DNLI1_RAT
ID DNLI1_RAT Reviewed; 918 AA.
AC Q9JHY8;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=DNA ligase 1;
DE EC=6.5.1.1;
DE AltName: Full=DNA ligase I;
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;
GN Name=Lig1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Chen D., Cao G., Chen J.;
RT "Molecular cloning and characterization of rat DNA ligase I.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67 AND THR-78, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA
CC replication, DNA recombination and DNA repair.
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with PCNA. {ECO:0000250|UniProtKB:P12004}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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; AF276774; AAF82585.1; -; mRNA.
DR AlphaFoldDB; Q9JHY8; -.
DR SMR; Q9JHY8; -.
DR STRING; 10116.ENSRNOP00000019799; -.
DR iPTMnet; Q9JHY8; -.
DR PhosphoSitePlus; Q9JHY8; -.
DR jPOST; Q9JHY8; -.
DR PaxDb; Q9JHY8; -.
DR PRIDE; Q9JHY8; -.
DR UCSC; RGD:621424; rat.
DR RGD; 621424; Lig1.
DR eggNOG; KOG0967; Eukaryota.
DR InParanoid; Q9JHY8; -.
DR PhylomeDB; Q9JHY8; -.
DR PRO; PR:Q9JHY8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
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:0003909; F:DNA ligase activity; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006284; P:base-excision repair; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0006260; P:DNA replication; ISO:RGD.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISO:RGD.
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 GO; GO:0042542; P:response to hydrogen peroxide; ISO:RGD.
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; PS00333; DNA_LIGASE_A2; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell cycle; Cell division; DNA damage;
KW DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..918
FT /note="DNA ligase 1"
FT /id="PRO_0000059572"
FT REGION 1..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..644
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT REGION 881..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 568
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 566
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P18858"
FT BINDING 573
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P18858"
FT BINDING 621
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P18858"
FT BINDING 621
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 720
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 725
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P18858"
FT BINDING 744
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P18858"
FT SITE 305
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT SITE 590
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT SITE 770
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT SITE 795
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18858"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18858"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 78
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 145
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P37913"
FT MOD_RES 195
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18858"
FT MOD_RES 227
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P37913"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18858"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18858"
FT MOD_RES 234
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18858"
FT MOD_RES 798
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18858"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18858"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P37913"
FT MOD_RES 909
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P37913"
FT MOD_RES 913
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18858"
SQ SEQUENCE 918 AA; 102482 MW; B4ECA8861C521567 CRC64;
MQRSIMSFFQ PTTTEGKAKK PEKEIPSSIR EKEPPPKVAL KERNRAVPES DSPVKRPGRK
VAQVLSSEGE DEDEAPGTPQ VQKPVSDSKQ SSPPSPDSCP ENSPVFNCSP SMDISPSGFP
KRRTARKQLP KRTIQDTLEE PNEDKAKAVK KRKKEDPQTP PESLTEAEEV NQKEEQVEDQ
PTVPPEPTES PESVTLTKTE NIPMCKAGVK QKPQEEEQSK PPARGAKPLS SFFTPRKPAV
KTEVKQEESD TPRKEETKGA PDPTNYNPSK SNYHPIEDAC WKHGQKVPFL AVARTFEKIE
EVSARLKMVE TLSNLLRSVV ALSPTDLLPV LYLSLNRLGP PQQGLELGVG DGVLLKAVAQ
ATGRQLESIR AEVAEKGDVG LVAENSRSTQ RLMLPSPPLT VSGVFTKFCD IARLTGSASM
AKKMDIIKGL FVACRYSEAR FIARSLSGRL RLGLAEQSVL AALAQAGSLT PPGQEFPTVV
VDAGKGKTAE ARKMWLEEQG MILKQTFCEV PDLDRIIPVL LEHGLESLPE HCKLSPGVPL
KPMLAHPTRG VREVLKRFEE VDFTCEYKYY GQRAQIHVLE GGEVKIFSRN QEDNSGKYPD
IISRIPKIKH PSVTSFILDT EAVAWDREKK QIQPFQVLTT RKRKEVDASE IQVQVCLYAF
DLIYLNGESL ARQPLSRRRQ LLRENFVETE GEFVFATSLD TKDIEQIAEF LEQSVKDSCE
GLMVKTLDVD ATYEIAKRSH NWLKLKKDYL EGVGDTLDLV VIGAYLGRGK RPGRYGGFLL
AAYDEESEEL AAICKLGTGF SDEELEEHHQ NMQALLLPTP RPYVRIDGAV APNHWLDPSI
VWEVKCADLT LSPIYRAARG MVDKEKGISL RFPRFIRVRE DKQPEQATTS DQVASLYRKQ
SQIQNQQSSD LDSDVEDY
