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Database: UniProt
Entry: V9D5F9_9EURO
LinkDB: V9D5F9_9EURO
Original site: V9D5F9_9EURO 
ID   V9D5F9_9EURO            Unreviewed;       494 AA.
AC   V9D5F9;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   22-FEB-2023, entry version 28.
DE   RecName: Full=Catalase core domain-containing protein {ECO:0000259|SMART:SM01060};
GN   ORFNames=G647_07875 {ECO:0000313|EMBL:ETI21528.1};
OS   Cladophialophora carrionii CBS 160.54.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=1279043 {ECO:0000313|EMBL:ETI21528.1, ECO:0000313|Proteomes:UP000030678};
RN   [1] {ECO:0000313|EMBL:ETI21528.1, ECO:0000313|Proteomes:UP000030678}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 160.54 {ECO:0000313|EMBL:ETI21528.1,
RC   ECO:0000313|Proteomes:UP000030678};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora carrionii CBS 160.54.";
RL   Submitted (MAR-2013) 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; KB822707; ETI21528.1; -; Genomic_DNA.
DR   RefSeq; XP_008730409.1; XM_008732187.1.
DR   AlphaFoldDB; V9D5F9; -.
DR   GeneID; 19986368; -.
DR   VEuPathDB; FungiDB:G647_07875; -.
DR   HOGENOM; CLU_010645_2_0_1; -.
DR   OrthoDB; 3198922at2759; -.
DR   Proteomes; UP000030678; 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;  55509 MW;  71AF29C3A3A92C97 CRC64;
     MIVAGPHNFY TLAEGKPLPS NDTSIQVRNK QGGGLVLLQD TQLIETLAHF SRERIPERVV
     HAKAIGARGY FQVTHDISDI TDADFLNGIG KKTEVLTRIS TVGPESGSAD TIRDFHGWAI
     KFKTAEGNND WVFNNQPVFF VRDPIKFPSL NRSHKRHPAT HSNDADMFWD FHVGSPESVH
     ALMFLFSDRG TPASLRNING YSGHTYKFTK KDGSFHYVRI HIHADEGVKN LTNDEAVRLA
     GTSPDHLTLD MFNAIEEGNY PSYTVSIQTI HPADVGLSPV NIFDMTKVLP HAQYPLRPVG
     KLVFDRNPIN YFSEIEQAAF SPSTMVPGIE PSADPMLQAR MFAYPDAARY RLGVNYQMLP
     TNAAKVPVYI PTERDGFMNF SANYGAEPNY VNSSIHPTGF HDAARSEYKP TEEVLTGPVV
     FTSEITDEDF KQPRALWNNV FSEEEQESFV NNISGNIAAV KRDWLREKVF DLFRRVDQSL
     GDRIEEAVNK IVKM
//
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