ID R1H368_BOTPV Unreviewed; 458 AA.
AC R1H368;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Putative cytochrome p450 protein {ECO:0000313|EMBL:EOD52869.1};
GN ORFNames=UCRNP2_330 {ECO:0000313|EMBL:EOD52869.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD52869.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
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}.
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DR EMBL; KB915680; EOD52869.1; -; Genomic_DNA.
DR RefSeq; XP_007579658.1; XM_007579596.1.
DR AlphaFoldDB; R1H368; -.
DR KEGG; npa:UCRNP2_330; -.
DR eggNOG; KOG0159; Eukaryota.
DR HOGENOM; CLU_022195_0_1_1; -.
DR OMA; CKDEWVE; -.
DR OrthoDB; 1351063at2759; -.
DR Proteomes; UP000013521; Unassembled WGS sequence.
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; cd11041; CYP503A1-like; 1.
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; PTHR46206; CYTOCHROME P450; 1.
DR PANTHER; PTHR46206:SF9; CYTOCHROME P450 MONOOXYGENASE AN1598-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
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|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000013521}.
FT BINDING 395
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 458 AA; 52283 MW; 056DD9A790FD1B76 CRC64;
MTGARAMVRE GYKKFKSSMF KVRRNDKDIL VISNKYIDEL RNLPDSKLSA IGAQVRNLLG
RYSTTPILLE SDLHTRVLQT KLTPNLPSLI PILKDELDHA LPKEIPECKD EWVEVQIYEI
LCQIVARLTA RVFLGEKGCE SEEWLAKSIE YTENIFKTVM VLRVFPTYIR PFIAPFLPPY
WKMQSDLVTA KKIISPMVRE RRQQEALLGA EYAKPHDLLQ WMMDASDDDD GQPDKLAHRQ
LLLSLASIHT TTMSAAHALY DLCAYPECFE PLRDEAIRVL SEDEGWKKTT LTKMRNLDSF
LKESQRINPP IFMTFNRVVR SPITLSDGTQ LPVGTHLTVA SDATSHDPDI IPSPDRFDPF
RWARLRQSDP SSAHKHQFAT TDVNSLHFGH GRHACPGRFF AAAEIKMLLA QLLLDYDFKY
PQGQGRPINL SADDWLFPDP NARLLIRRRS GEGQQGAV
//
