ID   Q2K0P1_RHIEC            Unreviewed;       354 AA.
AC   Q2K0P1;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   OrderedLocusNames=RHE_PE00251 {ECO:0000313|EMBL:ABC93686.1};
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OG   Plasmid p42e {ECO:0000313|EMBL:ABC93686.1,
OG   ECO:0000313|Proteomes:UP000001936}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC93686.1, ECO:0000313|Proteomes:UP000001936};
RN   [1] {ECO:0000313|EMBL:ABC93686.1, ECO:0000313|Proteomes:UP000001936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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; CP000137; ABC93686.1; -; Genomic_DNA.
DR   RefSeq; WP_011428105.1; NC_007765.1.
DR   AlphaFoldDB; Q2K0P1; -.
DR   KEGG; ret:RHE_PE00251; -.
DR   HOGENOM; CLU_008325_4_2_5; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000001936; Plasmid p42e.
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   CDD; cd07971; OBF_DNA_ligase_LigD; 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:ABC93686.1};
KW   Plasmid {ECO:0000313|EMBL:ABC93686.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001936}.
FT   DOMAIN          138..230
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   354 AA;  39597 MW;  A73477B36C00886F CRC64;
     MTRSRRPSAP LLRDSSSSIQ SRPVRRRDPD QPNLPFDAMP SRVEPCLALL KQTVPQGPDW
     LYEVKWDGYR LALHIEPKGI RILTRGGHDW TRRFPTIAAR ARELGVSSCI LDGEAVVLDE
     EGRSDFGALQ RSLGGRGGKR ISTESIFYAF DLLYLDGHDL TRTELSVRRH LLEDLIPAAD
     GGAIRFSQEL DLGGEELLEH ACRLGMEGII AKRTDSPYRS GRLGDWQKIK CVQSESFMIV
     GYEESASTRG GLGSLLLAGR KGHDWIYVGS VGTGFNRTEA EYLRKTLNRL QTKKPIVPLK
     GKRLVFSQPT LIAEIEFRGW TREGSLRHPS YKGLREIQDN AAVFDMADGP AAIR
//