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Database: UniProt
Entry: A0A163GL72_DIDRA
LinkDB: A0A163GL72_DIDRA
Original site: A0A163GL72_DIDRA 
ID   A0A163GL72_DIDRA        Unreviewed;       510 AA.
AC   A0A163GL72;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Heme binding {ECO:0000313|EMBL:KZM24905.1};
GN   ORFNames=EKO05_0002667 {ECO:0000313|EMBL:UPX12096.1}, EKO05_001977
GN   {ECO:0000313|EMBL:KAF9710988.1}, ST47_g3918
GN   {ECO:0000313|EMBL:KZM24905.1};
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:KZM24905.1, ECO:0000313|Proteomes:UP000076837};
RN   [1] {ECO:0000313|EMBL:KZM24905.1, ECO:0000313|Proteomes:UP000076837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ArDII {ECO:0000313|EMBL:KZM24905.1,
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:KAF9710988.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:KAF9710988.1};
RA   Syme R.A., Farfan-Caceres L., Lichtenzveig J.;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAF9710988.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:KAF9710988.1};
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:KAF9710988.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:KAF9710988.1};
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:UPX12096.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:UPX12096.1};
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: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; RYYQ01000004; KAF9710988.1; -; Genomic_DNA.
DR   EMBL; JYNV01000148; KZM24905.1; -; Genomic_DNA.
DR   EMBL; CP095291; UPX12096.1; -; Genomic_DNA.
DR   STRING; 5454.A0A163GL72; -.
DR   OrthoDB; 408598at2759; -.
DR   Proteomes; UP000076837; Unassembled WGS sequence.
DR   Proteomes; UP000617380; Chromosome 4.
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; cd11060; CYP57A1-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; PTHR24305; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24305:SF215; CYTOCHROME P450 MONOOXYGENASE CICH-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
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|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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076837}.
FT   BINDING         454
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   510 AA;  57327 MW;  E1AD28F228240937 CRC64;
     MALASLLVKA LSLGAIALVV QYIVTYLNSP LKKIPGPFLA KFSNIWRFYN HYSQTHIETQ
     KELHERYGDV VRLGPNTVSV TDASLLKTIY STRGTFLKSD YYSVNDALQN GHLIQNLFST
     RSNEFHAKGI KPVQKLYSLQ SALQLEPLMD EDLRVFGAEL ERRFMTGDHR GRTCDIADWI
     SYFAWDFLGD MTWSKRMGFM EQGKDVGGML QTAENVMRYF SVIGQIPALD KLLGKNPQLT
     KLYKFDDFAV AAGFAVERFM ERMQNLSEFK DKKDFVNGFL AAKKEHPDLV TDNEVIGYMI
     LNILGGADTL AICTKATFYH LLKSPTAKAK LAHELRSAHL PSPAPYEALS KLPYLDACIK
     EGLRIHPVIG HMLERVVPAT GLVLPSGTIL PPGTIVGTNP WLMHTNKAIF GDDAASYRPE
     RWLQSADESS GAYAARLKKM QDADMSFGGG NRVCLGRPLA LVELYKVVGF VFGTYDIELE
     DPTKEWDLHK QWFVWPHDVK VKMSLVGRAQ
//
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