ID Q0CZZ6_ASPTN Unreviewed; 482 AA.
AC Q0CZZ6;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=ATEG_00738 {ECO:0000313|EMBL:EAU39384.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU39384.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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|RuleBase:RU000461}.
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DR EMBL; CH476594; EAU39384.1; -; Genomic_DNA.
DR RefSeq; XP_001210824.1; XM_001210824.1.
DR AlphaFoldDB; Q0CZZ6; -.
DR STRING; 341663.Q0CZZ6; -.
DR EnsemblFungi; EAU39384; EAU39384; ATEG_00738.
DR GeneID; 4355493; -.
DR VEuPathDB; FungiDB:ATEG_00738; -.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_001570_14_2_1; -.
DR OMA; SWANPIR; -.
DR OrthoDB; 509202at2759; -.
DR Proteomes; UP000007963; 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; cd11062; CYP58-like; 1.
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; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF156; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000007963}.
SQ SEQUENCE 482 AA; 53804 MW; A617477D4EFAD115 CRC64;
MYKSLLERGP VVLGGFLLVL IAFCVCKSIY RVYFHPLSHV PGPKLAAATS LWLAYHTFIG
DECTTVSELH KRYGPVLRVA PNDIDIADGE AIEPIYLAHG GFPKTRAYSK FDIDGHTTIF
SSLTLSERAT RAKAVAPLFS TASIRQSEQA LGVVFDDFVA RTRREAQTGR PVNVLNATRC
MAIDAVSMYL FQKRYGAIDE GSKTMSASPF VDAYVGVGAF FNLAHGKISD ALMRFIDRWN
TTQATETAFQ LMDAYTSQLV KTAVPKSGSY QSRLLEREIS EELSQIELKD VCFAGTDSTG
MNMATIMWNL AKHPDVYARL RQELQDSAAR DEDLTSCAYL RGVVREALRL SWANPTRLPR
AVPSGGWRFK DYFFPAGTSV GVAGFQLHQD EEVFPEAQRF RPERWLQPTD AMLNNFFAFG
KGTRACIAQN LGTAELVWAT IKVVQADLLR GARIVDKEIQ ILEWFNSRVK GEKILIQFDV
QS
//
