ID A0A0M5JAF5_DROBS Unreviewed; 496 AA.
AC A0A0M5JAF5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Cyp6a22 {ECO:0000313|EMBL:ALC41931.1};
GN ORFNames=Dbus_chr2Rg1510 {ECO:0000313|EMBL:ALC41931.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC41931.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC41931.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC41931.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004406}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Microsome membrane
CC {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004174}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; CP012524; ALC41931.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M5JAF5; -.
DR SMR; A0A0M5JAF5; -.
DR STRING; 30019.A0A0M5JAF5; -.
DR OMA; MHSCVAR; -.
DR OrthoDB; 1611592at2759; -.
DR Proteomes; UP000494163; Chromosome 2r sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd11056; CYP6-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24292:SF100; CYP6A16, ISOFORM B-RELATED; 1.
DR PANTHER; PTHR24292; CYTOCHROME P450; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000494163}.
SQ SEQUENCE 496 AA; 57766 MW; F1536BDD72393D6F CRC64;
MLDLLALLFI TMSLGLWYVR IKMTYWVRRR ICHEHPSFPM GNMQGLRTQR HIKDILTPMY
EAFKDCGDPF AGMYILLRPV VLVLDLELAK HVLIRDFPNF EDRGLYHNEQ ADPLTGHLFR
LDGAKWRALR QKMTPAFSSG RMKYMFPNIC AVGAELATVC GELAENSICN IVDVSELISR
YTSDVIGSCA FGLDCNGLRN PQAEFVLMGR RAFRQQRHGQ LVTALIENLP NWARRLHMRI
VHQDISDFYT RIVRDIVKQR EEQRIVKNDF MHLLIEMKRR GEITMQELTA QAFVFFIAGF
DTSASTTAFA LYELAKQPQL QLMLRAEMEL ALEQHDNEFN YDTMQELRYM ELVIAETLRK
YPILPQLTRT SAHYYIAKND HHFYIEPGQM VQIPIYAIQN DPDIYPEPHK FIPERFLAHQ
MSQRPTASWL PFGDGPRNCI GMRFGKMQTT IALFQLLRQF QFSVCARTES KIQFDKNNLL
LSPANGIYLK VEKLHK
//
