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Conserved domains on  [gi|547184715|ref|WP_021926717|]
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MULTISPECIES: elongation factor P [Clostridia]

Protein Classification

elongation factor P( domain architecture ID 11415475)

elongation factor P (EF-P) is an essential protein that stimulates ribosomal peptidyltransferase activity

Gene Ontology:  GO:0005737|GO:0005829|GO:0003746
PubMed:  23239624|31178848

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 1-185 9.13e-115

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: 323.51  E-value: 9.13e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715   1 MISAGDFRNGVTVEIDGNVCQIVEFQHVKPGKGAAFVRTKYKNIITGSVLEKSFRPTEKFPTARIERVDMQYLYNDGGLY 80
Cdd:COG0231    1 MISANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715  81 YFMNVETFDQVGLTEEQVGDSLKFVKENEMVKICSHNGNVFAIEPPLFVELVVTETEPGFAGNTAQGATKPATVETGAQV 160
Cdd:COG0231   81 VFMDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGAVV 160

                        170       180
                 ....*....|....*....|....*
gi 547184715 161 MVPLFVNQGDKLKIDTRTGEYLSRV 185
Cdd:COG0231  161 QVPLFIEEGDKIKVDTRTGEYVERA 185
 
Name Accession Description Interval E-value
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 1-185 9.13e-115

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: 323.51  E-value: 9.13e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715   1 MISAGDFRNGVTVEIDGNVCQIVEFQHVKPGKGAAFVRTKYKNIITGSVLEKSFRPTEKFPTARIERVDMQYLYNDGGLY 80
Cdd:COG0231    1 MISANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715  81 YFMNVETFDQVGLTEEQVGDSLKFVKENEMVKICSHNGNVFAIEPPLFVELVVTETEPGFAGNTAQGATKPATVETGAQV 160
Cdd:COG0231   81 VFMDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGAVV 160

                        170       180
                 ....*....|....*....|....*
gi 547184715 161 MVPLFVNQGDKLKIDTRTGEYLSRV 185
Cdd:COG0231  161 QVPLFIEEGDKIKVDTRTGEYVERA 185
PRK00529 PRK00529
elongation factor P; Validated
 1-185 3.69e-109

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 309.29  E-value: 3.69e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715   1 MISAGDFRNGVTVEIDGNVCQIVEFQHVKPGKGAAFVRTKYKNIITGSVLEKSFRPTEKFPTARIERVDMQYLYNDGGLY 80
Cdd:PRK00529   1 MISANDLRKGLVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGDGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715  81 YFMNVETFDQVGLTEEQVGDSLKFVKENEMVKICSHNGNVFAIEPPLFVELVVTETEPGFAGNTAQGATKPATVETGAQV 160
Cdd:PRK00529  81 VFMDTETYEQIEVPADQVGDAAKFLKEGMEVTVVFYNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLETGAVV 160

                        170       180
                 ....*....|....*....|....*
gi 547184715 161 MVPLFVNQGDKLKIDTRTGEYLSRV 185
Cdd:PRK00529 161 QVPLFINEGEKIKVDTRTGEYVERA 185
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 2-185 2.18e-102

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: 292.06  E-value: 2.18e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715    2 ISAGDFRNGVTVEIDGNVCQIVEFQHVKPGKGAAFVRTKYKNIITGSVLEKSFRPTEKFPTARIERVDMQYLYNDGGLYY 81
Cdd:TIGR00038   1 ISANDLRKGLKIELDGEPYVVLEFEHVKPGKGQAFVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715   82 FMNVETFDQVGLTEEQVGDSLKFVKENEMVKICSHNGNVFAIEPPLFVELVVTETEPGFAGNTAQGATKPATVETGAQVM 161
Cdd:TIGR00038  81 FMDTETYEQIELPKDLLGDAAKFLKENMEVSVVFYNGEPIGVELPNFVELEVTETEPGVKGDTASGSTKPATLETGAVVQ 160

                         170       180
                  ....*....|....*....|....
gi 547184715  162 VPLFVNQGDKLKIDTRTGEYLSRV 185
Cdd:TIGR00038 161 VPLFIEEGEKIKVDTRTGEYVERA 184
Elong-fact-P_C pfam09285
Elongation factor P, C-terminal; Members of this family of nucleic acid binding domains are ...
 129-184 1.33e-31

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: 108.62  E-value: 1.33e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 547184715  129 VELVVTETEPGFAGNTAQGATKPATVETGAQVMVPLFVNQGDKLKIDTRTGEYLSR 184
Cdd:pfam09285   1 VELEVTETEPGVKGDTASGATKPATLETGAEVQVPLFINEGDKIKVDTRTGEYVER 56
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 129-184 1.76e-27

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: 97.91  E-value: 1.76e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 547184715   129 VELVVTETEPGFAGNTAQGATK-PATVETGAQVMVPLFVNQGDKLKIDTRTGEYLSR 184
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. ...
 129-184 2.30e-26

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: 95.28  E-value: 2.30e-26
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 547184715 129 VELVVTETEPGFAGNTAQGATKPATVETGAQVMVPLFVNQGDKLKIDTRTGEYLSR 184
Cdd:cd05794    1 VELEVTETEPGVKGDTASSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 56
 
Name Accession Description Interval E-value
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 1-185 9.13e-115

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: 323.51  E-value: 9.13e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715   1 MISAGDFRNGVTVEIDGNVCQIVEFQHVKPGKGAAFVRTKYKNIITGSVLEKSFRPTEKFPTARIERVDMQYLYNDGGLY 80
Cdd:COG0231    1 MISANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715  81 YFMNVETFDQVGLTEEQVGDSLKFVKENEMVKICSHNGNVFAIEPPLFVELVVTETEPGFAGNTAQGATKPATVETGAQV 160
Cdd:COG0231   81 VFMDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGAVV 160

                        170       180
                 ....*....|....*....|....*
gi 547184715 161 MVPLFVNQGDKLKIDTRTGEYLSRV 185
Cdd:COG0231  161 QVPLFIEEGDKIKVDTRTGEYVERA 185
PRK00529 PRK00529
elongation factor P; Validated
 1-185 3.69e-109

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 309.29  E-value: 3.69e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715   1 MISAGDFRNGVTVEIDGNVCQIVEFQHVKPGKGAAFVRTKYKNIITGSVLEKSFRPTEKFPTARIERVDMQYLYNDGGLY 80
Cdd:PRK00529   1 MISANDLRKGLVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGDGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715  81 YFMNVETFDQVGLTEEQVGDSLKFVKENEMVKICSHNGNVFAIEPPLFVELVVTETEPGFAGNTAQGATKPATVETGAQV 160
Cdd:PRK00529  81 VFMDTETYEQIEVPADQVGDAAKFLKEGMEVTVVFYNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLETGAVV 160

                        170       180
                 ....*....|....*....|....*
gi 547184715 161 MVPLFVNQGDKLKIDTRTGEYLSRV 185
Cdd:PRK00529 161 QVPLFINEGEKIKVDTRTGEYVERA 185
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 2-185 2.18e-102

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: 292.06  E-value: 2.18e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715    2 ISAGDFRNGVTVEIDGNVCQIVEFQHVKPGKGAAFVRTKYKNIITGSVLEKSFRPTEKFPTARIERVDMQYLYNDGGLYY 81
Cdd:TIGR00038   1 ISANDLRKGLKIELDGEPYVVLEFEHVKPGKGQAFVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715   82 FMNVETFDQVGLTEEQVGDSLKFVKENEMVKICSHNGNVFAIEPPLFVELVVTETEPGFAGNTAQGATKPATVETGAQVM 161
Cdd:TIGR00038  81 FMDTETYEQIELPKDLLGDAAKFLKENMEVSVVFYNGEPIGVELPNFVELEVTETEPGVKGDTASGSTKPATLETGAVVQ 160

                         170       180
                  ....*....|....*....|....
gi 547184715  162 VPLFVNQGDKLKIDTRTGEYLSRV 185
Cdd:TIGR00038 161 VPLFIEEGEKIKVDTRTGEYVERA 184
PRK14578 PRK14578
elongation factor P; Provisional
 1-184 5.61e-43

elongation factor P; Provisional


Pssm-ID: 173042 [Multi-domain]  Cd Length: 187  Bit Score: 141.90  E-value: 5.61e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715   1 MISAGDFRNGVTVEIDGNVCQIVE--FQHVKPGKGAAFVRTKYKNIITGSVLEKSFRPTEKFPTARIERVDMQYLYNDGG 78
Cdd:PRK14578   1 MYTTSDFKKGLVIQLDGAPCLLLDvtFQSPSARGANTMVKTKYRNLLTGQVLEKTFRSGDKVEEADFERHKGQFLYADGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715  79 LYYFMNVETFDQVGLTEEQVGDSLKFVKENEMVKICSHNGNVFAIEPPLFVELVVTETEPGFAGNTAQGATKPATVETGA 158
Cdd:PRK14578  81 RGVFMDLETYEQFEMEEDAFSAIAPFLLDGTEVQLGLFQGRMVNVDLPMTVELTVTDTAPVMKNATATAQTKEAVLETGL 160

                        170       180
                 ....*....|....*....|....*.
gi 547184715 159 QVMVPLFVNQGDKLKIDTRTGEYLSR 184
Cdd:PRK14578 161 RLQVPPYLESGEKIKVDTRDGRFISR 186
PRK04542 PRK04542
elongation factor P; Provisional
 1-184 2.48e-36

elongation factor P; Provisional


Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 124.69  E-value: 2.48e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715   1 MISAGDFRNGVTVEIDGNVCQIVEFQHVKP-GKGAAfvrTKYK----NIITGSVLEKSFRPTEKFPTARIERVDMQYLYN 75
Cdd:PRK04542   1 MPKANEIKKGMVVEYNGKLLLVKDIDRQSPsGRGGA---TLYKmrfyDVRTGLKVEERFKGDDILDTVDLTRRPVTFSYI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715  76 DGGLYYFMNVETFDQVGLTEEQVGDSLKFVKEN-EMVKICSHNGNVFAIEPPLFVELVVTETEPGFAGNTAQGATKPATV 154
Cdd:PRK04542  78 DGDEYVFMDNEDYTPYTFKKDQIEDELLFIPEGmPGMQVLTVDGQPVALELPQTVDLEIVETAPSIKGASASARTKPATL 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 547184715 155 ETGAQVMVPLFVNQGDKLKIDTRTGEYLSR 184
Cdd:PRK04542 158 STGLVIQVPEYISTGEKIRINTEERKFMGR 187
PRK12426 PRK12426
elongation factor P; Provisional
 1-185 3.69e-35

elongation factor P; Provisional


Pssm-ID: 183522 [Multi-domain]  Cd Length: 185  Bit Score: 121.88  E-value: 3.69e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715   1 MISAGDFRNGVTVEIDGNVCQIVEFQHVKPGKGAAFVRTKYKNIITGSVLEKSFRPTEKFPTARIERVDMQYLYNDGGLY 80
Cdd:PRK12426   1 MVLSSQLSVGMFISTKDGLYKVVSVSKVTGPKGETFIKVSLQAADSDVVVERNFKAGQEVKEAQFEPRNLEYLYLEGDEY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715  81 YFMNVETFDQVGLTEEQVGDSLKFVKENEMVKICSHNGNVFAIEPPLFVELVVTETEPGFAGNTAQGATKPATVETGAQV 160
Cdd:PRK12426  81 LFLDLGNYDKIYIPKEIMKDNFLFLKAGVTVSALVYDGTVFSVELPHFLELMVSKTDFPGDSLSLSGGAKKALLETGVEV 160

                        170       180
                 ....*....|....*....|....*
gi 547184715 161 MVPLFVNQGDKLKIDTRTGEYLSRV 185
Cdd:PRK12426 161 LVPPFVEIGDVIKVDTRTCEYIQRV 185
Elong-fact-P_C pfam09285
Elongation factor P, C-terminal; Members of this family of nucleic acid binding domains are ...
 129-184 1.33e-31

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: 108.62  E-value: 1.33e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 547184715  129 VELVVTETEPGFAGNTAQGATKPATVETGAQVMVPLFVNQGDKLKIDTRTGEYLSR 184
Cdd:pfam09285   1 VELEVTETEPGVKGDTASGATKPATLETGAEVQVPLFINEGDKIKVDTRTGEYVER 56
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 129-184 1.76e-27

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: 97.91  E-value: 1.76e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 547184715   129 VELVVTETEPGFAGNTAQGATK-PATVETGAQVMVPLFVNQGDKLKIDTRTGEYLSR 184
Cdd:smart00841   1 VELEVTETEPGVKGDTASGGTKkPATLETGAVVQVPLFINEGDKIKVDTRTGEYVSR 57
EFP_N pfam08207
Elongation factor P (EF-P) KOW-like domain;
3-60 7.59e-27

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


Pssm-ID: 429864 [Multi-domain]  Cd Length: 58  Bit Score: 96.35  E-value: 7.59e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 547184715    3 SAGDFRNGVTVEIDGNVCQIVEFQHVKPGKGAAFVRTKYKNIITGSVLEKSFRPTEKF 60
Cdd:pfam08207   1 SANELRKGNVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLRTGAKVEKTFKAGDKV 58
S1_EF-P_repeat_2 cd05794
S1_EF-P_repeat_2: Translation elongation factor P (EF-P), S1-like RNA-binding domain, repeat 1. ...
 129-184 2.30e-26

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: 95.28  E-value: 2.30e-26
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 547184715 129 VELVVTETEPGFAGNTAQGATKPATVETGAQVMVPLFVNQGDKLKIDTRTGEYLSR 184
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. ...
 66-126 5.86e-25

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: 91.75  E-value: 5.86e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 547184715  66 ERVDMQYLYNDGGLYYFMNVETFDQVGLTEEQVGDSLKFVKENEMVKICSHNGNVFAIEPP 126
Cdd:cd04470    1 EEREMQYLYKDGDNYVFMDTETYEQIELPKEALGDAAKFLKEGMEVIVLFYNGEPIGVELP 61
EFP pfam01132
Elongation factor P (EF-P) OB domain;
68-120 1.05e-23

Elongation factor P (EF-P) OB domain;


Pssm-ID: 460077 [Multi-domain]  Cd Length: 54  Bit Score: 88.23  E-value: 1.05e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 547184715   68 VDMQYLYNDGGLYYFMNVETFDQVGLTEEQVGDSLKFVKENEMVKICSHNGNV 120
Cdd:pfam01132   1 REMQYLYNDGDDYVFMDNETYEQIELPKEQLGDAAKFLKEGMEVTVLFYEGKP 53
eIF_5A TIGR00037
translation elongation factor IF5A; Recent work (2009) changed the view of eIF5A in eukaryotes ...
 5-102 2.03e-05

translation elongation factor IF5A; Recent work (2009) changed the view of eIF5A in eukaryotes and aIF5A in archaea, hypusine-containing proteins, from translation initiation factor to translation elongation factor. [Protein synthesis, Translation factors]


Pssm-ID: 272866 [Multi-domain]  Cd Length: 130  Bit Score: 42.12  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715    5 GDFRNGVTVEIDGNVCQIVEFQHVKPGK-GAAFVRTKYKNIITGSVLEKSFRPTEKFPTARIERVDMQYLYNDGGLYYFM 83
Cdd:TIGR00037  10 SALRVGGYVVIDGEPCKIVDISTSKPGKhGHAKARVVAIGIFDGQKREFVSPVTSKVEVPIVDRREAQVLAIMGGMVQLM 89

                          90       100
                  ....*....|....*....|
gi 547184715   84 NVETFDQVGL-TEEQVGDSL 102
Cdd:TIGR00037  90 DLETYETFELpIPEELGDSL 109
PRK03999 PRK03999
translation initiation factor IF-5A; Provisional
 5-100 9.02e-03

translation initiation factor IF-5A; Provisional


Pssm-ID: 235193 [Multi-domain]  Cd Length: 129  Bit Score: 34.89  E-value: 9.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547184715   5 GDFRNGVTVEIDGNVCQIVEFQHVKPGK-GAAFVRTKYKNIITGSVLEKSFRPTEKFPTARIERVDMQYLYNDGGLYYFM 83
Cdd:PRK03999   9 GELKEGSYVVIDGEPCKIVEISKSKPGKhGSAKARIVAIGIFDGQKRSLVQPVDAKVEVPIIEKKTGQVLSIMGDVVQLM 88

                         90
                 ....*....|....*....
gi 547184715  84 NVETFD--QVGLTEEQVGD 100
Cdd:PRK03999  89 DLETYEtfEIPIPEELKDK 107
 
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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