I3LG77 · I3LG77_PIG

  • Protein
    Deoxynucleoside triphosphate triphosphohydrolase SAMHD1
  • Gene
    SAMHD1
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site116dGTP 1 (UniProtKB | ChEBI)
Binding site119dGTP 2 (UniProtKB | ChEBI)
Binding site137dGTP 1 (UniProtKB | ChEBI)
Binding site142dGTP 1 (UniProtKB | ChEBI)
Binding site145dGTP 1 (UniProtKB | ChEBI)
Binding site149dGTP 3 (UniProtKB | ChEBI)
Binding site150dGTP 3 (UniProtKB | ChEBI)
Binding site156dGTP 2 (UniProtKB | ChEBI)
Binding site164dGTP 3 (UniProtKB | ChEBI)
Binding site210dGTP 3 (UniProtKB | ChEBI)
Binding site215dGTP 3 (UniProtKB | ChEBI)
Binding site233dGTP 3 (UniProtKB | ChEBI)
Binding site312dGTP 3 (UniProtKB | ChEBI)
Binding site315dGTP 3 (UniProtKB | ChEBI)
Binding site319dGTP 3 (UniProtKB | ChEBI)
Binding site330dGTP 2 (UniProtKB | ChEBI)
Binding site333dGTP 2 (UniProtKB | ChEBI)
Binding site352dGTP 2 (UniProtKB | ChEBI)
Binding site354dGTP 2 (UniProtKB | ChEBI)
Binding site358dGTP 2 (UniProtKB | ChEBI)
Binding site366dGTP 3 (UniProtKB | ChEBI)
Binding site372dGTP 2 (UniProtKB | ChEBI)
Binding site374dGTP 3 (UniProtKB | ChEBI)
Binding site375dGTP 3 (UniProtKB | ChEBI)
Binding site376dGTP 2 (UniProtKB | ChEBI)
Binding site377dGTP 2 (UniProtKB | ChEBI)
Binding site451dGTP 1 (UniProtKB | ChEBI)
Binding site524dGTP 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular Componentsite of double-strand break
Cellular Componenttetraspanin-enriched microdomain
Molecular Functiondeoxynucleoside triphosphate hydrolase activity
Molecular FunctiondGTP binding
Molecular FunctiondGTPase activity
Molecular FunctionGTP binding
Molecular Functionidentical protein binding
Molecular FunctionRNA binding
Molecular FunctionRNA nuclease activity
Molecular Functionsingle-stranded DNA binding
Molecular Functionzinc ion binding
Biological ProcessdATP catabolic process
Biological Processdefense response to virus
Biological ProcessdGTP catabolic process
Biological ProcessDNA strand resection involved in replication fork processing
Biological Processdouble-strand break repair via homologous recombination
Biological Processnegative regulation of type I interferon-mediated signaling pathway
Biological Processprotein homotetramerization
Biological Processregulation of innate immune response
Biological Processsomatic hypermutation of immunoglobulin genes

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

Gene names

    • Name
      SAMHD1

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Duroc
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Suina > Suidae > Sus

Accessions

  • Primary accession
    I3LG77

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Proteomic databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias1-18Polar residues
Region1-41Disordered
Domain45-110SAM
Domain164-316HD

Sequence similarities

Belongs to the SAMHD1 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    627
  • Mass (Da)
    71,968
  • Last updated
    2017-11-22 v2
  • Checksum
    ACF90BFD6766FDAB
MQSADSQQPSKRPRCDGSPTTPPNTPPAAAERSLGPNLHPDHRTWGPEQVCGFLNRSGFGDSELLERCREKKITGSILPFLDESLLEDLGVSSYEKRMKLLNYIQRLGQTHVDTVKVINDPIHGHIELHPLLIRIIDTPQFQRLRYIKQLGGGYYVFPGASHNRFEHSLGVGYLAGCLVRELSEKQPELQISERDMLCVQIAGLCHDLGHGPFSHMFDGRFIPLARPDVKWTHEQGSVNMFEHLVNSNGLIDVMEHYGLIPEEDIWFIKEQITGPLESPVKNATWPYKGRPKEKSFLYEIVANKRNGIDVDKWDYFARDCHHLGIQNNFDYKRFIKFARVCEVDNKKHICTREKEVGNLYDMFHTRNCLHRRAYQHKVGNIIDTMITDAFLKADPYIEITGSEGKKYRISTAIDDMEAFTKLTDNIFLEILYSTDPKLDAARAILKKIECRNLYKFVGETQPGRQDKIKRENYESLPKGVASAKPSNIQLEAELKAEDFIVDVINMDYGMEDKNPIDNVRFYCKSDPNKAIIITKNQVSQLLPERFAEQLIRVYCKKTDEKSLFAARQHFVQWCLDNDFTKPQDGDVVAPLITPRKLEWNSTHSAQSQARTREASKSRVRLFAKDSV

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A5G2RD15A0A5G2RD15_PIGSAMHD1575
A0A5G2Q7I5A0A5G2Q7I5_PIGSAMHD1592
A0A5G2QZ64A0A5G2QZ64_PIGSAMHD1590
I3LSQ7I3LSQ7_PIGSAMHD1621
A0A5G2QUS9A0A5G2QUS9_PIGSAMHD1557

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-18Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQIR01095001
EMBL· GenBank· DDBJ
HDA50477.1
EMBL· GenBank· DDBJ
Transcribed RNA
DQIR01222192
EMBL· GenBank· DDBJ
HDB77669.1
EMBL· GenBank· DDBJ
Transcribed RNA

Genome annotation databases

Similar Proteins

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