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Conserved domains on  [gi|918752919|ref|WP_052605970|]
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MULTISPECIES: elongation factor P [Acidithrix]

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, ...
 6-188 1.82e-105

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: 300.01  E-value: 1.82e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919   6 SSNDFKNGMTLDLPDGLFAIVEFQHVKPGKGGAFVRTKLKNLKTKAVIDRTYRGDEKVDQAIIEKHDMQYLYRDGESYVF 85
Cdd:COG0231    3 SANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGYVF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919  86 MDNSSYDQISVSPDELGSAASFIKEGDTASVSSYQEVVVGVELSASANLTVTNTEPGIQGDRVSGARKPATLETGFVLQV 165
Cdd:COG0231   83 MDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGAVVQV 162

                        170       180
                 ....*....|....*....|...
gi 918752919 166 PLFIEQGEKITVDTRTGEYISRA 188
Cdd:COG0231  163 PLFIEEGDKIKVDTRTGEYVERA 185
 
Name Accession Description Interval E-value
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 6-188 1.82e-105

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: 300.01  E-value: 1.82e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919   6 SSNDFKNGMTLDLPDGLFAIVEFQHVKPGKGGAFVRTKLKNLKTKAVIDRTYRGDEKVDQAIIEKHDMQYLYRDGESYVF 85
Cdd:COG0231    3 SANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGYVF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919  86 MDNSSYDQISVSPDELGSAASFIKEGDTASVSSYQEVVVGVELSASANLTVTNTEPGIQGDRVSGARKPATLETGFVLQV 165
Cdd:COG0231   83 MDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGAVVQV 162

                        170       180
                 ....*....|....*....|...
gi 918752919 166 PLFIEQGEKITVDTRTGEYISRA 188
Cdd:COG0231  163 PLFIEEGDKIKVDTRTGEYVERA 185
PRK00529 PRK00529
elongation factor P; Validated
 6-188 6.37e-105

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 298.89  E-value: 6.37e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919   6 SSNDFKNGMTLDLPDGLFAIVEFQHVKPGKGGAFVRTKLKNLKTKAVIDRTYRGDEKVDQAIIEKHDMQYLYRDGESYVF 85
Cdd:PRK00529   3 SANDLRKGLVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGDGYVF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919  86 MDNSSYDQISVSPDELGSAASFIKEGDTASVSSYQEVVVGVELSASANLTVTNTEPGIQGDRVSGARKPATLETGFVLQV 165
Cdd:PRK00529  83 MDTETYEQIEVPADQVGDAAKFLKEGMEVTVVFYNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLETGAVVQV 162

                        170       180
                 ....*....|....*....|...
gi 918752919 166 PLFIEQGEKITVDTRTGEYISRA 188
Cdd:PRK00529 163 PLFINEGEKIKVDTRTGEYVERA 185
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 6-188 4.91e-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: 291.67  E-value: 4.91e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919    6 SSNDFKNGMTLDLPDGLFAIVEFQHVKPGKGGAFVRTKLKNLKTKAVIDRTYRGDEKVDQAIIEKHDMQYLYRDGESYVF 85
Cdd:TIGR00038   2 SANDLRKGLKIELDGEPYVVLEFEHVKPGKGQAFVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSYVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919   86 MDNSSYDQISVSPDELGSAASFIKEGDTASVSSYQEVVVGVELSASANLTVTNTEPGIQGDRVSGARKPATLETGFVLQV 165
Cdd:TIGR00038  82 MDTETYEQIELPKDLLGDAAKFLKENMEVSVVFYNGEPIGVELPNFVELEVTETEPGVKGDTASGSTKPATLETGAVVQV 161

                         170       180
                  ....*....|....*....|...
gi 918752919  166 PLFIEQGEKITVDTRTGEYISRA 188
Cdd:TIGR00038 162 PLFIEEGEKIKVDTRTGEYVERA 184
Elong-fact-P_C pfam09285
Elongation factor P, C-terminal; Members of this family of nucleic acid binding domains are ...
 134-187 1.23e-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: 103.61  E-value: 1.23e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 918752919  134 LTVTNTEPGIQGDRVSGARKPATLETGFVLQVPLFIEQGEKITVDTRTGEYISR 187
Cdd:pfam09285   3 LEVTETEPGVKGDTASGATKPATLETGAEVQVPLFINEGDKIKVDTRTGEYVER 56
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 134-187 7.87e-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: 96.37  E-value: 7.87e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 918752919   134 LTVTNTEPGIQGDRVSGARK-PATLETGFVLQVPLFIEQGEKITVDTRTGEYISR 187
Cdd:smart00841   3 LEVTETEPGVKGDTASGGTKkPATLETGAVVQVPLFINEGDKIKVDTRTGEYVSR 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. ...
 134-187 3.45e-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: 94.90  E-value: 3.45e-26
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 918752919 134 LTVTNTEPGIQGDRVSGARKPATLETGFVLQVPLFIEQGEKITVDTRTGEYISR 187
Cdd:cd05794    3 LEVTETEPGVKGDTASSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 56
 
Name Accession Description Interval E-value
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 6-188 1.82e-105

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: 300.01  E-value: 1.82e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919   6 SSNDFKNGMTLDLPDGLFAIVEFQHVKPGKGGAFVRTKLKNLKTKAVIDRTYRGDEKVDQAIIEKHDMQYLYRDGESYVF 85
Cdd:COG0231    3 SANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGYVF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919  86 MDNSSYDQISVSPDELGSAASFIKEGDTASVSSYQEVVVGVELSASANLTVTNTEPGIQGDRVSGARKPATLETGFVLQV 165
Cdd:COG0231   83 MDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGAVVQV 162

                        170       180
                 ....*....|....*....|...
gi 918752919 166 PLFIEQGEKITVDTRTGEYISRA 188
Cdd:COG0231  163 PLFIEEGDKIKVDTRTGEYVERA 185
PRK00529 PRK00529
elongation factor P; Validated
 6-188 6.37e-105

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 298.89  E-value: 6.37e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919   6 SSNDFKNGMTLDLPDGLFAIVEFQHVKPGKGGAFVRTKLKNLKTKAVIDRTYRGDEKVDQAIIEKHDMQYLYRDGESYVF 85
Cdd:PRK00529   3 SANDLRKGLVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGDGYVF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919  86 MDNSSYDQISVSPDELGSAASFIKEGDTASVSSYQEVVVGVELSASANLTVTNTEPGIQGDRVSGARKPATLETGFVLQV 165
Cdd:PRK00529  83 MDTETYEQIEVPADQVGDAAKFLKEGMEVTVVFYNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLETGAVVQV 162

                        170       180
                 ....*....|....*....|...
gi 918752919 166 PLFIEQGEKITVDTRTGEYISRA 188
Cdd:PRK00529 163 PLFINEGEKIKVDTRTGEYVERA 185
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 6-188 4.91e-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: 291.67  E-value: 4.91e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919    6 SSNDFKNGMTLDLPDGLFAIVEFQHVKPGKGGAFVRTKLKNLKTKAVIDRTYRGDEKVDQAIIEKHDMQYLYRDGESYVF 85
Cdd:TIGR00038   2 SANDLRKGLKIELDGEPYVVLEFEHVKPGKGQAFVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSYVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919   86 MDNSSYDQISVSPDELGSAASFIKEGDTASVSSYQEVVVGVELSASANLTVTNTEPGIQGDRVSGARKPATLETGFVLQV 165
Cdd:TIGR00038  82 MDTETYEQIELPKDLLGDAAKFLKENMEVSVVFYNGEPIGVELPNFVELEVTETEPGVKGDTASGSTKPATLETGAVVQV 161

                         170       180
                  ....*....|....*....|...
gi 918752919  166 PLFIEQGEKITVDTRTGEYISRA 188
Cdd:TIGR00038 162 PLFIEEGEKIKVDTRTGEYVERA 184
PRK14578 PRK14578
elongation factor P; Provisional
 6-188 4.65e-44

elongation factor P; Provisional


Pssm-ID: 173042 [Multi-domain]  Cd Length: 187  Bit Score: 144.59  E-value: 4.65e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919   6 SSNDFKNGMTLDLPDGLFAIVEFQHVKPGKGGA--FVRTKLKNLKTKAVIDRTYRGDEKVDQAIIEKHDMQYLYRDGESY 83
Cdd:PRK14578   3 TTSDFKKGLVIQLDGAPCLLLDVTFQSPSARGAntMVKTKYRNLLTGQVLEKTFRSGDKVEEADFERHKGQFLYADGDRG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919  84 VFMDNSSYDQISVSPDELGSAASFIKEGDTASVSSYQEVVVGVELSASANLTVTNTEPGIQGDRVSGARKPATLETGFVL 163
Cdd:PRK14578  83 VFMDLETYEQFEMEEDAFSAIAPFLLDGTEVQLGLFQGRMVNVDLPMTVELTVTDTAPVMKNATATAQTKEAVLETGLRL 162

                        170       180
                 ....*....|....*....|....*
gi 918752919 164 QVPLFIEQGEKITVDTRTGEYISRA 188
Cdd:PRK14578 163 QVPPYLESGEKIKVDTRDGRFISRA 187
PRK12426 PRK12426
elongation factor P; Provisional
 7-187 4.90e-39

elongation factor P; Provisional


Pssm-ID: 183522 [Multi-domain]  Cd Length: 185  Bit Score: 131.89  E-value: 4.90e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919   7 SNDFKNGMTLDLPDGLFAIVEFQHVKPGKGGAFVRTKLKNLKTKAVIDRTYRGDEKVDQAIIEKHDMQYLYRDGESYVFM 86
Cdd:PRK12426   4 SSQLSVGMFISTKDGLYKVVSVSKVTGPKGETFIKVSLQAADSDVVVERNFKAGQEVKEAQFEPRNLEYLYLEGDEYLFL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919  87 DNSSYDQISVSPDELGSAASFIKEGDTASVSSYQEVVVGVELSASANLTVTNTEPGIQGDRVSGARKPATLETGFVLQVP 166
Cdd:PRK12426  84 DLGNYDKIYIPKEIMKDNFLFLKAGVTVSALVYDGTVFSVELPHFLELMVSKTDFPGDSLSLSGGAKKALLETGVEVLVP 163

                        170       180
                 ....*....|....*....|.
gi 918752919 167 LFIEQGEKITVDTRTGEYISR 187
Cdd:PRK12426 164 PFVEIGDVIKVDTRTCEYIQR 184
PRK04542 PRK04542
elongation factor P; Provisional
 8-188 6.42e-38

elongation factor P; Provisional


Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 128.93  E-value: 6.42e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919   8 NDFKNGMTLDLPDGLFAIVEFQHVKP-GKGGAFV-RTKLKNLKTKAVIDRTYRGDEKVDQAIIEKHDMQYLYRDGESYVF 85
Cdd:PRK04542   5 NEIKKGMVVEYNGKLLLVKDIDRQSPsGRGGATLyKMRFYDVRTGLKVEERFKGDDILDTVDLTRRPVTFSYIDGDEYVF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919  86 MDNSSYDQISVSPDELGSAASFIKEGDTA-SVSSYQEVVVGVELSASANLTVTNTEPGIQGDRVSGARKPATLETGFVLQ 164
Cdd:PRK04542  85 MDNEDYTPYTFKKDQIEDELLFIPEGMPGmQVLTVDGQPVALELPQTVDLEIVETAPSIKGASASARTKPATLSTGLVIQ 164

                        170       180
                 ....*....|....*....|....
gi 918752919 165 VPLFIEQGEKITVDTRTGEYISRA 188
Cdd:PRK04542 165 VPEYISTGEKIRINTEERKFMGRA 188
Elong-fact-P_C pfam09285
Elongation factor P, C-terminal; Members of this family of nucleic acid binding domains are ...
 134-187 1.23e-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: 103.61  E-value: 1.23e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 918752919  134 LTVTNTEPGIQGDRVSGARKPATLETGFVLQVPLFIEQGEKITVDTRTGEYISR 187
Cdd:pfam09285   3 LEVTETEPGVKGDTASGATKPATLETGAEVQVPLFINEGDKIKVDTRTGEYVER 56
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 134-187 7.87e-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: 96.37  E-value: 7.87e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 918752919   134 LTVTNTEPGIQGDRVSGARK-PATLETGFVLQVPLFIEQGEKITVDTRTGEYISR 187
Cdd:smart00841   3 LEVTETEPGVKGDTASGGTKkPATLETGAVVQVPLFINEGDKIKVDTRTGEYVSR 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. ...
 134-187 3.45e-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: 94.90  E-value: 3.45e-26
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 918752919 134 LTVTNTEPGIQGDRVSGARKPATLETGFVLQVPLFIEQGEKITVDTRTGEYISR 187
Cdd:cd05794    3 LEVTETEPGVKGDTASSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 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. ...
 69-128 6.26e-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: 91.75  E-value: 6.26e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919  69 EKHDMQYLYRDGESYVFMDNSSYDQISVSPDELGSAASFIKEGDTASVSSYQEVVVGVEL 128
Cdd:cd04470    1 EEREMQYLYKDGDNYVFMDTETYEQIELPKEALGDAAKFLKEGMEVIVLFYNGEPIGVEL 60
EFP_N pfam08207
Elongation factor P (EF-P) KOW-like domain;
6-63 1.37e-24

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


Pssm-ID: 429864 [Multi-domain]  Cd Length: 58  Bit Score: 90.57  E-value: 1.37e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 918752919    6 SSNDFKNGMTLDLPDGLFAIVEFQHVKPGKGGAFVRTKLKNLKTKAVIDRTYRGDEKV 63
Cdd:pfam08207   1 SANELRKGNVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLRTGAKVEKTFKAGDKV 58
EFP pfam01132
Elongation factor P (EF-P) OB domain;
71-124 7.52e-22

Elongation factor P (EF-P) OB domain;


Pssm-ID: 460077 [Multi-domain]  Cd Length: 54  Bit Score: 83.61  E-value: 7.52e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 918752919   71 HDMQYLYRDGESYVFMDNSSYDQISVSPDELGSAASFIKEGDTASVSSYQEVVV 124
Cdd:pfam01132   1 REMQYLYNDGDDYVFMDNETYEQIELPKEQLGDAAKFLKEGMEVTVLFYEGKPI 54
PRK03999 PRK03999
translation initiation factor IF-5A; Provisional
 25-112 8.59e-03

translation initiation factor IF-5A; Provisional


Pssm-ID: 235193 [Multi-domain]  Cd Length: 129  Bit Score: 34.89  E-value: 8.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918752919  25 IVEFQHVKPGK-GGAFVRtklknLKTKAVID---RTYRG--DEKVDQAIIEKHDMQYLYRDGESYVFMDNSSYDQISVS- 97
Cdd:PRK03999  26 IVEISKSKPGKhGSAKAR-----IVAIGIFDgqkRSLVQpvDAKVEVPIIEKKTGQVLSIMGDVVQLMDLETYETFEIPi 100

                         90
                 ....*....|....*
gi 918752919  98 PDELGSAasfIKEGD 112
Cdd:PRK03999 101 PEELKDK---LEPGV 112
 
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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