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Database: UniProt/SWISS-PROT
Entry: DNLI4_SCHPO
LinkDB: DNLI4_SCHPO
Original site: DNLI4_SCHPO 
ID   DNLI4_SCHPO             Reviewed;         913 AA.
AC   O74833;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 3.
DT   05-JUL-2017, entry version 121.
DE   RecName: Full=DNA ligase 4;
DE            EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE   AltName: Full=DNA ligase IV;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4;
GN   Name=lig4; ORFNames=SPCC1183.05c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
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.,
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   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K.,
RA   Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.,
RA   Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L.,
RA   FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D.,
RA   Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M.,
RA   Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M.,
RA   Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D.,
RA   Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H.,
RA   Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
RP   FUNCTION.
RX   PubMed=11029034; DOI=10.1091/mbc.11.10.3265;
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).
RN   [4]
RP   FUNCTION.
RX   PubMed=11172711; DOI=10.1016/S1097-2765(01)00154-X;
RA   Ferreira M.G., Cooper J.P.;
RT   "The fission yeast Taz1 protein protects chromosomes from Ku-dependent
RT   end-to-end fusions.";
RL   Mol. Cell 7:55-63(2001).
RN   [5]
RP   FUNCTION.
RX   PubMed=15226425; DOI=10.1128/MCB.24.14.6215-6230.2004;
RA   Nakamura T.M., Du L.-L., Redon C., Russell P.;
RT   "Histone H2A phosphorylation controls Crb2 recruitment at DNA breaks,
RT   maintains checkpoint arrest, and influences DNA repair in fission
RT   yeast.";
RL   Mol. Cell. Biol. 24:6215-6230(2004).
CC   -!- FUNCTION: Involved in ds DNA break repair.
CC       {ECO:0000269|PubMed:11029034, ECO:0000269|PubMed:11172711,
CC       ECO:0000269|PubMed:15226425}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000255|PROSITE-ProRule:PRU10135}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
DR   EMBL; CU329672; CAA21085.3; -; Genomic_DNA.
DR   PIR; T40845; T40845.
DR   RefSeq; NP_587888.2; NM_001022880.2.
DR   ProteinModelPortal; O74833; -.
DR   SMR; O74833; -.
DR   BioGrid; 275615; 6.
DR   STRING; 4896.SPCC1183.05c.1; -.
DR   PRIDE; O74833; -.
DR   EnsemblFungi; SPCC1183.05c.1; SPCC1183.05c.1:pep; SPCC1183.05c.
DR   GeneID; 2539042; -.
DR   KEGG; spo:SPCC1183.05c; -.
DR   EuPathDB; FungiDB:SPCC1183.05c; -.
DR   PomBase; SPCC1183.05c; lig4.
DR   InParanoid; O74833; -.
DR   KO; K10777; -.
DR   OMA; HMCPSTK; -.
DR   OrthoDB; EOG092C18KW; -.
DR   PRO; PR:O74833; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0032807; C:DNA ligase IV complex; IPI:PomBase.
DR   GO; GO:0000790; C:nuclear chromatin; IDA:PomBase.
DR   GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IC:PomBase.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; ISO:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IBA:GO_Central.
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 nonhomologous end joining; IBA:GO_Central.
DR   GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IBA:GO_Central.
DR   Gene3D; 3.40.50.10190; -; 2.
DR   InterPro; IPR001357; BRCT_dom.
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; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR10459:SF84; PTHR10459:SF84; 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   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52113; SSF52113; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS50172; BRCT; 2.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; DNA damage; DNA recombination;
KW   DNA repair; DNA replication; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Nucleus; Reference proteome; Repeat.
FT   CHAIN         1    913       DNA ligase 4.
FT                                /FTId=PRO_0000059581.
FT   DOMAIN      660    753       BRCT 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   DOMAIN      821    913       BRCT 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   ACT_SITE    281    281       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135}.
FT   METAL       341    341       Magnesium 1. {ECO:0000255}.
FT   METAL       438    438       Magnesium 2. {ECO:0000255}.
FT   BINDING     279    279       ATP. {ECO:0000250}.
FT   BINDING     286    286       ATP. {ECO:0000250}.
FT   BINDING     301    301       ATP. {ECO:0000250}.
FT   BINDING     443    443       ATP. {ECO:0000250}.
FT   BINDING     454    454       ATP. {ECO:0000250}.
FT   BINDING     460    460       ATP. {ECO:0000250}.
SQ   SEQUENCE   913 AA;  106025 MW;  18891DCE634EB752 CRC64;
     MDEAKETVFT KPQNHSSTLE FYDFVTTLLE PLSRIGKTRK SKTSNLDPYE LKRKILLDYF
     NKWRQHVGPD LYPLLRLMLP DLDRERGSYG FKEFGLGKLF IRAMHLSPTS EDAKSLKNWR
     GSESKHTGDF STMLQDILQR RAYRTFPGAF TVGDVNALLD QLADASSEDT RVNILEQFYR
     SLSPLELRWL IPILLKVRKY GTSEKFILSV FHPDAARLYR LCSSLKRICW ELYDPSRSLD
     ETETDVEVFS CFQPQLANFK KKDLHQTLEA MGNKPFWIEE KLDGERIQLH MSSGKFQFYS
     RNARSYTYAY GSSYFDEQSR LTQYIIGAFD KRISQIILDG EMVTWDPVLE TVIPYGSLRS
     IFEDSSSHSS YSPYYVVFDI LYLNGKSLVK YSLESRRRIL EKVIVRESHR MSILPYKVGS
     TIEDIEAELR NVIQEGSEGL VIKKPSGSYH LGERMDDWIK VKPYYLQGFG EDLDCLILGG
     YFGRGKQSGK INSFLCGLRM DYTPKDHSEK FQSFVRVGGG FTYFDRDIIR KETEGKWLPW
     SSDALEYMEL AGTKQDFEKP DMWIHPKDSL VLQIKAAEVV VSNRFKTNYT LRFPRLEKVR
     LDRSWKDALT INEFFTLKNA VEKQDNVSFH VNKKRKVSQK REKQKKFLYD EPTFKKEASP
     HSDVLKNLHF VVLPPTELHE TKAGLQQIII ENGGLIHQGV GNFGKERLFL VADRVSTRVS
     IERSKNMCTI IRSQWVMDSV NNQRLMPQWS YLLFSKDEKY SWKTALESLS AKSLSNLLVE
     LKQLDLSKEY SKISDDTSIL NLTISKEEAS FVGAFPFLKF TVFLDLKGIE NSELYDVRMG
     QYRLTKCILL WNGATIEKDI SSKKLTHVVM FVEDSTRLEQ LTKACELYQI EPKFVNFEWV
     VNEWKKASTN ILG
//
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