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Database: UniProt
Entry: P51892
LinkDB: P51892
Original site: P51892 
ID   DNLI1_XENLA             Reviewed;        1070 AA.
AC   P51892;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 109.
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=lig1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8682316; DOI=10.1016/0378-1119(96)00175-8;
RA   Lepetit D., Thiebaud P., Aoufouchi S., Prigent C., Guesne R., Theze N.;
RT   "The cloning and characterization of a cDNA encoding Xenopus laevis DNA
RT   ligase I.";
RL   Gene 172:273-277(1996).
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; 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; L43496; AAB37754.1; -; mRNA.
DR   PIR; JC4852; JC4852.
DR   RefSeq; NP_001081653.1; NM_001088184.1.
DR   AlphaFoldDB; P51892; -.
DR   SMR; P51892; -.
DR   GeneID; 397978; -.
DR   KEGG; xla:397978; -.
DR   CTD; 397978; -.
DR   Xenbase; XB-GENE-1009783; lig1.L.
DR   OrthoDB; 961at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 397978; Expressed in egg cell and 19 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; 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:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   2: Evidence at transcript level;
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..1070
FT                   /note="DNA ligase 1"
FT                   /id="PRO_0000059573"
FT   REGION          1..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..611
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          795..797
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        15..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..253
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..284
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..301
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..354
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..395
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        721
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10135"
FT   BINDING         719
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P18858"
FT   BINDING         726
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P18858"
FT   BINDING         774
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P18858"
FT   BINDING         774
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         873
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         878
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P18858"
FT   BINDING         897
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P18858"
FT   SITE            458
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   SITE            743
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   SITE            923
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   SITE            948
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1070 AA;  120234 MW;  065D6E5B8C6E4E52 CRC64;
     MQRTIKSFFQ PKLGAEVKTK EEKVKNDVQK EKEEPEKSVP ERPLKERNGR ALCGDTESPV
     KRVSKKSARV LESDSEEEEE NSKVQATPEK MNNESDPKND VKETPPSARK ETPPSARKET
     PPSARKETPQ SARKETPPSA RKDAKSEGAS EMNTSQDFVS PCSSKSIDSP LCSDSPGISP
     SGIPKRKTAR KQLPKRKLEI SPSESNPPKD DFDVKGAVKR QKKEAEGDIQ QEEPMETSHN
     ISMEEECPIK KETNPDVVQE TISNADDPNI ELVDQKDVVS GEKQSEPKCQ EQPQPKLTSP
     TVEPKASKGK ARKKNSPLPK KVKFSDKVSF KDNDSEEKSN EEKSDEEPQK KADSAKPVKQ
     ISSFFAPRKP AIKTEKREEN LNEKNVTETS LEESPKPKKN VGSFFGASKQ EATEEQTEYN
     PSKSKYHPID DACWCNGQKV PYLAVARTFE RIEEESARLK NVETLSNFLR SVIALTPEDL
     LPCIYLCLNR LGPAYEGLEL GIGETILMKA VAQATGRQLE KIKAEAQEKG DLGLVAESSR
     SNQRTMFTPP KLMASGVFGK LKDIARMTGN ASMNKKIDII KGLFVACRHS EARYIARSLG
     GKLRIGLAEQ SVLSSIAQAV CLTPPGRDAP PTVMDAGKGM SADARKSWIE EKAMILKQTF
     CELPNYDAII PILLEHGIDD LPKHCRLTPG IPLKPMLAHP TKGIGEVLKR FDEAAFTCEY
     KYDGERAQIH ILENGEVHVY SRNQENNTTK YPDIISRIPK IKKESVKSCI LDTEAVAGDA
     EKKQIQPFQV LTTRKRKDVD ASEIKVQVCV YAFDMLYLNG ESLVKEPFAK RRQLLRDSFL
     ETEGQFMFAT YMDKSNTDEI SEFLDQSIKD SCEGLMVKTL EQDATYEIAK RSHNWLKLKK
     DYLEGVGDTL DLVVIGAYLG KGKRTGIYGG FLLASYDEES EEYQTICKIG TGFTDDDLEK
     HYNFLKDHVI ENPRSYYRWD SATEPDHWFD PVQVWEVKCA DLSISPVHKA ALGLVEDQKG
     ISLRFPRFLR IRDDKKPEES TNSFQVADLY RKQQQIQNTS STEKAEEDFY
//
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