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Conserved domains on  [gi|489952666|ref|WP_003855973|]
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MULTISPECIES: elongation factor P [Corynebacterium]

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, ...
 1-186 6.83e-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: 306.18  E-value: 6.83e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489952666   1 MATTADFKNGLVLKNEGKLQQIIEFQHVKPGKGPAFVRTKLKDVVTGKTIDKTWNAGVKVETATVDRRDVTYLYNDGTSF 80
Cdd:COG0231    1 MISANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489952666  81 IVMDDKTFEQYELSPDAFGDAGRFLLENMRVQVSFHEGEALFGELPVSVDLRVEHTDPGLQGDRSTGGTKPATLETGAEI 160
Cdd:COG0231   81 VFMDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGAVV 160

                        170       180
                 ....*....|....*....|....*.
gi 489952666 161 QVPLFIETGNVLKVDTRDGSYLSRVN 186
Cdd:COG0231  161 QVPLFIEEGDKIKVDTRTGEYVERAK 186
 
Name Accession Description Interval E-value
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 1-186 6.83e-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: 306.18  E-value: 6.83e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489952666   1 MATTADFKNGLVLKNEGKLQQIIEFQHVKPGKGPAFVRTKLKDVVTGKTIDKTWNAGVKVETATVDRRDVTYLYNDGTSF 80
Cdd:COG0231    1 MISANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489952666  81 IVMDDKTFEQYELSPDAFGDAGRFLLENMRVQVSFHEGEALFGELPVSVDLRVEHTDPGLQGDRSTGGTKPATLETGAEI 160
Cdd:COG0231   81 VFMDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGAVV 160

                        170       180
                 ....*....|....*....|....*.
gi 489952666 161 QVPLFIETGNVLKVDTRDGSYLSRVN 186
Cdd:COG0231  161 QVPLFIEEGDKIKVDTRTGEYVERAK 186
PRK00529 PRK00529
elongation factor P; Validated
 1-186 1.81e-106

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 302.74  E-value: 1.81e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489952666   1 MATTADFKNGLVLKNEGKLQQIIEFQHVKPGKGPAFVRTKLKDVVTGKTIDKTWNAGVKVETATVDRRDVTYLYNDGTSF 80
Cdd:PRK00529   1 MISANDLRKGLVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGDGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489952666  81 IVMDDKTFEQYELSPDAFGDAGRFLLENMRVQVSFHEGEALFGELPVSVDLRVEHTDPGLQGDRSTGGTKPATLETGAEI 160
Cdd:PRK00529  81 VFMDTETYEQIEVPADQVGDAAKFLKEGMEVTVVFYNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLETGAVV 160

                        170       180
                 ....*....|....*....|....*.
gi 489952666 161 QVPLFIETGNVLKVDTRDGSYLSRVN 186
Cdd:PRK00529 161 QVPLFINEGEKIKVDTRTGEYVERAK 186
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 2-185 1.47e-100

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: 287.82  E-value: 1.47e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489952666    2 ATTADFKNGLVLKNEGKLQQIIEFQHVKPGKGPAFVRTKLKDVVTGKTIDKTWNAGVKVETATVDRRDVTYLYNDGTSFI 81
Cdd:TIGR00038   1 ISANDLRKGLKIELDGEPYVVLEFEHVKPGKGQAFVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489952666   82 VMDDKTFEQYELSPDAFGDAGRFLLENMRVQVSFHEGEALFGELPVSVDLRVEHTDPGLQGDRSTGGTKPATLETGAEIQ 161
Cdd:TIGR00038  81 FMDTETYEQIELPKDLLGDAAKFLKENMEVSVVFYNGEPIGVELPNFVELEVTETEPGVKGDTASGSTKPATLETGAVVQ 160

                         170       180
                  ....*....|....*....|....
gi 489952666  162 VPLFIETGNVLKVDTRDGSYLSRV 185
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 ...
 129-184 5.35e-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: 101.69  E-value: 5.35e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489952666  129 VDLRVEHTDPGLQGDRSTGGTKPATLETGAEIQVPLFIETGNVLKVDTRDGSYLSR 184
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. ...
 129-184 8.05e-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: 8.05e-26
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489952666 129 VDLRVEHTDPGLQGDRSTGGTKPATLETGAEIQVPLFIETGNVLKVDTRDGSYLSR 184
Cdd:cd05794    1 VELEVTETEPGVKGDTASSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 56
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 129-184 1.13e-25

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: 93.29  E-value: 1.13e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 489952666   129 VDLRVEHTDPGLQGDRSTGGTK-PATLETGAEIQVPLFIETGNVLKVDTRDGSYLSR 184
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, ...
 1-186 6.83e-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: 306.18  E-value: 6.83e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489952666   1 MATTADFKNGLVLKNEGKLQQIIEFQHVKPGKGPAFVRTKLKDVVTGKTIDKTWNAGVKVETATVDRRDVTYLYNDGTSF 80
Cdd:COG0231    1 MISANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489952666  81 IVMDDKTFEQYELSPDAFGDAGRFLLENMRVQVSFHEGEALFGELPVSVDLRVEHTDPGLQGDRSTGGTKPATLETGAEI 160
Cdd:COG0231   81 VFMDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGAVV 160

                        170       180
                 ....*....|....*....|....*.
gi 489952666 161 QVPLFIETGNVLKVDTRDGSYLSRVN 186
Cdd:COG0231  161 QVPLFIEEGDKIKVDTRTGEYVERAK 186
PRK00529 PRK00529
elongation factor P; Validated
 1-186 1.81e-106

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 302.74  E-value: 1.81e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489952666   1 MATTADFKNGLVLKNEGKLQQIIEFQHVKPGKGPAFVRTKLKDVVTGKTIDKTWNAGVKVETATVDRRDVTYLYNDGTSF 80
Cdd:PRK00529   1 MISANDLRKGLVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGDGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489952666  81 IVMDDKTFEQYELSPDAFGDAGRFLLENMRVQVSFHEGEALFGELPVSVDLRVEHTDPGLQGDRSTGGTKPATLETGAEI 160
Cdd:PRK00529  81 VFMDTETYEQIEVPADQVGDAAKFLKEGMEVTVVFYNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLETGAVV 160

                        170       180
                 ....*....|....*....|....*.
gi 489952666 161 QVPLFIETGNVLKVDTRDGSYLSRVN 186
Cdd:PRK00529 161 QVPLFINEGEKIKVDTRTGEYVERAK 186
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 2-185 1.47e-100

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: 287.82  E-value: 1.47e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489952666    2 ATTADFKNGLVLKNEGKLQQIIEFQHVKPGKGPAFVRTKLKDVVTGKTIDKTWNAGVKVETATVDRRDVTYLYNDGTSFI 81
Cdd:TIGR00038   1 ISANDLRKGLKIELDGEPYVVLEFEHVKPGKGQAFVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489952666   82 VMDDKTFEQYELSPDAFGDAGRFLLENMRVQVSFHEGEALFGELPVSVDLRVEHTDPGLQGDRSTGGTKPATLETGAEIQ 161
Cdd:TIGR00038  81 FMDTETYEQIELPKDLLGDAAKFLKENMEVSVVFYNGEPIGVELPNFVELEVTETEPGVKGDTASGSTKPATLETGAVVQ 160

                         170       180
                  ....*....|....*....|....
gi 489952666  162 VPLFIETGNVLKVDTRDGSYLSRV 185
Cdd:TIGR00038 161 VPLFIEEGEKIKVDTRTGEYVERA 184
PRK14578 PRK14578
elongation factor P; Provisional
 1-184 9.40e-44

elongation factor P; Provisional


Pssm-ID: 173042 [Multi-domain]  Cd Length: 187  Bit Score: 143.82  E-value: 9.40e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489952666   1 MATTADFKNGLVLKNEGKLQQIIE--FQHVKPGKGPAFVRTKLKDVVTGKTIDKTWNAGVKVETATVDRRDVTYLYNDGT 78
Cdd:PRK14578   1 MYTTSDFKKGLVIQLDGAPCLLLDvtFQSPSARGANTMVKTKYRNLLTGQVLEKTFRSGDKVEEADFERHKGQFLYADGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489952666  79 SFIVMDDKTFEQYELSPDAFGDAGRFLLENMRVQVSFHEGEALFGELPVSVDLRVEHTDPGLQGDRSTGGTKPATLETGA 158
Cdd:PRK14578  81 RGVFMDLETYEQFEMEEDAFSAIAPFLLDGTEVQLGLFQGRMVNVDLPMTVELTVTDTAPVMKNATATAQTKEAVLETGL 160

                        170       180
                 ....*....|....*....|....*.
gi 489952666 159 EIQVPLFIETGNVLKVDTRDGSYLSR 184
Cdd:PRK14578 161 RLQVPPYLESGEKIKVDTRDGRFISR 186
PRK04542 PRK04542
elongation factor P; Provisional
 1-184 1.09e-39

elongation factor P; Provisional


Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 133.55  E-value: 1.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489952666   1 MATTADFKNGLVLKNEGKLQQIIEFQHVKP-GKGPAFV-RTKLKDVVTGKTIDKTWNAGVKVETATVDRRDVTYLYNDGT 78
Cdd:PRK04542   1 MPKANEIKKGMVVEYNGKLLLVKDIDRQSPsGRGGATLyKMRFYDVRTGLKVEERFKGDDILDTVDLTRRPVTFSYIDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489952666  79 SFIVMDDKTFEQYELSPDAFGDAGRFLLENMR-VQVSFHEGEALFGELPVSVDLRVEHTDPGLQGDRSTGGTKPATLETG 157
Cdd:PRK04542  81 EYVFMDNEDYTPYTFKKDQIEDELLFIPEGMPgMQVLTVDGQPVALELPQTVDLEIVETAPSIKGASASARTKPATLSTG 160

                        170       180
                 ....*....|....*....|....*..
gi 489952666 158 AEIQVPLFIETGNVLKVDTRDGSYLSR 184
Cdd:PRK04542 161 LVIQVPEYISTGEKIRINTEERKFMGR 187
PRK12426 PRK12426
elongation factor P; Provisional
 1-185 3.08e-32

elongation factor P; Provisional


Pssm-ID: 183522 [Multi-domain]  Cd Length: 185  Bit Score: 114.17  E-value: 3.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489952666   1 MATTADFKNGLVLKNEGKLQQIIEFQHVKPGKGPAFVRTKLKDVVTGKTIDKTWNAGVKVETATVDRRDVTYLYNDGTSF 80
Cdd:PRK12426   1 MVLSSQLSVGMFISTKDGLYKVVSVSKVTGPKGETFIKVSLQAADSDVVVERNFKAGQEVKEAQFEPRNLEYLYLEGDEY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489952666  81 IVMDDKTFEQYELSPDAFGDAGRFLLENMRVQVSFHEGEALFGELPVSVDLRVEHTDpgLQGDRS--TGGTKPATLETGA 158
Cdd:PRK12426  81 LFLDLGNYDKIYIPKEIMKDNFLFLKAGVTVSALVYDGTVFSVELPHFLELMVSKTD--FPGDSLslSGGAKKALLETGV 158

                        170       180
                 ....*....|....*....|....*..
gi 489952666 159 EIQVPLFIETGNVLKVDTRDGSYLSRV 185
Cdd:PRK12426 159 EVLVPPFVEIGDVIKVDTRTCEYIQRV 185
Elong-fact-P_C pfam09285
Elongation factor P, C-terminal; Members of this family of nucleic acid binding domains are ...
 129-184 5.35e-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: 101.69  E-value: 5.35e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489952666  129 VDLRVEHTDPGLQGDRSTGGTKPATLETGAEIQVPLFIETGNVLKVDTRDGSYLSR 184
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. ...
 129-184 8.05e-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: 8.05e-26
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489952666 129 VDLRVEHTDPGLQGDRSTGGTKPATLETGAEIQVPLFIETGNVLKVDTRDGSYLSR 184
Cdd:cd05794    1 VELEVTETEPGVKGDTASSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 56
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 129-184 1.13e-25

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: 93.29  E-value: 1.13e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 489952666   129 VDLRVEHTDPGLQGDRSTGGTK-PATLETGAEIQVPLFIETGNVLKVDTRDGSYLSR 184
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. ...
 66-126 6.70e-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: 91.37  E-value: 6.70e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489952666  66 DRRDVTYLYNDGTSFIVMDDKTFEQYELSPDAFGDAGRFLLENMRVQVSFHEGEALFGELP 126
Cdd:cd04470    1 EEREMQYLYKDGDNYVFMDTETYEQIELPKEALGDAAKFLKEGMEVIVLFYNGEPIGVELP 61
EFP pfam01132
Elongation factor P (EF-P) OB domain;
68-121 4.72e-23

Elongation factor P (EF-P) OB domain;


Pssm-ID: 460077 [Multi-domain]  Cd Length: 54  Bit Score: 86.69  E-value: 4.72e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489952666   68 RDVTYLYNDGTSFIVMDDKTFEQYELSPDAFGDAGRFLLENMRVQVSFHEGEAL 121
Cdd:pfam01132   1 REMQYLYNDGDDYVFMDNETYEQIELPKEQLGDAAKFLKEGMEVTVLFYEGKPI 54
EFP_N pfam08207
Elongation factor P (EF-P) KOW-like domain;
3-60 5.68e-23

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


Pssm-ID: 429864 [Multi-domain]  Cd Length: 58  Bit Score: 86.33  E-value: 5.68e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489952666    3 TTADFKNGLVLKNEGKLQQIIEFQHVKPGKGPAFVRTKLKDVVTGKTIDKTWNAGVKV 60
Cdd:pfam08207   1 SANELRKGNVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLRTGAKVEKTFKAGDKV 58
 
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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