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Conserved domains on  [gi|948929662|gb|KRN43533|]
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Elongation factor P [Fructilactobacillus fructivorans]

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, ...
 8-191 3.80e-105

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: 299.63  E-value: 3.80e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662   8 ISIVKVKNGMTIQADNNIWKIVSFQHVKPGKGGAFVRTKLKNLRTGAVQEKTFRASAKVEKANIETKKMQYLYDDGSGLV 87
Cdd:COG0231    2 ISANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGYV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662  88 FMDMDNYEQLTIPREQVKEEMNYLQENMEVQVIQYGGETLGVEVPKTVTLEVSDTEPGIKGDTASGGSKPATMTTGLTLQ 167
Cdd:COG0231   82 FMDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGAVVQ 161

                        170       180
                 ....*....|....*....|....
gi 948929662 168 VPFFVNKGDKLVINTDDGTYISRA 191
Cdd:COG0231  162 VPLFIEEGDKIKVDTRTGEYVERA 185
 
Name Accession Description Interval E-value
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 8-191 3.80e-105

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: 299.63  E-value: 3.80e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662   8 ISIVKVKNGMTIQADNNIWKIVSFQHVKPGKGGAFVRTKLKNLRTGAVQEKTFRASAKVEKANIETKKMQYLYDDGSGLV 87
Cdd:COG0231    2 ISANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGYV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662  88 FMDMDNYEQLTIPREQVKEEMNYLQENMEVQVIQYGGETLGVEVPKTVTLEVSDTEPGIKGDTASGGSKPATMTTGLTLQ 167
Cdd:COG0231   82 FMDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGAVVQ 161

                        170       180
                 ....*....|....*....|....
gi 948929662 168 VPFFVNKGDKLVINTDDGTYISRA 191
Cdd:COG0231  162 VPLFIEEGDKIKVDTRTGEYVERA 185
PRK00529 PRK00529
elongation factor P; Validated
 8-191 1.03e-104

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 298.50  E-value: 1.03e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662   8 ISIVKVKNGMTIQADNNIWKIVSFQHVKPGKGGAFVRTKLKNLRTGAVQEKTFRASAKVEKANIETKKMQYLYDDGSGLV 87
Cdd:PRK00529   2 ISANDLRKGLVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGDGYV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662  88 FMDMDNYEQLTIPREQVKEEMNYLQENMEVQVIQYGGETLGVEVPKTVTLEVSDTEPGIKGDTASGGSKPATMTTGLTLQ 167
Cdd:PRK00529  82 FMDTETYEQIEVPADQVGDAAKFLKEGMEVTVVFYNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLETGAVVQ 161

                        170       180
                 ....*....|....*....|....
gi 948929662 168 VPFFVNKGDKLVINTDDGTYISRA 191
Cdd:PRK00529 162 VPLFINEGEKIKVDTRTGEYVERA 185
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 8-191 4.06e-101

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: 289.36  E-value: 4.06e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662    8 ISIVKVKNGMTIQADNNIWKIVSFQHVKPGKGGAFVRTKLKNLRTGAVQEKTFRASAKVEKANIETKKMQYLYDDGSGLV 87
Cdd:TIGR00038   1 ISANDLRKGLKIELDGEPYVVLEFEHVKPGKGQAFVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662   88 FMDMDNYEQLTIPREQVKEEMNYLQENMEVQVIQYGGETLGVEVPKTVTLEVSDTEPGIKGDTASGGSKPATMTTGLTLQ 167
Cdd:TIGR00038  81 FMDTETYEQIELPKDLLGDAAKFLKENMEVSVVFYNGEPIGVELPNFVELEVTETEPGVKGDTASGSTKPATLETGAVVQ 160

                         170       180
                  ....*....|....*....|....
gi 948929662  168 VPFFVNKGDKLVINTDDGTYISRA 191
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 ...
 135-190 1.15e-27

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: 98.61  E-value: 1.15e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 948929662  135 VTLEVSDTEPGIKGDTASGGSKPATMTTGLTLQVPFFVNKGDKLVINTDDGTYISR 190
Cdd:pfam09285   1 VELEVTETEPGVKGDTASGATKPATLETGAEVQVPLFINEGDKIKVDTRTGEYVER 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. ...
 72-132 9.19e-27

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: 96.37  E-value: 9.19e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 948929662  72 ETKKMQYLYDDGSGLVFMDMDNYEQLTIPREQVKEEMNYLQENMEVQVIQYGGETLGVEVP 132
Cdd:cd04470    1 EEREMQYLYKDGDNYVFMDTETYEQIELPKEALGDAAKFLKEGMEVIVLFYNGEPIGVELP 61
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 135-190 1.18e-24

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: 90.98  E-value: 1.18e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 948929662   135 VTLEVSDTEPGIKGDTASGGSK-PATMTTGLTLQVPFFVNKGDKLVINTDDGTYISR 190
Cdd:smart00841   1 VELEVTETEPGVKGDTASGGTKkPATLETGAVVQVPLFINEGDKIKVDTRTGEYVSR 57
 
Name Accession Description Interval E-value
Efp COG0231
Translation elongation factor P (EF-P)/translation initiation factor 5A (eIF-5A) [Translation, ...
 8-191 3.80e-105

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: 299.63  E-value: 3.80e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662   8 ISIVKVKNGMTIQADNNIWKIVSFQHVKPGKGGAFVRTKLKNLRTGAVQEKTFRASAKVEKANIETKKMQYLYDDGSGLV 87
Cdd:COG0231    2 ISANDLRKGLVIEIDGEPYVVVEFQHVKPGKGGAFVRTKLKNLLTGKVVEKTFKSGDKVEEADLERREMQYLYNDGDGYV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662  88 FMDMDNYEQLTIPREQVKEEMNYLQENMEVQVIQYGGETLGVEVPKTVTLEVSDTEPGIKGDTASGGSKPATMTTGLTLQ 167
Cdd:COG0231   82 FMDTETYEQIELPKEVVGDAAKFLKEGMEVTVLFYNGKPISVELPNFVELEVTETEPGVKGDTATGGTKPATLETGAVVQ 161

                        170       180
                 ....*....|....*....|....
gi 948929662 168 VPFFVNKGDKLVINTDDGTYISRA 191
Cdd:COG0231  162 VPLFIEEGDKIKVDTRTGEYVERA 185
PRK00529 PRK00529
elongation factor P; Validated
 8-191 1.03e-104

elongation factor P; Validated


Pssm-ID: 234788 [Multi-domain]  Cd Length: 186  Bit Score: 298.50  E-value: 1.03e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662   8 ISIVKVKNGMTIQADNNIWKIVSFQHVKPGKGGAFVRTKLKNLRTGAVQEKTFRASAKVEKANIETKKMQYLYDDGSGLV 87
Cdd:PRK00529   2 ISANDLRKGLVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLLTGSVVEKTFKAGDKVERADVERREMQYLYNDGDGYV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662  88 FMDMDNYEQLTIPREQVKEEMNYLQENMEVQVIQYGGETLGVEVPKTVTLEVSDTEPGIKGDTASGGSKPATMTTGLTLQ 167
Cdd:PRK00529  82 FMDTETYEQIEVPADQVGDAAKFLKEGMEVTVVFYNGEPISVELPNFVELEVTETEPGVKGDTASGGTKPATLETGAVVQ 161

                        170       180
                 ....*....|....*....|....
gi 948929662 168 VPFFVNKGDKLVINTDDGTYISRA 191
Cdd:PRK00529 162 VPLFINEGEKIKVDTRTGEYVERA 185
efp TIGR00038
translation elongation factor P; function: involved in peptide bond synthesis. stimulate ...
 8-191 4.06e-101

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: 289.36  E-value: 4.06e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662    8 ISIVKVKNGMTIQADNNIWKIVSFQHVKPGKGGAFVRTKLKNLRTGAVQEKTFRASAKVEKANIETKKMQYLYDDGSGLV 87
Cdd:TIGR00038   1 ISANDLRKGLKIELDGEPYVVLEFEHVKPGKGQAFVRVKLKNLLTGKVLEKTFRSGEKVEKADVEEREMQYLYKDGDSYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662   88 FMDMDNYEQLTIPREQVKEEMNYLQENMEVQVIQYGGETLGVEVPKTVTLEVSDTEPGIKGDTASGGSKPATMTTGLTLQ 167
Cdd:TIGR00038  81 FMDTETYEQIELPKDLLGDAAKFLKENMEVSVVFYNGEPIGVELPNFVELEVTETEPGVKGDTASGSTKPATLETGAVVQ 160

                         170       180
                  ....*....|....*....|....
gi 948929662  168 VPFFVNKGDKLVINTDDGTYISRA 191
Cdd:TIGR00038 161 VPLFIEEGEKIKVDTRTGEYVERA 184
PRK14578 PRK14578
elongation factor P; Provisional
 14-191 4.83e-43

elongation factor P; Provisional


Pssm-ID: 173042 [Multi-domain]  Cd Length: 187  Bit Score: 142.28  E-value: 4.83e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662  14 KNGMTIQADNNIWKI--VSFQHVKPGKGGAFVRTKLKNLRTGAVQEKTFRASAKVEKANIETKKMQYLYDDGSGLVFMDM 91
Cdd:PRK14578   8 KKGLVIQLDGAPCLLldVTFQSPSARGANTMVKTKYRNLLTGQVLEKTFRSGDKVEEADFERHKGQFLYADGDRGVFMDL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662  92 DNYEQLTIPREQVKEEMNYLQENMEVQVIQYGGETLGVEVPKTVTLEVSDTEPGIKGDTASGGSKPATMTTGLTLQVPFF 171
Cdd:PRK14578  88 ETYEQFEMEEDAFSAIAPFLLDGTEVQLGLFQGRMVNVDLPMTVELTVTDTAPVMKNATATAQTKEAVLETGLRLQVPPY 167

                        170       180
                 ....*....|....*....|
gi 948929662 172 VNKGDKLVINTDDGTYISRA 191
Cdd:PRK14578 168 LESGEKIKVDTRDGRFISRA 187
PRK04542 PRK04542
elongation factor P; Provisional
 13-191 1.22e-41

elongation factor P; Provisional


Pssm-ID: 179863 [Multi-domain]  Cd Length: 189  Bit Score: 138.56  E-value: 1.22e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662  13 VKNGMTIQADNNIWKIVSFQHVKP-GKGGAFV-RTKLKNLRTGAVQEKTFRASAKVEKANIETKKMQYLYDDGSGLVFMD 90
Cdd:PRK04542   7 IKKGMVVEYNGKLLLVKDIDRQSPsGRGGATLyKMRFYDVRTGLKVEERFKGDDILDTVDLTRRPVTFSYIDGDEYVFMD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662  91 MDNYEQLTIPREQVKEEMNYLQENME-VQVIQYGGETLGVEVPKTVTLEVSDTEPGIKGDTASGGSKPATMTTGLTLQVP 169
Cdd:PRK04542  87 NEDYTPYTFKKDQIEDELLFIPEGMPgMQVLTVDGQPVALELPQTVDLEIVETAPSIKGASASARTKPATLSTGLVIQVP 166

                        170       180
                 ....*....|....*....|..
gi 948929662 170 FFVNKGDKLVINTDDGTYISRA 191
Cdd:PRK04542 167 EYISTGEKIRINTEERKFMGRA 188
PRK12426 PRK12426
elongation factor P; Provisional
 16-190 1.10e-36

elongation factor P; Provisional


Pssm-ID: 183522 [Multi-domain]  Cd Length: 185  Bit Score: 125.73  E-value: 1.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662  16 GMTIQADNNIWKIVSFQHVKPGKGGAFVRTKLKNLRTGAVQEKTFRASAKVEKANIETKKMQYLYDDGSGLVFMDMDNYE 95
Cdd:PRK12426  10 GMFISTKDGLYKVVSVSKVTGPKGETFIKVSLQAADSDVVVERNFKAGQEVKEAQFEPRNLEYLYLEGDEYLFLDLGNYD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662  96 QLTIPREQVKEEMNYLQENMEVQVIQYGGETLGVEVPKTVTLEVSDTEPGIKGDTASGGSKPATMTTGLTLQVPFFVNKG 175
Cdd:PRK12426  90 KIYIPKEIMKDNFLFLKAGVTVSALVYDGTVFSVELPHFLELMVSKTDFPGDSLSLSGGAKKALLETGVEVLVPPFVEIG 169

                        170
                 ....*....|....*
gi 948929662 176 DKLVINTDDGTYISR 190
Cdd:PRK12426 170 DVIKVDTRTCEYIQR 184
Elong-fact-P_C pfam09285
Elongation factor P, C-terminal; Members of this family of nucleic acid binding domains are ...
 135-190 1.15e-27

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: 98.61  E-value: 1.15e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 948929662  135 VTLEVSDTEPGIKGDTASGGSKPATMTTGLTLQVPFFVNKGDKLVINTDDGTYISR 190
Cdd:pfam09285   1 VELEVTETEPGVKGDTASGATKPATLETGAEVQVPLFINEGDKIKVDTRTGEYVER 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. ...
 72-132 9.19e-27

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: 96.37  E-value: 9.19e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 948929662  72 ETKKMQYLYDDGSGLVFMDMDNYEQLTIPREQVKEEMNYLQENMEVQVIQYGGETLGVEVP 132
Cdd:cd04470    1 EEREMQYLYKDGDNYVFMDTETYEQIELPKEALGDAAKFLKEGMEVIVLFYNGEPIGVELP 61
Elong-fact-P_C smart00841
Elongation factor P, C-terminal; These nucleic acid binding domains are predominantly found in ...
 135-190 1.18e-24

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: 90.98  E-value: 1.18e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 948929662   135 VTLEVSDTEPGIKGDTASGGSK-PATMTTGLTLQVPFFVNKGDKLVINTDDGTYISR 190
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. ...
 135-190 2.19e-24

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: 90.28  E-value: 2.19e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 948929662 135 VTLEVSDTEPGIKGDTASGGSKPATMTTGLTLQVPFFVNKGDKLVINTDDGTYISR 190
Cdd:cd05794    1 VELEVTETEPGVKGDTASSGTKPATLETGAEVQVPLFIKEGEKIKVDTRTGEYVER 56
EFP pfam01132
Elongation factor P (EF-P) OB domain;
74-127 3.04e-23

Elongation factor P (EF-P) OB domain;


Pssm-ID: 460077 [Multi-domain]  Cd Length: 54  Bit Score: 87.07  E-value: 3.04e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 948929662   74 KKMQYLYDDGSGLVFMDMDNYEQLTIPREQVKEEMNYLQENMEVQVIQYGGETL 127
Cdd:pfam01132   1 REMQYLYNDGDDYVFMDNETYEQIELPKEQLGDAAKFLKEGMEVTVLFYEGKPI 54
EFP_N pfam08207
Elongation factor P (EF-P) KOW-like domain;
13-66 5.95e-23

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


Pssm-ID: 429864 [Multi-domain]  Cd Length: 58  Bit Score: 86.72  E-value: 5.95e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 948929662   13 VKNGMTIQADNNIWKIVSFQHVKPGKGGAFVRTKLKNLRTGAVQEKTFRASAKV 66
Cdd:pfam08207   5 LRKGNVIEIDGEPYVVLEFEHVKPGKGQAFVRTKLKNLRTGAKVEKTFKAGDKV 58
PRK03999 PRK03999
translation initiation factor IF-5A; Provisional
 3-124 2.11e-08

translation initiation factor IF-5A; Provisional


Pssm-ID: 235193 [Multi-domain]  Cd Length: 129  Bit Score: 50.68  E-value: 2.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929662   3 GMKMSISIVKVKNGMTIQADNNIWKIVSFQHVKPGK-GGAFVRTKLKNLRTGAVQEKTFRASAKVEKANIETKKMQYLYD 81
Cdd:PRK03999   1 MSKKQVEVGELKEGSYVVIDGEPCKIVEISKSKPGKhGSAKARIVAIGIFDGQKRSLVQPVDAKVEVPIIEKKTGQVLSI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 948929662  82 DGSGLVFMDMDNYEQLTIPR-EQVKEEmnyLQENMEVQVIQYGG 124
Cdd:PRK03999  81 MGDVVQLMDLETYETFEIPIpEELKDK---LEPGVEVEYWEAMG 121
 
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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