ID A0A1J7JBW1_9PEZI Unreviewed; 498 AA.
AC A0A1J7JBW1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 28-JUN-2023, entry version 18.
DE SubName: Full=Catalase-domain-containing protein {ECO:0000313|EMBL:OIW30785.1};
GN ORFNames=CONLIGDRAFT_653541 {ECO:0000313|EMBL:OIW30785.1};
OS Coniochaeta ligniaria NRRL 30616.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW30785.1, ECO:0000313|Proteomes:UP000182658};
RN [1] {ECO:0000313|EMBL:OIW30785.1, ECO:0000313|Proteomes:UP000182658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW30785.1,
RC ECO:0000313|Proteomes:UP000182658};
RG DOE Joint Genome Institute;
RA Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA Van Elsas J.D., Nichols N.N.;
RT "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT hydrolysates.";
RL Submitted (OCT-2016) 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; KV875096; OIW30785.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J7JBW1; -.
DR STRING; 1408157.A0A1J7JBW1; -.
DR InParanoid; A0A1J7JBW1; -.
DR OrthoDB; 3198922at2759; -.
DR Proteomes; UP000182658; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000182658}.
FT DOMAIN 7..396
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 58
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 131
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 498 AA; 55188 MW; 79908DD7EF5849C8 CRC64;
MSAPVYTLAE GCPYADATTA QRFSDGSPIK GLMLLQDTQL IETLAHFSRE RIPERVVHAS
AVGAWGEFEV THDISHLTSA KFLTGIGKKS KTLSRISTVG PGAGSPNTVR DVRGWALKIF
TEEGNQDFVF NDIPVFFIRD PIKFPSLNRS HKRHPATNVT DATMFWDFHS QNQEGIHALM
LLFSDRGTPK SVRHVNAYSG HTYKMTKPDG SFHYVKFHFK SNQGNDTLTD AEATRLAGED
PDNHTADLYD AIESGNFPSW TLYIQAMTPQ QAETYRWNVF DMTKVWPHSD VPLQPVGKLT
FNKNPDNYFA DIEQAAFSPS TMVPGLAPSA DPILQARQFA YPDAARYRLG ANYQQLPCNR
ALCPVYSPYQ RDGASTINGN YGADPNYVRS ALKAVAFRQP VADDSGKKHH DVWTMGCVAD
YASQVTDEDF VQARMFWEGV LGAQEGQKEV LVGNVAAHLG RAKPVVWEAT FDMFSRIAPD
LGKAVRNAVA GQGQKTQV
//
