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Q8PVR7

- DNLI1_METMA

UniProt

Q8PVR7 - DNLI1_METMA

Protein

DNA ligase 1

Gene

lig1

Organism
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      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.UniRule annotation

    Catalytic activityi

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

    Cofactori

    Divalent metal cations.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei244 – 2441ATPUniRule annotation
    Active sitei246 – 2461N6-AMP-lysine intermediateUniRule annotation
    Binding sitei251 – 2511ATPUniRule annotation
    Binding sitei266 – 2661ATPUniRule annotation
    Binding sitei296 – 2961ATPUniRule annotation
    Binding sitei342 – 3421ATPUniRule annotation
    Binding sitei419 – 4191ATPUniRule annotation
    Binding sitei425 – 4251ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. DNA binding Source: InterPro
    3. DNA ligase (ATP) activity Source: UniProtKB-HAMAP
    4. 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-HAMAP
    5. DNA replication Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

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

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMMAZ192952:GCK2-1944-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA ligase 1UniRule annotation (EC:6.5.1.1UniRule annotation)
    Alternative name(s):
    Polydeoxyribonucleotide synthase [ATP] 1UniRule annotation
    Gene namesi
    Name:lig1UniRule annotation
    Ordered Locus Names:MM_1895
    OrganismiMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
    Taxonomic identifieri192952 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
    ProteomesiUP000000595: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 579579DNA ligase 1PRO_0000365259Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi192952.MM_1895.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8PVR7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATP-dependent DNA ligase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1793.
    HOGENOMiHOG000036008.
    KOiK10747.
    OMAiCTDIGEL.

    Family and domain databases

    Gene3Di1.10.3260.10. 1 hit.
    2.40.50.140. 1 hit.
    HAMAPiMF_00407. DNA_ligase.
    InterProiIPR022865. DNA_ligae_ATP-dep_bac/arc.
    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]
    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.
    PS50160. DNA_LIGASE_A3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8PVR7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRFKELAELF EELEKTTSHR EIVRKISEFF KNLRGDEVKD SAYLFLGSTG    50
    PAFENTTLGI KDMLAIRAIA GAYGVTREDV RKRYARTGDL GDVAFELSKK 100
    RESSLTIEDV FQRLLQIRET SGKGSQEEKT ALFSDILQKA TPEEGKYIVR 150
    LVLGRLRLGF GDQFLLEAFA IAFTGDKKHA AKIKESYSVC TDIGELAKIL 200
    AENGARATGF ISIKPGRPVK SMLSQRVESF EELEKRVKGK KAAEEKYDGE 250
    RVQVHKTGEG IKAFSRRLED ITSQYPEIIE DVRKTVPANE IVLDGEIVAY 300
    AELERNGNRI EEFYPFQNLM QRRRKYEIEN YRKKCPVAVF FFDILYLNGE 350
    PLLKRPYPER RALLEMNVVE SGIIRLSKRI VTESVEEIED FFNETIEKGL 400
    EGIVVKSMSS NSYYEAGKRS WFWFKWKQEY SEGMRETFDL VVVGSYYGRG 450
    RRKGSFGALL CAVLNKEGQR FETLTKVGTG FTEADAEEIN RLLSDHIVSE 500
    IPKGVSIKKG MLPDIFIEPA VVIEVLGSEI TNSPGHTAGE GEEETGLALR 550
    FPRFLRIRHD KTPYDAMTVK EVRDLKDGT 579
    Length:579
    Mass (Da):65,867
    Last modified:October 1, 2002 - v1
    Checksum:i9E11E66075B8DEEC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE008384 Genomic DNA. Translation: AAM31591.1.
    RefSeqiNP_633919.1. NC_003901.1.
    WP_011033828.1. NC_003901.1.

    Genome annotation databases

    EnsemblBacteriaiAAM31591; AAM31591; MM_1895.
    GeneIDi1480237.
    KEGGimma:MM_1895.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE008384 Genomic DNA. Translation: AAM31591.1 .
    RefSeqi NP_633919.1. NC_003901.1.
    WP_011033828.1. NC_003901.1.

    3D structure databases

    ProteinModelPortali Q8PVR7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 192952.MM_1895.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM31591 ; AAM31591 ; MM_1895 .
    GeneIDi 1480237.
    KEGGi mma:MM_1895.

    Phylogenomic databases

    eggNOGi COG1793.
    HOGENOMi HOG000036008.
    KOi K10747.
    OMAi CTDIGEL.

    Enzyme and pathway databases

    BioCyci MMAZ192952:GCK2-1944-MONOMER.

    Family and domain databases

    Gene3Di 1.10.3260.10. 1 hit.
    2.40.50.140. 1 hit.
    HAMAPi MF_00407. DNA_ligase.
    InterProi IPR022865. DNA_ligae_ATP-dep_bac/arc.
    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.
    PS50160. DNA_LIGASE_A3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
      Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R.
      , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
      J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.

    Entry informationi

    Entry nameiDNLI1_METMA
    AccessioniPrimary (citable) accession number: Q8PVR7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 3, 2009
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic 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