ID A0A1G1C8V6_9BACT Unreviewed; 571 AA.
AC A0A1G1C8V6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN ORFNames=A2783_04525 {ECO:0000313|EMBL:OGV90928.1};
OS Microgenomates group bacterium RIFCSPHIGHO2_01_FULL_45_11.
OC Bacteria.
OX NCBI_TaxID=1817749 {ECO:0000313|EMBL:OGV90928.1, ECO:0000313|Proteomes:UP000178267};
RN [1] {ECO:0000313|EMBL:OGV90928.1, ECO:0000313|Proteomes:UP000178267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGV90928.1}.
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DR EMBL; MHDE01000022; OGV90928.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1C8V6; -.
DR Proteomes; UP000178267; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 327..451
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 571 AA; 64693 MW; ECC7F328F7F028A4 CRC64;
MLLTELANFL QQLESTSSRL AITQILSELF KKADADEIDK IVYLVLGSLA PQYEGLVFNL
ADRLLIRAVS LAYQLSEEKT KAFYQRKGDL GTVVAELAKE KGESVTVSQV YQTLRQIAED
EGENSQERKI NHFAKLLKEL DPLSAKYVIR IPLGKLRLGF SDKTVLDALS WLERGDKSAK
ARLEKSYQVV PDVGLLAKRV KDLGIDKATK DIQPVVGVPV LPMLAQRLKS PKEMIEKMGK
VFVEPKFDGL RVLIHFKRNQ PTNFIKAFTR NLNDVSNMFT ELTDIGNYIN ARQVILDTEA
VGMDPEMVRL ADFQTTMRRR RKYQIDTKVK EIPLRFQVFD IITKDGKSYL DTPYHQRREI
LKRAIKANQL LLVDEATVTD DPEVINQEYR DKIRQGLEGV IVKKYDTAYV PGRRGWRWVK
MKEAELAVGK LADTVDCVVM GYYAGRGKRA SFGLGGFLVG VGDGDTFKSI TKIGTGLTDV
QFRNMFQRLK KLGVKAKPKQ YSLVNKILIP DFWVTPSLIV EIAADEITKS PSHSAGFALR
FPRLVRFRFD KSASQITTVA EIKKLYSLQR A
//
