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Database: UniProt
Entry: A0A0D2CNN6_9EURO
LinkDB: A0A0D2CNN6_9EURO
Original site: A0A0D2CNN6_9EURO 
ID   A0A0D2CNN6_9EURO        Unreviewed;       522 AA.
AC   A0A0D2CNN6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   22-FEB-2023, entry version 28.
DE   RecName: Full=Catalase core domain-containing protein {ECO:0000259|SMART:SM01060};
GN   ORFNames=PV07_03262 {ECO:0000313|EMBL:KIW31645.1};
OS   Cladophialophora immunda.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW31645.1, ECO:0000313|Proteomes:UP000054466};
RN   [1] {ECO:0000313|EMBL:KIW31645.1, ECO:0000313|Proteomes:UP000054466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW31645.1,
RC   ECO:0000313|Proteomes:UP000054466};
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 Cladophialophora immunda CBS83496.";
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; KN847041; KIW31645.1; -; Genomic_DNA.
DR   RefSeq; XP_016251861.1; XM_016389959.1.
DR   AlphaFoldDB; A0A0D2CNN6; -.
DR   STRING; 569365.A0A0D2CNN6; -.
DR   GeneID; 27342456; -.
DR   VEuPathDB; FungiDB:PV07_03262; -.
DR   HOGENOM; CLU_010645_2_0_1; -.
DR   OrthoDB; 3198922at2759; -.
DR   Proteomes; UP000054466; 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   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
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; PS00438; CATALASE_2; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054466}.
FT   DOMAIN          7..396
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        57
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         341
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   522 AA;  58449 MW;  5954BF61CE7B19AB CRC64;
     MSEPHYTLAE GVPLPRNDII EQLSTGSGGG YVLLTSTQLL ENLAHFSRER IPERTVHAKA
     AGARGHFEVT DDVSDVTDAD FLNGIGKKTE VLMRISTVGP ARGSADTVRD FRGFAIKFKT
     NEGNQDWVFN NQPVFFVRDP MKFPSLNRSH KPHPRTNASD ASMFWDFHVN NQESIHALMF
     LFGDRGLPSS VRHVNGYSGN TYKFTKDNGA SYVYTRITFK TVQGIHYYTN AEGADIAGKD
     PDAHLLDLQN AIDKGDFPQW DVYIQVIRPE EVAAAPINIF DMTKVWPKGR YPLRKMGRVT
     LDTNPLNWFA EIEQAAFSPS NMVPGIAASP DPMLQARMFA YPDAARYRLG VNYQFLPTNA
     ARGPVYCPIE RDGFMNFTTN YGADPNYLGT RLKPVRFSNR TSAAAVASTD FATVQELKRL
     SLGSADEVQL AHPVAAFTQV DDHRDFEQAT ALWKIMEKQE GAQARFVDNV AAHVSGVGEK
     WLREAAYAMF AKVDKQLSEK IQKVTETKIQ NDHKHPHKSA WH
//
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