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Conserved domains on  [gi|2720541826|ref|WP_341907573|]
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elongation factor P [Fluviicola taffensis]

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, ...
 1-187 8.44e-100

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: 285.76  E-value: 8.44e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720541826   1 MATTADIRNGLCIKFNDKISQIIEFQHVKPGKGPAFVRTKMRIIETGKVIDNTFSAGHKIEIVRVENREYQYLYQEDQDY 80
Cdd:COG0231     1 MISANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720541826  81 IFMNNETFEQVTIPAKMI-ERPAFLLEGMVCNILYdaNDEVPLVVELPMYLVSEVTYTEPGIKGDTATNSMKAATIATGA 159
Cdd:COG0231    81 VFMDTETYEQIELPKEVVgDAAKFLKEGMEVTVLF--YNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGA 158

                         170       180
                  ....*....|....*....|....*...
gi 2720541826 160 EVKVPLFIDMGEIIKVDTRTGVYVERVK 187
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, ...
 1-187 8.44e-100

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: 285.76  E-value: 8.44e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720541826   1 MATTADIRNGLCIKFNDKISQIIEFQHVKPGKGPAFVRTKMRIIETGKVIDNTFSAGHKIEIVRVENREYQYLYQEDQDY 80
Cdd:COG0231     1 MISANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720541826  81 IFMNNETFEQVTIPAKMI-ERPAFLLEGMVCNILYdaNDEVPLVVELPMYLVSEVTYTEPGIKGDTATNSMKAATIATGA 159
Cdd:COG0231    81 VFMDTETYEQIELPKEVVgDAAKFLKEGMEVTVLF--YNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGA 158

                         170       180
                  ....*....|....*....|....*...
gi 2720541826 160 EVKVPLFIDMGEIIKVDTRTGVYVERVK 187
Cdd:COG0231   159 VVQVPLFIEEGDKIKVDTRTGEYVERAK 186
PRK00529 PRK00529
elongation factor P; Validated
 1-187 1.09e-93

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 270.39  E-value: 1.09e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720541826   1 MATTADIRNGLCIKFNDKISQIIEFQHVKPGKGPAFVRTKMRIIETGKVIDNTFSAGHKIEIVRVENREYQYLYQEDQDY 80
Cdd:PRK00529    1 MISANDLRKGLVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGDGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720541826  81 IFMNNETFEQVTIPAKMIE-RPAFLLEGMVCNILYdaNDEVPLVVELPMYLVSEVTYTEPGIKGDTATNSMKAATIATGA 159
Cdd:PRK00529   81 VFMDTETYEQIEVPADQVGdAAKFLKEGMEVTVVF--YNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLETGA 158

                         170       180
                  ....*....|....*....|....*...
gi 2720541826 160 EVKVPLFIDMGEIIKVDTRTGVYVERVK 187
Cdd:PRK00529  159 VVQVPLFINEGEKIKVDTRTGEYVERAK 186
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 2-186 5.58e-87

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: 253.54  E-value: 5.58e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720541826   2 ATTADIRNGLCIKFNDKISQIIEFQHVKPGKGPAFVRTKMRIIETGKVIDNTFSAGHKIEIVRVENREYQYLYQEDQDYI 81
Cdd:TIGR00038   1 ISANDLRKGLKIELDGEPYVVLEFEHVKPGKGQAFVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720541826  82 FMNNETFEQVTIPAKMIERPA-FLLEGMVCNILYDanDEVPLVVELPMYLVSEVTYTEPGIKGDTATNSMKAATIATGAE 160
Cdd:TIGR00038  81 FMDTETYEQIELPKDLLGDAAkFLKENMEVSVVFY--NGEPIGVELPNFVELEVTETEPGVKGDTASGSTKPATLETGAV 158

                         170       180
                  ....*....|....*....|....*.
gi 2720541826 161 VKVPLFIDMGEIIKVDTRTGVYVERV 186
Cdd:TIGR00038 159 VQVPLFIEEGEKIKVDTRTGEYVERA 184
Elong-fact-P_C pfam09285
Elongation factor P, C-terminal; Members of this family of nucleic acid binding domains are ...
 133-185 6.54e-28

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: 98.99  E-value: 6.54e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2720541826 133 EVTYTEPGIKGDTATNSMKAATIATGAEVKVPLFIDMGEIIKVDTRTGVYVER 185
Cdd:pfam09285   4 EVTETEPGVKGDTASGATKPATLETGAEVQVPLFINEGDKIKVDTRTGEYVER 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. ...
 133-185 2.85e-24

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: 89.89  E-value: 2.85e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2720541826 133 EVTYTEPGIKGDTATNSMKAATIATGAEVKVPLFIDMGEIIKVDTRTGVYVER 185
Cdd:cd05794     4 EVTETEPGVKGDTASSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 56
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 133-185 2.87e-23

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: 87.13  E-value: 2.87e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2720541826  133 EVTYTEPGIKGDTATNSMK-AATIATGAEVKVPLFIDMGEIIKVDTRTGVYVER 185
Cdd:smart00841   4 EVTETEPGVKGDTASGGTKkPATLETGAVVQVPLFINEGDKIKVDTRTGEYVSR 57
 
Name Accession Description Interval E-value
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 1-187 8.44e-100

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: 285.76  E-value: 8.44e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720541826   1 MATTADIRNGLCIKFNDKISQIIEFQHVKPGKGPAFVRTKMRIIETGKVIDNTFSAGHKIEIVRVENREYQYLYQEDQDY 80
Cdd:COG0231     1 MISANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720541826  81 IFMNNETFEQVTIPAKMI-ERPAFLLEGMVCNILYdaNDEVPLVVELPMYLVSEVTYTEPGIKGDTATNSMKAATIATGA 159
Cdd:COG0231    81 VFMDTETYEQIELPKEVVgDAAKFLKEGMEVTVLF--YNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGA 158

                         170       180
                  ....*....|....*....|....*...
gi 2720541826 160 EVKVPLFIDMGEIIKVDTRTGVYVERVK 187
Cdd:COG0231   159 VVQVPLFIEEGDKIKVDTRTGEYVERAK 186
PRK00529 PRK00529
elongation factor P; Validated
 1-187 1.09e-93

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 270.39  E-value: 1.09e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720541826   1 MATTADIRNGLCIKFNDKISQIIEFQHVKPGKGPAFVRTKMRIIETGKVIDNTFSAGHKIEIVRVENREYQYLYQEDQDY 80
Cdd:PRK00529    1 MISANDLRKGLVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGDGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720541826  81 IFMNNETFEQVTIPAKMIE-RPAFLLEGMVCNILYdaNDEVPLVVELPMYLVSEVTYTEPGIKGDTATNSMKAATIATGA 159
Cdd:PRK00529   81 VFMDTETYEQIEVPADQVGdAAKFLKEGMEVTVVF--YNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLETGA 158

                         170       180
                  ....*....|....*....|....*...
gi 2720541826 160 EVKVPLFIDMGEIIKVDTRTGVYVERVK 187
Cdd:PRK00529  159 VVQVPLFINEGEKIKVDTRTGEYVERAK 186
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 2-186 5.58e-87

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: 253.54  E-value: 5.58e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720541826   2 ATTADIRNGLCIKFNDKISQIIEFQHVKPGKGPAFVRTKMRIIETGKVIDNTFSAGHKIEIVRVENREYQYLYQEDQDYI 81
Cdd:TIGR00038   1 ISANDLRKGLKIELDGEPYVVLEFEHVKPGKGQAFVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720541826  82 FMNNETFEQVTIPAKMIERPA-FLLEGMVCNILYDanDEVPLVVELPMYLVSEVTYTEPGIKGDTATNSMKAATIATGAE 160
Cdd:TIGR00038  81 FMDTETYEQIELPKDLLGDAAkFLKENMEVSVVFY--NGEPIGVELPNFVELEVTETEPGVKGDTASGSTKPATLETGAV 158

                         170       180
                  ....*....|....*....|....*.
gi 2720541826 161 VKVPLFIDMGEIIKVDTRTGVYVERV 186
Cdd:TIGR00038 159 VQVPLFIEEGEKIKVDTRTGEYVERA 184
PRK12426 PRK12426
elongation factor P; Provisional
 1-186 7.70e-32

elongation factor P; Provisional


Pssm-ID: 183522 [Multi-domain]  Cd Length: 185  Bit Score: 113.40  E-value: 7.70e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720541826   1 MATTADIRNGLCIKFNDKISQIIEFQHVKPGKGPAFVRTKMRIIETGKVIDNTFSAGHKIEIVRVENREYQYLYQEDQDY 80
Cdd:PRK12426    1 MVLSSQLSVGMFISTKDGLYKVVSVSKVTGPKGETFIKVSLQAADSDVVVERNFKAGQEVKEAQFEPRNLEYLYLEGDEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720541826  81 IFMNNETFEQVTIPAK-MIERPAFLLEGMVCNILYdaNDEVPLVVELPMYLVSEVTYTEPGIKGDTATNSMKAATIATGA 159
Cdd:PRK12426   81 LFLDLGNYDKIYIPKEiMKDNFLFLKAGVTVSALV--YDGTVFSVELPHFLELMVSKTDFPGDSLSLSGGAKKALLETGV 158

                         170       180
                  ....*....|....*....|....*..
gi 2720541826 160 EVKVPLFIDMGEIIKVDTRTGVYVERV 186
Cdd:PRK12426  159 EVLVPPFVEIGDVIKVDTRTCEYIQRV 185
PRK14578 PRK14578
elongation factor P; Provisional
 1-185 3.42e-31

elongation factor P; Provisional


Pssm-ID: 173042 [Multi-domain]  Cd Length: 187  Bit Score: 111.85  E-value: 3.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720541826   1 MATTADIRNGLCIKFNDKISQIIE--FQHVKPGKGPAFVRTKMRIIETGKVIDNTFSAGHKIEIVRVENREYQYLYQEDQ 78
Cdd:PRK14578    1 MYTTSDFKKGLVIQLDGAPCLLLDvtFQSPSARGANTMVKTKYRNLLTGQVLEKTFRSGDKVEEADFERHKGQFLYADGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720541826  79 DYIFMNNETFEQVTIPAKMIERPA-FLLEGMVCNI-LYDA---NDEVPLVVELpmylvsEVTYTEPGIKGDTATNSMKAA 153
Cdd:PRK14578   81 RGVFMDLETYEQFEMEEDAFSAIApFLLDGTEVQLgLFQGrmvNVDLPMTVEL------TVTDTAPVMKNATATAQTKEA 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2720541826 154 TIATGAEVKVPLFIDMGEIIKVDTRTGVYVER 185
Cdd:PRK14578  155 VLETGLRLQVPPYLESGEKIKVDTRDGRFISR 186
PRK04542 PRK04542
elongation factor P; Provisional
 1-185 4.70e-30

elongation factor P; Provisional


Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 108.90  E-value: 4.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720541826   1 MATTADIRNGLCIKFNDKISQIIEFQHVKPGKGPAFVRTKMRI--IETGKVIDNTFSAGHKIEIVRVENREYQYLYQEDQ 78
Cdd:PRK04542    1 MPKANEIKKGMVVEYNGKLLLVKDIDRQSPSGRGGATLYKMRFydVRTGLKVEERFKGDDILDTVDLTRRPVTFSYIDGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720541826  79 DYIFMNNETFEQVTIPAKMIERPA-FL---LEGMVCNILydanDEVPLVVELPMYLVSEVTYTEPGIKGDTATNSMKAAT 154
Cdd:PRK04542   81 EYVFMDNEDYTPYTFKKDQIEDELlFIpegMPGMQVLTV----DGQPVALELPQTVDLEIVETAPSIKGASASARTKPAT 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2720541826 155 IATGAEVKVPLFIDMGEIIKVDTRTGVYVER 185
Cdd:PRK04542  157 LSTGLVIQVPEYISTGEKIRINTEERKFMGR 187
Elong-fact-P_C pfam09285
Elongation factor P, C-terminal; Members of this family of nucleic acid binding domains are ...
 133-185 6.54e-28

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: 98.99  E-value: 6.54e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2720541826 133 EVTYTEPGIKGDTATNSMKAATIATGAEVKVPLFIDMGEIIKVDTRTGVYVER 185
Cdd:pfam09285   4 EVTETEPGVKGDTASGATKPATLETGAEVQVPLFINEGDKIKVDTRTGEYVER 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. ...
 133-185 2.85e-24

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: 89.89  E-value: 2.85e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2720541826 133 EVTYTEPGIKGDTATNSMKAATIATGAEVKVPLFIDMGEIIKVDTRTGVYVER 185
Cdd:cd05794     4 EVTETEPGVKGDTASSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 56
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 133-185 2.87e-23

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: 87.13  E-value: 2.87e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2720541826  133 EVTYTEPGIKGDTATNSMK-AATIATGAEVKVPLFIDMGEIIKVDTRTGVYVER 185
Cdd:smart00841   4 EVTETEPGVKGDTASGGTKkPATLETGAVVQVPLFINEGDKIKVDTRTGEYVSR 57
EFP_N pfam08207
Elongation factor P (EF-P) KOW-like domain;
3-60 1.51e-19

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


Pssm-ID: 429864 [Multi-domain]  Cd Length: 58  Bit Score: 77.86  E-value: 1.51e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2720541826   3 TTADIRNGLCIKFNDKISQIIEFQHVKPGKGPAFVRTKMRIIETGKVIDNTFSAGHKI 60
Cdd:pfam08207   1 SANELRKGNVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLRTGAKVEKTFKAGDKV 58
S1_EF-P_repeat_1 cd04470
S1_EF-P_repeat_1: Translation elongation factor P (EF-P), S1-like RNA-binding domain, repeat 1. ...
 66-127 1.25e-17

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: 72.88  E-value: 1.25e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2720541826  66 ENREYQYLYQEDQDYIFMNNETFEQVTIPAKMIERPA-FLLEGMVCNILYDanDEVPLVVELP 127
Cdd:cd04470     1 EEREMQYLYKDGDNYVFMDTETYEQIELPKEALGDAAkFLKEGMEVIVLFY--NGEPIGVELP 61
EFP pfam01132
Elongation factor P (EF-P) OB domain;
68-114 1.19e-15

Elongation factor P (EF-P) OB domain;


Pssm-ID: 460077 [Multi-domain]  Cd Length: 54  Bit Score: 67.43  E-value: 1.19e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2720541826  68 REYQYLYQEDQDYIFMNNETFEQVTIPAKMI-ERPAFLLEGMVCNILY 114
Cdd:pfam01132   1 REMQYLYNDGDDYVFMDNETYEQIELPKEQLgDAAKFLKEGMEVTVLF 48
 
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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