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Database: UniProt
Entry: A0A1F8B4W9_9BACT
LinkDB: A0A1F8B4W9_9BACT
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ID   A0A1F8B4W9_9BACT        Unreviewed;       583 AA.
AC   A0A1F8B4W9;
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=A3A75_05410 {ECO:0000313|EMBL:OGM59074.1};
OS   Candidatus Woesebacteria bacterium RIFCSPLOWO2_01_FULL_39_10.
OC   Bacteria; Candidatus Woesebacteria.
OX   NCBI_TaxID=1802516 {ECO:0000313|EMBL:OGM59074.1, ECO:0000313|Proteomes:UP000179018};
RN   [1] {ECO:0000313|EMBL:OGM59074.1, ECO:0000313|Proteomes:UP000179018}
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:OGM59074.1}.
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DR   EMBL; MGHC01000027; OGM59074.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8B4W9; -.
DR   STRING; 1802516.A3A75_05410; -.
DR   Proteomes; UP000179018; 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          338..474
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   583 AA;  66303 MW;  D90A8EF5206A69E8 CRC64;
     MKFRELSLYL QQLEKTASRI EITKILAEFF RKADAAEIDK ATYLLLGKLA PNYKGIVFNI
     KDRMMIRILA KAYGKDQRVV LSKYKQKGDL GGVAQDLASG RGGNISVTEV YEKLLKVAEE
     HGEDSQERKV LGLAQILSLL DPLSSRYVTR IPLGRLRLGF SDKTILDALS WMEKGDKSAK
     NALERAYEVL PDVGLLAKEV KLKGIERATK DASPMLGVPI MPMLAQRLKS PSEMIEKMGE
     VAVEPKFDGL RISIHFKSKG FAKDVTEGLK SNNDKVKAFT RNMNETSWMF PELKLAESFI
     KADEVILDSE AVGVDETRKI LANFQQTMTR RRKHEIEKIS AQIPIKFYVF DILYKDGKSL
     IDLKYLERRK MLEKTVKDGR LFEVVAYQIT DKPEEIKFQN SQKRKMGFEG IIIKRLSSEY
     VPGRTGWRWV KMKEAEESVG KMADTVDCVV MGYTRGKGKR VSFGLGQFLV GVRDNEEIKT
     VTKVGTGLTD EQFRELKKRL SGLEVKEKPK NYEVNKLLEP DFWVVPEVVV EIAADEVTKS
     PTHSSGYALR FPRLVRFRDD KDPTGATTVK ELKKLLDMQK FDI
//
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