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Database: UniProt
Entry: A0A365T511_9EURY
LinkDB: A0A365T511_9EURY
Original site: A0A365T511_9EURY 
ID   A0A365T511_9EURY        Unreviewed;       322 AA.
AC   A0A365T511;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=C-terminal binding protein {ECO:0000313|EMBL:RBI59230.1};
GN   ORFNames=DMJ13_24005 {ECO:0000313|EMBL:RBI59230.1};
OS   halophilic archaeon.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales.
OX   NCBI_TaxID=29295 {ECO:0000313|EMBL:RBI59230.1, ECO:0000313|Proteomes:UP000252983};
RN   [1] {ECO:0000313|EMBL:RBI59230.1, ECO:0000313|Proteomes:UP000252983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H22 {ECO:0000313|EMBL:RBI59230.1,
RC   ECO:0000313|Proteomes:UP000252983};
RA   Chen S.;
RT   "Draft genome sequence of Haloarchaeon sp. H22 isolated from a salt mine.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RBI59230.1}.
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DR   EMBL; QNGA01000010; RBI59230.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A365T511; -.
DR   Proteomes; UP000252983; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR   CDD; cd05299; CtBP_dh; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR043322; CtBP.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 1.
DR   PANTHER; PTHR43761:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252983}.
FT   DOMAIN          20..319
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          111..287
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   322 AA;  34560 MW;  94D5B33F974ECC6F CRC64;
     MTHTVVVTDH DFEDLSIERS VLGHLAEVVE LTDDVGETAE DVEETLAAAD AVINLRYDVD
     ADAIAVMDDV RVISRYGIGV DNVDVDAAAD RDIPVTNVPD YCLEEVSTHA LALLLSMARS
     VPRYDRSVER GEWNRDVGTP VHRFSTRTVG VVGYGAIGRE VGARAASLGA DVLASDPFLS
     ADDLADDPAD LVAFEELLER ADFVSVHSPL TDDTRGLFDA EAFARMKDSA YLVNVARGPI
     VDGDALLDAL NAGEIAGAGL DVFPDEPPAA DAPLRDHDRV VATPHVAWYS EEANEERRRT
     VAEIVASVLS GGEPWNVVNG VE
//
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