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Conserved domains on  [gi|491003094|ref|WP_004864815|]
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MULTISPECIES: elongation factor P-like protein YeiP [Raoultella]

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 3.47e-132

elongation factor P; Provisional


:

Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 368.14  E-value: 3.47e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094   1 MPRANEIKKGMVLNYNGKLLIVKNIDIQSPSARGAATLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRFVDFSYVDGN 80
Cdd:PRK04542   1 MPKANEIKKGMVVEYNGKLLLVKDIDRQSPSGRGGATLYKMRFYDVRTGLKVEERFKGDDILDTVDLTRRPVTFSYIDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094  81 EYVFMDKEDYTPYTFTKEQIEEELLFIPEgGMPDMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASSRTKPATLST 160
Cdd:PRK04542  81 EYVFMDNEDYTPYTFKKDQIEDELLFIPE-GMPGMQVLTVDGQPVALELPQTVDLEIVETAPSIKGASASARTKPATLST 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 491003094 161 GLVIQVPEYLTTGEKIRIHIEESRYMGRAD 190
Cdd:PRK04542 160 GLVIQVPEYISTGEKIRINTEERKFMGRAD 189
 
Name Accession Description Interval E-value
PRK04542 PRK04542
elongation factor P; Provisional
 1-190 3.47e-132

elongation factor P; Provisional


Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 368.14  E-value: 3.47e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094   1 MPRANEIKKGMVLNYNGKLLIVKNIDIQSPSARGAATLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRFVDFSYVDGN 80
Cdd:PRK04542   1 MPKANEIKKGMVVEYNGKLLLVKDIDRQSPSGRGGATLYKMRFYDVRTGLKVEERFKGDDILDTVDLTRRPVTFSYIDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094  81 EYVFMDKEDYTPYTFTKEQIEEELLFIPEgGMPDMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASSRTKPATLST 160
Cdd:PRK04542  81 EYVFMDNEDYTPYTFKKDQIEDELLFIPE-GMPGMQVLTVDGQPVALELPQTVDLEIVETAPSIKGASASARTKPATLST 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 491003094 161 GLVIQVPEYLTTGEKIRIHIEESRYMGRAD 190
Cdd:PRK04542 160 GLVIQVPEYISTGEKIRINTEERKFMGRAD 189
yeiP TIGR02178
elongation factor P-like protein YeiP; This model represents the family of Escherichia coli ...
 3-189 5.67e-114

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: 321.83  E-value: 5.67e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094    3 RANEIKKGMVLNYNGKLLIVKNIDIQSPSARGAATLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRFVDFSYVDGNEY 82
Cdd:TIGR02178   1 KASEMKKGSIVEYNGKTLLIKDIQRSSPQGRGGNVRYKFRMYDVPTGSKVEERFKADDMLDTVELLRREASFSYKDGEEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094   83 VFMDKEDYTPYTFTKEQIEEELLFIPEgGMPDMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASSRTKPATLSTGL 162
Cdd:TIGR02178  81 VFMDEEDYTPYTFDKDAIEDELLFISE-GLSGMYVQLIDGSPVALELPQHVVLEIVETPPEIKGASASKRPKPAKLITGL 159

                         170       180
                  ....*....|....*....|....*..
gi 491003094  163 VIQVPEYLTTGEKIRIHIEESRYMGRA 189
Cdd:TIGR02178 160 VVQVPEYITTGERILINTTERAFMGRA 186
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 1-190 1.02e-80

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: 237.61  E-value: 1.02e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094   1 MPRANEIKKGMVLNYNGKLLIVKNIDIQSPSaRGAAtLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRFVDFSYVDGN 80
Cdd:COG0231    1 MISANDLRKGLVIEIDGEPYVVVEFQHVKPG-KGGA-FVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094  81 EYVFMDKEDYTPYTFTKEQIEEELLFIPEGGMpdMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASSRTKPATLST 160
Cdd:COG0231   79 GYVFMDTETYEQIELPKEVVGDAAKFLKEGME--VTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLET 156

                        170       180       190
                 ....*....|....*....|....*....|
gi 491003094 161 GLVIQVPEYLTTGEKIRIHIEESRYMGRAD 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 1.33e-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: 88.21  E-value: 1.33e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 491003094  133 VDLEIVETAPGIKGASASSRTKPATLSTGLVIQVPEYLTTGEKIRIHIEESRYMGR 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 4.17e-22

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: 84.43  E-value: 4.17e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 491003094   133 VDLEIVETAPGIKGASASSRTK-PATLSTGLVIQVPEYLTTGEKIRIHIEESRYMGR 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 2.45e-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: 79.88  E-value: 2.45e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491003094 133 VDLEIVETAPGIKGASASSRTKPATLSTGLVIQVPEYLTTGEKIRIHIEESRYMGR 188
Cdd:cd05794    1 VELEVTETEPGVKGDTASSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 56
 
Name Accession Description Interval E-value
PRK04542 PRK04542
elongation factor P; Provisional
 1-190 3.47e-132

elongation factor P; Provisional


Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 368.14  E-value: 3.47e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094   1 MPRANEIKKGMVLNYNGKLLIVKNIDIQSPSARGAATLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRFVDFSYVDGN 80
Cdd:PRK04542   1 MPKANEIKKGMVVEYNGKLLLVKDIDRQSPSGRGGATLYKMRFYDVRTGLKVEERFKGDDILDTVDLTRRPVTFSYIDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094  81 EYVFMDKEDYTPYTFTKEQIEEELLFIPEgGMPDMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASSRTKPATLST 160
Cdd:PRK04542  81 EYVFMDNEDYTPYTFKKDQIEDELLFIPE-GMPGMQVLTVDGQPVALELPQTVDLEIVETAPSIKGASASARTKPATLST 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 491003094 161 GLVIQVPEYLTTGEKIRIHIEESRYMGRAD 190
Cdd:PRK04542 160 GLVIQVPEYISTGEKIRINTEERKFMGRAD 189
yeiP TIGR02178
elongation factor P-like protein YeiP; This model represents the family of Escherichia coli ...
 3-189 5.67e-114

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: 321.83  E-value: 5.67e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094    3 RANEIKKGMVLNYNGKLLIVKNIDIQSPSARGAATLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRFVDFSYVDGNEY 82
Cdd:TIGR02178   1 KASEMKKGSIVEYNGKTLLIKDIQRSSPQGRGGNVRYKFRMYDVPTGSKVEERFKADDMLDTVELLRREASFSYKDGEEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094   83 VFMDKEDYTPYTFTKEQIEEELLFIPEgGMPDMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASSRTKPATLSTGL 162
Cdd:TIGR02178  81 VFMDEEDYTPYTFDKDAIEDELLFISE-GLSGMYVQLIDGSPVALELPQHVVLEIVETPPEIKGASASKRPKPAKLITGL 159

                         170       180
                  ....*....|....*....|....*..
gi 491003094  163 VIQVPEYLTTGEKIRIHIEESRYMGRA 189
Cdd:TIGR02178 160 VVQVPEYITTGERILINTTERAFMGRA 186
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 1-190 1.02e-80

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: 237.61  E-value: 1.02e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094   1 MPRANEIKKGMVLNYNGKLLIVKNIDIQSPSaRGAAtLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRFVDFSYVDGN 80
Cdd:COG0231    1 MISANDLRKGLVIEIDGEPYVVVEFQHVKPG-KGGA-FVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094  81 EYVFMDKEDYTPYTFTKEQIEEELLFIPEGGMpdMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASSRTKPATLST 160
Cdd:COG0231   79 GYVFMDTETYEQIELPKEVVGDAAKFLKEGME--VTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLET 156

                        170       180       190
                 ....*....|....*....|....*....|
gi 491003094 161 GLVIQVPEYLTTGEKIRIHIEESRYMGRAD 190
Cdd:COG0231  157 GAVVQVPLFIEEGDKIKVDTRTGEYVERAK 186
PRK00529 PRK00529
elongation factor P; Validated
 1-189 2.66e-62

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 191.03  E-value: 2.66e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094   1 MPRANEIKKGMVLNYNGKLLIVknIDIQ-SPSARGAAtLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRFVDFSYVDG 79
Cdd:PRK00529   1 MISANDLRKGLVIEIDGEPYVV--LEFEhVKPGKGQA-FVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094  80 NEYVFMDKEDYTPYTFTKEQIEEELLFIPEGGMpdMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASSRTKPATLS 159
Cdd:PRK00529  78 DGYVFMDTETYEQIEVPADQVGDAAKFLKEGME--VTVVFYNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLE 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 491003094 160 TGLVIQVPEYLTTGEKIRIHIEESRYMGRA 189
Cdd:PRK00529 156 TGAVVQVPLFINEGEKIKVDTRTGEYVERA 185
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 3-189 3.72e-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: 3.72e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094    3 RANEIKKGMVLNYNGKLLIVKNIDIQSPsARGAAtLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRFVDFSYVDGNEY 82
Cdd:TIGR00038   2 SANDLRKGLKIELDGEPYVVLEFEHVKP-GKGQA-FVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094   83 VFMDKEDYTPYTFTKEQIEEELLFIPEGGMpdMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASSRTKPATLSTGL 162
Cdd:TIGR00038  80 VFMDTETYEQIELPKDLLGDAAKFLKENME--VSVVFYNGEPIGVELPNFVELEVTETEPGVKGDTASGSTKPATLETGA 157

                         170       180
                  ....*....|....*....|....*..
gi 491003094  163 VIQVPEYLTTGEKIRIHIEESRYMGRA 189
Cdd:TIGR00038 158 VVQVPLFIEEGEKIKVDTRTGEYVERA 184
PRK14578 PRK14578
elongation factor P; Provisional
 1-189 7.44e-43

elongation factor P; Provisional


Pssm-ID: 173042 [Multi-domain]  Cd Length: 187  Bit Score: 141.51  E-value: 7.44e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094   1 MPRANEIKKGMVLNYNGKLLIVKNIDIQSPSARGAATLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRFVDFSYVDGN 80
Cdd:PRK14578   1 MYTTSDFKKGLVIQLDGAPCLLLDVTFQSPSARGANTMVKTKYRNLLTGQVLEKTFRSGDKVEEADFERHKGQFLYADGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094  81 EYVFMDKEDYTPYTFTKEQIEEELLFIPEGgmPDMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASSRTKPATLST 160
Cdd:PRK14578  81 RGVFMDLETYEQFEMEEDAFSAIAPFLLDG--TEVQLGLFQGRMVNVDLPMTVELTVTDTAPVMKNATATAQTKEAVLET 158

                        170       180
                 ....*....|....*....|....*....
gi 491003094 161 GLVIQVPEYLTTGEKIRIHIEESRYMGRA 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 1.33e-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: 88.21  E-value: 1.33e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 491003094  133 VDLEIVETAPGIKGASASSRTKPATLSTGLVIQVPEYLTTGEKIRIHIEESRYMGR 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 4.17e-22

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: 84.43  E-value: 4.17e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 491003094   133 VDLEIVETAPGIKGASASSRTK-PATLSTGLVIQVPEYLTTGEKIRIHIEESRYMGR 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 2.45e-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: 79.88  E-value: 2.45e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491003094 133 VDLEIVETAPGIKGASASSRTKPATLSTGLVIQVPEYLTTGEKIRIHIEESRYMGR 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 5.18e-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: 5.18e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491003094  68 TRRFVDFSYVDGNEYVFMDKEDYTPYTFTKEQIEEELLFIPEGGMpdMQVLTWDGQLLALELP 130
Cdd:cd04470    1 EEREMQYLYKDGDNYVFMDTETYEQIELPKEALGDAAKFLKEGME--VIVLFYNGEPIGVELP 61
PRK12426 PRK12426
elongation factor P; Provisional
 1-188 1.67e-16

elongation factor P; Provisional


Pssm-ID: 183522 [Multi-domain]  Cd Length: 185  Bit Score: 73.34  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094   1 MPRANEIKKGMVLNYNGKLLIVknIDIQSPSARGAATLYKMRFSDVRTGLKVEERFKGDDIVDTVTLTRRFVDFSYVDGN 80
Cdd:PRK12426   1 MVLSSQLSVGMFISTKDGLYKV--VSVSKVTGPKGETFIKVSLQAADSDVVVERNFKAGQEVKEAQFEPRNLEYLYLEGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003094  81 EYVFMDKEDYTPYTFTKEQIEEELLFIPEGgmPDMQVLTWDGQLLALELPQTVDLEIVETAPGIKGASASSRTKPATLST 160
Cdd:PRK12426  79 EYLFLDLGNYDKIYIPKEIMKDNFLFLKAG--VTVSALVYDGTVFSVELPHFLELMVSKTDFPGDSLSLSGGAKKALLET 156

                        170       180
                 ....*....|....*....|....*...
gi 491003094 161 GLVIQVPEYLTTGEKIRIHIEESRYMGR 188
Cdd:PRK12426 157 GVEVLVPPFVEIGDVIKVDTRTCEYIQR 184
EFP_N pfam08207
Elongation factor P (EF-P) KOW-like domain;
4-62 4.67e-15

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


Pssm-ID: 429864 [Multi-domain]  Cd Length: 58  Bit Score: 66.30  E-value: 4.67e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 491003094    4 ANEIKKGMVLNYNGKLLIVknIDIQSPSARGAATLYKMRFSDVRTGLKVEERFKGDDIV 62
Cdd:pfam08207   2 ANELRKGNVIEIDGEPYVV--LEFEHVKPGKGQAFVRTKLKNLRTGAKVEKTFKAGDKV 58
EFP pfam01132
Elongation factor P (EF-P) OB domain;
74-125 2.83e-12

Elongation factor P (EF-P) OB domain;


Pssm-ID: 460077 [Multi-domain]  Cd Length: 54  Bit Score: 58.95  E-value: 2.83e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 491003094   74 FSYVDGNEYVFMDKEDYTPYTFTKEQIEEELLFIPEGGMpdMQVLTWDGQLL 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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