ID A0C1A3_PARTE Unreviewed; 416 AA.
AC A0C1A3;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Chromosome undetermined scaffold_141, whole genome shotgun sequence {ECO:0000313|EMBL:CAK64570.1};
GN ORFNames=GSPATT00034046001 {ECO:0000313|EMBL:CAK64570.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK64570.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK64570.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK64570.1,
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).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
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DR EMBL; CT868032; CAK64570.1; -; Genomic_DNA.
DR RefSeq; XP_001431968.1; XM_001431931.1.
DR AlphaFoldDB; A0C1A3; -.
DR STRING; 5888.A0C1A3; -.
DR EnsemblProtists; CAK64570; CAK64570; GSPATT00034046001.
DR GeneID; 5017752; -.
DR KEGG; ptm:GSPATT00034046001; -.
DR eggNOG; ENOG502QTYC; Eukaryota.
DR HOGENOM; CLU_661337_0_0_1; -.
DR InParanoid; A0C1A3; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd07896; Adenylation_kDNA_ligase_like; 1.
DR CDD; cd08041; OBF_kDNA_ligase_like; 1.
DR Gene3D; 3.30.1490.70; -; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR InterPro; IPR029319; DNA_ligase_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR47810; DNA LIGASE; 1.
DR PANTHER; PTHR47810:SF1; DNA LIGASE B; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF14743; DNA_ligase_OB_2; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 4: Predicted;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600}.
FT DOMAIN 250..345
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 416 AA; 47695 MW; A9B27F6E140E25FF CRC64;
MKKQQSPEMY LIKNDQFWHC QFIQLKPITI QIRNGFLNGN IEKQETIEIS LTKFPTMERG
IEVMSEQIQQ KLQKGFREIN SNDILKANEQ QFQEKTVASS KKDLMQQKIL KKVNLPEQRK
PVVALTDDAT QGKLVGEWPK YRARTHLGET LELGPPGDTK PIACLLAGQW NENINPTNYL
LSEKLDGMRI IWSGCEMFTR NGNSLNFPTS FVEGWPTTYL DGELWLDRGQ FQKLVSIAKK
KQPDYKAWKD IKFMVFDAPL LDEPFVNRYA KFKKAIEKIK NPHLVYVPHV VCRGYEHLKE
ELALAQQAGG EGLMLRDPQS KYEGKRSNTL LKVKTTMDSE ATVIDHISGM GKFKDQLGAL
KVQTDAGITF QIGVGFNSKL RKDPPKIGSR VSYSYYGLTD DGKPRFPVFE RIREDI
//
