ID DNLI_METS3 Reviewed; 551 AA. AC A5UKX2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 16-JUN-2009, entry version 16. DE RecName: Full=DNA ligase; DE EC=6.5.1.1; DE AltName: Full=Polydeoxyribonucleotide synthase [ATP]; GN Name=lig; OrderedLocusNames=Msm_0645; OS Methanobrevibacter smithii (strain PS / ATCC 35061 / DSM 861). OC Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; OC Methanobacteriaceae; Methanobrevibacter. OX NCBI_TaxID=420247; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17563350; DOI=10.1073/pnas.0704189104; RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., RA Henrissat B., Fulton R., Latreille P., Kim K., Wilson R.K., RA Gordon J.I.; RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to RT the human gut."; RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007). CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA CC during DNA replication, DNA recombination and DNA repair (By CC similarity). CC -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) + CC (deoxyribonucleotide)(m) = AMP + diphosphate + CC (deoxyribonucleotide)(n+m). CC -!- COFACTOR: Divalent metal cations (By similarity). CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000678; ABQ86850.1; -; Genomic_DNA. DR RefSeq; YP_001273218.1; -. DR GeneID; 5216232; -. DR GenomeReviews; CP000678_GR; Msm_0645. DR KEGG; msi:Msm_0645; -. DR OMA; A5UKX2; SNLHLGA. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IEA:HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:HAMAP. DR GO; GO:0006260; P:DNA replication; IEA:HAMAP. DR HAMAP; MF_00407; -; 1. DR InterPro; IPR000977; DNA_ligase. DR InterPro; IPR012309; DNA_ligase_A_C. DR InterPro; IPR012310; DNA_ligase_A_M. DR InterPro; IPR012308; DNA_ligase_A_N. DR InterPro; IPR016059; DNA_ligase_CS. DR Pfam; PF04679; DNA_ligase_A_C; 1. DR Pfam; PF01068; DNA_ligase_A_M; 1. DR Pfam; PF04675; DNA_ligase_A_N; 1. DR TIGRFAMs; TIGR00574; dnl1; 1. DR PROSITE; PS00697; DNA_LIGASE_A1; FALSE_NEG. DR PROSITE; PS00333; DNA_LIGASE_A2; 1. DR PROSITE; PS50160; DNA_LIGASE_A3; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Cell division; Complete proteome; DNA damage; KW DNA recombination; DNA repair; DNA replication; Ligase; Metal-binding; KW Nucleotide-binding. FT CHAIN 1 551 DNA ligase. FT /FTId=PRO_1000049872. FT ACT_SITE 248 248 N6-AMP-lysine intermediate (By FT similarity). FT BINDING 246 246 ATP (By similarity). FT BINDING 253 253 ATP (By similarity). FT BINDING 268 268 ATP (By similarity). FT BINDING 298 298 ATP (By similarity). FT BINDING 337 337 ATP (By similarity). FT BINDING 414 414 ATP (By similarity). FT BINDING 420 420 ATP (By similarity). SQ SEQUENCE 551 AA; 61948 MW; 5CB10B16F770ACFB CRC64; MKYQELVDVY SALENTTKRL EKTQIISNFL LKLDSTTLEQ VGLLILGSIF PAWSDKEIGI GNKLVMQAVG EAVGVTPDKV EDAVRDQGDI GLACISLYAK KSQTTFFSQP LTIDFVFKSL RKLSEKSGAR STKRKIDIIL EMLSQASASE AKYLTRTILE ELRIGVGEGV VRDAIAQAFN IDKSVVERAM MLTNDLGLIA VVAKEKGEGG LKELNLTPGT PVKPMLAQLA PPIPEIINEM GVAICETKYD GIRLQVHRHS DEIKIFTRRL ENITHALPEI VDLFNEYLPH EDYIVEGEVI ATRDGNPLSF QNILHRVRRK HNIDEAMEQV PLKVFLFDLL YYIVPMIDEP LLKRRKKLEE IVNTTPDEIN LSNMVYGTPD TIKEVEDLFE LSIAQHHEGI MIKDAGEPYI PGLRGKKMLK YKAEPETLDM VVVGGTYGIG KRGDFVGSYL VSLRDEDNNL KTVAYVATGL DDATLEYLTK KMKEYELSTK GREIVVEPKI VLEVAFSEIV ESPEYETGYS LRFPVVKNIR KDKGVDDIDT VERLISMYET Q //