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Database: UniProt
Entry: A0A5B1QXV3_9AGAM
LinkDB: A0A5B1QXV3_9AGAM
Original site: A0A5B1QXV3_9AGAM 
ID   A0A5B1QXV3_9AGAM        Unreviewed;       361 AA.
AC   A0A5B1QXV3;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-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=DENSPDRAFT_803852 {ECO:0000313|EMBL:KAA1474286.1};
OS   Dentipellis sp. KUC8613.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Russulales; Hericiaceae; Dentipellis.
OX   NCBI_TaxID=1883078 {ECO:0000313|EMBL:KAA1474286.1, ECO:0000313|Proteomes:UP000322482};
RN   [1] {ECO:0000313|EMBL:KAA1474286.1, ECO:0000313|Proteomes:UP000322482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KUC8613 {ECO:0000313|EMBL:KAA1474286.1,
RC   ECO:0000313|Proteomes:UP000322482};
RX   PubMed=31482283; DOI=.1007/s00253-019-10089-6;
RA   Park H., Min B., Jang Y., Kim J., Lipzen A., Sharma A., Andreopoulos B.,
RA   Johnson J., Riley R., Spatafora J.W., Henrissat B., Kim K.H.,
RA   Grigoriev I.V., Kim J.J., Choi I.G.;
RT   "Comprehensive genomic and transcriptomic analysis of polycyclic aromatic
RT   hydrocarbon degradation by a mycoremediation fungus, Dentipellis sp.
RT   KUC8613.";
RL   Appl. Microbiol. Biotechnol. 103:8145-8155(2019).
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:KAA1474286.1}.
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DR   EMBL; NSJX01000026; KAA1474286.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5B1QXV3; -.
DR   InParanoid; A0A5B1QXV3; -.
DR   Proteomes; UP000322482; 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; IPR019794; Peroxidases_AS.
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; 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:UP000322482};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU363051}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|RuleBase:RU363051"
FT   CHAIN           19..361
FT                   /note="Peroxidase"
FT                   /evidence="ECO:0000256|RuleBase:RU363051"
FT                   /id="PRO_5023016715"
FT   DOMAIN          66..341
FT                   /note="Plant heme peroxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50873"
FT   REGION          341..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..361
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        71
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-1"
FT   BINDING         72
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            67
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-3"
FT   DISULFID        26..39
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
FT   DISULFID        38..308
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
FT   DISULFID        58..144
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
FT   DISULFID        272..337
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
SQ   SEQUENCE   361 AA;  38043 MW;  76FEFCDE23F22E4B CRC64;
     MSWKTLAAFV ALIGAANAAI TRRVACPDGK NTATNAACCV LFAVRDDIQE NLFDNGQCGE
     DVHESLRLTF HDAIGWSLSA IAAGTFGGNG ADGSISTFST TETNFHANNG IDEIVEEQRP
     FLSRHNITAG DFIQFAGAVG VSNCPGAPQL EFMLGRPPAV APAPDKTVPE PFDTVDSILA
     RFADADFSTD EVIALLSSHT IAAADKVDVT IPGTPFDSTP EIFDTQFFIE TQLRGTLFPG
     TGGNQGEVES PLKGEMRLQS DSELARDSRT ACLWQGFVNE QEKMVTAFKS AMAKLAVTGQ
     DTTSMVDCSE LIPTPPPPKG TAHLPAGLTH NDIEQACAST PFPTLPTDPG PVTSVAAVPP
     S
//
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