ID A0A1F8PTU0_9CHLR Unreviewed; 578 AA.
AC A0A1F8PTU0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=A2W33_05950 {ECO:0000313|EMBL:OGO26604.1};
OS Chloroflexi bacterium RBG_16_52_11.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797646 {ECO:0000313|EMBL:OGO26604.1, ECO:0000313|Proteomes:UP000179327};
RN [1] {ECO:0000313|EMBL:OGO26604.1, ECO:0000313|Proteomes:UP000179327}
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=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:OGO26604.1}.
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DR EMBL; MGNN01000077; OGO26604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8PTU0; -.
DR Proteomes; UP000179327; 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; 6.20.10.30; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
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; IPR041663; DisA/LigA_HHH.
DR InterPro; IPR001679; DNA_ligase.
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 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 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.
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:OGO26604.1};
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 9..458
FT /note="NAD-dependent DNA ligase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00532"
FT DOMAIN 456..475
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 490..509
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 522..541
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 554..573
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT NON_TER 578
FT /evidence="ECO:0000313|EMBL:OGO26604.1"
SQ SEQUENCE 578 AA; 63757 MW; E15F0F3A5261F805 CRC64;
METGIDQDNL KQKLDRLRQE INFHNYRYHV QDSPVISDYE FDQLMQRLRQ IEEDHPEWIT
SDSPTRRAGA SPAEKFVKVR HPAPILSLGN AFSAEDLLAW YERILKIDER VISTDYIVEP
KIDGLTVVLH YRDGIFVQGA TRGDGEIGED ITHNLRTIRT LPLRIPVSQD GPIPPSYLVV
RGEAYISPLD FAALNRKLEE AGEKTYLNPR NTAAGSLRQL DPTLTASRPL KLLTYSIVTI
DGDNRPVVNT EVEMLGYLRA AGFPVVNNIY CPDLNSTLAA YEHLANTRDE LEFEADGMVI
KINELALVAD LGVVGKDPRG LVAYKFPARE VTTLLLDIGV NVGRTGVLTP YAVLDAVNIG
GVIVRQATLH NFDYIAEKDI RIGDRVAVKR AGDVIPYVIG PVISTRTGTE RVYTPPVNCP
ACGQPVEHFT GEVAWYCVNA SCPAQLIRNI EHFVSRGAMD IVGLGIKIVE QLVDAGLVTD
VADLYTLQRE SLLQLEGFAS KKAENLLQSI ADSKSQSLVR LITALGIRGV GEVVAADLAR
NFRNLDALAN SSEAELQSIE GIGPNIAQAI VDWFGREV
//
