLGQSMPLLPYGEEWRAHRRLAHSALSPTAVRRYHGIQEDMAALLCMRLLREPEAFFSHVRLIAGNIILSVVYGLPVETSEDEYIAHAERTMQVIGKATVPGAYLCDLMPFLKHLPSWVPFQREASTGREMIERLVTKPFEHVKRAMEAGSAPPSVTQDLLSTNIDDMHDVEQRIKWTTGAMYGAGGETTYSTVLVFIMA... | Function: Cytochrome P450 monooxygenase that is able to use 3,5-dimethoxy-trans-stilbene and 3,5,4'-trimethoxy-trans-stilbene as substrates for oxidation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56646
Sequence Length: 508
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Memb... |
F1SY74 | MALPPGVPFLIRVSLILAFAPVCVVIVANFIWRHTDVALPTWPVTLLSVASTPLTILVRVWYRQWKYQRAAARLGAIMPPRWVGKKLGNLDILKEMLQTMQSGYIADFAWKLFNNLGNTVQMNVLGGTAYLTCDPNIIKSVLATDFNNFEKGDLFKQEMASVLGTGVFNADGDMWKWHRAMTRPFFSRDRISHFELFDRRSEQAVAKMTERFHSGYAVDFQDLISRFTLDSATEFLFGSCVNSLHSPLPYPHNQHPTPFSHPSSKSLASNPSRAEAVASAFMRAQIVLAERVAMGAIWPLLEMRKSRTGEHMRIIDEYLD... | Function: Cytochrome P450 monooxygenase that is able to use carbazole and 3,5,4'-trimethoxy-trans-stilbene as substrates for oxidation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69844
Sequence Length: 613
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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F1SY77 | MSTDNIPTQLGIAGAVAVLLFLLRRWSSRSTLRNIPGPPPQSQWTGNLKQWFARDGADFQRDVSFNYGPVAKIHGFLGRPILYVADPKALQTILVKEEQVYQETKAFFAMTYLLFGPGLLATAGEKHRKQRKLLNPVFSIKHMRHMLPIFYGVLHKVRDAITMRVSDGPQEIDMLKWMGRTALELIGQGGLGYSFDKLVEDGDNEYGRALKHLQPTLQRINVLRRLIPYVYKLGPAWFRRMVMHYFPLGQVRDAKEIVDTMQRCSSEIFASKKIALARGDEAVMKQVGEGKDIMSILMKANSMASEADRIPEEELVAQMS... | Function: Cytochrome P450 monooxygenase that is able to use dehydroabietic acid as a substrate for oxidation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61636
Sequence Length: 547
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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F1SY82 | MFLQIVTSVLATGLLYALISVLQQNRTLSASLPPGPPGHWLFGNAPPKAFPYRHFAELTETYGPVFTLRFGRRIVCVIGRYQAAVDILMKHSAETSDRPRSVAANEIMSKGHRVLMTPAGERLKKYRRALHAFLQPSSSATYKPMQYKNAKNYVLDCLHDGGHHLDHGRKYAASVVMSVAYGKTTPTSYSDPEVLQINKSLARLGAALKPGAYLVDTYPILKYCPGYASHLRRYREEELALITKQANAVRELLAKGEAPPSFTAYLIENQERLGISDDELAYLSGAIFGAGSDTTAAALGIMTMAAACYPEAQARVQAQL... | Function: Cytochrome P450 monooxygenase that is able to use 4-ethoxybenzoic acid as a substrate for oxidation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 54876
Sequence Length: 495
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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F1SY83 | MDSSTSLLPPLGSIILACEGLTSLVPLILSVLVCLVATVTISPTLLAYFNDPFELRAYPGPFLAKFTSAWISWIISQNRWSETVDLMHRQHGPIVRLSPDHVSVASPAAFAAVYGHSSGALKAPFYNAFANFKTRSIFNTRDRAEHSRKRRVEAHMFSPRSIRALEDTARVHFQVLVRQWDALCAPTGKTGRGSAEGTLGTISWKVHGDRVWFDCMPWFNFWSFDTISDLAFGRPFGMLEAAKGSAHVSKSNTKSVQAVSQDTSHSDEAQSELLEIPAMEVLSELLDFTVALAYLPAWVQPVFGRLPMFRDGYDAAPKLA... | Function: Cytochrome P450 monooxygenase that is able to use trans-stilbene as a substrate for oxidation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 62454
Sequence Length: 568
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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Q111E9 | MKKFFISVVFIVLLTFTTFINSATAAKLDDNVRTLPLNEDKEVVLTIKEYTQGKREFTNVCSQCHVGGITKTNPDVSLDPETLALAYPARDNIEGLIDYMQNPTTYDGFIEISEFHPSIKSADIYPEMRNLTEDDLYAIAGYILVQPKVLGKQWGGGKIFR | Cofactor: Binds 1 heme c group covalently per subunit.
Function: Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18118
Sequence Length: 161
Subcellular Location: Cellular thylakoid membrane
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Q56247 | MKWKLAAMFLGVSLALAACGGGGDNAGEKNGGSNGGGDTAAAAEQIFKQNCASCHGQDLSGGVGPNLQKVGSKYSKDEIKNIIANGRGAMPAGIIKGEDADKVAEWLAAKK | Function: Appears to mediate electron flow from the cytochrome b6f complex to an alternative terminal oxidase.
PTM: Binds 1 heme c group covalently per subunit.
Location Topology: Lipid-anchor
Sequence Mass (Da): 11136
Sequence Length: 111
Subcellular Location: Cell membrane
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O34594 | MKSKLSILMIGFALSVLLAACGSNDAKEEKTDTGSKTEATASEGEELYQQSCVGCHGKDLEGVSGPNLQEVGGKYDEHKIESIIKNGRGNMPKGLVDDNEAAVIAKWLSEKK | Function: Electron carrier protein.
PTM: Binds 1 heme c group covalently per subunit.
Location Topology: Lipid-anchor
Sequence Mass (Da): 11928
Sequence Length: 112
Subcellular Location: Cell membrane
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O07091 | MDKNSNGKLIALAVGGAVLMGALFFSVSFLTGYIPAPNHSAILTPLRSFMGWFLLIFCASIIIMGLGKMSSAISDKWFLSFPLSIFVIVMVMFLSLRVYWEKGRTTTVDGKYIRTTAELKEFLNKPAATSDVPPAPAGFDFDAAKKLVDVRCNKCHTLDSVADLFRTKYKKTGQVNLIVKRMQGFPGSGISDDDAKTIGIWLHEKF | Function: Monoheme cytochrome which is the immediate electron donor to P840 of the photosynthetic reaction center complex.
PTM: Binds 1 heme group per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22715
Sequence Length: 206
Subcellular Location: Cell inner membrane
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P00099 | MKPYALLSLLATGTLLAQGAWAEDPEVLFKNKGCVACHAIDTKMVGPAYKDVAAKFAGQAGAEAELAQRIKNGSQGVWGPIPMPPNAVSDDEAQTLAKWVLSQK | Function: Electron donor for cytochrome cd1 in nitrite and nitrate respiration.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 10967
Sequence Length: 104
Subcellular Location: Periplasm
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P00101 | MKKILIPMLALGGALAMQPALAQDGEALFKSKPCAACHSVDTKMVGPALKEVAAKNAGVEGAADTLALHIKNGSQGVWGPIPMPPNPVTEEEAKILAEWVLSLK | Function: Electron donor for cytochrome cd1 in nitrite and nitrate respiration.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 10797
Sequence Length: 104
Subcellular Location: Periplasm
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P74917 | MTTYLSQDRLRNKENDTMTYQHSKMYQSRTFLLFSALLLVAGQASAAVGSADAPAPYRVSSDCMVCHGMTGRDTLYPIVPRLAGQHKSYMEAQLKAYKDHSRADQNGEIYMWPVAQALDSAKITALADYFNAQKPPMQSSGIKHAGAKEGKAIFNQGVTNEQIPACMECHGSDGQGAGPFPRLAGQRYGYIIQQLTYFHNGTRVNTLMNQIAKNITVAQMKDVAAYLSSL | Function: Diheme, high potential cytochrome c.
PTM: Binds 2 heme c groups covalently per subunit.
Sequence Mass (Da): 25298
Sequence Length: 230
Subcellular Location: Periplasm
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P56773 | MSKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRPTVTEAFASVQYIMTEANFGWLIRSVHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVTGVVLGVLTASFGVTGYSLPWDQIGYWAVKIVTGVPDAIPVIGSPLVELLRGSASVGQSTLTRFYSLHTFVLPLLTAVFMLMHFLMIRKQGISGPL | Cofactor: Binds 2 heme b groups non-covalently with two histidine residues as axial ligands.
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Multi-pass m... |
Q06J43 | MAVIYNWFNDRLEIQAVADDITAKYVPPHVNLFYCLGGITLTCFLIQVATGFALTFYYRPTVGEALSSVRSIMLDTNFGWLIRSVHRWCASMMVLMMVLHVFRVYLTGGFKNPRESTWVTGVIMASCTVSFGVTGYSLPWDQVGYWAVKIVTGVPEAIPVIGPAIVQLLRGNSSVGQATLTRFYSLHTFVLPLLTAVFMLGHFLMIRKQGISGPL | Cofactor: Binds 2 heme b groups non-covalently with two histidine residues as axial ligands.
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Multi-pass m... |
Q00471 | MSKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCIGGITFTCFLVQVATGFAMTFYYRPTVAEAFASVQYIMTDVNFGWLIRSIHRWSASMMVLMMVLHVFRVYLTGGFKRPRELTWVTGVIMAVCTVSFGVTGYSLPWDQVGYWAVKIVTGVPDAIPGVGGFIVELLRGGVGVGQATLTRFYSLHTFVLPLLTAVFMLMHFLMIRKQGISGPL | Cofactor: Binds 2 heme b groups non-covalently with two histidine residues as axial ligands.
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
PTM: The N-terminus is blocked.... |
Q59297 | MAENTPKPAAGTAPAKPKPAAPGAAKPAAPKAARPGAAKPAAKPAAPRAAAPSGVYKKPPVDRPDPNPFKDSKRDAVAGWFQERFYVLNPIIDYLKHKEVPKHALSFWYYFGGLGLFFFVIQILTGLLLLQYYKPTETDAFASFLFIQGEVPFGWLLRQIHAWSANLMIMMLFIHMFSTFFMKSYRKPRELMWVSGFVLLLLSLGFGFTGYLLPWNELAFFATQVGTEVPKVAPGGAFLVEILRGGPEVGGETLTRMFSLHVVLLPGLVMLVLAAHLTLVQILGTSAPIGYKEAGLIKGYDKFFPTFLAKDGIGWLIGFA... | Cofactor: Binds 2 heme b groups non-covalently.
Function: Component of the green S-bacteria bc complex, which consists of the Rieske protein and cytochrome b subunit but appears to lack a cytochrome c1-equivalent. This complex has a comparatively low redox potential.
Location Topology: Multi-pass membrane protein
Seque... |
P92848 | MPHQKILMLFGLLPVATNISTWWNFGSMLLTCSMIQVLTGFFLAVHYTANINLAFSSIVHIMRDVPCGWMVQNLHAIGASMFFICIYIHIARGLYYGSYLNKETWLSGTTLLIMLMATAFFGYVLPWGQMSFWAATVITNLLTAIPYLGGTMTTWLWGGFAINDPTLTRFFALHFILPFGIISLSSLHVLLLHEEGSSNPLGTNSDIDKIPFHPYHTMKDLLMLTTTLTLLLMTISFFPDIFNDPENFSKANPLVTPQHIKPEWYFLFAYGILRSIPNKLGGALALAMSIMILFTVPFIHTSKLRSMTFRPLMQLMFWTF... | Cofactor: Binds 2 heme b groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a... |
P92850 | YINYKNMSHQHLLTLFNLLPVGANISTWWNFGSMLLSCLMIQIATGFFLAIHYTANINMAFSSIVHISRDVPYGWIMQNTHAIGASLFFICIYIHIARGIYYGSYLNKEVWLSGTTLLIILMATAFFGYVLPWGQMSFWAATVITNLLTAIPYLGTTLTTWLWGGFAINDPTLTRFFALHFILPFAIISLSSLHILLLHNEGSNNPLGTNSDID | Cofactor: Binds 2 heme b groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a... |
Q9MI64 | MTNIRKTHPLMKILNKTFIDLPTPSNISSWWNFGSLLGLCLTVQILTGLFLAMHYTPDTSTAFSSITHICRDVNYGWMIRHLHANGASMFFICLYIHIGRGLYYGSYLFKKTWNIGVLLLFTTMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWVWGGFSVDKATLTRFFALHFILPFIIVALTTVHLLFLHETGSNNPMGIPSNMDKIPFHPYHTIKDILGALLLMFVLLTLTLLAPDLLGDPDNYTPANPLNTPAHIKPEWYFLFAYAILRSIPNKLGGVLALLFSILILLFIPLLHTSKQRSMMFRPL... | Cofactor: Binds 2 heme b groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a... |
P15585 | MLNIFNYFKNLRVSFHEVFSLFGFFTFMTIIVQLVSGTMLAFSSVPEPMLIPTVRDEEDIEDLYTDDFFWLHERGVDLIFIFSYFHLLRKLYLNVFDLETEASWKSGVFSFLVFQVVVFFGLVLCCTHLSEITLTIAANIFHTFFMFKGKAYWFLFTDKQLNTDTLIRLAYAHYVSAFYLSFLGLLHGIDIHYDWKNEPFYDGLSSEMLWWDEALSNELTNFFVLLVFITLAFFLLFEEPEALSYEIFMWGDIGLSTDVRFYGVAPHWYFRPFMAWLIACPFHKTGIFGLLFFFVTLYYQPNLHGVSDQNSYGKKTLTIS... | Cofactor: Binds 2 heme b groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a... |
G1CWH0 | GIPCGESCVFIPCITGAIGCSCKSKVCYRNHVIAAEAKTMDDHHLLCQSHEDCITKGTGNFCAPFPDQDIKYGWCFRAESEGFMLKDHLKMSITN | Function: Probably participates in a plant defense mechanism (Probable). Active against Gram-negative bacteria E.coli ATCC 700926 (MIC=1.1 uM), K.pneumoniae ATTC 13883 (MIC=2.7 uM) and P.aeruginosa ATCC 39018 (MIC=4.7 uM) . Has hemolytic and cytotoxic activity .
PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 1047... |
P04657 | MGSGDAENGKKIFVQKCAQCHTYEVGGKHKVGPNLGGVVGRKCGTAAGYKYTDANIKKGVTWTEGNLDEYLKDPKKYIPGTKMVFAGLKKAEERADLIAFLKSNK | Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-trans... |
Q9AJE4 | MKDRAADPVTKFSPSPYETGQFLRISERADVGTPQIDYLLATQRPDGLWGSVGFELVPTLGAVAGLSSRPEYADRAGVTDAVARACEKLWELALGEGGLPKLPDTVASEIIVPSLIDLLSEVLQRHRPAVGGKAGQEQEFPSPPGANAELWRQLSDRIARGQAIPKTAWHTLEAFHPLPKQFAATVTPAADGAVTCSPSSTAAWLSAVGTDAGASTRAYLDEAQSRYGGAIPMGSSMPYFEVLWVLNLVLKYFPDVPIPREIIEEIAAGFSDSGIGGGPGLPPDGDDTAYANLAGDKLGAPTHPEILMKFWAEDHFVSYP... | Function: Involved in the production of the isoprenoid antibiotic terpentecin. Converts geranylgeranyl diphosphate (GGDP) into terpentedienol diphosphate (TDP) by a protonation-initiated cyclization.
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate = terpentedienyl diphosphate
Sequence Mass (Da): 54163
Sequen... |
Q9K499 | MHAFPHGTTATPTAIAVPPSLRLPVIEAAFPRQLHPYWPKLQETTRTWLLEKRLMPADKVEEYADGLCYTDLMAGYYLGAPDEVLQAIADYSAWFFVWDDRHDRDIVHGRAGAWRRLRGLLHTALDSPGDHLHHEDTLVAGFADSVRRLYAFLPATWNARFARHFHTVIEAYDREFHNRTRGIVPGVEEYLELRRLTFAHWIWTDLLEPSSGCELPDAVRKHPAYRRAALLSQEFAAWYNDLCSLPKEIAGDEVHNLGISLITHHSLTLEEAIGEVRRRVEECITEFLAVERDALRFADELADGTVRGKELSGAVRANVG... | Cofactor: Binds 3 Mg(2+) ions per subunit. Can also use Mn(2+) and Fe(3+) but less efficiently, and other divalent cations such as Zn(2+), Fe(2+), Co(2+), Cu(2+) and Ni(2+) are nearly completely inefficient as cofactors.
Function: Catalyzes the cyclization of farnesyl diphosphate (FPP) to the sesquiterpene epi-isozizae... |
P00044 | MTEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKKNVLWDENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE | Cofactor: Binds 1 heme c group covalently per subunit.
Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of ubiquinol-cytochrome c oxidoreductase. Cytochrome c then transfers this electron to the dinuclear copper ... |
P19974 | MSDIPAGDYEKGKKVYKQRCLQCHVVDSTATKTGPTLHGVIGRTSGTVSGFDYSAANKNKGVVWTKETLFEYLLNPKKYIPGTKMVFAGLKKADERADLIKYIEVESAKSL | Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-trans... |
C0HJS8 | DLQCAETCVHSPCIGPCYCKHGLICYRN | Function: Probably participates in a plant defense mechanism. Not active against Gram-negative bacterium E.coli ATCC 700926 or Gram-positive bacterium S.aureus ATCC 12600 up to a concentration of 100 uM under low-salt conditions.
PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 3128
Sequence Length: 28
Domain: The ... |
Q23240 | MGKKKSDTASGGAIPEGDNEKGKKIFKQRCEQCHVVNSLQTKTGPTLNGVIGRQSGQVAGFDYSAANKNKGVVWDRQTLFDYLADPKKYIPGTKMVFAGLKKADERADLIKFIEVEAAKKPSA | Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-trans... |
P68099 | MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAVGFSYTDANKNKGITWGEETLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE | Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-trans... |
P53698 | MPAPFEKGSEKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGVFGRKSGLAEGYSYTDANKKKGVEWTEQTMSDYLENPKKYIPGTKMAFGGLKKPKDRNDLVTYLKKATS | Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-trans... |
P00011 | MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWGEETLMEYLENPKKYIPGTKMIFAGIKKTGERADLIAYLKKATKE | Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-trans... |
Q5JEK6 | MLDLVVIGHVSIDTLIFPDGRRVTMPGGAAAGVATSAALAGAKVGLVTKIGTDFPKEWLQALSSVLDISGVQILPGKTIHIQMIYHEDGSVDAPVEMGVAQKMGEIPIPEEYLDAKVFHISPIPPEEQLKLLNRLKGKRVTVDFNPTYKEEYIKRRDLLREIVSRVEIVFPNEREALMITGAEDVKDAARILHGWGAKLVVITRGEKGVLVYDGSFREFPALPIKPEEIVDPTGGGDAFAGGFLAGYSRGRPLEECVRLGLERAREVLKKWGDWSITV | Cofactor: Mg(2+) is the preferred cation, followed by Mn(2+) and Co(2+).
Function: Involved in nucleoside degradation. Phosphorylates cytidine to CMP. Can also act on deoxycytidine and uridine, but is most active with cytidine. ATP is the most preferred phosphate donor, but it can also use GTP, CTP or UTP.
Catalytic Ac... |
Q2YKD6 | MWYFSWLLGLPLAAAFAVLNAMWYELMDDRARKRLAADPTAELALEGNKHH | Function: Required for correct functioning of cytochrome bd oxidase.
Catalytic Activity: 2 a ubiquinol + 4 H(+)(in) + O2(in) = 2 a ubiquinone + 4 H(+)(out) + 2 H2O(in)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5876
Sequence Length: 51
Pathway: Energy metabolism; oxidative phosphorylation.
Subc... |
P56100 | MWYFAWILGTLLACSFGVITALALEHVESGKAGQEDI | Function: Required for correct functioning of cytochrome bd-I oxidase. This protein and AppX may have some functional overlap.
Catalytic Activity: 2 a ubiquinol + 4 H(+)(in) + O2(in) = 2 a ubiquinone + 4 H(+)(out) + 2 H2O(in)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4042
Sequence Length: 37
P... |
Q9KII6 | MTRSPCSTTSRWISSMSTSEYRAVDAESDLPISAAELAALASQLYAASIRPGPDSPPQQAPVAPRGSVPDATAATSAGRTAAGTADVYPGPVPQVGGRDVYLPPPASPAPEAPPQAAPPAPRGSAPDATAATSAGRAAAGTSDVYSSWVPQLGVADIYLGAPTPAGPEAPPQSAPPAPRGQVPDTTAAATAYGADLSAFAVPTGIVSTAPGVQAGTAPPVPVVPRAATAPSWLPEAPSVADLGWSDAPAPDAPAGDEHDYHFLTKTDPVPQFRDEHEVFDVAAIRSDFPILKETVNGKPLIWFDNAATTQKPQVVIDRLS... | Function: Cargo protein of a type 2A encapsulin nanocompartment involved in sulfur metabolism. Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules.
Catalytic Activity: [sulfur carrier]-H + L-... |
Q8KUU5 | MTNTVPSVPAVPNLPTQSDPFFNERSLEQLTQTVLQDLQQAGVSEAESAPTPLSVPTPALPTTSALAVPQSPTAIANVPAPPSSIDERSLAQLAQAVLQDPQLASAIASIFPSVTLPTSASVPRSVPVPPSFLPSLVPTAPPIHDEVGVIPHHQLPVPSQPTPAGLQQTASSKSGSGFYFIDEQVETAIAALHSNLTVFPQLTTSSIPTLTGAHSAGAVGFDIHQVRRDFPILQERVNGRPLVWFDNAATTQKPQVVIDRLSHYYQHENSNIHRAAHELAARSTDAYEAAREQVRHFLNAASTEEVVFVRGTTEAINLVA... | Function: Cargo protein of a type 2A encapsulin nanocompartment probably involved in sulfur metabolism. Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules.
Catalytic Activity: [sulfur carrie... |
C7YTF5 | MANEGRIATLDSTVADRLPVYSKLLFDGKAAKGLSFETIAKHLDRSEVACAALFYGQATASPEDIDRLSDLLEISKETLTTQMTGFPNRGQASPMPPVEPLIYRLYEIVQNYGYAYKAILNEKFGDGIMSAICFSTTVDKEVDEAGAPWVVITLKGKWLPFSRF | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Mass (Da): 18108
Sequence Length: 164
EC: 4.2.1.104
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B0DN41 | MSFASAPTVPTNTSHYADLPAASSALFQAKARRGLTFDQIAKAIGKDEVWLAAAFYGQARFTEDELITVGEVLGIGSSELVSQLGSHWWPNRGLGPMPPTDPVIYRLYESVLVYGHAIKAVIHEKFGDGIMSMIDCKINVERKEDPKGDRVLLTFDGKFLPYARW | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Mass (Da): 18218
Sequence Length: 165
EC: 4.2.1.104
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B6TTW1 | MEASGEKAAVVRRLMEAKEVSGKTFSGIAAETGLTNVYVAQLLRRQAQLKADTVPALRAALPTLTDDLIELMMQPPFRSYHPNIVHEPAIYRLNEAVMHFGESIKEIINEEFGDGIMSAIDFYCSVDKVEGADGKDRVVVTFDGKYLPYTEQKSEHMMSRPTRKTS | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Mass (Da): 18526
Sequence Length: 166
EC: 4.2.1.104
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B7FKW7 | MAQNKANTVSQLQSLKNKSGKSYNQLAEETGLTNVYVAQLLRRQAHLKPETAPKLKAALPELPEELIHEMMKPPLRSYDPNIIQDPTVYRLNEAVMHFGESIKEIINEEFGDGIMSAIDFYCSVDKVQGVDGKDRVVLTFDGKYLPHSEQKTEHMVSRTRPLEKQ | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Mass (Da): 18725
Sequence Length: 165
EC: 4.2.1.104
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A0QL81 | MLGRMTRNQLTEQIVVARLAKGLTWQELADAIGRPLLWTTSALLGQHPIPAELGRILVDKLGLDESAVPVLAAPPMRGGLPTAVPTDPTIYRFYEALQVYGGALKEVIAEQFGDGIMSAINFSVDLQKKPHPSGDRVVVTFDGKFLPYQWVSSEQ | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Mass (Da): 16941
Sequence Length: 155
EC: 4.2.1.104
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A1T8R2 | MTREDATAEILAARLARGLSWQQLAEAIDRPLVWTISALLGQHPVPVESAEILVELLGLDQSAVPVLAAVPMRGGLPTAVPTDPTIYRFYEVLQVYGGAIKELIHEEFGDGIMSAINFSVDVERKPHPDGDRVVVTFDGKFLPYAWTAADGRR | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Mass (Da): 16722
Sequence Length: 153
EC: 4.2.1.104
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A2Z8F9 | MEGGGGERAAGVVRRLMAAKAESRKSFSEIGEEAGLTNVYVAQLLRRQAQLKPETAPALRAAVPGLTDDLVALMMEPPFRSYHPDIVHEPAIYRLNEAVMHFGESIKEIINEEFGDGIMSAIDFYCSVDKVQGADGKDRVVVTFDGKYLPYSEQRSDHMMSRLTRKTS | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Mass (Da): 18608
Sequence Length: 168
EC: 4.2.1.104
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C1FZ35 | MSNINLATLDISEHPNLPSSSAVLFEAKAKKKLSFEAIASAIGRNEVATAAIFYGQAKASAEDIVKLSEVLGIDHLYLESLLSGFPDRGKSMTFPPKDPLIYRLFEIVQNYGYAYKAVMNEKFGDGIMSAISFSTKVEKETDLDGNNWAVVTWRGKWLPYSRF | Function: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Catalytic Activity: cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+)
Sequence Mass (Da): 18093
Sequence Length: 163
EC: 4.2.1.104
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Q9WWR4 | MANAHDTHHEGNHGSVKSYMIGFILSIILTAIPFGLAMSPSLPKNLTVLIIVAMAVIQVVVHLVYFLHMDRSKEQRNNVWTFLFTTLVIALLVGLSLWIMFSIHFEMLAK | Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron (By similarity).
Location Topology: Multi-p... |
Q825I8 | MTEPGTSVSAPVAFPQDRTCPYDPPTAYDPLREGRPLSRVSLYDGRSVWVVTGHAAARALLSDQRLSSDRTLPRFPATTERFEAVRTRRVALLGVDDPEHRTQRRMLVPSFTLKRAAALRPRIQETVDGLLDAMEAQGPPAELVSAFALPLPSMVICALLGVPYADHDFFESQSRRLLRGPGIAEVQDARAQLDDYLYALIDRKRKEPGDGLLDDLIQEQLNRGTVDRAELVSLATLLLIAGHETTANMISLGTFTLLRHPEQLAELRAEPGLMPAAVEELLRFLSIADGLLRVATEDIEVAGTTIRADEGVVFATSVIN... | Function: Catalyzes the conversion of 1-deoxypentalenic acid to pentalenic acid in the biosynthesis of neopentalenolactone antibiotic.
Catalytic Activity: 1-deoxypentalenate + 2 H(+) + O2 + reduced 2[4Fe-4S]-[ferredoxin] = H2O + oxidized 2[4Fe-4S]-[ferredoxin] + pentalenate
Sequence Mass (Da): 44113
Sequence Length: 40... |
G4MWA8 | MKLRVSQSPTPQMVITMLHGSSTYSLLASKKRNSNVVGQYIKNGIPFRMRNPADPSQPQVILPFKYLSEMKNAAESSWSFMHFSNQSFLLEYINAPLGSSIAHQVVRGELNKNLDWTALQPYMLFANTIARTTSLVLAGPELSANPEWTTIMVTFTMTLMQTSQEVRAKYSPWLRWLVPWIHPGAKNLYKIRKRCAQLLAPSYQNRRAGMVGDEKPFMDAIQWLMNKRTYKSKDLMKLSDDQLFLSVASIHSTSASTLSTLYDLLDRPECMDGILHEIRTIRAESKSSDWTKHDLDRLVKLDSFMKESQRYHPVGQVTVQ... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of a tyrosine-derived cytochalasan acting as a fungal signal recognized by resistant rice plants and leads to avirulence in Pi33 resistant rice cultivars . The first step in the pathway is catalyzed by the hybrid PKS-NRPS A... |
P52010 | MPRVKVFFDITIGGKKGGRIVMELYNDIVPKTAENFRALCTGEKGKGKSGKKLHFKGSKFHRIIPEFMIQGGDFTEGNGTGGESIHGEKFDDENFKEKHTGPGVLSMANCGANTNGSQFFLCTVKTTWLDGKHVVFGKVIEGMDVVKAIESKGSEDGAPSAPCVIADCGEMK | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 18535
Sequence Length: 172
EC: 5.2.1.8
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A0A4D6Q414 | MTMTSLDIILFISAIVFLSIYYYNLFSNAKRSNGLKLPPGPKGYPVLGNLPQLGAKPHQALQAFSRVYGPLMRLRLGSVDLVVASSPSVAAQFLKNDSNFCARPPNSGAEHMAFNYHDLVFAPYGPRWRLLRKLSAVHLLGPKALDDNQNVREEELAVLARMLYERSRGGEPVNVGKEMHVCSTNALSRAMMGRRVFEKLAVGGGGVEEEEEMKKAEEFKDMVVEVMTLAGVFNIGDFVPWLKPFDIQGVVRKMKRVHRRYNVFLDKFIAECRSSAKPGANDLLSVLIGQRGKSDGSGGEITDTAIKALVLNLLTAGTDT... | Function: Flavonoid 3',5'-hydroxylase that catalyzes the 3'- and 5'-hydroxylation of flavanones, dihydroflavonols and flavonols . Converts narigenin to dihydrotricetin, dihydrokaempferol to dihydromyricetin and kaempferol to myricetin .
Catalytic Activity: a 3',5'-unsubstituted flavanone + 2 O2 + 2 reduced [NADPH--hemo... |
A0A0D1DT62 | MLNETIFGRQVADVREHGLFGRPFWLNALYAFLLYSAFLGYKSYFLHKTSRIPGPWHLHWTMLPALFYYVRGTQWRYVDKLHEKYGPLFRLGSRQIYVSDKDAIRQLLAKENLPKVNWYASLSRDPKTAGMFTTVNKEYHRSRRRLMSPAFAVEFTRQLEPFLVDATTKLFEGYHQRVQKASDPFKPLLFNVYEDLACLAMDILGETAFGVSFNLVACRDDPGADRKFADINKLLAKYLHDGGIRFFCRPFDKYMKRDLNVYKLTNPLVDARFAETEARRAAAGDAAEQVETREDILQYLVDASLEMQKGQKEKLTRTHV... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the glycolipid biosurfactant ustilagic acid (UA) . UA is a secreted cellobiose glycolipid that is toxic for many microorganisms and confers biocontrol activity to U.maydis . UA consists of 15,16-dihydroxypalmitic or 2,15... |
P82869 | MASPLSSSTVVSHRLFFLHPSPLNRKFLFVKPKLPFNRTNSGDFRMRLHSTSSKTGTKELIHSCNSSIDSKLNTFEAGSKNLEKLVATILIFVQVWSPLPLFGLDSAYISPAEAVLYSPDTKVPRTGELALRRAIPANPSMKIIQASLEDISYLLRIPQRKPYGTMESNVKKALKVAIDDKDKILASIPVDLKDKGSELYTTLIDGKGGLQALITSIKKQDPDKVSLGLAASLDTVADLELLQASGLSFLLPQQYLNYPRLAGRGTVEITIEKADGSTFSAEAGGDQRKSATVQIVIDGYSAPLTAGNFAKLVTSGAYDG... | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 50483
Sequence Length: 466
Subcellular Loca... |
Q9SSA5 | MAAAFASLPTFSVVNSSRFPRRRIGFSCSKKPLEVRCSSGNTRYTKQRGAFTSLKECAISLALSVGLMVSVPSIALPPNAHAVANPVIPDVSVLISGPPIKDPEALLRYALPIDNKAIREVQKPLEDITDSLKIAGVKALDSVERNVRQASRTLQQGKSIIVAGFAESKKDHGNEMIEKLEAGMQDMLKIVEDRKRDAVAPKQKEILKYVGGIEEDMVDGFPYEVPEEYRNMPLLKGRASVDMKVKIKDNPNIEDCVFRIVLDGYNAPVTAGNFVDLVERHFYDGMEIQRSDGFVVQTGDPEGPAEGFIDPSTEKTRTVP... | Function: Required for the assembly and stabilization of PSII, but has no PPIases activity.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 47982
Sequence Length: 437
Domain: The N-terminal helical domain blocks the interaction with the potential targe... |
G4MWB2 | MLPRSLGHSTSELSPPFDGPNGVERYVSETRSLLRKGYEKYLRRGVPFQMRNPVEELGAQVVLPPKYLDEVKRAPTDLFSFEAYSEKAFLLNYSRAPRQTEAAAHIVRVDLTRNLGKLITFYSDFAIFEVCLPLVLIRDLGALVTDLWNESALYLDKTYNSEWQTKQAYEVVCGFVARVTSVAMVGAPLCRNPVWNRIVVETTMASFGAAQAIKDKYSARWRWLAPWSESIQKDLRRIRKESIELLKPLYEDRKAAVSRSDDVQGSSEMFRDTLYWLITSNQKDRSLSGITESQLFLSLAAIHTTSATLNSFVYDWIAHP... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of a tyrosine-derived cytochalasan acting as a fungal signal recognized by resistant rice plants and leads to avirulence in Pi33 resistant rice cultivars . The first step in the pathway is catalyzed by the hybrid PKS-NRPS A... |
A0A0U2V7I8 | MNTTKLLGTGALSPSFVFDHDSGNAIFGLSSSTLVVLVAMIAVSTLTLKSVLPGDRSINLPGPRGWPIVGSWFDLGNNWAEYFRQAAKEYGDVFKVHIGNRTVVVVNSPKAAHILFNEHGSSLISRPWFYTFHGVLSKSSAFTIGTSAWSDSTKNKRKAAATALNRPAVQSYMPIIVEESLDAVRRILNDGNAGKNGIVPYSYFQRLALNTSFQVNYGFRMGERDDGLFDEISEVIAKVASVRAVTGSLQDYVPLMRYLPANAKSKAAASYGLRRKKFMSKLYEELEQRVNQGKDESCITGNILKDTESRKKLSRLEIDS... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of itaconic acid and 2-hydroxyparaconate . Cis-aconitate is secreted by the mitochondrial tricarboxylate transporter MTT1. In the cytosol cis-aconitate is converted into trans-aconitate via isomerization by the aconitate-de... |
Q9C566 | MGRSKCFMDISIGGELEGRIVIELYDDVVPKTAENFRLLCTGEKGLGPNTGVPLHYKGNRFHRVIKGFMIQGGDISANDGTGGESIYGLKFDDENFELKHERKGMLSMANSGPNTNGSQFFITTTRTSHLDGKHVVFGRVTKGMGVVRSIEHVSIEEQSCPSQDVVIHDCGEIPEGADDGICDFFKDGDVYPDWPIDLNESPAELSWWMETVDFVKAHGNEHFKKQDYKMALRKYRKALRYLDICWEKEGIDEETSTALRKTKSQIFTNSAACKLKFGDAKGALLDTEFAMRDEDNNVKALFRQGQAYMALNNVDAAAES... | Function: PPIases accelerate the folding of proteins . It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides . Involved in promoting the expression of the juvenile phase of vegetative development, and, to a lower extent, in regulating the positioning of floral buds, floral morphogene... |
G4MWB3 | MLSLLETKIIEPFMVVRQTLAPLRLSRWQIFKHMTRILIFSSNTRTIIFCVLMSLVGYIVSRIIWGRQEKYPDHGLPIVKTNDYHFDNIVAEGKRLYPNQAFMGINKRYKFVIYPSSSWEELKRIPEQTASIMDFQHVCNSGEWSLVGGETHELVKTITAELTRSLPARVPNRQQDAKMTFDTIIGHCPEEKGFNLLMTSLEIIAKINACTFVGRELGANKSWVTAVVYSPLWVYFAVTLCNATPDILRPLLRPLFFLPALRNYWNMQKLLKPKLDREMETFRQTDDKRKLLVPKSDQDLPFTHFLLSRYTEAAATIKQL... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of a tyrosine-derived cytochalasan acting as a fungal signal recognized by resistant rice plants and leads to avirulence in Pi33 resistant rice cultivars . The first step in the pathway is catalyzed by the hybrid PKS-NRPS A... |
Q1JPY5 | MTILEVGSQLIESAVLQMSLTSVLLTASVFTLTLGYFSKLLFTQHSSEHTKYPPHIPSSLPFLGQAVAFGRSPIEFLEKAYEQYGPVVSFTMVGKTFTYLLGSDAAALMFNSKNEDLNAEDVYARLTTPVFGKGVAYDVPNPLFLEQKKMLKTGLNIAQFKQHVEIIEEETKDYFRRWGESGERNLFDALSELIILTASRCLHGCEIRSLLDERVAQLYADLDGGFTHAAWLLPGWLPLPSFRRRDRAHLEIKKIFYNVIKKRREDTEKHDDILQTLIDATYKDGRPLSDDEIAGMLIGLLLAGQHTSSTTSAWMGFFLA... | Function: Sterol 14alpha-demethylase that plays a critical role in the cholesterol biosynthesis pathway, being cholesterol the major sterol component in deuterostome membranes as well as a precursor for steroid hormone synthesis . Cytochrome P450 monooxygenase that catalyzes the three-step oxidative removal of the 14al... |
Q6Q151 | MSVLIVTSLGDIVIDLHSDKCPLTCKNFLKLCKIKYYNGCLFHTVQKDFTAQTGDPTGTGAGGDSIYKFLYGEQARFYKDEIHLDLKHSKTGTVAMASGGENLNASQFYFTLRDDLDYLDGKHTVFGQIAEGFDTLTRINEAYVDPKNRPYKNIRIKHTHILDDPFDDPPQLAEMMPDASPEGKPKEEVKDDVRLEDDWVPMDEELGAQELEEVIREKAAHSSAVVLESIGDIPEAEVKPPDNVLFVCKLNPVTEDEDLHTIFSRFGTVVSADVIRDFKTGDSLCYAFIEFENKESCEQAYFKMDNALIDDRRIHVDFSQ... | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Influences somehow regulation of RNA pol II (CTD) phosphorylation. Binds RNA with preferences for GC-rich sequences. Probably involved in activities connecting transcription a... |
P52013 | MKSLLVVAAVLAVGALAQGDDAKGPKVTDKVYFDMEIGGKPIGRIVIGLFGKTVPKTATNFIELAKKPKGEGYPGSKFHRVIADFMIQGGDFTRGDGTGGRSIYGEKFADENFKLKHYGAGWLSMANAGADTNGSQFFITTVKTPWLDGRHVVFGKILEGMDVVRKIEQTEKLPGDRPKQDVIIAASGHIAVDTPFSVEREAVV | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 21927
Sequence Length: 204
Subcellular Location: Cytoplasm
... |
Q9LY75 | MTKKKNPNVFLDVSIGGDPVQRIVIELFADVVPKTAENFRALCTGEAGVGKSTGKPLHFKGSSFHRVIKGFMAQGGDFSNGNGTGGESIYGGKFSDENFRLDHDGAGVLSMANCGPNTNGSQFFILFKRQPHLDGKHVVFGKVVEGMAVIKKMELVGTSDGKPTSPVKIIDCGETSQIRAHDAAEREKGKSKKSNKNFSPGDVSDREAKETRKKESNEKRIKRKRRYSSSDSYSSSSDSDSDSESEAYSSSSYESSSSSDGKHRKRKSTTRHKGRRGERKSKGRSGKKKARPDRKPSTNSSSDTESSSSSDDEKVGHKAI... | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be implicated in the folding, transport, and assembly of proteins. Probably involved in early steps of spliceosomal assembly.
Catalytic Activity: [protein]-peptidylproline... |
A5G863 | MAENGLNIVWHSRSLTKADYYDRNGHRPLVVWFTGLSGSGKSTLAHAAEEALFKKGCYTYILDGDNMRHGLNSDLGFSEADRRENIRRIGEVAKLFVDAGIVVLAAFISPYQEDRDRVRALFEPAEFIEIYVKCDLDTCESRDPKGLYRKARAGQLPQFTGIDSPYEEPQAPELVIDTCRLGVEESVAAIIRFVERRSADGGRLTADG | Function: Catalyzes the synthesis of activated sulfate.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 23233
Sequence Length: 208
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
EC: 2.7.1.25
|
B8D0S4 | MRNQKGVTVWFTGLSGAGKTTVAREVERQLKEKGYYVQRLDGDIVRQHLTRDLGFTKEDRDENIRRNSFVAKLLTQNDIITLCSFISPYRKARQTAREIIGEFIEVYVNAPLEVCEDRDVKGLYAKARAGEIDNFTGISDPYEPPQNPDLELRTDKETVEESASKVIEYLEEKGYINLPEDVLAG | Function: Catalyzes the synthesis of activated sulfate.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 21106
Sequence Length: 185
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
EC: 2.7.1.25
|
B0JL16 | MKQRGVTVWLTGLSGAGKSTITEALQAKLIAEGYSIEVLDGDIVRTNLTKGLGFSKEDRDENIRRIGFVSNLLTRHGVIVLVSAISPYREIREEVRGKIGNFVEVFVNAPLSVCEDRDVKGLYKRARAGEIKSFTGIDDPYEPPFNPEVECRTDLETLEESVAKVWNKLTELGYIHQAVAV | Function: Catalyzes the synthesis of activated sulfate.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 20110
Sequence Length: 181
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
EC: 2.7.1.25
|
Q1D6P1 | MGRSAGFILWLTGLSGAGKSTLSRALRAHLASSMPVEVLDGDEVRTWLSRGLGFTREDREENVRRIGHVARLLAKHGVGVIAAAISPYASSRAEVRRLAEEAGIPFVEIYVQAPLDVLIARDVKGLYKKALAGELAHFTGVSDPYEAPDAPDVTVHSDVDTVEAGLWRVLETLRKRGLLDAAAAA | Function: Catalyzes the synthesis of activated sulfate.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 19866
Sequence Length: 185
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
EC: 2.7.1.25
|
B2T3K5 | MSASRGAVIWMTGLSGAGKSTLANALHQRLMEAGHAAIVLDGDVLRRGLNADLGFTPEDRTENLRRIAHVAALFMQQGFVVIAAVISPEHRHRCSAREIVGDGFIEVFVNAPLNVCEARDAKGLYARARRGEIPHFTGISGPFEAPLAPDVVIESDRMPVDESVDRLLAHLAAMGRPGH | Function: Catalyzes the synthesis of activated sulfate.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 19265
Sequence Length: 179
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
EC: 2.7.1.25
|
Q13ZJ7 | MSAARGAVIWMTGLSGAGKSTLANALHLRLKEAGQAAIVLDGDVLRRGLNADLGFTPEDRTENLRRVAHVAALFMQQGFVVIAAVISPEHRHRRAAREIVGEGFVEVFVNAPLQVCEARDAKGLYARARRGEIAHFTGISDPFEAPLAADLVIETDRMPVNEGVDRLLAHLVTMGRVSG | Function: Catalyzes the synthesis of activated sulfate.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 19272
Sequence Length: 179
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
EC: 2.7.1.25
|
A6KXG9 | MEEENIYPIFDRMLSRKDKEELLGQRGVMLWLTGLSGSGKSTIAIALERELHKRGLLCRILDGDNIRSGINNNLGFSAEDRVENIRRIAEIGKLFVDTGIITIAAFISPGNELRQMAARIIGIEDFLEIYVSTPLVECEKRDVKGLYAKARRGEIKNFTGISAPFEAPEHPALSLDTSKLSLEESVNTLLELVLPIVGKKGEKI | Function: Catalyzes the synthesis of activated sulfate.
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Mass (Da): 22680
Sequence Length: 204
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
EC: 2.7.1.25
|
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