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Conserved domains on  [gi|90111399|ref|NP_416676|]
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elongation factor P-like protein YeiP [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

elongation factor P-like protein YeiP( domain architecture ID 11480291)

elongation factor P-like protein YeiP may act as a translation factor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK04542 PRK04542
elongation factor P; Provisional
 1-190 9.61e-133

elongation factor P; Provisional


:

Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 369.29  E-value: 9.61e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399    1 MPRANEIKKGMVLNYNGKLLLVKDIDIQSPTARGAATLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYVDGN 80
Cdd:PRK04542   1 MPKANEIKKGMVVEYNGKLLLVKDIDRQSPSGRGGATLYKMRFYDVRTGLKVEERFKGDDILDTVDLTRRPVTFSYIDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399   81 EYVFMDKEDYTPYTFTKDQIEEELLFMPEgGMPDMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASARNKPATLST 160
Cdd:PRK04542  81 EYVFMDNEDYTPYTFKKDQIEDELLFIPE-GMPGMQVLTVDGQPVALELPQTVDLEIVETAPSIKGASASARTKPATLST 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 90111399  161 GLVIQVPEYLSPGEKIRIHIEERRYMGRAD 190
Cdd:PRK04542 160 GLVIQVPEYISTGEKIRINTEERKFMGRAD 189
 
Name Accession Description Interval E-value
PRK04542 PRK04542
elongation factor P; Provisional
 1-190 9.61e-133

elongation factor P; Provisional


Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 369.29  E-value: 9.61e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399    1 MPRANEIKKGMVLNYNGKLLLVKDIDIQSPTARGAATLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYVDGN 80
Cdd:PRK04542   1 MPKANEIKKGMVVEYNGKLLLVKDIDRQSPSGRGGATLYKMRFYDVRTGLKVEERFKGDDILDTVDLTRRPVTFSYIDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399   81 EYVFMDKEDYTPYTFTKDQIEEELLFMPEgGMPDMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASARNKPATLST 160
Cdd:PRK04542  81 EYVFMDNEDYTPYTFKKDQIEDELLFIPE-GMPGMQVLTVDGQPVALELPQTVDLEIVETAPSIKGASASARTKPATLST 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 90111399  161 GLVIQVPEYLSPGEKIRIHIEERRYMGRAD 190
Cdd:PRK04542 160 GLVIQVPEYISTGEKIRINTEERKFMGRAD 189
yeiP TIGR02178
elongation factor P-like protein YeiP; This model represents the family of Escherichia coli ...
 3-189 8.40e-118

elongation factor P-like protein YeiP; This model represents the family of Escherichia coli protein YeiP, a close homolog of elongation factor P (TIGR00038) and probably itself a translation factor. Member of this family are found only in some Gammaproteobacteria, including E. coli and Vibrio cholerae. [Protein synthesis, Translation factors]


Pssm-ID: 131233  Cd Length: 186  Bit Score: 331.46  E-value: 8.40e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399     3 RANEIKKGMVLNYNGKLLLVKDIDIQSPTARGAATLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYVDGNEY 82
Cdd:TIGR02178   1 KASEMKKGSIVEYNGKTLLIKDIQRSSPQGRGGNVRYKFRMYDVPTGSKVEERFKADDMLDTVELLRREASFSYKDGEEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399    83 VFMDKEDYTPYTFTKDQIEEELLFMPEgGMPDMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASARNKPATLSTGL 162
Cdd:TIGR02178  81 VFMDEEDYTPYTFDKDAIEDELLFISE-GLSGMYVQLIDGSPVALELPQHVVLEIVETPPEIKGASASKRPKPAKLITGL 159

                         170       180
                  ....*....|....*....|....*..
gi 90111399   163 VIQVPEYLSPGEKIRIHIEERRYMGRA 189
Cdd:TIGR02178 160 VVQVPEYITTGERILINTTERAFMGRA 186
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 1-190 7.39e-81

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: 238.00  E-value: 7.39e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399   1 MPRANEIKKGMVLNYNGKLLLVKDIDIQSPtARGAAtLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYVDGN 80
Cdd:COG0231   1 MISANDLRKGLVIEIDGEPYVVVEFQHVKP-GKGGA-FVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399  81 EYVFMDKEDYTPYTFTKDQIEEELLFMPEGGMpdMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASARNKPATLST 160
Cdd:COG0231  79 GYVFMDTETYEQIELPKEVVGDAAKFLKEGME--VTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLET 156

                       170       180       190
                ....*....|....*....|....*....|
gi 90111399 161 GLVIQVPEYLSPGEKIRIHIEERRYMGRAD 190
Cdd:COG0231 157 GAVVQVPLFIEEGDKIKVDTRTGEYVERAK 186
Elong-fact-P_C pfam09285
Elongation factor P, C-terminal; Members of this family of nucleic acid binding domains are ...
 133-188 4.26e-23

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: 87.05  E-value: 4.26e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 90111399   133 VDLEIVETAPGIKGASASARNKPATLSTGLVIQVPEYLSPGEKIRIHIEERRYMGR 188
Cdd:pfam09285   1 VELEVTETEPGVKGDTASGATKPATLETGAEVQVPLFINEGDKIKVDTRTGEYVER 56
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 133-188 2.39e-21

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: 82.50  E-value: 2.39e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 90111399    133 VDLEIVETAPGIKGASASARNK-PATLSTGLVIQVPEYLSPGEKIRIHIEERRYMGR 188
Cdd:smart00841   1 VELEVTETEPGVKGDTASGGTKkPATLETGAVVQVPLFINEGDKIKVDTRTGEYVSR 57
S1_EF-P_repeat_2 cd05794
S1_EF-P_repeat_2: Translation elongation factor P (EF-P), S1-like RNA-binding domain, repeat 1. ...
 133-188 5.32e-20

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: 79.10  E-value: 5.32e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 90111399 133 VDLEIVETAPGIKGASASARNKPATLSTGLVIQVPEYLSPGEKIRIHIEERRYMGR 188
Cdd:cd05794   1 VELEVTETEPGVKGDTASSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 56
 
Name Accession Description Interval E-value
PRK04542 PRK04542
elongation factor P; Provisional
 1-190 9.61e-133

elongation factor P; Provisional


Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 369.29  E-value: 9.61e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399    1 MPRANEIKKGMVLNYNGKLLLVKDIDIQSPTARGAATLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYVDGN 80
Cdd:PRK04542   1 MPKANEIKKGMVVEYNGKLLLVKDIDRQSPSGRGGATLYKMRFYDVRTGLKVEERFKGDDILDTVDLTRRPVTFSYIDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399   81 EYVFMDKEDYTPYTFTKDQIEEELLFMPEgGMPDMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASARNKPATLST 160
Cdd:PRK04542  81 EYVFMDNEDYTPYTFKKDQIEDELLFIPE-GMPGMQVLTVDGQPVALELPQTVDLEIVETAPSIKGASASARTKPATLST 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 90111399  161 GLVIQVPEYLSPGEKIRIHIEERRYMGRAD 190
Cdd:PRK04542 160 GLVIQVPEYISTGEKIRINTEERKFMGRAD 189
yeiP TIGR02178
elongation factor P-like protein YeiP; This model represents the family of Escherichia coli ...
 3-189 8.40e-118

elongation factor P-like protein YeiP; This model represents the family of Escherichia coli protein YeiP, a close homolog of elongation factor P (TIGR00038) and probably itself a translation factor. Member of this family are found only in some Gammaproteobacteria, including E. coli and Vibrio cholerae. [Protein synthesis, Translation factors]


Pssm-ID: 131233  Cd Length: 186  Bit Score: 331.46  E-value: 8.40e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399     3 RANEIKKGMVLNYNGKLLLVKDIDIQSPTARGAATLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYVDGNEY 82
Cdd:TIGR02178   1 KASEMKKGSIVEYNGKTLLIKDIQRSSPQGRGGNVRYKFRMYDVPTGSKVEERFKADDMLDTVELLRREASFSYKDGEEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399    83 VFMDKEDYTPYTFTKDQIEEELLFMPEgGMPDMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASARNKPATLSTGL 162
Cdd:TIGR02178  81 VFMDEEDYTPYTFDKDAIEDELLFISE-GLSGMYVQLIDGSPVALELPQHVVLEIVETPPEIKGASASKRPKPAKLITGL 159

                         170       180
                  ....*....|....*....|....*..
gi 90111399   163 VIQVPEYLSPGEKIRIHIEERRYMGRA 189
Cdd:TIGR02178 160 VVQVPEYITTGERILINTTERAFMGRA 186
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 1-190 7.39e-81

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: 238.00  E-value: 7.39e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399   1 MPRANEIKKGMVLNYNGKLLLVKDIDIQSPtARGAAtLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYVDGN 80
Cdd:COG0231   1 MISANDLRKGLVIEIDGEPYVVVEFQHVKP-GKGGA-FVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399  81 EYVFMDKEDYTPYTFTKDQIEEELLFMPEGGMpdMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASARNKPATLST 160
Cdd:COG0231  79 GYVFMDTETYEQIELPKEVVGDAAKFLKEGME--VTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLET 156

                       170       180       190
                ....*....|....*....|....*....|
gi 90111399 161 GLVIQVPEYLSPGEKIRIHIEERRYMGRAD 190
Cdd:COG0231 157 GAVVQVPLFIEEGDKIKVDTRTGEYVERAK 186
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 3-189 3.13e-61

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: 188.05  E-value: 3.13e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399     3 RANEIKKGMVLNYNGKLLLVKDIDIQSPtARGAAtLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYVDGNEY 82
Cdd:TIGR00038   2 SANDLRKGLKIELDGEPYVVLEFEHVKP-GKGQA-FVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399    83 VFMDKEDYTPYTFTKDQIEEELLFMPEGGMpdMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASARNKPATLSTGL 162
Cdd:TIGR00038  80 VFMDTETYEQIELPKDLLGDAAKFLKENME--VSVVFYNGEPIGVELPNFVELEVTETEPGVKGDTASGSTKPATLETGA 157

                         170       180
                  ....*....|....*....|....*..
gi 90111399   163 VIQVPEYLSPGEKIRIHIEERRYMGRA 189
Cdd:TIGR00038 158 VVQVPLFIEEGEKIKVDTRTGEYVERA 184
PRK00529 PRK00529
elongation factor P; Validated
 1-189 9.75e-61

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 187.18  E-value: 9.75e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399    1 MPRANEIKKGMVLNYNGKLLLVKDIDIQSPtARGAAtLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYVDGN 80
Cdd:PRK00529   1 MISANDLRKGLVIEIDGEPYVVLEFEHVKP-GKGQA-FVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399   81 EYVFMDKEDYTPYTFTKDQIEEELLFMPEGGMpdMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASARNKPATLST 160
Cdd:PRK00529  79 GYVFMDTETYEQIEVPADQVGDAAKFLKEGME--VTVVFYNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLET 156

                        170       180
                 ....*....|....*....|....*....
gi 90111399  161 GLVIQVPEYLSPGEKIRIHIEERRYMGRA 189
Cdd:PRK00529 157 GAVVQVPLFINEGEKIKVDTRTGEYVERA 185
PRK14578 PRK14578
elongation factor P; Provisional
 1-189 1.98e-43

elongation factor P; Provisional


Pssm-ID: 173042 [Multi-domain]  Cd Length: 187  Bit Score: 143.05  E-value: 1.98e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399    1 MPRANEIKKGMVLNYNGKLLLVKDIDIQSPTARGAATLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYVDGN 80
Cdd:PRK14578   1 MYTTSDFKKGLVIQLDGAPCLLLDVTFQSPSARGANTMVKTKYRNLLTGQVLEKTFRSGDKVEEADFERHKGQFLYADGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399   81 EYVFMDKEDYTPYTFTKDQIEEELLFMPEGgmPDMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASARNKPATLST 160
Cdd:PRK14578  81 RGVFMDLETYEQFEMEEDAFSAIAPFLLDG--TEVQLGLFQGRMVNVDLPMTVELTVTDTAPVMKNATATAQTKEAVLET 158

                        170       180
                 ....*....|....*....|....*....
gi 90111399  161 GLVIQVPEYLSPGEKIRIHIEERRYMGRA 189
Cdd:PRK14578 159 GLRLQVPPYLESGEKIKVDTRDGRFISRA 187
Elong-fact-P_C pfam09285
Elongation factor P, C-terminal; Members of this family of nucleic acid binding domains are ...
 133-188 4.26e-23

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: 87.05  E-value: 4.26e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 90111399   133 VDLEIVETAPGIKGASASARNKPATLSTGLVIQVPEYLSPGEKIRIHIEERRYMGR 188
Cdd:pfam09285   1 VELEVTETEPGVKGDTASGATKPATLETGAEVQVPLFINEGDKIKVDTRTGEYVER 56
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 133-188 2.39e-21

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: 82.50  E-value: 2.39e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 90111399    133 VDLEIVETAPGIKGASASARNK-PATLSTGLVIQVPEYLSPGEKIRIHIEERRYMGR 188
Cdd:smart00841   1 VELEVTETEPGVKGDTASGGTKkPATLETGAVVQVPLFINEGDKIKVDTRTGEYVSR 57
S1_EF-P_repeat_2 cd05794
S1_EF-P_repeat_2: Translation elongation factor P (EF-P), S1-like RNA-binding domain, repeat 1. ...
 133-188 5.32e-20

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: 79.10  E-value: 5.32e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 90111399 133 VDLEIVETAPGIKGASASARNKPATLSTGLVIQVPEYLSPGEKIRIHIEERRYMGR 188
Cdd:cd05794   1 VELEVTETEPGVKGDTASSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 56
S1_EF-P_repeat_1 cd04470
S1_EF-P_repeat_1: Translation elongation factor P (EF-P), S1-like RNA-binding domain, repeat 1. ...
 68-130 5.76e-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: 71.34  E-value: 5.76e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111399  68 TRRYVDFSYVDGNEYVFMDKEDYTPYTFTKDQIEEELLFMPEGGMpdMQVLTWDGQLLALELP 130
Cdd:cd04470   1 EEREMQYLYKDGDNYVFMDTETYEQIELPKEALGDAAKFLKEGME--VIVLFYNGEPIGVELP 61
EFP_N pfam08207
Elongation factor P (EF-P) KOW-like domain;
4-62 3.25e-16

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


Pssm-ID: 429864 [Multi-domain]  Cd Length: 58  Bit Score: 69.00  E-value: 3.25e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111399     4 ANEIKKGMVLNYNGKLLLVKDIDiQSPTARGAAtLYKMRFSDVRTGLKVEERFKGDDIV 62
Cdd:pfam08207   2 ANELRKGNVIEIDGEPYVVLEFE-HVKPGKGQA-FVRTKLKNLRTGAKVEKTFKAGDKV 58
PRK12426 PRK12426
elongation factor P; Provisional
 1-188 1.48e-15

elongation factor P; Provisional


Pssm-ID: 183522 [Multi-domain]  Cd Length: 185  Bit Score: 71.03  E-value: 1.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399    1 MPRANEIKKGMVLNYNGKLLLVkdIDIQSPTARGAATLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYVDGN 80
Cdd:PRK12426   1 MVLSSQLSVGMFISTKDGLYKV--VSVSKVTGPKGETFIKVSLQAADSDVVVERNFKAGQEVKEAQFEPRNLEYLYLEGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111399   81 EYVFMDKEDYTPYTFTKDQIEEELLFMPEGgmPDMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASARNKPATLST 160
Cdd:PRK12426  79 EYLFLDLGNYDKIYIPKEIMKDNFLFLKAG--VTVSALVYDGTVFSVELPHFLELMVSKTDFPGDSLSLSGGAKKALLET 156

                        170       180
                 ....*....|....*....|....*...
gi 90111399  161 GLVIQVPEYLSPGEKIRIHIEERRYMGR 188
Cdd:PRK12426 157 GVEVLVPPFVEIGDVIKVDTRTCEYIQR 184
EFP pfam01132
Elongation factor P (EF-P) OB domain;
74-125 2.68e-12

Elongation factor P (EF-P) OB domain;


Pssm-ID: 460077 [Multi-domain]  Cd Length: 54  Bit Score: 58.95  E-value: 2.68e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 90111399    74 FSYVDGNEYVFMDKEDYTPYTFTKDQIEEELLFMPEGGMpdMQVLTWDGQLL 125
Cdd:pfam01132   5 YLYNDGDDYVFMDNETYEQIELPKEQLGDAAKFLKEGME--VTVLFYEGKPI 54
 
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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