ID DNLI_ARCFU Reviewed; 555 AA. AC O29632; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2001, sequence version 2. DT 16-JUN-2009, entry version 61. DE RecName: Full=DNA ligase; DE EC=6.5.1.1; DE AltName: Full=Polydeoxyribonucleotide synthase [ATP]; GN Name=lig; OrderedLocusNames=AF_0623; OS Archaeoglobus fulgidus. OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; OC Archaeoglobaceae; Archaeoglobus. OX NCBI_TaxID=2234; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126; RX MEDLINE=98049343; PubMed=9389475; DOI=10.1038/37052; RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., RA Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., RA Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., RA Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., RA Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., RA Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., RA Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., RA Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., RA Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., RA Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., RA Woese C.R., Venter J.C.; RT "The complete genome sequence of the hyperthermophilic, sulphate- RT reducing archaeon Archaeoglobus fulgidus."; RL Nature 390:364-370(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; AE000782; AAB90616.1; ALT_INIT; Genomic_DNA. DR PIR; G69327; G69327. DR RefSeq; NP_069457.1; -. DR HSSP; P00969; 1A0I. DR GeneID; 1483841; -. DR GenomeReviews; AE000782_GR; AF_0623. DR KEGG; afu:AF0623; -. DR NMPDR; fig|224325.1.peg.616; -. DR TIGR; AF_0623; -. DR HOGENOM; O29632; -. DR OMA; O29632; SNLHLGA. DR BioCyc; AFUL224325:AF_0623-MON; -. DR BRENDA; 6.5.1.1; 7576. 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; Complete proteome; DNA damage; KW DNA recombination; DNA repair; DNA replication; Ligase; Metal-binding; KW Nucleotide-binding. FT CHAIN 1 555 DNA ligase. FT /FTId=PRO_0000059601. FT ACT_SITE 249 249 N6-AMP-lysine intermediate (By FT similarity). FT BINDING 247 247 ATP (By similarity). FT BINDING 254 254 ATP (By similarity). FT BINDING 269 269 ATP (By similarity). FT BINDING 298 298 ATP (By similarity). FT BINDING 337 337 ATP (By similarity). FT BINDING 411 411 ATP (By similarity). FT BINDING 417 417 ATP (By similarity). SQ SEQUENCE 555 AA; 63553 MW; D050FE80B2341EDB CRC64; MLFAEFAEFC ERLEKISSTL ELTARIAAFL QKIEDERDLY DVVLFITGKV YPPWDERELG VGIGLLYEAL ENVSGVKRSE IESMIREYGD LGLVAEQLIK KKKMTTLAFE ELTVRKVRET FDEIASLTGE GSMKRKIMLL TGLYGLATPL EARYLTRLIL NEMRLGVGEG IMRDAIARAF RADPETVERA YMITNDLGRV AVVAKKEGEE GLRKMKIEIH IPVRMMLAQV AESLESAVRE MRTAAVEWKF DGSRVQVHWD GSRVTIYSRR LENVTNALPD IVEEIKKSVK PGVILDGEVI AVKEGKPMPF QHVLRRFRRK HDVAKMVEKI PLEAHFFDIL YHDGECIDLP LRERRKLLES AVNESEKIKL AKQIVTDSVD EVRKMYDEAI SAGHEGVMIK LPSSPYIPGK RGKNWLKVKA IMETLDLVVV GGEWGEGKRS HWLSSFELAC LDPVTGKLLK VGRVATGFTE EDLEELTEMF RPLIVSQQGK KVEFIPKYVF EVAYQEIQKS PKYESGYALR FPRFVRLRDD KDVDEADTIE RVENLYKLQF EVKRQ //