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Database: UniProt
Entry: K3W3K2_FUSPC
LinkDB: K3W3K2_FUSPC
Original site: K3W3K2_FUSPC 
ID   K3W3K2_FUSPC            Unreviewed;       378 AA.
AC   K3W3K2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Catalase core domain-containing protein {ECO:0000259|SMART:SM01060};
GN   ORFNames=FPSE_00230 {ECO:0000313|EMBL:EKJ79545.1};
OS   Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ79545.1, ECO:0000313|Proteomes:UP000007978};
RN   [1] {ECO:0000313|EMBL:EKJ79545.1, ECO:0000313|Proteomes:UP000007978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS3096 {ECO:0000313|EMBL:EKJ79545.1,
RC   ECO:0000313|Proteomes:UP000007978};
RX   PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA   Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA   Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT   "Comparative pathogenomics reveals horizontally acquired novel virulence
RT   genes in fungi infecting cereal hosts.";
RL   PLoS Pathog. 8:E1002952-E1002952(2012).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKJ79545.1}.
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DR   EMBL; AFNW01000006; EKJ79545.1; -; Genomic_DNA.
DR   RefSeq; XP_009251625.1; XM_009253350.1.
DR   AlphaFoldDB; K3W3K2; -.
DR   EnsemblFungi; EKJ79545; EKJ79545; FPSE_00230.
DR   GeneID; 20358850; -.
DR   KEGG; fpu:FPSE_00230; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   HOGENOM; CLU_045961_0_0_1; -.
DR   OrthoDB; 1744730at2759; -.
DR   Proteomes; UP000007978; Chromosome 1.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd08153; srpA_like; 1.
DR   Gene3D; 1.20.1280.120; -; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR024168; Catalase_SrpA-type_pred.
DR   PANTHER; PTHR11465; CATALASE; 1.
DR   PANTHER; PTHR11465:SF62; CATALASE T; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007978}.
FT   DOMAIN          33..378
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
SQ   SEQUENCE   378 AA;  41728 MW;  27883F786C514815 CRC64;
     MSIQVVPQTT ITVGLTNDAT DHKSHACLND VCHKPEPSKD ELPQHLVTAM QGIFGKHPGY
     RTTHAKGILV EGSFTPTEEA KSLSTAVHFN NASTKVIARF SVGGGLPRVS DVADGATPKG
     VAIRFQIDDH THTDLIAHSF NGFATRNGED FLTFLKLFGM DGYTEAMLKK AQAADGDISK
     EKKDYDQAHA AFVTFLGNPD HKSALVFVQS EKPNPHNYGT ITYYEPNTHV LTNKDGKITN
     VRYRLVPADG EHLYPNKTPE DKQTLAKLGN DYLEDDLRER FPSKPLVLTI QAHIAGPDDV
     LDDATKPYTS EEYVTVGRLE INKVSDDNAA QQQHISFHPN PEKGGIQGIK SSNDPLIQAR
     KGVYYISSDQ RRHETQLE
//
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