ID   F7XBW7_SINMM            Unreviewed;       314 AA.
AC   F7XBW7;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   OrderedLocusNames=SM11_pC1481 {ECO:0000313|EMBL:AEH82554.1};
OS   Sinorhizobium meliloti (strain SM11).
OG   Plasmid pSmeSM11c {ECO:0000313|EMBL:AEH82554.1,
OG   ECO:0000313|Proteomes:UP000009045}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=707241 {ECO:0000313|EMBL:AEH82554.1, ECO:0000313|Proteomes:UP000009045};
RN   [1] {ECO:0000313|EMBL:AEH82554.1, ECO:0000313|Proteomes:UP000009045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM11 {ECO:0000313|EMBL:AEH82554.1,
RC   ECO:0000313|Proteomes:UP000009045};
RC   PLASMID=pSmeSM11c {ECO:0000313|Proteomes:UP000009045};
RX   PubMed=21396969; DOI=10.1016/j.jbiotec.2010.12.018;
RA   Schneiker-Bekel S., Wibberg D., Bekel T., Blom J., Linke B., Neuweger H.,
RA   Stiens M., Vorholter F.J., Weidner S., Goesmann A., Puhler A., Schluter A.;
RT   "The complete genome sequence of the dominant Sinorhizobium meliloti field
RT   isolate SM11 extends the S. meliloti pan-genome.";
RL   J. Biotechnol. 155:20-33(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};
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DR   EMBL; CP001831; AEH82554.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7XBW7; -.
DR   KEGG; smx:SM11_pC1481; -.
DR   PATRIC; fig|707241.3.peg.5406; -.
DR   HOGENOM; CLU_008325_4_2_5; -.
DR   Proteomes; UP000009045; Plasmid pSmeSM11c.
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:InterPro.
DR   CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 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; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR014146; LigD_ligase_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   NCBIfam; TIGR02779; NHEJ_ligase_lig; 1.
DR   PANTHER; PTHR45674:SF15; DNA LIGASE (ATP); 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 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   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AEH82554.1};
KW   Plasmid {ECO:0000313|EMBL:AEH82554.1}.
FT   DOMAIN          134..256
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   314 AA;  34415 MW;  DDDF01C81518DC81 CRC64;
     MSRRAKPLLQ DDSVAKSKPA RPRDPAQPNL PFDPMPERIE PCLALLKPVP PKGPDWVFEV
     KWDGYRLAIH IEPKGVRIIT RGGHDWTHHF PAIAEATSKL GVGTAILDGE AVVLDEEGRS
     DFGALQRSLG GRGGKRSSTE SVFFAFDLLY FDGHDLSGTE LSVRRHLLEG FLDGPTGAIQ
     SSEEVFGDGA LLEKACSMGL EGIIAKHRDR PYRSGRTGDW LKIKCLQSES FMIVGYEQSL
     TARGGLGSLL LAGRKGHDWI YVGSVGTGFN TKDAEYLRKT LDRLKTSKPA VPLKGKNLVF
     AQPTLIAEIE FRGP
//