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Conserved domains on  [gi|1276317628|ref|NP_001344736|]
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large ribosomal subunit protein uL10m isoform 2 [Mus musculus]

Protein Classification

uL10 family ribosomal protein( domain architecture ID 2031)

uL10 family ribosomal protein forms a tight complex with multiple copies of the small acidic protein; the complex forms a stalk structure on the large subunit of the ribosome

Gene Ontology:  GO:0070180|GO:0003735|GO:0002181
PubMed:  24524803

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ribosomal_L10_P0 super family cl00376
Ribosomal protein L10 family; composed of the large subunit ribosomal protein called L10 in ...
 81-158 9.39e-13

Ribosomal protein L10 family; composed of the large subunit ribosomal protein called L10 in bacteria, P0 in eukaryotes, and L10e in archaea, as well as uncharacterized P0-like eukaryotic proteins. In all three kingdoms, L10 forms a tight complex with multiple copies of the small acidic protein L12(e). This complex forms a stalk structure on the large subunit of the ribosome. The N-terminal domain (NTD) of L10 interacts with L11 protein and forms the base of the L7/L12 stalk, while the extended C-terminal helix binds to two or three dimers of the NTD of L7/L12 (L7 and L12 are identical except for an acetylated N-terminus). The L7/L12 stalk is known to contain the binding site for elongation factors G and Tu (EF-G and EF-Tu, respectively); however, there is disagreement as to whether or not L10 is involved in forming the binding site. The stalk is believed to be associated with GTPase activities in protein synthesis. In a neuroblastoma cell line, L10 has been shown to interact with the SH3 domain of Src and to activate the binding of the Nck1 adaptor protein with skeletal proteins such as the Wiskott-Aldrich Syndrome Protein (WASP) and the WASP-interacting protein (WIP). Some eukaryotic P0 sequences have an additional C-terminal domain homologous with acidic proteins P1 and P2.


The actual alignment was detected with superfamily member cd05797:

Pssm-ID: 469747  Cd Length: 157  Bit Score: 62.52  E-value: 9.39e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276317628  81 LLRQDIVAVFRDNRMIAVCQNVALSAEDKLLLRHQLRKHKIFIKVFPSQVLKPFLENSKYRNLLPLFVGHNLLLVSEE 158
Cdd:cd05797     7 EIVAELKEKLKEAKSVVVADYRGLTVAQLTELRKELREAGVKLKVVKNTLAKRALEGTGFEDLDDLLKGPTAIAFSEE 84
 
Name Accession Description Interval E-value
Ribosomal_L10 cd05797
Ribosomal protein L10 family, L10 subfamily; composed of bacterial 50S ribosomal protein and ...
 81-158 9.39e-13

Ribosomal protein L10 family, L10 subfamily; composed of bacterial 50S ribosomal protein and eukaryotic mitochondrial 39S ribosomal protein, L10. L10 occupies the L7/L12 stalk of the ribosome. The N-terminal domain (NTD) of L10 interacts with L11 protein and forms the base of the L7/L12 stalk, while the extended C-terminal helix binds to two or three dimers of the NTD of L7/L12 (L7 and L12 are identical except for an acetylated N-terminus). The L7/L12 stalk is known to contain the binding site for elongation factors G and Tu (EF-G and EF-Tu, respectively); however, there is disagreement as to whether or not L10 is involved in forming the binding site. The stalk is believed to be associated with GTPase activities in protein synthesis. In a neuroblastoma cell line, L10 has been shown to interact with the SH3 domain of Src and to activate the binding of the Nck1 adaptor protein with skeletal proteins such as the Wiskott-Aldrich Syndrome Protein (WASP) and the WASP-interacting protein (WIP). These bacteria and eukaryotic sequences have no additional C-terminal domain, present in other eukaryotic and archaeal orthologs.


Pssm-ID: 240223  Cd Length: 157  Bit Score: 62.52  E-value: 9.39e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276317628  81 LLRQDIVAVFRDNRMIAVCQNVALSAEDKLLLRHQLRKHKIFIKVFPSQVLKPFLENSKYRNLLPLFVGHNLLLVSEE 158
Cdd:cd05797     7 EIVAELKEKLKEAKSVVVADYRGLTVAQLTELRKELREAGVKLKVVKNTLAKRALEGTGFEDLDDLLKGPTAIAFSEE 84
Ribosomal_L10 pfam00466
Ribosomal protein L10;
85-162 2.26e-03

Ribosomal protein L10;


Pssm-ID: 459822 [Multi-domain]  Cd Length: 99  Bit Score: 35.98  E-value: 2.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276317628  85 DIVAVFRDNRMIAVCQNVALSAEDKLLLRHQLRKHKIFIKVFPSQVLKPFLENSKYRNLLPLFVGHNLLLVSEEPKVK 162
Cdd:pfam00466  12 ELKELLKEYKSVVVVDYRGLTVAQLTELRKKLRENGAELKVGKNTLMRRALEETGEEKLEDYLKGPTALLFTNEDPVA 89
 
Name Accession Description Interval E-value
Ribosomal_L10 cd05797
Ribosomal protein L10 family, L10 subfamily; composed of bacterial 50S ribosomal protein and ...
 81-158 9.39e-13

Ribosomal protein L10 family, L10 subfamily; composed of bacterial 50S ribosomal protein and eukaryotic mitochondrial 39S ribosomal protein, L10. L10 occupies the L7/L12 stalk of the ribosome. The N-terminal domain (NTD) of L10 interacts with L11 protein and forms the base of the L7/L12 stalk, while the extended C-terminal helix binds to two or three dimers of the NTD of L7/L12 (L7 and L12 are identical except for an acetylated N-terminus). The L7/L12 stalk is known to contain the binding site for elongation factors G and Tu (EF-G and EF-Tu, respectively); however, there is disagreement as to whether or not L10 is involved in forming the binding site. The stalk is believed to be associated with GTPase activities in protein synthesis. In a neuroblastoma cell line, L10 has been shown to interact with the SH3 domain of Src and to activate the binding of the Nck1 adaptor protein with skeletal proteins such as the Wiskott-Aldrich Syndrome Protein (WASP) and the WASP-interacting protein (WIP). These bacteria and eukaryotic sequences have no additional C-terminal domain, present in other eukaryotic and archaeal orthologs.


Pssm-ID: 240223  Cd Length: 157  Bit Score: 62.52  E-value: 9.39e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276317628  81 LLRQDIVAVFRDNRMIAVCQNVALSAEDKLLLRHQLRKHKIFIKVFPSQVLKPFLENSKYRNLLPLFVGHNLLLVSEE 158
Cdd:cd05797     7 EIVAELKEKLKEAKSVVVADYRGLTVAQLTELRKELREAGVKLKVVKNTLAKRALEGTGFEDLDDLLKGPTAIAFSEE 84
Ribosomal_L10_P0 cd00379
Ribosomal protein L10 family; composed of the large subunit ribosomal protein called L10 in ...
 81-162 1.08e-08

Ribosomal protein L10 family; composed of the large subunit ribosomal protein called L10 in bacteria, P0 in eukaryotes, and L10e in archaea, as well as uncharacterized P0-like eukaryotic proteins. In all three kingdoms, L10 forms a tight complex with multiple copies of the small acidic protein L12(e). This complex forms a stalk structure on the large subunit of the ribosome. The N-terminal domain (NTD) of L10 interacts with L11 protein and forms the base of the L7/L12 stalk, while the extended C-terminal helix binds to two or three dimers of the NTD of L7/L12 (L7 and L12 are identical except for an acetylated N-terminus). The L7/L12 stalk is known to contain the binding site for elongation factors G and Tu (EF-G and EF-Tu, respectively); however, there is disagreement as to whether or not L10 is involved in forming the binding site. The stalk is believed to be associated with GTPase activities in protein synthesis. In a neuroblastoma cell line, L10 has been shown to interact with the SH3 domain of Src and to activate the binding of the Nck1 adaptor protein with skeletal proteins such as the Wiskott-Aldrich Syndrome Protein (WASP) and the WASP-interacting protein (WIP). Some eukaryotic P0 sequences have an additional C-terminal domain homologous with acidic proteins P1 and P2.


Pssm-ID: 238222 [Multi-domain]  Cd Length: 155  Bit Score: 51.41  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317628  81 LLRQDIVAVFRDNRMIAVCQNVALSAEDKLLLRHQLRKHKIFIKVFPSQVLKPFLENSKYRNLLPLFVGHNLLLVSEEPK 160
Cdd:cd00379     5 ELVEELKELLKKYKSVVVVDYRGLTVAQLTELRKELRESGAKLKVGKNTLMRRALKGTGFEELKPLLKGPTALAFTNEDP 84


                  ..
gi 1276317628 161 VK 162
Cdd:cd00379    85 VE 86
Ribosomal_L10 pfam00466
Ribosomal protein L10;
85-162 2.26e-03

Ribosomal protein L10;


Pssm-ID: 459822 [Multi-domain]  Cd Length: 99  Bit Score: 35.98  E-value: 2.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276317628  85 DIVAVFRDNRMIAVCQNVALSAEDKLLLRHQLRKHKIFIKVFPSQVLKPFLENSKYRNLLPLFVGHNLLLVSEEPKVK 162
Cdd:pfam00466  12 ELKELLKEYKSVVVVDYRGLTVAQLTELRKKLRENGAELKVGKNTLMRRALEETGEEKLEDYLKGPTALLFTNEDPVA 89
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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