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Conserved domains on  [gi|310750664|gb|ADP09125|]
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elongation factor 2, partial [Halobacterium salinarum]

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;
1-168 3.35e-101

elongation factor G-like protein;


The actual alignment was detected with superfamily member PRK07560:

Pssm-ID: 481252 [Multi-domain]  Cd Length: 731  Bit Score: 306.02  E-value: 3.35e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750664   1 VSMPSMQRTGMDFGDIIDLERSDKREELHEQTPLADVVLDMVAEHFPNPIDAQPRRIPTVWRGDADSEIAESMRLVDEDG 80
Cdd:PRK07560 210 ISVPMMQKTGIKFKDIIDYYEKGKQKELAEKAPLHEVVLDMVVKHLPNPIEAQKYRIPKIWKGDLNSEVGKAMLNCDPNG 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750664  81 EVVLMVTDIGVDPHAGEIAAGRVFSGTLEKGQELYVSGTAGKNRVQSVGIYMGGEREEVDEVPAGNIAAVTGLKDAIAGS 160
Cdd:PRK07560 290 PLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKNRVQQVGIYMGPEREEVEEIPAGNIAAVTGLKDARAGE 369


                 ....*....
gi 310750664 161 TVSN-EEMT 168
Cdd:PRK07560 370 TVVSvEDMT 378
 
Name Accession Description Interval E-value
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 1-168 3.35e-101

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 306.02  E-value: 3.35e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750664   1 VSMPSMQRTGMDFGDIIDLERSDKREELHEQTPLADVVLDMVAEHFPNPIDAQPRRIPTVWRGDADSEIAESMRLVDEDG 80
Cdd:PRK07560 210 ISVPMMQKTGIKFKDIIDYYEKGKQKELAEKAPLHEVVLDMVVKHLPNPIEAQKYRIPKIWKGDLNSEVGKAMLNCDPNG 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750664  81 EVVLMVTDIGVDPHAGEIAAGRVFSGTLEKGQELYVSGTAGKNRVQSVGIYMGGEREEVDEVPAGNIAAVTGLKDAIAGS 160
Cdd:PRK07560 290 PLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKNRVQQVGIYMGPEREEVEEIPAGNIAAVTGLKDARAGE 369


                 ....*....
gi 310750664 161 TVSN-EEMT 168
Cdd:PRK07560 370 TVVSvEDMT 378
EF2_II cd16268
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ...
 81-163 1.96e-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: 106.15  E-value: 1.96e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750664  81 EVVLMVTDIGV-DPHAGEIAAGRVFSGTLEKGQELYVSG---------TAGKNRVQSVGIYMGGEREEVDEVPAGNIAAV 150
Cdd:cd16268    1 PLVMYVSKMVPtDKGAGFVAFGRVFSGTVRRGQEVYILGpkyvpgkkdDLKKKRIQQTYLMMGREREPVDEVPAGNIVGL 80

                         90
                 ....*....|....*
gi 310750664 151 TGLKD--AIAGSTVS 163
Cdd:cd16268   81 VGLDDflAKSGTTTS 95
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 38-166 4.28e-21

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: 88.95  E-value: 4.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750664  38 VLDMVAEHFPNPIDAQPRRiptvwrGDADSEIAESMRLVDEDGEVVLMVTDIGVDPHAGEIAAGRVFSGTLEKGQELYVS 117
Cdd:COG0480  269 LLDAVVDYLPSPLDVPAIK------GVDPDTGEEVERKPDDDEPFSALVFKTMTDPFVGKLSFFRVYSGTLKSGSTVYNS 342

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 310750664 118 GTAGKNRVQsvGIY--MGGEREEVDEVPAGNIAAVTGLKDAIAGSTVSNEE 166
Cdd:COG0480  343 TKGKKERIG--RLLrmHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCDED 391
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 96-163 1.30e-12

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: 59.59  E-value: 1.30e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 310750664   96 GEIAAGRVFSGTLEKGQELYV--SGTAGKN---RVQSVGIYMGGEREEVDEVPAGNIAAVTGLKDAIAGSTVS 163
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRIlpNGTGKKKivtRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
 
Name Accession Description Interval E-value
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 1-168 3.35e-101

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 306.02  E-value: 3.35e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750664   1 VSMPSMQRTGMDFGDIIDLERSDKREELHEQTPLADVVLDMVAEHFPNPIDAQPRRIPTVWRGDADSEIAESMRLVDEDG 80
Cdd:PRK07560 210 ISVPMMQKTGIKFKDIIDYYEKGKQKELAEKAPLHEVVLDMVVKHLPNPIEAQKYRIPKIWKGDLNSEVGKAMLNCDPNG 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750664  81 EVVLMVTDIGVDPHAGEIAAGRVFSGTLEKGQELYVSGTAGKNRVQSVGIYMGGEREEVDEVPAGNIAAVTGLKDAIAGS 160
Cdd:PRK07560 290 PLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKNRVQQVGIYMGPEREEVEEIPAGNIAAVTGLKDARAGE 369


                 ....*....
gi 310750664 161 TVSN-EEMT 168
Cdd:PRK07560 370 TVVSvEDMT 378
EF2_II cd16268
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ...
 81-163 1.96e-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: 106.15  E-value: 1.96e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750664  81 EVVLMVTDIGV-DPHAGEIAAGRVFSGTLEKGQELYVSG---------TAGKNRVQSVGIYMGGEREEVDEVPAGNIAAV 150
Cdd:cd16268    1 PLVMYVSKMVPtDKGAGFVAFGRVFSGTVRRGQEVYILGpkyvpgkkdDLKKKRIQQTYLMMGREREPVDEVPAGNIVGL 80

                         90
                 ....*....|....*
gi 310750664 151 TGLKD--AIAGSTVS 163
Cdd:cd16268   81 VGLDDflAKSGTTTS 95
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 38-166 4.28e-21

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: 88.95  E-value: 4.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750664  38 VLDMVAEHFPNPIDAQPRRiptvwrGDADSEIAESMRLVDEDGEVVLMVTDIGVDPHAGEIAAGRVFSGTLEKGQELYVS 117
Cdd:COG0480  269 LLDAVVDYLPSPLDVPAIK------GVDPDTGEEVERKPDDDEPFSALVFKTMTDPFVGKLSFFRVYSGTLKSGSTVYNS 342

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 310750664 118 GTAGKNRVQsvGIY--MGGEREEVDEVPAGNIAAVTGLKDAIAGSTVSNEE 166
Cdd:COG0480  343 TKGKKERIG--RLLrmHGNKREEVDEAGAGDIVAVVKLKDTTTGDTLCDED 391
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
38-166 1.12e-20

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 87.87  E-value: 1.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750664  38 VLDMVAEHFPNPIDAQPRriptvwrgDADSEIAESMRLVDEDGEVVLMVTDIGVDPHAGEIAAGRVFSGTLEKGQELYVS 117
Cdd:PRK12740 253 LLDAVVDYLPSPLEVPPV--------DGEDGEEGAELAPDPDGPLVALVFKTMDDPFVGKLSLVRVYSGTLKKGDTLYNS 324

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 310750664 118 GTAGKNRVQSVGIYMGGEREEVDEVPAGNIAAVTGLKDAIAGSTVSNEE 166
Cdd:PRK12740 325 GTGKKERVGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTLCDKG 373
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
 33-166 4.18e-19

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 83.23  E-value: 4.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750664  33 PLADVVLDMVAEHFPNPIDAQPRRIPTVWRGDADSEIAESMRLVDEDGEVVLMVTDIGVDPHAGE-IAAGRVFSGTLEKG 111
Cdd:PLN00116 327 PASDALLEMIIFHLPSPAKAQRYRVENLYEGPLDDKYATAIRNCDPNGPLMLYVSKMIPASDKGRfFAFGRVFSGTVATG 406

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 310750664 112 QELYVSGTA---GKNR------VQSVGIYMGGEREEVDEVPAGNIAAVTGLKDAIAGS-TVSNEE 166
Cdd:PLN00116 407 MKVRIMGPNyvpGEKKdlyvksVQRTVIWMGKKQESVEDVPCGNTVAMVGLDQFITKNaTLTNEK 471
PTZ00416 PTZ00416
elongation factor 2; Provisional
 33-166 1.29e-18

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 82.02  E-value: 1.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750664  33 PLADVVLDMVAEHFPNPIDAQPRRIPTVWRGDADSEIAESMRLVDEDGEVVLMVTDIGVDPHAGEIAA-GRVFSGTLEKG 111
Cdd:PTZ00416 323 PAADTLLEMIVDHLPSPKEAQKYRVENLYEGPMDDEAANAIRNCDPNGPLMMYISKMVPTSDKGRFYAfGRVFSGTVATG 402

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 310750664 112 QEL------YVSGTAG----KNrVQSVGIYMGGEREEVDEVPAGNIAAVTGLKDAIAGS-TVSNEE 166
Cdd:PTZ00416 403 QKVriqgpnYVPGKKEdlfeKN-IQRTVLMMGRYVEQIEDVPCGNTVGLVGVDQYLVKSgTITTSE 467
EFG_mtEFG_II cd04088
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ...
 91-163 8.30e-18

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: 73.33  E-value: 8.30e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 310750664  91 VDPHAGEIAAGRVFSGTLEKGQELYVSGTAGKNRVQSVGIYMGGEREEVDEVPAGNIAAVTGLKDAIAGSTVS 163
Cdd:cd04088   10 ADPFVGKLTFFRVYSGTLKSGSTVYNSTKGKKERVGRLLRMHGKKREEVEELGAGDIGAVVGLKDTRTGDTLC 82
PRK13351 PRK13351
elongation factor G-like protein;
38-162 3.00e-14

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 69.21  E-value: 3.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750664  38 VLDMVAEHFPNPIDAQPRRiptvwrGDADSEIAESMRLvDEDGEVVLMVTDIGVDPHAGEIAAGRVFSGTLEKGQELYVS 117
Cdd:PRK13351 269 LLDAVVDYLPSPLEVPPPR------GSKDNGKPVKVDP-DPEKPLLALVFKVQYDPYAGKLTYLRVYSGTLRAGSQLYNG 341

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 310750664 118 GtaGKNRVQSVGIY--MGGEREEVDEVPAGNIAAVTGLKDAIAGSTV 162
Cdd:PRK13351 342 T--GGKREKVGRLFrlQGNKREEVDRAKAGDIVAVAGLKELETGDTL 386
BipA_TypA_II cd03691
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ...
 84-162 9.28e-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: 63.36  E-value: 9.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750664  84 LMVTDIGVDPHAGEIAAGRVFSGTLEKGQELYV---SGTAGKNRVQSVGIYMGGEREEVDEVPAGNIAAVTGLKDAIAGS 160
Cdd:cd03691    3 MLVTTLDYDDYLGRIAIGRIFSGTVKVGQQVTVvdeDGKIEKGRVTKLFGFEGLERVEVEEAEAGDIVAIAGLEDITIGD 82


                 ..
gi 310750664 161 TV 162
Cdd:cd03691   83 TI 84
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 96-163 1.30e-12

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: 59.59  E-value: 1.30e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 310750664   96 GEIAAGRVFSGTLEKGQELYV--SGTAGKN---RVQSVGIYMGGEREEVDEVPAGNIAAVTGLKDAIAGSTVS 163
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 ...
 83-163 4.70e-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: 50.73  E-value: 4.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310750664  83 VLMVTDIGVDPHAGEIAAGRVFSGTLEKGQELYVSGTAGKNRVQSvgIYMGgeREEVDEVPAGNIAAVTGL--KDAIAGS 160
Cdd:cd01342    2 VMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTS--IERF--HEEVDEAKAGDIVGIGILgvKDILTGD 77


                 ...
gi 310750664 161 TVS 163
Cdd:cd01342   78 TLT 80
mtEFG2_II_like cd04092
Domain II of mitochondrial elongation factor G2-like proteins found in eukaryotes; Eukaryotic ...
 92-162 8.84e-09

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: 50.01  E-value: 8.84e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 310750664  92 DPHAGEIAAGRVFSGTLEKGQELYVSGTAGKNRVQSVGIYMGGEREEVDEVPAGNIAAVTGLKDAIAGSTV 162
Cdd:cd04092   11 DPQRGPLVFVRVYSGTLKAGSNVYNTTTGKKERISRLLKMHADQTEEVDSLSAGNIGVITGLKVTSTGDTL 81
Tet_II cd03690
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain ...
 102-155 5.86e-08

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: 48.00  E-value: 5.86e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 310750664 102 RVFSGTLEKGQELYVSGTAGKNRVQSVGIYMGGEREEVDEVPAGNIAAVTGLKD 155
Cdd:cd03690   24 RLYSGTLRLRDSVRVSGEEEKIKITELRTFENGELVKVDRVYAGDIAILVGLKS 77
EF2_snRNP_like_II cd03700
Domain II of elongation factor 2 and C-terminal domain of the spliceosomal human 116kD U5 ...
 99-153 5.69e-07

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: 45.68  E-value: 5.69e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 310750664  99 AAGRVFSGTLEKGQELYVSG---TAGKN------RVQSVGIYMGGEREEVDEVPAGNIAAVTGL 153
Cdd:cd03700   19 AFGRVFAGTVHAGQKVRILGpnyTPGKKedlrikAIQRLWLMMGRYVEEINDVPAGNIVGLVGI 82
mtEFG1_II_like cd04091
Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic ...
 102-163 1.65e-06

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: 43.82  E-value: 1.65e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 310750664 102 RVFSGTLEKGQELYVSGTAGKNRVQSVGIYMGGEREEVDEVPAGNIAAVTGLkDAIAGSTVS 163
Cdd:cd04091   20 RVYQGVLRKGDTIYNVRTGKKVRVPRLVRMHSDEMEDIEEVYAGDICALFGI-DCASGDTFT 80
EF2_II_snRNP cd04090
Domain II of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component; This ...
 101-157 7.29e-06

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: 42.61  E-value: 7.29e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 310750664 101 GRVFSGTLEKGQELYVSGTA---------GKNRVQSVGIYMGGEREEVDEVPAGNIAAVTGLKDAI 157
Cdd:cd04090   21 GRIYSGTLRKGQKVKVLGENysledeedmTVCTVGRLWILGARYKYEVNSAPAGNWVLIKGIDQSI 86
EF4_II cd03699
Domain II of Elongation Factor 4 (EF4); Elongation factor 4 (EF4 or LepA) is a highly ...
 92-164 2.65e-05

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: 40.86  E-value: 2.65e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 310750664  92 DPHAGEIAAGRVFSGTLEKGQELYVSGTAGKNRVQSVGIYMgGEREEVDEVPAGN----IAAVTGLKDAIAGSTVSN 164
Cdd:cd03699   11 DPYRGVVVLVRVFDGTLKKGDKIRFMATGKEYEVLEVGVFT-PKMVPTDELSAGEvgyiIAGIKSVKDARVGDTITL 86
RF3_II cd03689
Domain II of bacterial Release Factor 3; This subfamily represents domain II of bacterial ...
 92-147 1.27e-04

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: 38.79  E-value: 1.27e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 310750664  92 DP-HAGEIAAGRVFSGTLEKGQELYVSGTAGKNRVQSVGIYMGGEREEVDEVPAGNI 147
Cdd:cd03689   13 DPkHRDRIAFLRVCSGKFERGMKVKHVRTGKEVRLSNATTFMAQDRETVEEAYPGDI 69
prfC PRK00741
peptide chain release factor 3; Provisional
 92-147 7.14e-03

peptide chain release factor 3; Provisional


Pssm-ID: 179105 [Multi-domain]  Cd Length: 526  Bit Score: 35.88  E-value: 7.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 310750664  92 DP-HAGEIAAGRVFSGTLEKGQELYVSGTAGKNRVQSVGIYMGGEREEVDEVPAGNI 147
Cdd:PRK00741 305 DPkHRDRIAFVRVCSGKFEKGMKVRHVRTGKDVRISNALTFMAQDREHVEEAYAGDI 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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