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 03-AUG-2022, entry version 170.
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; Schizosaccharomycetaceae;
OC 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 fission
RT 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., 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).
CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA
CC replication, DNA recombination and DNA repair. {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}.
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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 AlphaFoldDB; P12000; -.
DR SMR; P12000; -.
DR BioGRID; 278340; 21.
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 PomBase; SPAC20G8.01; cdc17.
DR VEuPathDB; FungiDB:SPAC20G8.01; -.
DR eggNOG; KOG0967; Eukaryota.
DR HOGENOM; CLU_005138_4_2_1; -.
DR InParanoid; P12000; -.
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: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 Gene3D; 2.40.50.140; -; 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; DNA damage; DNA recombination;
KW DNA repair; DNA replication; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..768
FT /note="DNA ligase 1"
FT /id="PRO_0000059585"
FT REGION 42..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..318
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT REGION 490..492
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT COMPBIAS 55..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 416
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10135"
FT BINDING 414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 421
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 568
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 573
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 587
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 593
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 165
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT SITE 438
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT SITE 619
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT SITE 644
FT /note="Interaction with target DNA"
FT /evidence="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
