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Database: UniProt
Entry: Q9W1H4
LinkDB: Q9W1H4
Original site: Q9W1H4 
ID   DNLI1_DROME             Reviewed;         747 AA.
AC   Q9W1H4; Q960P4;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   24-JAN-2024, entry version 181.
DE   RecName: Full=DNA ligase 1;
DE            EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE   AltName: Full=DNA ligase I;
DE            Short=DmDNA Lig I;
GN   Name=DNAlig1 {ECO:0000312|FlyBase:FBgn0262619};
GN   Synonyms=DNA-ligI {ECO:0000303|PubMed:17937809};
GN   ORFNames=CG5602 {ECO:0000312|FlyBase:FBgn0262619};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17937809; DOI=10.1186/1471-2121-8-42;
RA   Easwaran H.P., Leonhardt H., Cardoso M.C.;
RT   "Distribution of DNA replication proteins in Drosophila cells.";
RL   BMC Cell Biol. 8:42-42(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=17372656; DOI=10.1039/b617545g;
RA   Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA   Eng J.K., Aebersold R., Tao W.A.;
RT   "An integrated chemical, mass spectrometric and computational strategy for
RT   (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT   Kc167 cells.";
RL   Mol. Biosyst. 3:275-286(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-20; SER-42; SER-44;
RP   SER-46; SER-60 AND SER-65, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17937809}. Note=Does
CC       not accumulate at the replication foci (RF).
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
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DR   EMBL; AE013599; AAF47090.3; -; Genomic_DNA.
DR   EMBL; AY051939; AAK93363.1; -; mRNA.
DR   EMBL; BT016103; AAV36988.1; -; mRNA.
DR   RefSeq; NP_611843.2; NM_137999.3.
DR   AlphaFoldDB; Q9W1H4; -.
DR   SMR; Q9W1H4; -.
DR   BioGRID; 63384; 2.
DR   IntAct; Q9W1H4; 1.
DR   STRING; 7227.FBpp0072041; -.
DR   iPTMnet; Q9W1H4; -.
DR   PaxDb; 7227-FBpp0072041; -.
DR   DNASU; 37791; -.
DR   EnsemblMetazoa; FBtr0072132; FBpp0072041; FBgn0262619.
DR   GeneID; 37791; -.
DR   KEGG; dme:Dmel_CG5602; -.
DR   UCSC; CG5602-RA; d. melanogaster.
DR   AGR; FB:FBgn0262619; -.
DR   CTD; 37791; -.
DR   FlyBase; FBgn0262619; DNAlig1.
DR   VEuPathDB; VectorBase:FBgn0262619; -.
DR   eggNOG; KOG0967; Eukaryota.
DR   GeneTree; ENSGT00940000157783; -.
DR   HOGENOM; CLU_005138_4_2_1; -.
DR   InParanoid; Q9W1H4; -.
DR   OMA; WIKYKRD; -.
DR   OrthoDB; 961at2759; -.
DR   PhylomeDB; Q9W1H4; -.
DR   Reactome; R-DME-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR   Reactome; R-DME-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR   Reactome; R-DME-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR   Reactome; R-DME-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-DME-69183; Processive synthesis on the lagging strand.
DR   BioGRID-ORCS; 37791; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 37791; -.
DR   PRO; PR:Q9W1H4; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0262619; Expressed in secondary oocyte and 18 other cell types or tissues.
DR   Genevisible; Q9W1H4; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
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; IDA:FlyBase.
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   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   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; DNA damage; DNA recombination;
KW   DNA repair; DNA replication; Ligase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..747
FT                   /note="DNA ligase 1"
FT                   /id="PRO_0000372657"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          725..747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..84
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        725..741
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        395
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10135"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         44
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         60
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         65
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17372656,
FT                   ECO:0000269|PubMed:18327897"
FT   CONFLICT        361..387
FT                   /note="Missing (in Ref. 3; AAK93363)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   747 AA;  84719 MW;  9203F51CFFE3EF1D CRC64;
     MQKSITSFFK KKSDATDSPS PPKKVPKIDA KTELPDEPHI KSESASPETK PKVEPMSVDS
     EEKTSPVKNV KKEPKEVDDK TTDKKVTTIG LNSTAATKED VENYDPSADS YHPLKNAYWK
     DKKVTPYLAL ARTFQVIEET KGRLKMIDTL SNFFCSVMLV SPEDLVPSVY LSINQLAPAY
     EGLELGVAET TLMKAICKAT GRNLAHIKSQ TQLTGDLGIV AEQSRVSQRM MFQPAPLNVR
     DVFRKLREIA KLSGQSKMDL VYNMFVACRS SEARFFIRSL IGKLRIGIAE QSLLTALAIG
     LVKKNHIDDC KASKVPDVYK DEIVDTTLLL KTAYCQCPNY DIIIPAILKY DIKELQERCP
     MHPGMPLRPM LAQPTKGVHE VFERFGGMQI TCEWKYDGER AQIHRNEKGE ISIFSRNSEN
     NTAKYPDLIA RSTALLKGDV KSYIIDSEIV AWDVERKQIL PFQVLSTRKR KNVDIEEIKV
     QVCVYIFDLL YINGTALVTK NLSERRKLLL EHFQEVEGEW KFATALDTND IDEVQQFLEE
     SIKGNCEGLM VKTLDEEATY EIAKRSRNWL KLKKDYLSNV GDSLDLVVIG GYKGKGRRTG
     TYGGFLLACY DTENEEYQSI CKIGTGFTDE DLQTHSEFLG KHVTSAAKSY YRYDPSLEPD
     HWFEPVQVWE VKCADLSLSP IHRAAIGIVD GERGISLRFP RFIRIRDDKN SENATDANQV
     AHMYQSQDQV KNNQKSSTQM EMEDEFY
//
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