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Database: UniProt
Entry: A0A0B2VEB1_TOXCA
LinkDB: A0A0B2VEB1_TOXCA
Original site: A0A0B2VEB1_TOXCA 
ID   A0A0B2VEB1_TOXCA        Unreviewed;       438 AA.
AC   A0A0B2VEB1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Cytochrome P450 2H1 {ECO:0000313|EMBL:KHN79335.1};
GN   Name=CYP2H1 {ECO:0000313|EMBL:KHN79335.1};
GN   ORFNames=Tcan_04467 {ECO:0000313|EMBL:KHN79335.1};
OS   Toxocara canis (Canine roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX   NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN79335.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN79335.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN79335.1};
RA   Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA   von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA   Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA   Gasser R.B.;
RT   "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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:KHN79335.1}.
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DR   EMBL; JPKZ01001927; KHN79335.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2VEB1; -.
DR   STRING; 6265.A0A0B2VEB1; -.
DR   OMA; RWHIAYM; -.
DR   Proteomes; UP000031036; 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; 2.
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; 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   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:UP000031036};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   438 AA;  50008 MW;  A4A4B929FBF47E33 CRC64;
     MFWVILIIVV FIVLYLAKYY AYIKNYPKGP MPIPLLGNLH QLKTHNTHLH FDELAKAYGD
     VFTVFMPRPV VIITKFQNMK KALIRRGDDF VGRSGLFPDN IFQSFPNGGI TFASGDSWRE
     QRRISLRILK DFGMGSGITE DQTNFGTEDQ SKKYRLRCGS ADGSVVSSSI KESQQLKDDA
     DKLKVFIREQ VDKQKAQFDP CKEPQTFVHA LLLEMHKGNR FLCYEQLVDI TMDFWLAAME
     TTSITLRWAI LFLIANPQVQ HRMRAEIIDI VGKDRRICMA DKLSMPYCTV AVVEIQRRAN
     VLPQNVMHRT VKQTMVSGHC IPADTLVLPQ ISSVLSDSSL FENPDEFKPE RFLQDDGKTP
     HKELLQYVVP FSMGKRQCAG EPLASVKLFL ILTTLLQNFI LEKPLDGALP DLEPDFAFFA
     FPKQYKLRIV PISGCEES
//
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