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Database: UniProt
Entry: G9MU22_HYPVG
LinkDB: G9MU22_HYPVG
Original site: G9MU22_HYPVG 
ID   G9MU22_HYPVG            Unreviewed;       509 AA.
AC   G9MU22;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Cytochrome P450 monooxygenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TRIVIDRAFT_222494 {ECO:0000313|EMBL:EHK22060.1};
OS   Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS   (Trichoderma virens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK22060.1, ECO:0000313|Proteomes:UP000007115};
RN   [1] {ECO:0000313|EMBL:EHK22060.1, ECO:0000313|Proteomes:UP000007115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX   PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA   Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA   Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA   Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA   Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA   McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA   Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA   Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA   Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA   Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA   Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA   Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA   Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA   Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT   "Comparative genome sequence analysis underscores mycoparasitism as the
RT   ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(2011).
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, 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:EHK22060.1}.
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DR   EMBL; ABDF02000037; EHK22060.1; -; Genomic_DNA.
DR   RefSeq; XP_013956253.1; XM_014100778.1.
DR   AlphaFoldDB; G9MU22; -.
DR   STRING; 413071.G9MU22; -.
DR   EnsemblFungi; EHK22060; EHK22060; TRIVIDRAFT_222494.
DR   GeneID; 25791678; -.
DR   VEuPathDB; FungiDB:TRIVIDRAFT_222494; -.
DR   eggNOG; KOG0158; Eukaryota.
DR   HOGENOM; CLU_001570_14_11_1; -.
DR   InParanoid; G9MU22; -.
DR   OMA; EQEPTFK; -.
DR   OrthoDB; 928042at2759; -.
DR   Proteomes; UP000007115; 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   CDD; cd11058; CYP60B-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:SF230; CYTOCHROME P450 MONOOXYGENASE STHF; 1.
DR   Pfam; PF00067; p450; 1.
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|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU000461};
KW   Iron {ECO:0000256|RuleBase:RU000461}; Membrane {ECO:0000256|SAM:Phobius};
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:UP000007115};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   509 AA;  57852 MW;  B9FEBC4F7A6136D4 CRC64;
     MDVLIGNGGA KVVIPVKLSL ALPLAVVAFG FGYFFWRCIY NLYLHPLHRF PGPKLSALSY
     YPYYRLLVSG VGYLTVMDLH MKYGPVVRIS PNSLSFSHPD AMNDIRGHRK AGQPEHPKEP
     MGREFHLKDI IGAERADHAR YRRSLANGFS YQAMLDQEPI IQEYIDQLME SIEKHSANGT
     QQIDMVRWFN YTTFDIIGDL SFGEPFGCLQ SSTYDPWVQL IFSTVKSLVH IAALKYLRII
     PRRILNYLMP YLMPKGLSTK HAENQRLSAM KVKKRLEANS TRPDFIASMT KSRNGESLTF
     EELTANASIL IIAGSETTAT VLSSAAYYLG LFPEAQAKLA HEVRTTFNSA QDITTTSVQH
     LKYMLAVINE VMRVHPAVVT GLPRVISEGG ATIAGEYVPE DTCVEVWQWP LFRNPKYWTQ
     PDDFIPERWL GDPKFANDRR ECFQPFSTGP RNCVGMNLAY SEMRLILARV ILKYDIKLAE
     GTEGWDSRSK VYLLWEKGPV NVYMIPRKI
//
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