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Database: UniProt
Entry: A0A167FSE3_9ASCO
LinkDB: A0A167FSE3_9ASCO
Original site: A0A167FSE3_9ASCO 
ID   A0A167FSE3_9ASCO        Unreviewed;       422 AA.
AC   A0A167FSE3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   22-FEB-2023, entry version 22.
DE   RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU363051};
DE            EC=1.11.1.- {ECO:0000256|RuleBase:RU363051};
GN   Name=CCP1 {ECO:0000313|EMBL:ANB15643.1};
GN   ORFNames=AWJ20_3280 {ECO:0000313|EMBL:ANB15643.1};
OS   Sugiyamaella lignohabitans.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Trichomonascaceae; Sugiyamaella.
OX   NCBI_TaxID=796027 {ECO:0000313|EMBL:ANB15643.1, ECO:0000313|Proteomes:UP000189580};
RN   [1] {ECO:0000313|EMBL:ANB15643.1, ECO:0000313|Proteomes:UP000189580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10342 {ECO:0000313|EMBL:ANB15643.1,
RC   ECO:0000313|Proteomes:UP000189580};
RA   Bellasio M., Peymann A., Valli M., Sipitzky M., Graf A., Sauer M., Marx H.,
RA   Mattanovich D.;
RT   "Complete genome sequence and transcriptome regulation of the pentose
RT   utilising yeast Sugiyamaella lignohabitans.";
RL   Submitted (FEB-2016) 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}.
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DR   EMBL; CP014503; ANB15643.1; -; Genomic_DNA.
DR   RefSeq; XP_018738120.1; XM_018880287.1.
DR   AlphaFoldDB; A0A167FSE3; -.
DR   GeneID; 30035285; -.
DR   KEGG; slb:AWJ20_3280; -.
DR   OrthoDB; 168803at2759; -.
DR   Proteomes; UP000189580; Chromosome b.
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:SF36; L-ASCORBATE PEROXIDASE 3; 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:UP000189580}.
FT   DOMAIN          151..422
FT                   /note="Plant heme peroxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50873"
SQ   SEQUENCE   422 AA;  46924 MW;  FF84D53CBA264158 CRC64;
     MHANGFSPVL NIPTPPSQSS VLLIHISSVR NKSHEQAKVV SRTVNNFIIA SLSSVDLDLI
     RSEASLSDLS RSAAISTPTQ SRNLLHTHEF NSNLSGATPK ELKTHSSNYY NPRYLIFPAV
     IDKIVHRIKL TAVKSLKMSK PGDYNALAEA IRKIIPQEDY DDGSIGPILV RLAWHASGTY
     DAATGTGGSN GATMRYSLEA KDSANNGLEH ARRFLEPIKE QFPWISYADL WTFAGAVAVE
     YMDGPKIPWK PGRVDYVDEK NVPPNGRLPD GALGQDHLRQ IFYRMGFNDQ EIVALCGAHN
     LGRTHADRSG FDGPWVPNPT KFGNTYYKLL LHEEWTLSKS PAGLPQYYDA DKELMMLPAD
     FSLILDPEFK KWVEIYAEDK DRFYADFAKA FGKLLELGVR RGPNGLAKVN ELGKINVDPA
     KI
//
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