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Database: UniProt
Entry: Q9JHY8
LinkDB: Q9JHY8
Original site: Q9JHY8 
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   08-NOV-2023, entry version 147.
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 during DNA
CC       repair. Also involved in DNA replication and DNA recombination.
CC       {ECO:0000250|UniProtKB:P18858}.
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. Interacts with POLB.
CC       {ECO:0000250|UniProtKB:P12004}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
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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; 10116-ENSRNOP00000019799; -.
DR   UCSC; RGD:621424; rat.
DR   AGR; RGD:621424; -.
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:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISO: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   CDD; cd07900; Adenylation_DNA_ligase_I_Euk; 1.
DR   CDD; cd07969; OBF_DNA_ligase_I; 1.
DR   Gene3D; 3.30.1490.70; -; 1.
DR   Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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   NCBIfam; TIGR00574; dnl1; 1.
DR   PANTHER; PTHR45674:SF4; DNA LIGASE 1; 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 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; ATP-dependent DNA ligase DNA-binding domain; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 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
//
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