NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|495237896|ref|WP_007962665|]
View 

MULTISPECIES: elongation factor P [Xanthomonas]

Protein Classification

elongation factor P( domain architecture ID 11478847)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK00529 PRK00529
elongation factor P; Validated
 3-188 1.67e-92

elongation factor P; Validated


:

Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 267.30  E-value: 1.67e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495237896   3 TVGMNDVKNGMKILVNNEPAVITETEYVKPGKGQAFTRMKYRFIKSGRVVEMTMKATDDVEVADVVDTDMRYLYSDGEYW 82
Cdd:PRK00529   1 MISANDLRKGLVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGDGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495237896  83 HFMDPETFEQVQTDKAGMGGADKWLKGEEDCIVTLWNGTPIWVQPPNFVELKITETDPGVRGDTSGGGGKPATLETGAVV 162
Cdd:PRK00529  81 VFMDTETYEQIEVPADQVGDAAKFLKEGMEVTVVFYNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLETGAVV 160

                        170       180
                 ....*....|....*....|....*.
gi 495237896 163 RVPLFVNQDEIIKVDTRSGEYSARVK 188
Cdd:PRK00529 161 QVPLFINEGEKIKVDTRTGEYVERAK 186
 
Name Accession Description Interval E-value
PRK00529 PRK00529
elongation factor P; Validated
 3-188 1.67e-92

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 267.30  E-value: 1.67e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495237896   3 TVGMNDVKNGMKILVNNEPAVITETEYVKPGKGQAFTRMKYRFIKSGRVVEMTMKATDDVEVADVVDTDMRYLYSDGEYW 82
Cdd:PRK00529   1 MISANDLRKGLVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGDGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495237896  83 HFMDPETFEQVQTDKAGMGGADKWLKGEEDCIVTLWNGTPIWVQPPNFVELKITETDPGVRGDTSGGGGKPATLETGAVV 162
Cdd:PRK00529  81 VFMDTETYEQIEVPADQVGDAAKFLKEGMEVTVVFYNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLETGAVV 160

                        170       180
                 ....*....|....*....|....*.
gi 495237896 163 RVPLFVNQDEIIKVDTRSGEYSARVK 188
Cdd:PRK00529 161 QVPLFINEGEKIKVDTRTGEYVERAK 186
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 1-188 9.30e-92

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: 265.35  E-value: 9.30e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495237896   1 MATVgmNDVKNGMKILVNNEPAVITETEYVKPGKGQAFTRMKYRFIKSGRVVEMTMKATDDVEVADVVDTDMRYLYSDGE 80
Cdd:COG0231    1 MISA--NDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495237896  81 YWHFMDPETFEQVQTDKAGMGGADKWLKGEEDCIVTLWNGTPIWVQPPNFVELKITETDPGVRGDTSGGGGKPATLETGA 160
Cdd:COG0231   79 GYVFMDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGA 158

                        170       180
                 ....*....|....*....|....*...
gi 495237896 161 VVRVPLFVNQDEIIKVDTRSGEYSARVK 188
Cdd:COG0231  159 VVQVPLFIEEGDKIKVDTRTGEYVERAK 186
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 4-187 1.07e-91

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: 265.48  E-value: 1.07e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495237896    4 VGMNDVKNGMKILVNNEPAVITETEYVKPGKGQAFTRMKYRFIKSGRVVEMTMKATDDVEVADVVDTDMRYLYSDGEYWH 83
Cdd:TIGR00038   1 ISANDLRKGLKIELDGEPYVVLEFEHVKPGKGQAFVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495237896   84 FMDPETFEQVQTDKAGMGGADKWLKGEEDCIVTLWNGTPIWVQPPNFVELKITETDPGVRGDTSGGGGKPATLETGAVVR 163
Cdd:TIGR00038  81 FMDTETYEQIELPKDLLGDAAKFLKENMEVSVVFYNGEPIGVELPNFVELEVTETEPGVKGDTASGSTKPATLETGAVVQ 160

                         170       180
                  ....*....|....*....|....
gi 495237896  164 VPLFVNQDEIIKVDTRSGEYSARV 187
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 ...
 131-186 1.51e-29

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: 103.23  E-value: 1.51e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 495237896  131 VELKITETDPGVRGDTSGGGGKPATLETGAVVRVPLFVNQDEIIKVDTRSGEYSAR 186
Cdd:pfam09285   1 VELEVTETEPGVKGDTASGATKPATLETGAEVQVPLFINEGDKIKVDTRTGEYVER 56
S1_EF-P_repeat_2 cd05794
S1_EF-P_repeat_2: Translation elongation factor P (EF-P), S1-like RNA-binding domain, repeat 1. ...
 131-186 6.15e-27

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: 96.82  E-value: 6.15e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495237896 131 VELKITETDPGVRGDTSGGGGKPATLETGAVVRVPLFVNQDEIIKVDTRSGEYSAR 186
Cdd:cd05794    1 VELEVTETEPGVKGDTASSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 56
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 131-186 2.68e-26

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: 95.22  E-value: 2.68e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 495237896   131 VELKITETDPGVRGDTSGGGGK-PATLETGAVVRVPLFVNQDEIIKVDTRSGEYSAR 186
Cdd:smart00841   1 VELEVTETEPGVKGDTASGGTKkPATLETGAVVQVPLFINEGDKIKVDTRTGEYVSR 57
 
Name Accession Description Interval E-value
PRK00529 PRK00529
elongation factor P; Validated
 3-188 1.67e-92

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 267.30  E-value: 1.67e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495237896   3 TVGMNDVKNGMKILVNNEPAVITETEYVKPGKGQAFTRMKYRFIKSGRVVEMTMKATDDVEVADVVDTDMRYLYSDGEYW 82
Cdd:PRK00529   1 MISANDLRKGLVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGDGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495237896  83 HFMDPETFEQVQTDKAGMGGADKWLKGEEDCIVTLWNGTPIWVQPPNFVELKITETDPGVRGDTSGGGGKPATLETGAVV 162
Cdd:PRK00529  81 VFMDTETYEQIEVPADQVGDAAKFLKEGMEVTVVFYNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLETGAVV 160

                        170       180
                 ....*....|....*....|....*.
gi 495237896 163 RVPLFVNQDEIIKVDTRSGEYSARVK 188
Cdd:PRK00529 161 QVPLFINEGEKIKVDTRTGEYVERAK 186
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 1-188 9.30e-92

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: 265.35  E-value: 9.30e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495237896   1 MATVgmNDVKNGMKILVNNEPAVITETEYVKPGKGQAFTRMKYRFIKSGRVVEMTMKATDDVEVADVVDTDMRYLYSDGE 80
Cdd:COG0231    1 MISA--NDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495237896  81 YWHFMDPETFEQVQTDKAGMGGADKWLKGEEDCIVTLWNGTPIWVQPPNFVELKITETDPGVRGDTSGGGGKPATLETGA 160
Cdd:COG0231   79 GYVFMDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGA 158

                        170       180
                 ....*....|....*....|....*...
gi 495237896 161 VVRVPLFVNQDEIIKVDTRSGEYSARVK 188
Cdd:COG0231  159 VVQVPLFIEEGDKIKVDTRTGEYVERAK 186
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 4-187 1.07e-91

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: 265.48  E-value: 1.07e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495237896    4 VGMNDVKNGMKILVNNEPAVITETEYVKPGKGQAFTRMKYRFIKSGRVVEMTMKATDDVEVADVVDTDMRYLYSDGEYWH 83
Cdd:TIGR00038   1 ISANDLRKGLKIELDGEPYVVLEFEHVKPGKGQAFVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495237896   84 FMDPETFEQVQTDKAGMGGADKWLKGEEDCIVTLWNGTPIWVQPPNFVELKITETDPGVRGDTSGGGGKPATLETGAVVR 163
Cdd:TIGR00038  81 FMDTETYEQIELPKDLLGDAAKFLKENMEVSVVFYNGEPIGVELPNFVELEVTETEPGVKGDTASGSTKPATLETGAVVQ 160

                         170       180
                  ....*....|....*....|....
gi 495237896  164 VPLFVNQDEIIKVDTRSGEYSARV 187
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 ...
 131-186 1.51e-29

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: 103.23  E-value: 1.51e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 495237896  131 VELKITETDPGVRGDTSGGGGKPATLETGAVVRVPLFVNQDEIIKVDTRSGEYSAR 186
Cdd:pfam09285   1 VELEVTETEPGVKGDTASGATKPATLETGAEVQVPLFINEGDKIKVDTRTGEYVER 56
S1_EF-P_repeat_2 cd05794
S1_EF-P_repeat_2: Translation elongation factor P (EF-P), S1-like RNA-binding domain, repeat 1. ...
 131-186 6.15e-27

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: 96.82  E-value: 6.15e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495237896 131 VELKITETDPGVRGDTSGGGGKPATLETGAVVRVPLFVNQDEIIKVDTRSGEYSAR 186
Cdd:cd05794    1 VELEVTETEPGVKGDTASSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 56
PRK04542 PRK04542
elongation factor P; Provisional
 7-186 8.89e-27

elongation factor P; Provisional


Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 100.42  E-value: 8.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495237896   7 NDVKNGMKILVNNEPAVITETEYVKPGKGQAFTRMKYRF--IKSGRVVEMTMKATDDVEVADVVDTDMRYLYSDGEYWHF 84
Cdd:PRK04542   5 NEIKKGMVVEYNGKLLLVKDIDRQSPSGRGGATLYKMRFydVRTGLKVEERFKGDDILDTVDLTRRPVTFSYIDGDEYVF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495237896  85 MDPETFEQVQTDKAGMGGADKWL-KGEEDCIVTLWNGTPIWVQPPNFVELKITETDPGVRGDTSGGGGKPATLETGAVVR 163
Cdd:PRK04542  85 MDNEDYTPYTFKKDQIEDELLFIpEGMPGMQVLTVDGQPVALELPQTVDLEIVETAPSIKGASASARTKPATLSTGLVIQ 164

                        170       180
                 ....*....|....*....|...
gi 495237896 164 VPLFVNQDEIIKVDTRSGEYSAR 186
Cdd:PRK04542 165 VPEYISTGEKIRINTEERKFMGR 187
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 131-186 2.68e-26

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: 95.22  E-value: 2.68e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 495237896   131 VELKITETDPGVRGDTSGGGGK-PATLETGAVVRVPLFVNQDEIIKVDTRSGEYSAR 186
Cdd:smart00841   1 VELEVTETEPGVKGDTASGGTKkPATLETGAVVQVPLFINEGDKIKVDTRTGEYVSR 57
PRK14578 PRK14578
elongation factor P; Provisional
 1-186 5.75e-25

elongation factor P; Provisional


Pssm-ID: 173042 [Multi-domain]  Cd Length: 187  Bit Score: 95.67  E-value: 5.75e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495237896   1 MATVgmNDVKNGMKILVNNEPAVITETEYVKPGKGQAFT--RMKYRFIKSGRVVEMTMKATDDVEVADVVDTDMRYLYSD 78
Cdd:PRK14578   1 MYTT--SDFKKGLVIQLDGAPCLLLDVTFQSPSARGANTmvKTKYRNLLTGQVLEKTFRSGDKVEEADFERHKGQFLYAD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495237896  79 GEYWHFMDPETFEQVQTDKAGMGGADKWLKGEEDCIVTLWNGTPIWVQPPNFVELKITETDPGVRGDTSGGGGKPATLET 158
Cdd:PRK14578  79 GDRGVFMDLETYEQFEMEEDAFSAIAPFLLDGTEVQLGLFQGRMVNVDLPMTVELTVTDTAPVMKNATATAQTKEAVLET 158

                        170       180
                 ....*....|....*....|....*...
gi 495237896 159 GAVVRVPLFVNQDEIIKVDTRSGEYSAR 186
Cdd:PRK14578 159 GLRLQVPPYLESGEKIKVDTRDGRFISR 186
S1_EF-P_repeat_1 cd04470
S1_EF-P_repeat_1: Translation elongation factor P (EF-P), S1-like RNA-binding domain, repeat 1. ...
 72-128 7.36e-24

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: 89.05  E-value: 7.36e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495237896  72 MRYLYSDGEYWHFMDPETFEQVQTDKAGMGGADKWLKGEEDCIVTLWNGTPIWVQPP 128
Cdd:cd04470    5 MQYLYKDGDNYVFMDTETYEQIELPKEALGDAAKFLKEGMEVIVLFYNGEPIGVELP 61
PRK12426 PRK12426
elongation factor P; Provisional
 7-187 1.06e-22

elongation factor P; Provisional


Pssm-ID: 183522 [Multi-domain]  Cd Length: 185  Bit Score: 89.52  E-value: 1.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495237896   7 NDVKNGMKILVNNEPAVITETEYVKPGKGQAFTRMKYRFIKSGRVVEMTMKATDDVEVADVVDTDMRYLYSDGEYWHFMD 86
Cdd:PRK12426   5 SQLSVGMFISTKDGLYKVVSVSKVTGPKGETFIKVSLQAADSDVVVERNFKAGQEVKEAQFEPRNLEYLYLEGDEYLFLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495237896  87 PETFEQVQTDKAGMGGADKWLKGEEDCIVTLWNGTPIWVQPPNFVELKITETD-PGVRGDTSgGGGKPATLETGAVVRVP 165
Cdd:PRK12426  85 LGNYDKIYIPKEIMKDNFLFLKAGVTVSALVYDGTVFSVELPHFLELMVSKTDfPGDSLSLS-GGAKKALLETGVEVLVP 163

                        170       180
                 ....*....|....*....|..
gi 495237896 166 LFVNQDEIIKVDTRSGEYSARV 187
Cdd:PRK12426 164 PFVEIGDVIKVDTRTCEYIQRV 185
EFP pfam01132
Elongation factor P (EF-P) OB domain;
72-123 1.71e-19

Elongation factor P (EF-P) OB domain;


Pssm-ID: 460077 [Multi-domain]  Cd Length: 54  Bit Score: 77.44  E-value: 1.71e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 495237896   72 MRYLYSDGEYWHFMDPETFEQVQTDKAGMGGADKWLKGEEDCIVTLWNGTPI 123
Cdd:pfam01132   3 MQYLYNDGDDYVFMDNETYEQIELPKEQLGDAAKFLKEGMEVTVLFYEGKPI 54
EFP_N pfam08207
Elongation factor P (EF-P) KOW-like domain;
6-58 4.29e-18

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


Pssm-ID: 429864 [Multi-domain]  Cd Length: 58  Bit Score: 74.00  E-value: 4.29e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 495237896    6 MNDVKNGMKILVNNEPAVITETEYVKPGKGQAFTRMKYRFIKSGRVVEMTMKA 58
Cdd:pfam08207   2 ANELRKGNVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLRTGAKVEKTFKA 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