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Database: UniProt
Entry: A0A0D7BBN1_9AGAR
LinkDB: A0A0D7BBN1_9AGAR
Original site: A0A0D7BBN1_9AGAR 
ID   A0A0D7BBN1_9AGAR        Unreviewed;       361 AA.
AC   A0A0D7BBN1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU363051};
DE            EC=1.11.1.- {ECO:0000256|RuleBase:RU363051};
GN   ORFNames=CYLTODRAFT_490247 {ECO:0000313|EMBL:KIY67923.1};
OS   Cylindrobasidium torrendii FP15055 ss-10.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC   Cylindrobasidium.
OX   NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY67923.1, ECO:0000313|Proteomes:UP000054007};
RN   [1] {ECO:0000313|EMBL:KIY67923.1, ECO:0000313|Proteomes:UP000054007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY67923.1,
RC   ECO:0000313|Proteomes:UP000054007};
RX   PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA   Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA   Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA   LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA   Hibbett D.S.;
RT   "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT   genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL   Fungal Genet. Biol. 76:78-92(2015).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|ARBA:ARBA00003917}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-
CC         [cytochrome c] + 2 H2O; Xref=Rhea:RHEA:16581, Rhea:RHEA-COMP:10350,
CC         Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.11.1.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00035967};
CC   -!- SUBUNIT: Forms a one-to-one complex with cytochrome c.
CC       {ECO:0000256|ARBA:ARBA00038574}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Cytochrome c peroxidase
CC       subfamily. {ECO:0000256|ARBA:ARBA00005997}.
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DR   EMBL; KN880514; KIY67923.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D7BBN1; -.
DR   STRING; 1314674.A0A0D7BBN1; -.
DR   OrthoDB; 168803at2759; -.
DR   Proteomes; UP000054007; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004130; F:cytochrome-c peroxidase activity; IEA:RHEA.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR   CDD; cd00691; ascorbate_peroxidase; 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; IPR002207; Peroxidase_I.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   PANTHER; PTHR31356:SF58; CYTOCHROME C PEROXIDASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR31356; THYLAKOID LUMENAL 29 KDA PROTEIN, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00459; ASPEROXIDASE.
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   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
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:UP000054007};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          108..361
FT                   /note="Plant heme peroxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50873"
SQ   SEQUENCE   361 AA;  40082 MW;  2B8D8DF4A782B2BC CRC64;
     MSFQTTLRRA RAPIRAAALA SAPRSATFAR AAFRRYSTEP EPPKKGNTAL YIGLTAAALG
     VGAYFIYTSD ESPLGVKATY VPTREDYQKV YNRIAEIIES ASDAGYDDGS YGPVLLRLAW
     HSSGTYDEQT KTGGSNYATM RFNPESGHGA NAGLDVARNL MEGVKKEFPW ISYGDLWTLA
     GVAAIQEMAG PKVPWRPGRV DGFTENCTPD GRLPDAAQGA DHVRAIFYRM GFNDQEIVAL
     SGAHALGRCH TNRSGFDGPW TFSPTTVTND YYKLLFEESW VWRKWNGPKQ LQDKKTKSLM
     MLPTDYVLVQ DKSFKKYAKA YADNQDLFFK DFAAAVARLF ELGVPTNQFS EEPYTLKSTL
     D
//
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