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Database: UniProt
Entry: A0A084QB93_STAC4
LinkDB: A0A084QB93_STAC4
Original site: A0A084QB93_STAC4 
ID   A0A084QB93_STAC4        Unreviewed;       297 AA.
AC   A0A084QB93;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFA61228.1};
GN   ORFNames=S40285_06470 {ECO:0000313|EMBL:KFA61228.1};
OS   Stachybotrys chlorohalonata (strain IBT 40285).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX   NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA61228.1, ECO:0000313|Proteomes:UP000028524};
RN   [1] {ECO:0000313|EMBL:KFA61228.1, ECO:0000313|Proteomes:UP000028524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA61228.1,
RC   ECO:0000313|Proteomes:UP000028524};
RX   PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA   Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT   "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT   the toxigenic black mold Stachybotrys.";
RL   BMC Genomics 15:590-590(2014).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
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DR   EMBL; KL660865; KFA61228.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084QB93; -.
DR   STRING; 1283841.A0A084QB93; -.
DR   HOGENOM; CLU_010194_12_1_1; -.
DR   InParanoid; A0A084QB93; -.
DR   OrthoDB; 1585106at2759; -.
DR   Proteomes; UP000028524; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd05233; SDR_c; 1.
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; PTHR43618; 7-ALPHA-HYDROXYSTEROID DEHYDROGENASE; 1.
DR   PANTHER; PTHR43618:SF18; SHORT CHAIN DEHYDROGENASE_REDUCTASE FAMILY (AFU_ORTHOLOGUE AFUA_5G12480); 1.
DR   Pfam; PF00106; adh_short; 1.
DR   Pfam; PF13561; adh_short_C2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028524};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   297 AA;  31094 MW;  C1484C8125B779D8 CRC64;
     MDPSSLFRVD GLVAVVTGGG TGIAYMMAKA LAAAGARKVY ILGRRQATLE AAAAAHPAIS
     PIVCDVTSKG ALQHAVDVVS EETGHVNLVI ASSGILGPYQ SYDKEKSIKE LRKDLFDETS
     MGSFTETYHV NVTGAWYTAV AFLELLEAGN QNALKGGFGA PLKPGSKAPA IQSQILFVTS
     LGAYSREAAT PPAYAASKAA IAQLAAHAAT NLAPYQIRVN TLAPGWFSSE LADPIISSRD
     PEDEGLDHHA FMPARRFGTE DEMGGTVLYL ASMAGAYCNG LVLLNDGGRL SVVPSTY
//
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