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
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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 | MFASAGQQHPQIVPKEEESILNYLLEVRSSLAKLKQNRTQYLNSKDVQTTYQHVLTKVRELDDIRKNSHETPAKSAATLIHSTELHNRVDSVLDDVFQLLSLCFLTVGLKNSAPATYASLSTVESLLEHLNESNVFTHHDLSPIKERLEEISKIVEQKNSSPAYDEDGNDDRLREIDNERKKNKIEEDLLLRAKLKHCKDEYDILEGKLEEIDPSLSTVMEKLFRIRRGLLSLVASAKKTMSKSDINTNSLLQEQNDLQTNNESLTDDKHLVSQEYVHEKLSVLKNELSELESNRDDSGKFKSLESHQVAEKGQSVLNGLLDDCHDLVNDLSHQKNGGLTLDPYLQPIYEQLIDIKTTLENLMITRRWTLRETDLFSYQKKLNEIDNKRINGKFPTKSQDSKGQSILLYLLRRCYAIIYKLLESSEPVSEALQPIHNQLSTVRRCLLELKRMGGVNNERELYPYQMKLASLDNLRTEGIFYDSDGNIPEGQGILNALLAECFDILHELKVEAEEKAQNSTSSDGSDDDDNGESGIDSNSNDSEPESEYQQE | 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
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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: cutin + H2O = cutin monomers.
Sequence Mass (Da): 26074
Sequence Length: 255
Subcellular Location: Secreted
EC: 3.1.1.74
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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 2 disulfide bonds play a critical role in holding the catalytic residues in juxta-position; reduction of the disulfide bridges results in the complete inactivation of the enzyme.
Catalytic Activity: cutin + H2O = cutin monomers.
Sequence Mass (Da): 21602
Sequence Length: 214
Subcellular Location: Secreted
EC: 3.1.1.74
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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).
Catalytic Activity: cutin + H2O = cutin monomers.
Sequence Mass (Da): 23074
Sequence Length: 221
Subcellular Location: Secreted
EC: 3.1.1.74
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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 similarity).
PTM: The 2 disulfide bonds play a critical role in holding the catalytic residues in juxta-position; reduction of the disulfide bridges results in the complete inactivation of the enzyme.
Catalytic Activity: cutin + H2O = cutin monomers.
Sequence Mass (Da): 22699
Sequence Length: 223
Subcellular Location: Secreted
EC: 3.1.1.74
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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, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9063
Sequence Length: 80
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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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, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 2628
Sequence Length: 23
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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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, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9118
Sequence Length: 79
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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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, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 2636
Sequence Length: 23
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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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, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3222
Sequence Length: 29
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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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, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3171
Sequence Length: 29
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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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, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9396
Sequence Length: 83
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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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, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9353
Sequence Length: 83
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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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, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9077
Sequence Length: 81
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Mitochondrion inner membrane
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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 Location: Secreted
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O00574 | MAEHDYHEDYGFSSFNDSSQEEHQDFLQFSKVFLPCMYLVVFVCGLVGNSLVLVISIFYHKLQSLTDVFLVNLPLADLVFVCTLPFWAYAGIHEWVFGQVMCKSLLGIYTINFYTSMLILTCITVDRFIVVVKATKAYNQQAKRMTWGKVTSLLIWVISLLVSLPQIIYGNVFNLDKLICGYHDEAISTVVLATQMTLGFFLPLLTMIVCYSVIIKTLLHAGGFQKHRSLKIIFLVMAVFLLTQMPFNLMKFIRSTHWEYYAMTSFHYTIMVTEAIAYLRACLNPVLYAFVSLKFRKNFWKLVKDIGCLPYLGVSHQWKSSEDNSKTFSASHNVEATSMFQL | 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 | MDDGHQESALYDGHYEGDFWLFNNSSDNSQENKRFLKFKEVFLPCVYLVVFVFGLLGNSLVLIIYIFYQKLRTLTDVFLLNLPLADLVFVCTLPFWAYAGTYEWVFGTVMCKTLRGMYTMNFYVSMLTLTCITVDRFIVVVQATKAFNRQAKWKIWGQVICLLIWVVSLLVSLPQIIYGHVQDIDKLICQYHSEEISTMVLVIQMTLGFFLPLLTMILCYSGIIKTLLHARNFQKHKSLKIIFLVVAVFLLTQTPFNLAMLIQSTSWEYYTITSFKYAIVVTEAIAYFRACLNPVLYAFVGLKFRKNVWKLMKDIGCLSHLGVSSQWKSSEDSSKTCSASHNVETTSMFQL | 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 membrane
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O54851 | MGEWTILERLLEAAVQQHSTMIGRILLTVVVIFRILIVAIVGETVYDDEQTMFVCNTLQPGCNQACYDRAFPISHIRYWVFQIIMVCTPSLCFITYSVHQSAKQRERRYSTVFLALDRDPAESIGGPGGTGGGGSGGSKREDKKLQNAIVNGVLQNTETTSKETEPDCLEVKELTPHPSGLRTAARSKLRRQEGISRFYIIQVVFRNALEIGFLVGQYFLYGFSVPGLYECNRYPCIKEVECYVSRPTEKTVFLVFMFAVSGICVVLNLAELNHLGWRKIKLAVRGAQAKRKSVYEIRNKDLPRVSVPNFGRTQSSDSAYV | 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 membrane
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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 membrane
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Q96KN9 | MEGVDLLGFLIITLNCNVTMVGKLWFVLTMLLRMLVIVLAGRPVYQDEQERFVCNTLQPGCANVCYDVFSPVSHLRFWLIQGVCVLLPSAVFSVYVLHRGATLAALGPRRCPDPREPASGQRRCPRPFGERGGLQVPDFSAGYIIHLLLRTLLEAAFGALHYFLFGFLAPKKFPCTRPPCTGVVDCYVSRPTEKSLLMLFLWAVSALSFLLGLADLVCSLRRRMRRRPGPPTSPSIRKQSGASGHAEGRRTDEEGGREEEGAPAPPGARAGGEGAGSPRRTSRVSGHTKIPDEDESEVTSSASEKLGRQPRGRPHREAAQDPRGSGSEEQPSAAPSRLAAPPSCSSLQPPDPPASSSGAPHLRARKSEWV | 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 membrane
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Q8BSD4 | MEKLNLLGFLIITLNCNVTIMGMIWLIVEVLLRMLVVVLAGSPIYEDEQERFICNTLQPGCANVCYDLFSPVSPLRFWLVQSLALLLPSVVFGTYTLHRGAKLAAVGGACRPQVPDLSTAYLVHLLLRMLLEAGLAFLHYFLFGFSVPARVSCSHVPCSGAVDCYVSRPTEKSLLILFFWAVSALSFLLSLADLLWILPRRKTLRTTQWVNGEARPVCEVPAPPPCLLQNPQGYLSQGQVDQEDRQEEQVVPEFPCMWTAGQSDNSNVGQACVSGLLEHSDQDASEATSSAGDRLTVAHTAHELRFHRETSLDLGGKNTQADELSLATQSHLARHSSASKPQAPCRLTTSGSAPHLRTKKSEWV | 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 membrane
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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 | MHSVLAQAASGALSFELRLGQSSVLTICILALLTFVLREIVLYFTRHSMPPGPFRWPLIGNALQLPQDHPWVKYTEWAKMYGPLMQLDVLGQHMLVITSAQTARDLMEKRSSIYSDRPHLVMAGDLAGFGDTLILQNYGEEFRYQRKLVSHSFSPSVIHRYYDLQEAAARRLVLAIIEDPDSLENSTRLHIASIILRMTYGYTVKGVDDPLFTTGIAVINGFSEATRPGAWPVDFVPILQYVPHWVPGFVFTRKAREWRGVLERAMWAPYHWCKENYARDAAHGLCLCGSILAAEGSQLSSDQEWLFVNAAVTVMGGGLDTNISTILSFVLAMLRFPEVQKKAQAEIDAVIGPNRLPLISDRHSLPYVRSVVTEVYRWIPAVPLGIPHALRQDDHYDGLFLSKGSVVVPNVWGMLHDPSIYPAPHEFKPERYGGLDAEMTKVTDIAFGFGRRACPGFYFAEGTIFAIVATVLAICDVVPTVDEHGQEVIPEVSLTSGAIVSPENVKCAFRPRSGRVKDILVEAVETEQE | 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 | MPASFLASLRAWIASSTIGQRILLALALGLLLITARVISKSKGTMPPGPRGLPLLGNIFQLPKLPWYRFTEWKEEFGPIFSLNFAGTPVVVLNSHEVVGDLLERKSTIYSDRPRFIMAGEILTGGMLIVFTGYGKVWRKLRRAGQEGLNVRASEKYQPLQESEARLLTTNMLREPAEWDAHLQRAAASSIASAVYAWPPLTKSDDGLVHRIDELMRRLVMAGLPGRYLVEIFPIMKHLPTWMAKWKREGLEWHRRDTEMFEGFYDNVARFMASGKYKPSLTAGLIERQEKNGLSKKEVSWLAGTMIGAGAETTAASLSVFMLAMTLYPDVMRKAQAEIDALVGRERMPTFADRPHLPYVCALVKEVLRWRPVGPVGVPRRTSEDDWYKGYFIPKGTLVIANVWAMNRDPAIYPDYDEFRPDRFLDASGNEIDIAGTHGQGHVTYGFGRRICIGMHVANQALFIDIAALLWAFNIEAPTGPDGNPILPSRTDFVDEGLVFRPAAFRCKVTPRIDDVATMLATLEKNA | 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 | MRDSLARNILLPTAPSLGAIACLLLAIAIGLLLLPRSQPHCFPPGPPVKPIVGSILQVSPQGAWYKFSEYQKVYGDLLFFRGLGSHVLVLNSMKAINDLLDKRSSVYSNRPTFTVVGELMGLGQSMPLLPYGEEWRAHRRLAHSALSPTAVRRYHGIQEDMAALLCMRLLREPEAFFSHVRLIAGNIILSVVYGLPVETSEDEYIAHAERTMQVIGKATVPGAYLCDLMPFLKHLPSWVPFQREASTGREMIERLVTKPFEHVKRAMEAGSAPPSVTQDLLSTNIDDMHDVEQRIKWTTGAMYGAGGETTYSTVLVFIMAMALHPEKQQRAQQEIDRVIGIERFPRISDRAHLPYVNAVIKETMRWHPVLPLSIARMSAQDDLYDGYSIPEGTVVIPNIWGIANDCPRATEFDPERFLNEGAPVDPSSWAFGFGKRLCPGKFLGENSVFILITALLAIFDITPNSSEDLQPDFTLDLVSYPRPFKCRIQPRSEGHAQLAISRAAQRSF | 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: Membrane
EC: 1.-.-.-
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F1SY74 | MALPPGVPFLIRVSLILAFAPVCVVIVANFIWRHTDVALPTWPVTLLSVASTPLTILVRVWYRQWKYQRAAARLGAIMPPRWVGKKLGNLDILKEMLQTMQSGYIADFAWKLFNNLGNTVQMNVLGGTAYLTCDPNIIKSVLATDFNNFEKGDLFKQEMASVLGTGVFNADGDMWKWHRAMTRPFFSRDRISHFELFDRRSEQAVAKMTERFHSGYAVDFQDLISRFTLDSATEFLFGSCVNSLHSPLPYPHNQHPTPFSHPSSKSLASNPSRAEAVASAFMRAQIVLAERVAMGAIWPLLEMRKSRTGEHMRIIDEYLDPILKDALRRKEDMANIGAGIHDDKESSDTDGETLLDHLVRLTSDPVVLHDEVLNILIAGRDTTAGTLTFVVYFLCMYPDVFNRLRAEVLEKVGPNARPTYADIKEMRYLRAVINETLRLYPVVPFNIRWSIHEGTLPNPDPNGKPFYLPPKTPVTYTVFAMHRRKEYWGPDADEFDPDRFLDDRVAKYLTKNPFIFLPFNAGPRICLGQQFAYNEMSFFLIKLMQHFSAMELAPEAAPPESLPPAEWAVTGWGRKRIERFWPKSHLTLYSNGGMWVKMVEADDFDKDDRDVGI | 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 | MSTDNIPTQLGIAGAVAVLLFLLRRWSSRSTLRNIPGPPPQSQWTGNLKQWFARDGADFQRDVSFNYGPVAKIHGFLGRPILYVADPKALQTILVKEEQVYQETKAFFAMTYLLFGPGLLATAGEKHRKQRKLLNPVFSIKHMRHMLPIFYGVLHKVRDAITMRVSDGPQEIDMLKWMGRTALELIGQGGLGYSFDKLVEDGDNEYGRALKHLQPTLQRINVLRRLIPYVYKLGPAWFRRMVMHYFPLGQVRDAKEIVDTMQRCSSEIFASKKIALARGDEAVMKQVGEGKDIMSILMKANSMASEADRIPEEELVAQMSTFLFAATDTTSNTLARILQQLAIHPDTQQKLREEILAANAEEYMAYDDLDALPLLDGVCRETLRVFPGVTNLARTPTQDTILPLSEPVVGTDGTVMREILVPRGTEILIGIQGSNGRKERWGEDSYEWKPERWLSPLPKTVTENPVPGVYSNLMTFMAGRRACIGFKFSEMEMKVVLAVLLSNFTFELTDKPIQWNISGVRYPTVGKDSNVAQLPLKVGLYKKPTLQ | 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 | MFLQIVTSVLATGLLYALISVLQQNRTLSASLPPGPPGHWLFGNAPPKAFPYRHFAELTETYGPVFTLRFGRRIVCVIGRYQAAVDILMKHSAETSDRPRSVAANEIMSKGHRVLMTPAGERLKKYRRALHAFLQPSSSATYKPMQYKNAKNYVLDCLHDGGHHLDHGRKYAASVVMSVAYGKTTPTSYSDPEVLQINKSLARLGAALKPGAYLVDTYPILKYCPGYASHLRRYREEELALITKQANAVRELLAKGEAPPSFTAYLIENQERLGISDDELAYLSGAIFGAGSDTTAAALGIMTMAAACYPEAQARVQAQLDEVVGRDRAPTFEDEDLLPEVTAFVLEAYRWRPVSAGGFSHRATKDVVWNGYVIPAGAEIIGNHWAISRDPEVYPNPEDFKPARWLNEHGRVRNDLKFTNFGFGRRVCVGQHVADQSLFINTALVLWAFIISQDAQCPIDTYAFTDTANVHPLPFSLHFEPRVKDMEAMLGAQAE | 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 | MDSSTSLLPPLGSIILACEGLTSLVPLILSVLVCLVATVTISPTLLAYFNDPFELRAYPGPFLAKFTSAWISWIISQNRWSETVDLMHRQHGPIVRLSPDHVSVASPAAFAAVYGHSSGALKAPFYNAFANFKTRSIFNTRDRAEHSRKRRVEAHMFSPRSIRALEDTARVHFQVLVRQWDALCAPTGKTGRGSAEGTLGTISWKVHGDRVWFDCMPWFNFWSFDTISDLAFGRPFGMLEAAKGSAHVSKSNTKSVQAVSQDTSHSDEAQSELLEIPAMEVLSELLDFTVALAYLPAWVQPVFGRLPMFRDGYDAAPKLANLSLTAVANRVASQTDRADMLSELLRGRDEEGKPYGLEELSTEAELLIIAGGDTTANTSCATAYYIARDLQIQAKLQAELDVALDGVESDVAPYDAVKDLPYLDAVINEGLRLHSTIGAGLPRVVPSGGMTVLGQHLKEGTVVSSPIYTLHRNEAVWGKNACEFYPERWLEASADAKKEMMQSFAPFSMGPRACLGRSLALQQLHILLATIFHRYSLVLENNAPAQLPLRDGFARKPMKCIVGVQRRK | 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 membrane protein
Sequence Mass (Da): 24153
Sequence Length: 215
Subcellular Location: Plastid
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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 membrane protein
Sequence Mass (Da): 23925
Sequence Length: 215
Subcellular Location: Plastid
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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.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24165
Sequence Length: 215
Subcellular Location: Plastid
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Q59297 | MAENTPKPAAGTAPAKPKPAAPGAAKPAAPKAARPGAAKPAAKPAAPRAAAPSGVYKKPPVDRPDPNPFKDSKRDAVAGWFQERFYVLNPIIDYLKHKEVPKHALSFWYYFGGLGLFFFVIQILTGLLLLQYYKPTETDAFASFLFIQGEVPFGWLLRQIHAWSANLMIMMLFIHMFSTFFMKSYRKPRELMWVSGFVLLLLSLGFGFTGYLLPWNELAFFATQVGTEVPKVAPGGAFLVEILRGGPEVGGETLTRMFSLHVVLLPGLVMLVLAAHLTLVQILGTSAPIGYKEAGLIKGYDKFFPTFLAKDGIGWLIGFALLIYLAVMFPWEIGVKANPLSPAPLGIKPEWYFWAQFQLLKDFKFEGGELLAIILFTIGGVVWLLVPFIDRQASEEKKSPIFTIFGILVLAFLLINTYRVYAEYSMLK | 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
Sequence Mass (Da): 47477
Sequence Length: 428
Subcellular Location: Cell inner membrane
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P92848 | MPHQKILMLFGLLPVATNISTWWNFGSMLLTCSMIQVLTGFFLAVHYTANINLAFSSIVHIMRDVPCGWMVQNLHAIGASMFFICIYIHIARGLYYGSYLNKETWLSGTTLLIMLMATAFFGYVLPWGQMSFWAATVITNLLTAIPYLGGTMTTWLWGGFAINDPTLTRFFALHFILPFGIISLSSLHVLLLHEEGSSNPLGTNSDIDKIPFHPYHTMKDLLMLTTTLTLLLMTISFFPDIFNDPENFSKANPLVTPQHIKPEWYFLFAYGILRSIPNKLGGALALAMSIMILFTVPFIHTSKLRSMTFRPLMQLMFWTFTSTFVLITWAATKPVEPPFISISQVASIIYFTFFISNPILGWAENKIMKNT | 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 proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42008
Sequence Length: 371
Subcellular Location: Mitochondrion inner membrane
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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 proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24078
Sequence Length: 214
Subcellular Location: Mitochondrion inner membrane
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Q9MI64 | MTNIRKTHPLMKILNKTFIDLPTPSNISSWWNFGSLLGLCLTVQILTGLFLAMHYTPDTSTAFSSITHICRDVNYGWMIRHLHANGASMFFICLYIHIGRGLYYGSYLFKKTWNIGVLLLFTTMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWVWGGFSVDKATLTRFFALHFILPFIIVALTTVHLLFLHETGSNNPMGIPSNMDKIPFHPYHTIKDILGALLLMFVLLTLTLLAPDLLGDPDNYTPANPLNTPAHIKPEWYFLFAYAILRSIPNKLGGVLALLFSILILLFIPLLHTSKQRSMMFRPLSQLLFWLLMTDLLVLTWIGGQPVEHPYIIMGQLASILYFLLILVMMPTASFIENKILKW | 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 proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43021
Sequence Length: 379
Subcellular Location: Mitochondrion inner membrane
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P15585 | MLNIFNYFKNLRVSFHEVFSLFGFFTFMTIIVQLVSGTMLAFSSVPEPMLIPTVRDEEDIEDLYTDDFFWLHERGVDLIFIFSYFHLLRKLYLNVFDLETEASWKSGVFSFLVFQVVVFFGLVLCCTHLSEITLTIAANIFHTFFMFKGKAYWFLFTDKQLNTDTLIRLAYAHYVSAFYLSFLGLLHGIDIHYDWKNEPFYDGLSSEMLWWDEALSNELTNFFVLLVFITLAFFLLFEEPEALSYEIFMWGDIGLSTDVRFYGVAPHWYFRPFMAWLIACPFHKTGIFGLLFFFVTLYYQPNLHGVSDQNSYGKKTLTISSTVLAKKNTATPFSISIDSNLYHQITYFFFIMCCLYTPSFLPYGRFFNQIGGNWGFLFSYFYVFCYLAFTD | 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 proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46044
Sequence Length: 391
Subcellular Location: Mitochondrion inner membrane
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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): 10476
Sequence Length: 95
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
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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-transport chain.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 11369
Sequence Length: 105
Subcellular Location: Mitochondrion intermembrane space
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Q9AJE4 | MKDRAADPVTKFSPSPYETGQFLRISERADVGTPQIDYLLATQRPDGLWGSVGFELVPTLGAVAGLSSRPEYADRAGVTDAVARACEKLWELALGEGGLPKLPDTVASEIIVPSLIDLLSEVLQRHRPAVGGKAGQEQEFPSPPGANAELWRQLSDRIARGQAIPKTAWHTLEAFHPLPKQFAATVTPAADGAVTCSPSSTAAWLSAVGTDAGASTRAYLDEAQSRYGGAIPMGSSMPYFEVLWVLNLVLKYFPDVPIPREIIEEIAAGFSDSGIGGGPGLPPDGDDTAYANLAGDKLGAPTHPEILMKFWAEDHFVSYPGEQTPSETVNAHALEYLNHLRMRRGITEFGAVEDACAEWVISQQTEDGCWYDKWNVSPYYSTAACVEALLDARKQDEPQLDSLRRAREWLLRHQTDSGGWGMAEPSPEETAYAVLALDLFASRGGEGAEECAAAISRAKEFFTDESRENPPLWMGKDLYTPFRIVDVTVMCGRAVVGRY | 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
Sequence Length: 499
Pathway: Antibiotic biosynthesis.
EC: 5.5.1.15
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Q9K499 | MHAFPHGTTATPTAIAVPPSLRLPVIEAAFPRQLHPYWPKLQETTRTWLLEKRLMPADKVEEYADGLCYTDLMAGYYLGAPDEVLQAIADYSAWFFVWDDRHDRDIVHGRAGAWRRLRGLLHTALDSPGDHLHHEDTLVAGFADSVRRLYAFLPATWNARFARHFHTVIEAYDREFHNRTRGIVPGVEEYLELRRLTFAHWIWTDLLEPSSGCELPDAVRKHPAYRRAALLSQEFAAWYNDLCSLPKEIAGDEVHNLGISLITHHSLTLEEAIGEVRRRVEECITEFLAVERDALRFADELADGTVRGKELSGAVRANVGNMRNWFSSVYWFHHESGRYMVDSWDDRSTPPYVNNEAAGEK | 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-isozizaene.
Catalytic Activity: (2E,6E)-farnesyl diphosphate = (+)-epi-isozizaene + diphosphate
Sequence Mass (Da): 41388
Sequence Length: 361
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Sesquiterpene biosynthesis; epi-isozizaene biosynthesis.
EC: 4.2.3.37
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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 A center (CU(A)) of the COX2 subunit of cytochrome oxidase, the final protein carrier in the mitochondrial electron-transport chain. Isoform 1 (CYC1) is the predominant cytochrome c during aerobic/normoxic growth.
PTM: Methylation may enhance its transport into mitochondria. Methylation occurs in fungi, plants, and some protozoa, but not in animals. The precise role of methylation at Lys-79 is unknown, but it seems to preclude pro-apoptotic activity, possibly by lowering affinity for APAF1.
Sequence Mass (Da): 12182
Sequence Length: 109
Subcellular Location: Mitochondrion intermembrane space
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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-transport chain.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 12233
Sequence Length: 111
Subcellular Location: Mitochondrion intermembrane space
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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 presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
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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-transport chain (By similarity).
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 13362
Sequence Length: 123
Subcellular Location: Mitochondrion intermembrane space
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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-transport chain.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 11648
Sequence Length: 105
Subcellular Location: Mitochondrion intermembrane space
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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-transport chain.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 12180
Sequence Length: 110
Subcellular Location: Mitochondrion intermembrane space
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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-transport chain.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 11633
Sequence Length: 105
Subcellular Location: Mitochondrion intermembrane space
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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 Activity: ATP + cytidine = ADP + CMP + H(+)
Sequence Mass (Da): 30419
Sequence Length: 278
EC: 2.7.1.213
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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.
Subcellular Location: Cell inner membrane
EC: 7.1.1.7
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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
Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Cell inner membrane
EC: 7.1.1.7
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Q9KII6 | MTRSPCSTTSRWISSMSTSEYRAVDAESDLPISAAELAALASQLYAASIRPGPDSPPQQAPVAPRGSVPDATAATSAGRTAAGTADVYPGPVPQVGGRDVYLPPPASPAPEAPPQAAPPAPRGSAPDATAATSAGRAAAGTSDVYSSWVPQLGVADIYLGAPTPAGPEAPPQSAPPAPRGQVPDTTAAATAYGADLSAFAVPTGIVSTAPGVQAGTAPPVPVVPRAATAPSWLPEAPSVADLGWSDAPAPDAPAGDEHDYHFLTKTDPVPQFRDEHEVFDVAAIRSDFPILKETVNGKPLIWFDNAATTQKPQVVIDRLSHFYAHENSNIHRAAHELAARATDAYEEARDTVAEFIGAPSSDNIVFVRGTTEAINLVAHAWGAKHLQPGDEIVITHLEHHANIVPWQLISQKTGAILKVAPIDDAGNLLLSEFEGLLGPRTKLVAASHVSNALGTVMPVDKIVELGHRYGARVLIDGAQSIQHIPIDVAELGADFFVFSGHKIYGPTGIGALYGTEEALTETPPWQGGGHMIADVTLERSLYQGPPTKFEAGTGNIADAVGLTEALRYVQRLGVERIAAYEHALLEYATPRLADIPGVRLIGTAQEKASVLSFVLAGHEPLEVGKALNAEGIAVRAGHHCAQPALRRLGLEATVRPSFAFYNTFEEIDVFLRAVRRIAEGGANVG | 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-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 71595
Sequence Length: 685
Subcellular Location: Encapsulin nanocompartment
EC: 2.8.1.7
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Q8KUU5 | MTNTVPSVPAVPNLPTQSDPFFNERSLEQLTQTVLQDLQQAGVSEAESAPTPLSVPTPALPTTSALAVPQSPTAIANVPAPPSSIDERSLAQLAQAVLQDPQLASAIASIFPSVTLPTSASVPRSVPVPPSFLPSLVPTAPPIHDEVGVIPHHQLPVPSQPTPAGLQQTASSKSGSGFYFIDEQVETAIAALHSNLTVFPQLTTSSIPTLTGAHSAGAVGFDIHQVRRDFPILQERVNGRPLVWFDNAATTQKPQVVIDRLSHYYQHENSNIHRAAHELAARSTDAYEAAREQVRHFLNAASTEEVVFVRGTTEAINLVAKSWGSQNLKEGDEIVITWLEHHANIVPWQQLSAETGARLRVVPVDDYGQVRLDEYQKLLSDRTKIVSFTQVSNALGTITPAKEIIELAHRYGAKVLLDGAQSVSHLAVDVQALDCDWFVFSGHKVFGPTGIGVLYGKQELLDATLPWQSGGNMIADVTFEKTVYQPAPARFEAGTGNIADAVGLGAALEYVQKIGLEAIAAYEHELLVHGTALLSQIPGLRLIGTAPHKAAVLSFVLEGFSPEAIGQALNREGIAVRAGHHCAQPILRRFGLETTVRPSLAFYNTFEELETLAAAIRRIQTGSLAL | 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 carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 67205
Sequence Length: 626
Domain: Has a disordered N-terminal domain of about 225 residues that functions as a cargo-loading domain (tested with GFP) and a conserved C-terminal cysteine desulfurase domain. The first 100 residues also function as a cargo-loading domain but not as well as the first 225 residues.
Subcellular Location: Encapsulin nanocompartment
EC: 2.8.1.7
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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-pass membrane protein
Sequence Mass (Da): 12376
Sequence Length: 110
Subcellular Location: Cell inner membrane
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Q825I8 | MTEPGTSVSAPVAFPQDRTCPYDPPTAYDPLREGRPLSRVSLYDGRSVWVVTGHAAARALLSDQRLSSDRTLPRFPATTERFEAVRTRRVALLGVDDPEHRTQRRMLVPSFTLKRAAALRPRIQETVDGLLDAMEAQGPPAELVSAFALPLPSMVICALLGVPYADHDFFESQSRRLLRGPGIAEVQDARAQLDDYLYALIDRKRKEPGDGLLDDLIQEQLNRGTVDRAELVSLATLLLIAGHETTANMISLGTFTLLRHPEQLAELRAEPGLMPAAVEELLRFLSIADGLLRVATEDIEVAGTTIRADEGVVFATSVINRDAAGFAEPDALDWHRSARHHVAFGFGIHQCLGQNLARAEMEIALGTLFERLPGLRLAAPADEIPFKPGDTIQGMLELPVTW | 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: 402
Pathway: Antibiotic biosynthesis; neopentalenolactone biosynthesis.
EC: 1.14.15.11
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G4MWA8 | MKLRVSQSPTPQMVITMLHGSSTYSLLASKKRNSNVVGQYIKNGIPFRMRNPADPSQPQVILPFKYLSEMKNAAESSWSFMHFSNQSFLLEYINAPLGSSIAHQVVRGELNKNLDWTALQPYMLFANTIARTTSLVLAGPELSANPEWTTIMVTFTMTLMQTSQEVRAKYSPWLRWLVPWIHPGAKNLYKIRKRCAQLLAPSYQNRRAGMVGDEKPFMDAIQWLMNKRTYKSKDLMKLSDDQLFLSVASIHSTSASTLSTLYDLLDRPECMDGILHEIRTIRAESKSSDWTKHDLDRLVKLDSFMKESQRYHPVGQVTVQRSNPRAYEFSDGLKIPANTQTCFLSYELNHDPDVYPDPETFDADRFLRMREKVDPQKYHFAYVSEDSINFGAGAHSCPGRHFAANEIKLMLCELLLGYEMKWPDGQSRPPTMFHDFSSNPNPGFDICIRERRL | 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 ACE1, assisted by the enoyl reductase RAP1, that are responsible for fusion of the tyrosine precursor and the polyketide backbone . The polyketide synthase module (PKS) of ACE1 is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the tyrosine precursor . Because ACE1 lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase RAP1 . Reduction by the hydrolyase ORFZ, followed by dehydration and intra-molecular Diels-Alder cyclization by the Diels-Alderase ORF3 then yield the required isoindolone-fused macrocycle (Probable). A number of oxidative steps catalyzed by the tailoring enzymes identified within the cluster, including cytochrome P450 monooxygenases CYP1 to CYP4, the FAD-linked oxidoreductase OXR2 and the short-chain dehydrogenase/reductase OXR1, are further required to afford the final cytochalasans that confer avirulence and which have still to be identified (Probable). The monooxygenase CYP1 has been shown to be a site-selective C-18 hydroxylase whereas the function of CYP3 is the site-selective epoxidation of the C-6/C-7 olefin that is present in some intermediate compounds . Finally, SYN2 and RAP2 are not required for avirulence in Pi33 resistant rice cultivars .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 52002
Sequence Length: 453
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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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 | MTMTSLDIILFISAIVFLSIYYYNLFSNAKRSNGLKLPPGPKGYPVLGNLPQLGAKPHQALQAFSRVYGPLMRLRLGSVDLVVASSPSVAAQFLKNDSNFCARPPNSGAEHMAFNYHDLVFAPYGPRWRLLRKLSAVHLLGPKALDDNQNVREEELAVLARMLYERSRGGEPVNVGKEMHVCSTNALSRAMMGRRVFEKLAVGGGGVEEEEEMKKAEEFKDMVVEVMTLAGVFNIGDFVPWLKPFDIQGVVRKMKRVHRRYNVFLDKFIAECRSSAKPGANDLLSVLIGQRGKSDGSGGEITDTAIKALVLNLLTAGTDTSSSTIEWALTELIRHPDILKKAQQEIDSAVGRDRLVTESDVPKLPYLQAIVKENFRMHPATPLSLPRMSIEECDIGGYHIPKNSTLFVNIWAMGRDPSIWPDPMEFRPSRFLPGGQGEHLEVRGNHFELMPFGAGRRICAGTSMGIRVVHSTVATLIHAFDWKLPEGLTAEKIDMEEAFGISLQKAIPLMAHPIPRLAPKAYSPKMK | 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--hemoprotein reductase] = a 3',5'-dihydroxyflavanone + 2 H(+) + 2 H2O + 2 oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58429
Sequence Length: 527
Pathway: Flavonoid metabolism.
Subcellular Location: Membrane
EC: 1.14.14.81
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A0A0D1DT62 | MLNETIFGRQVADVREHGLFGRPFWLNALYAFLLYSAFLGYKSYFLHKTSRIPGPWHLHWTMLPALFYYVRGTQWRYVDKLHEKYGPLFRLGSRQIYVSDKDAIRQLLAKENLPKVNWYASLSRDPKTAGMFTTVNKEYHRSRRRLMSPAFAVEFTRQLEPFLVDATTKLFEGYHQRVQKASDPFKPLLFNVYEDLACLAMDILGETAFGVSFNLVACRDDPGADRKFADINKLLAKYLHDGGIRFFCRPFDKYMKRDLNVYKLTNPLVDARFAETEARRAAAGDAAEQVETREDILQYLVDASLEMQKGQKEKLTRTHVRDQCVELLIAGGETTSNTITYILKALLENPAKLAKLYETIEPEPLDDAVPGFTQLPETPYLDACIQEGMRMYPVTSELGRRTGKEPTVVLGHVIPPRTAISASLRALHYSPKYWASPNRYWPERFLPADSIHSASDPAPAADMEAFMPFGCGPRNCIGSKFAWHEMRMVLHTLLARYTISAVEATDKVDFRQFVTFQLAKPEYRIAVTPRMALKA | 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 2,15,16-trihydroxypalmitic acid, which is O-glycosidically linked to cellobiose at its terminal hydroxyl group . In addition, the cellobiose moiety is acetylated and acylated with a short-chain hydroxy fatty acid . UA biosynthesis starts with omega-hydroxylation of palmitic acid catalyzed by the cytochrome P450 monooxygenase cyp1 . Terminal hydroxylation of palmitic acid precedes subterminal hydroxylation catalyzed by the cytochrome P450 monooxygenase cyp2 . Sequential glucosylation of the hydroxy fatty acid is probably catalyzed by the glycosyltransferase ugt1 (Probable). The cellobiose lipid is further decorated by acetylation of the proximal glucose residue and by acylation with a short-chain beta-hydroxy fatty acid at the distal glucose residue (Probable). The acyltransferase uat1 may be a good candidate for catalyzing either acetylation or acylation of the cellobiose lipid (Probable). The fatty acid synthase fas2 may be involved in synthesis of the carbon backbone of the short-chain beta-hydroxy fatty acid esterified to the cellobiose disaccharide (Probable). The secreted UA consists of a mixture of both alpha-hydroxylated and non-hydroxylated glycolipids; therefore, alpha-hydroxylation of the long-chain fatty, catalyzed by the fatty acid hydroxylase ahd1, occurs late in UA biosynthesis and may be the last step before secretion .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 61290
Sequence Length: 535
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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P82869 | MASPLSSSTVVSHRLFFLHPSPLNRKFLFVKPKLPFNRTNSGDFRMRLHSTSSKTGTKELIHSCNSSIDSKLNTFEAGSKNLEKLVATILIFVQVWSPLPLFGLDSAYISPAEAVLYSPDTKVPRTGELALRRAIPANPSMKIIQASLEDISYLLRIPQRKPYGTMESNVKKALKVAIDDKDKILASIPVDLKDKGSELYTTLIDGKGGLQALITSIKKQDPDKVSLGLAASLDTVADLELLQASGLSFLLPQQYLNYPRLAGRGTVEITIEKADGSTFSAEAGGDQRKSATVQIVIDGYSAPLTAGNFAKLVTSGAYDGAKLNTVNQAVITEDGSGKVESVSVPLEVMPSGQFEPLYRTPLSVQDGELPVLPLSVYGAVAMAHSENSEEYSSPYQFFFYLYDKRNSGLGGLSFDEGQFSVFGYTIAGKDILGQIKTGDIIKSAKLIEGQDRLSLPVQNNNINEST | 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 Location: Plastid
EC: 5.2.1.8
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Q9SSA5 | MAAAFASLPTFSVVNSSRFPRRRIGFSCSKKPLEVRCSSGNTRYTKQRGAFTSLKECAISLALSVGLMVSVPSIALPPNAHAVANPVIPDVSVLISGPPIKDPEALLRYALPIDNKAIREVQKPLEDITDSLKIAGVKALDSVERNVRQASRTLQQGKSIIVAGFAESKKDHGNEMIEKLEAGMQDMLKIVEDRKRDAVAPKQKEILKYVGGIEEDMVDGFPYEVPEEYRNMPLLKGRASVDMKVKIKDNPNIEDCVFRIVLDGYNAPVTAGNFVDLVERHFYDGMEIQRSDGFVVQTGDPEGPAEGFIDPSTEKTRTVPLEIMVTGEKTPFYGSTLEELGLYKAQVVIPFNAFGTMAMAREEFENDSGSSQVFWLLKESELTPSNSNILDGRYAVFGYVTDNEDFLADLKVGDVIESIQVVSGLENLANPSYKIAG | 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 target PSII subunit chlorophyll protein 47 (CP47).
Subcellular Location: Plastid
EC: 5.2.1.8
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G4MWB2 | MLPRSLGHSTSELSPPFDGPNGVERYVSETRSLLRKGYEKYLRRGVPFQMRNPVEELGAQVVLPPKYLDEVKRAPTDLFSFEAYSEKAFLLNYSRAPRQTEAAAHIVRVDLTRNLGKLITFYSDFAIFEVCLPLVLIRDLGALVTDLWNESALYLDKTYNSEWQTKQAYEVVCGFVARVTSVAMVGAPLCRNPVWNRIVVETTMASFGAAQAIKDKYSARWRWLAPWSESIQKDLRRIRKESIELLKPLYEDRKAAVSRSDDVQGSSEMFRDTLYWLITSNQKDRSLSGITESQLFLSLAAIHTTSATLNSFVYDWIAHPEYHGEILAEVKETLAQVQLNGGKWTLQHVAMLRKLDSFMKESARINPIGFVSIQRYTLKPYTFKDGFQLPAGVSFVFHSDGVHHDADNYPDPEKFDAYRHLHLRETVDPNRFHFASVSDSALGFGAGNHACPGRFLSAIIMKFFLIQFMTAYEMKYEHGGIERLPNHDNSNTTAPNRTVNLLVRRCDGTSNNA | 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 ACE1, assisted by the enoyl reductase RAP1, that are responsible for fusion of the tyrosine precursor and the polyketide backbone . The polyketide synthase module (PKS) of ACE1 is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the tyrosine precursor . Because ACE1 lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase RAP1 . Reduction by the hydrolyase ORFZ, followed by dehydration and intra-molecular Diels-Alder cyclization by the Diels-Alderase ORF3 then yield the required isoindolone-fused macrocycle (Probable). A number of oxidative steps catalyzed by the tailoring enzymes identified within the cluster, including cytochrome P450 monooxygenases CYP1 to CYP4, the FAD-linked oxidoreductase OXR2 and the short-chain dehydrogenase/reductase OXR1, are further required to afford the final cytochalasans that confer avirulence and which have still to be identified (Probable). The monooxygenase CYP1 has been shown to be a site-selective C-18 hydroxylase whereas the function of CYP3 is the site-selective epoxidation of the C-6/C-7 olefin that is present in some intermediate compounds . Finally, SYN2 and RAP2 are not required for avirulence in Pi33 resistant rice cultivars .
Sequence Mass (Da): 58346
Sequence Length: 513
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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A0A0U2V7I8 | MNTTKLLGTGALSPSFVFDHDSGNAIFGLSSSTLVVLVAMIAVSTLTLKSVLPGDRSINLPGPRGWPIVGSWFDLGNNWAEYFRQAAKEYGDVFKVHIGNRTVVVVNSPKAAHILFNEHGSSLISRPWFYTFHGVLSKSSAFTIGTSAWSDSTKNKRKAAATALNRPAVQSYMPIIVEESLDAVRRILNDGNAGKNGIVPYSYFQRLALNTSFQVNYGFRMGERDDGLFDEISEVIAKVASVRAVTGSLQDYVPLMRYLPANAKSKAAASYGLRRKKFMSKLYEELEQRVNQGKDESCITGNILKDTESRKKLSRLEIDSICLSMVSAGLDTFANTMIWTIGFLAKHPEIQRKAQAELLAHYPNRELPHVDSEDLVYIHAMAKEASRLFNVFRICLPRTNVSDVTYNNAVIPAGTTFFLNSWACNVDAEKFADPFEFKPERFMDKSASNAHVENKMGGVETYAFGMGRRMCPGVFLALREIYTTLVFLTHFFDIAPDGEYDIDPLTAVEDGRAFSVRPKPFKVRCTPRPGVDLSPVLDKQ | 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-delta-isomerase ADI1 . Decarboxylation of trans-aconitate by the trans-aconitate decarboxylase TAD1 then leads then to the production of itaconic acid . The cytochrome P450 monooxygenase CYP3 further converts itaconate to 2-hydroxyparaconate via oxidation of the double bond, leading to a transient epoxide, which can subsequently be lactonized to produce 2-hydroxyparaconate . Secretion of itaconate and possibly 2-hydroxyparaconate into the medium is mediated by the major facilitator ITP1 . The glyoxalase domain-containing protein RDO1 is not involved in the biosynthesis of itaconate and 2-hydroxyparaconate, however, it might play a role in the further conversion of 2-hydroxyparaconate to itatartarate .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 60000
Sequence Length: 540
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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Q9C566 | MGRSKCFMDISIGGELEGRIVIELYDDVVPKTAENFRLLCTGEKGLGPNTGVPLHYKGNRFHRVIKGFMIQGGDISANDGTGGESIYGLKFDDENFELKHERKGMLSMANSGPNTNGSQFFITTTRTSHLDGKHVVFGRVTKGMGVVRSIEHVSIEEQSCPSQDVVIHDCGEIPEGADDGICDFFKDGDVYPDWPIDLNESPAELSWWMETVDFVKAHGNEHFKKQDYKMALRKYRKALRYLDICWEKEGIDEETSTALRKTKSQIFTNSAACKLKFGDAKGALLDTEFAMRDEDNNVKALFRQGQAYMALNNVDAAAESLEKALQFEPNDAGIKKEYAAVMKKIAFRDNEEKKQYRKMFV | 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 morphogenesis and the expression of HSPs . Collaboratively with RBL and ULT1, influences floral meristem (FM) determinacy in an AGAMOUS and SUPERMAN-dependent manner, thus contributing to the floral developmental homeostasis .
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 40607
Sequence Length: 361
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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G4MWB3 | MLSLLETKIIEPFMVVRQTLAPLRLSRWQIFKHMTRILIFSSNTRTIIFCVLMSLVGYIVSRIIWGRQEKYPDHGLPIVKTNDYHFDNIVAEGKRLYPNQAFMGINKRYKFVIYPSSSWEELKRIPEQTASIMDFQHVCNSGEWSLVGGETHELVKTITAELTRSLPARVPNRQQDAKMTFDTIIGHCPEEKGFNLLMTSLEIIAKINACTFVGRELGANKSWVTAVVYSPLWVYFAVTLCNATPDILRPLLRPLFFLPALRNYWNMQKLLKPKLDREMETFRQTDDKRKLLVPKSDQDLPFTHFLLSRYTEAAATIKQLVIDYIQVSYTSTPTTASALFHALWELAQHPEAAEVMRRELATVMIDGNLPKTHLQELKRMDSFLRESFRLHPITRFTLQRYVKEPFQLSDGSRIPPGVMAVVDAQEINRSPEIWENPDEFDMDRFYRLREISGNDNRYHFVTTSSNSPGWGDGTQACPGRFFATSTLKIVMAHIVMNYDVSLRKVAPLKSQPLVNGSYSPDDSVEIFFKSRNVE | 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 ACE1, assisted by the enoyl reductase RAP1, that are responsible for fusion of the tyrosine precursor and the polyketide backbone . The polyketide synthase module (PKS) of ACE1 is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the tyrosine precursor . Because ACE1 lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase RAP1 . Reduction by the hydrolyase ORFZ, followed by dehydration and intra-molecular Diels-Alder cyclization by the Diels-Alderase ORF3 then yield the required isoindolone-fused macrocycle (Probable). A number of oxidative steps catalyzed by the tailoring enzymes identified within the cluster, including cytochrome P450 monooxygenases CYP1 to CYP4, the FAD-linked oxidoreductase OXR2 and the short-chain dehydrogenase/reductase OXR1, are further required to afford the final cytochalasans that confer avirulence and which have still to be identified (Probable). The monooxygenase CYP1 has been shown to be a site-selective C-18 hydroxylase whereas the function of CYP3 is the site-selective epoxidation of the C-6/C-7 olefin that is present in some intermediate compounds . Finally, SYN2 and RAP2 are not required for avirulence in Pi33 resistant rice cultivars .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 61603
Sequence Length: 534
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
|
Q1JPY5 | MTILEVGSQLIESAVLQMSLTSVLLTASVFTLTLGYFSKLLFTQHSSEHTKYPPHIPSSLPFLGQAVAFGRSPIEFLEKAYEQYGPVVSFTMVGKTFTYLLGSDAAALMFNSKNEDLNAEDVYARLTTPVFGKGVAYDVPNPLFLEQKKMLKTGLNIAQFKQHVEIIEEETKDYFRRWGESGERNLFDALSELIILTASRCLHGCEIRSLLDERVAQLYADLDGGFTHAAWLLPGWLPLPSFRRRDRAHLEIKKIFYNVIKKRREDTEKHDDILQTLIDATYKDGRPLSDDEIAGMLIGLLLAGQHTSSTTSAWMGFFLARDRALQERCYSEQKSVCGEELPPLHYDQLKDLSLLDRCLKETLRLRPPIMTMMRMAKTPQKVGEYTIPPGHQVCVSPTVNHRLQDTWAERLDFDPDRYLHDNPAAGEKFAYIPFGAGRHRCIGENFAYVQIKTIWSTLLRMFDFELVDGHFPPVNYTTMIHTPHNPIIRYTRRNTQPQQ | 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 14alpha-methyl group (C-32) of sterols such as lanosterol (lanosta-8,24-dien-3beta-ol) and 24,25-dihydrolanosterol (DHL) in the form of formate, and converts the sterols to 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol and 4,4-dimethyl-8,14-cholestadien-3beta-ol, respectively, which are intermediates of cholesterol biosynthesis . Can also demethylate susbtrates not intrinsic to deuterostomes, such as eburicol (24-methylene-24,25-dihydrolanosterol), but at a lower rate than DHL (By similarity).
Catalytic Activity: a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57001
Sequence Length: 499
Pathway: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.14.154
|
Q6Q151 | MSVLIVTSLGDIVIDLHSDKCPLTCKNFLKLCKIKYYNGCLFHTVQKDFTAQTGDPTGTGAGGDSIYKFLYGEQARFYKDEIHLDLKHSKTGTVAMASGGENLNASQFYFTLRDDLDYLDGKHTVFGQIAEGFDTLTRINEAYVDPKNRPYKNIRIKHTHILDDPFDDPPQLAEMMPDASPEGKPKEEVKDDVRLEDDWVPMDEELGAQELEEVIREKAAHSSAVVLESIGDIPEAEVKPPDNVLFVCKLNPVTEDEDLHTIFSRFGTVVSADVIRDFKTGDSLCYAFIEFENKESCEQAYFKMDNALIDDRRIHVDFSQSVSKLWSQFRQKDSQKGKGNGCFKCGSTDHIAKDCVGGPSSKFIVKDQNRQHGGGEGYEMVFEGDVHETPKHNSHERERSEKIQRRSPHGNGEGKRQHRDERDDGRRQHDREDARELERKHRERKERESREDEDRRRRRRREESRDKESRRERDEDDHRSHRDYKERRRERDDRHGREARHERRDR | 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 and pre-mRNA processing. Involved in brassinostroid response.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 58829
Sequence Length: 506
Subcellular Location: Nucleus
EC: 5.2.1.8
|
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
EC: 5.2.1.8
|
Q9LY75 | MTKKKNPNVFLDVSIGGDPVQRIVIELFADVVPKTAENFRALCTGEAGVGKSTGKPLHFKGSSFHRVIKGFMAQGGDFSNGNGTGGESIYGGKFSDENFRLDHDGAGVLSMANCGPNTNGSQFFILFKRQPHLDGKHVVFGKVVEGMAVIKKMELVGTSDGKPTSPVKIIDCGETSQIRAHDAAEREKGKSKKSNKNFSPGDVSDREAKETRKKESNEKRIKRKRRYSSSDSYSSSSDSDSDSESEAYSSSSYESSSSSDGKHRKRKSTTRHKGRRGERKSKGRSGKKKARPDRKPSTNSSSDTESSSSSDDEKVGHKAIKSVKVDNADQHANLDDSVKSRSRSPIRRRNQNSRSKSPSRSPVRVLGNGNRSPSRSPVRDLGNGSRSPREKPTEETVGKSFRSPSPSGVPKRIRKGRGFTERYSFARKYHTPSPERSPPRHWPDRRNFQDRNRDRYPSNRSYSERSPRGRFRSPPRRRSPPRYNRRRRSTSRSPDGYRRRLRDGSRSQSPRHRSRSQSPRKRQPISQDLKSRLGPQRSPIRGGRTSPAESLSPSHSPSPPGKRGLVSYAD | 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 (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 63540
Sequence Length: 570
Subcellular Location: Nucleus
EC: 5.2.1.8
|
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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