ID A0A0W0WTZ7_9GAMM Unreviewed; 529 AA.
AC A0A0W0WTZ7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN Name=ykoU {ECO:0000313|EMBL:KTD35822.1};
GN ORFNames=Lnau_0806 {ECO:0000313|EMBL:KTD35822.1};
OS Legionella nautarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45070 {ECO:0000313|EMBL:KTD35822.1, ECO:0000313|Proteomes:UP000054725};
RN [1] {ECO:0000313|EMBL:KTD35822.1, ECO:0000313|Proteomes:UP000054725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49506 {ECO:0000313|EMBL:KTD35822.1,
RC ECO:0000313|Proteomes:UP000054725};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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 -!- 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:KTD35822.1}.
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DR EMBL; LNYO01000013; KTD35822.1; -; Genomic_DNA.
DR RefSeq; WP_058503865.1; NZ_LNYO01000013.1.
DR AlphaFoldDB; A0A0W0WTZ7; -.
DR STRING; 45070.Lnau_0806; -.
DR PATRIC; fig|45070.6.peg.855; -.
DR OrthoDB; 9767858at2; -.
DR Proteomes; UP000054725; Unassembled WGS sequence.
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; 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:KTD35822.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 306..430
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 529 AA; 61535 MW; 80903A539207FEBA CRC64;
MKKFAQLLDR LYFSYRHKTK LNLLHDFFKS TADPERGYAL AIMADTLEFP TFNRELIREL
IHQRIDPFLF ELSLDYVGDL SETIALLWPQ KQESKLPSLT EIVTIFQQLS KTEMASFLAE
LLNQSNKIER WALLKIGTGN LRVGVSARFL KKALACYGQV NVLEIEQVWH NIKPPYLELF
AWLEGKSSIP HSFDANFFHP VMLSHPLKEK DLALIKPEDF YAEYKYDGIR VQLVCTSESK
ALYSRSGDNI SQSFPDVLQE VNEPAVLDGE LVIQSQNRIG SFNDLQKRLN RKKPSKKILQ
EQPAAIILYD LLEEQTQDLR SFSLVDRRKR LEAWFRNYRP SNMLLSELLF FDSLQSLLEL
KQKAIIKQEV AVEGLMLKRK NSLYIAGRPL GLWFKWKREP RLIDAVLMYA QRGHGKRSSF
YSDYTFGLWR AEELVPIGKA YFGFTDEELY QLDKWIRYHT LNHFGPVREV EKALVFEIAF
DAVNYSSRHK SGVALRFPRI NRVRWDKPAN EADKLENLIA LIRGGIPSA
//
