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Database: UniProt
Entry: A0A158NPF3_ATTCE
LinkDB: A0A158NPF3_ATTCE
Original site: A0A158NPF3_ATTCE 
ID   A0A158NPF3_ATTCE        Unreviewed;       375 AA.
AC   A0A158NPF3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=C-terminal-binding protein {ECO:0008006|Google:ProtNLM};
GN   Name=105622604 {ECO:0000313|EnsemblMetazoa:XP_012059411.1};
OS   Atta cephalotes (Leafcutter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Atta.
OX   NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012059411.1, ECO:0000313|Proteomes:UP000005205};
RN   [1] {ECO:0000313|Proteomes:UP000005205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA   Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA   Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA   Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA   Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA   Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA   Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA   Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA   Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA   Weinstock G.M., Gerardo N.M., Currie C.R.;
RT   "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT   insights into its obligate symbiotic lifestyle.";
RL   PLoS Genet. 7:e1002007-e1002007(2011).
RN   [2] {ECO:0000313|EnsemblMetazoa:XP_012059411.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (APR-2016) 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; ADTU01022481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012059411.1; XM_012204021.1.
DR   AlphaFoldDB; A0A158NPF3; -.
DR   STRING; 12957.A0A158NPF3; -.
DR   EnsemblMetazoa; XM_012204021.1; XP_012059411.1; LOC105622604.
DR   GeneID; 105622604; -.
DR   KEGG; acep:105622604; -.
DR   eggNOG; KOG0067; Eukaryota.
DR   InParanoid; A0A158NPF3; -.
DR   OrthoDB; 4204864at2759; -.
DR   Proteomes; UP000005205; 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; 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: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; 2.
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:UP000005205}.
FT   DOMAIN          39..359
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          135..324
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   375 AA;  41287 MW;  AAB2D2559340725A CRC64;
     MDKRKMMPKR PRMENLRGPI ANGPIQTRPL VALLDGRDCS IEMPILKDVA TVAFCDAQST
     SEIHEKVLNE AVGALMWHTI ILTKEDLEKF KTLRIIVRIG SGVDNIDVKA AGELGIAVCN
     VPGYGVEEVA DTTLCLILNL YRRTYWLANM VREGKKFTGP EQVREAATGC ARIRGDTLGI
     VGLGRIGSAV ALRAKAFGFT VIFYDPYLPD GIEKSLGLTR VYTLQDLLFQ SDCVSLHCTL
     NEHNHHLINE YTIKQMRPGA FLVNTARGGL VDDDALAAAL KQGRIRAAAL DVHENEPYNV
     FQGQSANQCP LKDAPNLLCT PHAAFYSDAS CTELREMAAS EIRRAIVGRI PDCLRNCVNK
     EYFLSSTGNG FSSRC
//
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