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 03-AUG-2022, entry version 142.
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; Schizosaccharomycetaceae;
OC 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., 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).
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., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., 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 end-
RT 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 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:
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 {ECO:0000250}.
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; CU329672; CAA21085.3; -; Genomic_DNA.
DR PIR; T40845; T40845.
DR RefSeq; NP_587888.2; NM_001022880.2.
DR AlphaFoldDB; O74833; -.
DR SMR; O74833; -.
DR BioGRID; 275615; 7.
DR STRING; 4896.SPCC1183.05c.1; -.
DR iPTMnet; O74833; -.
DR PaxDb; O74833; -.
DR PRIDE; O74833; -.
DR EnsemblFungi; SPCC1183.05c.1; SPCC1183.05c.1:pep; SPCC1183.05c.
DR GeneID; 2539042; -.
DR KEGG; spo:SPCC1183.05c; -.
DR PomBase; SPCC1183.05c; lig4.
DR VEuPathDB; FungiDB:SPCC1183.05c; -.
DR eggNOG; KOG0966; Eukaryota.
DR HOGENOM; CLU_004844_1_1_1; -.
DR InParanoid; O74833; -.
DR OMA; FYPVLRI; -.
DR PRO; PR:O74833; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0032807; C:DNA ligase IV complex; IPI:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
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; IEA:InterPro.
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 CDD; cd07903; Adenylation_DNA_ligase_IV; 1.
DR Gene3D; 1.10.3260.10; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.10190; -; 2.
DR InterPro; IPR044125; Adenylation_DNA_ligase_IV.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
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; IPR029710; LIG4.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR45997; PTHR45997; 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; DNA damage; DNA recombination; DNA repair; DNA replication;
KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..913
FT /note="DNA ligase 4"
FT /id="PRO_0000059581"
FT DOMAIN 660..753
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 821..913
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT ACT_SITE 281
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10135"
FT BINDING 279
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 438
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 443
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="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
