ID   A0A0Q6BCP1_9PROT        Unreviewed;       278 AA.
AC   A0A0Q6BCP1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=ATP-dependent DNA ligase {ECO:0000313|EMBL:KQT43471.1};
GN   ORFNames=ASG34_01390 {ECO:0000313|EMBL:KQT43471.1};
OS   Methylophilus sp. Leaf416.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylophilus.
OX   NCBI_TaxID=1736373 {ECO:0000313|EMBL:KQT43471.1, ECO:0000313|Proteomes:UP000050891};
RN   [1] {ECO:0000313|EMBL:KQT43471.1, ECO:0000313|Proteomes:UP000050891}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf416 {ECO:0000313|EMBL:KQT43471.1,
RC   ECO:0000313|Proteomes:UP000050891};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT43471.1, ECO:0000313|Proteomes:UP000050891}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf416 {ECO:0000313|EMBL:KQT43471.1,
RC   ECO:0000313|Proteomes:UP000050891};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQT43471.1}.
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DR   EMBL; LMQS01000001; KQT43471.1; -; Genomic_DNA.
DR   RefSeq; WP_055825622.1; NZ_LMQS01000001.1.
DR   AlphaFoldDB; A0A0Q6BCP1; -.
DR   OrthoDB; 9767858at2; -.
DR   Proteomes; UP000050891; Unassembled WGS sequence.
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.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   4: Predicted;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000313|EMBL:KQT43471.1}.
FT   DOMAIN          127..228
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   278 AA;  31306 MW;  29CFE17FD1862E22 CRC64;
     MCLIKACIIL VFTIWVFPAY AKAPDILLAH IYQQGLDFRE YLVSEKLDGI RAVWDGKQLV
     SRQGHQIHAP AWFTKQFPAQ ALDGELWIAR GQFELLSATV RQTVPEDAAW RKVIYYVFEL
     PNAEGSFADR ALRLEQLAQK INSPYLKAIK QFHVQDEQSL KRTLDNVVAK HGEGLMLHRA
     DAPYLTGRNH ALLKLKPQLD AEAIVIAHVP GKGKYVGKMG ALLVEMPDGL QFKLGTGFSD
     AERANPPQIG SQVTYTYRDI TKKGKPKFAS FVRVRPPE
//