ID A0A132AJZ4_SARSC Unreviewed; 419 AA.
AC A0A132AJZ4;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=C-terminal-binding protein-like protein {ECO:0000313|EMBL:KPM11243.1};
GN ORFNames=QR98_0098130 {ECO:0000313|EMBL:KPM11243.1};
OS Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC Sarcoptidae; Sarcoptinae; Sarcoptes.
OX NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM11243.1, ECO:0000313|Proteomes:UP000616769};
RN [1] {ECO:0000313|EMBL:KPM11243.1, ECO:0000313|Proteomes:UP000616769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM11243.1};
RX PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT "Draft genome of the scabies mite.";
RL Parasit. Vectors 8:585-585(2015).
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:KPM11243.1}.
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DR EMBL; JXLN01016753; KPM11243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A132AJZ4; -.
DR VEuPathDB; VectorBase:SSCA006148; -.
DR OMA; RRNTWLC; -.
DR OrthoDB; 4204864at2759; -.
DR Proteomes; UP000616769; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; PTHR46029; C-TERMINAL-BINDING PROTEIN; 1.
DR PANTHER; PTHR46029:SF7; C-TERMINAL-BINDING PROTEIN; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 38..342
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 134..307
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 419 AA; 45955 MW; B87FB842677B7446 CRC64;
MDKKKPIKRP RMDFRGPSVP NGPLHARPLV ALLDGRDCSV EMPILKDVAT VAFCDAQSTQ
EIHEKVLNEA IGALMWHTIT LTKEDLEKFK ALRIIVRIGS GVDNVDIKAA GELGIAVCNV
PGFGVEEVAD STLCLILNLY RRTYWLANMV REGKKFQGPE QVREAASGCA RIRRVGTAVA
LRAKAFGFNV IFYDPYLPDG IDKSLGLTRV YTLQDLLFQS DCVSLHCNLN EHNHHLINEF
TIKQMRPGAF LVNTARGGLV DENALAAALK DGRIRAAALD VHENEPFNAN HGPLKDAPNL
ICTPHAAWYS DASSTELREM AATEIRRAIM GRIPESLRNC VNKEYFTSGA SYGDSINGSS
SYNYTGPIVP HSTTVEPLPN VSLPNSLTTS HSTPHATPHS TLQDTNNHLS VKAESSEVH
//
