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Conserved domains on  [gi|780959649|gb|AJZ71563|]
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elongation factor 2, partial [Visia cayennensis]

Protein Classification

elongation factor 2 family protein( domain architecture ID 999991)

elongation factor 2 (EF-2) family protein simmilar to EF-2 that catalyzes the GTP-dependent ribosomal translocation step during translation elongation

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;
1-276 2.89e-172

elongation factor G-like protein;


The actual alignment was detected with superfamily member PLN00116:

Pssm-ID: 481252 [Multi-domain]  Cd Length: 843  Bit Score: 496.94  E-value: 2.89e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649   1 EKGTVAFSAGLHGWAFTLNRFAAMYSKKFGVELSKMRARLWGDNFFNKSDKKWTKKAGGDSS--RAFCEFIIKPIKKIIE 78
Cdd:PLN00116 205 EKGTVAFSAGLHGWAFTLTNFAKMYASKFGVDESKMMERLWGENFFDPATKKWTTKNTGSPTckRGFVQFCYEPIKQIIN 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649  79 LCMADKVDDLQKLLAGLDIKL*SEDRELRQKPLMKRVLQKWLPADQALLEMMVLHLPSPAIAQKYRAETLYEGPLDDICC 158
Cdd:PLN00116 285 TCMNDQKDKLWPMLEKLGVTLKSDEKELMGKALMKRVMQTWLPASDALLEMIIFHLPSPAKAQRYRVENLYEGPLDDKYA 364

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649 159 TAIRNCDPDGPLMLYVSKMIPSADKGRFIAYGRVFSGTVRTGMKVRIMGPNYVPGTKKDLNVKNIQRTLLMMGRRQDAVE 238
Cdd:PLN00116 365 TAIRNCDPNGPLMLYVSKMIPASDKGRFFAFGRVFSGTVATGMKVRIMGPNYVPGEKKDLYVKSVQRTVIWMGKKQESVE 444

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 780959649 239 SVPCGNTVGLVGLDQYLIKSGTLSD--CEEAFPLKDMKYS 276
Cdd:PLN00116 445 DVPCGNTVAMVGLDQFITKNATLTNekEVDAHPIKAMKFS 484
 
Name Accession Description Interval E-value
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
 1-276 2.89e-172

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 496.94  E-value: 2.89e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649   1 EKGTVAFSAGLHGWAFTLNRFAAMYSKKFGVELSKMRARLWGDNFFNKSDKKWTKKAGGDSS--RAFCEFIIKPIKKIIE 78
Cdd:PLN00116 205 EKGTVAFSAGLHGWAFTLTNFAKMYASKFGVDESKMMERLWGENFFDPATKKWTTKNTGSPTckRGFVQFCYEPIKQIIN 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649  79 LCMADKVDDLQKLLAGLDIKL*SEDRELRQKPLMKRVLQKWLPADQALLEMMVLHLPSPAIAQKYRAETLYEGPLDDICC 158
Cdd:PLN00116 285 TCMNDQKDKLWPMLEKLGVTLKSDEKELMGKALMKRVMQTWLPASDALLEMIIFHLPSPAKAQRYRVENLYEGPLDDKYA 364

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649 159 TAIRNCDPDGPLMLYVSKMIPSADKGRFIAYGRVFSGTVRTGMKVRIMGPNYVPGTKKDLNVKNIQRTLLMMGRRQDAVE 238
Cdd:PLN00116 365 TAIRNCDPNGPLMLYVSKMIPASDKGRFFAFGRVFSGTVATGMKVRIMGPNYVPGEKKDLYVKSVQRTVIWMGKKQESVE 444

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 780959649 239 SVPCGNTVGLVGLDQYLIKSGTLSD--CEEAFPLKDMKYS 276
Cdd:PLN00116 445 DVPCGNTVAMVGLDQFITKNATLTNekEVDAHPIKAMKFS 484
EF2_II cd16268
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ...
 169-263 1.14e-47

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: 153.91  E-value: 1.14e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649 169 PLMLYVSKMIPsADKG-RFIAYGRVFSGTVRTGMKVRIMGPNYVPGTKKDLNVKNIQRTLLMMGRRQDAVESVPCGNTVG 247
Cdd:cd16268    1 PLVMYVSKMVP-TDKGaGFVAFGRVFSGTVRRGQEVYILGPKYVPGKKDDLKKKRIQQTYLMMGREREPVDEVPAGNIVG 79

                         90
                 ....*....|....*.
gi 780959649 248 LVGLDQYLIKSGTLSD 263
Cdd:cd16268   80 LVGLDDFLAKSGTTTS 95
aEF-2 TIGR00490
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ...
 104-251 9.11e-25

translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]


Pssm-ID: 129581 [Multi-domain]  Cd Length: 720  Bit Score: 103.44  E-value: 9.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649  104 RELRQKPLMKRVlqkwlPADQALLEMMVLHLPSPAIAQKYRAETLYEGPLDDICCTAIRNCDPDGPLMLYVSKMIPSADK 183
Cdd:TIGR00490 229 KEDKQKELAKKS-----PLHQVVLDMVIRHLPSPIEAQKYRIPVIWKGDLNSEVGKAMLNCDPKGPLALMITKIVVDKHA 303

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 780959649  184 GRfIAYGRVFSGTVRTGMKVrimgpnYVPGTKKDlnvKNIQRTLLMMGRRQDAVESVPCGNTVGLVGL 251
Cdd:TIGR00490 304 GE-VAVGRLYSGTIRPGMEV------YIVDRKAK---ARIQQVGVYMGPERVEVDEIPAGNIVAVIGL 361
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 186-256 1.45e-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: 64.21  E-value: 1.45e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 780959649  186 FIAYGRVFSGTVRTGMKVRIMGpnyvPGTKKDLNVKNIQRTLLMMGRRQDAVESVPCGNTVGLVGLDQYLI 256
Cdd:pfam03144   2 TVATGRVESGTLKKGDKVRILP----NGTGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRV 68
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 124-275 5.16e-13

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: 68.53  E-value: 5.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649 124 QALLEMMVLHLPSPAIAQKYRAETLYEGPlddiccTAIRNCDPDGPLMLYVSKMIpsADK--GRfIAYGRVFSGTVRTGM 201
Cdd:COG0480  267 QPLLDAVVDYLPSPLDVPAIKGVDPDTGE------EVERKPDDDEPFSALVFKTM--TDPfvGK-LSFFRVYSGTLKSGS 337

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 780959649 202 KVrimgpnYVPGTKKDlnvKNIQRTLLMMGRRQDAVESVPCGNTVGLVGLDQylIKSG-TLSDCEEAFPLKDMKY 275
Cdd:COG0480  338 TV------YNSTKGKK---ERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKD--TTTGdTLCDEDHPIVLEPIEF 401
 
Name Accession Description Interval E-value
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
 1-276 2.89e-172

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 496.94  E-value: 2.89e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649   1 EKGTVAFSAGLHGWAFTLNRFAAMYSKKFGVELSKMRARLWGDNFFNKSDKKWTKKAGGDSS--RAFCEFIIKPIKKIIE 78
Cdd:PLN00116 205 EKGTVAFSAGLHGWAFTLTNFAKMYASKFGVDESKMMERLWGENFFDPATKKWTTKNTGSPTckRGFVQFCYEPIKQIIN 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649  79 LCMADKVDDLQKLLAGLDIKL*SEDRELRQKPLMKRVLQKWLPADQALLEMMVLHLPSPAIAQKYRAETLYEGPLDDICC 158
Cdd:PLN00116 285 TCMNDQKDKLWPMLEKLGVTLKSDEKELMGKALMKRVMQTWLPASDALLEMIIFHLPSPAKAQRYRVENLYEGPLDDKYA 364

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649 159 TAIRNCDPDGPLMLYVSKMIPSADKGRFIAYGRVFSGTVRTGMKVRIMGPNYVPGTKKDLNVKNIQRTLLMMGRRQDAVE 238
Cdd:PLN00116 365 TAIRNCDPNGPLMLYVSKMIPASDKGRFFAFGRVFSGTVATGMKVRIMGPNYVPGEKKDLYVKSVQRTVIWMGKKQESVE 444

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 780959649 239 SVPCGNTVGLVGLDQYLIKSGTLSD--CEEAFPLKDMKYS 276
Cdd:PLN00116 445 DVPCGNTVAMVGLDQFITKNATLTNekEVDAHPIKAMKFS 484
PTZ00416 PTZ00416
elongation factor 2; Provisional
 1-276 1.36e-163

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 474.54  E-value: 1.36e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649   1 EKGTVAFSAGLHGWAFTLNRFAAMYSKKFGVELSKMRARLWGDNFFNKSDKKWTKKAGGDS----SRAFCEFIIKPIKKI 76
Cdd:PTZ00416 199 EKGTVAFGSGLQGWAFTLTTFARIYAKKFGVEESKMMERLWGDNFFDAKTKKWIKDETNAQgkklKRAFCQFILDPICQL 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649  77 IELCMADKVDDLQKLLAGLDIKL*SEDRELRQKPLMKRVLQKWLPADQALLEMMVLHLPSPAIAQKYRAETLYEGPLDDI 156
Cdd:PTZ00416 279 FDAVMNEDKEKYDKMLKSLNISLTGEDKELTGKPLLKAVMQKWLPAADTLLEMIVDHLPSPKEAQKYRVENLYEGPMDDE 358

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649 157 CCTAIRNCDPDGPLMLYVSKMIPSADKGRFIAYGRVFSGTVRTGMKVRIMGPNYVPGTKKDLNVKNIQRTLLMMGRRQDA 236
Cdd:PTZ00416 359 AANAIRNCDPNGPLMMYISKMVPTSDKGRFYAFGRVFSGTVATGQKVRIQGPNYVPGKKEDLFEKNIQRTVLMMGRYVEQ 438

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 780959649 237 VESVPCGNTVGLVGLDQYLIKSGTLSDCEEAFPLKDMKYS 276
Cdd:PTZ00416 439 IEDVPCGNTVGLVGVDQYLVKSGTITTSETAHNIRDMKYS 478
EF2_II cd16268
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ...
 169-263 1.14e-47

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: 153.91  E-value: 1.14e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649 169 PLMLYVSKMIPsADKG-RFIAYGRVFSGTVRTGMKVRIMGPNYVPGTKKDLNVKNIQRTLLMMGRRQDAVESVPCGNTVG 247
Cdd:cd16268    1 PLVMYVSKMVP-TDKGaGFVAFGRVFSGTVRRGQEVYILGPKYVPGKKDDLKKKRIQQTYLMMGREREPVDEVPAGNIVG 79

                         90
                 ....*....|....*.
gi 780959649 248 LVGLDQYLIKSGTLSD 263
Cdd:cd16268   80 LVGLDDFLAKSGTTTS 95
EF2_snRNP_like_II cd03700
Domain II of elongation factor 2 and C-terminal domain of the spliceosomal human 116kD U5 ...
 170-262 6.10e-41

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: 136.59  E-value: 6.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649 170 LMLYVSKMIPSADKGRFIAYGRVFSGTVRTGMKVRIMGPNYVPGTKKDLNVKNIQRTLLMMGRRQDAVESVPCGNTVGLV 249
Cdd:cd03700    1 LMVYSSKMVPTSDKGRFYAFGRVFAGTVHAGQKVRILGPNYTPGKKEDLRIKAIQRLWLMMGRYVEEINDVPAGNIVGLV 80

                         90
                 ....*....|...
gi 780959649 250 GLDQYLIKSGTLS 262
Cdd:cd03700   81 GIDQFLQKTGTTT 93
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 1-275 3.45e-30

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 119.20  E-value: 3.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649   1 EKGTVAFSAGLHGWAFTLNrfaamYSKKFGVELSKMrarlwgdnffnksdkkwtkkaggdssrafcefiikpikkiIELC 80
Cdd:PRK07560 195 EDGTVAFGSALYNWAISVP-----MMQKTGIKFKDI----------------------------------------IDYY 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649  81 MADKVDdlqkllagldikl*sedrELRQKplmkrvlqkwLPADQALLEMMVLHLPSPAIAQKYRAETLYEGPLDDICCTA 160
Cdd:PRK07560 230 EKGKQK------------------ELAEK----------APLHEVVLDMVVKHLPNPIEAQKYRIPKIWKGDLNSEVGKA 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649 161 IRNCDPDGPLMLYVSKMI--PSAdkgRFIAYGRVFSGTVRTGMKVrimgpnYVPGTKKdlnvKN-IQRTLLMMGRRQDAV 237
Cdd:PRK07560 282 MLNCDPNGPLVMMVTDIIvdPHA---GEVATGRVFSGTLRKGQEV------YLVGAKK----KNrVQQVGIYMGPEREEV 348

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 780959649 238 ESVPCGNTVGLVGLDQyLIKSGTLSDCEEAFPLKDMKY 275
Cdd:PRK07560 349 EEIPAGNIAAVTGLKD-ARAGETVVSVEDMTPFESLKH 385
aEF-2 TIGR00490
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ...
 104-251 9.11e-25

translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]


Pssm-ID: 129581 [Multi-domain]  Cd Length: 720  Bit Score: 103.44  E-value: 9.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649  104 RELRQKPLMKRVlqkwlPADQALLEMMVLHLPSPAIAQKYRAETLYEGPLDDICCTAIRNCDPDGPLMLYVSKMIPSADK 183
Cdd:TIGR00490 229 KEDKQKELAKKS-----PLHQVVLDMVIRHLPSPIEAQKYRIPVIWKGDLNSEVGKAMLNCDPKGPLALMITKIVVDKHA 303

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 780959649  184 GRfIAYGRVFSGTVRTGMKVrimgpnYVPGTKKDlnvKNIQRTLLMMGRRQDAVESVPCGNTVGLVGL 251
Cdd:TIGR00490 304 GE-VAVGRLYSGTIRPGMEV------YIVDRKAK---ARIQQVGVYMGPERVEVDEIPAGNIVAVIGL 361
EF2_II_snRNP cd04090
Domain II of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component; This ...
 170-263 2.26e-22

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: 88.45  E-value: 2.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649 170 LMLYVSKMIPSADKGRFIAYGRVFSGTVRTGMKVRIMGPNYVPGTKKDLNVKNIQRTLLMMGRRQDAVESVPCGNTVGLV 249
Cdd:cd04090    1 LVVHVTKLYSSSDGGSFWALGRIYSGTLRKGQKVKVLGENYSLEDEEDMTVCTVGRLWILGARYKYEVNSAPAGNWVLIK 80

                         90
                 ....*....|....
gi 780959649 250 GLDQYLIKSGTLSD 263
Cdd:cd04090   81 GIDQSIVKTATITS 94
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 186-256 1.45e-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: 64.21  E-value: 1.45e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 780959649  186 FIAYGRVFSGTVRTGMKVRIMGpnyvPGTKKDLNVKNIQRTLLMMGRRQDAVESVPCGNTVGLVGLDQYLI 256
Cdd:pfam03144   2 TVATGRVESGTLKKGDKVRILP----NGTGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRV 68
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
124-275 2.05e-13

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 69.77  E-value: 2.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649 124 QALLEMMVLHLPSPAIAQKYRAETLYEGPLddicctaiRNCDPDGPLMLYVSKMIPSADKGRfIAYGRVFSGTVRTGMKV 203
Cdd:PRK12740 251 QRLLDAVVDYLPSPLEVPPVDGEDGEEGAE--------LAPDPDGPLVALVFKTMDDPFVGK-LSLVRVYSGTLKKGDTL 321

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 780959649 204 rimgpnYVPGTKKDLNVKNIQRtllMMGRRQDAVESVPCGNTVGLVGLDQylIKSG-TLSDCEEAFPLKDMKY 275
Cdd:PRK12740 322 ------YNSGTGKKERVGRLYR---MHGKQREEVDEAVAGDIVAVAKLKD--AATGdTLCDKGDPILLEPMEF 383
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 124-275 5.16e-13

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: 68.53  E-value: 5.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649 124 QALLEMMVLHLPSPAIAQKYRAETLYEGPlddiccTAIRNCDPDGPLMLYVSKMIpsADK--GRfIAYGRVFSGTVRTGM 201
Cdd:COG0480  267 QPLLDAVVDYLPSPLDVPAIKGVDPDTGE------EVERKPDDDEPFSALVFKTM--TDPfvGK-LSFFRVYSGTLKSGS 337

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 780959649 202 KVrimgpnYVPGTKKDlnvKNIQRTLLMMGRRQDAVESVPCGNTVGLVGLDQylIKSG-TLSDCEEAFPLKDMKY 275
Cdd:COG0480  338 TV------YNSTKGKK---ERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKD--TTTGdTLCDEDHPIVLEPIEF 401
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 170-259 7.02e-08

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: 48.80  E-value: 7.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649 170 LMLYVSKMIPSADKGRfIAYGRVFSGTVRTGMKVRIMgpnyvpGTKKDLNVKNIQRtllMMGRrqdaVESVPCGNTVGLV 249
Cdd:cd01342    1 LVMQVFKVFYIPGRGR-VAGGRVESGTLKVGDEIRIL------PKGITGRVTSIER---FHEE----VDEAKAGDIVGIG 66

                         90
                 ....*....|
gi 780959649 250 GLDQYLIKSG 259
Cdd:cd01342   67 ILGVKDILTG 76
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
 1-26 5.00e-06

Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.


Pssm-ID: 206672 [Multi-domain]  Cd Length: 218  Bit Score: 46.46  E-value: 5.00e-06
                         10        20
                 ....*....|....*....|....*.
gi 780959649   1 EKGTVAFSAGLHGWAFTLNRFAAMYS 26
Cdd:cd01885  181 QKGNVAFGSALDGWGFTIIKFADIYA 206
BipA_TypA_II cd03691
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ...
 183-271 2.26e-05

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: 42.17  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649 183 KGRfIAYGRVFSGTVRTGMKVRIMGPNyvpGTKKDLNVKNIQrtlLMMGRRQDAVESVPCGNTVGLVGLDQYLIKSgTLS 262
Cdd:cd03691   14 LGR-IAIGRIFSGTVKVGQQVTVVDED---GKIEKGRVTKLF---GFEGLERVEVEEAEAGDIVAIAGLEDITIGD-TIC 85


                 ....*....
gi 780959649 263 DCEEAFPLK 271
Cdd:cd03691   86 DPEVPEPLP 94
EFG_mtEFG_II cd04088
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ...
 187-252 9.48e-05

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: 40.20  E-value: 9.48e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 780959649 187 IAYGRVFSGTVRTGMKVrimgpnYVPGTKKDlnvKNIQRTLLMMGRRQDAVESVPCGNTVGLVGLD 252
Cdd:cd04088   17 LTFFRVYSGTLKSGSTV------YNSTKGKK---ERVGRLLRMHGKKREEVEELGAGDIGAVVGLK 73
Tet_II cd03690
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain ...
 167-252 2.59e-03

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: 36.06  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959649 167 DGPLMLYVSKMIPSaDKGRFIAYGRVFSGTVRTGMKVRImgpnyvPGTKKDLNVKNIQRtlLMMGRRQDaVESVPCGNTV 246
Cdd:cd03690    1 ESELSGTVFKIEYD-PKGERLAYLRLYSGTLRLRDSVRV------SGEEEKIKITELRT--FENGELVK-VDRVYAGDIA 70


                 ....*.
gi 780959649 247 GLVGLD 252
Cdd:cd03690   71 ILVGLK 76
 
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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