ID DNLI_METTF Reviewed; 557 AA. AC P54875; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 24-MAR-2009, entry version 51. DE RecName: Full=DNA ligase; DE EC=6.5.1.1; DE AltName: Full=Polydeoxyribonucleotide synthase [ATP]; GN Name=lig; OS Methanobacterium thermoformicicum. OC Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; OC Methanobacteriaceae; Methanothermobacter. OX NCBI_TaxID=145262; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=DSM 3720 / Z-245; RX MEDLINE=97158688; PubMed=9006048; RA Noelling J., Reeve J.N.; RT "Growth- and substrate-dependent transcription of the formate RT dehydrogenase (fdhCAB) operon in Methanobacterium thermoformicicum Z- RT 245."; RL J. Bacteriol. 179:899-908(1997). 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; U52681; AAC44823.1; -; Genomic_DNA. DR BRENDA; 6.5.1.1; 258835. 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 InterPro; IPR012340; NA-bd_OB-fold. DR Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1. 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; 1. 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; DNA damage; DNA recombination; KW DNA repair; DNA replication; Ligase; Metal-binding; KW Nucleotide-binding. FT CHAIN 1 557 DNA ligase. FT /FTId=PRO_0000059608. FT ACT_SITE 251 251 N6-AMP-lysine intermediate (By FT similarity). FT BINDING 249 249 ATP (By similarity). FT BINDING 256 256 ATP (By similarity). FT BINDING 271 271 ATP (By similarity). FT BINDING 301 301 ATP (By similarity). FT BINDING 340 340 ATP (By similarity). FT BINDING 417 417 ATP (By similarity). FT BINDING 423 423 ATP (By similarity). SQ SEQUENCE 557 AA; 62822 MW; C328FE239AD1CBAA CRC64; MKELLYMELA EVYHRLESTT KRLEKTEILA ELLRSVDKEL LPDVTILMLG RVFPIWSEEE LGVGIKLLMK AISLVVGVSM DEIEDEIREQ GDIGLASEKL FSRKTQTTFF SQPLTVEFVY SRLKALASAS GDRAQSKKIN ILVEVLSQAK PLEARYITRT VLEELRVGVA EGIIRDAIAR AFEVDPALVE RAHMLTNDLG MVAAVAREEG EPGLGRLNLE PGRPVKPMLA QLASSIESAI TELGRAFCET KYDGIRVQIH RCGDEVSIFT RRLENITAAV PEILEGVEEA LPADDYIVEG EIIVTMDGRP ASFQYILQRV RRKYDVDRLT REVPLSLFLF DVLYHRGPLI DEPLWHRREV LESILSEIPG RVEASRMVDV GPDNLDDALW LFKESIREGH EGIMIKDTEA PYIPGIRGKK MLKFKAEPET LDLIVVGGTY GRGKRAHLVG SYLLAVRDEK SGELKTIAHV ATGLDDQTLQ DLSERMENLK VERRGRKIRV KPEIILEVAY SEIVRSPEYE SGYSLRFPVV KRIRDDLSPD DIDTLGRVIS LFKQGFS //