ID A0A0G0EQQ7_9BACT Unreviewed; 607 AA.
AC A0A0G0EQQ7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN ORFNames=UR73_C0021G0004 {ECO:0000313|EMBL:KKP77495.1};
OS candidate division WS6 bacterium GW2011_GWF1_35_23.
OC Bacteria; Candidatus Dojkabacteria.
OX NCBI_TaxID=1619097 {ECO:0000313|EMBL:KKP77495.1, ECO:0000313|Proteomes:UP000034816};
RN [1] {ECO:0000313|EMBL:KKP77495.1, ECO:0000313|Proteomes:UP000034816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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 -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}.
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:KKP77495.1}.
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DR EMBL; LBQH01000021; KKP77495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0EQQ7; -.
DR Proteomes; UP000034816; 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:0071897; P:DNA biosynthetic process; IEA:InterPro.
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 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; IPR000977; DNA_ligase_ATP-dep.
DR InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR InterPro; IPR036599; DNA_ligase_N_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR00574; dnl1; 1.
DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45674:SF9; DNA LIGASE 3; 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; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKP77495.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 357..491
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 607 AA; 68100 MW; AA91595720938DD4 CRC64;
MGITFHHIAT KFEELEKISS RNDMSKIIAE LFISLDVEER QALSYILQGR VAPLFVVSEF
NLSEKSIFKL LGNILSSKGG KYDLKGRKVK LGDVGEVVRE VTEELGYESK GLSLMDIYES
MWQIINSSGT GSSEKKANIV GELFSKMSPI ESKYLARIIC GELRLGINAK SVLDAFSNIL
QGDKSKRELL DRVYGINPDL GYVSTILGEE NNISTTIFPG VPILPRLVER VGSFEEVFER
FEEEFLVQPK YDGLRCQIHK YDESVQGESS LIWRKHLKKE HANGLFGESS ASKAVKLFTR
NLEDVTEMFP EIVEDAMAMK AESFILDSEI LGWDHAKNNF LSYQETMQRR RKYGVGEKAK
DIPVKAMVFD VLYLNGKDIS ELDTEIRART IKEVVPDTTR GISQSPTEAI GEMSRLKEVF
DNRVSEGLEG IIVKQKSGRY LPGVRNYEWI KLKKSMEKGL VDTIDLVAVG YYHGSGKRGA
LGVGAVLGAI YNSESNSYEA VCKVGTGFSD ELLANISEKF KDISLVKKPV NVLVEDTLIP
DIWVNPEVVF SVESDEITRN LKADKGIAGG LSLRFPRLIE WGRDKTAEEA TSLEELMRLF
SLQKKNK
//
