ID A0A316VHU4_9BASI Unreviewed; 318 AA.
AC A0A316VHU4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU363051};
DE EC=1.11.1.- {ECO:0000256|RuleBase:RU363051};
GN ORFNames=FA14DRAFT_11854 {ECO:0000313|EMBL:PWN37227.1};
OS Meira miltonrushii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Brachybasidiaceae; Meira.
OX NCBI_TaxID=1280837 {ECO:0000313|EMBL:PWN37227.1, ECO:0000313|Proteomes:UP000245771};
RN [1] {ECO:0000313|EMBL:PWN37227.1, ECO:0000313|Proteomes:UP000245771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 3882 {ECO:0000313|EMBL:PWN37227.1,
RC ECO:0000313|Proteomes:UP000245771};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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; KZ819602; PWN37227.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316VHU4; -.
DR STRING; 1280837.A0A316VHU4; -.
DR InParanoid; A0A316VHU4; -.
DR OrthoDB; 168803at2759; -.
DR Proteomes; UP000245771; 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:UP000245771}.
FT DOMAIN 88..280
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 289..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 318 AA; 35895 MW; DA15DBBB8112A869 CRC64;
MSKEGDFDAV RKDIEAILKQ KGYDDGHIGP VLVRLAWHAS GTYCKDTDTG GSNGAGMRYE
KEGGDPANAG LQHARVFVEP IKRKYPWITY SDLWTLAGVV AIRSMGGPDI PWKAGRSDFD
DDSLLPPRGR LPDGSQAQDH LRHIFYRMGF NDQEIVALSG AHNLGRCHAD RSGFEGAWVN
NPTRFSNQYY KLLLKLKWQK KDLNREGAPW QWVATTPGMD EDDEPLMMLP TDYSLTQDAE
FKKWVEKYAE DQDLFFDHFS KVFAKLVELG VYRDEDGVAR FNNLTKGKYE SAPPKSLTPG
APERRPAQVT HISTKARL
//
