ID B1J1A8_PSEPW Unreviewed; 553 AA.
AC B1J1A8;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 76.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN OrderedLocusNames=PputW619_1134 {ECO:0000313|EMBL:ACA71639.1};
OS Pseudomonas putida (strain W619).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=390235 {ECO:0000313|EMBL:ACA71639.1};
RN [1] {ECO:0000313|EMBL:ACA71639.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W619 {ECO:0000313|EMBL:ACA71639.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA Richardson P.;
RT "Complete sequence of Psuedomonas putida W619.";
RL Submitted (FEB-2008) 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};
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DR EMBL; CP000949; ACA71639.1; -; Genomic_DNA.
DR AlphaFoldDB; B1J1A8; -.
DR STRING; 390235.PputW619_1134; -.
DR KEGG; ppw:PputW619_1134; -.
DR eggNOG; COG1793; Bacteria.
DR HOGENOM; CLU_005138_6_2_6; -.
DR OMA; WLFEESY; -.
DR OrthoDB; 9767858at2; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA 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 GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd07897; Adenylation_DNA_ligase_Bac1; 1.
DR CDD; cd07972; OBF_DNA_ligase_Arch_LigB; 1.
DR Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 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; IPR026333; ATP_dep_DNA_lig_pp_1105_fam.
DR InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR InterPro; IPR036599; DNA_ligase_N_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR04120; DNA_lig_bact; 1.
DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45674:SF13; DNA LIGASE-RELATED; 1.
DR Pfam; PF04679; DNA_ligase_A_C; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF04675; DNA_ligase_A_N; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ACA71639.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 322..454
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 553 AA; 61980 MW; 08E15B0AB7F5B3C4 CRC64;
MKAFAQLYLR LDATTSSNGK LQALRDYFAA APAEDAAWAV YFLSGGRPRQ LVPTRVLREL
ATALAGLPGW LFDESYQAVG DLAETISLLL PENQQGSKSG LAHWVETHLL PLRGLPAEEV
QQRLPPLWAE LDRPSLMLCL KLITGSFRVG VSKLLVTRAL AQLAGLDAKR IAQRLVGYTD
ISHRPTANSY HKLIAAESAD EHSQRGGQPY PFFLAHALQA PLEQFDALLG PPSAWQIEWK
WDGIRAQVVK RDGQVWVWSR GEELVTDRFP ELHGLAQNLP DGVVLDGEIL VWKPDSGNDQ
ALAVQPFALL QQRIGRKTLG KKLLADAPVV LQAYDLLEWQ GEDWRNHPQH ERRQQLQRLV
EDYPLAPILL SPLLEGKDWH ALAIQRDRSR SLGVEGLMLK QRDALYGVGR TKDMGVWWKW
KIDPFSVDAV LIYAQRGHGR RASLYSDYTF AVWNAPPGAP ERALVPFAKA YSGLSDEEMR
KVDAIIRKTT VETFGPVRSV KPTLVFELGF EGIALSKRHK SGIAVRFPRM LRWRLDKPVE
EADDLATLQA LLA
//