ID DNLI4_SCHPO Reviewed; 923 AA. AC O74833; DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 2. DT 16-JUN-2009, entry version 51. DE RecName: Full=DNA ligase 4; DE EC=6.5.1.1; DE AltName: Full=DNA ligase IV; DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4; GN Name=lig4; ORFNames=SPCC1183.05c; 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 [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). RN [2] RP FUNCTION. RX PubMed=11029034; RA Baumann P., Cech T.R.; RT "Protection of telomeres by the Ku protein in fission yeast."; RL Mol. Biol. Cell 11:3265-3275(2000). CC -!- FUNCTION: Involved in ds DNA break repair. CC -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) + CC (deoxyribonucleotide)(m) = AMP + diphosphate + CC (deoxyribonucleotide)(n+m). CC -!- COFACTOR: Magnesium (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family. CC -!- SIMILARITY: Contains 1 BRCT domain. 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; CU329672; CAA21085.2; -; Genomic_DNA. DR PIR; T40845; T40845. DR RefSeq; NP_587888.1; -. DR GeneID; 2539042; -. DR KEGG; spo:SPCC1183.05c; -. DR NMPDR; fig|4896.1.peg.226; -. DR GeneDB_Spombe; SPCC1183.05c; -. DR OMA; O74833; RRLKDYS. DR BRENDA; 6.5.1.1; 653. DR ArrayExpress; O74833; -. DR GO; GO:0032807; C:DNA ligase IV complex; TAS:GeneDB_SPombe. DR GO; GO:0005524; F:ATP binding; IC:GeneDB_SPombe. DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0006303; P:double-strand break repair via nonhomologou...; IMP:GeneDB_SPombe. DR InterPro; IPR001357; BRCT. DR InterPro; IPR000977; DNA_ligase. DR InterPro; IPR012309; DNA_ligase_A_C. DR InterPro; IPR012310; DNA_ligase_A_M. 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; PF00533; BRCT; 1. DR Pfam; PF04679; DNA_ligase_A_C; 1. DR Pfam; PF01068; DNA_ligase_A_M; 1. DR TIGRFAMs; TIGR00574; dnl1; 1. DR PROSITE; PS50172; BRCT; 1. DR PROSITE; PS00697; DNA_LIGASE_A1; 1. DR PROSITE; PS00333; DNA_LIGASE_A2; FALSE_NEG. DR PROSITE; PS50160; DNA_LIGASE_A3; 1. PE 2: Evidence at transcript level; KW ATP-binding; Complete proteome; DNA damage; DNA recombination; KW DNA repair; DNA replication; Ligase; Magnesium; Metal-binding; KW Nucleotide-binding; Nucleus. FT CHAIN 1 923 DNA ligase 4. FT /FTId=PRO_0000059581. FT DOMAIN 674 767 BRCT. FT ACT_SITE 295 295 N6-AMP-lysine intermediate (By FT similarity). FT METAL 355 355 Magnesium 1 (Potential). FT METAL 452 452 Magnesium 2 (Potential). FT BINDING 293 293 ATP (By similarity). FT BINDING 300 300 ATP (By similarity). FT BINDING 315 315 ATP (By similarity). FT BINDING 457 457 ATP (By similarity). FT BINDING 468 468 ATP (By similarity). FT BINDING 474 474 ATP (By similarity). SQ SEQUENCE 923 AA; 107259 MW; 6ED79683AB57DCE0 CRC64; MDEAKETVFT KPQNHSSTLE FYDFVTTLLE PLSRIGKTRK SKTSNLDPYE LKRKILLDYF NKWRQHVGPD LYPLLRLSNL IFLDRERGSY GFKEFGLGKL FIRAMHLSPT SEDAKSLKNW RGSESKHTGD FSTMLQDILQ RRAYRTFPGA FTVGDVNALL DQLADASSEY VLNFLPYLTL IRDTRVNILE QFYRSLSPLE LRWLIPILLK VRKYGTSEKF ILSVFHPDAA RLYRLCSSLK RICWELYDPS RSLDETETDV EVFSCFQPQL ANFKKKDLHQ TLEAMGNKPF WIEEKLDGER IQLHMSSGKF QFYSRNARSY TYAYGSSYFD EQSRLTQYII GAFDKRISQI ILDGEMVTWD PVLETVIPYG SLRSIFEDSS SHSSYSPYYV VFDILYLNGK SLVKYSLESR RRILEKVIVR ESHRMSILPY KVGSTIEDIE AELRNVIQEG SEGLVIKKPS GSYHLGERMD DWIKVKPYYL QGFGEDLDCL ILGGYFGRGK QSGKINSFLC GLRMDYTPKD HSEKFQSFVR VGGGFTYFDR DIIRKETEGK WLPWSSDALE YMELAGTKQD FEKPDMWIHP KDSLVLQIKA AEVVVSNRFK TNYTLRFPRL EKVRLDRSWK DALTINEFFT LKNAVEKQDN VSFHVNKKRK VSQKREKQKK FLYDEPTFKK EASPHSDVLK NLHFVVLPPT ELHETKAGLQ QIIIENGGLI HQGVGNFGKE RLFLVADRVS TRVSIERSKN MCTIIRSQWV MDSVNNQRLM PQWSYLLFSK DEKYSWKTAL ESLSAKSLSN LLVELKQLDL SKEYSKISDD TSILNLTISK EEASFVGAFP FLKFTVFLDL KGIENSELYD VRMGQYRLTK CILLWNGATI EKDISSKKLT HVVMFVEDST RLEQLTKACE LTQHRKFTQP SYFQRYGGSF CIP //