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Database: UniProt
Entry: F2SBS7_TRIRC
LinkDB: F2SBS7_TRIRC
Original site: F2SBS7_TRIRC 
ID   F2SBS7_TRIRC            Unreviewed;       382 AA.
AC   F2SBS7;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Short-chain dehydrogenase/reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TERG_01311 {ECO:0000313|EMBL:EGD85038.1};
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:EGD85038.1, 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; GG700648; EGD85038.1; -; Genomic_DNA.
DR   RefSeq; XP_003239329.1; XM_003239281.1.
DR   AlphaFoldDB; F2SBS7; -.
DR   STRING; 559305.F2SBS7; -.
DR   GeneID; 10374562; -.
DR   VEuPathDB; FungiDB:TERG_01311; -.
DR   eggNOG; KOG1208; Eukaryota.
DR   HOGENOM; CLU_010194_44_6_1; -.
DR   InParanoid; F2SBS7; -.
DR   OMA; HQPARIY; -.
DR   OrthoDB; 5472990at2759; -.
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; PTHR24320:SF148; NAZGUL, ISOFORM A; 1.
DR   PANTHER; PTHR24320; RETINOL DEHYDROGENASE; 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}.
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   382 AA;  42159 MW;  EB7BAF8D71CEEA43 CRC64;
     MSEITQRRTG GAGGSTAQGH KTSAAQGRPQ PKNGSSHAFK ELVALLTLTR VVLARPLETA
     RLVFLLIHQF AQQVYGSAFR PDRDITDQSD RVILITGGNT GLGKETVLEL AKHQPARIYI
     GARNEQKARK AMEDIQSRLK QTVDIRYLPL DLSSFESIRE AAKLFTGESE RLDTLILNAG
     VMGLEPYRTK DGYEVQFGTN YLGHFLLTSL LLPTLRKTAS QPGSDVRVLS ISSAAWQMAP
     SSPSRLLSLM TSTDDLLACN RWTRYGISKA GNILLASELA RRYPEITSVS IHPGVILTAL
     YEQGRASSIA LKYGLALLVP FASSEKNGAK NHLWAAGCAR SQLRNGEYYS PVGIPDWKND
     LVHDKDTARR LWEWSEQHVT NN
//
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