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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
 
 
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