ID J2TE88_9BURK Unreviewed; 274 AA.
AC J2TE88;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=ATP dependent DNA ligase-like protein {ECO:0000313|EMBL:EJL76582.1};
GN ORFNames=PMI12_02344 {ECO:0000313|EMBL:EJL76582.1};
OS Variovorax sp. CF313.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1144315 {ECO:0000313|EMBL:EJL76582.1, ECO:0000313|Proteomes:UP000007277};
RN [1] {ECO:0000313|EMBL:EJL76582.1, ECO:0000313|Proteomes:UP000007277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF313 {ECO:0000313|EMBL:EJL76582.1,
RC ECO:0000313|Proteomes:UP000007277};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJL76582.1}.
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DR EMBL; AKIW01000033; EJL76582.1; -; Genomic_DNA.
DR AlphaFoldDB; J2TE88; -.
DR PATRIC; fig|1144315.3.peg.2344; -.
DR Proteomes; UP000007277; 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.
PE 4: Predicted;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000313|EMBL:EJL76582.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..274
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003755836"
FT DOMAIN 78..193
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|Pfam:PF01068"
FT DOMAIN 208..272
FT /note="DNA ligase OB-like"
FT /evidence="ECO:0000259|Pfam:PF14743"
SQ SEQUENCE 274 AA; 30511 MW; AE201E15A3079C2A CRC64;
MLLAVFGVIV APSAFAREAA PSLMLADVYR PGMSLNDYWV SEKYDGVRGY WDGKQLWTRG
GERIMAPAWF TAPLPRQPLD GELWAGRGRF AHAMSTVRSQ TPNDVAWHEM RFMVFDLPAQ
GGDFTTRLAA LRNLLPITDA PWVVPVPQQR ATTHAELQAL LDKTIKMGGE GLMLHRGSSQ
YRGERNSDLL KVKPYEDAEA RVIEHVAGKG RHSARLGALV VETSDGKRFK LGTGLTDAER
ENPPAIGSWV TYRYNGTTAK GLPRFARFMR VREG
//
