NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1698038986|ref|WP_141428625|]
View 

MULTISPECIES: elongation factor P [Alistipes]

Protein Classification

elongation factor P( domain architecture ID 11415475)

elongation factor P (EF-P) is an essential protein that stimulates ribosomal peptidyltransferase activity

Gene Ontology:  GO:0005737|GO:0005829|GO:0003746
PubMed:  23239624|31178848

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 1-188 1.59e-98

Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ribosomal structure and biogenesis]; Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) is part of the Pathway/BioSystem: Translation factors


:

Pssm-ID: 440001 [Multi-domain]  Cd Length: 186  Bit Score: 282.68  E-value: 1.59e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698038986   1 MATTADIKIGMCIELDGKTFQIVDFQHVKPGKGPAFVRTKLKNLENGRVLDNTFSAGVKIEPVRVERRPYQFTYEDDLGM 80
Cdd:COG0231     1 MISANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698038986  81 HFMHTETFEEINIDKNLI-NNYDLMADGQIVEVMFHteKETVLSAELPPIVDMEVTYTEPGVKGDTAsTNSLKPATVNTG 159
Cdd:COG0231    81 VFMDTETYEQIELPKEVVgDAAKFLKEGMEVTVLFY--NGKPISVELPNFVELEVTETEPGVKGDTA-TGGTKPATLETG 157

                         170       180
                  ....*....|....*....|....*....
gi 1698038986 160 ATIRVPLFINTGDKIRVDTRTREYYERIK 188
Cdd:COG0231   158 AVVQVPLFIEEGDKIKVDTRTGEYVERAK 186
 
Name Accession Description Interval E-value
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 1-188 1.59e-98

Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ribosomal structure and biogenesis]; Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440001 [Multi-domain]  Cd Length: 186  Bit Score: 282.68  E-value: 1.59e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698038986   1 MATTADIKIGMCIELDGKTFQIVDFQHVKPGKGPAFVRTKLKNLENGRVLDNTFSAGVKIEPVRVERRPYQFTYEDDLGM 80
Cdd:COG0231     1 MISANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698038986  81 HFMHTETFEEINIDKNLI-NNYDLMADGQIVEVMFHteKETVLSAELPPIVDMEVTYTEPGVKGDTAsTNSLKPATVNTG 159
Cdd:COG0231    81 VFMDTETYEQIELPKEVVgDAAKFLKEGMEVTVLFY--NGKPISVELPNFVELEVTETEPGVKGDTA-TGGTKPATLETG 157

                         170       180
                  ....*....|....*....|....*....
gi 1698038986 160 ATIRVPLFINTGDKIRVDTRTREYYERIK 188
Cdd:COG0231   158 AVVQVPLFIEEGDKIKVDTRTGEYVERAK 186
PRK00529 PRK00529
elongation factor P; Validated
 1-188 6.94e-93

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 268.46  E-value: 6.94e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698038986   1 MATTADIKIGMCIELDGKTFQIVDFQHVKPGKGPAFVRTKLKNLENGRVLDNTFSAGVKIEPVRVERRPYQFTYEDDLGM 80
Cdd:PRK00529    1 MISANDLRKGLVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGDGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698038986  81 HFMHTETFEEINIDKNLI-NNYDLMADGQIVEVMFHteKETVLSAELPPIVDMEVTYTEPGVKGDTAsTNSLKPATVNTG 159
Cdd:PRK00529   81 VFMDTETYEQIEVPADQVgDAAKFLKEGMEVTVVFY--NGEPISVELPNFVELEVTETEPGVKGDTA-SGGTKPATLETG 157

                         170       180
                  ....*....|....*....|....*....
gi 1698038986 160 ATIRVPLFINTGDKIRVDTRTREYYERIK 188
Cdd:PRK00529  158 AVVQVPLFINEGEKIKVDTRTGEYVERAK 186
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 2-187 5.13e-88

translation elongation factor P; function: involved in peptide bond synthesis. stimulate efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (by similarity). The trusted cutoff of this model is set high enough to exclude members of TIGR02178, an EFP-like protein of certain Gammaproteobacteria. [Protein synthesis, Translation factors]


Pssm-ID: 272867 [Multi-domain]  Cd Length: 184  Bit Score: 255.85  E-value: 5.13e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698038986   2 ATTADIKIGMCIELDGKTFQIVDFQHVKPGKGPAFVRTKLKNLENGRVLDNTFSAGVKIEPVRVERRPYQFTYEDDLGMH 81
Cdd:TIGR00038   1 ISANDLRKGLKIELDGEPYVVLEFEHVKPGKGQAFVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698038986  82 FMHTETFEEINIDKNLI-NNYDLMADGQIVEVMFHteKETVLSAELPPIVDMEVTYTEPGVKGDTAsTNSLKPATVNTGA 160
Cdd:TIGR00038  81 FMDTETYEQIELPKDLLgDAAKFLKENMEVSVVFY--NGEPIGVELPNFVELEVTETEPGVKGDTA-SGSTKPATLETGA 157

                         170       180
                  ....*....|....*....|....*..
gi 1698038986 161 TIRVPLFINTGDKIRVDTRTREYYERI 187
Cdd:TIGR00038 158 VVQVPLFIEEGEKIKVDTRTGEYVERA 184
Elong-fact-P_C pfam09285
Elongation factor P, C-terminal; Members of this family of nucleic acid binding domains are ...
 130-186 5.89e-30

Elongation factor P, C-terminal; Members of this family of nucleic acid binding domains are predominantly found in elongation factor P, where they adopt an OB-fold, with five beta-strands forming a beta-barrel in a Greek-key topology.


Pssm-ID: 430503 [Multi-domain]  Cd Length: 56  Bit Score: 104.38  E-value: 5.89e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1698038986 130 VDMEVTYTEPGVKGDTAStNSLKPATVNTGATIRVPLFINTGDKIRVDTRTREYYER 186
Cdd:pfam09285   1 VELEVTETEPGVKGDTAS-GATKPATLETGAEVQVPLFINEGDKIKVDTRTGEYVER 56
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 130-186 1.10e-28

Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in elongation factor P, where they adopt an OB-fold, with five beta-strands forming a beta-barrel in a Greek-key topology.


Pssm-ID: 214849 [Multi-domain]  Cd Length: 57  Bit Score: 100.99  E-value: 1.10e-28
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1698038986  130 VDMEVTYTEPGVKGDTASTNSLKPATVNTGATIRVPLFINTGDKIRVDTRTREYYER 186
Cdd:smart00841   1 VELEVTETEPGVKGDTASGGTKKPATLETGAVVQVPLFINEGDKIKVDTRTGEYVSR 57
S1_EF-P_repeat_2 cd05794
S1_EF-P_repeat_2: Translation elongation factor P (EF-P), S1-like RNA-binding domain, repeat 1. ...
 130-186 7.04e-26

S1_EF-P_repeat_2: Translation elongation factor P (EF-P), S1-like RNA-binding domain, repeat 1. EF-P stimulates the peptidyltransferase activity in the prokaryotic 70S ribosome. EF-P enhances the synthesis of certain dipeptides with N-formylmethionyl-tRNA and puromycine in vitro. EF-P binds to both the 30S and 50S ribosomal subunits. EF-P binds near the streptomycine binding site of the 16S rRNA in the 30S subunit. EF-P interacts with domains 2 and 5 of the 23S rRNA. The L16 ribosomal protein of the 50S or its N-terminal fragment are required for EF-P mediated peptide bond synthesis, whereas L11, L15, and L7/L12 are not required in this reaction, suggesting that EF-P may function at a different ribosomal site than most other translation factors. EF-P is essential for cell viability and is required for protein synthesis. EF-P is mainly present in bacteria. The EF-P homologs in archaea and eukaryotes are the initiation factors aIF5A and eIF5A, respectively. EF-P has 3 domains (domains I, II, and III). Domains II and III are S1-like domains. This CD includes domain III (the second S1 domain of EF_P). Domains II and III of have structural homology to the eIF5A domain C, suggesting that domains II and III evolved by duplication.


Pssm-ID: 240220 [Multi-domain]  Cd Length: 56  Bit Score: 94.13  E-value: 7.04e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1698038986 130 VDMEVTYTEPGVKGDTAsTNSLKPATVNTGATIRVPLFINTGDKIRVDTRTREYYER 186
Cdd:cd05794     1 VELEVTETEPGVKGDTA-SSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 56
 
Name Accession Description Interval E-value
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 1-188 1.59e-98

Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ribosomal structure and biogenesis]; Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440001 [Multi-domain]  Cd Length: 186  Bit Score: 282.68  E-value: 1.59e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698038986   1 MATTADIKIGMCIELDGKTFQIVDFQHVKPGKGPAFVRTKLKNLENGRVLDNTFSAGVKIEPVRVERRPYQFTYEDDLGM 80
Cdd:COG0231     1 MISANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698038986  81 HFMHTETFEEINIDKNLI-NNYDLMADGQIVEVMFHteKETVLSAELPPIVDMEVTYTEPGVKGDTAsTNSLKPATVNTG 159
Cdd:COG0231    81 VFMDTETYEQIELPKEVVgDAAKFLKEGMEVTVLFY--NGKPISVELPNFVELEVTETEPGVKGDTA-TGGTKPATLETG 157

                         170       180
                  ....*....|....*....|....*....
gi 1698038986 160 ATIRVPLFINTGDKIRVDTRTREYYERIK 188
Cdd:COG0231   158 AVVQVPLFIEEGDKIKVDTRTGEYVERAK 186
PRK00529 PRK00529
elongation factor P; Validated
 1-188 6.94e-93

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 268.46  E-value: 6.94e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698038986   1 MATTADIKIGMCIELDGKTFQIVDFQHVKPGKGPAFVRTKLKNLENGRVLDNTFSAGVKIEPVRVERRPYQFTYEDDLGM 80
Cdd:PRK00529    1 MISANDLRKGLVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGDGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698038986  81 HFMHTETFEEINIDKNLI-NNYDLMADGQIVEVMFHteKETVLSAELPPIVDMEVTYTEPGVKGDTAsTNSLKPATVNTG 159
Cdd:PRK00529   81 VFMDTETYEQIEVPADQVgDAAKFLKEGMEVTVVFY--NGEPISVELPNFVELEVTETEPGVKGDTA-SGGTKPATLETG 157

                         170       180
                  ....*....|....*....|....*....
gi 1698038986 160 ATIRVPLFINTGDKIRVDTRTREYYERIK 188
Cdd:PRK00529  158 AVVQVPLFINEGEKIKVDTRTGEYVERAK 186
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 2-187 5.13e-88

translation elongation factor P; function: involved in peptide bond synthesis. stimulate efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (by similarity). The trusted cutoff of this model is set high enough to exclude members of TIGR02178, an EFP-like protein of certain Gammaproteobacteria. [Protein synthesis, Translation factors]


Pssm-ID: 272867 [Multi-domain]  Cd Length: 184  Bit Score: 255.85  E-value: 5.13e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698038986   2 ATTADIKIGMCIELDGKTFQIVDFQHVKPGKGPAFVRTKLKNLENGRVLDNTFSAGVKIEPVRVERRPYQFTYEDDLGMH 81
Cdd:TIGR00038   1 ISANDLRKGLKIELDGEPYVVLEFEHVKPGKGQAFVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698038986  82 FMHTETFEEINIDKNLI-NNYDLMADGQIVEVMFHteKETVLSAELPPIVDMEVTYTEPGVKGDTAsTNSLKPATVNTGA 160
Cdd:TIGR00038  81 FMDTETYEQIELPKDLLgDAAKFLKENMEVSVVFY--NGEPIGVELPNFVELEVTETEPGVKGDTA-SGSTKPATLETGA 157

                         170       180
                  ....*....|....*....|....*..
gi 1698038986 161 TIRVPLFINTGDKIRVDTRTREYYERI 187
Cdd:TIGR00038 158 VVQVPLFIEEGEKIKVDTRTGEYVERA 184
PRK04542 PRK04542
elongation factor P; Provisional
 1-186 4.69e-32

elongation factor P; Provisional


Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 113.90  E-value: 4.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698038986   1 MATTADIKIGMCIELDGKTFQIVDFQHVKP-GKGPAFV-RTKLKNLENGRVLDNTFSAGVKIEPVRVERRPYQFTYEDDL 78
Cdd:PRK04542    1 MPKANEIKKGMVVEYNGKLLLVKDIDRQSPsGRGGATLyKMRFYDVRTGLKVEERFKGDDILDTVDLTRRPVTFSYIDGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698038986  79 GMHFMHTETFEEINIDKNLINNYDLMADGQIVEVMFHTEKETVLSAELPPIVDMEVTYTEPGVKGDTASTNSlKPATVNT 158
Cdd:PRK04542   81 EYVFMDNEDYTPYTFKKDQIEDELLFIPEGMPGMQVLTVDGQPVALELPQTVDLEIVETAPSIKGASASART-KPATLST 159

                         170       180
                  ....*....|....*....|....*...
gi 1698038986 159 GATIRVPLFINTGDKIRVDTRTREYYER 186
Cdd:PRK04542  160 GLVIQVPEYISTGEKIRINTEERKFMGR 187
PRK14578 PRK14578
elongation factor P; Provisional
 1-186 4.83e-31

elongation factor P; Provisional


Pssm-ID: 173042 [Multi-domain]  Cd Length: 187  Bit Score: 111.47  E-value: 4.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698038986   1 MATTADIKIGMCIELDGKTFQIVD--FQHVKPGKGPAFVRTKLKNLENGRVLDNTFSAGVKIEPVRVERRPYQFTYEDDL 78
Cdd:PRK14578    1 MYTTSDFKKGLVIQLDGAPCLLLDvtFQSPSARGANTMVKTKYRNLLTGQVLEKTFRSGDKVEEADFERHKGQFLYADGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698038986  79 GMHFMHTETFEEINIDKNLINNYDL-MADGqiVEVMFHTEKETVLSAELPPIVDMEVTYTEPGVKGDTAsTNSLKPATVN 157
Cdd:PRK14578   81 RGVFMDLETYEQFEMEEDAFSAIAPfLLDG--TEVQLGLFQGRMVNVDLPMTVELTVTDTAPVMKNATA-TAQTKEAVLE 157

                         170       180
                  ....*....|....*....|....*....
gi 1698038986 158 TGATIRVPLFINTGDKIRVDTRTREYYER 186
Cdd:PRK14578  158 TGLRLQVPPYLESGEKIKVDTRDGRFISR 186
Elong-fact-P_C pfam09285
Elongation factor P, C-terminal; Members of this family of nucleic acid binding domains are ...
 130-186 5.89e-30

Elongation factor P, C-terminal; Members of this family of nucleic acid binding domains are predominantly found in elongation factor P, where they adopt an OB-fold, with five beta-strands forming a beta-barrel in a Greek-key topology.


Pssm-ID: 430503 [Multi-domain]  Cd Length: 56  Bit Score: 104.38  E-value: 5.89e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1698038986 130 VDMEVTYTEPGVKGDTAStNSLKPATVNTGATIRVPLFINTGDKIRVDTRTREYYER 186
Cdd:pfam09285   1 VELEVTETEPGVKGDTAS-GATKPATLETGAEVQVPLFINEGDKIKVDTRTGEYVER 56
PRK12426 PRK12426
elongation factor P; Provisional
 1-187 7.40e-30

elongation factor P; Provisional


Pssm-ID: 183522 [Multi-domain]  Cd Length: 185  Bit Score: 108.39  E-value: 7.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698038986   1 MATTADIKIGMCIELDGKTFQIVDFQHVKPGKGPAFVRTKLKNLENGRVLDNTFSAGVKIEPVRVERRPYQFTYEDDLGM 80
Cdd:PRK12426    1 MVLSSQLSVGMFISTKDGLYKVVSVSKVTGPKGETFIKVSLQAADSDVVVERNFKAGQEVKEAQFEPRNLEYLYLEGDEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698038986  81 HFMHTETFEEINIDKNLI-NNYDLMADGQIVEVMFHteKETVLSAELPPIVDMEVTYTEpgVKGDTAS-TNSLKPATVNT 158
Cdd:PRK12426   81 LFLDLGNYDKIYIPKEIMkDNFLFLKAGVTVSALVY--DGTVFSVELPHFLELMVSKTD--FPGDSLSlSGGAKKALLET 156

                         170       180
                  ....*....|....*....|....*....
gi 1698038986 159 GATIRVPLFINTGDKIRVDTRTREYYERI 187
Cdd:PRK12426  157 GVEVLVPPFVEIGDVIKVDTRTCEYIQRV 185
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 130-186 1.10e-28

Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in elongation factor P, where they adopt an OB-fold, with five beta-strands forming a beta-barrel in a Greek-key topology.


Pssm-ID: 214849 [Multi-domain]  Cd Length: 57  Bit Score: 100.99  E-value: 1.10e-28
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1698038986  130 VDMEVTYTEPGVKGDTASTNSLKPATVNTGATIRVPLFINTGDKIRVDTRTREYYER 186
Cdd:smart00841   1 VELEVTETEPGVKGDTASGGTKKPATLETGAVVQVPLFINEGDKIKVDTRTGEYVSR 57
S1_EF-P_repeat_2 cd05794
S1_EF-P_repeat_2: Translation elongation factor P (EF-P), S1-like RNA-binding domain, repeat 1. ...
 130-186 7.04e-26

S1_EF-P_repeat_2: Translation elongation factor P (EF-P), S1-like RNA-binding domain, repeat 1. EF-P stimulates the peptidyltransferase activity in the prokaryotic 70S ribosome. EF-P enhances the synthesis of certain dipeptides with N-formylmethionyl-tRNA and puromycine in vitro. EF-P binds to both the 30S and 50S ribosomal subunits. EF-P binds near the streptomycine binding site of the 16S rRNA in the 30S subunit. EF-P interacts with domains 2 and 5 of the 23S rRNA. The L16 ribosomal protein of the 50S or its N-terminal fragment are required for EF-P mediated peptide bond synthesis, whereas L11, L15, and L7/L12 are not required in this reaction, suggesting that EF-P may function at a different ribosomal site than most other translation factors. EF-P is essential for cell viability and is required for protein synthesis. EF-P is mainly present in bacteria. The EF-P homologs in archaea and eukaryotes are the initiation factors aIF5A and eIF5A, respectively. EF-P has 3 domains (domains I, II, and III). Domains II and III are S1-like domains. This CD includes domain III (the second S1 domain of EF_P). Domains II and III of have structural homology to the eIF5A domain C, suggesting that domains II and III evolved by duplication.


Pssm-ID: 240220 [Multi-domain]  Cd Length: 56  Bit Score: 94.13  E-value: 7.04e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1698038986 130 VDMEVTYTEPGVKGDTAsTNSLKPATVNTGATIRVPLFINTGDKIRVDTRTREYYER 186
Cdd:cd05794     1 VELEVTETEPGVKGDTA-SSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 56
EFP_N pfam08207
Elongation factor P (EF-P) KOW-like domain;
3-60 3.71e-23

Elongation factor P (EF-P) KOW-like domain;


Pssm-ID: 429864 [Multi-domain]  Cd Length: 58  Bit Score: 87.10  E-value: 3.71e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1698038986   3 TTADIKIGMCIELDGKTFQIVDFQHVKPGKGPAFVRTKLKNLENGRVLDNTFSAGVKI 60
Cdd:pfam08207   1 SANELRKGNVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLRTGAKVEKTFKAGDKV 58
S1_EF-P_repeat_1 cd04470
S1_EF-P_repeat_1: Translation elongation factor P (EF-P), S1-like RNA-binding domain, repeat 1. ...
 66-127 3.38e-13

S1_EF-P_repeat_1: Translation elongation factor P (EF-P), S1-like RNA-binding domain, repeat 1. EF-P stimulates the peptidyltransferase activity in the prokaryotic 70S ribosome. EF-P enhances the synthesis of certain dipeptides with N-formylmethionyl-tRNA and puromycine in vitro. EF-P binds to both the 30S and 50S ribosomal subunits. EF-P binds near the streptomycine binding site of the 16S rRNA in the 30S subunit. EF-P interacts with domains 2 and 5 of the 23S rRNA. The L16 ribosomal protein of the 50S or its N-terminal fragment are required for EF-P mediated peptide bond synthesis, whereas L11, L15, and L7/L12 are not required in this reaction, suggesting that EF-P may function at a different ribosomal site than most other translation factors. EF-P is essential for cell viability and is required for protein synthesis. EF-P is mainly present in bacteria. The EF-P homologs in archaea and eukaryotes are the initiation factors aIF5A and eIF5A, respectively. EF-P has 3 domains (domains I, II, and III). Domains II and III are S1-like domains. This CD includes domain II (the first S1 domain of EF_P). Domains II and III have structural homology to the eIF5A domain C, suggesting that domains II and III evolved by duplication.


Pssm-ID: 239916 [Multi-domain]  Cd Length: 61  Bit Score: 61.32  E-value: 3.38e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1698038986  66 ERRPYQFTYEDDLGMHFMHTETFEEINIDKNLI-NNYDLMADGQIVEVMFHteKETVLSAELP 127
Cdd:cd04470     1 EEREMQYLYKDGDNYVFMDTETYEQIELPKEALgDAAKFLKEGMEVIVLFY--NGEPIGVELP 61
EFP pfam01132
Elongation factor P (EF-P) OB domain;
68-118 5.20e-11

Elongation factor P (EF-P) OB domain;


Pssm-ID: 460077 [Multi-domain]  Cd Length: 54  Bit Score: 55.49  E-value: 5.20e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1698038986  68 RPYQFTYEDDLGMHFMHTETFEEINIDKNLI-NNYDLMADGQIVEVMFHTEK 118
Cdd:pfam01132   1 REMQYLYNDGDDYVFMDNETYEQIELPKEQLgDAAKFLKEGMEVTVLFYEGK 52
 
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