ID   K0G071_ACTSU            Unreviewed;       256 AA.
AC   K0G071;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=DNA ligase {ECO:0000313|EMBL:AFU20312.1};
DE            EC=6.5.1.1 {ECO:0000313|EMBL:AFU20312.1};
GN   ORFNames=ASU2_10920 {ECO:0000313|EMBL:AFU20312.1};
OS   Actinobacillus suis H91-0380.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=696748 {ECO:0000313|EMBL:AFU20312.1, ECO:0000313|Proteomes:UP000006303};
RN   [1] {ECO:0000313|EMBL:AFU20312.1, ECO:0000313|Proteomes:UP000006303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H91-0380 {ECO:0000313|EMBL:AFU20312.1,
RC   ECO:0000313|Proteomes:UP000006303};
RX   PubMed=23144422; DOI=10.1128/JB.01633-12;
RA   Macinnes J.I., Mackinnon J., Bujold A.R., Ziebell K., Kropinski A.M.,
RA   Nash J.H.;
RT   "Complete Genome Sequence of Actinobacillus suis H91-0380, a Virulent
RT   Serotype O2 Strain.";
RL   J. Bacteriol. 194:6686-6687(2012).
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; CP003875; AFU20312.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0G071; -.
DR   KEGG; asi:ASU2_10920; -.
DR   PATRIC; fig|696748.4.peg.2216; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_021047_0_0_6; -.
DR   Proteomes; UP000006303; 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; 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   Ligase {ECO:0000313|EMBL:AFU20312.1}.
FT   DOMAIN          98..168
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   256 AA;  29378 MW;  BC1740E3942F2658 CRC64;
     MLLGQYRDQD INGWVMSEKL DGVRGYWDGK QLISRQGNPL APPDYFIKDF PPFAIDGELF
     SERGKFEEIS SITRASEPKG WYKLKFYIFD VPNAQGNLFE RLAKLKNYLL QHPTPYIQII
     EQIPIQNKAH LMQFYQQVLA QHGEGVVVRN PNTAYIKGRS AQILKLKPVL DEECTVIAHH
     NGKGKYRDKL GAITCENQRG RFRIGSGFKD KDRANPPPIG SLITYKYRGL TKQGKPRFAT
     FFRMRTDIGS IHVVTE
//