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Database: UniProt
Entry: A0A1Y1ZYF2_9PLEO
LinkDB: A0A1Y1ZYF2_9PLEO
Original site: A0A1Y1ZYF2_9PLEO 
ID   A0A1Y1ZYF2_9PLEO        Unreviewed;       314 AA.
AC   A0A1Y1ZYF2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   22-FEB-2023, entry version 15.
DE   RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU363051};
DE            EC=1.11.1.- {ECO:0000256|RuleBase:RU363051};
GN   ORFNames=BCR34DRAFT_622936 {ECO:0000313|EMBL:ORY15291.1};
OS   Clohesyomyces aquaticus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Lindgomycetaceae; Clohesyomyces.
OX   NCBI_TaxID=1231657 {ECO:0000313|EMBL:ORY15291.1, ECO:0000313|Proteomes:UP000193144};
RN   [1] {ECO:0000313|EMBL:ORY15291.1, ECO:0000313|Proteomes:UP000193144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115471 {ECO:0000313|EMBL:ORY15291.1,
RC   ECO:0000313|Proteomes:UP000193144};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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:ORY15291.1}.
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DR   EMBL; MCFA01000026; ORY15291.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1ZYF2; -.
DR   STRING; 1231657.A0A1Y1ZYF2; -.
DR   OrthoDB; 1010072at2759; -.
DR   Proteomes; UP000193144; 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:SF64; L-ASCORBATE PEROXIDASE 7, CHLOROPLASTIC-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:UP000193144};
KW   Signal {ECO:0000256|RuleBase:RU363051}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|RuleBase:RU363051"
FT   CHAIN           18..314
FT                   /note="Peroxidase"
FT                   /evidence="ECO:0000256|RuleBase:RU363051"
FT                   /id="PRO_5011811734"
FT   DOMAIN          67..202
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         197
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         198
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-2"
FT   BINDING         215
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         222
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        63..142
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601621-4"
SQ   SEQUENCE   314 AA;  33273 MW;  012D419A5819F999 CRC64;
     MRVTNVLFLA ATASALSFPD LSPVTDRFND LFRRKDGGNG NCDPKWNDIS KILTAKFLSG
     GECNDDARAA IRAVFHDCGA WETKLGATGG CDGSLALSGE VSRPENGGLA PIAAYLKSLA
     QQKGVGVADM IVFAGSHAIV TCPGGPRVQT WIGRKDSSTP PPGGLLPDVH APAADLFKLF
     QNKGYDAVGL AALLGAHSTS KAFGQSEAPA GTAQDSTPGK WDVKYYAETL NPPQGVFVFP
     SDDKLSKFND VGKEFKGFVN NQGKWSGKFA DAMAKMELFG VASTSGMVDC TNALPQSTQS
     KREMKGFNMF KPRH
//
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