ID   A0A0R0D1L1_9GAMM        Unreviewed;       277 AA.
AC   A0A0R0D1L1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=DNA ligase {ECO:0000313|EMBL:KRG72674.1};
GN   ORFNames=ABB27_00315 {ECO:0000313|EMBL:KRG72674.1};
OS   Stenotrophomonas terrae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=405446 {ECO:0000313|EMBL:KRG72674.1, ECO:0000313|Proteomes:UP000051863};
RN   [1] {ECO:0000313|EMBL:KRG72674.1, ECO:0000313|Proteomes:UP000051863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18941 {ECO:0000313|EMBL:KRG72674.1,
RC   ECO:0000313|Proteomes:UP000051863};
RA   Patil P.P., Midha S., Patil P.B.;
RT   "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL   Submitted (MAY-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:KRG72674.1}.
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DR   EMBL; LDJJ01000002; KRG72674.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R0D1L1; -.
DR   PATRIC; fig|405446.3.peg.767; -.
DR   Proteomes; UP000051863; 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; 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:KRG72674.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..277
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006394924"
FT   DOMAIN          126..227
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   277 AA;  30579 MW;  6903AFEBABC0E733 CRC64;
     MRLLLLLLCC LGSVLGHAHA APPPLMLAGT WQDGPDVSLY LVSEKLDGVR ARWDGQALWT
     RAGHRIAAPV WFTQGWPGQA MDGELWMARG QFEATSALIR SSPGDEAQWR RLRFMTFDLP
     DAAGGFADRH AQLKRMIAAQ RSPHLLAIEQ QRLPDSEGLH RQLRAVVAAG AEGLMLHHQD
     NPYSDGRSPR LLKLKLYDDA EARVIGYAPG KGKYSGMVGA LLMRSDSGAQ FRIGSGLSDA
     QRIDPPAIGS QVTYRYNGLT VHGLPRFPRF LRVRDEP
//