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Database: UniProt
Entry: G9MUZ1_HYPVG
LinkDB: G9MUZ1_HYPVG
Original site: G9MUZ1_HYPVG 
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
//
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