ID   G2ZVZ5_9RALS            Unreviewed;       304 AA.
AC   G2ZVZ5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Putative ATP-dependent DNA ligase from phage {ECO:0000313|EMBL:CCA83276.1};
GN   ORFNames=BDB_mp60442 {ECO:0000313|EMBL:CCA83276.1};
OS   blood disease bacterium R229.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=741978 {ECO:0000313|EMBL:CCA83276.1};
RN   [1] {ECO:0000313|EMBL:CCA83276.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R229 {ECO:0000313|EMBL:CCA83276.1};
RX   PubMed=21931687; DOI=10.1371/journal.pone.0024356;
RA   Remenant B., de Cambiaire J.C., Cellier G., Jacobs J.M., Mangenot S.,
RA   Barbe V., Lajus A., Vallenet D., Medigue C., Fegan M., Allen C., Prior P.;
RT   "Ralstonia syzygii, the Blood Disease Bacterium and some Asian R.
RT   solanacearum strains form a single genomic species despite divergent
RT   lifestyles.";
RL   PLoS ONE 6:e24356-e24356(2011).
RN   [2] {ECO:0000313|EMBL:CCA83276.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R229 {ECO:0000313|EMBL:CCA83276.1};
RA   Genoscope - CEA;
RL   Submitted (APR-2011) 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};
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DR   EMBL; FR854082; CCA83276.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2ZVZ5; -.
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; cd08041; OBF_kDNA_ligase_like; 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:CCA83276.1}.
FT   DOMAIN          120..241
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   304 AA;  33823 MW;  1B38E33BD0D38024 CRC64;
     MAEYLIHKAV EFDKVTAKAK KEKGLTDLAS LAIRYGAQRK YDGCNGILLV KPNETALLSR
     TGEVVRSCDH IRKAGRVLMS PLLEKGRAVV LLGEVWQAGQ PQSKISGDFR RHDPAPHLQF
     IAFDTLYLDE YQEGISYRPF AERYIQLHTF LRATHPTDTV RLCETYNPGT YGDPQAFADQ
     LVEQGGYDGL ILRDPFAIWT RGSGTGGEIL KVKNTETFDL RVIGVEEGKG KYAGTLGALV
     LRGPKGPVTC SGMSDEQRNQ WWAEPSLIVG QIVEVAALGF TVKGSLREPR FKGIRHDKEH
     ADYE
//