ID B3DWU2_METI4 Unreviewed; 689 AA. AC B3DWU2; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 14-APR-2009, entry version 10. DE SubName: Full=NAD-dependent DNA ligase; GN Name=lig; OrderedLocusNames=Minf_1701; OS Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum OS (strain V4)). OC Bacteria; Verrucomicrobia; unclassified Verrucomicrobia; OC Methylacidiphilum. OX NCBI_TaxID=481448; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 (By similarity). CC -!- CATALYTIC ACTIVITY: NAD(+) + (deoxyribonucleotide)(n) + CC (deoxyribonucleotide)(m) = AMP + nicotinamide nucleotide + CC (deoxyribonucleotide)(n+m). 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 RefSeq; YP_001940353.1; -. DR GeneID; 6352646; -. DR GenomeReviews; CP000975_GR; Minf_1701. DR KEGG; min:Minf_1701; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:InterPro. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR InterPro; IPR001357; BRCT. DR InterPro; IPR018239; DNA_ligase_AS. DR InterPro; IPR004150; DNA_ligase_OB. DR InterPro; IPR001679; DNAligase. DR InterPro; IPR013839; DNAligase_adenylation. DR InterPro; IPR013840; DNAligase_N. DR InterPro; IPR003583; HHH1_DNA-bd_CS. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004149; Znf_DNAligase_C4. DR Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 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 PIRSF; PIRSF001604; LigA; 1. DR SMART; SM00292; BRCT; 1. DR SMART; SM00278; HhH1; 3. DR SMART; SM00532; LIGANc; 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; Metal-binding; NAD; Zinc. 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 //