ID   G2HU99_9BACT            Unreviewed;       267 AA.
AC   G2HU99;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=DNA ligase {ECO:0000313|EMBL:BAK72702.1};
GN   ORFNames=ABLL_0827 {ECO:0000313|EMBL:BAK72702.1};
OS   Arcobacter sp. L.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Arcobacteraceae; Arcobacter.
OX   NCBI_TaxID=944547 {ECO:0000313|EMBL:BAK72702.1, ECO:0000313|Proteomes:UP000001290};
RN   [1] {ECO:0000313|EMBL:BAK72702.1, ECO:0000313|Proteomes:UP000001290}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L {ECO:0000313|Proteomes:UP000001290};
RX   PubMed=22038970; DOI=10.1128/JB.06084-11;
RA   Toh H., Sharma V.K., Oshima K., Kondo S., Hattori M., Ward F.B., Free A.,
RA   Taylor T.D.;
RT   "Complete Genome Sequences of Arcobacter butzleri ED-1 and Arcobacter sp.
RT   Strain L, Both Isolated from a Microbial Fuel Cell.";
RL   J. Bacteriol. 193:6411-6412(2011).
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; AP012048; BAK72702.1; -; Genomic_DNA.
DR   RefSeq; WP_014473541.1; NC_017192.1.
DR   AlphaFoldDB; G2HU99; -.
DR   STRING; 944547.ABLL_0827; -.
DR   KEGG; arc:ABLL_0827; -.
DR   PATRIC; fig|944547.4.peg.834; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_021047_0_0_7; -.
DR   Proteomes; UP000001290; 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:BAK72702.1}.
FT   DOMAIN          119..188
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   267 AA;  31530 MW;  5452EC1BAB347952 CRC64;
     MKLILIFLLN ISMYALDLQK ANIYDETKHQ INGWYMSEKL DGIRAYWNGK ELLSKNGNKI
     YAPIWFTKNF PPFELDGELY TKRDDFENIQ NIVLDTNPSK DWQQITYNIF EVPNVKGNFD
     KRLEKIRIWL NKNPNNYIKI IPQIICKDKK HLNKYLEELV NKKAEGIILK NPYLDYENGR
     TNNILKVKTF FDDEGVVIGH NYNKEKNFKS LVIKLKNGIV FNLGGGFSNK ERLNPPKIGE
     IITFKYYGFT KNNKPKFASF LRIRKKE
//