ID A0A154PPN0_DUFNO Unreviewed; 511 AA.
AC A0A154PPN0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Cytochrome P450 4C1 {ECO:0000313|EMBL:KZC13846.1};
GN ORFNames=WN55_05750 {ECO:0000313|EMBL:KZC13846.1};
OS Dufourea novaeangliae (Sweat bee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Halictidae; Rophitinae; Dufourea.
OX NCBI_TaxID=178035 {ECO:0000313|EMBL:KZC13846.1, ECO:0000313|Proteomes:UP000076502};
RN [1] {ECO:0000313|EMBL:KZC13846.1, ECO:0000313|Proteomes:UP000076502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0120121106 {ECO:0000313|EMBL:KZC13846.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KZC13846.1};
RA Pan H., Kapheim K.;
RT "The genome of Dufourea novaeangliae.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in the metabolism of insect hormones and in
CC the breakdown of synthetic insecticides.
CC {ECO:0000256|ARBA:ARBA00003690}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; KQ435012; KZC13846.1; -; Genomic_DNA.
DR RefSeq; XP_015436624.1; XM_015581138.1.
DR RefSeq; XP_015436625.1; XM_015581139.1.
DR AlphaFoldDB; A0A154PPN0; -.
DR STRING; 178035.A0A154PPN0; -.
DR EnsemblMetazoa; XM_015581138.1; XP_015436624.1; LOC107191982.
DR EnsemblMetazoa; XM_015581139.1; XP_015436625.1; LOC107191982.
DR GeneID; 107191982; -.
DR OrthoDB; 1611592at2759; -.
DR Proteomes; UP000076502; Unassembled WGS sequence.
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 CDD; cd20628; CYP4; 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; PTHR24291:SF105; CYTOCHROME P450 4P1-RELATED; 1.
DR PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 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}; Iron {ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000076502}.
SQ SEQUENCE 511 AA; 59485 MW; 5D36F75280E6F7F1 CRC64;
MIIGILLFIV LGVLSHFFIL HYRRFGRMVN NIPGPQVMPI FGNLIAFQVS SAELWNMVRE
MNRTYYPIFR LWGFTEPFLN IRHPDDLEKI LGNPKSTQKS SIYNLLLPWF NTGLLTSAGR
KWQERRKILT PAFHFNVLQQ FADIFIEDSE RVSKSLKSEG GPVVKDLLPL ISEHTLNVIC
ETAMGTSLKD KGAFQTKYRN AVYHMGQLLV YRFLRPWVQN DFLFKFFPEG WRQSKLLGIL
HGFTKQIIKE RKEYHEQTNG AYLSHIADNQ GQKKDDMYFG IRKRRLAMLD LLIAAHRNNQ
IDDEGIREEV DTFMFRGHDT TAMSICFTIM LLAEHKDIQE RARYEVTAIM NENDGKMTMA
AMANLPYLER CIKESLRLYP SVPFISRSPE TDITLSNFLV PANSIVNIHI MDVHRDPKYW
PNPDAFDPDR FLPNNIQGRH PYCYVPFSAG PRNCIGQRFA MMELKTVLAY LLYNFHFEPV
DYLKDVCINT DLVIRPAHSL RTKFIPIENP C
//
