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Conserved domains on  [gi|493737087|ref|WP_006686282|]
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MULTISPECIES: elongation factor P [Citrobacter]

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, ...
 1-188 1.47e-112

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: 318.12  E-value: 1.47e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087   1 MATyySNDFRAGLKIMLDGEPYAVEASEFVKPGKGQAFARVKLRRLLTGTRVEKTFKSTDSAEGADVADMNLTFLYSDGE 80
Cdd:COG0231    1 MIS--ANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087  81 FWHFMNNTTFEQLAADEKAVGDNAKWLLDQAECIVTLWNGQPISVTPPNFVELEVIETDPGLKGDTAGTGGKPATLSTGA 160
Cdd:COG0231   79 GYVFMDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGA 158

                        170       180
                 ....*....|....*....|....*...
gi 493737087 161 VVKVPLFVQIGEVIKVDTRSGEYVSRVK 188
Cdd:COG0231  159 VVQVPLFIEEGDKIKVDTRTGEYVERAK 186
 
Name Accession Description Interval E-value
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 1-188 1.47e-112

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: 318.12  E-value: 1.47e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087   1 MATyySNDFRAGLKIMLDGEPYAVEASEFVKPGKGQAFARVKLRRLLTGTRVEKTFKSTDSAEGADVADMNLTFLYSDGE 80
Cdd:COG0231    1 MIS--ANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087  81 FWHFMNNTTFEQLAADEKAVGDNAKWLLDQAECIVTLWNGQPISVTPPNFVELEVIETDPGLKGDTAGTGGKPATLSTGA 160
Cdd:COG0231   79 GYVFMDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGA 158

                        170       180
                 ....*....|....*....|....*...
gi 493737087 161 VVKVPLFVQIGEVIKVDTRSGEYVSRVK 188
Cdd:COG0231  159 VVQVPLFIEEGDKIKVDTRTGEYVERAK 186
PRK00529 PRK00529
elongation factor P; Validated
 6-188 1.29e-111

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 315.84  E-value: 1.29e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087   6 SNDFRAGLKIMLDGEPYAVEASEFVKPGKGQAFARVKLRRLLTGTRVEKTFKSTDSAEGADVADMNLTFLYSDGEFWHFM 85
Cdd:PRK00529   4 ANDLRKGLVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGDGYVFM 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087  86 NNTTFEQLAADEKAVGDNAKWLLDQAECIVTLWNGQPISVTPPNFVELEVIETDPGLKGDTAGTGGKPATLSTGAVVKVP 165
Cdd:PRK00529  84 DTETYEQIEVPADQVGDAAKFLKEGMEVTVVFYNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLETGAVVQVP 163

                        170       180
                 ....*....|....*....|...
gi 493737087 166 LFVQIGEVIKVDTRSGEYVSRVK 188
Cdd:PRK00529 164 LFINEGEKIKVDTRTGEYVERAK 186
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 6-187 4.31e-107

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: 304.38  E-value: 4.31e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087    6 SNDFRAGLKIMLDGEPYAVEASEFVKPGKGQAFARVKLRRLLTGTRVEKTFKSTDSAEGADVADMNLTFLYSDGEFWHFM 85
Cdd:TIGR00038   3 ANDLRKGLKIELDGEPYVVLEFEHVKPGKGQAFVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSYVFM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087   86 NNTTFEQLAADEKAVGDNAKWLLDQAECIVTLWNGQPISVTPPNFVELEVIETDPGLKGDTAGTGGKPATLSTGAVVKVP 165
Cdd:TIGR00038  83 DTETYEQIELPKDLLGDAAKFLKENMEVSVVFYNGEPIGVELPNFVELEVTETEPGVKGDTASGSTKPATLETGAVVQVP 162

                         170       180
                  ....*....|....*....|..
gi 493737087  166 LFVQIGEVIKVDTRSGEYVSRV 187
Cdd:TIGR00038 163 LFIEEGEKIKVDTRTGEYVERA 184
Elong-fact-P_C pfam09285
Elongation factor P, C-terminal; Members of this family of nucleic acid binding domains are ...
 131-186 5.21e-32

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: 109.78  E-value: 5.21e-32
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 493737087  131 VELEVIETDPGLKGDTAGTGGKPATLSTGAVVKVPLFVQIGEVIKVDTRSGEYVSR 186
Cdd:pfam09285   1 VELEVTETEPGVKGDTASGATKPATLETGAEVQVPLFINEGDKIKVDTRTGEYVER 56
S1_EF-P_repeat_2 cd05794
S1_EF-P_repeat_2: Translation elongation factor P (EF-P), S1-like RNA-binding domain, repeat 1. ...
 131-186 6.62e-30

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: 104.14  E-value: 6.62e-30
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493737087 131 VELEVIETDPGLKGDTAGTGGKPATLSTGAVVKVPLFVQIGEVIKVDTRSGEYVSR 186
Cdd:cd05794    1 VELEVTETEPGVKGDTASSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 56
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 131-186 3.25e-29

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: 102.53  E-value: 3.25e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 493737087   131 VELEVIETDPGLKGDTAGTGGK-PATLSTGAVVKVPLFVQIGEVIKVDTRSGEYVSR 186
Cdd:smart00841   1 VELEVTETEPGVKGDTASGGTKkPATLETGAVVQVPLFINEGDKIKVDTRTGEYVSR 57
 
Name Accession Description Interval E-value
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 1-188 1.47e-112

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: 318.12  E-value: 1.47e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087   1 MATyySNDFRAGLKIMLDGEPYAVEASEFVKPGKGQAFARVKLRRLLTGTRVEKTFKSTDSAEGADVADMNLTFLYSDGE 80
Cdd:COG0231    1 MIS--ANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087  81 FWHFMNNTTFEQLAADEKAVGDNAKWLLDQAECIVTLWNGQPISVTPPNFVELEVIETDPGLKGDTAGTGGKPATLSTGA 160
Cdd:COG0231   79 GYVFMDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGA 158

                        170       180
                 ....*....|....*....|....*...
gi 493737087 161 VVKVPLFVQIGEVIKVDTRSGEYVSRVK 188
Cdd:COG0231  159 VVQVPLFIEEGDKIKVDTRTGEYVERAK 186
PRK00529 PRK00529
elongation factor P; Validated
 6-188 1.29e-111

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 315.84  E-value: 1.29e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087   6 SNDFRAGLKIMLDGEPYAVEASEFVKPGKGQAFARVKLRRLLTGTRVEKTFKSTDSAEGADVADMNLTFLYSDGEFWHFM 85
Cdd:PRK00529   4 ANDLRKGLVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGDGYVFM 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087  86 NNTTFEQLAADEKAVGDNAKWLLDQAECIVTLWNGQPISVTPPNFVELEVIETDPGLKGDTAGTGGKPATLSTGAVVKVP 165
Cdd:PRK00529  84 DTETYEQIEVPADQVGDAAKFLKEGMEVTVVFYNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLETGAVVQVP 163

                        170       180
                 ....*....|....*....|...
gi 493737087 166 LFVQIGEVIKVDTRSGEYVSRVK 188
Cdd:PRK00529 164 LFINEGEKIKVDTRTGEYVERAK 186
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 6-187 4.31e-107

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: 304.38  E-value: 4.31e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087    6 SNDFRAGLKIMLDGEPYAVEASEFVKPGKGQAFARVKLRRLLTGTRVEKTFKSTDSAEGADVADMNLTFLYSDGEFWHFM 85
Cdd:TIGR00038   3 ANDLRKGLKIELDGEPYVVLEFEHVKPGKGQAFVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSYVFM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087   86 NNTTFEQLAADEKAVGDNAKWLLDQAECIVTLWNGQPISVTPPNFVELEVIETDPGLKGDTAGTGGKPATLSTGAVVKVP 165
Cdd:TIGR00038  83 DTETYEQIELPKDLLGDAAKFLKENMEVSVVFYNGEPIGVELPNFVELEVTETEPGVKGDTASGSTKPATLETGAVVQVP 162

                         170       180
                  ....*....|....*....|..
gi 493737087  166 LFVQIGEVIKVDTRSGEYVSRV 187
Cdd:TIGR00038 163 LFIEEGEKIKVDTRTGEYVERA 184
PRK14578 PRK14578
elongation factor P; Provisional
 4-186 2.10e-39

elongation factor P; Provisional


Pssm-ID: 173042 [Multi-domain]  Cd Length: 187  Bit Score: 132.65  E-value: 2.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087   4 YYSNDFRAGLKIMLDGEPYAVEASEFVKPGK--GQAFARVKLRRLLTGTRVEKTFKSTDSAEGADVADMNLTFLYSDGEF 81
Cdd:PRK14578   2 YTTSDFKKGLVIQLDGAPCLLLDVTFQSPSArgANTMVKTKYRNLLTGQVLEKTFRSGDKVEEADFERHKGQFLYADGDR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087  82 WHFMNNTTFEQLAADEKAVGDNAKWLLDQAECIVTLWNGQPISVTPPNFVELEVIETDPGLKGDTAGTGGKPATLSTGAV 161
Cdd:PRK14578  82 GVFMDLETYEQFEMEEDAFSAIAPFLLDGTEVQLGLFQGRMVNVDLPMTVELTVTDTAPVMKNATATAQTKEAVLETGLR 161

                        170       180
                 ....*....|....*....|....*
gi 493737087 162 VKVPLFVQIGEVIKVDTRSGEYVSR 186
Cdd:PRK14578 162 LQVPPYLESGEKIKVDTRDGRFISR 186
PRK04542 PRK04542
elongation factor P; Provisional
 7-186 9.05e-39

elongation factor P; Provisional


Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 131.24  E-value: 9.05e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087   7 NDFRAGLKIMLDGEPYAVEASEFVKPGK--GQAFARVKLRRLLTGTRVEKTFKSTDSAEGADVADMNLTFLYSDGEFWHF 84
Cdd:PRK04542   5 NEIKKGMVVEYNGKLLLVKDIDRQSPSGrgGATLYKMRFYDVRTGLKVEERFKGDDILDTVDLTRRPVTFSYIDGDEYVF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087  85 MNNTTFEQLAADEKAVGDNAKWLLDQAECI-VTLWNGQPISVTPPNFVELEVIETDPGLKGDTAGTGGKPATLSTGAVVK 163
Cdd:PRK04542  85 MDNEDYTPYTFKKDQIEDELLFIPEGMPGMqVLTVDGQPVALELPQTVDLEIVETAPSIKGASASARTKPATLSTGLVIQ 164

                        170       180
                 ....*....|....*....|...
gi 493737087 164 VPLFVQIGEVIKVDTRSGEYVSR 186
Cdd:PRK04542 165 VPEYISTGEKIRINTEERKFMGR 187
Elong-fact-P_C pfam09285
Elongation factor P, C-terminal; Members of this family of nucleic acid binding domains are ...
 131-186 5.21e-32

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: 109.78  E-value: 5.21e-32
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 493737087  131 VELEVIETDPGLKGDTAGTGGKPATLSTGAVVKVPLFVQIGEVIKVDTRSGEYVSR 186
Cdd:pfam09285   1 VELEVTETEPGVKGDTASGATKPATLETGAEVQVPLFINEGDKIKVDTRTGEYVER 56
PRK12426 PRK12426
elongation factor P; Provisional
 6-187 1.79e-30

elongation factor P; Provisional


Pssm-ID: 183522 [Multi-domain]  Cd Length: 185  Bit Score: 109.93  E-value: 1.79e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087   6 SNDFRAGLKIMLDGEPYAVEASEFVKPGKGQAFARVKLRRLLTGTRVEKTFKSTDSAEGADVADMNLTFLYSDGEFWHFM 85
Cdd:PRK12426   4 SSQLSVGMFISTKDGLYKVVSVSKVTGPKGETFIKVSLQAADSDVVVERNFKAGQEVKEAQFEPRNLEYLYLEGDEYLFL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087  86 NNTTFEQLAADEKAVGDNAKWLLDQAECIVTLWNGQPISVTPPNFVELEVIETD-PGLKGDTAGtGGKPATLSTGAVVKV 164
Cdd:PRK12426  84 DLGNYDKIYIPKEIMKDNFLFLKAGVTVSALVYDGTVFSVELPHFLELMVSKTDfPGDSLSLSG-GAKKALLETGVEVLV 162

                        170       180
                 ....*....|....*....|...
gi 493737087 165 PLFVQIGEVIKVDTRSGEYVSRV 187
Cdd:PRK12426 163 PPFVEIGDVIKVDTRTCEYIQRV 185
S1_EF-P_repeat_2 cd05794
S1_EF-P_repeat_2: Translation elongation factor P (EF-P), S1-like RNA-binding domain, repeat 1. ...
 131-186 6.62e-30

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: 104.14  E-value: 6.62e-30
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493737087 131 VELEVIETDPGLKGDTAGTGGKPATLSTGAVVKVPLFVQIGEVIKVDTRSGEYVSR 186
Cdd:cd05794    1 VELEVTETEPGVKGDTASSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 56
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 131-186 3.25e-29

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: 102.53  E-value: 3.25e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 493737087   131 VELEVIETDPGLKGDTAGTGGK-PATLSTGAVVKVPLFVQIGEVIKVDTRSGEYVSR 186
Cdd:smart00841   1 VELEVTETEPGVKGDTASGGTKkPATLETGAVVQVPLFINEGDKIKVDTRTGEYVSR 57
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 5.25e-28

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: 99.45  E-value: 5.25e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493737087  69 DMNLTFLYSDGEFWHFMNNTTFEQLAADEKAVGDNAKWLLDQAECIVTLWNGQPISVTPP 128
Cdd:cd04470    2 EREMQYLYKDGDNYVFMDTETYEQIELPKEALGDAAKFLKEGMEVIVLFYNGEPIGVELP 61
EFP pfam01132
Elongation factor P (EF-P) OB domain;
71-123 2.80e-23

Elongation factor P (EF-P) OB domain;


Pssm-ID: 460077 [Multi-domain]  Cd Length: 54  Bit Score: 87.07  E-value: 2.80e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 493737087   71 NLTFLYSDGEFWHFMNNTTFEQLAADEKAVGDNAKWLLDQAECIVTLWNGQPI 123
Cdd:pfam01132   2 EMQYLYNDGDDYVFMDNETYEQIELPKEQLGDAAKFLKEGMEVTVLFYEGKPI 54
EFP_N pfam08207
Elongation factor P (EF-P) KOW-like domain;
6-61 4.76e-23

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


Pssm-ID: 429864 [Multi-domain]  Cd Length: 58  Bit Score: 86.72  E-value: 4.76e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 493737087    6 SNDFRAGLKIMLDGEPYAVEASEFVKPGKGQAFARVKLRRLLTGTRVEKTFKSTDS 61
Cdd:pfam08207   2 ANELRKGNVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLRTGAKVEKTFKAGDK 57
 
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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