ID A0A163CPM2_DIDRA Unreviewed; 538 AA.
AC A0A163CPM2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Heme binding {ECO:0000313|EMBL:KZM22613.1};
GN ORFNames=EKO05_0009710 {ECO:0000313|EMBL:UPX19449.1}, EKO05_008599
GN {ECO:0000313|EMBL:KAF9704818.1}, ST47_g6177
GN {ECO:0000313|EMBL:KZM22613.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM22613.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM22613.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM22613.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
RN [2] {ECO:0000313|EMBL:KAF9704818.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9704818.1};
RA Syme R.A., Farfan-Caceres L., Lichtenzveig J.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF9704818.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9704818.1};
RX PubMed=32345704; DOI=10.1534/g3.120.401265;
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RT "Reference Genome Assembly for Australian Ascochyta rabiei Isolate
RT ArME14.";
RL G3 (Bethesda) 10:2131-2140(2020).
RN [4] {ECO:0000313|EMBL:KAF9704818.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9704818.1};
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:UPX19449.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:UPX19449.1};
RA Mobegi F.M., Debler J.W.D., Lee R.C.L.;
RL Submitted (MAR-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR602402-1};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; RYYQ01000017; KAF9704818.1; -; Genomic_DNA.
DR EMBL; JYNV01000212; KZM22613.1; -; Genomic_DNA.
DR EMBL; CP095304; UPX19449.1; -; Genomic_DNA.
DR STRING; 5454.A0A163CPM2; -.
DR OrthoDB; 4950799at2759; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR Proteomes; UP000617380; Chromosome 17.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of 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; IPR002974; Cyt_P450_E_CYP52_ascomycetes.
DR InterPro; IPR047146; Cyt_P450_E_CYP52_fungi.
DR InterPro; IPR002402; Cyt_P450_E_grp-II.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24287; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR24287:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00464; EP450II.
DR PRINTS; PR01239; EP450IICYP52.
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:PIRSR602402-1, ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|PIRSR:PIRSR602402-1, ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602402-1,
KW ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837}.
FT BINDING 473
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:PIRSR602402-1"
SQ SEQUENCE 538 AA; 61034 MW; 6D5560EE42AE960A CRC64;
MHNSILLVLW AGVSFVLYKL IAVVLTERHH RNAAARLGCE PAHQSKIFDF QGIRNVSRMI
AADKQSRFPD YLKARVDTAC AEEGKTITTF YQKVLGTRSA FTVDPKNIQA VLATQFKDFG
LGERRNGNFS PLLGQGIFST DGAEWQHARS LLRPQFAREQ VSDLDLEEEH IKNLMRVLPA
GKDGWTEITD IQPLFFRLTI DSATEFLFGE SVDSQLAVLP NYTSSRPPMA VNEKDFANSF
DQSQAAVAMA SRMGELWWIA FDKTFRQHRD ICWQFIDHYV HKALSQEKIS EKRTVNGKQK
YVFLDALAES TRDPVELRSH MISILLAGRD TTASLLSFVF MLFTKHPEVY QKLRTVVLEN
FGTYNNPRNI TFATLKSCNY IQWVLNETLR LYPVVPLDGR RALKDTTIPT GGGPNGTSPV
YIRKGQQVDY SVYVMHRRKD LWGQDADEFR PDRWDGRKSG WEYLPFNGGP RICIGQQFAL
TEAGYVLVRL AQRFEEIVGV GNSWESTEDG GQGYVKTKVS LTGCPADGVK VRMKEAME
//
