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Conserved domains on  [gi|154758281|emb|CAO82546|]
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Elongation Factor 2, partial [Halorubrum sp. TP312]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13351 super family cl46912
elongation factor G-like protein;
1-167 3.06e-104

elongation factor G-like protein;


The actual alignment was detected with superfamily member PRK07560:

Pssm-ID: 481252 [Multi-domain]  Cd Length: 731  Bit Score: 314.11  E-value: 3.06e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154758281   1 GVSMPSMQRTGMDFGDIMELEQNDKRQELHERTPLSDVVLDMVCEHFPNPVDAQPRRVPRIWRGDPESDLADTMRLVDED 80
Cdd:PRK07560 209 AISVPMMQKTGIKFKDIIDYYEKGKQKELAEKAPLHEVVLDMVVKHLPNPIEAQKYRIPKIWKGDLNSEVGKAMLNCDPN 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154758281  81 GEVVFMVTDISMDPHAGEIATGRVFSGTLEKGQELYVSGTAGKNRIQSVGLFMGSEREEVDRVPAGNIASVTGLRDAIAG 160
Cdd:PRK07560 289 GPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKNRVQQVGIYMGPEREEVEEIPAGNIAAVTGLKDARAG 368


                 ....*..
gi 154758281 161 STVSSVE 167
Cdd:PRK07560 369 ETVVSVE 375
 
Name Accession Description Interval E-value
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 1-167 3.06e-104

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 314.11  E-value: 3.06e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154758281   1 GVSMPSMQRTGMDFGDIMELEQNDKRQELHERTPLSDVVLDMVCEHFPNPVDAQPRRVPRIWRGDPESDLADTMRLVDED 80
Cdd:PRK07560 209 AISVPMMQKTGIKFKDIIDYYEKGKQKELAEKAPLHEVVLDMVVKHLPNPIEAQKYRIPKIWKGDLNSEVGKAMLNCDPN 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154758281  81 GEVVFMVTDISMDPHAGEIATGRVFSGTLEKGQELYVSGTAGKNRIQSVGLFMGSEREEVDRVPAGNIASVTGLRDAIAG 160
Cdd:PRK07560 289 GPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKNRVQQVGIYMGPEREEVEEIPAGNIAAVTGLKDARAG 368


                 ....*..
gi 154758281 161 STVSSVE 167
Cdd:PRK07560 369 ETVVSVE 375
EF2_II cd16268
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ...
 82-165 6.20e-30

Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 (EF-2) found in eukaryotes and archaea. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. This translocation step is catalyzed by EF-2_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site.


Pssm-ID: 293913 [Multi-domain]  Cd Length: 96  Bit Score: 104.99  E-value: 6.20e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154758281  82 EVVFMVTDI-SMDPHAGEIATGRVFSGTLEKGQELYVSG---------TAGKNRIQSVGLFMGSEREEVDRVPAGNIASV 151
Cdd:cd16268    1 PLVMYVSKMvPTDKGAGFVAFGRVFSGTVRRGQEVYILGpkyvpgkkdDLKKKRIQQTYLMMGREREPVDEVPAGNIVGL 80

                         90
                 ....*....|....*.
gi 154758281 152 TGLRD--AIAGSTVSS 165
Cdd:cd16268   81 VGLDDflAKSGTTTSS 96
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 39-165 2.05e-19

Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440248 [Multi-domain]  Cd Length: 693  Bit Score: 84.33  E-value: 2.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154758281  39 VLDMVCEHFPNPVDAQPRRvpriwrGDPESDLADTMRLVDEDGEVVFMVTDISMDPHAGEIATGRVFSGTLEKGQELYVS 118
Cdd:COG0480  269 LLDAVVDYLPSPLDVPAIK------GVDPDTGEEVERKPDDDEPFSALVFKTMTDPFVGKLSFFRVYSGTLKSGSTVYNS 342

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 154758281 119 GTAGKNRIQSVGLFMGSEREEVDRVPAGNIASVTGLRDAIAGSTVSS 165
Cdd:COG0480  343 TKGKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCD 389
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 97-164 1.61e-13

Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 61.90  E-value: 1.61e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154758281   97 GEIATGRVFSGTLEKGQELYV--SGTAGKN---RIQSVGLFMGSEREEVDRVPAGNIASVTGLRDAIAGSTVS 164
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRIlpNGTGKKKivtRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
 
Name Accession Description Interval E-value
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 1-167 3.06e-104

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 314.11  E-value: 3.06e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154758281   1 GVSMPSMQRTGMDFGDIMELEQNDKRQELHERTPLSDVVLDMVCEHFPNPVDAQPRRVPRIWRGDPESDLADTMRLVDED 80
Cdd:PRK07560 209 AISVPMMQKTGIKFKDIIDYYEKGKQKELAEKAPLHEVVLDMVVKHLPNPIEAQKYRIPKIWKGDLNSEVGKAMLNCDPN 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154758281  81 GEVVFMVTDISMDPHAGEIATGRVFSGTLEKGQELYVSGTAGKNRIQSVGLFMGSEREEVDRVPAGNIASVTGLRDAIAG 160
Cdd:PRK07560 289 GPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKNRVQQVGIYMGPEREEVEEIPAGNIAAVTGLKDARAG 368


                 ....*..
gi 154758281 161 STVSSVE 167
Cdd:PRK07560 369 ETVVSVE 375
EF2_II cd16268
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ...
 82-165 6.20e-30

Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 (EF-2) found in eukaryotes and archaea. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. This translocation step is catalyzed by EF-2_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site.


Pssm-ID: 293913 [Multi-domain]  Cd Length: 96  Bit Score: 104.99  E-value: 6.20e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154758281  82 EVVFMVTDI-SMDPHAGEIATGRVFSGTLEKGQELYVSG---------TAGKNRIQSVGLFMGSEREEVDRVPAGNIASV 151
Cdd:cd16268    1 PLVMYVSKMvPTDKGAGFVAFGRVFSGTVRRGQEVYILGpkyvpgkkdDLKKKRIQQTYLMMGREREPVDEVPAGNIVGL 80

                         90
                 ....*....|....*.
gi 154758281 152 TGLRD--AIAGSTVSS 165
Cdd:cd16268   81 VGLDDflAKSGTTTSS 96
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
39-165 4.12e-20

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 86.33  E-value: 4.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154758281  39 VLDMVCEHFPNPVDAQPRrvpriwrgDPESDLADTMRLVDEDGEVVFMVTDISMDPHAGEIATGRVFSGTLEKGQELYVS 118
Cdd:PRK12740 253 LLDAVVDYLPSPLEVPPV--------DGEDGEEGAELAPDPDGPLVALVFKTMDDPFVGKLSLVRVYSGTLKKGDTLYNS 324

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 154758281 119 GTAGKNRIQSVGLFMGSEREEVDRVPAGNIASVTGLRDAIAGSTVSS 165
Cdd:PRK12740 325 GTGKKERVGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCD 371
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 39-165 2.05e-19

Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440248 [Multi-domain]  Cd Length: 693  Bit Score: 84.33  E-value: 2.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154758281  39 VLDMVCEHFPNPVDAQPRRvpriwrGDPESDLADTMRLVDEDGEVVFMVTDISMDPHAGEIATGRVFSGTLEKGQELYVS 118
Cdd:COG0480  269 LLDAVVDYLPSPLDVPAIK------GVDPDTGEEVERKPDDDEPFSALVFKTMTDPFVGKLSFFRVYSGTLKSGSTVYNS 342

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 154758281 119 GTAGKNRIQSVGLFMGSEREEVDRVPAGNIASVTGLRDAIAGSTVSS 165
Cdd:COG0480  343 TKGKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCD 389
EFG_mtEFG_II cd04088
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ...
 90-164 1.79e-17

Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation factors G1 and G2; This family represents the domain II of bacterial Elongation factor G (EF-G)and mitochondrial Elongation factors G1 (mtEFG1) and G2 (mtEFG2). During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. mtEFG1 and mtEFG2 show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants in the yeast homolog of mtEFG2, MEF2.


Pssm-ID: 293905 [Multi-domain]  Cd Length: 83  Bit Score: 72.55  E-value: 1.79e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 154758281  90 ISMDPHAGEIATGRVFSGTLEKGQELYVSGTAGKNRIQSVgLFM-GSEREEVDRVPAGNIASVTGLRDAIAGSTVS 164
Cdd:cd04088    8 TMADPFVGKLTFFRVYSGTLKSGSTVYNSTKGKKERVGRL-LRMhGKKREEVEELGAGDIGAVVGLKDTRTGDTLC 82
PTZ00416 PTZ00416
elongation factor 2; Provisional
 18-167 1.67e-16

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 75.86  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154758281  18 MELEQNDK---RQELHERT-----PLSDVVLDMVCEHFPNPVDAQPRRVPRIWRGDPESDLADTMRLVDEDGEVVFMVTd 89
Cdd:PTZ00416 299 ISLTGEDKeltGKPLLKAVmqkwlPAADTLLEMIVDHLPSPKEAQKYRVENLYEGPMDDEAANAIRNCDPNGPLMMYIS- 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154758281  90 iSMDPHAGE---IATGRVFSGTLEKGQEL------YVSGTAG----KNrIQSVGLFMGSEREEVDRVPAGNIASVTGLRD 156
Cdd:PTZ00416 378 -KMVPTSDKgrfYAFGRVFSGTVATGQKVriqgpnYVPGKKEdlfeKN-IQRTVLMMGRYVEQIEDVPCGNTVGLVGVDQ 455

                        170
                 ....*....|..
gi 154758281 157 AIAGS-TVSSVE 167
Cdd:PTZ00416 456 YLVKSgTITTSE 467
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
 34-154 2.14e-15

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 72.83  E-value: 2.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154758281  34 PLSDVVLDMVCEHFPNPVDAQPRRVPRIWRGDPESDLADTMRLVDEDGEVVFMVTdiSMDPHAGE---IATGRVFSGTLE 110
Cdd:PLN00116 327 PASDALLEMIIFHLPSPAKAQRYRVENLYEGPLDDKYATAIRNCDPNGPLMLYVS--KMIPASDKgrfFAFGRVFSGTVA 404

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 154758281 111 KGQELYVSGTA---GKNR------IQSVGLFMGSEREEVDRVPAGNIASVTGL 154
Cdd:PLN00116 405 TGMKVRIMGPNyvpGEKKdlyvksVQRTVIWMGKKQESVEDVPCGNTVAMVGL 457
BipA_TypA_II cd03691
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ...
 85-167 1.59e-14

Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.


Pssm-ID: 293892 [Multi-domain]  Cd Length: 94  Bit Score: 65.29  E-value: 1.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154758281  85 FMVTDISMDPHAGEIATGRVFSGTLEKGQELYV---SGTAGKNRIQSVGLFMGSEREEVDRVPAGNIASVTGLRDAIAGS 161
Cdd:cd03691    3 MLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVTVvdeDGKIEKGRVTKLFGFEGLERVEVEEAEAGDIVAIAGLEDITIGD 82


                 ....*.
gi 154758281 162 TVSSVE 167
Cdd:cd03691   83 TICDPE 88
PRK13351 PRK13351
elongation factor G-like protein;
39-165 1.23e-13

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 67.67  E-value: 1.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154758281  39 VLDMVCEHFPNPVDAQPRRvpriwrGDPESDLADTMRLvDEDGEVVFMVTDISMDPHAGEIATGRVFSGTLEKGQELYVS 118
Cdd:PRK13351 269 LLDAVVDYLPSPLEVPPPR------GSKDNGKPVKVDP-DPEKPLLALVFKVQYDPYAGKLTYLRVYSGTLRAGSQLYNG 341

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 154758281 119 GTAGKNRIQSVGLFMGSEREEVDRVPAGNIASVTGLRDAIAGSTVSS 165
Cdd:PRK13351 342 TGGKREKVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLHD 388
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 97-164 1.61e-13

Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 61.90  E-value: 1.61e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154758281   97 GEIATGRVFSGTLEKGQELYV--SGTAGKN---RIQSVGLFMGSEREEVDRVPAGNIASVTGLRDAIAGSTVS 164
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRIlpNGTGKKKivtRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 93-164 2.75e-09

Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.


Pssm-ID: 293888 [Multi-domain]  Cd Length: 80  Bit Score: 51.11  E-value: 2.75e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 154758281  93 DPHAGEIATGRVFSGTLEKGQELYVSGTAGKNRIQSVGLFMgserEEVDRVPAGNI--ASVTGLRDAIAGSTVS 164
Cdd:cd01342   11 IPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFH----EEVDEAKAGDIvgIGILGVKDILTGDTLT 80
EF2_snRNP_like_II cd03700
Domain II of elongation factor 2 and C-terminal domain of the spliceosomal human 116kD U5 ...
 100-154 2.00e-08

Domain II of elongation factor 2 and C-terminal domain of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein; This subfamily represents domain II of elongation factor (EF) EF-2 found in eukaryotes and archaea, and the C-terminal portion of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and its yeast counterpart Snu114p. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. This translocation step is catalyzed by EF-2_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Yeast Snu114p is essential for cell viability and for splicing in vivo. U5-116 kD binds GTP. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of U5-116 kD/Snu114p.


Pssm-ID: 293901 [Multi-domain]  Cd Length: 95  Bit Score: 49.53  E-value: 2.00e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 154758281 100 ATGRVFSGTLEKGQELYVSG---TAGKN------RIQSVGLFMGSEREEVDRVPAGNIASVTGL 154
Cdd:cd03700   19 AFGRVFAGTVHAGQKVRILGpnyTPGKKedlrikAIQRLWLMMGRYVEEINDVPAGNIVGLVGI 82
mtEFG2_II_like cd04092
Domain II of mitochondrial elongation factor G2-like proteins found in eukaryotes; Eukaryotic ...
 93-165 2.39e-07

Domain II of mitochondrial elongation factor G2-like proteins found in eukaryotes; Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. No clear phenotype has been found for mutants in the yeast homolog of mtEFG2, MEF2. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s); mtEFG1s are not present in this group.


Pssm-ID: 293909 [Multi-domain]  Cd Length: 83  Bit Score: 46.16  E-value: 2.39e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154758281  93 DPHAGEIATGRVFSGTLEKGQELYVSGTAGKNRIQSVGLFMGSEREEVDRVPAGNIASVTGLRDAIAGSTVSS 165
Cdd:cd04092   11 DPQRGPLVFVRVYSGTLKAGSNVYNTTTGKKERISRLLKMHADQTEEVDSLSAGNIGVITGLKVTSTGDTLVS 83
EF2_II_snRNP cd04090
Domain II of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component; This ...
 83-165 4.21e-07

Domain II of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component; This subfamily includes domain II of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and its yeast counterpart Snu114p. This domain is homologous to domain II of the eukaryotic translational elongation factor EF-2. U5-116 kD is a GTPase which is a component of the spliceosome complex which processes precursor mRNAs to produce mature mRNAs.


Pssm-ID: 293907 [Multi-domain]  Cd Length: 94  Bit Score: 45.69  E-value: 4.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154758281  83 VVFMVTDISMDPHAGEIATGRVFSGTLEKGQELYVSGTA---------GKNRIQSVGLFMGSEREEVDRVPAGNIASVTG 153
Cdd:cd04090    2 VVHVTKLYSSSDGGSFWALGRIYSGTLRKGQKVKVLGENysledeedmTVCTVGRLWILGARYKYEVNSAPAGNWVLIKG 81

                         90
                 ....*....|...
gi 154758281 154 LRDAIA-GSTVSS 165
Cdd:cd04090   82 IDQSIVkTATITS 94
Tet_II cd03690
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain ...
 103-156 5.59e-06

Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain II of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology to domain II of the elongation factors EF-G and EF-2. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner thereby mediating Tc resistance. Tcs are broad-spectrum antibiotics. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA.


Pssm-ID: 293891 [Multi-domain]  Cd Length: 86  Bit Score: 42.61  E-value: 5.59e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 154758281 103 RVFSGTLEKGQELYVSGTAGKNRIQSVGLFMGSEREEVDRVPAGNIASVTGLRD 156
Cdd:cd03690   24 RLYSGTLRLRDSVRVSGEEEKIKITELRTFENGELVKVDRVYAGDIAILVGLKS 77
mtEFG1_II_like cd04091
Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic ...
 103-165 2.25e-05

Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s); mtEFG2s are not present in this group.


Pssm-ID: 293908 [Multi-domain]  Cd Length: 81  Bit Score: 40.73  E-value: 2.25e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154758281 103 RVFSGTLEKGQELYVSGTAGKNRIQSVGLFMGSEREEVDRVPAGNIASVTGLrDAIAGSTVSS 165
Cdd:cd04091   20 RVYQGVLRKGDTIYNVRTGKKVRVPRLVRMHSDEMEDIEEVYAGDICALFGI-DCASGDTFTD 81
RF3_II cd03689
Domain II of bacterial Release Factor 3; This subfamily represents domain II of bacterial ...
 92-148 6.54e-05

Domain II of bacterial Release Factor 3; This subfamily represents domain II of bacterial Release Factor 3 (RF3). Termination of protein synthesis by the ribosome requires two release factor (RF) classes. The class II RF3 is a GTPase that removes class I RFs (RF1 or RF2) from the ribosome after release of the nascent polypeptide. RF3 in the GDP state binds to the ribosomal class I RF complex, followed by an exchange of GDP for GTP and release of the class I RF. Sequence comparison of class II release factors with elongation factors shows that prokaryotic RF3 is more similar to EF-G whereas eukaryotic eRF3 is more similar to eEF1A, implying that their precise function may differ.


Pssm-ID: 293890 [Multi-domain]  Cd Length: 87  Bit Score: 39.56  E-value: 6.54e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 154758281  92 MDP-HAGEIATGRVFSGTLEKGQELYVSGTAGKNRIQSVGLFMGSEREEVDRVPAGNI 148
Cdd:cd03689   12 MDPkHRDRIAFLRVCSGKFERGMKVKHVRTGKEVRLSNATTFMAQDRETVEEAYPGDI 69
EF4_II cd03699
Domain II of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ...
 93-165 1.76e-04

Domain II of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly conserved guanosine triphosphatase found in bacteria and eukaryotic mitochondria and chloroplasts. EF4 functions as a translation factor, which promotes back-translocation of tRNAs on posttranslocational ribosome complexes and competes with elongation factor G for interaction with pretranslocational ribosomes, inhibiting the elongation phase of protein synthesis.


Pssm-ID: 293900 [Multi-domain]  Cd Length: 86  Bit Score: 38.55  E-value: 1.76e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 154758281  93 DPHAGEIATGRVFSGTLEKGQELYVSGTAGKNRIQSVGLFMgSEREEVDRVPAGN----IASVTGLRDAIAGSTVSS 165
Cdd:cd03699   11 DPYRGVVVLVRVFDGTLKKGDKIRFMATGKEYEVLEVGVFT-PKMVPTDELSAGEvgyiIAGIKSVKDARVGDTITL 86
prfC PRK00741
peptide chain release factor 3; Provisional
 92-148 1.10e-03

peptide chain release factor 3; Provisional


Pssm-ID: 179105 [Multi-domain]  Cd Length: 526  Bit Score: 38.58  E-value: 1.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 154758281  92 MDP-HAGEIATGRVFSGTLEKGQELYVSGTAGKNRIQSVGLFMGSEREEVDRVPAGNI 148
Cdd:PRK00741 304 MDPkHRDRIAFVRVCSGKFEKGMKVRHVRTGKDVRISNALTFMAQDREHVEEAYAGDI 361
 
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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