Conserved Protein Domain Family

cd00387: Ribosomal_L7_L12 
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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
View PSSM: cd00387
Aligned: 128 rows
Threshold Bit Score: 72.9585
Threshold Setting Gi: 115252764
Created: 6-Mar-2002
Updated: 2-Oct-2020
Aligned Rows:
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Conserved site includes 26 residues -Click on image for an interactive view with Cn3D
Feature 1:core dimer interface [polypeptide binding site]
  • Structure:1YL3_J; Thermus thermophilus ribosomal protein L7/L12 forms a dimer with another L7/L12 monomer (1YL3_I), defined using 3.5 A contacts
    View structure with Cn3D
  • Structure:1DD3_A; Thermotoga maritima ribosomal protein L7/L12 forms a dimer with another L7/L12 monomer (1DD3_B), defined using 3.5 A contacts
    View structure with Cn3D
  • Comment:The core dimer interface is formed mainly by interactions in the helical N-terminal domain (NTD). The NTD is also essential in binding the L10 helix.

Sequence Alignment
Format: Row Display: Color Bits: Type Selection:
Feature 1        #            ###  ##  #  #                                                      
1YL3_J         1 MTIDEIIEAIEKLTVSELAELVKKLEDKFGVta----------------------------------------------- 33  Thermus thermop...
XP_001609524  57 DRVIRLVDEILNLTLIESADLCDLCQERLAGpnvnggfipgrspfph--------------------------------- 103 Babesia bovis T2Bo
XP_765342     65 LKVIKLVDEILNLTLIEVADLCNLCQDKLSTnnvnnrlpfph-------------------------------------- 106 Theileria parva...
XP_001446675 110 KEKEQIEAYMKELFGENVPDFKAIFGGVGSIgs----------------------------------------------- 142 Paramecium tetr...
XP_001027843  90 KRVEFIADAFIELNIMEIRYLNHTLKERLIKttglsplkvnidwpslkqlengswppanpnwflqqeaiaklwpagqagl 169 Tetrahymena the...
XP_001701596  54 PKVQKLAEEIMGLTVLECSMLSEILRKKLGVqqpafsmg----------------------------------------- 92  Chlamydomonas r...
YP_506557      4 VECSEIAQKILSLSLVEAAELAAELKKVLNLpdv---------------------------------------------- 37  Neorickettsia s...
NP_870737     15 AEAKELGDKIANMTLKQAKELSDYLKDEHGIepaag-------------------------------------------- 50  Rhodopirellula ...
ZP_01088693   12 EELKTLGDKIATLTLKQAVELGDYLKDAHGIeaa---------------------------------------------- 45  Blastopirellula...
ZP_01855697   12 EETKELGDKIAGLTLLQAKDLAEYLDEVHGIkaa---------------------------------------------- 45  Planctomyces ma...
Feature 1                               #  ## ###                            ##                  
1YL3_J        34 ------------------aaPVAVAAAPVAGAaagaa-------------------qeekTEFDVVLKSFGq-NKIQVIK 75  Thermus thermop...
XP_001609524 104 ----phtffsgvgmmperlsPMGVMPQPVAATvetaepppae--------tpqptkpaqkSTGTLTLVGFDatKKIALIK 171 Babesia bovis T2Bo
XP_765342    107 ----------pnsffqyngfAGNMNFTPPPTPtnttdstdstpkntnvstkeepvkekvpVKRTIKLVGFDkeKKIDVIK 176 Theileria parva...
XP_001446675 143 -------------------qAPSQSAASSEAPkqeqkkaea-----------apkveaekKNYDVELSAIDaaQKIKIIK 192 Paramecium tetr...
XP_001027843 170 sqlfggmmgggaaggsgapqAAAAAAAPAAEKpkeea-------------------pkekQNYDVELSAIDaaQKIKIIK 230 Tetrahymena the...
XP_001701596  93 -------------ampfaaaPAAPAAAPAAAAapekke-----------------ekkekTEFDVKLESFSaeGKIKVIK 142 Chlamydomonas r...
YP_506557     38 -----------------amaPAAVAAAPATSEsvek--------------------kgeaSKFTLILKSYGe-KKTNAIK 79  Neorickettsia s...
NP_870737     51 ----------------ggavMMAGPAGDGGGAaev-----------------------eqTEFDVVLTGFGe-KKLNVVK 90  Rhodopirellula ...
ZP_01088693   46 ------------------agGGVMMAGPAAGPaeea---------------------avqTEFDVVMTSFGg-NKISVIK 85  Blastopirellula...
ZP_01855697   46 ------------------agGAVMMAGPAAEAgpaa---------------------eekTEFDVILTGFGd-NKIPVIK 85  Planctomyces ma...
Feature 1           # #      # # ##                ## #  #                 
XP_765342    177 TIRTIL------NISLRESKELIESYp---KVIKKNVSEEELEKLTKLIKDSGGHVEV 225 Theileria parva strain Muguga
XP_001446675 193 EVRQLL------NLGLKEAKDLVEKLp---ANLGKQVPKEKANELKEKLTAAGCTINL 241 Paramecium tetraurelia strain d4-2
XP_001027843 231 EVRTIL------NLGLKEAKDMVEKTp---CILKSACKKAEAEELKEKLAAIGCTINL 279 Tetrahymena thermophila SB210
XP_001701596 143 EIRALT------TLGLKEAKELVEKAp---VVIKVGVSKADAEAMKKQLETAGGKVSY 191 Chlamydomonas reinhardtii
YP_506557     80 ALKTIFkqelgqDMGLKELKDKVEAVp---VDVLSGLTKEKADAYAKILKEAECEPEL 134 Neorickettsia sennetsu str. Miyayama
NP_870737     91 VVKNIT------GASLMDAKKMVEGCp---ATLKEAVSKEDAEKVKAEIEEAGGSVEL 139 Rhodopirellula baltica SH 1
ZP_01088693   86 AIRSIT------GLGLKEAKELTEGVp---SKVKEGVSKEDAEKVKAELTDAGAEVEI 134 Blastopirellula marina DSM 3645

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