ID A0A0D2CHD3_9EURO Unreviewed; 494 AA.
AC A0A0D2CHD3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Catalase core domain-containing protein {ECO:0000259|SMART:SM01060};
GN ORFNames=PV04_09559 {ECO:0000313|EMBL:KIW64636.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW64636.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW64636.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW64636.1,
RC ECO:0000313|Proteomes:UP000054266};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR038928-2};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329}.
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DR EMBL; KN846961; KIW64636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2CHD3; -.
DR STRING; 5601.A0A0D2CHD3; -.
DR HOGENOM; CLU_010645_2_0_1; -.
DR OrthoDB; 3198922at2759; -.
DR Proteomes; UP000054266; Unassembled WGS sequence.
DR GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd08157; catalase_fungal; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024711; Catalase_clade1/3.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR020835; Catalase_sf.
DR PANTHER; PTHR11465; CATALASE; 1.
DR PANTHER; PTHR11465:SF26; CATALASE 2; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038928-2};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR038928-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559}.
FT DOMAIN 11..399
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 61
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 134
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 344
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-2"
SQ SEQUENCE 494 AA; 55374 MW; 0A494DD275396536 CRC64;
MIVAGPHDFY TLAEGRPLPR NDTSVQVRNK HGGGLVLLQD TQLIETLAHF SRERIPERVV
HAKAIGARGY FQVTHDISDI TDADFLNGIG KKTEVLTRIS TVGPESGSAD TIRDFHGWAI
KFKTAEGNND WVFNNQPVFF VRDPIKFPSL NRSHKRHPAT HSTDADMFWD FHVGAPESVH
ALMFLFSSRG TPASLRNING YSGHTYKFTK KDGSFHYVKI HIHADQGVKN LTDAEATRLA
GTSPDHLTLD MFNAIEEGNY PSYTVSIQTI HPADVALCPV NIFDMTKVLP HAQYPLRPVG
KLVFDQNPVN YFSEIEQAAF TPSNMVPGIE PSADPMLQAR MFAYPDAARY RLGVNYQMLP
TNAAKVPVYI PTERDGFMNF SANYAADPNY VGSSIHPTGF HDAAQSEYKP TEEELTGPVV
FTSDVTDEDF KQPRALWRDV FTKEEQETFV ANISGNIAGV KRDWLREKVY DLFRRVDPSL
GDRIQETVNK IVKA
//
