ID DNLI_SCHPO Reviewed; 768 AA. AC P12000; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 15-JAN-2008, entry version 63. DE DNA ligase (EC 6.5.1.1) (Polydeoxyribonucleotide synthase [ATP]). GN Name=cdc17; ORFNames=SPAC20G8.01, SPAC57A10.13c; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=87161837; PubMed=3549293; RA Barker D.G., White J.H.M., Johnston L.H.; RT "Molecular characterisation of the DNA ligase gene, CDC17, from the RT fission yeast Schizosaccharomyces pombe."; RL Eur. J. Biochem. 162:659-667(1987). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; 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., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). CC -!- FUNCTION: This protein seals, during DNA replication, DNA CC recombination and DNA repair, nicks in double-stranded DNA. CC -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) + CC (deoxyribonucleotide)(m) = AMP + diphosphate + CC (deoxyribonucleotide)(n+m). CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family. 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; -. DR GeneID; 2541849; -. DR KEGG; spo:SPAC20G8.01; -. DR GeneDB_Spombe; SPAC20G8.01; -. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-001954-MONOMER; -. DR ArrayExpress; P12000; -. DR GO; GO:0005739; C:mitochondrion; IDA:GeneDB_SPombe. DR GO; GO:0005634; C:nucleus; IDA:GeneDB_SPombe. DR GO; GO:0005657; C:replication fork; IC:GeneDB_SPombe. DR GO; GO:0003910; F:DNA ligase (ATP) activity; IGI:GeneDB_SPombe. DR GO; GO:0005515; F:protein binding; IPI:GeneDB_SPombe. DR GO; GO:0043137; P:DNA replication, removal of RNA primer; TAS:GeneDB_SPombe. DR GO; GO:0000723; P:telomere maintenance; IMP:GeneDB_SPombe. 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; 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 2: Evidence at transcript level; KW ATP-binding; Cell cycle; Cell division; Complete proteome; DNA damage; KW DNA recombination; DNA repair; DNA replication; Ligase; KW Nucleotide-binding; Nucleus. FT CHAIN 1 768 DNA ligase. FT /FTId=PRO_0000059585. FT ACT_SITE 416 416 N6-AMP-lysine intermediate (By FT similarity). 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 //