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Database: UniProt
Entry: F2SUA4_TRIRC
LinkDB: F2SUA4_TRIRC
Original site: F2SUA4_TRIRC 
ID   F2SUA4_TRIRC            Unreviewed;       401 AA.
AC   F2SUA4;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 2.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Catalase core domain-containing protein {ECO:0000259|SMART:SM01060};
GN   ORFNames=TERG_06053 {ECO:0000313|EMBL:EGD89816.2};
OS   Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD89816.2, ECO:0000313|Proteomes:UP000008864};
RN   [1] {ECO:0000313|Proteomes:UP000008864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
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DR   EMBL; GG700654; EGD89816.2; -; Genomic_DNA.
DR   AlphaFoldDB; F2SUA4; -.
DR   STRING; 559305.F2SUA4; -.
DR   VEuPathDB; FungiDB:TERG_06053; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   HOGENOM; CLU_010645_2_0_1; -.
DR   InParanoid; F2SUA4; -.
DR   OMA; GSFKYVH; -.
DR   OrthoDB; 3198922at2759; -.
DR   Proteomes; UP000008864; Unassembled WGS sequence.
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   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; CATALASE; 1.
DR   PANTHER; PTHR11465:SF9; CATALASE; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008864}.
FT   DOMAIN          1..316
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
SQ   SEQUENCE   401 AA;  46116 MW;  B0B8E27EDE41F5AB CRC64;
     MLLGVGKKTQ CVTRFSTTGL ERGSSDGVRD LKGMAVKFFT EQGDWDWVSL NFPFFFIRDP
     AKFPDMIHSQ RRDPQTNLLN PNMTWDFVTK NPEALHMTLL QHSDFGTMFT WRTLSSYVGH
     AFKWVMPDGS FKYVHFFLAS DRGPNFTDGS TAKIDPNDPD FATKDLFEAI ERGDYPSWTA
     NVQVVDPKDA PKLGFNILDI TKHWNLGTYP KGLDTIPSRP FGKLTLNRNV KDYFSEVEKL
     AFSPSNLVPG VEPSEDPILQ ARMFAYPDAQ RYRLGIDHLK APLRRKETAC QQDLGPEFEK
     WLSQVTSEAW SHPYEDDYKF AREYYEVLPE FRSQEFQDRM VENLCRSIAP GPEELRKRVF
     DTFELVSSEL ARRLREGVEA IVAEKARPDS PSRAQPGQLR L
//
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