DNLI1_CAEEL
ID DNLI1_CAEEL Reviewed; 773 AA.
AC Q27474; Q8MQB3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 159.
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=lig-1; ORFNames=C29A12.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q27474-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q27474-2; Sequence=VSP_013778, VSP_013779;
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000305}.
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DR EMBL; Z73970; CAA98242.2; -; Genomic_DNA.
DR EMBL; Z73970; CAD44112.2; -; Genomic_DNA.
DR PIR; T19544; T19544.
DR RefSeq; NP_741625.2; NM_171537.3. [Q27474-1]
DR RefSeq; NP_741626.2; NM_171538.3. [Q27474-2]
DR AlphaFoldDB; Q27474; -.
DR SMR; Q27474; -.
DR BioGRID; 44531; 7.
DR STRING; 6239.C29A12.3a; -.
DR iPTMnet; Q27474; -.
DR EPD; Q27474; -.
DR PaxDb; Q27474; -.
DR PeptideAtlas; Q27474; -.
DR PRIDE; Q27474; -.
DR EnsemblMetazoa; C29A12.3a.1; C29A12.3a.1; WBGene00002985. [Q27474-1]
DR EnsemblMetazoa; C29A12.3b.1; C29A12.3b.1; WBGene00002985. [Q27474-2]
DR GeneID; 179502; -.
DR KEGG; cel:CELE_C29A12.3; -.
DR UCSC; C29A12.3a; c. elegans. [Q27474-1]
DR CTD; 179502; -.
DR WormBase; C29A12.3a; CE37480; WBGene00002985; lig-1. [Q27474-1]
DR WormBase; C29A12.3b; CE37481; WBGene00002985; lig-1. [Q27474-2]
DR eggNOG; KOG0967; Eukaryota.
DR GeneTree; ENSGT00940000157783; -.
DR HOGENOM; CLU_005138_4_1_1; -.
DR InParanoid; Q27474; -.
DR OMA; WIKYKRD; -.
DR OrthoDB; 274264at2759; -.
DR PhylomeDB; Q27474; -.
DR Reactome; R-CEL-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR Reactome; R-CEL-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR Reactome; R-CEL-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-CEL-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-CEL-69183; Processive synthesis on the lagging strand.
DR PRO; PR:Q27474; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00002985; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR GO; GO:1903461; P:Okazaki fragment processing involved in mitotic DNA replication; IBA:GO_Central.
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 Alternative splicing; ATP-binding; Cell cycle; Cell division; DNA damage;
KW DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..773
FT /note="DNA ligase 1"
FT /id="PRO_0000059583"
FT REGION 180..189
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT REGION 362..364
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT REGION 626..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..651
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..773
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 289
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10135"
FT BINDING 287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P18858"
FT BINDING 294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P18858"
FT BINDING 342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P18858"
FT BINDING 342
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 444
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P18858"
FT BINDING 463
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P18858"
FT SITE 37
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT SITE 311
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT SITE 489
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT SITE 514
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT VAR_SEQ 208..210
FT /note="VRG -> RMP (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_013778"
FT VAR_SEQ 211..773
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_013779"
SQ SEQUENCE 773 AA; 86310 MW; 458B676F9FCE0BA0 CRC64;
MFFSKAGKAA VEWAKGSKVP YKEFALTLEK IEELSGKKKV DELAQFFTKV LDFSPDDLTA
CVYMSVNQLG PSYEGLELGV AENSLIKAVA KATGRTEGKI KEDLRAKGDL GTVAQQSRSN
QKMLAVPKAL TVPTVFNKLT EIAKLSGTSA MNKKVDAISA LLIACQGIEA RFLVRMLAGK
MRIGLGEQSV LSALGHAFTL SKITDQKVRG DKLDSLKDAN VKRVKTAYCE CPNYNRLIEV
ALTEGVEALV EKCKLSPGIP LKPMLAHPTK GIDEIMRRFR NQTMTCEWKY DGERGQIHKR
EDGQIFIYSR NQENNTTKYP DIIEKISSCI GDGVTSFIVD AEVVAIDEAG LILPFQVLST
RKRKNATDDN GVKVVVFLFD LLYFNGEPLV RKPLRKRREL LRTNFKKIDG SFYFATSVDT
NDTDEINSFF DEAVQNKCEG LMIKTLDTEA TYEISRRSHS WLKMKKDYVD GVGDTLDLVV
MGAYSGVGKR TGVYGGYLLG CYNPTTEEYE SVCKIGTGFT DEDLAEQYKI LQDKKIDKSP
SYYQFDHTLK PDDTFSPYLV FEVKCADITI SPRHKAASGL TDDGKGISLR FPRFLRIRDD
KNSDDATSSE QVLEMYKNQE AFANQKIEKA DAVDEDDEFE EKEDEEEELN MTNVSEGSSK
ENPVKEEIKK ETPKSVSPKK FEKKPPVKSS PVNKSPVKSS PIKKEAEKKK GPVASIFSSS
TKKNEKDVKV ESPSPIRKKK LPSDSDESDE ETSTNKKQPA KKRSRVAIDS DSD
