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Database: UniProt
Entry: N1QJL1_SPHMS
LinkDB: N1QJL1_SPHMS
Original site: N1QJL1_SPHMS 
ID   N1QJL1_SPHMS            Unreviewed;       530 AA.
AC   N1QJL1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Catalase-domain-containing protein {ECO:0000313|EMBL:EMF10724.1};
DE   Flags: Fragment;
GN   ORFNames=SEPMUDRAFT_90079 {ECO:0000313|EMBL:EMF10724.1};
OS   Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS   musiva).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX   NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF10724.1, ECO:0000313|Proteomes:UP000016931};
RN   [1] {ECO:0000313|EMBL:EMF10724.1, ECO:0000313|Proteomes:UP000016931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO2202 {ECO:0000313|EMBL:EMF10724.1,
RC   ECO:0000313|Proteomes:UP000016931};
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; KB456267; EMF10724.1; -; Genomic_DNA.
DR   RefSeq; XP_016758845.1; XM_016910519.1.
DR   AlphaFoldDB; N1QJL1; -.
DR   STRING; 692275.N1QJL1; -.
DR   GeneID; 27907656; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   HOGENOM; CLU_010645_2_0_1; -.
DR   OMA; SQTDKDH; -.
DR   OrthoDB; 3198922at2759; -.
DR   Proteomes; UP000016931; 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:SF9; CATALASE; 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:UP000016931};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..530
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004110890"
FT   DOMAIN          61..443
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        108
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        181
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         389
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"
FT   NON_TER         530
FT                   /evidence="ECO:0000313|EMBL:EMF10724.1"
SQ   SEQUENCE   530 AA;  59655 MW;  55190B2850CF2BEA CRC64;
     MRLTSFALLA TPLLADAQSY SILRKVTQPP QNRVDYKTDL FEGTNLKQEQ SVLNNSDLTY
     TDRNGKKNWQ PLGAQRAGEK GPLLLQDVAL IDTLATFNRE RIPERIVHAR GAGAHGFFEA
     TTDYASQFSA ASVFEKGTRT SVTMRFSTVG GARGSADTAR DPRGFSIKFR TKEGILDWVF
     NNTPVFFIRD PAKFPRFIHT QKTDPARNVR DWNTFWSWPA QFPESLLQFL RLFSDLGTPY
     GFRHMDGWSG HTYKLVKPDG SWVYTRVYLS TDQGVRNMTA DEAAKHAGEN DAWATDDLYN
     NIQSGNYPSW TVGIATMTPE QAEAYRYDIL DLTKDWLGVE YHEIGRITLT QNPENYHAEI
     EQSHFSPANM VPGWEPSNDP VLQSRLFAYN DAGRYRVGVN AEEIPVNCPF SSVANFDRDG
     HLSSHGNQGG RLNFPAEILD PIHIIDRPGT AIDHPLEGAS TVQWLSEIDE NIDYEQPRLF
     YEGFSQTDKD HLYSNIAGTL VNVDHQPVLD ALFEQFGKIS PALLTGVQTA
//
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