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Database: UniProt
Entry: A0A0C2G4Q6_9BILA
LinkDB: A0A0C2G4Q6_9BILA
Original site: A0A0C2G4Q6_9BILA 
ID   A0A0C2G4Q6_9BILA        Unreviewed;       378 AA.
AC   A0A0C2G4Q6;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Unspecific monooxygenase {ECO:0000313|EMBL:KIH55955.1};
GN   ORFNames=ANCDUO_13874 {ECO:0000313|EMBL:KIH55955.1};
OS   Ancylostoma duodenale.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH55955.1, ECO:0000313|Proteomes:UP000054047};
RN   [1] {ECO:0000313|EMBL:KIH55955.1, ECO:0000313|Proteomes:UP000054047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zhejiang {ECO:0000313|EMBL:KIH55955.1,
RC   ECO:0000313|Proteomes:UP000054047};
RA   Mitreva M.;
RT   "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; KN736471; KIH55955.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2G4Q6; -.
DR   Proteomes; UP000054047; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; PTHR24284; CYTOCHROME P450 FAMILY; 1.
DR   PANTHER; PTHR24284:SF1; CYTOCHROME P450 FAMILY; 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   Membrane {ECO:0000256|SAM:Phobius};
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:UP000054047};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        46..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   378 AA;  43351 MW;  0026CF559D7A2AB7 CRC64;
     MGKNLMEEQV LLSAQEFLAH MASIKNKEEI DLRTPIQASI LTHIRLIIFL FARLICMYNF
     AVFVANIINK TLFGFSYEYA RSDRLMASVD VIVRIFDEMK GSKLTMLAQV FTFIHRLPVI
     GYYSKGRFER MIEEVKKNIT EDVERCLKTY DPDQEPECFV HAYYQKMQTN PNLNYDNLLN
     VCMDFFLAGM ETTTTTLRWG TLFMAKHPNV QDKIRQEIFS VLGADGRPST SLRNRMPYTN
     AAIQEIQRYA NIIPLNVIHR TVKDTSVESV PIPGDTLHVM AHSPVYKDAQ EFRPERFLMD
     DGITPNKEAV EQLCPFSVGK RQCAGEGLAK VELFIGLITL LQNYKIEPVR GRPLDLEPIF
     ASVLLPKQQP LRLTPVSV
//
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