DNLI1_XENLA
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 03-AUG-2022, entry version 104.
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 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; 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 PRIDE; P51892; -.
DR GeneID; 397978; -.
DR KEGG; xla:397978; -.
DR CTD; 397978; -.
DR Xenbase; XB-GENE-1009783; lig1.L.
DR OrthoDB; 274264at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 397978; Expressed in egg cell and 19 other 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 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 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
