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Database: UniProt
Entry: M2N0F5_BAUPA
LinkDB: M2N0F5_BAUPA
Original site: M2N0F5_BAUPA 
ID   M2N0F5_BAUPA            Unreviewed;       580 AA.
AC   M2N0F5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   03-MAY-2023, entry version 38.
DE   RecName: Full=Catalase core domain-containing protein {ECO:0000259|SMART:SM01060};
GN   ORFNames=BAUCODRAFT_288212 {ECO:0000313|EMBL:EMC92419.1};
OS   Baudoinia panamericana (strain UAMH 10762) (Angels' share fungus)
OS   (Baudoinia compniacensis (strain UAMH 10762)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Baudoinia.
OX   NCBI_TaxID=717646 {ECO:0000313|EMBL:EMC92419.1, ECO:0000313|Proteomes:UP000011761};
RN   [1] {ECO:0000313|EMBL:EMC92419.1, ECO:0000313|Proteomes:UP000011761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 10762 {ECO:0000313|EMBL:EMC92419.1,
RC   ECO:0000313|Proteomes:UP000011761};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
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; KB445562; EMC92419.1; -; Genomic_DNA.
DR   RefSeq; XP_007680764.1; XM_007682574.1.
DR   AlphaFoldDB; M2N0F5; -.
DR   STRING; 717646.M2N0F5; -.
DR   GeneID; 19110785; -.
DR   KEGG; bcom:BAUCODRAFT_288212; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   HOGENOM; CLU_010645_0_0_1; -.
DR   OMA; QVTWLFG; -.
DR   OrthoDB; 3198922at2759; -.
DR   Proteomes; UP000011761; 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:SF13; CATALASE (EUROFUNG); 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:UP000011761}.
FT   DOMAIN          55..441
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         385
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   580 AA;  66503 MW;  F4EFB13191237C04 CRC64;
     MDAIKTASRI AGAGEPRGNR MHHMMSANEG PMDIIAKVSG YSKEGIREDD GPYFTNNEGI
     PLPDPEHSKT IGGIPVASDV HLFQKQQHFN RSKNLERMVH PCGSGAFGYF ECTNDVSDLT
     KADFLQRPGE RTPIFIRFST VTLGREFPDE ARNPRGFAVK FYTHEGNYDI VGLNFPVFFC
     RDPIQGPDVI RSQARNPKNF FLDYDATFDL LGATPEGNHA GLMFFSDHGT PDGWVNEHGY
     GCHTFKWVNK EGKFVYIKYH FLAKHGQKQL TEPEAIRISG EDPDYSKRQL WELIEAGQEV
     EWTAKVQIMQ PDEADPEKLG FDPFDVTKVW PRGQFPMHEF GKLVLNKNPE NFHRDVEQAA
     FSPGSMVPGI EDSPDPLLQF RMFFYRDAQY HRIGVNLHQV PVNCPFMAQS LSSVNFDGPM
     RVDGNHSGNK QYVPNSFMGD RFRPDVAEAP YKVSDNIVSR KSHYYHEGKL SEYDQPRELY
     KRVMTDQQRK NLHHNTAKML SHVNFPIIQK QYLSQIYNVA PEYAKGVYDL TKFKHKEPFE
     FSEVESMSKQ AHLFFKNPKF RPDPGNRLVG MVPEKPFYHV
//
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