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Database: UniProt
Entry: Q2HG83_CHAGB
LinkDB: Q2HG83_CHAGB
Original site: Q2HG83_CHAGB 
ID   Q2HG83_CHAGB            Unreviewed;       537 AA.
AC   Q2HG83;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Cytochrome P450 monooxygenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CHGG_00771 {ECO:0000313|EMBL:EAQ92536.1};
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ92536.1, ECO:0000313|Proteomes:UP000001056};
RN   [1] {ECO:0000313|Proteomes:UP000001056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC   {ECO:0000313|Proteomes:UP000001056};
RX   PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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|ARBA:ARBA00010617}.
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DR   EMBL; CH408029; EAQ92536.1; -; Genomic_DNA.
DR   RefSeq; XP_001219992.1; XM_001219991.1.
DR   AlphaFoldDB; Q2HG83; -.
DR   STRING; 306901.Q2HG83; -.
DR   GeneID; 4386859; -.
DR   VEuPathDB; FungiDB:CHGG_00771; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_001570_5_11_1; -.
DR   InParanoid; Q2HG83; -.
DR   OMA; DIDHMPY; -.
DR   OrthoDB; 2954533at2759; -.
DR   Proteomes; UP000001056; 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:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   CDD; cd11069; CYP_FUM15-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24305:SF227; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00022617};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001056};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        31..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   537 AA;  59418 MW;  9CF561C3A47DFCE8 CRC64;
     MAPYRSMLAA ALGGAYLLSS GRIPQWPAPG FLTAFAVLWG TQVLAWAAWV VILYPKVFSP
     LRGLPEPSGN SWFMGQWKAI VALPTGGPML NWIDSIPNKG LIRYLGPFNQ ERLFITSPKA
     LAEVLVTKNY EFIKPEALRF SIGRILGVGV LLAEGDEHKA QRRNLLPAFA FRHIKNIYPV
     FWTKSREGVE AMTEAILKEA AQRNDAEKNT AVIEAGNWAS RVTLDIIGVA GLGRDFDAIK
     NPDNRLTQAY ARIFRPSRQA RILQLLGMMI SPKLVALLPV KRNEDIGVSA NLIRAECAKI
     IQEKKQKLAQ KEPSDPDILS LMTFLAAGHE TTASAMTWAA YLLAKHTDVQ ARLRAEVREH
     LPPLSGDDST VSSVDIDRMP YLNAVCNEVL RYFGPVPVTL RMSACDTSIQ GQFVPKGTQI
     MLVPWAINRS EGLWGADARV FDPERWIAKS DADKRAASGG AESNYAFMTF LHGPRSCIGM
     SFAKAEFACL LATWVGRFKM ELHNKEEMDE SNIDIKGGVT SRPAKGMYVK TTVLEGW
//
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