ID W5MYK4_LEPOC Unreviewed; 402 AA.
AC W5MYK4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=C-terminal binding protein 1 {ECO:0000313|Ensembl:ENSLOCP00000013463.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000013463.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000013463.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR EMBL; AHAT01001565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01001566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01001567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01001568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01001569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01001570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01001571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015200436.1; XM_015344950.1.
DR AlphaFoldDB; W5MYK4; -.
DR Ensembl; ENSLOCT00000013492.1; ENSLOCP00000013463.1; ENSLOCG00000010970.1.
DR GeneID; 102685595; -.
DR GeneTree; ENSGT00940000157061; -.
DR HOGENOM; CLU_019796_1_3_1; -.
DR OrthoDB; 4204864at2759; -.
DR Proteomes; UP000018468; Linkage group LG4.
DR Bgee; ENSLOCG00000010970; Expressed in zone of skin and 13 other cell types or tissues.
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; IPR029752; D-isomer_DH_CS1.
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:SF2; C-TERMINAL-BINDING PROTEIN 1; 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; PS00065; D_2_HYDROXYACID_DH_1; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 44..357
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 140..323
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 402 AA; 44660 MW; FD6FB5BAD5FA33DB CRC64;
MSLMDKHKVK RQRLDRIFEG IRPPIMNGPM HPRPLVALLD GRDCTVEMPI LKDVATVAFC
DAQSTQEIHE KVLNEAVGAL MYHTITLTRE DLEKFKALRI IVRIGSGFDN IDIKSAGDLG
IAVCNMPAAS VEETADSTMC QILNLYRRTT WLHQALREGT RVQSVEQIRE VSSGAARIRG
ETLGIIGLGR VGQAVALRAK AFGFSVIFYD PYLSDGIERA LGLQRVNTLQ DLLFHSDCVT
LHCSLNEHNH HLINDFTIKQ MRQGAFLVNT ARGGLVDEKA LAQALKEGRI RGAALDVHET
EPFSFSQGPL KDAPNLICTP HAAWYSEQAS IEMREEAARE IRRAVTGRIP DSLKNCVNKD
YLTQATHWAS MDPTVVHPEL NGAYSHIQAV VQNLRMSDHA GI
//
