ID A0A093J580_FULGA Unreviewed; 430 AA.
AC A0A093J580;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=C-terminal-binding protein 2 {ECO:0000313|EMBL:KFW10120.1};
DE Flags: Fragment;
GN ORFNames=N327_11095 {ECO:0000313|EMBL:KFW10120.1};
OS Fulmarus glacialis (Northern fulmar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Procellariiformes; Procellariidae;
OC Fulmarus.
OX NCBI_TaxID=30455 {ECO:0000313|EMBL:KFW10120.1, ECO:0000313|Proteomes:UP000053806};
RN [1] {ECO:0000313|EMBL:KFW10120.1, ECO:0000313|Proteomes:UP000053806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N327 {ECO:0000313|EMBL:KFW10120.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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}.
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DR EMBL; KK607705; KFW10120.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093J580; -.
DR Proteomes; UP000053806; 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:SF3; C-TERMINAL-BINDING PROTEIN 2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053806}.
FT DOMAIN 25..343
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 122..308
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT REGION 399..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW10120.1"
FT NON_TER 430
FT /evidence="ECO:0000313|EMBL:KFW10120.1"
SQ SEQUENCE 430 AA; 47052 MW; 146FF55A6D571DDE CRC64;
GIRPQIMNGP MHPRPLVALL DGRDCTVEMP ILKDLATVAF CDAQSTQEIH EKVLNEAVGA
MMYHTITLTR EDLEKFKALR VIVRIGSGYD NIDIKAAGEL GIAVCNIPSA AVEETADSTI
CHVLNLYRRN TWLYQALREG TRVQSVEQIR EVASGAARIR GGPPQQSLGQ AGGGRTAQAV
AVRAKAFGFN VIFYDPYLQD GIERSLGVQR VYTLQDLLYQ SDCVSLHCNL NEHNHHLIND
FTIKQMRQGA FLVNTARGGL VDEKALTQAL KEGRIRGAAL DVHESEPFSF AQGPLKDAPN
LICTPHTAWY SEQASLEMRE AAATEIRRAI TGRIPESLRN CVNKEFFVTT APWSVIDQQA
IHPELNGATY RYPPGMVSVA PGGIPAAMEG IIPGGIPVTH NLPTVAHPSQ APSPNQPTKH
GDNREHPNEQ
//
