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Conserved domains on  [gi|51315778|sp|Q7VJY4|]
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RecName: Full=Elongation factor P; Short=EF-P

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

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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, ...
 3-187 3.00e-108

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: 307.33  E-value: 3.00e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778   3 IGMSELKKGLKIEIDGIPYRITEYQHVKPGKGAAFVRAKIKSFLDGKVIEKTFHAGDKCEEPNLQEKTMQFLYHDGGAFQ 82
Cdd:COG0231   2 ISANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGYV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778  83 FMDTTTYEQIALSDDQVGDVAKWIIDGLNVQILFHNEKAISVDVPLVVELTITETAPNFKGDTSSGGKKPATLETGAVVQ 162
Cdd:COG0231  82 FMDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGAVVQ 161

                       170       180
                ....*....|....*....|....*
gi 51315778 163 VPFHVLEGEKIKVNTETGEYLEKVK 187
Cdd:COG0231 162 VPLFIEEGDKIKVDTRTGEYVERAK 186
 
Name Accession Description Interval E-value
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 3-187 3.00e-108

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: 307.33  E-value: 3.00e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778   3 IGMSELKKGLKIEIDGIPYRITEYQHVKPGKGAAFVRAKIKSFLDGKVIEKTFHAGDKCEEPNLQEKTMQFLYHDGGAFQ 82
Cdd:COG0231   2 ISANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGYV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778  83 FMDTTTYEQIALSDDQVGDVAKWIIDGLNVQILFHNEKAISVDVPLVVELTITETAPNFKGDTSSGGKKPATLETGAVVQ 162
Cdd:COG0231  82 FMDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGAVVQ 161

                       170       180
                ....*....|....*....|....*
gi 51315778 163 VPFHVLEGEKIKVNTETGEYLEKVK 187
Cdd:COG0231 162 VPLFIEEGDKIKVDTRTGEYVERAK 186
PRK00529 PRK00529
elongation factor P; Validated
 3-187 3.66e-107

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 304.28  E-value: 3.66e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778    3 IGMSELKKGLKIEIDGIPYRITEYQHVKPGKGAAFVRAKIKSFLDGKVIEKTFHAGDKCEEPNLQEKTMQFLYHDGGAFQ 82
Cdd:PRK00529   2 ISANDLRKGLVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGDGYV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778   83 FMDTTTYEQIALSDDQVGDVAKWIIDGLNVQILFHNEKAISVDVPLVVELTITETAPNFKGDTSSGGKKPATLETGAVVQ 162
Cdd:PRK00529  82 FMDTETYEQIEVPADQVGDAAKFLKEGMEVTVVFYNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLETGAVVQ 161

                        170       180
                 ....*....|....*....|....*
gi 51315778  163 VPFHVLEGEKIKVNTETGEYLEKVK 187
Cdd:PRK00529 162 VPLFINEGEKIKVDTRTGEYVERAK 186
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 3-186 6.41e-102

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: 291.29  E-value: 6.41e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778     3 IGMSELKKGLKIEIDGIPYRITEYQHVKPGKGAAFVRAKIKSFLDGKVIEKTFHAGDKCEEPNLQEKTMQFLYHDGGAFQ 82
Cdd:TIGR00038   1 ISANDLRKGLKIELDGEPYVVLEFEHVKPGKGQAFVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778    83 FMDTTTYEQIALSDDQVGDVAKWIIDGLNVQILFHNEKAISVDVPLVVELTITETAPNFKGDTSSGGKKPATLETGAVVQ 162
Cdd:TIGR00038  81 FMDTETYEQIELPKDLLGDAAKFLKENMEVSVVFYNGEPIGVELPNFVELEVTETEPGVKGDTASGSTKPATLETGAVVQ 160

                         170       180
                  ....*....|....*....|....
gi 51315778   163 VPFHVLEGEKIKVNTETGEYLEKV 186
Cdd:TIGR00038 161 VPLFIEEGEKIKVDTRTGEYVERA 184
Elong-fact-P_C pfam09285
Elongation factor P, C-terminal; Members of this family of nucleic acid binding domains are ...
 130-185 2.29e-29

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: 102.84  E-value: 2.29e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 51315778   130 VELTITETAPNFKGDTSSGGKKPATLETGAVVQVPFHVLEGEKIKVNTETGEYLEK 185
Cdd:pfam09285   1 VELEVTETEPGVKGDTASGATKPATLETGAEVQVPLFINEGDKIKVDTRTGEYVER 56
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 130-185 2.88e-27

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: 97.53  E-value: 2.88e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 51315778    130 VELTITETAPNFKGDTSSGG-KKPATLETGAVVQVPFHVLEGEKIKVNTETGEYLEK 185
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. ...
 130-185 9.47e-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: 93.74  E-value: 9.47e-26
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 51315778 130 VELTITETAPNFKGDTSSGGKKPATLETGAVVQVPFHVLEGEKIKVNTETGEYLEK 185
Cdd:cd05794   1 VELEVTETEPGVKGDTASSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 56
 
Name Accession Description Interval E-value
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 3-187 3.00e-108

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: 307.33  E-value: 3.00e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778   3 IGMSELKKGLKIEIDGIPYRITEYQHVKPGKGAAFVRAKIKSFLDGKVIEKTFHAGDKCEEPNLQEKTMQFLYHDGGAFQ 82
Cdd:COG0231   2 ISANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGYV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778  83 FMDTTTYEQIALSDDQVGDVAKWIIDGLNVQILFHNEKAISVDVPLVVELTITETAPNFKGDTSSGGKKPATLETGAVVQ 162
Cdd:COG0231  82 FMDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGAVVQ 161

                       170       180
                ....*....|....*....|....*
gi 51315778 163 VPFHVLEGEKIKVNTETGEYLEKVK 187
Cdd:COG0231 162 VPLFIEEGDKIKVDTRTGEYVERAK 186
PRK00529 PRK00529
elongation factor P; Validated
 3-187 3.66e-107

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 304.28  E-value: 3.66e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778    3 IGMSELKKGLKIEIDGIPYRITEYQHVKPGKGAAFVRAKIKSFLDGKVIEKTFHAGDKCEEPNLQEKTMQFLYHDGGAFQ 82
Cdd:PRK00529   2 ISANDLRKGLVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGDGYV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778   83 FMDTTTYEQIALSDDQVGDVAKWIIDGLNVQILFHNEKAISVDVPLVVELTITETAPNFKGDTSSGGKKPATLETGAVVQ 162
Cdd:PRK00529  82 FMDTETYEQIEVPADQVGDAAKFLKEGMEVTVVFYNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLETGAVVQ 161

                        170       180
                 ....*....|....*....|....*
gi 51315778  163 VPFHVLEGEKIKVNTETGEYLEKVK 187
Cdd:PRK00529 162 VPLFINEGEKIKVDTRTGEYVERAK 186
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 3-186 6.41e-102

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: 291.29  E-value: 6.41e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778     3 IGMSELKKGLKIEIDGIPYRITEYQHVKPGKGAAFVRAKIKSFLDGKVIEKTFHAGDKCEEPNLQEKTMQFLYHDGGAFQ 82
Cdd:TIGR00038   1 ISANDLRKGLKIELDGEPYVVLEFEHVKPGKGQAFVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778    83 FMDTTTYEQIALSDDQVGDVAKWIIDGLNVQILFHNEKAISVDVPLVVELTITETAPNFKGDTSSGGKKPATLETGAVVQ 162
Cdd:TIGR00038  81 FMDTETYEQIELPKDLLGDAAKFLKENMEVSVVFYNGEPIGVELPNFVELEVTETEPGVKGDTASGSTKPATLETGAVVQ 160

                         170       180
                  ....*....|....*....|....
gi 51315778   163 VPFHVLEGEKIKVNTETGEYLEKV 186
Cdd:TIGR00038 161 VPLFIEEGEKIKVDTRTGEYVERA 184
PRK14578 PRK14578
elongation factor P; Provisional
 6-185 9.92e-45

elongation factor P; Provisional


Pssm-ID: 173042 [Multi-domain]  Cd Length: 187  Bit Score: 146.52  E-value: 9.92e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778    6 SELKKGLKIEIDGIPYRITEYQHVKP-GKGA-AFVRAKIKSFLDGKVIEKTFHAGDKCEEPNLQEKTMQFLYHDGGAFQF 83
Cdd:PRK14578   5 SDFKKGLVIQLDGAPCLLLDVTFQSPsARGAnTMVKTKYRNLLTGQVLEKTFRSGDKVEEADFERHKGQFLYADGDRGVF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778   84 MDTTTYEQIALSDDQVGDVAKWIIDGLNVQILFHNEKAISVDVPLVVELTITETAPNFKGDTSSGGKKPATLETGAVVQV 163
Cdd:PRK14578  85 MDLETYEQFEMEEDAFSAIAPFLLDGTEVQLGLFQGRMVNVDLPMTVELTVTDTAPVMKNATATAQTKEAVLETGLRLQV 164

                        170       180
                 ....*....|....*....|..
gi 51315778  164 PFHVLEGEKIKVNTETGEYLEK 185
Cdd:PRK14578 165 PPYLESGEKIKVDTRDGRFISR 186
PRK04542 PRK04542
elongation factor P; Provisional
 6-183 1.67e-39

elongation factor P; Provisional


Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 133.16  E-value: 1.67e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778    6 SELKKGLKIEIDGIPYRITEYQHVKPGKGAAFVRAKIKsFLD---GKVIEKTFHAGDKCEEPNLQEKTMQFLYHDGGAFQ 82
Cdd:PRK04542   5 NEIKKGMVVEYNGKLLLVKDIDRQSPSGRGGATLYKMR-FYDvrtGLKVEERFKGDDILDTVDLTRRPVTFSYIDGDEYV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778   83 FMDTTTYEQIALSDDQVGDVAKWIIDGL-NVQILFHNEKAISVDVPLVVELTITETAPNFKGDTSSGGKKPATLETGAVV 161
Cdd:PRK04542  84 FMDNEDYTPYTFKKDQIEDELLFIPEGMpGMQVLTVDGQPVALELPQTVDLEIVETAPSIKGASASARTKPATLSTGLVI 163

                        170       180
                 ....*....|....*....|..
gi 51315778  162 QVPFHVLEGEKIKVNTETGEYL 183
Cdd:PRK04542 164 QVPEYISTGEKIRINTEERKFM 185
PRK12426 PRK12426
elongation factor P; Provisional
 6-186 5.67e-33

elongation factor P; Provisional


Pssm-ID: 183522 [Multi-domain]  Cd Length: 185  Bit Score: 116.10  E-value: 5.67e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778    6 SELKKGLKIEIDGIPYRITEYQHVKPGKGAAFVRAKIKSFLDGKVIEKTFHAGDKCEEPNLQEKTMQFLYHDGGAFQFMD 85
Cdd:PRK12426   5 SQLSVGMFISTKDGLYKVVSVSKVTGPKGETFIKVSLQAADSDVVVERNFKAGQEVKEAQFEPRNLEYLYLEGDEYLFLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778   86 TTTYEQIALSDDQVGDVAKWIIDGLNVQILFHNEKAISVDVPLVVELTITETapNFKGDTS--SGGKKPATLETGAVVQV 163
Cdd:PRK12426  85 LGNYDKIYIPKEIMKDNFLFLKAGVTVSALVYDGTVFSVELPHFLELMVSKT--DFPGDSLslSGGAKKALLETGVEVLV 162

                        170       180
                 ....*....|....*....|...
gi 51315778  164 PFHVLEGEKIKVNTETGEYLEKV 186
Cdd:PRK12426 163 PPFVEIGDVIKVDTRTCEYIQRV 185
Elong-fact-P_C pfam09285
Elongation factor P, C-terminal; Members of this family of nucleic acid binding domains are ...
 130-185 2.29e-29

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: 102.84  E-value: 2.29e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 51315778   130 VELTITETAPNFKGDTSSGGKKPATLETGAVVQVPFHVLEGEKIKVNTETGEYLEK 185
Cdd:pfam09285   1 VELEVTETEPGVKGDTASGATKPATLETGAEVQVPLFINEGDKIKVDTRTGEYVER 56
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 130-185 2.88e-27

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: 97.53  E-value: 2.88e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 51315778    130 VELTITETAPNFKGDTSSGG-KKPATLETGAVVQVPFHVLEGEKIKVNTETGEYLEK 185
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. ...
 130-185 9.47e-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: 93.74  E-value: 9.47e-26
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 51315778 130 VELTITETAPNFKGDTSSGGKKPATLETGAVVQVPFHVLEGEKIKVNTETGEYLEK 185
Cdd:cd05794   1 VELEVTETEPGVKGDTASSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 56
S1_EF-P_repeat_1 cd04470
S1_EF-P_repeat_1: Translation elongation factor P (EF-P), S1-like RNA-binding domain, repeat 1. ...
 68-127 1.87e-25

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: 92.91  E-value: 1.87e-25
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778  68 EKTMQFLYHDGGAFQFMDTTTYEQIALSDDQVGDVAKWIIDGLNVQILFHNEKAISVDVP 127
Cdd:cd04470   2 EREMQYLYKDGDNYVFMDTETYEQIELPKEALGDAAKFLKEGMEVIVLFYNGEPIGVELP 61
EFP_N pfam08207
Elongation factor P (EF-P) KOW-like domain;
5-60 2.61e-24

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


Pssm-ID: 429864 [Multi-domain]  Cd Length: 58  Bit Score: 89.80  E-value: 2.61e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 51315778     5 MSELKKGLKIEIDGIPYRITEYQHVKPGKGAAFVRAKIKSFLDGKVIEKTFHAGDK 60
Cdd:pfam08207   2 ANELRKGNVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLRTGAKVEKTFKAGDK 57
EFP pfam01132
Elongation factor P (EF-P) OB domain;
69-122 1.75e-23

Elongation factor P (EF-P) OB domain;


Pssm-ID: 460077 [Multi-domain]  Cd Length: 54  Bit Score: 87.84  E-value: 1.75e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 51315778    69 KTMQFLYHDGGAFQFMDTTTYEQIALSDDQVGDVAKWIIDGLNVQILFHNEKAI 122
Cdd:pfam01132   1 REMQYLYNDGDDYVFMDNETYEQIELPKEQLGDAAKFLKEGMEVTVLFYEGKPI 54
PRK03999 PRK03999
translation initiation factor IF-5A; Provisional
 6-102 2.42e-10

translation initiation factor IF-5A; Provisional


Pssm-ID: 235193 [Multi-domain]  Cd Length: 129  Bit Score: 55.69  E-value: 2.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778    6 SELKKGLKIEIDGIPYRITEYQHVKPGK-GAAFVRAKIKSFLDGKVIEKTFHAGDKCEEPNLQEKTMQFLYHDGGAFQFM 84
Cdd:PRK03999   9 GELKEGSYVVIDGEPCKIVEISKSKPGKhGSAKARIVAIGIFDGQKRSLVQPVDAKVEVPIIEKKTGQVLSIMGDVVQLM 88

                         90       100
                 ....*....|....*....|
gi 51315778   85 DTTTYE--QIALSDDQVGDV 102
Cdd:PRK03999  89 DLETYEtfEIPIPEELKDKL 108
eIF_5A TIGR00037
translation elongation factor IF5A; Recent work (2009) changed the view of eIF5A in eukaryotes ...
 6-90 3.96e-06

translation elongation factor IF5A; Recent work (2009) changed the view of eIF5A in eukaryotes and aIF5A in archaea, hypusine-containing proteins, from translation initiation factor to translation elongation factor. [Protein synthesis, Translation factors]


Pssm-ID: 272866 [Multi-domain]  Cd Length: 130  Bit Score: 44.43  E-value: 3.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315778     6 SELKKGLKIEIDGIPYRITEYQHVKPGK-GAAFVRAKIKSFLDGKVIEKTFHAGDKCEEPNLQEKTMQFLYHDGGAFQFM 84
Cdd:TIGR00037  10 SALRVGGYVVIDGEPCKIVDISTSKPGKhGHAKARVVAIGIFDGQKREFVSPVTSKVEVPIVDRREAQVLAIMGGMVQLM 89


                  ....*.
gi 51315778    85 DTTTYE 90
Cdd:TIGR00037  90 DLETYE 95
 
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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