NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|6324534|ref|NP_014603|]
View 

ribosomal protein P2A [Saccharomyces cerevisiae S288C]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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. ...
 15-106 1.93e-18

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: 73.84  E-value: 1.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324534   15 NTPDATKIKAILESVGIEIEDEKVSSVLSALEGKSVDELITEGNEKLAAVPAAGPASA--GGAAAASGDAAAEEEKEEEA 92
Cdd:cd05833  16 ASPSAADVKKILGSVGVEVDDEKLNKVISELEGKDVEELIAAGKEKLASVPAGAGGAApaAAAAAAAAAAAKKEEKKEES 95

                        90
                ....*....|....
gi 6324534   93 AEESDDDMGFGLFD 106
Cdd:cd05833  96 EEESDDDMGFGLFD 109
 
Name Accession Description Interval E-value
Ribosomal_P2 cd05833
Ribosomal protein P2. This subfamily represents the eukaryotic large ribosomal protein P2. ...
 15-106 1.93e-18

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: 73.84  E-value: 1.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324534   15 NTPDATKIKAILESVGIEIEDEKVSSVLSALEGKSVDELITEGNEKLAAVPAAGPASA--GGAAAASGDAAAEEEKEEEA 92
Cdd:cd05833  16 ASPSAADVKKILGSVGVEVDDEKLNKVISELEGKDVEELIAAGKEKLASVPAGAGGAApaAAAAAAAAAAAKKEEKKEES 95

                        90
                ....*....|....
gi 6324534   93 AEESDDDMGFGLFD 106
Cdd:cd05833  96 EEESDDDMGFGLFD 109
PLN00138 PLN00138
large subunit ribosomal protein LP2; Provisional
 14-106 1.74e-10

large subunit ribosomal protein LP2; Provisional


Pssm-ID: 165706 [Multi-domain]  Cd Length: 113  Bit Score: 53.52  E-value: 1.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324534    14 GNT-PDATKIKAILESVGIEIEDEKVSSVLSALEGKSVDELITEGNEKLAAV------PAAGPASAGGAAAASGDAAAEE 86
Cdd:PLN00138  14 GNTcPSAEDLKDILGSVGADADDDRIELLLSEVKGKDITELIASGREKLASVpsgggvAVAAAAAPAAGGAAAPAAEAKK 93

                         90       100
                 ....*....|....*....|
gi 6324534    87 EKEEEAAEESDDDMGFGLFD 106
Cdd:PLN00138  94 EEKVEEKEESDDDMGFSLFD 113
Ribosomal_60s pfam00428
60s Acidic ribosomal protein; This family includes archaebacterial L12, eukaryotic P0, P1 and ...
 17-105 1.04e-08

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


Pssm-ID: 459808  Cd Length: 87  Bit Score: 48.02  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324534     17 PDATKIKAILESVGIEIEDEKVSSVLSALEGKSVDELITEGNEKLAAVpaaGPASAGGAAAASGDAAAEEEKEEEAAEES 96
Cdd:pfam00428   2 PTAANIKKVLKAAGVNVEAVRVKLFAKALEGKNIKELLANGGAKAAAA---AAAAAAAAAAAAAAAAAEEKKKEEEEEES 78


                  ....*....
gi 6324534     97 DDDMGFGLF 105
Cdd:pfam00428  79 DDDMGFGLF 87
 
Name Accession Description Interval E-value
Ribosomal_P2 cd05833
Ribosomal protein P2. This subfamily represents the eukaryotic large ribosomal protein P2. ...
 15-106 1.93e-18

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: 73.84  E-value: 1.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324534   15 NTPDATKIKAILESVGIEIEDEKVSSVLSALEGKSVDELITEGNEKLAAVPAAGPASA--GGAAAASGDAAAEEEKEEEA 92
Cdd:cd05833  16 ASPSAADVKKILGSVGVEVDDEKLNKVISELEGKDVEELIAAGKEKLASVPAGAGGAApaAAAAAAAAAAAKKEEKKEES 95

                        90
                ....*....|....
gi 6324534   93 AEESDDDMGFGLFD 106
Cdd:cd05833  96 EEESDDDMGFGLFD 109
Ribosomal_P1_P2_L12p cd04411
Ribosomal protein P1, P2, and L12p. Ribosomal proteins P1 and P2 are the eukaryotic proteins ...
 14-105 3.48e-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: 54.96  E-value: 3.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324534   14 GNTPDATKIKAILESVGIEIEDEKVSSVLSALEGKSVDELITEGNEKLAAVPAAGPASAGGAAAASGDAAAEEEKEEEAA 93
Cdd:cd04411  14 GKELTEDKIKELLSAAGAEIEPERVKLFLSALNGKNIDEVISKGKELMSSQAAAAAAPAATAAATAEPAEKAEEAKEEEE 93

                        90
                ....*....|..
gi 6324534   94 EESDDDMGFGLF 105
Cdd:cd04411  94 EEEDEDFGFGLF 105
PLN00138 PLN00138
large subunit ribosomal protein LP2; Provisional
 14-106 1.74e-10

large subunit ribosomal protein LP2; Provisional


Pssm-ID: 165706 [Multi-domain]  Cd Length: 113  Bit Score: 53.52  E-value: 1.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324534    14 GNT-PDATKIKAILESVGIEIEDEKVSSVLSALEGKSVDELITEGNEKLAAV------PAAGPASAGGAAAASGDAAAEE 86
Cdd:PLN00138  14 GNTcPSAEDLKDILGSVGADADDDRIELLLSEVKGKDITELIASGREKLASVpsgggvAVAAAAAPAAGGAAAPAAEAKK 93

                         90       100
                 ....*....|....*....|
gi 6324534    87 EKEEEAAEESDDDMGFGLFD 106
Cdd:PLN00138  94 EEKVEEKEESDDDMGFSLFD 113
Ribosomal_60s pfam00428
60s Acidic ribosomal protein; This family includes archaebacterial L12, eukaryotic P0, P1 and ...
 17-105 1.04e-08

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


Pssm-ID: 459808  Cd Length: 87  Bit Score: 48.02  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324534     17 PDATKIKAILESVGIEIEDEKVSSVLSALEGKSVDELITEGNEKLAAVpaaGPASAGGAAAASGDAAAEEEKEEEAAEES 96
Cdd:pfam00428   2 PTAANIKKVLKAAGVNVEAVRVKLFAKALEGKNIKELLANGGAKAAAA---AAAAAAAAAAAAAAAAAEEKKKEEEEEES 78


                  ....*....
gi 6324534     97 DDDMGFGLF 105
Cdd:pfam00428  79 DDDMGFGLF 87
PTZ00373 PTZ00373
60S Acidic ribosomal protein P2; Provisional
 17-106 2.16e-06

60S Acidic ribosomal protein P2; Provisional


Pssm-ID: 185582  Cd Length: 112  Bit Score: 42.59  E-value: 2.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324534    17 PDATKIKAILESVGIEIEDEKVSSVLSALEGKSVDELITEGNEKLAAV---PAAGPASAGGAAAASGDAAAEEEKEEEAA 93
Cdd:PTZ00373  20 PTKKEVKNVLSAVNADVEDDVLDNFFKSLEGKTPHELIAAGMKKLQNIgggVAAAAAPAAGAATAGAKAEAKKEEKKEEE 99

                         90
                 ....*....|...
gi 6324534    94 EESDDDMGFGLFD 106
Cdd:PTZ00373 100 EEEEDDLGFSLFG 112
Ribosomal_L12p cd05832
Ribosomal protein L12p. This subfamily includes archaeal L12p, the protein that is ...
 18-64 2.95e-03

Ribosomal protein L12p. This subfamily includes archaeal L12p, the protein that is functionally equivalent to L7/L12 in bacteria and the P1 and P2 proteins in eukaryotes. L12p is homologous to P1 and P2 but is not homologous to bacterial L7/L12. It is located in the L12 stalk, with proteins L10, L11, and 23S rRNA. L12p is the only protein 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 four copies (two heterodimers), and bacteria may have four or six copies (two or three homodimers), depending on the species. The organization of proteins within the stalk has been characterized primarily in bacteria, where L7/L12 forms either two or three homodimers and each homodimer binds to the extended C-terminal helix of L10. L7/L12 is attached to the ribosome through L10 and is the only ribosomal protein that does not directly interact with rRNA. Archaeal L12p is believed to function in a similar fashion. However, hybrid ribosomes containing the large subunit from E. coli with an archaeal stalk are able to bind archaeal and eukaryotic elongation factors but not bacterial elongation factors. In several mesophilic and thermophilic archaeal species, the binding of 23S rRNA to protein L11 and to the L10/L12p pentameric complex was found to be temperature-dependent and cooperative.


Pssm-ID: 100110 [Multi-domain]  Cd Length: 106  Bit Score: 34.39  E-value: 2.95e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 6324534   18 DATKIKAILESVGIEIEDEKVSSVLSALEGKSVDELITEGNEKLAAV 64
Cdd:cd05832  18 NEENLKKVLEAAGIEVDEARVKALVAALEEVNIDEAIKKAAVAAAAA 64
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH