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Database: UniProt
Entry: A0A010ZTW8_9ACTN
LinkDB: A0A010ZTW8_9ACTN
Original site: A0A010ZTW8_9ACTN 
ID   A0A010ZTW8_9ACTN        Unreviewed;       398 AA.
AC   A0A010ZTW8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:EXG82144.1};
GN   ORFNames=CryarDRAFT_3286 {ECO:0000313|EMBL:EXG82144.1};
OS   Cryptosporangium arvum DSM 44712.
OC   Bacteria; Actinomycetota; Actinomycetes; Cryptosporangiales;
OC   Cryptosporangiaceae; Cryptosporangium.
OX   NCBI_TaxID=927661 {ECO:0000313|EMBL:EXG82144.1, ECO:0000313|Proteomes:UP000021053};
RN   [1] {ECO:0000313|EMBL:EXG82144.1, ECO:0000313|Proteomes:UP000021053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44712 {ECO:0000313|EMBL:EXG82144.1,
RC   ECO:0000313|Proteomes:UP000021053};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (JUL-2013) 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:EXG82144.1}.
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DR   EMBL; JFBT01000001; EXG82144.1; -; Genomic_DNA.
DR   RefSeq; WP_035851741.1; NZ_KK073874.1.
DR   AlphaFoldDB; A0A010ZTW8; -.
DR   PATRIC; fig|927661.3.peg.3244; -.
DR   HOGENOM; CLU_033716_1_1_11; -.
DR   OrthoDB; 3664945at2; -.
DR   Proteomes; UP000021053; 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; cd11030; CYP105-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002397; Cyt_P450_B.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR46696; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   PANTHER; PTHR46696:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
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|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000021053}.
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          63..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   398 AA;  43828 MW;  8241892E4310360A CRC64;
     MTETETETAL VDFPLRQPGQ SFPPESYAGY RQQDRLVRSK LLNGAIVWLV SRHEDVRAVL
     SDPRISSNPT HQGFPNAQRT GGVPSTDEVP GWFVALDPPD HTRFRKALIP EFTVRRVRDM
     TAAVQGIVDD RIDAMLAAGD TADLVSDLAL PVPSLVISSL LGVPRVDRDF FEAKTRVLVT
     MSSTDAQREK AAGDLLRYLT RLIAIKRRRP GDDLLSRMLA NGDMTPEEMS GVGMLLLIAG
     HETTANNISL GVLTLLQNAE WIGDPRVVEE MLRFCSVADL VALRVAVRDV EIGGQLIKAG
     EGIVPLVASA NHDAAVFAHP ERFDPGRPAH GHVAFGYGVH QCLGQNLVRL EMDVLCRTLF
     TRIPTLELAV PVEDLPYKYD GVLYGLHALP VRWQRDTP
//
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