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Conserved domains on  [gi|1278835489|gb|PJD23655|]
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elongation factor P-like protein YeiP [Enterobacter roggenkampii]

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 1.23e-129

elongation factor P; Provisional


:

Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 361.59  E-value: 1.23e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489   1 MPRANEIKKGMVLNYNGKLLIVKDIDIQAPSARGAATLYKMRFADVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYIDGN 80
Cdd:PRK04542    1 MPKANEIKKGMVVEYNGKLLLVKDIDRQSPSGRGGATLYKMRFYDVRTGLKVEERFKGDDILDTVDLTRRPVTFSYIDGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489  81 EYVFMDKEDYTPYIFTKDQIEEELLFIPEgGMPDMQVLTWDGVLLALELPQTVDLEIVETAPGIKGASASARNKPATLTT 160
Cdd:PRK04542   81 EYVFMDNEDYTPYTFKKDQIEDELLFIPE-GMPGMQVLTVDGQPVALELPQTVDLEIVETAPSIKGASASARTKPATLST 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 1278835489 161 GLVVQVPEYLSAGEKIRIHIEEKRYMGRAD 190
Cdd:PRK04542  160 GLVIQVPEYISTGEKIRINTEERKFMGRAD 189
 
Name Accession Description Interval E-value
PRK04542 PRK04542
elongation factor P; Provisional
 1-190 1.23e-129

elongation factor P; Provisional


Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 361.59  E-value: 1.23e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489   1 MPRANEIKKGMVLNYNGKLLIVKDIDIQAPSARGAATLYKMRFADVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYIDGN 80
Cdd:PRK04542    1 MPKANEIKKGMVVEYNGKLLLVKDIDRQSPSGRGGATLYKMRFYDVRTGLKVEERFKGDDILDTVDLTRRPVTFSYIDGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489  81 EYVFMDKEDYTPYIFTKDQIEEELLFIPEgGMPDMQVLTWDGVLLALELPQTVDLEIVETAPGIKGASASARNKPATLTT 160
Cdd:PRK04542   81 EYVFMDNEDYTPYTFKKDQIEDELLFIPE-GMPGMQVLTVDGQPVALELPQTVDLEIVETAPSIKGASASARTKPATLST 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 1278835489 161 GLVVQVPEYLSAGEKIRIHIEEKRYMGRAD 190
Cdd:PRK04542  160 GLVIQVPEYISTGEKIRINTEERKFMGRAD 189
yeiP TIGR02178
elongation factor P-like protein YeiP; This model represents the family of Escherichia coli ...
 3-189 2.91e-112

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: 317.59  E-value: 2.91e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489   3 RANEIKKGMVLNYNGKLLIVKDIDIQAPSARGAATLYKMRFADVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYIDGNEY 82
Cdd:TIGR02178   1 KASEMKKGSIVEYNGKTLLIKDIQRSSPQGRGGNVRYKFRMYDVPTGSKVEERFKADDMLDTVELLRREASFSYKDGEEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489  83 VFMDKEDYTPYIFTKDQIEEELLFIPEgGMPDMQVLTWDGVLLALELPQTVDLEIVETAPGIKGASASARNKPATLTTGL 162
Cdd:TIGR02178  81 VFMDEEDYTPYTFDKDAIEDELLFISE-GLSGMYVQLIDGSPVALELPQHVVLEIVETPPEIKGASASKRPKPAKLITGL 159

                         170       180
                  ....*....|....*....|....*..
gi 1278835489 163 VVQVPEYLSAGEKIRIHIEEKRYMGRA 189
Cdd:TIGR02178 160 VVQVPEYITTGERILINTTERAFMGRA 186
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 1-190 4.04e-78

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: 231.06  E-value: 4.04e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489   1 MPRANEIKKGMVLNYNGKLLIVKDIDIQAPSaRGAAtLYKMRFADVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYIDGN 80
Cdd:COG0231     1 MISANDLRKGLVIEIDGEPYVVVEFQHVKPG-KGGA-FVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489  81 EYVFMDKEDYTPYIFTKDQIEEELLFIPEGGMpdMQVLTWDGVLLALELPQTVDLEIVETAPGIKGASASARNKPATLTT 160
Cdd:COG0231    79 GYVFMDTETYEQIELPKEVVGDAAKFLKEGME--VTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLET 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1278835489 161 GLVVQVPEYLSAGEKIRIHIEEKRYMGRAD 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 2.47e-22

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: 84.74  E-value: 2.47e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1278835489 133 VDLEIVETAPGIKGASASARNKPATLTTGLVVQVPEYLSAGEKIRIHIEEKRYMGR 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 4.05e-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: 81.73  E-value: 4.05e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835489  133 VDLEIVETAPGIKGASASARNK-PATLTTGLVVQVPEYLSAGEKIRIHIEEKRYMGR 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 1.23e-19

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: 77.95  E-value: 1.23e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1278835489 133 VDLEIVETAPGIKGASASARNKPATLTTGLVVQVPEYLSAGEKIRIHIEEKRYMGR 188
Cdd:cd05794     1 VELEVTETEPGVKGDTASSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 56
 
Name Accession Description Interval E-value
PRK04542 PRK04542
elongation factor P; Provisional
 1-190 1.23e-129

elongation factor P; Provisional


Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 361.59  E-value: 1.23e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489   1 MPRANEIKKGMVLNYNGKLLIVKDIDIQAPSARGAATLYKMRFADVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYIDGN 80
Cdd:PRK04542    1 MPKANEIKKGMVVEYNGKLLLVKDIDRQSPSGRGGATLYKMRFYDVRTGLKVEERFKGDDILDTVDLTRRPVTFSYIDGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489  81 EYVFMDKEDYTPYIFTKDQIEEELLFIPEgGMPDMQVLTWDGVLLALELPQTVDLEIVETAPGIKGASASARNKPATLTT 160
Cdd:PRK04542   81 EYVFMDNEDYTPYTFKKDQIEDELLFIPE-GMPGMQVLTVDGQPVALELPQTVDLEIVETAPSIKGASASARTKPATLST 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 1278835489 161 GLVVQVPEYLSAGEKIRIHIEEKRYMGRAD 190
Cdd:PRK04542  160 GLVIQVPEYISTGEKIRINTEERKFMGRAD 189
yeiP TIGR02178
elongation factor P-like protein YeiP; This model represents the family of Escherichia coli ...
 3-189 2.91e-112

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: 317.59  E-value: 2.91e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489   3 RANEIKKGMVLNYNGKLLIVKDIDIQAPSARGAATLYKMRFADVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYIDGNEY 82
Cdd:TIGR02178   1 KASEMKKGSIVEYNGKTLLIKDIQRSSPQGRGGNVRYKFRMYDVPTGSKVEERFKADDMLDTVELLRREASFSYKDGEEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489  83 VFMDKEDYTPYIFTKDQIEEELLFIPEgGMPDMQVLTWDGVLLALELPQTVDLEIVETAPGIKGASASARNKPATLTTGL 162
Cdd:TIGR02178  81 VFMDEEDYTPYTFDKDAIEDELLFISE-GLSGMYVQLIDGSPVALELPQHVVLEIVETPPEIKGASASKRPKPAKLITGL 159

                         170       180
                  ....*....|....*....|....*..
gi 1278835489 163 VVQVPEYLSAGEKIRIHIEEKRYMGRA 189
Cdd:TIGR02178 160 VVQVPEYITTGERILINTTERAFMGRA 186
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 1-190 4.04e-78

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: 231.06  E-value: 4.04e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489   1 MPRANEIKKGMVLNYNGKLLIVKDIDIQAPSaRGAAtLYKMRFADVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYIDGN 80
Cdd:COG0231     1 MISANDLRKGLVIEIDGEPYVVVEFQHVKPG-KGGA-FVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489  81 EYVFMDKEDYTPYIFTKDQIEEELLFIPEGGMpdMQVLTWDGVLLALELPQTVDLEIVETAPGIKGASASARNKPATLTT 160
Cdd:COG0231    79 GYVFMDTETYEQIELPKEVVGDAAKFLKEGME--VTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLET 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1278835489 161 GLVVQVPEYLSAGEKIRIHIEEKRYMGRAD 190
Cdd:COG0231   157 GAVVQVPLFIEEGDKIKVDTRTGEYVERAK 186
PRK00529 PRK00529
elongation factor P; Validated
 1-189 6.81e-60

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 184.87  E-value: 6.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489   1 MPRANEIKKGMVLNYNGKLLIVKDIDIQAPsARGAAtLYKMRFADVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYIDGN 80
Cdd:PRK00529    1 MISANDLRKGLVIEIDGEPYVVLEFEHVKP-GKGQA-FVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489  81 EYVFMDKEDYTPYIFTKDQIEEELLFIPEGGMpdMQVLTWDGVLLALELPQTVDLEIVETAPGIKGASASARNKPATLTT 160
Cdd:PRK00529   79 GYVFMDTETYEQIEVPADQVGDAAKFLKEGME--VTVVFYNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLET 156

                         170       180
                  ....*....|....*....|....*....
gi 1278835489 161 GLVVQVPEYLSAGEKIRIHIEEKRYMGRA 189
Cdd:PRK00529  157 GAVVQVPLFINEGEKIKVDTRTGEYVERA 185
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 3-189 2.57e-59

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: 183.43  E-value: 2.57e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489   3 RANEIKKGMVLNYNGKLLIVKDIDIQAPsARGAAtLYKMRFADVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYIDGNEY 82
Cdd:TIGR00038   2 SANDLRKGLKIELDGEPYVVLEFEHVKP-GKGQA-FVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489  83 VFMDKEDYTPYIFTKDQIEEELLFIPEGGMpdMQVLTWDGVLLALELPQTVDLEIVETAPGIKGASASARNKPATLTTGL 162
Cdd:TIGR00038  80 VFMDTETYEQIELPKDLLGDAAKFLKENME--VSVVFYNGEPIGVELPNFVELEVTETEPGVKGDTASGSTKPATLETGA 157

                         170       180
                  ....*....|....*....|....*..
gi 1278835489 163 VVQVPEYLSAGEKIRIHIEEKRYMGRA 189
Cdd:TIGR00038 158 VVQVPLFIEEGEKIKVDTRTGEYVERA 184
PRK14578 PRK14578
elongation factor P; Provisional
 1-189 6.37e-42

elongation factor P; Provisional


Pssm-ID: 173042 [Multi-domain]  Cd Length: 187  Bit Score: 139.20  E-value: 6.37e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489   1 MPRANEIKKGMVLNYNGKLLIVKDIDIQAPSARGAATLYKMRFADVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYIDGN 80
Cdd:PRK14578    1 MYTTSDFKKGLVIQLDGAPCLLLDVTFQSPSARGANTMVKTKYRNLLTGQVLEKTFRSGDKVEEADFERHKGQFLYADGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489  81 EYVFMDKEDYTPYIFTKDQIEEELLFIPEGgmPDMQVLTWDGVLLALELPQTVDLEIVETAPGIKGASASARNKPATLTT 160
Cdd:PRK14578   81 RGVFMDLETYEQFEMEEDAFSAIAPFLLDG--TEVQLGLFQGRMVNVDLPMTVELTVTDTAPVMKNATATAQTKEAVLET 158

                         170       180
                  ....*....|....*....|....*....
gi 1278835489 161 GLVVQVPEYLSAGEKIRIHIEEKRYMGRA 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 2.47e-22

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: 84.74  E-value: 2.47e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1278835489 133 VDLEIVETAPGIKGASASARNKPATLTTGLVVQVPEYLSAGEKIRIHIEEKRYMGR 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 4.05e-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: 81.73  E-value: 4.05e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1278835489  133 VDLEIVETAPGIKGASASARNK-PATLTTGLVVQVPEYLSAGEKIRIHIEEKRYMGR 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 1.23e-19

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: 77.95  E-value: 1.23e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1278835489 133 VDLEIVETAPGIKGASASARNKPATLTTGLVVQVPEYLSAGEKIRIHIEEKRYMGR 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 1.59e-15

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: 67.48  E-value: 1.59e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278835489  68 TRRYVDFSYIDGNEYVFMDKEDYTPYIFTKDQIEEELLFIPEGGMpdMQVLTWDGVLLALELP 130
Cdd:cd04470     1 EEREMQYLYKDGDNYVFMDTETYEQIELPKEALGDAAKFLKEGME--VIVLFYNGEPIGVELP 61
PRK12426 PRK12426
elongation factor P; Provisional
 1-188 2.09e-15

elongation factor P; Provisional


Pssm-ID: 183522 [Multi-domain]  Cd Length: 185  Bit Score: 70.64  E-value: 2.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489   1 MPRANEIKKGMVLNYNGKLL-IVKDIDIQAPSArgaATLYKMRFADVRTGLKVEERFKGDDIVDTVTLTRRYVDFSYIDG 79
Cdd:PRK12426    1 MVLSSQLSVGMFISTKDGLYkVVSVSKVTGPKG---ETFIKVSLQAADSDVVVERNFKAGQEVKEAQFEPRNLEYLYLEG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278835489  80 NEYVFMDKEDYTPYIFTKDQIEEELLFIPEGgmPDMQVLTWDGVLLALELPQTVDLEIVETAPGIKGASASARNKPATLT 159
Cdd:PRK12426   78 DEYLFLDLGNYDKIYIPKEIMKDNFLFLKAG--VTVSALVYDGTVFSVELPHFLELMVSKTDFPGDSLSLSGGAKKALLE 155

                         170       180
                  ....*....|....*....|....*....
gi 1278835489 160 TGLVVQVPEYLSAGEKIRIHIEEKRYMGR 188
Cdd:PRK12426  156 TGVEVLVPPFVEIGDVIKVDTRTCEYIQR 184
EFP_N pfam08207
Elongation factor P (EF-P) KOW-like domain;
4-62 2.89e-15

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


Pssm-ID: 429864 [Multi-domain]  Cd Length: 58  Bit Score: 66.69  E-value: 2.89e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1278835489   4 ANEIKKGMVLNYNGKLLIVKDIDIQAPsaRGAATLYKMRFADVRTGLKVEERFKGDDIV 62
Cdd:pfam08207   2 ANELRKGNVIEIDGEPYVVLEFEHVKP--GKGQAFVRTKLKNLRTGAKVEKTFKAGDKV 58
EFP pfam01132
Elongation factor P (EF-P) OB domain;
74-122 2.23e-11

Elongation factor P (EF-P) OB domain;


Pssm-ID: 460077 [Multi-domain]  Cd Length: 54  Bit Score: 56.26  E-value: 2.23e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1278835489  74 FSYIDGNEYVFMDKEDYTPYIFTKDQIEEELLFIPEGGMpdMQVLTWDG 122
Cdd:pfam01132   5 YLYNDGDDYVFMDNETYEQIELPKEQLGDAAKFLKEGME--VTVLFYEG 51
 
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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