ID DNLJ_METI4 Reviewed; 689 AA. AC B3DWU2; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 1. DT 22-JUL-2015, entry version 53. DE RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_01588}; DE EC=6.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01588}; DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] {ECO:0000255|HAMAP-Rule:MF_01588}; GN Name=ligA {ECO:0000255|HAMAP-Rule:MF_01588}; GN OrderedLocusNames=Minf_1701; OS Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum OS (strain V4)). OC Bacteria; Verrucomicrobia; unclassified Verrucomicrobia; OC Methylacidiphilales; Methylacidiphilaceae; Methylacidiphilum. OX NCBI_TaxID=481448; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate V4; RX PubMed=18593465; DOI=10.1186/1745-6150-3-26; RA Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y., RA Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., RA Koonin E.V., Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., RA Dunfield P.F., Feng L., Wang L., Alam M.; RT "Complete genome sequence of the extremely acidophilic methanotroph RT isolate V4, Methylacidiphilum infernorum, a representative of the RT bacterial phylum Verrucomicrobia."; RL Biol. Direct 3:26-26(2008). CC -!- FUNCTION: DNA ligase that catalyzes the formation of CC phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl CC groups in double-stranded DNA using NAD as a coenzyme and as the CC energy source for the reaction. It is essential for DNA CC replication and repair of damaged DNA. {ECO:0000255|HAMAP- CC Rule:MF_01588}. CC -!- CATALYTIC ACTIVITY: NAD(+) + (deoxyribonucleotide)(n) + CC (deoxyribonucleotide)(m) = AMP + beta-nicotinamide D- CC ribonucleotide + (deoxyribonucleotide)(n+m). {ECO:0000255|HAMAP- CC Rule:MF_01588}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01588}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01588}; CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01588}. CC -!- SIMILARITY: Contains 1 BRCT domain. {ECO:0000255|HAMAP- CC Rule:MF_01588}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000975; ACD83755.1; -; Genomic_DNA. DR ProteinModelPortal; B3DWU2; -. DR STRING; 481448.Minf_1701; -. DR EnsemblBacteria; ACD83755; ACD83755; Minf_1701. DR PATRIC; 22492577; VBIMetInf111569_1765. DR eggNOG; COG0272; -. DR HOGENOM; HOG000218458; -. DR OMA; VCELKID; -. DR OrthoDB; EOG6TTVM9; -. DR BioCyc; MINF481448:GJEI-1737-MONOMER; -. DR Proteomes; UP000009149; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-HAMAP. 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 Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.10190; -; 1. DR HAMAP; MF_01588; DNA_ligase_A; 1. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR018239; DNA_ligase_AS. DR InterPro; IPR001679; DNAligase. 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 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 PIRSF; PIRSF001604; LigA; 1. DR SMART; SM00292; BRCT; 1. DR SMART; SM00278; HhH1; 3. DR SMART; SM00532; LIGANc; 1. DR SUPFAM; SSF47781; SSF47781; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF52113; SSF52113; 1. DR TIGRFAMs; TIGR00575; dnlj; 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 Complete proteome; DNA damage; DNA repair; DNA replication; Ligase; KW Magnesium; Manganese; Metal-binding; NAD; Reference proteome; Zinc. FT CHAIN 1 689 DNA ligase. FT /FTId=PRO_0000380416. FT DOMAIN 611 689 BRCT. {ECO:0000255|HAMAP-Rule:MF_01588}. FT NP_BIND 58 62 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT NP_BIND 107 108 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT ACT_SITE 140 140 N6-AMP-lysine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 432 432 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 435 435 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 448 448 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 453 453 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 138 138 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 161 161 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 198 198 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 314 314 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 338 338 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. SQ SEQUENCE 689 AA; 77418 MW; A067A22CB46CB6DE CRC64; MIESYLAFIF LNKVNKKKAP SLDSLGYEEI KKRHDELVKL IRKYDYAYYV EAHPLVSDQE YDNLYHELET LEKLHPELIT PDSPTQRIGE TPLSGFSQVT HEIPMLSLEN TYSKEELFAF LERIKRALPG KKISFTVEPK IDGVSISAVY KNGLFSLGAT RGNGTVGDDI TQNLKTIRSL PLRLETPDPP EYLEVRGEAY MSPKDFERLN AQREKEGKVL FANPRNATAG SLKQLDPRVV AERPLAVVFY GAGKLVGMKC KTQEEWLNFL KKIGLPIPIV FWVCSNENEV YEAIGKLNEC RNQLPYPTDG AAVKVNEWEY YSLLGYTAKA PRWAFAYKYG AERAKTRLNN VIFQVGRSGT ITPVAEMDPV FLSGTTVSRA TLHNFDQVKR LDVKIGDVVY LEKAGEVIPE VVGVDLNQRR GTEKEIVPPE FCPSCGEKLS WEGIFLRCEN ENCPAQLKER ILHFAQRNAM DIQGLGESLV DQLVDKGIVK DVADIYDLDE ETLVNLDRMG KKSAQNLLKA IEESKKKDLS RLIFGLGIPH IGQKASEDLA RYFGTMDKLS HATEEELLNL PFIGEIMARS IVNYFRKEAN RRRLEKLRKK GLNFVSTLSQ ASSGTLSGKT FVITGTLSEP RESIAQKIIS KGGRVSNSLS RKTSYLVVGS DPGSKLQEAK KLGIPLINEQ ELLEMLHGG //