ID A0A0V1CZB3_TRIBR Unreviewed; 1041 AA.
AC A0A0V1CZB3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=C-terminal-binding protein 1 {ECO:0000313|EMBL:KRY54560.1};
DE Flags: Fragment;
GN Name=Ctbp1 {ECO:0000313|EMBL:KRY54560.1};
GN ORFNames=T03_13515 {ECO:0000313|EMBL:KRY54560.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY54560.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY54560.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY54560.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617}.
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:KRY54560.1}.
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DR EMBL; JYDI01000067; KRY54560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CZB3; -.
DR STRING; 45882.A0A0V1CZB3; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; 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; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR043322; CtBP.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
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 Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 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 Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653}.
FT DOMAIN 19..333
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 115..298
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT REGION 439..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY54560.1"
SQ SEQUENCE 1041 AA; 115063 MW; 4BB157271751D2B3 CRC64;
LDRSMNRKPL VALLDGRDCT YEMPILKDVA TVAFCDAQST SEVHERVLNE AFGALLWHGM
SLNRDDLLQY KALKVIVRIG SDVDNIDIKA AGDLGITVCN VPGIDVEEVA DSTLCLILNL
YRRTYWLANA VSNGKHVFGP EMIREAASGT VRIRGQTLGI VGFGCVGTAV ALRAKVFGFN
VIFYDPTVAD GTDKVFNIKQ MSSLNELLAQ ADCITLHCPL TPNSYHMINE SSIMQMKQNA
MIVNVSRGAL VDEIALARAL RTGRIRSAAL DVFEFDQQNP AFGHFADVRN LIRTPHCSWY
SEEACREMRE AAAHEIRRAI TGTIPDDLRN CVNRKFLVLS NSAEHLNFVR KSVDLGIPFN
PFSARGDGLN GVGLPGSNLL PYPPTYLNVG GPQVPVTMSF PNLVGNADAA AMTVGSMVKR
SRPPSAMSAS VSIPSRSHQH LQQALCSPAP TISAPPPTPT PTPPATALAS TLAATLAAPP
TTPTPSLSAL LPMLQSGVSS NSRNSPTPKS PDSNQVDSVS SAEIAVALRL LCVKVCSFVV
ESIHTHTDTK MCLAIVICIL VIGFSLLWWT CRGGGKSPPG PFGLPIVGYM PWLGSKMNLT
LTKLWEQYGD VYSIRVGSRQ LVVVNGQRAI RGALATNDHF AGRPDFFTFR LVSGFDDFSP
AYKRRKKLIL KAMAMFTNRR RAELESVAAK AVGFLMAELK HAAGKPVDPK KPLYRAVCTI
MGYVCYGQHF DKDSAEVGRI LETADEFART ARFGVLCDYI PWASWLVRKQ VAKFVDLLRR
IRAYSDQLTE KHVRTYDQEN LRDVTDFFYK ISTTQVEDGD DDSNEYDRDM LKGLSGSLFG
AGFGTIALTL QWAIMLMAKY PQWQGRVRRE LDDQIGLDHH HQLVWSDRGK LPLTMATLCE
VYRYSSISPL AIVHKATKDC QLCGYEIAEG TPVLFNLYSA HRDRTVFDRV DEFDPGRFLH
EDGSLDPTKA DLIMPYSLGR RRCGGELVAR FEIFIFFASL IQRCIIQEDA LNKLDLNNYI
CTLALHPKPF KVIFLSRTGE W
//
