ID A0A2T4BS54_TRILO Unreviewed; 506 AA.
AC A0A2T4BS54;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:PTB72147.1};
GN ORFNames=M440DRAFT_1385341 {ECO:0000313|EMBL:PTB72147.1};
OS Trichoderma longibrachiatum ATCC 18648.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983965 {ECO:0000313|EMBL:PTB72147.1, ECO:0000313|Proteomes:UP000240760};
RN [1] {ECO:0000313|EMBL:PTB72147.1, ECO:0000313|Proteomes:UP000240760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18648 {ECO:0000313|EMBL:PTB72147.1,
RC ECO:0000313|Proteomes:UP000240760};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KZ679143; PTB72147.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4BS54; -.
DR STRING; 983965.A0A2T4BS54; -.
DR Proteomes; UP000240760; 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:UP000240760};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 506 AA; 57319 MW; 4F976DBA93641BA1 CRC64;
MGVLFGSDAL GVDPPVKLSV ALPLAVVALG FGYLVWSCIY NVFFHPLRKF PGPKLAAISR
IPYSRMLLNG VGHREVLDLH IKYGPIVRVA PDFLSFSHPD AMNDIRGHRK AGQPEHRKDP
LRQEMNVHNI IGADRHNHTR FRRALANGFS HQAMLDQEPI ISEYIEQLME AIEKQAEGGS
KPVDMVRWFN YTTFDVIGDL AFGESFGCLQ SSNYDPWIQL LFDSVKTLVW MGTLKHFEMI
PRWLIKYIMP KGLERKYAEN QRLSTMKVQK RLDTGSNRPD FITSMTAKRN GESLTFEELA
ANASILIIAG SETTATALSA VAYFLSLNLE VQAKLAQEVR STFNSPQEIT ITSVQHLTYM
LAVIDEAMRL YPPVVAGLTR LISEGGAVVA GEYVPEGTYV EVWQWPLFHN PSYWTKPEEF
IPERWLGDPM FADDKREAFQ PFSTGPRNCV GKNLAYSEMR LILARVIFQY DLKAAEGTEG
WDYRSKAFTL WSKGPVNVYL TPRKME
//
