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Database: UniProt
Entry: G9NDL1_HYPVG
LinkDB: G9NDL1_HYPVG
Original site: G9NDL1_HYPVG 
ID   G9NDL1_HYPVG            Unreviewed;       534 AA.
AC   G9NDL1;
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 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TRIVIDRAFT_74291 {ECO:0000313|EMBL:EHK15777.1};
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:EHK15777.1, ECO:0000313|Proteomes:UP000007115};
RN   [1] {ECO:0000313|EMBL:EHK15777.1, 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:EHK15777.1}.
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DR   EMBL; ABDF02000092; EHK15777.1; -; Genomic_DNA.
DR   RefSeq; XP_013949970.1; XM_014094495.1.
DR   AlphaFoldDB; G9NDL1; -.
DR   STRING; 413071.G9NDL1; -.
DR   EnsemblFungi; EHK15777; EHK15777; TRIVIDRAFT_74291.
DR   GeneID; 25797695; -.
DR   VEuPathDB; FungiDB:TRIVIDRAFT_74291; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_14_4_1; -.
DR   InParanoid; G9NDL1; -.
DR   OMA; ERWFNAT; -.
DR   OrthoDB; 3184603at2759; -.
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; 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:SF242; CYTOCHROME P450 MONOOXYGENASE ATNE-RELATED; 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..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   534 AA;  61272 MW;  2687398190CFB14A CRC64;
     MEQLKTRLTE PNLSTEQKLL VLIGLPVLYV VGLTVYRLYF HPLARFPGPK LAAATKWYEF
     YHDIIKGQGG QYFVRVSEMH DKYGPIVRVN PDEIHIRDPS FLDTLYATNP TKRDKYPPSA
     EMAGLTYGTH GTVDHDMHRR RRMANSRMFS KRAVASAQEL IHGHIKELTE AFERKVGSPE
     PVEMQTTFLA YTTDVIYHYM FNKDVGFQKD WNKAQSWRHS MEAVAQATPF CKQFPWLNGK
     LLMLPEWILK VIVAKLQPDI AGLLATHKLM GRIAAEYVAH RSTDKGKRES EEDEKNIKPL
     TIFHSIDRSA LPNEEKTALR LMQEGLTVLF AGGETGSRLL AHTIYHLLDN PEILEKVRKE
     ILEAAGDSKE LPDVKVLESL PWLAASVRES LRLRATTTSR LPLVSKKELI YKDWVIPAGT
     PVSMSHPDIL HNDEIYPEAL KFKPERWFNA TEQQNKMFIP FGKGTRMCIG VDFAYIELYM
     SLSTLITRFD LELYDTTWER DVAYTRDCFL GEASRDSPGI RVKVLADNKR WVSD
//
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