ID A0A1Y0N947_9BURK Unreviewed; 300 AA.
AC A0A1Y0N947;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=DNA ligase {ECO:0000313|EMBL:ARV19317.1};
DE EC=6.5.1.1 {ECO:0000313|EMBL:ARV19317.1};
GN Name=ligA_2 {ECO:0000313|EMBL:ARV19317.1};
GN ORFNames=AEP_02390 {ECO:0000313|EMBL:ARV19317.1};
OS Curvibacter sp. AEP1-3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Curvibacter.
OX NCBI_TaxID=1844971 {ECO:0000313|EMBL:ARV19317.1, ECO:0000313|Proteomes:UP000196261};
RN [1] {ECO:0000313|EMBL:ARV19317.1, ECO:0000313|Proteomes:UP000196261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AEP1-3 {ECO:0000313|EMBL:ARV19317.1,
RC ECO:0000313|Proteomes:UP000196261};
RA Foret S., Pietschke C., Fraune S.;
RT "Curvibacter sp. AEP1.3.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC diphosphate.; EC=6.5.1.1; Evidence={ECO:0000256|ARBA:ARBA00034003};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
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DR EMBL; CP015698; ARV19317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0N947; -.
DR OrthoDB; 9782700at2; -.
DR Proteomes; UP000196261; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
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; 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.
PE 4: Predicted;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000313|EMBL:ARV19317.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000196261};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..300
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012801694"
FT DOMAIN 55..211
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|Pfam:PF01068"
FT DOMAIN 225..293
FT /note="DNA ligase OB-like"
FT /evidence="ECO:0000259|Pfam:PF14743"
SQ SEQUENCE 300 AA; 32421 MW; 0AD035107B1F5227 CRC64;
MTQPVAQDRR LCLQGLGAIA LSGVLPASSV WAADSAQRPP LMLAGEYRKE FVLADARVSE
KYDGVRAYWD GRRLITRGGN PIAAPAWFTA GWPARALDGE LWVGRGRFAD AVSTVRQQTP
DDAAWRALRY MVFDIPNHGG RFEERYLALQ TALSALGQAW VQAVEQAPAP DAASLRALLD
RTVAAGGEGL VLHRASALYV PGRSAELVKV KPFQDAEARV LAHVPGQGRL EGNTGALWVE
WPGGEGGRPH RFKLGSGFSD ADRRDPPAVG SWVTFRYRGL TAQGVPRFAT FLRPAGEAGL
//
