ID   A0A3Q2VXH8_HAPBU        Unreviewed;       995 AA.
AC   A0A3Q2VXH8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=C-terminal-binding protein 2 {ECO:0000313|Ensembl:ENSHBUP00000017363.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000017363.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000017363.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_005919575.1; XM_005919513.2.
DR   AlphaFoldDB; A0A3Q2VXH8; -.
DR   Ensembl; ENSHBUT00000034617.1; ENSHBUP00000017363.1; ENSHBUG00000019483.1.
DR   GeneID; 102290675; -.
DR   CTD; 548605; -.
DR   GeneTree; ENSGT00940000166669; -.
DR   OrthoDB; 4204864at2759; -.
DR   Proteomes; UP000264840; Unplaced.
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   4: Predicted;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264840}.
FT   DOMAIN          633..947
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          729..912
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          155..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..203
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   995 AA;  107111 MW;  9F5E1B513F00273A CRC64;
     MPNSSEQSYF GGSLSQRGPE WSEGQNDRAA SRCHYCGNIA GCRNSSALCG EDGDVWFHGH
     LDLGEKRDPV LHSSLYRQIQ QDQHGQPPLK NTSVPDLSSS LYLKELMAGR ASAPPQDYYL
     TDATLSGHPP KESGFYRDNQ HLLTRSALHY GPSVGGVRSS WDQGQARATP SLLASASTPT
     PAPLPPPPPP PPPPPPPPPP LHELSRLYRE TLGSKMIPDV QRIGGSSPAT AIFGAQPPLP
     VYAAEPLSAR QTYNSINSLR LDPLQPAATS SLVDPASQGM DAAFPRAYGA VASQRLPYDP
     NYDPSSAMVA ATAGMVSTLP PHQPSAADPK KMVDPAFLAF LRGEGLAEST ITLLLQHGFD
     SLSTLGMMED HDVRSVAPNL AQARVLSRVV LSCKTGGTAT RARSNSFSHR NDLYVQPQGL
     TMDPNLMQQP PTTVQTVSPR MGEFLGRRPS SAPSQHLLET TTYPGARPLA PGAFPVSPGG
     YSSAVTQGRP FSMYNAHTGL AMSALGNQPP PAPGTPGAAP KTFSGSYSPM ELMKRAPNFP
     PASPVGAASP LHSPQLLRKG INAAPESTIV PVSSATTLQA QNLNNNKMVG RRTGPPVIVS
     TMVTTPDTSI RPQIMNGPMH PRPLVALLDG RDCTVEMPIL KDLATVAFCD AQSTQEIHEK
     VLNEAVGAMM YHTITLTRED LEKFKALRII IRIGSGYDNI DIKAAGELGI AVCNIPSAAV
     EETADSTLCH ILNLYRRNTW LYQALREGTR VQSVEQIREV ASGAARIRGE TLGLIGFGRS
     GQAVAVRAKV FGFNVIFYDP YLQDGLERSL GVQRVYTLQD LLYQSDCVSL HCNLNEHNHH
     LINDFTIKQM RQGAFLVNTA RGGLVDEKAL AQALKEGRIR GAALDVHETE PFSFAQGPLK
     DAPNLICTPH TAWYSEQASL EMREAAATEI RRAITGRIPD SLRNCVNKEF FVTTAPWAVM
     DQPGVHPEHN GAAYSQVNQT LPGVTTGIPQ DKINA
//