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Database: UniProt/SWISS-PROT
Entry: DNLI1_SCHPO
LinkDB: DNLI1_SCHPO
Original site: DNLI1_SCHPO 
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   13-FEB-2019, entry version 153.
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;
OC   Schizosaccharomycetaceae; 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
RT   fission 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.,
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: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair.
CC       {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}.
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   ProteinModelPortal; P12000; -.
DR   SMR; P12000; -.
DR   BioGrid; 278340; 14.
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   HOGENOM; HOG000036006; -.
DR   InParanoid; P12000; -.
DR   KO; K10747; -.
DR   OMA; WIKYKRD; -.
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; IEA:InterPro.
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; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN         1    768       DNA ligase 1.
FT                                /FTId=PRO_0000059585.
FT   REGION      309    318       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   REGION      490    492       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   ACT_SITE    416    416       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135}.
FT   METAL       469    469       Magnesium 1. {ECO:0000250}.
FT   METAL       568    568       Magnesium 2. {ECO:0000250}.
FT   BINDING     414    414       ATP. {ECO:0000250}.
FT   BINDING     421    421       ATP. {ECO:0000250}.
FT   BINDING     437    437       ATP. {ECO:0000250}.
FT   BINDING     573    573       ATP. {ECO:0000250}.
FT   BINDING     587    587       ATP. {ECO:0000250}.
FT   BINDING     593    593       ATP. {ECO:0000250}.
FT   SITE        165    165       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   SITE        438    438       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   SITE        619    619       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   SITE        644    644       Interaction with target DNA.
FT                                {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
//
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