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Database: UniProt
Entry: G9NZ83_HYPAI
LinkDB: G9NZ83_HYPAI
Original site: G9NZ83_HYPAI 
ID   G9NZ83_HYPAI            Unreviewed;       504 AA.
AC   G9NZ83;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TRIATDRAFT_37212 {ECO:0000313|EMBL:EHK43797.1};
OS   Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS   atroviride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK43797.1, ECO:0000313|Proteomes:UP000005426};
RN   [1] {ECO:0000313|EMBL:EHK43797.1, ECO:0000313|Proteomes:UP000005426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {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:EHK43797.1}.
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DR   EMBL; ABDG02000025; EHK43797.1; -; Genomic_DNA.
DR   RefSeq; XP_013941905.1; XM_014086430.1.
DR   AlphaFoldDB; G9NZ83; -.
DR   STRING; 452589.G9NZ83; -.
DR   GeneID; 25784109; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_001570_27_0_1; -.
DR   OMA; GPFNHGN; -.
DR   OrthoDB; 4950799at2759; -.
DR   Proteomes; UP000005426; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd11063; CYP52; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR047146; Cyt_P450_E_CYP52_fungi.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24287; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   PANTHER; PTHR24287:SF17; P450, PUTATIVE (EUROFUNG)-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|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
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:UP000005426};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..504
FT                   /note="Cytochrome P450"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003524984"
SQ   SEQUENCE   504 AA;  57365 MW;  94D579577BC0CC74 CRC64;
     MSSLSDSRCL ILCLFSLVVT YTLRHISHQI HQRQVSQAKG CKDAQSKAPV KDRFIGLDFI
     YDCLFTKPIE KYLDYTYKTF QQLGSTYVCQ RWTWEATYTC DSRNIKHILA SGFAEFKLPR
     LRVNAMMGLL GSGIFTLNGH SWSHARAVLR PCFAKQNKED MVSMLETHFQ ALLRRIPLGG
     ETVDVQPLFF WLTMDFATHF LMGHSTHVLD RASSHAKEKQ FVDDYLTCST EIVRKMQLGP
     LQIFSFNFGA MRARSRVFKY IDDFISVSLD KEGENDDATN SGLNVLQGLA ALTTDRKQLR
     DQILHILVAS RDTTACLLSN LFFVLSRKPH VYERLRQEVL SVAGTEPATS NQLNSMEYLK
     WCVQESLRLH PVIPTNAREA SKDTILPYGG GKDGNSPLLI KKGSLVMYNT YAMHRDTEVF
     GPDAEEFVPE RWNGLRPGWG YLPFNGGPRI CIGQKFALLE THYLVSRMVQ TFETIKTNKD
     TEWVELYALA TTCKDGVNVS LKRA
//
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