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Database: UniProt
Entry: F2SH31_TRIRC
LinkDB: F2SH31_TRIRC
Original site: F2SH31_TRIRC 
ID   F2SH31_TRIRC            Unreviewed;       344 AA.
AC   F2SH31;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Short-chain dehydrogenase/reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TERG_01615 {ECO:0000313|EMBL:EGD85340.1};
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:EGD85340.1, 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   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
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DR   EMBL; GG700649; EGD85340.1; -; Genomic_DNA.
DR   RefSeq; XP_003236889.1; XM_003236841.1.
DR   AlphaFoldDB; F2SH31; -.
DR   STRING; 559305.F2SH31; -.
DR   GeneID; 10373345; -.
DR   VEuPathDB; FungiDB:TERG_01615; -.
DR   eggNOG; KOG1208; Eukaryota.
DR   HOGENOM; CLU_010194_44_4_1; -.
DR   InParanoid; F2SH31; -.
DR   OMA; NEKTGHE; -.
DR   OrthoDB; 1661700at2759; -.
DR   Proteomes; UP000008864; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43157; PHOSPHATIDYLINOSITOL-GLYCAN BIOSYNTHESIS CLASS F PROTEIN-RELATED; 1.
DR   PANTHER; PTHR43157:SF68; SHORT CHAIN DEHYDROGENASE ATND-RELATED; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008864}.
SQ   SEQUENCE   344 AA;  38035 MW;  9F04469B84CB5FCE CRC64;
     MASFDTAVIQ KRATSLAFYH RQLFTTPPLA SPDEVDLAGK TAIITGSNTG LGFECAQQLL
     DLGLSKLILA VRNETKGEDA REKLLSGRNA NNHSIEVWKL DLLSYDSIVS FVGRTKSLEQ
     LNFFVNNAAF TRLSFVINEK TGHEEIIQVN YFSLALLTIL ILPVLRDKNS AQQPGRLVNV
     SSDTASWARF RERGSVPLLP AFDREENFHP QDRYATSKLL AQLFLTQLAK RLLPSIAIIN
     TPNPGLCQTS LTRNFKGSLQ GILFGIFKLV FARTATIGAC SITDAVVNHG SESHGQYLED
     GAVQPMAPFV YTDKGEEMAE LLWEETMAEF SFANVSEILE DLSN
//
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