ID DNLI1_SCHPO Reviewed; 768 AA. AC P12000; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 07-OCT-2020, entry version 162. DE RecName: Full=DNA ligase 1; DE EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135}; DE AltName: Full=DNA ligase I; DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1; GN Name=cdc17; ORFNames=SPAC20G8.01, SPAC57A10.13c; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3549293; DOI=10.1111/j.1432-1033.1987.tb10688.x; RA Barker D.G., White J.H.M., Johnston L.H.; RT "Molecular characterisation of the DNA ligase gene, CDC17, from the fission RT yeast Schizosaccharomyces pombe."; RL Eur. J. Biochem. 162:659-667(1987). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972 / ATCC 24843; RX PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., RA Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA CC replication, DNA recombination and DNA repair. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- CC (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + CC diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10135}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family. CC {ECO:0000305}. 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; X05107; CAA28754.1; -; Genomic_DNA. DR EMBL; CU329670; CAB08176.1; -; Genomic_DNA. DR PIR; A29066; A29066. DR RefSeq; NP_593318.2; NM_001018749.2. DR SMR; P12000; -. DR BioGRID; 278340; 20. DR STRING; 4896.SPAC20G8.01.1; -. DR iPTMnet; P12000; -. DR MaxQB; P12000; -. DR PaxDb; P12000; -. DR PRIDE; P12000; -. DR EnsemblFungi; SPAC20G8.01.1; SPAC20G8.01.1:pep; SPAC20G8.01. DR GeneID; 2541849; -. DR KEGG; spo:SPAC20G8.01; -. DR EuPathDB; FungiDB:SPAC20G8.01; -. DR PomBase; SPAC20G8.01; cdc17. DR eggNOG; KOG0967; Eukaryota. DR HOGENOM; CLU_005138_4_2_1; -. DR InParanoid; P12000; -. DR KO; K10747; -. DR OMA; PYPDWKP; -. DR PhylomeDB; P12000; -. DR Reactome; R-SPO-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha). DR Reactome; R-SPO-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta). DR Reactome; R-SPO-5651801; PCNA-Dependent Long Patch Base Excision Repair. DR Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER. DR Reactome; R-SPO-69183; Processive synthesis on the lagging strand. DR PRO; PR:P12000; -. DR Proteomes; UP000002485; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IDA:PomBase. DR GO; GO:0043596; C:nuclear replication fork; IC:PomBase. DR GO; GO:0005634; C:nucleus; IDA:PomBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003910; F:DNA ligase (ATP) activity; IGI:PomBase. DR GO; GO:0003909; F:DNA ligase activity; IDA:PomBase. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006284; P:base-excision repair; ISS:PomBase. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro. DR GO; GO:0006266; P:DNA ligation; IDA:PomBase. DR GO; GO:0051103; P:DNA ligation involved in DNA repair; IBA:GO_Central. DR GO; GO:0006310; P:DNA recombination; ISS:PomBase. DR GO; GO:0006281; P:DNA repair; IMP:PomBase. DR GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central. DR GO; GO:0006289; P:nucleotide-excision repair; ISS:PomBase. DR GO; GO:1903461; P:Okazaki fragment processing involved in mitotic DNA replication; IMP:PomBase. DR Gene3D; 1.10.3260.10; -; 1. DR InterPro; IPR000977; DNA_ligase_ATP-dep. DR InterPro; IPR012309; DNA_ligase_ATP-dep_C. DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent. DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS. DR InterPro; IPR012308; DNA_ligase_ATP-dep_N. DR InterPro; IPR036599; DNA_ligase_N_sf. DR InterPro; IPR012340; NA-bd_OB-fold. 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 SUPFAM; SSF117018; SSF117018; 1. DR SUPFAM; SSF50249; SSF50249; 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; Magnesium; Metal-binding; KW Nucleotide-binding; Nucleus; Reference proteome. FT CHAIN 1..768 FT /note="DNA ligase 1" FT /id="PRO_0000059585" FT REGION 309..318 FT /note="Interaction with target DNA" FT /evidence="ECO:0000250" FT REGION 490..492 FT /note="Interaction with target DNA" FT /evidence="ECO:0000250" FT ACT_SITE 416 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10135" FT METAL 469 FT /note="Magnesium 1" FT /evidence="ECO:0000250" FT METAL 568 FT /note="Magnesium 2" FT /evidence="ECO:0000250" FT BINDING 414 FT /note="ATP" FT /evidence="ECO:0000250" FT BINDING 421 FT /note="ATP" FT /evidence="ECO:0000250" FT BINDING 437 FT /note="ATP" FT /evidence="ECO:0000250" FT BINDING 573 FT /note="ATP" FT /evidence="ECO:0000250" FT BINDING 587 FT /note="ATP" FT /evidence="ECO:0000250" FT BINDING 593 FT /note="ATP" FT /evidence="ECO:0000250" FT SITE 165 FT /note="Interaction with target DNA" FT /evidence="ECO:0000250" FT SITE 438 FT /note="Interaction with target DNA" FT /evidence="ECO:0000250" FT SITE 619 FT /note="Interaction with target DNA" FT /evidence="ECO:0000250" FT SITE 644 FT /note="Interaction with target DNA" FT /evidence="ECO:0000250" SQ SEQUENCE 768 AA; 86581 MW; 6783FF3DDC675F31 CRC64; MRTVFSQIPR FKQVNQYIRM STRQSDISNF FISSASHKSE HVEVSQSSSD SKNVDGRSTS EKRKVESVKL VDESKHNNHD DTGTQNVERE NNIVSEAKKQ KTLGSSSSSS DAVSSNNDSG ASTPIPLPIK EPPLESNARN DKLKGHATFA EMVKAFTKIE NTSKRLEIID IMGTYFFGIL RDHPSDLLAC VYLSINKLGP DYSGLELGIG ESIIMKAIGE STGQTLQQIK LSFHKVGDLG LVAQTSRQNQ PTMFKPAALT IPFLFDSLKK IAQMSGNQSQ NRKIGVIKRL LSSCEGAEPK YLIRALEGKL RLQLAEKTIL VALANATAQY HADKNGEKLS QQDRIEGEQI LRDVYCQLPS YDLIVPHLIE HGLGTLRETC KLTPGIPTKP MLAKPTKQIS EVLNTFDQAA FTCEYKYDGE RAQVHFTEDG KFYVFSRNSE NMSVRYPDIS VSVSKWKKPD ARSFILDCEA VGWDRDENKI LPFQKLATRK RKDVKIGDIK VRACLFAFDI LYLNGQPLLE TPLNERRKLL YSMFQPSTGD FTFAKHSDQK SIESIEEFLE ESVKDSCEGL MVKMLEGPDS HYEPSKRSRH WLKVKKDYLS GVGDSLDLIV IGAYYGKGKR TSVYGAFLLG CYDPDTETVQ SICKLGTGFS EEHLETFYNQ LKDIVISKKK DFYAHSDVPA HQPDVWFEPK YLWEVLAADL SLSPVYKAAI GYVQEDKGIS LRFPRFIRIR EDKSWEDATT SEQVSEFYRS QVAYSQKEKE GSPAAEDY //