ID A0A4Z1PIL2_9PEZI Unreviewed; 803 AA.
AC A0A4Z1PIL2;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU363051};
DE EC=1.11.1.- {ECO:0000256|RuleBase:RU363051};
GN ORFNames=E6O75_ATG02234 {ECO:0000313|EMBL:TID23060.1};
OS Venturia nashicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Venturiaceae; Venturia.
OX NCBI_TaxID=86259 {ECO:0000313|EMBL:TID23060.1, ECO:0000313|Proteomes:UP000298493};
RN [1] {ECO:0000313|EMBL:TID23060.1, ECO:0000313|Proteomes:UP000298493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRI2 {ECO:0000313|EMBL:TID23060.1,
RC ECO:0000313|Proteomes:UP000298493};
RA Prokchorchik M., Won K., Lee Y., Choi E.D., Segonzac C., Sohn K.H.;
RT "High contiguity whole genome sequence and gene annotation resource for two
RT Venturia nashicola isolates.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR601621-2,
CC ECO:0000256|RuleBase:RU363051};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR601621-
CC 2, ECO:0000256|RuleBase:RU363051};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|PIRSR:PIRSR601621-2};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000256|PIRSR:PIRSR601621-2};
CC -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
CC {ECO:0000256|ARBA:ARBA00006089, ECO:0000256|RuleBase:RU363051}.
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:TID23060.1}.
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DR EMBL; SNSC02000007; TID23060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Z1PIL2; -.
DR STRING; 86259.A0A4Z1PIL2; -.
DR Proteomes; UP000298493; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR Gene3D; 1.10.520.10; -; 1.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 1.
DR InterPro; IPR044831; Ccp1-like.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR001621; Ligninase.
DR InterPro; IPR019794; Peroxidases_AS.
DR PANTHER; PTHR31356:SF8; L-ASCORBATE PEROXIDASE 6-RELATED; 1.
DR PANTHER; PTHR31356; THYLAKOID LUMENAL 29 KDA PROTEIN, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00462; LIGNINASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR601621-2, ECO:0000256|RuleBase:RU363051};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601621-4};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR601621-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR601621-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601621-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU363051};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU363051};
KW Reference proteome {ECO:0000313|Proteomes:UP000298493};
KW Signal {ECO:0000256|RuleBase:RU363051}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU363051"
FT CHAIN 19..803
FT /note="Peroxidase"
FT /evidence="ECO:0000256|RuleBase:RU363051"
FT /id="PRO_5021501743"
FT DOMAIN 203..278
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 426..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-1"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 277
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT BINDING 302
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT SITE 148
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-3"
FT DISULFID 118..373
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
FT DISULFID 139..220
FT /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
SQ SEQUENCE 803 AA; 85185 MW; 26C5A2EDE3E1E717 CRC64;
MKSNTLLLAS CLFSDVIACG FAKAATGSKA AAWKSKREEL LATVNRTAEA IEPGESSELL
GDLLTQGPRS NVGQLIADIL TGRTSDERLA LDNGPQWMPE VRLDQTVESL CNGNKDQCCP
WRIVAEEMFA TFSTKSGRCN SFARGAIRLG FHDAGAWRKG LDYGGADGGI LLTDELNRVE
NRGLEEIGAR TREWYTKYNR YGIGMADLIQ FGANVATVTC PLGPRVRTFI GRRDAQRGVQ
ASPNLLPDAN DSAEKLIALF EAKTISPKGL VALVGAHSTS QQRFFDTSRA LDPQDSTPGV
WDVLFYGQTT DARPNRIVKF PSDINLSRHP RTKPEWDAFT GPTGQQHWND DYAREYVRLS
LLGVNNINDL TDCTKVLPAA ITDNFRAEDQ YNVDQWANGG FQGFGGEFGA LVDLGEILTD
TTLQQNGIDP SYISSGWGTV PKPDTGGYRS SIKPGSGIPR PNPETSRSPP PRAQSNGGPN
GAGKDRPADF GGRPPKYSNG GGRPTGPPGA FQPYDLPNGN KPSNGTPGAF QPLDNPNGGK
PKEPAKEGDR SNPFGNNNPF NNGGKPKDPT KDPTKDPAKD PAKDPAKDPT KEPAKDPAKD
PAKEPAKEPA KEPAKEPAKE GDRSNPFGNN NPFNNGGKPK DPTNPTKDPA KEPAKEGDRS
NPFGNNNPFN NGGKPKEPAK EGDRSNPFGN NNPFNSGGKP KEPAKEGDRS NPFGNNNPFN
NGGKPKETPK PSGGNTNSNP FGVKPDAKGS NPPNNNSGRP GIQPTNNGGR LGNGGSRNGG
NNGGNQGGSG GGGGGGRGGK KSP
//
