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Database: UniProt
Entry: Q0CNQ9_ASPTN
LinkDB: Q0CNQ9_ASPTN
Original site: Q0CNQ9_ASPTN 
ID   Q0CNQ9_ASPTN            Unreviewed;       531 AA.
AC   Q0CNQ9;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAU35122.1};
GN   ORFNames=ATEG_04675 {ECO:0000313|EMBL:EAU35122.1};
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:EAU35122.1, 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         ECO:0000256|PIRSR:PIRSR602403-1};
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; CH476599; EAU35122.1; -; Genomic_DNA.
DR   RefSeq; XP_001213853.1; XM_001213853.1.
DR   AlphaFoldDB; Q0CNQ9; -.
DR   STRING; 341663.Q0CNQ9; -.
DR   EnsemblFungi; EAU35122; EAU35122; ATEG_04675.
DR   GeneID; 4320473; -.
DR   VEuPathDB; FungiDB:ATEG_04675; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_001570_14_2_1; -.
DR   OMA; VCNIPED; -.
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; cd11059; CYP_fungal; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24305:SF164; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
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|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602403-1};
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};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..531
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004170371"
FT   BINDING         457
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602403-1"
SQ   SEQUENCE   531 AA;  59986 MW;  D85F38A88E25F67F CRC64;
     MIPILCLGAL LFGLVLFHVH KNLISSPLRH LPGPKSFAFT KWRLGYEEYR GMRTQCVNNL
     HKKYGEVVRV SPYEVSFSSL SALRKIYGSG SRFERDDFYQ MFDAYDRKVL FSYSSGIDHR
     ERKKILNSAY TKTAIMSPSN VDMIEEKVKD FLALVQRDSS ATGAVEIFSA LHYFAMDSVS
     HFVYGATSPG RTTAMKGTRQ HRGIIDDMLD PARRKLFWYA VFWPRLTEML YAQGAIVQKS
     LASFGLLPMK TPTYTGLRKH NFPVIQHLET QQLLGSDDSL ASRLLAGTIP SAKASAPMDT
     LDVAAECSDH FLAGIDTTSN TLMWVIYQLS RPENEGFQSK LRAEIQALDG PAGSGTFIYP
     EKAGTLPYLD AVIRETLRLH APSPGSEPRW STNDEVIDGY TIPRGTVVSI SPYTLHRQPQ
     VFANPLRFDP ERWLGPEDQV AERKRWFWAF SSGARMCIGV HLAMAEMTTL LANIYQNYWT
     HIPSEYLQVS PGMSARGDLF YDEHLSQVEE HKCWIQFVPI RALSTCLQGC V
//
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