ID A0A2T0FBZ2_9ASCO Unreviewed; 281 AA.
AC A0A2T0FBZ2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU363051};
DE EC=1.11.1.- {ECO:0000256|RuleBase:RU363051};
GN ORFNames=B9G98_00079 {ECO:0000313|EMBL:PRT52459.1};
OS Wickerhamiella sorbophila.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Trichomonascaceae; Wickerhamiella.
OX NCBI_TaxID=45607 {ECO:0000313|EMBL:PRT52459.1, ECO:0000313|Proteomes:UP000238350};
RN [1] {ECO:0000313|EMBL:PRT52459.1, ECO:0000313|Proteomes:UP000238350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS02 {ECO:0000313|EMBL:PRT52459.1,
RC ECO:0000313|Proteomes:UP000238350};
RA Ahn J.O.;
RT "Genome sequencing of [Candida] sorbophila.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the peroxidase family. Cytochrome c peroxidase
CC subfamily. {ECO:0000256|ARBA:ARBA00005997}.
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:PRT52459.1}.
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DR EMBL; NDIQ01000001; PRT52459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0FBZ2; -.
DR STRING; 45607.A0A2T0FBZ2; -.
DR OrthoDB; 168803at2759; -.
DR Proteomes; UP000238350; 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; 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 PANTHER; PTHR31356:SF66; HEME-BINDING PEROXIDASE-RELATED; 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; 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 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:UP000238350}.
FT DOMAIN 71..269
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
SQ SEQUENCE 281 AA; 31331 MW; DA39531782F7008C CRC64;
MSKEGDYAAV AEAIRKIIPK EGYDDGSAGP VLVRLAWHAS GTYDKASDTG GSNGATMRYK
LEADDGANSG LEYARAFLEP IKQQFPWISY ADLWTFAGTV ALEYMGGPKI QWKPGRVDYA
DDSNVPPNGR LPDGAQGADH LRHIFYRMGF NDQEIVALSG AHNLGRTHAN RSGFDGPWVP
NPTRFSNTYF KLLLNEEWYE GKSPAGVRQF YDEDKDLMML PTDMALIEDP KFRSWVEKYA
KDKDAFYEDF AKVFAKLLEL GIKRGPDGKA VVNVLKAEAK L
//
