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Conserved domains on  [gi|46397855|sp|P99027|]
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RecName: Full=Large ribosomal subunit protein P2; AltName: Full=60S acidic ribosomal protein P2

Protein Classification

60S acidic ribosomal protein P2( domain architecture ID 10146786)

60S acidic ribosomal protein P2 plays an important role in the elongation step of protein synthesis

CATH:  1.10.10.1410
Gene Ontology:  GO:0003735|GO:0002182
PubMed:  20385603|9254014

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ribosomal_P2 cd05833
Ribosomal protein P2. This subfamily represents the eukaryotic large ribosomal protein P2. ...
 1-66 1.25e-34

Ribosomal protein P2. This subfamily represents the eukaryotic large ribosomal protein P2. Eukaryotic P1 and P2 are functionally equivalent to the bacterial protein L7/L12, but are not homologous to L7/L12. P2 is located in the L12 stalk, with proteins P1, P0, L11, and 28S rRNA. P1 and P2 are the only proteins in the ribosome to occur as multimers, always appearing as sets of heterodimers. Recent data indicate that eukaryotes have four copies (two heterodimers), while most archaeal species contain six copies of L12p (three homodimers). Bacteria may have four or six copies of L7/L12 (two or three homodimers) depending on the species. Experiments using S. cerevisiae P1 and P2 indicate that P1 proteins are positioned more internally with limited reactivity in the C-terminal domains, while P2 proteins seem to be more externally located and are more likely to interact with other cellular components. In lower eukaryotes, P1 and P2 are further subdivided into P1A, P1B, P2A, and P2B, which form P1A/P2B and P1B/P2A heterodimers. Some plants have a third P-protein, called P3, which is not homologous to P1 and P2. In humans, P1 and P2 are strongly autoimmunogenic. They play a significant role in the etiology and pathogenesis of systemic lupus erythema (SLE). In addition, the ribosome-inactivating protein trichosanthin (TCS) interacts with human P0, P1, and P2, with its primary binding site in the C-terminal region of P2. TCS inactivates the ribosome by depurinating a specific adenine in the sarcin-ricin loop of 28S rRNA.


:

Pssm-ID: 100111  Cd Length: 109  Bit Score: 115.05  E-value: 1.25e-34
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46397855   1 MRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGVGKLASVP 66
Cdd:cd05833   1 MKYVAAYLLAVLGGNASPSAADVKKILGSVGVEVDDEKLNKVISELEGKDVEELIAAGKEKLASVP 66
 
Name Accession Description Interval E-value
Ribosomal_P2 cd05833
Ribosomal protein P2. This subfamily represents the eukaryotic large ribosomal protein P2. ...
 1-66 1.25e-34

Ribosomal protein P2. This subfamily represents the eukaryotic large ribosomal protein P2. Eukaryotic P1 and P2 are functionally equivalent to the bacterial protein L7/L12, but are not homologous to L7/L12. P2 is located in the L12 stalk, with proteins P1, P0, L11, and 28S rRNA. P1 and P2 are the only proteins in the ribosome to occur as multimers, always appearing as sets of heterodimers. Recent data indicate that eukaryotes have four copies (two heterodimers), while most archaeal species contain six copies of L12p (three homodimers). Bacteria may have four or six copies of L7/L12 (two or three homodimers) depending on the species. Experiments using S. cerevisiae P1 and P2 indicate that P1 proteins are positioned more internally with limited reactivity in the C-terminal domains, while P2 proteins seem to be more externally located and are more likely to interact with other cellular components. In lower eukaryotes, P1 and P2 are further subdivided into P1A, P1B, P2A, and P2B, which form P1A/P2B and P1B/P2A heterodimers. Some plants have a third P-protein, called P3, which is not homologous to P1 and P2. In humans, P1 and P2 are strongly autoimmunogenic. They play a significant role in the etiology and pathogenesis of systemic lupus erythema (SLE). In addition, the ribosome-inactivating protein trichosanthin (TCS) interacts with human P0, P1, and P2, with its primary binding site in the C-terminal region of P2. TCS inactivates the ribosome by depurinating a specific adenine in the sarcin-ricin loop of 28S rRNA.


Pssm-ID: 100111  Cd Length: 109  Bit Score: 115.05  E-value: 1.25e-34
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46397855   1 MRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGVGKLASVP 66
Cdd:cd05833   1 MKYVAAYLLAVLGGNASPSAADVKKILGSVGVEVDDEKLNKVISELEGKDVEELIAAGKEKLASVP 66
PLN00138 PLN00138
large subunit ribosomal protein LP2; Provisional
 1-66 6.07e-23

large subunit ribosomal protein LP2; Provisional


Pssm-ID: 165706 [Multi-domain]  Cd Length: 113  Bit Score: 85.88  E-value: 6.07e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46397855    1 MRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGVGKLASVP 66
Cdd:PLN00138   1 MKVVAAYLLAVLGGNTCPSAEDLKDILGSVGADADDDRIELLLSEVKGKDITELIASGREKLASVP 66
Ribosomal_60s pfam00428
60s Acidic ribosomal protein; This family includes archaebacterial L12, eukaryotic P0, P1 and ...
 17-114 4.36e-04

60s Acidic ribosomal protein; This family includes archaebacterial L12, eukaryotic P0, P1 and P2.


Pssm-ID: 459808  Cd Length: 87  Bit Score: 36.47  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397855    17 SPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGVGKLASVPAGGAVAVSAAPGSAAPAAGSAPAAAEEKKD 96
Cdd:pfam00428   1 EPTAANIKKVLKAAGVNVEAVRVKLFAKALEGKNIKELLANGGAKAAAAAAAAAAAAAAAAAAAAAEEKKKEEEEEESDD 80

                          90
                  ....*....|....*...
gi 46397855    97 EkkeeseesdddMGFGLF 114
Cdd:pfam00428  81 D-----------MGFGLF 87
 
Name Accession Description Interval E-value
Ribosomal_P2 cd05833
Ribosomal protein P2. This subfamily represents the eukaryotic large ribosomal protein P2. ...
 1-66 1.25e-34

Ribosomal protein P2. This subfamily represents the eukaryotic large ribosomal protein P2. Eukaryotic P1 and P2 are functionally equivalent to the bacterial protein L7/L12, but are not homologous to L7/L12. P2 is located in the L12 stalk, with proteins P1, P0, L11, and 28S rRNA. P1 and P2 are the only proteins in the ribosome to occur as multimers, always appearing as sets of heterodimers. Recent data indicate that eukaryotes have four copies (two heterodimers), while most archaeal species contain six copies of L12p (three homodimers). Bacteria may have four or six copies of L7/L12 (two or three homodimers) depending on the species. Experiments using S. cerevisiae P1 and P2 indicate that P1 proteins are positioned more internally with limited reactivity in the C-terminal domains, while P2 proteins seem to be more externally located and are more likely to interact with other cellular components. In lower eukaryotes, P1 and P2 are further subdivided into P1A, P1B, P2A, and P2B, which form P1A/P2B and P1B/P2A heterodimers. Some plants have a third P-protein, called P3, which is not homologous to P1 and P2. In humans, P1 and P2 are strongly autoimmunogenic. They play a significant role in the etiology and pathogenesis of systemic lupus erythema (SLE). In addition, the ribosome-inactivating protein trichosanthin (TCS) interacts with human P0, P1, and P2, with its primary binding site in the C-terminal region of P2. TCS inactivates the ribosome by depurinating a specific adenine in the sarcin-ricin loop of 28S rRNA.


Pssm-ID: 100111  Cd Length: 109  Bit Score: 115.05  E-value: 1.25e-34
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46397855   1 MRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGVGKLASVP 66
Cdd:cd05833   1 MKYVAAYLLAVLGGNASPSAADVKKILGSVGVEVDDEKLNKVISELEGKDVEELIAAGKEKLASVP 66
PLN00138 PLN00138
large subunit ribosomal protein LP2; Provisional
 1-66 6.07e-23

large subunit ribosomal protein LP2; Provisional


Pssm-ID: 165706 [Multi-domain]  Cd Length: 113  Bit Score: 85.88  E-value: 6.07e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46397855    1 MRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGVGKLASVP 66
Cdd:PLN00138   1 MKVVAAYLLAVLGGNTCPSAEDLKDILGSVGADADDDRIELLLSEVKGKDITELIASGREKLASVP 66
PTZ00373 PTZ00373
60S Acidic ribosomal protein P2; Provisional
 1-65 1.28e-15

60S Acidic ribosomal protein P2; Provisional


Pssm-ID: 185582  Cd Length: 112  Bit Score: 66.86  E-value: 1.28e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46397855    1 MRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGVGKLASV 65
Cdd:PTZ00373   3 MKYVAAYLMCVLGGNENPTKKEVKNVLSAVNADVEDDVLDNFFKSLEGKTPHELIAAGMKKLQNI 67
Ribosomal_P1_P2_L12p cd04411
Ribosomal protein P1, P2, and L12p. Ribosomal proteins P1 and P2 are the eukaryotic proteins ...
 1-64 2.60e-11

Ribosomal protein P1, P2, and L12p. Ribosomal proteins P1 and P2 are the eukaryotic proteins that are functionally equivalent to bacterial L7/L12. L12p is the archaeal homolog. Unlike other ribosomal proteins, the archaeal L12p and eukaryotic P1 and P2 do not share sequence similarity with their bacterial counterparts. They are part of the ribosomal stalk (called the L7/L12 stalk in bacteria), along with 28S rRNA and the proteins L11 and P0 in eukaryotes (23S rRNA, L11, and L10e in archaea). In bacterial ribosomes, L7/L12 homodimers bind the extended C-terminal helix of L10 to anchor the L7/L12 molecules to the ribosome. Eukaryotic P1/P2 heterodimers and archaeal L12p homodimers are believed to bind the L10 equivalent proteins, eukaryotic P0 and archaeal L10e, in a similar fashion. P1 and P2 (L12p, L7/L12) are the only proteins in the ribosome to occur as multimers, always appearing as sets of dimers. Recent data indicate that most archaeal species contain six copies of L12p (three homodimers), while eukaryotes have two copies each of P1 and P2 (two heterodimers). Bacteria may have four or six copies (two or three homodimers), depending on the species. As in bacteria, the stalk is crucial for binding of initiation, elongation, and release factors in eukaryotes and archaea.


Pssm-ID: 100108  Cd Length: 105  Bit Score: 55.73  E-value: 2.60e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46397855   1 MRYVASYLLAALGGnSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGVGKLAS 64
Cdd:cd04411   1 MEYVAAYLLLHKGG-KELTEDKIKELLSAAGAEIEPERVKLFLSALNGKNIDEVISKGKELMSS 63
Ribosomal_60s pfam00428
60s Acidic ribosomal protein; This family includes archaebacterial L12, eukaryotic P0, P1 and ...
 17-114 4.36e-04

60s Acidic ribosomal protein; This family includes archaebacterial L12, eukaryotic P0, P1 and P2.


Pssm-ID: 459808  Cd Length: 87  Bit Score: 36.47  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397855    17 SPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGVGKLASVPAGGAVAVSAAPGSAAPAAGSAPAAAEEKKD 96
Cdd:pfam00428   1 EPTAANIKKVLKAAGVNVEAVRVKLFAKALEGKNIKELLANGGAKAAAAAAAAAAAAAAAAAAAAAEEKKKEEEEEESDD 80

                          90
                  ....*....|....*...
gi 46397855    97 EkkeeseesdddMGFGLF 114
Cdd:pfam00428  81 D-----------MGFGLF 87
 
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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