GenomeNet

Database: UniProt
Entry: Q869E1
LinkDB: Q869E1
Original site: Q869E1 
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   07-JUN-2017, entry version 100.
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; Mycetozoa; Dictyosteliida; 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.,
RA   Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G.,
RA   Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A.,
RA   Platzer M., Rosenthal A., 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.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   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.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   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
CC       during DNA replication, DNA recombination and DNA repair.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000255|PROSITE-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}.
DR   EMBL; AAFI02000012; EAL70139.1; -; Genomic_DNA.
DR   RefSeq; XP_644124.1; XM_639032.1.
DR   ProteinModelPortal; Q869E1; -.
DR   SMR; Q869E1; -.
DR   STRING; 44689.DDB0232265; -.
DR   PaxDb; 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   eggNOG; COG1793; LUCA.
DR   InParanoid; Q869E1; -.
DR   KO; K10747; -.
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   Proteomes; UP000002195; Unassembled WGS sequence.
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:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:1903461; P:Okazaki fragment processing involved in mitotic DNA replication; IBA:GO_Central.
DR   Gene3D; 1.10.3260.10; -; 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; 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; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN         1   1192       DNA ligase 1.
FT                                /FTId=PRO_0000351214.
FT   REGION      724    733       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   REGION      918    920       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   COMPBIAS     11    468       Lys-rich.
FT   COMPBIAS     13    512       Glu-rich.
FT   COMPBIAS    171    201       Asp-rich.
FT   COMPBIAS    395    425       Thr-rich.
FT   ACT_SITE    844    844       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135}.
FT   METAL       897    897       Magnesium 1. {ECO:0000250}.
FT   METAL       996    996       Magnesium 2. {ECO:0000250}.
FT   BINDING     842    842       ATP. {ECO:0000250}.
FT   BINDING     849    849       ATP. {ECO:0000250}.
FT   BINDING     865    865       ATP. {ECO:0000250}.
FT   BINDING    1001   1001       ATP. {ECO:0000250}.
FT   BINDING    1014   1014       ATP. {ECO:0000250}.
FT   BINDING    1020   1020       ATP. {ECO:0000250}.
FT   SITE        580    580       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   SITE        866    866       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   SITE       1046   1046       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   SITE       1071   1071       Interaction with target DNA.
FT                                {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
//
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