ID A0A0S8H2I1_9BACT Unreviewed; 638 AA.
AC A0A0S8H2I1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 24.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000618};
DE EC=6.5.1.2 {ECO:0000256|RuleBase:RU000618};
DE Flags: Fragment;
GN ORFNames=AMS25_12885 {ECO:0000313|EMBL:KPK79383.1};
OS Gemmatimonas sp. SM23_52.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1703359 {ECO:0000313|EMBL:KPK79383.1, ECO:0000313|Proteomes:UP000051975};
RN [1] {ECO:0000313|EMBL:KPK79383.1, ECO:0000313|Proteomes:UP000051975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_52 {ECO:0000313|EMBL:KPK79383.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- FUNCTION: DNA ligase that catalyzes the formation of phosphodiester
CC linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-
CC stranded DNA using NAD as a coenzyme and as the energy source for the
CC reaction. It is essential for DNA replication and repair of damaged
CC DNA. {ECO:0000256|ARBA:ARBA00004067}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-
CC nicotinamide D-nucleotide.; EC=6.5.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00034005,
CC ECO:0000256|RuleBase:RU000618};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:KPK79383.1}.
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DR EMBL; LJUM01000093; KPK79383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8H2I1; -.
DR Proteomes; UP000051975; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd00114; LIGANc; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 1.10.287.610; Helix hairpin bin; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_01588; DNA_ligase_A; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR041663; DisA/LigA_HHH.
DR InterPro; IPR001679; DNA_ligase.
DR InterPro; IPR018239; DNA_ligase_AS.
DR InterPro; IPR033136; DNA_ligase_CS.
DR InterPro; IPR013839; DNAligase_adenylation.
DR InterPro; IPR013840; DNAligase_N.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004150; NAD_DNA_ligase_OB.
DR InterPro; IPR010994; RuvA_2-like.
DR NCBIfam; TIGR00575; dnlj; 1.
DR PANTHER; PTHR23389; CHROMOSOME TRANSMISSION FIDELITY FACTOR 18; 1.
DR PANTHER; PTHR23389:SF9; DNA LIGASE; 1.
DR Pfam; PF01653; DNA_ligase_aden; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR Pfam; PF12826; HHH_2; 1.
DR Pfam; PF14520; HHH_5; 1.
DR PIRSF; PIRSF001604; LigA; 1.
DR SMART; SM00278; HhH1; 4.
DR SMART; SM00532; LIGANc; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS01055; DNA_LIGASE_N1; 1.
DR PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU000618};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU000618};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU000618};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000618};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU000618};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 600..638
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT NON_TER 638
FT /evidence="ECO:0000313|EMBL:KPK79383.1"
SQ SEQUENCE 638 AA; 70201 MW; FA1BB96993B0EAFE CRC64;
MTARTRKSAP SDDAQLARRR IAELRETIRH HDYLYYVLDR PEISDAEYDR LFQELRGLEE
RFPELITPDS PTQRVAGRPR PGFSEIEHTA RMLSLDSSAE EDAVRRFDAR LRSALADGAV
AYVVEPKLDG VSLELVYEDG SLAWAATRGD GRVGEDVTAN VRTIGSVPLK LRTGARAIPP
RLSLRGEAIM LIGEFERLNA RLTQEDKPVF ANPRNAAAGS LRQLDPSVTA ERPLTFYAYE
IMTIEGAAPA EQWDTLGALR DWGFKVSRHA RRAGSIDEAI EIHHELERER DDLEYEVDGV
VMKVDDLAAR DSLGVTAHHP RWAFAYKFEP RREVSEILDI VVQVGRTGKL TPVAMLRPVD
VGGVTVSRAS LHNREEIERK DIRVGDKARI QRAGDVIPQV VERVAEPGKK RKRAFKMPAR
CPSCGGPVVS HGPLDFCTNG LACPAQLKAR IQHFASRDAL DIHGLGERTV EQLLASGLVE
SVADLFRLEE TDLLQLEGFA ELSAKNLIDA IQRAKQVTLD RFLFALGIPE IGSQTARDLA
QHFGNLDAFL AASREELEAV PGVGPKVAEA VSDFLASPAT RKTIAELRKQ GVELSEPEVA
GDGQFAGLTF VFTGALASIT RGEAEEIVHS LGGRTSSS
//
