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Database: UniProt
Entry: A0A164WZP3_9CRUS
LinkDB: A0A164WZP3_9CRUS
Original site: A0A164WZP3_9CRUS 
ID   A0A164WZP3_9CRUS        Unreviewed;       524 AA.
AC   A0A164WZP3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Putative Cytochrome P450 304a1 {ECO:0000313|EMBL:KZS13731.1};
GN   ORFNames=APZ42_021108 {ECO:0000313|EMBL:KZS13731.1};
OS   Daphnia magna.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS13731.1, ECO:0000313|Proteomes:UP000076858};
RN   [1] {ECO:0000313|EMBL:KZS13731.1, ECO:0000313|Proteomes:UP000076858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xinb3 {ECO:0000313|EMBL:KZS13731.1,
RC   ECO:0000313|Proteomes:UP000076858};
RC   TISSUE=Complete organism {ECO:0000313|EMBL:KZS13731.1};
RA   Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT   "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZS13731.1}.
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DR   EMBL; LRGB01001036; KZS13731.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A164WZP3; -.
DR   STRING; 35525.A0A164WZP3; -.
DR   Proteomes; UP000076858; 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   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; PTHR24300:SF376; CYTOCHROME P450 18A1; 1.
DR   PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1.
DR   Pfam; PF00067; p450; 2.
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:UP000076858}.
SQ   SEQUENCE   524 AA;  58872 MW;  753811C6C58DC848 CRC64;
     MAILLIVFCT LIYVLINVVV YKLWVRPPNF PPGPRGVPLL GYAPLLAKKG PLFKLILSLT
     KKYGPVTGFY VGPTQPFICV AGPKAVKEAL HNDDLDGRPC GAILMSRTFG KRLGLLFVDG
     DSWQEQRRFV LRHLREFCMG KTLIEKQMMN EINDLIADIT ATSNANPDNI VDFKGMFVVS
     VINILWTFLG GKRFRRDDEM FKKLSINVEQ FLHGGNALKI SFPIPAFILR SFPSLPRLLG
     ISTQLFVPLQ KFIKETIEQH LYTRFKGDPA RDFIDVYLDQ IRAELEENSS TTFSKKQLIA
     IIQDLFGAGS DTSSSSIGLL AMTLIKHDTN LISKPRTTRL GFGILYLIHY PEIQQKLWEE
     INQICGDSLP SLSHRSRLPY TEAVLMEVIR LSSVAPLAVP HCALRETHLQ GFTIPQGSII
     AISLNSLMKD ISIWGDPENF RPERHLDQEG NLIQNESYTP FGTGKRMCLG EALARNTVFL
     FMACLVKKFE FKPVPGEPLP TLEPIIGIVL GPKPFRAVAI PRDH
//
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