ID G9MUZ1_HYPVG Unreviewed; 595 AA.
AC G9MUZ1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Cytochrome P450 monooxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=TRIVIDRAFT_53058 {ECO:0000313|EMBL:EHK21715.1};
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:EHK21715.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK21715.1, 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 ECO:0000256|PIRSR:PIRSR602403-1};
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:EHK21715.1}.
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DR EMBL; ABDF02000065; EHK21715.1; -; Genomic_DNA.
DR RefSeq; XP_013955909.1; XM_014100434.1.
DR AlphaFoldDB; G9MUZ1; -.
DR STRING; 413071.G9MUZ1; -.
DR EnsemblFungi; EHK21715; EHK21715; TRIVIDRAFT_53058.
DR GeneID; 25795271; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_53058; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_025001_1_0_1; -.
DR InParanoid; G9MUZ1; -.
DR OMA; RWGMKYL; -.
DR OrthoDB; 2900138at2759; -.
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 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:SF232; CYTOCHROME P450 MONOOXYGENASE APDB-RELATED; 1.
DR Pfam; PF00067; p450; 2.
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|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602403-1,
KW 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 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 541
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 595 AA; 67895 MW; 1C081890B7D26F60 CRC64;
MAEANENELF VPWSISTSVP ITLAVIWVLL YYLYIRHCPK PIPGNIPYNK SSANRILGDT
PEIKQYQKTG DFRRFFRDHN AKLNTPISQV FMFPYSKPFI LITDFREGYD ILSRRHREFD
RSKRNADIFG TIVPNFHLAM QTQDPRFKGN KELVRDLMTP TFLNEATVHI YDIATVLVDM
WAYKSTQAAG RPFPAYEDLH CVALDIILAA AFGIPLEQSA THKQFEFLQL QPPIIRSSKS
KDDPVIYSQI PLSESLMALI KVTGTVVVGY KSPFPRLHHW ILKNTIWRKD FAQKEAFITD
QINKSVERLT SENTQESRMR CAMDMMLLRE IGYAKKEGRK PNINAPRMRD ELFGYVATGH
DTSSTTLSWI TKFLTDNESS QAKLRHQLHS AFAEAHAEKR QPTVMEIIEK PAPFLDAFLE
ECLRLAKTLP TILREALTDV TILGHSVPKG TGIIIYNHGP GGQLESGFDI PESARSDTSQ
DSKHRVGEWN TDDISCFRPE RWLQRMTGVQ YDGERDAEFE GANYNANSGP FLTFGGGPRG
CFGKKLAYME LRIVLAMLVW NFEFQPCPAE LSSYEGIDMA TVVPKQCYVR LKQLL
//