ID A0A1G1PJ26_9BACT Unreviewed; 467 AA.
AC A0A1G1PJ26;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 13-SEP-2023, entry version 19.
DE RecName: Full=DNA ligase (NAD(+)) {ECO:0000256|ARBA:ARBA00012722};
DE EC=6.5.1.2 {ECO:0000256|ARBA:ARBA00012722};
DE Flags: Fragment;
GN ORFNames=A3F87_00085 {ECO:0000313|EMBL:OGX41955.1};
OS Omnitrophica WOR_2 bacterium RIFCSPLOWO2_12_FULL_51_24.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801869 {ECO:0000313|EMBL:OGX41955.1, ECO:0000313|Proteomes:UP000179359};
RN [1] {ECO:0000313|EMBL:OGX41955.1, ECO:0000313|Proteomes:UP000179359}
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 -!- 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 -!- 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:OGX41955.1}.
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DR EMBL; MHHC01000060; OGX41955.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1PJ26; -.
DR STRING; 1801869.A3F87_00085; -.
DR Proteomes; UP000179359; 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; cd17748; BRCT_DNA_ligase_like; 1.
DR Gene3D; 6.20.10.30; -; 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; 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; 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 InterPro; IPR004149; Znf_DNAligase_C4.
DR NCBIfam; TIGR00575; dnlj; 1.
DR PANTHER; PTHR23389; CHROMOSOME TRANSMISSION FIDELITY FACTOR 18; 1.
DR PANTHER; PTHR23389:SF9; DNA LIGASE; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF01653; DNA_ligase_aden; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR Pfam; PF03119; DNA_ligase_ZBD; 1.
DR Pfam; PF12826; HHH_2; 1.
DR Pfam; PF14520; HHH_5; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00278; HhH1; 3.
DR SMART; SM00532; LIGANc; 1.
DR SUPFAM; SSF52113; BRCT domain; 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; PS01056; DNA_LIGASE_N2; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OGX41955.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 387..467
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OGX41955.1"
SQ SEQUENCE 467 AA; 51921 MW; 6D87C72EAA33CEBA CRC64;
AAAGSLKLLD PRIVAKRGLD LFIHGLGYSE GIPFRSQSGL FDGLRDLGFR VNPNFKKCPA
IDEVLKFCDI WQKKRRELEY DIDGMVVKVD SFAQQKKLGA TTKSPRWMIA YKYPAERVET
KLLDIKVQVG RTGVLTPVAV LKPVFVAGTT VAHASLHNQD EIERKDVRLG DTVIIEKAGE
IIPQIVEVVK SKRTGKEKKF GIPKECPVCG APTKREEGEV AFRCENVFCP AQLKESLIHF
ASRAAMDIEG LGDAMVDQLV DKKLVRDYGD IYYLKFAQLR ELERMGDKSA QNLLVAIEKS
KGNRLNRLIF ALGIRHAGEH IADVLAKRFQ SIDKLSQQKA ENLIQVKEIG PVVAESIHEF
FSSRISRKVL DRLAKAGVKM EEKSHPASSA KLAGKSFVFT GELKNYSRTD AEQLVRDLGG
TVSSNVGNKT DFVVIGEAPG SKYGKAKKLG VKIIGEKEFE KILKEKR
//
