Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9W1H4

- DNLI1_DROME

UniProt

Q9W1H4 - DNLI1_DROME

Protein

DNA ligase 1

Gene

DNA-ligI

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (01 Oct 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.By similarity

    Catalytic activityi

    ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei395 – 3951N6-AMP-lysine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: InterPro
    3. DNA ligase (ATP) activity Source: FlyBase

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: UniProtKB-KW
    3. DNA ligation involved in DNA repair Source: InterPro
    4. DNA recombination Source: UniProtKB-KW
    5. DNA replication Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Cell cycle, Cell division, DNA damage, DNA recombination, DNA repair, DNA replication

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_209581. Gap-filling DNA repair synthesis and ligation in GG-NER.
    REACT_210849. Removal of DNA patch containing abasic residue.
    REACT_213876. Resolution of D-loop structures through Holliday junction intermediates.
    REACT_221569. Processive synthesis on the lagging strand.
    REACT_224877. Gap-filling DNA repair synthesis and ligation in TC-NER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA ligase 1 (EC:6.5.1.1)
    Alternative name(s):
    DNA ligase I
    Short name:
    DmDNA Lig I
    Gene namesi
    Name:DNA-ligI
    ORF Names:CG5602
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0262619. DNA-ligI.

    Subcellular locationi

    Nucleus 1 Publication
    Note: Does not accumulate at the replication foci (RF).

    GO - Cellular componenti

    1. cytoplasm Source: FlyBase
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 747747DNA ligase 1PRO_0000372657Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei18 – 181Phosphoserine1 Publication
    Modified residuei20 – 201Phosphoserine1 Publication
    Modified residuei42 – 421Phosphoserine1 Publication
    Modified residuei44 – 441Phosphoserine1 Publication
    Modified residuei46 – 461Phosphoserine1 Publication
    Modified residuei60 – 601Phosphoserine1 Publication
    Modified residuei65 – 651Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9W1H4.

    Expressioni

    Gene expression databases

    BgeeiQ9W1H4.

    Interactioni

    Protein-protein interaction databases

    BioGridi63384. 2 interactions.
    IntActiQ9W1H4. 1 interaction.
    MINTiMINT-920323.
    STRINGi7227.FBpp0072041.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9W1H4.
    SMRiQ9W1H4. Positions 100-727.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATP-dependent DNA ligase family.Curated

    Phylogenomic databases

    eggNOGiCOG1793.
    GeneTreeiENSGT00750000117745.
    InParanoidiQ9W1H4.
    KOiK10747.
    OMAiMVKMLEG.
    OrthoDBiEOG7RFTGN.
    PhylomeDBiQ9W1H4.

    Family and domain databases

    Gene3Di1.10.3260.10. 1 hit.
    2.40.50.140. 1 hit.
    InterProiIPR000977. DNA_ligase_ATP-dep.
    IPR012309. DNA_ligase_ATP-dep_C.
    IPR012310. DNA_ligase_ATP-dep_cent.
    IPR016059. DNA_ligase_ATP-dep_CS.
    IPR012308. DNA_ligase_ATP-dep_N.
    IPR012340. NA-bd_OB-fold.
    [Graphical view]
    PfamiPF04679. DNA_ligase_A_C. 1 hit.
    PF01068. DNA_ligase_A_M. 1 hit.
    PF04675. DNA_ligase_A_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF117018. SSF117018. 1 hit.
    SSF50249. SSF50249. 1 hit.
    TIGRFAMsiTIGR00574. dnl1. 1 hit.
    PROSITEiPS00697. DNA_LIGASE_A1. 1 hit.
    PS00333. DNA_LIGASE_A2. 1 hit.
    PS50160. DNA_LIGASE_A3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9W1H4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQKSITSFFK KKSDATDSPS PPKKVPKIDA KTELPDEPHI KSESASPETK    50
    PKVEPMSVDS EEKTSPVKNV KKEPKEVDDK TTDKKVTTIG LNSTAATKED 100
    VENYDPSADS YHPLKNAYWK DKKVTPYLAL ARTFQVIEET KGRLKMIDTL 150
    SNFFCSVMLV SPEDLVPSVY LSINQLAPAY EGLELGVAET TLMKAICKAT 200
    GRNLAHIKSQ TQLTGDLGIV AEQSRVSQRM MFQPAPLNVR DVFRKLREIA 250
    KLSGQSKMDL VYNMFVACRS SEARFFIRSL IGKLRIGIAE QSLLTALAIG 300
    LVKKNHIDDC KASKVPDVYK DEIVDTTLLL KTAYCQCPNY DIIIPAILKY 350
    DIKELQERCP MHPGMPLRPM LAQPTKGVHE VFERFGGMQI TCEWKYDGER 400
    AQIHRNEKGE ISIFSRNSEN NTAKYPDLIA RSTALLKGDV KSYIIDSEIV 450
    AWDVERKQIL PFQVLSTRKR KNVDIEEIKV QVCVYIFDLL YINGTALVTK 500
    NLSERRKLLL EHFQEVEGEW KFATALDTND IDEVQQFLEE SIKGNCEGLM 550
    VKTLDEEATY EIAKRSRNWL KLKKDYLSNV GDSLDLVVIG GYKGKGRRTG 600
    TYGGFLLACY DTENEEYQSI CKIGTGFTDE DLQTHSEFLG KHVTSAAKSY 650
    YRYDPSLEPD HWFEPVQVWE VKCADLSLSP IHRAAIGIVD GERGISLRFP 700
    RFIRIRDDKN SENATDANQV AHMYQSQDQV KNNQKSSTQM EMEDEFY 747
    Length:747
    Mass (Da):84,719
    Last modified:October 1, 2002 - v2
    Checksum:i9203F51CFFE3EF1D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti361 – 38727Missing in AAK93363. (PubMed:12537569)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013599 Genomic DNA. Translation: AAF47090.3.
    AY051939 mRNA. Translation: AAK93363.1.
    BT016103 mRNA. Translation: AAV36988.1.
    RefSeqiNP_611843.2. NM_137999.2.
    UniGeneiDm.19278.

    Genome annotation databases

    EnsemblMetazoaiFBtr0072132; FBpp0072041; FBgn0262619.
    GeneIDi37791.
    KEGGidme:Dmel_CG5602.
    UCSCiCG5602-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013599 Genomic DNA. Translation: AAF47090.3 .
    AY051939 mRNA. Translation: AAK93363.1 .
    BT016103 mRNA. Translation: AAV36988.1 .
    RefSeqi NP_611843.2. NM_137999.2.
    UniGenei Dm.19278.

    3D structure databases

    ProteinModelPortali Q9W1H4.
    SMRi Q9W1H4. Positions 100-727.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 63384. 2 interactions.
    IntActi Q9W1H4. 1 interaction.
    MINTi MINT-920323.
    STRINGi 7227.FBpp0072041.

    Proteomic databases

    PaxDbi Q9W1H4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0072132 ; FBpp0072041 ; FBgn0262619 .
    GeneIDi 37791.
    KEGGi dme:Dmel_CG5602.
    UCSCi CG5602-RA. d. melanogaster.

    Organism-specific databases

    CTDi 37791.
    FlyBasei FBgn0262619. DNA-ligI.

    Phylogenomic databases

    eggNOGi COG1793.
    GeneTreei ENSGT00750000117745.
    InParanoidi Q9W1H4.
    KOi K10747.
    OMAi MVKMLEG.
    OrthoDBi EOG7RFTGN.
    PhylomeDBi Q9W1H4.

    Enzyme and pathway databases

    Reactomei REACT_209581. Gap-filling DNA repair synthesis and ligation in GG-NER.
    REACT_210849. Removal of DNA patch containing abasic residue.
    REACT_213876. Resolution of D-loop structures through Holliday junction intermediates.
    REACT_221569. Processive synthesis on the lagging strand.
    REACT_224877. Gap-filling DNA repair synthesis and ligation in TC-NER.

    Miscellaneous databases

    GenomeRNAii 37791.
    NextBioi 805425.
    PROi Q9W1H4.

    Gene expression databases

    Bgeei Q9W1H4.

    Family and domain databases

    Gene3Di 1.10.3260.10. 1 hit.
    2.40.50.140. 1 hit.
    InterProi IPR000977. DNA_ligase_ATP-dep.
    IPR012309. DNA_ligase_ATP-dep_C.
    IPR012310. DNA_ligase_ATP-dep_cent.
    IPR016059. DNA_ligase_ATP-dep_CS.
    IPR012308. DNA_ligase_ATP-dep_N.
    IPR012340. NA-bd_OB-fold.
    [Graphical view ]
    Pfami PF04679. DNA_ligase_A_C. 1 hit.
    PF01068. DNA_ligase_A_M. 1 hit.
    PF04675. DNA_ligase_A_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF117018. SSF117018. 1 hit.
    SSF50249. SSF50249. 1 hit.
    TIGRFAMsi TIGR00574. dnl1. 1 hit.
    PROSITEi PS00697. DNA_LIGASE_A1. 1 hit.
    PS00333. DNA_LIGASE_A2. 1 hit.
    PS50160. DNA_LIGASE_A3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    2. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    4. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    5. "Distribution of DNA replication proteins in Drosophila cells."
      Easwaran H.P., Leonhardt H., Cardoso M.C.
      BMC Cell Biol. 8:42-42(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    6. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
      Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
      Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, IDENTIFICATION BY MASS SPECTROMETRY.
    7. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-20; SER-42; SER-44; SER-46; SER-60 AND SER-65, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiDNLI1_DROME
    AccessioniPrimary (citable) accession number: Q9W1H4
    Secondary accession number(s): Q960P4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 5, 2009
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 123 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3