NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2439149132|ref|WP_272123000|]
View 

ribosomal protein L7/L12 [[Clostridium] symbiosum]

Protein Classification

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_L7_L12 super family cl46846
Ribosomal protein L7/L12. Ribosomal protein L7/L12 refers to the large ribosomal subunit ...
 57-85 1.31e-05

Ribosomal protein L7/L12. Ribosomal protein L7/L12 refers to the large ribosomal subunit proteins L7 and L12, which are identical except that L7 is acetylated at the N terminus. It is a component of the L7/L12 stalk, which is located at the surface of the ribosome. The stalk base consists of a portion of the 23S rRNA and ribosomal proteins L11 and L10. An extended C-terminal helix of L10 provides the binding site for L7/L12. L7/L12 consists of two domains joined by a flexible hinge, with the helical N-terminal domain (NTD) forming pairs of homodimers that bind to the extended helix of L10. It is the only multimeric ribosomal component, with either four or six copies per ribosome that occur as two or three dimers bound to the L10 helix. L7/L12 is the only ribosomal protein that does not interact directly with rRNA, but instead has indirect interactions through L10. The globular C-terminal domains of L7/L12 are highly mobile. They are exposed to the cytoplasm and contain binding sites for other molecules. Initiation factors, elongation factors, and release factors are known to interact with the L7/L12 stalk during their GTP-dependent cycles. The binding site for the factors EF-Tu and EF-G comprises L7/L12, L10, L11, the L11-binding region of 23S rRNA, and the sarcin-ricin loop of 23S rRNA. Removal of L7/L12 has minimal effect on factor binding and it has been proposed that L7/L12 induces the catalytically active conformation of EF-Tu and EF-G, thereby stimulating the GTPase activity of both factors. In eukaryotes, the proteins that perform the equivalent function to L7/L12 are called P1 and P2, which do not share sequence similarity with L7/L12. However, a bacterial L7/L12 homolog is found in some eukaryotes, in mitochondria and chloroplasts. In archaea, the protein equivalent to L7/L12 is called aL12 or L12p, but it is closer in sequence to P1 and P2 than to L7/L12.


The actual alignment was detected with superfamily member COG0222:

Pssm-ID: 481186  Cd Length: 125  Bit Score: 42.41  E-value: 1.31e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2439149132  57 IYAIKELREMTNLGLKEAKDLCD----TIK--ASK 85
Cdd:COG0222    71 IAVIKVVREITGLGLKEAKDLVEgapkPVKegVSK 105
 
Name Accession Description Interval E-value
RplL COG0222
Ribosomal protein L7/L12 [Translation, ribosomal structure and biogenesis]; Ribosomal protein ...
 57-85 1.31e-05

Ribosomal protein L7/L12 [Translation, ribosomal structure and biogenesis]; Ribosomal protein L7/L12 is part of the Pathway/BioSystem: Ribosome 50S subunit


Pssm-ID: 439992  Cd Length: 125  Bit Score: 42.41  E-value: 1.31e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2439149132  57 IYAIKELREMTNLGLKEAKDLCD----TIK--ASK 85
Cdd:COG0222    71 IAVIKVVREITGLGLKEAKDLVEgapkPVKegVSK 105
Ribosomal_L7_L12 cd00387
Ribosomal protein L7/L12. Ribosomal protein L7/L12 refers to the large ribosomal subunit ...
 47-87 2.97e-05

Ribosomal protein L7/L12. Ribosomal protein L7/L12 refers to the large ribosomal subunit proteins L7 and L12, which are identical except that L7 is acetylated at the N terminus. It is a component of the L7/L12 stalk, which is located at the surface of the ribosome. The stalk base consists of a portion of the 23S rRNA and ribosomal proteins L11 and L10. An extended C-terminal helix of L10 provides the binding site for L7/L12. L7/L12 consists of two domains joined by a flexible hinge, with the helical N-terminal domain (NTD) forming pairs of homodimers that bind to the extended helix of L10. It is the only multimeric ribosomal component, with either four or six copies per ribosome that occur as two or three dimers bound to the L10 helix. L7/L12 is the only ribosomal protein that does not interact directly with rRNA, but instead has indirect interactions through L10. The globular C-terminal domains of L7/L12 are highly mobile. They are exposed to the cytoplasm and contain binding sites for other molecules. Initiation factors, elongation factors, and release factors are known to interact with the L7/L12 stalk during their GTP-dependent cycles. The binding site for the factors EF-Tu and EF-G comprises L7/L12, L10, L11, the L11-binding region of 23S rRNA, and the sarcin-ricin loop of 23S rRNA. Removal of L7/L12 has minimal effect on factor binding and it has been proposed that L7/L12 induces the catalytically active conformation of EF-Tu and EF-G, thereby stimulating the GTPase activity of both factors. In eukaryotes, the proteins that perform the equivalent function to L7/L12 are called P1 and P2, which do not share sequence similarity with L7/L12. However, a bacterial L7/L12 homolog is found in some eukaryotes, in mitochondria and chloroplasts. In archaea, the protein equivalent to L7/L12 is called aL12 or L12p, but it is closer in sequence to P1 and P2 than to L7/L12.


Pssm-ID: 100102 [Multi-domain]  Cd Length: 127  Bit Score: 41.76  E-value: 2.97e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2439149132  47 ILNRVLANESIYAIKELREMTNLGLKEAKDLCDtiKASKKV 87
Cdd:cd00387    64 VLESFGAAKKIAVIKEVREITGLGLKEAKDLVE--SAPKVL 102
Ribosomal_L12 pfam00542
Ribosomal protein L7/L12 C-terminal domain;
57-79 3.27e-05

Ribosomal protein L7/L12 C-terminal domain;


Pssm-ID: 425742  Cd Length: 67  Bit Score: 40.14  E-value: 3.27e-05
                          10        20
                  ....*....|....*....|...
gi 2439149132  57 IYAIKELREMTNLGLKEAKDLCD 79
Cdd:pfam00542  13 IAVIKAVREITGLGLKEAKDLVE 35
rpl12 CHL00083
ribosomal protein L12
 47-80 4.46e-04

ribosomal protein L12


Pssm-ID: 214358 [Multi-domain]  Cd Length: 131  Bit Score: 38.41  E-value: 4.46e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2439149132  47 ILNRVLANESIYAIKELREMTNLGLKEAKDLCDT 80
Cdd:CHL00083   67 ILEEVPADKRIAVLKVVRSLTGLGLKEAKELVES 100
L12 TIGR00855
ribosomal protein L7/L12; Ribosomal proteins L7 and L12 are synonymous except for ...
 51-99 4.62e-04

ribosomal protein L7/L12; Ribosomal proteins L7 and L12 are synonymous except for post-translational modification of the N-terminal amino acid. THis model resembles pfam00542 but matches the full length of prokaryotic and organellar proteins rather than just the C-terminus. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273301 [Multi-domain]  Cd Length: 123  Bit Score: 38.20  E-value: 4.62e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2439149132  51 VLANESIYAIKELREMTNLGLKEAKDLCDTIKASKKvpyeykyEDTAKS 99
Cdd:TIGR00855  63 GAGDNKIAVIKVVREITGLGLKEAKDLVEGAPKALK-------EGVSKE 104
 
Name Accession Description Interval E-value
RplL COG0222
Ribosomal protein L7/L12 [Translation, ribosomal structure and biogenesis]; Ribosomal protein ...
 57-85 1.31e-05

Ribosomal protein L7/L12 [Translation, ribosomal structure and biogenesis]; Ribosomal protein L7/L12 is part of the Pathway/BioSystem: Ribosome 50S subunit


Pssm-ID: 439992  Cd Length: 125  Bit Score: 42.41  E-value: 1.31e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2439149132  57 IYAIKELREMTNLGLKEAKDLCD----TIK--ASK 85
Cdd:COG0222    71 IAVIKVVREITGLGLKEAKDLVEgapkPVKegVSK 105
Ribosomal_L7_L12 cd00387
Ribosomal protein L7/L12. Ribosomal protein L7/L12 refers to the large ribosomal subunit ...
 47-87 2.97e-05

Ribosomal protein L7/L12. Ribosomal protein L7/L12 refers to the large ribosomal subunit proteins L7 and L12, which are identical except that L7 is acetylated at the N terminus. It is a component of the L7/L12 stalk, which is located at the surface of the ribosome. The stalk base consists of a portion of the 23S rRNA and ribosomal proteins L11 and L10. An extended C-terminal helix of L10 provides the binding site for L7/L12. L7/L12 consists of two domains joined by a flexible hinge, with the helical N-terminal domain (NTD) forming pairs of homodimers that bind to the extended helix of L10. It is the only multimeric ribosomal component, with either four or six copies per ribosome that occur as two or three dimers bound to the L10 helix. L7/L12 is the only ribosomal protein that does not interact directly with rRNA, but instead has indirect interactions through L10. The globular C-terminal domains of L7/L12 are highly mobile. They are exposed to the cytoplasm and contain binding sites for other molecules. Initiation factors, elongation factors, and release factors are known to interact with the L7/L12 stalk during their GTP-dependent cycles. The binding site for the factors EF-Tu and EF-G comprises L7/L12, L10, L11, the L11-binding region of 23S rRNA, and the sarcin-ricin loop of 23S rRNA. Removal of L7/L12 has minimal effect on factor binding and it has been proposed that L7/L12 induces the catalytically active conformation of EF-Tu and EF-G, thereby stimulating the GTPase activity of both factors. In eukaryotes, the proteins that perform the equivalent function to L7/L12 are called P1 and P2, which do not share sequence similarity with L7/L12. However, a bacterial L7/L12 homolog is found in some eukaryotes, in mitochondria and chloroplasts. In archaea, the protein equivalent to L7/L12 is called aL12 or L12p, but it is closer in sequence to P1 and P2 than to L7/L12.


Pssm-ID: 100102 [Multi-domain]  Cd Length: 127  Bit Score: 41.76  E-value: 2.97e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2439149132  47 ILNRVLANESIYAIKELREMTNLGLKEAKDLCDtiKASKKV 87
Cdd:cd00387    64 VLESFGAAKKIAVIKEVREITGLGLKEAKDLVE--SAPKVL 102
Ribosomal_L12 pfam00542
Ribosomal protein L7/L12 C-terminal domain;
57-79 3.27e-05

Ribosomal protein L7/L12 C-terminal domain;


Pssm-ID: 425742  Cd Length: 67  Bit Score: 40.14  E-value: 3.27e-05
                          10        20
                  ....*....|....*....|...
gi 2439149132  57 IYAIKELREMTNLGLKEAKDLCD 79
Cdd:pfam00542  13 IAVIKAVREITGLGLKEAKDLVE 35
rpl12 CHL00083
ribosomal protein L12
 47-80 4.46e-04

ribosomal protein L12


Pssm-ID: 214358 [Multi-domain]  Cd Length: 131  Bit Score: 38.41  E-value: 4.46e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2439149132  47 ILNRVLANESIYAIKELREMTNLGLKEAKDLCDT 80
Cdd:CHL00083   67 ILEEVPADKRIAVLKVVRSLTGLGLKEAKELVES 100
L12 TIGR00855
ribosomal protein L7/L12; Ribosomal proteins L7 and L12 are synonymous except for ...
 51-99 4.62e-04

ribosomal protein L7/L12; Ribosomal proteins L7 and L12 are synonymous except for post-translational modification of the N-terminal amino acid. THis model resembles pfam00542 but matches the full length of prokaryotic and organellar proteins rather than just the C-terminus. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273301 [Multi-domain]  Cd Length: 123  Bit Score: 38.20  E-value: 4.62e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2439149132  51 VLANESIYAIKELREMTNLGLKEAKDLCDTIKASKKvpyeykyEDTAKS 99
Cdd:TIGR00855  63 GAGDNKIAVIKVVREITGLGLKEAKDLVEGAPKALK-------EGVSKE 104
 
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