NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|940687070|ref|WP_055020721|]
View 

MULTISPECIES: elongation factor P-like protein YeiP [Pseudoalteromonas]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK04542 PRK04542
elongation factor P; Provisional
 1-189 9.63e-132

elongation factor P; Provisional


:

Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 366.98  E-value: 9.63e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070   1 MPKASEVKKGAAIEHNGRVLVVKDIQRSVPQGRAGGSLYRMRLYDVVTGGKVDETFKDSDMLKLADLIRREAMFSYIDGE 80
Cdd:PRK04542   1 MPKANEIKKGMVVEYNGKLLLVKDIDRQSPSGRGGATLYKMRFYDVRTGLKVEERFKGDDILDTVDLTRRPVTFSYIDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070  81 EYVFMDNEDYTPYNLNKEAISEEILFVNEETQGLHVIVIDGSPVGLDLPSSVELVVEETDPSIKGASASARSKPARLTTG 160
Cdd:PRK04542  81 EYVFMDNEDYTPYTFKKDQIEDELLFIPEGMPGMQVLTVDGQPVALELPQTVDLEIVETAPSIKGASASARTKPATLSTG 160

                        170       180
                 ....*....|....*....|....*....
gi 940687070 161 LTIQVPEHISTGDRIRINTVEHKFMGRAE 189
Cdd:PRK04542 161 LVIQVPEYISTGEKIRINTEERKFMGRAD 189
 
Name Accession Description Interval E-value
PRK04542 PRK04542
elongation factor P; Provisional
 1-189 9.63e-132

elongation factor P; Provisional


Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 366.98  E-value: 9.63e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070   1 MPKASEVKKGAAIEHNGRVLVVKDIQRSVPQGRAGGSLYRMRLYDVVTGGKVDETFKDSDMLKLADLIRREAMFSYIDGE 80
Cdd:PRK04542   1 MPKANEIKKGMVVEYNGKLLLVKDIDRQSPSGRGGATLYKMRFYDVRTGLKVEERFKGDDILDTVDLTRRPVTFSYIDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070  81 EYVFMDNEDYTPYNLNKEAISEEILFVNEETQGLHVIVIDGSPVGLDLPSSVELVVEETDPSIKGASASARSKPARLTTG 160
Cdd:PRK04542  81 EYVFMDNEDYTPYTFKKDQIEDELLFIPEGMPGMQVLTVDGQPVALELPQTVDLEIVETAPSIKGASASARTKPATLSTG 160

                        170       180
                 ....*....|....*....|....*....
gi 940687070 161 LTIQVPEHISTGDRIRINTVEHKFMGRAE 189
Cdd:PRK04542 161 LVIQVPEYISTGEKIRINTEERKFMGRAD 189
yeiP TIGR02178
elongation factor P-like protein YeiP; This model represents the family of Escherichia coli ...
 3-188 1.71e-92

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: 267.52  E-value: 1.71e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070    3 KASEVKKGAAIEHNGRVLVVKDIQRSVPQGRAGGSLYRMRLYDVVTGGKVDETFKDSDMLKLADLIRREAMFSYIDGEEY 82
Cdd:TIGR02178   1 KASEMKKGSIVEYNGKTLLIKDIQRSSPQGRGGNVRYKFRMYDVPTGSKVEERFKADDMLDTVELLRREASFSYKDGEEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070   83 VFMDNEDYTPYNLNKEAISEEILFVNEETQGLHVIVIDGSPVGLDLPSSVELVVEETDPSIKGASASARSKPARLTTGLT 162
Cdd:TIGR02178  81 VFMDEEDYTPYTFDKDAIEDELLFISEGLSGMYVQLIDGSPVALELPQHVVLEIVETPPEIKGASASKRPKPAKLITGLV 160

                         170       180
                  ....*....|....*....|....*.
gi 940687070  163 IQVPEHISTGDRIRINTVEHKFMGRA 188
Cdd:TIGR02178 161 VQVPEYITTGERILINTTERAFMGRA 186
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 1-188 2.23e-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: 236.84  E-value: 2.23e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070   1 MPKASEVKKGAAIEHNGRVLVVKDIQRSVPqGRaGGSLYRMRLYDVVTGGKVDETFKDSDMLKLADLIRREAMFSYIDGE 80
Cdd:COG0231    1 MISANDLRKGLVIEIDGEPYVVVEFQHVKP-GK-GGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070  81 EYVFMDNEDYTPYNLNKEAISEEILFVNEETQgLHVIVIDGSPVGLDLPSSVELVVEETDPSIKGASASARSKPARLTTG 160
Cdd:COG0231   79 GYVFMDTETYEQIELPKEVVGDAAKFLKEGME-VTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETG 157

                        170       180
                 ....*....|....*....|....*...
gi 940687070 161 LTIQVPEHISTGDRIRINTVEHKFMGRA 188
Cdd:COG0231  158 AVVQVPLFIEEGDKIKVDTRTGEYVERA 185
Elong-fact-P_C pfam09285
Elongation factor P, C-terminal; Members of this family of nucleic acid binding domains are ...
 132-187 8.34e-24

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: 88.59  E-value: 8.34e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 940687070  132 VELVVEETDPSIKGASASARSKPARLTTGLTIQVPEHISTGDRIRINTVEHKFMGR 187
Cdd:pfam09285   1 VELEVTETEPGVKGDTASGATKPATLETGAEVQVPLFINEGDKIKVDTRTGEYVER 56
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 132-187 9.98e-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: 83.27  E-value: 9.98e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 940687070   132 VELVVEETDPSIKGASASARSK-PARLTTGLTIQVPEHISTGDRIRINTVEHKFMGR 187
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. ...
 132-187 4.76e-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: 76.41  E-value: 4.76e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 940687070 132 VELVVEETDPSIKGASASARSKPARLTTGLTIQVPEHISTGDRIRINTVEHKFMGR 187
Cdd:cd05794    1 VELEVTETEPGVKGDTASSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 56
 
Name Accession Description Interval E-value
PRK04542 PRK04542
elongation factor P; Provisional
 1-189 9.63e-132

elongation factor P; Provisional


Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 366.98  E-value: 9.63e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070   1 MPKASEVKKGAAIEHNGRVLVVKDIQRSVPQGRAGGSLYRMRLYDVVTGGKVDETFKDSDMLKLADLIRREAMFSYIDGE 80
Cdd:PRK04542   1 MPKANEIKKGMVVEYNGKLLLVKDIDRQSPSGRGGATLYKMRFYDVRTGLKVEERFKGDDILDTVDLTRRPVTFSYIDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070  81 EYVFMDNEDYTPYNLNKEAISEEILFVNEETQGLHVIVIDGSPVGLDLPSSVELVVEETDPSIKGASASARSKPARLTTG 160
Cdd:PRK04542  81 EYVFMDNEDYTPYTFKKDQIEDELLFIPEGMPGMQVLTVDGQPVALELPQTVDLEIVETAPSIKGASASARTKPATLSTG 160

                        170       180
                 ....*....|....*....|....*....
gi 940687070 161 LTIQVPEHISTGDRIRINTVEHKFMGRAE 189
Cdd:PRK04542 161 LVIQVPEYISTGEKIRINTEERKFMGRAD 189
yeiP TIGR02178
elongation factor P-like protein YeiP; This model represents the family of Escherichia coli ...
 3-188 1.71e-92

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: 267.52  E-value: 1.71e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070    3 KASEVKKGAAIEHNGRVLVVKDIQRSVPQGRAGGSLYRMRLYDVVTGGKVDETFKDSDMLKLADLIRREAMFSYIDGEEY 82
Cdd:TIGR02178   1 KASEMKKGSIVEYNGKTLLIKDIQRSSPQGRGGNVRYKFRMYDVPTGSKVEERFKADDMLDTVELLRREASFSYKDGEEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070   83 VFMDNEDYTPYNLNKEAISEEILFVNEETQGLHVIVIDGSPVGLDLPSSVELVVEETDPSIKGASASARSKPARLTTGLT 162
Cdd:TIGR02178  81 VFMDEEDYTPYTFDKDAIEDELLFISEGLSGMYVQLIDGSPVALELPQHVVLEIVETPPEIKGASASKRPKPAKLITGLV 160

                         170       180
                  ....*....|....*....|....*.
gi 940687070  163 IQVPEHISTGDRIRINTVEHKFMGRA 188
Cdd:TIGR02178 161 VQVPEYITTGERILINTTERAFMGRA 186
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 1-188 2.23e-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: 236.84  E-value: 2.23e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070   1 MPKASEVKKGAAIEHNGRVLVVKDIQRSVPqGRaGGSLYRMRLYDVVTGGKVDETFKDSDMLKLADLIRREAMFSYIDGE 80
Cdd:COG0231    1 MISANDLRKGLVIEIDGEPYVVVEFQHVKP-GK-GGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070  81 EYVFMDNEDYTPYNLNKEAISEEILFVNEETQgLHVIVIDGSPVGLDLPSSVELVVEETDPSIKGASASARSKPARLTTG 160
Cdd:COG0231   79 GYVFMDTETYEQIELPKEVVGDAAKFLKEGME-VTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETG 157

                        170       180
                 ....*....|....*....|....*...
gi 940687070 161 LTIQVPEHISTGDRIRINTVEHKFMGRA 188
Cdd:COG0231  158 AVVQVPLFIEEGDKIKVDTRTGEYVERA 185
PRK00529 PRK00529
elongation factor P; Validated
 1-188 1.61e-59

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 184.10  E-value: 1.61e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070   1 MPKASEVKKGAAIEHNGRVLVVKDIQRSVPqGRaGGSLYRMRLYDVVTGGKVDETFKDSDMLKLADLIRREAMFSYIDGE 80
Cdd:PRK00529   1 MISANDLRKGLVIEIDGEPYVVLEFEHVKP-GK-GQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070  81 EYVFMDNEDYTPYNLNKEAISEEILFVNEetqGLHVIVI--DGSPVGLDLPSSVELVVEETDPSIKGASASARSKPARLT 158
Cdd:PRK00529  79 GYVFMDTETYEQIEVPADQVGDAAKFLKE---GMEVTVVfyNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLE 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 940687070 159 TGLTIQVPEHISTGDRIRINTVEHKFMGRA 188
Cdd:PRK00529 156 TGAVVQVPLFINEGEKIKVDTRTGEYVERA 185
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 4-188 2.57e-58

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: 180.73  E-value: 2.57e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070    4 ASEVKKGAAIEHNGRVLVVKDIQRSVPqGRaGGSLYRMRLYDVVTGGKVDETFKDSDMLKLADLIRREAMFSYIDGEEYV 83
Cdd:TIGR00038   3 ANDLRKGLKIELDGEPYVVLEFEHVKP-GK-GQAFVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070   84 FMDNEDYTPYNLNKEAISEEILFVNEetqGLHVIVI--DGSPVGLDLPSSVELVVEETDPSIKGASASARSKPARLTTGL 161
Cdd:TIGR00038  81 FMDTETYEQIELPKDLLGDAAKFLKE---NMEVSVVfyNGEPIGVELPNFVELEVTETEPGVKGDTASGSTKPATLETGA 157

                         170       180
                  ....*....|....*....|....*..
gi 940687070  162 TIQVPEHISTGDRIRINTVEHKFMGRA 188
Cdd:TIGR00038 158 VVQVPLFIEEGEKIKVDTRTGEYVERA 184
PRK14578 PRK14578
elongation factor P; Provisional
 1-188 2.42e-36

elongation factor P; Provisional


Pssm-ID: 173042 [Multi-domain]  Cd Length: 187  Bit Score: 124.95  E-value: 2.42e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070   1 MPKASEVKKGAAIEHNGRVLVVKDIQRSVPQGRAGGSLYRMRLYDVVTGGKVDETFKDSDMLKLADLIRREAMFSYIDGE 80
Cdd:PRK14578   1 MYTTSDFKKGLVIQLDGAPCLLLDVTFQSPSARGANTMVKTKYRNLLTGQVLEKTFRSGDKVEEADFERHKGQFLYADGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070  81 EYVFMDNEDYTPYNLNKEAISEEILFVNEETQgLHVIVIDGSPVGLDLPSSVELVVEETDPSIKGASASARSKPARLTTG 160
Cdd:PRK14578  81 RGVFMDLETYEQFEMEEDAFSAIAPFLLDGTE-VQLGLFQGRMVNVDLPMTVELTVTDTAPVMKNATATAQTKEAVLETG 159

                        170       180
                 ....*....|....*....|....*...
gi 940687070 161 LTIQVPEHISTGDRIRINTVEHKFMGRA 188
Cdd:PRK14578 160 LRLQVPPYLESGEKIKVDTRDGRFISRA 187
Elong-fact-P_C pfam09285
Elongation factor P, C-terminal; Members of this family of nucleic acid binding domains are ...
 132-187 8.34e-24

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: 88.59  E-value: 8.34e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 940687070  132 VELVVEETDPSIKGASASARSKPARLTTGLTIQVPEHISTGDRIRINTVEHKFMGR 187
Cdd:pfam09285   1 VELEVTETEPGVKGDTASGATKPATLETGAEVQVPLFINEGDKIKVDTRTGEYVER 56
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 132-187 9.98e-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: 83.27  E-value: 9.98e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 940687070   132 VELVVEETDPSIKGASASARSK-PARLTTGLTIQVPEHISTGDRIRINTVEHKFMGR 187
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. ...
 132-187 4.76e-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: 76.41  E-value: 4.76e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 940687070 132 VELVVEETDPSIKGASASARSKPARLTTGLTIQVPEHISTGDRIRINTVEHKFMGR 187
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. ...
 69-129 5.02e-18

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: 74.03  E-value: 5.02e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940687070  69 RREAMFSYIDGEEYVFMDNEDYTPYNLNKEAISEEILFVNEETQGlHVIVIDGSPVGLDLP 129
Cdd:cd04470    2 EREMQYLYKDGDNYVFMDTETYEQIELPKEALGDAAKFLKEGMEV-IVLFYNGEPIGVELP 61
EFP_N pfam08207
Elongation factor P (EF-P) KOW-like domain;
3-62 5.14e-16

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


Pssm-ID: 429864 [Multi-domain]  Cd Length: 58  Bit Score: 68.61  E-value: 5.14e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070    3 KASEVKKGAAIEHNGRVLVVKDIQrSVPQGRaGGSLYRMRLYDVVTGGKVDETFKDSDML 62
Cdd:pfam08207   1 SANELRKGNVIEIDGEPYVVLEFE-HVKPGK-GQAFVRTKLKNLRTGAKVEKTFKAGDKV 58
PRK12426 PRK12426
elongation factor P; Provisional
 16-187 8.10e-16

elongation factor P; Provisional


Pssm-ID: 183522 [Multi-domain]  Cd Length: 185  Bit Score: 71.80  E-value: 8.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070  16 NGRVLVVKDIQRSVPQGRaggSLYRMRLYDVVTGGKVDETFKDSDMLKLADLIRREAMFSYIDGEEYVFMDNEDYTPYNL 95
Cdd:PRK12426  17 DGLYKVVSVSKVTGPKGE---TFIKVSLQAADSDVVVERNFKAGQEVKEAQFEPRNLEYLYLEGDEYLFLDLGNYDKIYI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940687070  96 NKEAISEEILFVNEETQgLHVIVIDGSPVGLDLPSSVELVVEETDPSIKGASASARSKPARLTTGLTIQVPEHISTGDRI 175
Cdd:PRK12426  94 PKEIMKDNFLFLKAGVT-VSALVYDGTVFSVELPHFLELMVSKTDFPGDSLSLSGGAKKALLETGVEVLVPPFVEIGDVI 172

                        170
                 ....*....|..
gi 940687070 176 RINTVEHKFMGR 187
Cdd:PRK12426 173 KVDTRTCEYIQR 184
EFP pfam01132
Elongation factor P (EF-P) OB domain;
70-124 1.96e-13

Elongation factor P (EF-P) OB domain;


Pssm-ID: 460077 [Multi-domain]  Cd Length: 54  Bit Score: 61.65  E-value: 1.96e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 940687070   70 REAMFSYIDGEEYVFMDNEDYTPYNLNKEAISEEILFVNEETQgLHVIVIDGSPV 124
Cdd:pfam01132   1 REMQYLYNDGDDYVFMDNETYEQIELPKEQLGDAAKFLKEGME-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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH