ID A0DYX8_PARTE Unreviewed; 310 AA.
AC A0DYX8;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Chromosome undetermined scaffold_7, whole genome shotgun sequence {ECO:0000313|EMBL:CAK88245.1};
GN ORFNames=GSPATT00003213001 {ECO:0000313|EMBL:CAK88245.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK88245.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK88245.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK88245.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
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DR EMBL; CT868649; CAK88245.1; -; Genomic_DNA.
DR RefSeq; XP_001455642.1; XM_001455605.1.
DR STRING; 5888.A0DYX8; -.
DR EnsemblProtists; CAK88245; CAK88245; GSPATT00003213001.
DR GeneID; 5041427; -.
DR KEGG; ptm:GSPATT00003213001; -.
DR eggNOG; KOG1255; Eukaryota.
DR HOGENOM; CLU_052104_0_0_1; -.
DR InParanoid; A0DYX8; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0009361; C:succinate-CoA ligase complex (ADP-forming); IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IBA:GO_Central.
DR GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR005810; CoA_lig_alpha.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR11117:SF2; SUCCINATE--COA LIGASE [ADP_GDP-FORMING] SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11117; SUCCINYL-COA LIGASE SUBUNIT ALPHA; 1.
DR Pfam; PF02629; CoA_binding; 1.
DR PIRSF; PIRSF001553; SucCS_alpha; 2.
DR PRINTS; PR01798; SCOASYNTHASE.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
DR PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE 4: Predicted;
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 19..115
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT ACT_SITE 263
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001553-1"
SQ SEQUENCE 310 AA; 33048 MW; BC239A5146420CF6 CRC64;
MIGKQIFRAF SSTTAPYVWV NKHTKVICQG ITGNQGTFQT EQALNYFTKM VGGVSPKKAG
STHLGLPVFK NCQEAKQNTG CDASVIYVPP PTAASAIIEA IEAQIGLVVV ITDGIPQHDM
IKVKHALRSQ SVTRVIGPNC PGIIKPNECK IGIMPGYIHQ NGKIGIVSRS GTLTYEAVDQ
TTRAGLGQST VVGXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXSIVGFI AGITAPPERR MGHAGAIVSK GKGSAPEKIR ALEQAGIRVV KSPAQIGKTM
LEVMKERGLA
//
