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Q9JHY8

- DNLI1_RAT

UniProt

Q9JHY8 - DNLI1_RAT

Protein

DNA ligase 1

Gene

Lig1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).

    Cofactori

    Magnesium.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei305 – 3051Interaction with target DNABy similarity
    Binding sitei566 – 5661ATPBy similarity
    Active sitei568 – 5681N6-AMP-lysine intermediateBy similarity
    Binding sitei573 – 5731ATPBy similarity
    Binding sitei589 – 5891ATPBy similarity
    Sitei590 – 5901Interaction with target DNABy similarity
    Metal bindingi621 – 6211Magnesium 1By similarity
    Metal bindingi720 – 7201Magnesium 2By similarity
    Binding sitei725 – 7251ATPBy similarity
    Binding sitei738 – 7381ATPBy similarity
    Binding sitei744 – 7441ATPBy similarity
    Sitei770 – 7701Interaction with target DNABy similarity
    Sitei795 – 7951Interaction with target DNABy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: InterPro
    3. DNA ligase (ATP) activity Source: RefGenome
    4. DNA ligase activity Source: RGD
    5. metal ion binding Source: UniProtKB-KW

    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 repair Source: RGD
    6. lagging strand elongation Source: RefGenome

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

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

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA ligase 1 (EC:6.5.1.1)
    Alternative name(s):
    DNA ligase I
    Polydeoxyribonucleotide synthase [ATP] 1
    Gene namesi
    Name:Lig1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi621424. Lig1.

    Subcellular locationi

    GO - Cellular componenti

    1. chromosome Source: RefGenome
    2. mitochondrion Source: RefGenome
    3. nucleus Source: RGD

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 918918DNA ligase 1PRO_0000059572Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei50 – 501PhosphoserineBy similarity
    Modified residuei52 – 521PhosphoserineBy similarity
    Modified residuei66 – 661PhosphoserineBy similarity
    Modified residuei67 – 671PhosphoserineBy similarity
    Modified residuei78 – 781PhosphothreonineBy similarity
    Modified residuei145 – 1451N6-acetyllysineBy similarity
    Modified residuei195 – 1951PhosphothreonineBy similarity
    Modified residuei227 – 2271N6-acetyllysineBy similarity
    Modified residuei234 – 2341PhosphothreonineBy similarity
    Cross-linki422 – 422Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei913 – 9131PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ9JHY8.
    PRIDEiQ9JHY8.

    PTM databases

    PhosphoSiteiQ9JHY8.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9JHY8.

    Interactioni

    Protein-protein interaction databases

    BioGridi249510. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JHY8.
    SMRiQ9JHY8. Positions 262-901.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni642 – 6443Interaction with target DNABy similarity

    Sequence similaritiesi

    Belongs to the ATP-dependent DNA ligase family.Curated

    Phylogenomic databases

    eggNOGiCOG1793.
    HOGENOMiHOG000036006.
    HOVERGENiHBG005514.
    InParanoidiQ9JHY8.
    PhylomeDBiQ9JHY8.

    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.
    PROSITEiPS00333. DNA_LIGASE_A2. 1 hit.
    PS50160. DNA_LIGASE_A3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9JHY8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQRSIMSFFQ PTTTEGKAKK PEKEIPSSIR EKEPPPKVAL KERNRAVPES    50
    DSPVKRPGRK VAQVLSSEGE DEDEAPGTPQ VQKPVSDSKQ SSPPSPDSCP 100
    ENSPVFNCSP SMDISPSGFP KRRTARKQLP KRTIQDTLEE PNEDKAKAVK 150
    KRKKEDPQTP PESLTEAEEV NQKEEQVEDQ PTVPPEPTES PESVTLTKTE 200
    NIPMCKAGVK QKPQEEEQSK PPARGAKPLS SFFTPRKPAV KTEVKQEESD 250
    TPRKEETKGA PDPTNYNPSK SNYHPIEDAC WKHGQKVPFL AVARTFEKIE 300
    EVSARLKMVE TLSNLLRSVV ALSPTDLLPV LYLSLNRLGP PQQGLELGVG 350
    DGVLLKAVAQ ATGRQLESIR AEVAEKGDVG LVAENSRSTQ RLMLPSPPLT 400
    VSGVFTKFCD IARLTGSASM AKKMDIIKGL FVACRYSEAR FIARSLSGRL 450
    RLGLAEQSVL AALAQAGSLT PPGQEFPTVV VDAGKGKTAE ARKMWLEEQG 500
    MILKQTFCEV PDLDRIIPVL LEHGLESLPE HCKLSPGVPL KPMLAHPTRG 550
    VREVLKRFEE VDFTCEYKYY GQRAQIHVLE GGEVKIFSRN QEDNSGKYPD 600
    IISRIPKIKH PSVTSFILDT EAVAWDREKK QIQPFQVLTT RKRKEVDASE 650
    IQVQVCLYAF DLIYLNGESL ARQPLSRRRQ LLRENFVETE GEFVFATSLD 700
    TKDIEQIAEF LEQSVKDSCE GLMVKTLDVD ATYEIAKRSH NWLKLKKDYL 750
    EGVGDTLDLV VIGAYLGRGK RPGRYGGFLL AAYDEESEEL AAICKLGTGF 800
    SDEELEEHHQ NMQALLLPTP RPYVRIDGAV APNHWLDPSI VWEVKCADLT 850
    LSPIYRAARG MVDKEKGISL RFPRFIRVRE DKQPEQATTS DQVASLYRKQ 900
    SQIQNQQSSD LDSDVEDY 918
    Length:918
    Mass (Da):102,482
    Last modified:October 1, 2000 - v1
    Checksum:iB4ECA8861C521567
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF276774 mRNA. Translation: AAF82585.1.
    UniGeneiRn.20467.

    Genome annotation databases

    UCSCiRGD:621424. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF276774 mRNA. Translation: AAF82585.1 .
    UniGenei Rn.20467.

    3D structure databases

    ProteinModelPortali Q9JHY8.
    SMRi Q9JHY8. Positions 262-901.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 249510. 1 interaction.

    PTM databases

    PhosphoSitei Q9JHY8.

    Proteomic databases

    PaxDbi Q9JHY8.
    PRIDEi Q9JHY8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:621424. rat.

    Organism-specific databases

    RGDi 621424. Lig1.

    Phylogenomic databases

    eggNOGi COG1793.
    HOGENOMi HOG000036006.
    HOVERGENi HBG005514.
    InParanoidi Q9JHY8.
    PhylomeDBi Q9JHY8.

    Miscellaneous databases

    NextBioi 614997.
    PROi Q9JHY8.

    Gene expression databases

    Genevestigatori Q9JHY8.

    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 PS00333. DNA_LIGASE_A2. 1 hit.
    PS50160. DNA_LIGASE_A3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of rat DNA ligase I."
      Chen D., Cao G., Chen J.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.

    Entry informationi

    Entry nameiDNLI1_RAT
    AccessioniPrimary (citable) accession number: Q9JHY8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 106 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3