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Conserved domains on  [gi|1129799276|gb|APT68126|]
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elongation factor 1 alpha, partial [Cinara ponderosae]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 1-244 1.29e-160

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member PTZ00141:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 446  Bit Score: 452.28  E-value: 1.29e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSETRFEEIKKEVSSYIKK 80
Cdd:PTZ00141  101 NMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKK 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  81 IGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGwaverkegkadgKCLIEALDAILPPSRPTDKALRLPLQDVYKIGGIG 160
Cdd:PTZ00141  181 VGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276 161 TVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFVAGDTKNNPPKGAADF 240
Cdd:PTZ00141  249 TVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADF 328


                  ....
gi 1129799276 241 TAQV 244
Cdd:PTZ00141  329 TAQV 332
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-244 1.29e-160

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 452.28  E-value: 1.29e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSETRFEEIKKEVSSYIKK 80
Cdd:PTZ00141  101 NMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKK 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  81 IGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGwaverkegkadgKCLIEALDAILPPSRPTDKALRLPLQDVYKIGGIG 160
Cdd:PTZ00141  181 VGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276 161 TVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFVAGDTKNNPPKGAADF 240
Cdd:PTZ00141  249 TVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADF 328


                  ....
gi 1129799276 241 TAQV 244
Cdd:PTZ00141  329 TAQV 332
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-244 6.84e-117

Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 444074 [Multi-domain]  Cd Length: 423  Bit Score: 340.37  E-value: 6.84e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFTLGVKQLIVGVNKMDSTEppYSETRFEEIKKEVSSYIKK 80
Cdd:COG5256   101 NMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVN--YSEKRYEEVKEEVSKLLKM 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  81 IGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGwaverkegkadgKCLIEALDAILPPSRPTDKALRLPLQDVYKIGGIG 160
Cdd:COG5256   172 VGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNG------------PTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIG 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276 161 TVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFVAGDTkNNPPKGAADF 240
Cdd:COG5256   240 TVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHP-DNPPTVAEEF 318


                  ....
gi 1129799276 241 TAQV 244
Cdd:COG5256   319 TAQI 322
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-244 7.53e-117

translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]


Pssm-ID: 129574 [Multi-domain]  Cd Length: 426  Bit Score: 340.30  E-value: 7.53e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEagisKNGQTREHALLAFTLGVKQLIVGVNKMDSTEppYSETRFEEIKKEVSSYIKK 80
Cdd:TIGR00483 101 NMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVN--YDEEEFEAIKKEVSNLIKK 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  81 IGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGwaverkegkadgKCLIEALDAILPPSRPTDKALRLPLQDVYKIGGIG 160
Cdd:TIGR00483 175 VGYNPDTVPFIPISAWNGDNVIKKSENTPWYKG------------KTLLEALDALEPPEKPTDKPLRIPIQDVYSITGVG 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276 161 TVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFVAGDTKnNPPKGAADF 240
Cdd:TIGR00483 243 TVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDVCGHPD-NPPKVAKEF 321


                  ....
gi 1129799276 241 TAQV 244
Cdd:TIGR00483 322 TAQI 325
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-138 5.20e-80

Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 206670 [Multi-domain]  Cd Length: 219  Bit Score: 239.32  E-value: 5.20e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSETRFEEIKKEVSSYIKK 80
Cdd:cd01883    93 NMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKK 172

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1129799276  81 IGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGWaverkegkadgkCLIEALDAILPP 138
Cdd:cd01883   173 VGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPP 218
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-104 2.87e-26

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 100.68  E-value: 2.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFTLGVKqLIVGVNKMDSTeppySETRFEEIKKEVSS-YIK 79
Cdd:pfam00009  85 EVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV----DGAELEEVVEEVSReLLE 152

                          90       100
                  ....*....|....*....|....*
gi 1129799276  80 KIGYNPAAVAFVPISGWNGDNMLEV 104
Cdd:pfam00009 153 KYGEDGEFVPVVPGSALKGEGVQTL 177
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-244 1.29e-160

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 452.28  E-value: 1.29e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSETRFEEIKKEVSSYIKK 80
Cdd:PTZ00141  101 NMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKK 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  81 IGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGwaverkegkadgKCLIEALDAILPPSRPTDKALRLPLQDVYKIGGIG 160
Cdd:PTZ00141  181 VGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276 161 TVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFVAGDTKNNPPKGAADF 240
Cdd:PTZ00141  249 TVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADF 328


                  ....
gi 1129799276 241 TAQV 244
Cdd:PTZ00141  329 TAQV 332
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-244 5.58e-120

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 349.39  E-value: 5.58e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSETRFEEIKKEVSSYIKK 80
Cdd:PLN00043  101 NMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKK 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  81 IGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGwaverkegkadgKCLIEALDAILPPSRPTDKALRLPLQDVYKIGGIG 160
Cdd:PLN00043  181 VGYNPDKIPFVPISGFEGDNMIERSTNLDWYKG------------PTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276 161 TVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFVAGDTKNNPPKGAADF 240
Cdd:PLN00043  249 TVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVASNSKDDPAKEAANF 328


                  ....
gi 1129799276 241 TAQV 244
Cdd:PLN00043  329 TSQV 332
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-244 6.84e-117

Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 444074 [Multi-domain]  Cd Length: 423  Bit Score: 340.37  E-value: 6.84e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFTLGVKQLIVGVNKMDSTEppYSETRFEEIKKEVSSYIKK 80
Cdd:COG5256   101 NMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVN--YSEKRYEEVKEEVSKLLKM 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  81 IGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGwaverkegkadgKCLIEALDAILPPSRPTDKALRLPLQDVYKIGGIG 160
Cdd:COG5256   172 VGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNG------------PTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIG 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276 161 TVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFVAGDTkNNPPKGAADF 240
Cdd:COG5256   240 TVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHP-DNPPTVAEEF 318


                  ....
gi 1129799276 241 TAQV 244
Cdd:COG5256   319 TAQI 322
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-244 7.53e-117

translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]


Pssm-ID: 129574 [Multi-domain]  Cd Length: 426  Bit Score: 340.30  E-value: 7.53e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEagisKNGQTREHALLAFTLGVKQLIVGVNKMDSTEppYSETRFEEIKKEVSSYIKK 80
Cdd:TIGR00483 101 NMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVN--YDEEEFEAIKKEVSNLIKK 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  81 IGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGwaverkegkadgKCLIEALDAILPPSRPTDKALRLPLQDVYKIGGIG 160
Cdd:TIGR00483 175 VGYNPDTVPFIPISAWNGDNVIKKSENTPWYKG------------KTLLEALDALEPPEKPTDKPLRIPIQDVYSITGVG 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276 161 TVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFVAGDTKnNPPKGAADF 240
Cdd:TIGR00483 243 TVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDVCGHPD-NPPKVAKEF 321


                  ....
gi 1129799276 241 TAQV 244
Cdd:TIGR00483 322 TAQI 325
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-244 9.66e-115

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 334.97  E-value: 9.66e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAgtgefEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEppYSETRFEEIKKEVSSYIKK 80
Cdd:PRK12317  100 NMITGASQADAAVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVN--YDEKRYEEVKEEVSKLLKM 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  81 IGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGwaverkegkadgKCLIEALDAILPPSRPTDKALRLPLQDVYKIGGIG 160
Cdd:PRK12317  173 VGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNG------------PTLLEALDNLKPPEKPTDKPLRIPIQDVYSISGVG 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276 161 TVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFVAGDTkNNPPKGAADF 240
Cdd:PRK12317  241 TVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHP-DNPPTVAEEF 319


                  ....
gi 1129799276 241 TAQV 244
Cdd:PRK12317  320 TAQI 323
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-138 5.20e-80

Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 206670 [Multi-domain]  Cd Length: 219  Bit Score: 239.32  E-value: 5.20e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSETRFEEIKKEVSSYIKK 80
Cdd:cd01883    93 NMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKK 172

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1129799276  81 IGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGWaverkegkadgkCLIEALDAILPP 138
Cdd:cd01883   173 VGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPP 218
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 142-232 3.15e-60

Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.


Pssm-ID: 293894 [Multi-domain]  Cd Length: 91  Bit Score: 184.70  E-value: 3.15e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276 142 TDKALRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELR 221
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80

                          90
                  ....*....|.
gi 1129799276 222 RGFVAGDTKNN 232
Cdd:cd03693    81 RGDVAGDSKND 91
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-244 7.39e-56

Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 442140 [Multi-domain]  Cd Length: 430  Bit Score: 184.14  E-value: 7.39e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSETRFEEIKKEVSSYIKK 80
Cdd:COG2895   111 NMVTGASTADLAILLIDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVD--YSEEVFEEIVADYRAFAAK 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  81 IGYNPaaVAFVPISGWNGDNMLEVSEKMPWFkgwaverkegkaDGKCLIEALDAILPPSRPTDKALRLPLQDVYKiggig 160
Cdd:COG2895   182 LGLED--ITFIPISALKGDNVVERSENMPWY------------DGPTLLEHLETVEVAEDRNDAPFRFPVQYVNR----- 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276 161 tvP-------VGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVK---NVSvkelrRGFVAGDtK 230
Cdd:COG2895   243 --PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTLEdeiDIS-----RGDVIVA-A 314

                         250
                  ....*....|....
gi 1129799276 231 NNPPKGAADFTAQV 244
Cdd:COG2895   315 DAPPEVADQFEATL 328
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-244 2.74e-35

sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 213679 [Multi-domain]  Cd Length: 406  Bit Score: 129.41  E-value: 2.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSETRFEEIKKEVSSYIKK 80
Cdd:TIGR02034  96 NMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVD--YDEEVFENIKKDYLAFAEQ 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  81 IGynPAAVAFVPISGWNGDNMLEVSEKMPWFKgwaverkegkadGKCLIEALDAILPPSRPTDKALRLPLQDVYKI---- 156
Cdd:TIGR02034 167 LG--FRDVTFIPLSALKGDNVVSRSESMPWYS------------GPTLLEILETVEVERDAQDLPLRFPVQYVNRPnldf 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276 157 -GGIGTVPVGRVetgllKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSvkELRRG--FVAGDtknNP 233
Cdd:TIGR02034 233 rGYAGTIASGSV-----HVGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLDDEI--DISRGdlLAAAD---SA 302

                         250
                  ....*....|.
gi 1129799276 234 PKGAADFTAQV 244
Cdd:TIGR02034 303 PEVADQFAATL 313
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-244 9.77e-35

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 130.82  E-value: 9.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSETRFEEIKKEVSSYIKK 80
Cdd:PRK05506  120 NMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMDLVD--YDQEVFDEIVADYRAFAAK 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  81 IGYnpAAVAFVPISGWNGDNMLEVSEKMPWFKGWAverkegkadgkcLIEALDAILPPSRPTDKALRLPLQDVYKI---- 156
Cdd:PRK05506  191 LGL--HDVTFIPISALKGDNVVTRSARMPWYEGPS------------LLEHLETVEIASDRNLKDFRFPVQYVNRPnldf 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276 157 -GGIGTVPVGRVetgllKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKN---VSvkelrRG--FVAGDtk 230
Cdd:PRK05506  257 rGFAGTVASGVV-----RPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLADeidIS-----RGdmLARAD-- 324

                         250
                  ....*....|....
gi 1129799276 231 nNPPKGAADFTAQV 244
Cdd:PRK05506  325 -NRPEVADQFDATV 337
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-208 1.16e-34

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 128.88  E-value: 1.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSETRFEEIKKEVSSYIKK 80
Cdd:PRK05124  123 NMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVD--YSEEVFERIREDYLTFAEQ 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  81 IGYNPaAVAFVPISGWNGDNMLEVSEKMPWFKgwaverkegkadGKCLIEALDAILPPSRPTDKALRLPLQDVYKI---- 156
Cdd:PRK05124  194 LPGNL-DIRFVPLSALEGDNVVSQSESMPWYS------------GPTLLEVLETVDIQRVVDAQPFRFPVQYVNRPnldf 260

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1129799276 157 -GGIGTVPVGRVetgllKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNV 208
Cdd:PRK05124  261 rGYAGTLASGVV-----KVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAI 308
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-139 3.06e-34

CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.


Pssm-ID: 206729 [Multi-domain]  Cd Length: 209  Bit Score: 121.91  E-value: 3.06e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSETRFEEIKKEVSSYIKK 80
Cdd:cd04166    94 NMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVD--YDEEVFEEIKADYLAFAAS 164

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1129799276  81 IGYNPaaVAFVPISGWNGDNMLEVSEKMPWFKgwaverkegkadGKCLIEALDAILPPS 139
Cdd:cd04166   165 LGIED--ITFIPISALEGDNVVSRSENMPWYK------------GPTLLEHLETVEIAS 209
tufA CHL00071
elongation factor Tu
 1-225 6.95e-30

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 115.05  E-value: 6.95e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppySETRFEEIKKEVSSYIKK 80
Cdd:CHL00071   91 NMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKEDQVD---DEELLELVELEVRELLSK 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  81 IGYNPAAVAFVPISGWNGdnmLEVSEKMPwfkgwAVERKEGKADGKC--LIEALDAILP-PSRPTDKALRLPLQDVYKIG 157
Cdd:CHL00071  161 YDFPGDDIPIVSGSALLA---LEALTENP-----KIKRGENKWVDKIynLMDAVDSYIPtPERDTDKPFLMAIEDVFSIT 232

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1129799276 158 GIGTVPVGRVETGLLKPG---MVVVFAPANITTeVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 225
Cdd:CHL00071  233 GRGTVATGRIERGTVKVGdtvEIVGLRETKTTT-VTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMV 302
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-225 2.35e-29

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 113.36  E-value: 2.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTE-PPYSETRFEEIKKEVSSYik 79
Cdd:PRK00049   91 NMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVDdEELLELVEMEVRELLSKY-- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  80 kigynpaavafvpisGWNGDNMlevsekmPWFKGWAVERKEGKADGKC------LIEALDAILP-PSRPTDKALRLPLQD 152
Cdd:PRK00049  162 ---------------DFPGDDT-------PIIRGSALKALEGDDDEEWekkileLMDAVDSYIPtPERAIDKPFLMPIED 219

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1129799276 153 VYKIGGIGTVPVGRVETGLLKPGMVV--VFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 225
Cdd:PRK00049  220 VFSISGRGTVVTGRVERGIIKVGEEVeiVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQV 294
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-225 8.93e-29

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


Pssm-ID: 439820 [Multi-domain]  Cd Length: 396  Bit Score: 111.78  E-value: 8.93e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEPPY-SETRFEEIKKEVSSYik 79
Cdd:COG0050    91 NMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVDDEElLELVEMEVRELLSKY-- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  80 kigynpaavafvpisGWNGDNmlevsekMPWFKGWAVERKEGKADGKC------LIEALDAILP-PSRPTDKALRLPLQD 152
Cdd:COG0050   162 ---------------GFPGDD-------TPIIRGSALKALEGDPDPEWekkileLMDAVDSYIPePERDTDKPFLMPVED 219

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1129799276 153 VYKIGGIGTVPVGRVETGLLKPG---MVVVFAPANITTeVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 225
Cdd:COG0050   220 VFSITGRGTVVTGRVERGIIKVGdevEIVGIRDTQKTV-VTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQV 294
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-225 1.03e-28

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 111.85  E-value: 1.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSETRFE-EIKKEVSSYik 79
Cdd:PRK12735   91 NMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEmEVRELLSKY-- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  80 kigynpaavafvpisGWNGDNMlevsekmPWFKGWAVERKEGKADGKC------LIEALDAILP-PSRPTDKALRLPLQD 152
Cdd:PRK12735  162 ---------------DFPGDDT-------PIIRGSALKALEGDDDEEWeakileLMDAVDSYIPePERAIDKPFLMPIED 219

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1129799276 153 VYKIGGIGTVPVGRVETGLLKPGMVV--VFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 225
Cdd:PRK12735  220 VFSISGRGTVVTGRVERGIVKVGDEVeiVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQV 294
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-225 1.12e-28

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 112.23  E-value: 1.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSETRFEEIKKEVSSYIKk 80
Cdd:PLN03127  140 NMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYK- 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  81 igynpaavafvpisgWNGDNMlevsekmPWFKGWAVERKEGKAD--GKC----LIEALDAILP-PSRPTDKALRLPLQDV 153
Cdd:PLN03127  212 ---------------FPGDEI-------PIIRGSALSALQGTNDeiGKNailkLMDAVDEYIPePVRVLDKPFLMPIEDV 269

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1129799276 154 YKIGGIGTVPVGRVETGLLKPG----MVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 225
Cdd:PLN03127  270 FSIQGRGTVATGRVEQGTIKVGeeveIVGLRPGGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQV 345
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-225 2.27e-28

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 110.80  E-value: 2.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSETRFE-EIKKEVSSYik 79
Cdd:PRK12736   91 NMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEmEVRELLSEY-- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  80 kigynpaavafvpisGWNGDNMlevsekmPWFKGWAVERKEGKADG----KCLIEALDAILP-PSRPTDKALRLPLQDVY 154
Cdd:PRK12736  162 ---------------DFPGDDI-------PVIRGSALKALEGDPKWedaiMELMDAVDEYIPtPERDTDKPFLMPVEDVF 219

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1129799276 155 KIGGIGTVPVGRVETGLLKPG--MVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 225
Cdd:PRK12736  220 TITGRGTVVTGRVERGTVKVGdeVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQV 292
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-225 3.79e-28

translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]


Pssm-ID: 129576 [Multi-domain]  Cd Length: 394  Bit Score: 110.25  E-value: 3.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMD-STEPPYSETRFEEIKKEVSSYik 79
Cdd:TIGR00485  91 NMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDmVDDEELLELVEMEVRELLSQY-- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  80 kigynpaavafvpisGWNGDNMlevsekmPWFKGWAVERKEGKADGKC----LIEALDAILP-PSRPTDKALRLPLQDVY 154
Cdd:TIGR00485 162 ---------------DFPGDDT-------PIIRGSALKALEGDAEWEAkileLMDAVDEYIPtPEREIDKPFLLPIEDVF 219

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1129799276 155 KIGGIGTVPVGRVETGLLKPGMVV--VFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 225
Cdd:TIGR00485 220 SITGRGTVVTGRVERGIIKVGEEVeiVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMV 292
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-104 2.87e-26

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 100.68  E-value: 2.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFTLGVKqLIVGVNKMDSTeppySETRFEEIKKEVSS-YIK 79
Cdd:pfam00009  85 EVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV----DGAELEEVVEEVSReLLE 152

                          90       100
                  ....*....|....*....|....*
gi 1129799276  80 KIGYNPAAVAFVPISGWNGDNMLEV 104
Cdd:pfam00009 153 KYGEDGEFVPVVPGSALKGEGVQTL 177
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-225 5.48e-26

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 105.08  E-value: 5.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppySETRFEEIKKEVSSYIKK 80
Cdd:PLN03126  160 NMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD---DEELLELVELEVRELLSS 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  81 IGYNPAAVafvPISGWNGDNMLEVSEKMPwfkgwAVERKEGKADGKC--LIEALDAILP-PSRPTDKALRLPLQDVYKIG 157
Cdd:PLN03126  230 YEFPGDDI---PIISGSALLALEALMENP-----NIKRGDNKWVDKIyeLMDAVDSYIPiPQRQTDLPFLLAVEDVFSIT 301

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276 158 GIGTVPVGRVETGLLKPGMVV--VFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 225
Cdd:PLN03126  302 GRGTVATGRVERGTVKVGETVdiVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMV 371
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 1-225 6.48e-24

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 99.99  E-value: 6.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAgtgefEAGISKngQTREH-ALLAFtLGVKQLIVGVNKMDSTEPpyseTRFEEIKKEVSSYIK 79
Cdd:COG3276    67 NMLAGAGGIDLVLLVVAA-----DEGVMP--QTREHlAILDL-LGIKRGIVVLTKADLVDE----EWLELVEEEIRELLA 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  80 KIGYNPAAVafVPISgwngdnmlevsekmpwfkgwAVErKEGKADgkcLIEALDAIL--PPSRPTDKALRLPLQDVYKIG 157
Cdd:COG3276   135 GTFLEDAPI--VPVS--------------------AVT-GEGIDE---LRAALDALAaaVPARDADGPFRLPIDRVFSIK 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1129799276 158 GIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 225
Cdd:COG3276   189 GFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDV 256
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 1-226 1.10e-19

selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]


Pssm-ID: 129567 [Multi-domain]  Cd Length: 581  Bit Score: 87.62  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppysETRFEEIKKEVSSYIKK 80
Cdd:TIGR00475  66 NAIAGGGGIDAALLVVDADEGVMT-------QTGEHLAVLDLLGIPHTIVVITKADRVN----EEEIKRTEMFMKQILNS 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  81 IGYNPAAVAFVpISGWNGDNMLEVSEKMpwfkgwaverkegkadgKCLIEALDAilppsRPTDKALRLPLQDVYKIGGIG 160
Cdd:TIGR00475 135 YIFLKNAKIFK-TSAKTGQGIGELKKEL-----------------KNLLESLDI-----KRIQKPLRMAIDRAFKVKGAG 191

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1129799276 161 TVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFVA 226
Cdd:TIGR00475 192 TVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLI 257
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 146-225 1.51e-19

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: 80.00  E-value: 1.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276 146 LRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNvsVKELRRGFV 225
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 146-225 2.04e-17

Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.


Pssm-ID: 293897 [Multi-domain]  Cd Length: 83  Bit Score: 74.49  E-value: 2.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276 146 LRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 225
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-103 1.24e-16

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 75.02  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFtLGVKQLIVGVNKMDSTeppySETRFEEIKKEVSSYIKK 80
Cdd:cd00881    78 ETVRGLAQADGALLVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAVNKIDRV----GEEDFDEVLREIKELLKL 145

                          90       100
                  ....*....|....*....|....*.
gi 1129799276  81 IGY---NPAAVAFVPISGWNGDNMLE 103
Cdd:cd00881   146 IGFtflKGKDVPIIPISALTGEGIEE 171
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 148-225 1.25e-15

Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.


Pssm-ID: 293898 [Multi-domain]  Cd Length: 87  Bit Score: 69.85  E-value: 1.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276 148 LPLQDVYKIGGIGTVPVGRVETGLLKPGMVV--VFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 225
Cdd:cd03697     3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEVeiVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 160-225 1.64e-15

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: 68.83  E-value: 1.64e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1129799276 160 GTVPVGRVETGLLKPGMVVVFAPA-----NITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 225
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNgtgkkKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 146-228 7.42e-14

Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.


Pssm-ID: 293912 [Multi-domain]  Cd Length: 84  Bit Score: 64.84  E-value: 7.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276 146 LRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 225
Cdd:cd16267     2 FRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGSI 81


                  ...
gi 1129799276 226 AGD 228
Cdd:cd16267    82 LCD 84
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-138 8.96e-14

Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.


Pssm-ID: 206671 [Multi-domain]  Cd Length: 195  Bit Score: 67.61  E-value: 8.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppySETRFEEIKKEVSSYIKK 80
Cdd:cd01884    81 NMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMVD---DEELLELVEMEVRELLSK 150

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1129799276  81 IGYnpaavafvpisgwNGDNmlevsekMPWFKGWAVERKEGKADGKC------LIEALDAILPP 138
Cdd:cd01884   151 YGF-------------DGDD-------TPIVRGSALKALEGDDPNKWvdkileLLDALDSYIPT 194
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 146-225 1.57e-11

Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.


Pssm-ID: 293906 [Multi-domain]  Cd Length: 82  Bit Score: 58.65  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276 146 LRLPLQDVYKigGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 225
Cdd:cd04089     2 LRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGFV 79
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 152-225 1.15e-10

Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.


Pssm-ID: 293895 [Multi-domain]  Cd Length: 87  Bit Score: 56.46  E-value: 1.15e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1129799276 152 DVYKIGGIGTVPVGRVETGLLKPGMVVVFAPAN----ITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 225
Cdd:cd03694     7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 146-228 1.34e-10

Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 293899 [Multi-domain]  Cd Length: 84  Bit Score: 56.36  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276 146 LRLPLQDVYKiGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMH-HEALTEAVPGDNVGFNVKNVSVKELRRGF 224
Cdd:cd03698     2 FRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPGD 80


                  ....
gi 1129799276 225 VAGD 228
Cdd:cd03698    81 ILSS 84
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 1-106 1.14e-08

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 52.99  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAgtgefEAGISKngQTREHALLAFTLGVKQLIVGVNKMDSTEPPysetRFEEIKKEVSSYIKK 80
Cdd:cd04171    66 NMLAGAGGIDAVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLVDED----RLELVEEEILELLAG 134

                          90       100
                  ....*....|....*....|....*.
gi 1129799276  81 IGYNPAAVafVPISGWNGDNMLEVSE 106
Cdd:cd04171   135 TFLADAPI--FPVSSVTGEGIEELKN 158
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 146-210 2.51e-08

Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.


Pssm-ID: 293896 [Multi-domain]  Cd Length: 81  Bit Score: 49.87  E-value: 2.51e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1129799276 146 LRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGF 210
Cdd:cd03695     1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTL 65
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 2-209 1.32e-04

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 42.53  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   2 MITGTSQADCAVLIVAAGTGEFEAgiskngQTREHaLLAFT-LGVKQLIVGVNKMDSTEPPYSETRFEEIKKEVSSYIkk 80
Cdd:PRK04000  102 MLSGAALMDGAILVIAANEPCPQP------QTKEH-LMALDiIGIKNIVIVQNKIDLVSKERALENYEQIKEFVKGTV-- 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  81 igynpAAVA-FVPISGWNGDNMlevsekmpwfkgwaverkegkadgKCLIEALDAILP-PSRPTDKALRLPLQ---DVYK 155
Cdd:PRK04000  173 -----AENApIIPVSALHKVNI------------------------DALIEAIEEEIPtPERDLDKPPRMYVArsfDVNK 223

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1129799276 156 --------IGGI--GTVPVGRVETG---LLKPGMVVVFAPAN----ITTEVKSVEMHHEALTEAVPGDNVG 209
Cdd:PRK04000  224 pgtppeklKGGVigGSLIQGVLKVGdeiEIRPGIKVEEGGKTkwepITTKIVSLRAGGEKVEEARPGGLVG 294
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 151-209 2.52e-04

Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2.


Pssm-ID: 293910 [Multi-domain]  Cd Length: 80  Bit Score: 38.81  E-value: 2.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1129799276 151 QDVYKIGGiGTVPVGRVETGLLKPGMVVVfaPANITTEVKSVEMHHEALTEAVPGDNVG 209
Cdd:cd16265     6 EKVFKILG-RQVLTGEVESGVIYVGYKVK--GDKGVALIRAIEREHRKVDFAVAGDEVA 61
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 1-223 2.81e-04

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 41.58  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   1 NMITGTSQADCAVLIVAAGTGEFeagisknGQTREH-ALLAFTlGVKQLIVGVNKMDSTEPPysetRFEEIKKEVSSYIK 79
Cdd:PRK10512   67 NMLAGVGGIDHALLVVACDDGVM-------AQTREHlAILQLT-GNPMLTVALTKADRVDEA----RIAEVRRQVKAVLR 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  80 KIGYnPAAVAFVPisgwngdnmlevsekmpwfkgwAVERKEGkadgkclIEALDAIL----PPSRPTDKALRLPLQDVYK 155
Cdd:PRK10512  135 EYGF-AEAKLFVT----------------------AATEGRG-------IDALREHLlqlpEREHAAQHRFRLAIDRAFT 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1129799276 156 IGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVK-NVSVKELRRG 223
Cdd:PRK10512  185 VKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIAgDAEKEQINRG 253
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 5-108 1.00e-03

Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 38.61  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   5 GTSQADCAVLIVAAGTGeFEAgiskngQTRE---HALLAFTlgvkQLIVGVNKMDstEPPYSETRFEEIKKEVSSY---I 78
Cdd:cd01887    69 GASVTDIAILVVAADDG-VMP------QTIEainHAKAANV----PIIVAINKID--KPYGTEADPERVKNELSELglvG 135

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1129799276  79 KKIGYNpaaVAFVPISGWNGDNM-------LEVSEKM 108
Cdd:cd01887   136 EEWGGD---VSIVPISAKTGEGIddlleaiLLLAEVL 169
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 2-109 1.03e-03

Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 39.17  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   2 MITGTSQADCAVLIVAAgtgefeagiskN-----GQTREHaLLAF-TLGVKQLIVGVNKMDSTEPPYSETRFEEIKKevs 75
Cdd:cd01888    94 MLSGAAVMDGALLLIAA-----------NepcpqPQTSEH-LAALeIMGLKHIIILQNKIDLVKEEQALENYEQIKE--- 158

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1129799276  76 sYIKKIGYNPAAVafVPIS---GWNGDNMLEVSEKMP 109
Cdd:cd01888   159 -FVKGTIAENAPI--IPISaqlKYNIDVLCEYIVKKI 192
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 2-205 7.34e-03

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 37.29  E-value: 7.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276   2 MITGTSQADCAVLIVAAgtgefeagiskN-----GQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSETRFEEIKKEVSS 76
Cdd:PTZ00327  134 MLNGAAVMDAALLLIAA-----------NescpqPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKG 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129799276  77 YIKKigynpaAVAFVPIS---GWNGDNMLE-VSEKMPwfkgwaVERKEGKADGK-CLIEALDAILPPSRPtdKALRlplq 151
Cdd:PTZ00327  203 TIAD------NAPIIPISaqlKYNIDVVLEyICTQIP------IPKRDLTSPPRmIVIRSFDVNKPGEDI--ENLK---- 264

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1129799276 152 dvykiggiGTVPVGRVETGLLK--------PGMVVVFAPANIT-----TEVKSVEMHHEALTEAVPG 205
Cdd:PTZ00327  265 --------GGVAGGSILQGVLKvgdeieirPGIISKDSGGEFTcrpirTRIVSLFAENNELQYAVPG 323
 
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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