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Database: UniProt
Entry: A0A4Y7QF19_9AGAM
LinkDB: A0A4Y7QF19_9AGAM
Original site: A0A4Y7QF19_9AGAM 
ID   A0A4Y7QF19_9AGAM        Unreviewed;       362 AA.
AC   A0A4Y7QF19;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU363051};
DE            EC=1.11.1.- {ECO:0000256|RuleBase:RU363051};
GN   ORFNames=BD410DRAFT_895652 {ECO:0000313|EMBL:TDL26244.1};
OS   Rickenella mellea.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Hymenochaetales; Rickenellaceae; Rickenella.
OX   NCBI_TaxID=50990 {ECO:0000313|EMBL:TDL26244.1, ECO:0000313|Proteomes:UP000294933};
RN   [1] {ECO:0000313|EMBL:TDL26244.1, ECO:0000313|Proteomes:UP000294933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZMC22713 {ECO:0000313|EMBL:TDL26244.1,
RC   ECO:0000313|Proteomes:UP000294933};
RG   DOE Joint Genome Institute;
RA   Krizsan K., Almasi E., Merenyi Z., Sahu N., Viragh M., Koszo T., Mondo S.,
RA   Kiss B., Balint B., Kues U., Barry K., Hegedus J.C., Henrissat B.,
RA   Johnson J., Lipzen A., Ohm R., Nagy I., Pangilinan J., Yan J., Xiong Y.,
RA   Grigoriev I.V., Hibbett D.S., Nagy L.G.;
RT   "A transcriptomic atlas of mushroom development highlights an independent
RT   origin of complex multicellularity.";
RL   Submitted (JUN-2018) 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}.
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DR   EMBL; ML170162; TDL26244.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Y7QF19; -.
DR   STRING; 50990.A0A4Y7QF19; -.
DR   VEuPathDB; FungiDB:BD410DRAFT_895652; -.
DR   Proteomes; UP000294933; 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   CDD; cd00692; ligninase; 1.
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; IPR024589; Ligninase_C.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
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   Pfam; PF11895; Peroxidase_ext; 1.
DR   PRINTS; PR00462; LIGNINASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS00435; PEROXIDASE_1; 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|PIRSR:PIRSR601621-2};
KW   Iron {ECO:0000256|PIRSR:PIRSR601621-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601621-2,
KW   ECO:0000256|RuleBase:RU363051};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU363051};
KW   Peroxidase {ECO:0000256|RuleBase:RU363051, ECO:0000313|EMBL:TDL26244.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000294933};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU363051}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|RuleBase:RU363051"
FT   CHAIN           23..362
FT                   /note="Peroxidase"
FT                   /evidence="ECO:0000256|RuleBase:RU363051"
FT                   /id="PRO_5021493898"
FT   DOMAIN          71..341
FT                   /note="Plant heme peroxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50873"
FT   ACT_SITE        76
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-1"
FT   BINDING         77
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT   BINDING         90
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT   BINDING         92
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT   BINDING         94
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT   BINDING         199
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         200
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT   BINDING         217
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT   BINDING         219
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT   BINDING         224
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT   SITE            72
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-3"
FT   DISULFID        44..308
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
FT   DISULFID        63..144
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
FT   DISULFID        272..337
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
SQ   SEQUENCE   362 AA;  37600 MW;  28845353D3FA0593 CRC64;
     MAIKSLLAST ITVVALFNAS QAGVINKRKT ACAGTVHQAA NPACCTWFEV LDDLQSNVLF
     SECGEASHTA LRMVFHDAIG FSNTQQFGGG ADGSMIMFGD AELAFAANNG LDEIAGDLKT
     VADAHGKTYG DIIQLAGAVG VANCAGAPRL KFLAGRPNAT APAPDGTVPD PFQPVDTILA
     RMSDAGFSPD ELVALLASHT IAAADKVDVT IPGTPFDSTA DTFDTQFFIE TQLKGVGFPG
     TGANQGEVES PLVGEMRLQS DFALARDSRT ACTWQSFVTD HALMNQRFSD AMDKLAVLGQ
     NTQGFLDCSE VIPHPHSLKV IPHLPAGKTS ADVEPACAAT PFPDLPTAPG AATTVKPVPP
     GS
//
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