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Database: UniProt
Entry: A0A1J1IG58_9DIPT
LinkDB: A0A1J1IG58_9DIPT
Original site: A0A1J1IG58_9DIPT 
ID   A0A1J1IG58_9DIPT        Unreviewed;       492 AA.
AC   A0A1J1IG58;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=CLUMA_CG012623, isoform A {ECO:0000313|EMBL:CRK99229.1};
GN   Name=similar to Cytochrome P450 4C1 {ECO:0000313|EMBL:CRK99229.1};
GN   ORFNames=CLUMA_CG012623 {ECO:0000313|EMBL:CRK99229.1};
OS   Clunio marinus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC   Clunio.
OX   NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK99229.1, ECO:0000313|Proteomes:UP000183832};
RN   [1] {ECO:0000313|EMBL:CRK99229.1, ECO:0000313|Proteomes:UP000183832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-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; CVRI01000050; CRK99229.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J1IG58; -.
DR   STRING; 568069.A0A1J1IG58; -.
DR   OrthoDB; 1611592at2759; -.
DR   Proteomes; UP000183832; Unassembled WGS 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   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:SF189; CYTOCHROME P450 4V2; 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:UP000183832}.
SQ   SEQUENCE   492 AA;  56876 MW;  D4FC6F3A7712F321 CRC64;
     MYKVILLGIF SLTLFCYLIY RSKHRTFFQH ASKIPTVPAG FIRRIKSLIG ANQEELFQVL
     KETICPGPSP RKAWLGPLMF VFVDDPDQVN QYLNSPYGID KPKIYSVLGL DKGLFVSNGA
     LWKAHRKLLD PSFNAKVLSS FNPIFNEKSK LLIKKLEDEL DAEEFNIFSY FISFGLDNIL
     RTSTGVDKKI MEEKNNKYVN DCTIGVNIFA SKIVKFWLQL KPIMRMSNLY ELEQKHILNG
     MFKMAHDLIQ EKEENIRNNN DVKYKSEKPQ IFIDQLFKKR NEFSFDEMAD EINTIILAGF
     ETIATLSSTV VLLAALYPDV QEKIFEELKT VFNSVDEEVT DRKLQELSYL DQVVNESARY
     WTTLPYIARS LSTDIEIGSK IVPSGSIICV PIILLHSNKE IWGEDADKFI PERFSSERLT
     DTQRKAFMPF GRGPRICIGN KYAIKSIKIA LSHFFRNYKS STNVKEENLT FEYTVFIKLV
     QGYMVKISKR EF
//
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