DNLI1_DICDI
ID DNLI1_DICDI Reviewed; 1192 AA.
AC Q869E1; Q556E8;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
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; ORFNames=DDB_G0274493;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000012; EAL70139.1; -; Genomic_DNA.
DR RefSeq; XP_644124.1; XM_639032.1.
DR AlphaFoldDB; Q869E1; -.
DR SMR; Q869E1; -.
DR STRING; 44689.DDB0232265; -.
DR REBASE; 165447; Fba101ORF1712P.
DR PaxDb; Q869E1; -.
DR PRIDE; Q869E1; -.
DR EnsemblProtists; EAL70139; EAL70139; DDB_G0274493.
DR GeneID; 8619554; -.
DR KEGG; ddi:DDB_G0274493; -.
DR dictyBase; DDB_G0274493; lig1.
DR eggNOG; KOG0967; Eukaryota.
DR HOGENOM; CLU_005138_0_1_1; -.
DR InParanoid; Q869E1; -.
DR PhylomeDB; Q869E1; -.
DR Reactome; R-DDI-110362; POLB-Dependent Long Patch Base Excision Repair.
DR Reactome; R-DDI-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR Reactome; R-DDI-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR Reactome; R-DDI-69183; Processive synthesis on the lagging strand.
DR PRO; PR:Q869E1; -.
DR Proteomes; UP000002195; Chromosome 2.
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 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..1192
FT /note="DNA ligase 1"
FT /id="PRO_0000351214"
FT REGION 29..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..733
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT REGION 918..920
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT REGION 1157..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..111
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..197
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..508
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1165..1182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 844
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10135"
FT BINDING 842
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 849
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 865
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 897
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 996
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1001
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 1014
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 1020
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 580
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT SITE 866
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT SITE 1046
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
FT SITE 1071
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1192 AA; 137514 MW; B52A5842CD779766 CRC64;
MQSSMWSFLQ KKEGGEIEDI EKKISNAQEL NKLKTSPKKK REAVVKEKVE KKEKKETKPK
RKSSKKNKEE EEEEEQEEQD GEEEQEEEEE YQQQDEEIEE DINGEEEMEL DENEKEKNKK
KKQSLKTKEN KESKSSSSSK KTIENKETKK PEKQSSKQSN NLKRLKRKKM DDDEEDEEDE
NKTDDNDLDD MLDDDSDNEK DSISSKDKEY KEKVLKDKEK KEKEKKEKEL KEKESKEKEK
KEKEKKEKEE KDKKEKELKE KELKEKELKD KKEKELKEKE KELKDKEKKE KELKEKEKKE
KEEKEKEKKE KKEKELKEKE EKEKKEKELK EKELKEKELK EKELKEKELT SPKKETIDIS
DLFKRANAEA KSSVPTSTSK NSKTNKKQKV DHKPTATTKK PSPVLEAKQS TTTTTTTTTT
STATTISSKS ISSPSKKEEK EVITSKKQVE ATKVEVKKEK EKEKEKEKED DEEEEEEEED
DDEKLEDIDE EEYEEEEEED EEGISENEEE EEKKSTQIKS KFIKKVPISK KKGNAKTIQA
DLKVIGKYRP IEDAQWKKGE AVPYMVLAKT FEMMESTSSR LIIIEHLANL FRSIMLLSPK
DLVMTIYLSI NKIGPSYQSK ELGIGEHVLI KSLAESTGRS VDVIKQELTE VGDLGIIAQN
SRSTQTLMGK PTPLTIQSVF KTFQQIADLS GTGGQQKKKD LIKKLLVSCK DCETLYIIRS
LQGKLRIGLA ERSVLMALAK SVLVTPPIDG SGQQIFDIRK QMKQEEFEER YQNVVSKVTR
AYSQLPNYDL FVPHLIAVNG IDNILSTCSL KVGIPVKPML AQPTTGISQM LDRFSDMEFT
CEFKYDGERA QIHRLPDGTT HIYTRNLEDY TQKYPDIVAN VTKFVGPNVK SFILDCEAVA
FDAATKKILS FQVLSTRARK SVQLSQIKVP VCVFAFDLLY LNGQSLIDEP LIKRREHLVE
NFIASDGVFA FAKYSNISDV NDIQSYLEEA VEGNCEGLMV KTLKEKSIYE PSRRSYNWLK
IKKDYMQGMT DSLDLVPIGA WYGKGKRTGT YGAYLLACYD ENNEEFQTLC KIGTGFSDEQ
LTTFTSQLKP HLINQPRNQF RFSDSIKPDV WFSPSCVWEV LAADLSISPV HTAASGILDP
NKGIALRFPR FIRIRPDKSP EDATSSDQVV DMYQNQKINS QSSKINEKDE DY
