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Conserved domains on  [gi|1327839087|ref|WP_102137509|]
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MULTISPECIES: GTPase Era [Providencia]

Protein Classification

GTPase Era( domain architecture ID 11439328)

GTPase Era is an essential protein that binds the 16S rRNA of the 30S subunit, couples cell growth with cytokinesis, and plays a role in cell division and energy metabolism

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
7-297 1.71e-180

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 499.13  E-value: 1.71e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087   7 HCGFVAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLHiEEKRAINRLMNRAASSSI 86
Cdd:COG1159     2 RSGFVAIVGRPNVGKSTLLNALVGQKVSIVSPKPQTTRHRIRGIVTREDAQIVFVDTPGIH-KPKRKLGRRMNKAAWSAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  87 GDVELVIFVVEGTN-WTADDEMVLTKLSSLRCPVILAINKIDNVtDKTVLLPHIGMISQKMNFLDVVPISAEKGVGVDTI 165
Cdd:COG1159    81 EDVDVILFVVDATEkIGEGDEFILELLKKLKTPVILVINKIDLV-KKEELLPLLAEYSELLDFAEIVPISALKGDNVDEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087 166 AKIVKQHIPEAVHHFPEDYITDRSQRFMASEIIREKLMRFLGDELPYSVTVEIEQFKVTDvGIYHINGLILVEREGQKKM 245
Cdd:COG1159   160 LDEIAKLLPEGPPYYPEDQITDRPERFLAAEIIREKILRLLRDELPYSVAVEIEEFEERE-GLLRIRATIYVERDSQKGI 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1327839087 246 VIGNKGSKLKTIGTEARIDMERMFDNKVHLELWVKVKSGWADDERALRSLGY 297
Cdd:COG1159   239 IIGKGGSMLKKIGTEARKDIEKLLGKKVFLELWVKVKKNWRDDERALRELGY 290
 
Name Accession Description Interval E-value
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
7-297 1.71e-180

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 499.13  E-value: 1.71e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087   7 HCGFVAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLHiEEKRAINRLMNRAASSSI 86
Cdd:COG1159     2 RSGFVAIVGRPNVGKSTLLNALVGQKVSIVSPKPQTTRHRIRGIVTREDAQIVFVDTPGIH-KPKRKLGRRMNKAAWSAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  87 GDVELVIFVVEGTN-WTADDEMVLTKLSSLRCPVILAINKIDNVtDKTVLLPHIGMISQKMNFLDVVPISAEKGVGVDTI 165
Cdd:COG1159    81 EDVDVILFVVDATEkIGEGDEFILELLKKLKTPVILVINKIDLV-KKEELLPLLAEYSELLDFAEIVPISALKGDNVDEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087 166 AKIVKQHIPEAVHHFPEDYITDRSQRFMASEIIREKLMRFLGDELPYSVTVEIEQFKVTDvGIYHINGLILVEREGQKKM 245
Cdd:COG1159   160 LDEIAKLLPEGPPYYPEDQITDRPERFLAAEIIREKILRLLRDELPYSVAVEIEEFEERE-GLLRIRATIYVERDSQKGI 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1327839087 246 VIGNKGSKLKTIGTEARIDMERMFDNKVHLELWVKVKSGWADDERALRSLGY 297
Cdd:COG1159   239 IIGKGGSMLKKIGTEARKDIEKLLGKKVFLELWVKVKKNWRDDERALRELGY 290
era PRK00089
GTPase Era; Reviewed
7-297 1.45e-179

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 496.88  E-value: 1.45e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087   7 HCGFVAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLHiEEKRAINRLMNRAASSSI 86
Cdd:PRK00089    4 KSGFVAIVGRPNVGKSTLLNALVGQKISIVSPKPQTTRHRIRGIVTEDDAQIIFVDTPGIH-KPKRALNRAMNKAAWSSL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  87 GDVELVIFVVEGTN-WTADDEMVLTKLSSLRCPVILAINKIDNVTDKTVLLPHIGMISQKMNFLDVVPISAEKGVGVDTI 165
Cdd:PRK00089   83 KDVDLVLFVVDADEkIGPGDEFILEKLKKVKTPVILVLNKIDLVKDKEELLPLLEELSELMDFAEIVPISALKGDNVDEL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087 166 AKIVKQHIPEAVHHFPEDYITDRSQRFMASEIIREKLMRFLGDELPYSVTVEIEQFKVTdvGIYHINGLILVEREGQKKM 245
Cdd:PRK00089  163 LDVIAKYLPEGPPYYPEDQITDRPERFLAAEIIREKLLRLLGDELPYSVAVEIEKFEER--GLVRIEATIYVERDSQKGI 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1327839087 246 VIGNKGSKLKTIGTEARIDMERMFDNKVHLELWVKVKSGWADDERALRSLGY 297
Cdd:PRK00089  241 IIGKGGAMLKKIGTEARKDIEKLLGKKVFLELWVKVKKGWRDDEKALRELGY 292
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
9-280 3.83e-137

GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other bacteria. It plays a role in ribosome biogenesis. Few bacteria lack this protein. [Protein synthesis, Other]


Pssm-ID: 129528 [Multi-domain]  Cd Length: 270  Bit Score: 388.67  E-value: 3.83e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087   9 GFVAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLHiEEKRAINRLMNRAASSSIGD 88
Cdd:TIGR00436   1 GFVAILGRPNVGKSTLLNQLHGQKISITSPKAQTTRNRISGIHTTGASQIIFIDTPGFH-EKKHSLNRLMMKEARSAIGG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  89 VELVIFVVEGTNWTADDEMVLTKLSSLRCPVILAINKIDNVTdKTVLLPHIGMISQKMNFLDVVPISAEKGVGVDTIAKI 168
Cdd:TIGR00436  80 VDLILFVVDSDQWNGDGEFVLTKLQNLKRPVVLTRNKLDNKF-KDKLLPLIDKYAILEDFKDIVPISALTGDNTSFLAAF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087 169 VKQHIPEAVHHFPEDYITDRSQRFMASEIIREKLMRFLGDELPYSVTVEIEQFKVTDVGIYHINGLILVEREGQKKMVIG 248
Cdd:TIGR00436 159 IEVHLPEGPFRYPEDYVTDQPDRFKISEIIREKIIRYTKEEIPHSVRVEIERKSFNEKGLLKIHALISVERESQKKIIIG 238
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1327839087 249 NKGSKLKTIGTEARIDMERMFDNKVHLELWVK 280
Cdd:TIGR00436 239 KNGSMIKAIGIAARKDILELFDCDVFLELFVK 270
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
7-172 6.75e-84

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 249.69  E-value: 6.75e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087   7 HCGFVAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLHIEEKRAINRlMNRAASSSI 86
Cdd:cd04163     2 KSGFVAIIGRPNVGKSTLLNALVGQKISIVSPKPQTTRNRIRGIYTDDDAQIIFVDTPGIHKPKKKLGER-MVKAAWSAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  87 GDVELVIFVVEGTNW-TADDEMVLTKLSSLRCPVILAINKIDNVTDKTVLLPHIGMISQKMNFLDVVPISAEKGVGVDTI 165
Cdd:cd04163    81 KDVDLVLFVVDASEWiGEGDEFILELLKKSKTPVILVLNKIDLVKDKEDLLPLLEKLKELHPFAEIFPISALKGENVDEL 160

                  ....*..
gi 1327839087 166 AKIVKQH 172
Cdd:cd04163   161 LEYIVEY 167
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
10-125 1.30e-29

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 108.48  E-value: 1.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  10 FVAIVGRPNVGKSTLLNQLLGQKvSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLhIEEkrAINRLMNRAASSSIGDV 89
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK-AIVSDYPGTTRDPNEGRLELKGKQIILVDTPGL-IEG--ASEGEGLGRAFLAIIEA 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1327839087  90 ELVIFVVEGTN-WTADDEMVLTKLSSLRCPVILAINK 125
Cdd:pfam01926  77 DLILFVVDSEEgITPLDEELLELLRENKKPIILVLNK 113
 
Name Accession Description Interval E-value
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
7-297 1.71e-180

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 499.13  E-value: 1.71e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087   7 HCGFVAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLHiEEKRAINRLMNRAASSSI 86
Cdd:COG1159     2 RSGFVAIVGRPNVGKSTLLNALVGQKVSIVSPKPQTTRHRIRGIVTREDAQIVFVDTPGIH-KPKRKLGRRMNKAAWSAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  87 GDVELVIFVVEGTN-WTADDEMVLTKLSSLRCPVILAINKIDNVtDKTVLLPHIGMISQKMNFLDVVPISAEKGVGVDTI 165
Cdd:COG1159    81 EDVDVILFVVDATEkIGEGDEFILELLKKLKTPVILVINKIDLV-KKEELLPLLAEYSELLDFAEIVPISALKGDNVDEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087 166 AKIVKQHIPEAVHHFPEDYITDRSQRFMASEIIREKLMRFLGDELPYSVTVEIEQFKVTDvGIYHINGLILVEREGQKKM 245
Cdd:COG1159   160 LDEIAKLLPEGPPYYPEDQITDRPERFLAAEIIREKILRLLRDELPYSVAVEIEEFEERE-GLLRIRATIYVERDSQKGI 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1327839087 246 VIGNKGSKLKTIGTEARIDMERMFDNKVHLELWVKVKSGWADDERALRSLGY 297
Cdd:COG1159   239 IIGKGGSMLKKIGTEARKDIEKLLGKKVFLELWVKVKKNWRDDERALRELGY 290
era PRK00089
GTPase Era; Reviewed
7-297 1.45e-179

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 496.88  E-value: 1.45e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087   7 HCGFVAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLHiEEKRAINRLMNRAASSSI 86
Cdd:PRK00089    4 KSGFVAIVGRPNVGKSTLLNALVGQKISIVSPKPQTTRHRIRGIVTEDDAQIIFVDTPGIH-KPKRALNRAMNKAAWSSL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  87 GDVELVIFVVEGTN-WTADDEMVLTKLSSLRCPVILAINKIDNVTDKTVLLPHIGMISQKMNFLDVVPISAEKGVGVDTI 165
Cdd:PRK00089   83 KDVDLVLFVVDADEkIGPGDEFILEKLKKVKTPVILVLNKIDLVKDKEELLPLLEELSELMDFAEIVPISALKGDNVDEL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087 166 AKIVKQHIPEAVHHFPEDYITDRSQRFMASEIIREKLMRFLGDELPYSVTVEIEQFKVTdvGIYHINGLILVEREGQKKM 245
Cdd:PRK00089  163 LDVIAKYLPEGPPYYPEDQITDRPERFLAAEIIREKLLRLLGDELPYSVAVEIEKFEER--GLVRIEATIYVERDSQKGI 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1327839087 246 VIGNKGSKLKTIGTEARIDMERMFDNKVHLELWVKVKSGWADDERALRSLGY 297
Cdd:PRK00089  241 IIGKGGAMLKKIGTEARKDIEKLLGKKVFLELWVKVKKGWRDDEKALRELGY 292
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
9-280 3.83e-137

GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other bacteria. It plays a role in ribosome biogenesis. Few bacteria lack this protein. [Protein synthesis, Other]


Pssm-ID: 129528 [Multi-domain]  Cd Length: 270  Bit Score: 388.67  E-value: 3.83e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087   9 GFVAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLHiEEKRAINRLMNRAASSSIGD 88
Cdd:TIGR00436   1 GFVAILGRPNVGKSTLLNQLHGQKISITSPKAQTTRNRISGIHTTGASQIIFIDTPGFH-EKKHSLNRLMMKEARSAIGG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  89 VELVIFVVEGTNWTADDEMVLTKLSSLRCPVILAINKIDNVTdKTVLLPHIGMISQKMNFLDVVPISAEKGVGVDTIAKI 168
Cdd:TIGR00436  80 VDLILFVVDSDQWNGDGEFVLTKLQNLKRPVVLTRNKLDNKF-KDKLLPLIDKYAILEDFKDIVPISALTGDNTSFLAAF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087 169 VKQHIPEAVHHFPEDYITDRSQRFMASEIIREKLMRFLGDELPYSVTVEIEQFKVTDVGIYHINGLILVEREGQKKMVIG 248
Cdd:TIGR00436 159 IEVHLPEGPFRYPEDYVTDQPDRFKISEIIREKIIRYTKEEIPHSVRVEIERKSFNEKGLLKIHALISVERESQKKIIIG 238
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1327839087 249 NKGSKLKTIGTEARIDMERMFDNKVHLELWVK 280
Cdd:TIGR00436 239 KNGSMIKAIGIAARKDILELFDCDVFLELFVK 270
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
7-172 6.75e-84

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 249.69  E-value: 6.75e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087   7 HCGFVAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLHIEEKRAINRlMNRAASSSI 86
Cdd:cd04163     2 KSGFVAIIGRPNVGKSTLLNALVGQKISIVSPKPQTTRNRIRGIYTDDDAQIIFVDTPGIHKPKKKLGER-MVKAAWSAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  87 GDVELVIFVVEGTNW-TADDEMVLTKLSSLRCPVILAINKIDNVTDKTVLLPHIGMISQKMNFLDVVPISAEKGVGVDTI 165
Cdd:cd04163    81 KDVDLVLFVVDASEWiGEGDEFILELLKKSKTPVILVLNKIDLVKDKEDLLPLLEKLKELHPFAEIFPISALKGENVDEL 160

                  ....*..
gi 1327839087 166 AKIVKQH 172
Cdd:cd04163   161 LEYIVEY 167
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
12-171 4.43e-42

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 142.77  E-value: 4.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  12 AIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRI---MGIHTEDNYQIIyvDTPGLHieEKRAINRLMNRAASSSIGD 88
Cdd:cd00880     1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVrkeWELLPLGPVVLI--DTPGLD--EEGGLGRERVEEARQVADR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  89 VELVIFVVEGTNWTADDEMVLTKLSSLRCPVILAINKIDNVTDKTVLLPHIGMISQKMNFLDVVPISAEKGVGVDTI-AK 167
Cdd:cd00880    77 ADLVLLVVDSDLTPVEEEAKLGLLRERGKPVLLVLNKIDLVPESEEEELLRERKLELLPDLPVIAVSALPGEGIDELrKK 156

                  ....
gi 1327839087 168 IVKQ 171
Cdd:cd00880   157 IAEL 160
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
8-170 2.18e-38

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 133.27  E-value: 2.18e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087   8 CGFVAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDN--YQIIYVDTPGlhIEEKRAINRLMNRAASSS 85
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEDGktYKFNLLDTAG--QEDYDAIRRLYYPQVERS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  86 IGDVELVIFVVEGTNWTADDEMVLTKLSSLRCPVILAINKIDNVTDKtvLLPHIGMISQKMNFLDVVPISAEKGVGVDTI 165
Cdd:TIGR00231  79 LRVFDIVILVLDVEEILEKQTKEIIHHADSGVPIILVGNKIDLKDAD--LKTHVASEFAKLNGEPIIPLSAETGKNIDSA 156

                  ....*
gi 1327839087 166 AKIVK 170
Cdd:TIGR00231 157 FKIVE 161
KH-II_Era cd22534
type II K-homology (KH) RNA-binding domain found in GTPase Era and similar proteins; GTPase ...
195-281 2.16e-36

type II K-homology (KH) RNA-binding domain found in GTPase Era and similar proteins; GTPase Era, also called ERA or GTP-binding protein Era, is an essential GTPase that binds both GDP and GTP, with nucleotide exchange occurring in the order of seconds whereas hydrolysis occurs in the order of minutes. It plays a role in numerous processes, including cell cycle regulation, energy metabolism, as a chaperone for 16S rRNA processing, and 30S ribosomal subunit biogenesis. Its presence in the 30S subunit may prevent translation initiation. GTPase Era may also be critical for maintaining cell growth and cell division rates. Members of this family contain only one canonical type II K-homology (KH) domain that has the signature motif GXXG (where X represents any amino acid).


Pssm-ID: 411791 [Multi-domain]  Cd Length: 87  Bit Score: 125.25  E-value: 2.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087 195 SEIIREKLMRFLGDELPYSVTVEIEQFKVTDVGIYHINGLILVEREGQKKMVIGNKGSKLKTIGTEARIDMERMFDNKVH 274
Cdd:cd22534     1 AEIIREKLLELLRQELPYSVAVEIEEWEEREDGSLRIEAEIIVEKESQKKIIIGKGGATIKKIGIEARKDLEKLFGRKVY 80

                  ....*..
gi 1327839087 275 LELWVKV 281
Cdd:cd22534    81 LKLWVKV 87
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
12-171 3.90e-33

EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206681 [Multi-domain]  Cd Length: 157  Bit Score: 119.08  E-value: 3.90e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  12 AIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLHIEEKRaINRLMNRAASSSIGDVEL 91
Cdd:cd01894     1 AIVGRPNVGKSTLFNRLTGRRDAIVSDTPGVTRDRKYGEAEWGGREFILIDTGGIEPDDEG-ISKEIREQAEIAIEEADV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  92 VIFVVEGTN-WTADDEMVLTKLSSLRCPVILAINKIDNVTDKTVLLPhigmiSQKMNFLDVVPISAEKGVGVDT-IAKIV 169
Cdd:cd01894    80 ILFVVDGREgLTPADEEIAKYLRKSKKPVILVVNKIDNIKEEEEAAE-----FYSLGFGEPIPISAEHGRGIGDlLDAIL 154

                  ..
gi 1327839087 170 KQ 171
Cdd:cd01894   155 EL 156
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
11-176 4.34e-31

Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 120.51  E-value: 4.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLHIEEKRAINRLMNRAASSSIGDVE 90
Cdd:COG1160     5 VAIVGRPNVGKSTLFNRLTGRRDAIVDDTPGVTRDRIYGEAEWGGREFTLIDTGGIEPDDDDGLEAEIREQAELAIEEAD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  91 LVIFVVEGTN-WTADDEMVLTKLSSLRCPVILAINKIDNVTDKTVLLP--HIGmisqkmnFLDVVPISAEKGVGVDTIAK 167
Cdd:COG1160    85 VILFVVDGRAgLTPLDEEIAKLLRRSGKPVILVVNKVDGPKREADAAEfySLG-------LGEPIPISAEHGRGVGDLLD 157

                  ....*....
gi 1327839087 168 IVKQHIPEA 176
Cdd:COG1160   158 AVLELLPEE 166
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
11-185 3.43e-30

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 117.84  E-value: 3.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLHIEEKrAINRLMNRAASSSIGDVE 90
Cdd:PRK00093    4 VAIVGRPNVGKSTLFNRLTGKRDAIVADTPGVTRDRIYGEAEWLGREFILIDTGGIEPDDD-GFEKQIREQAELAIEEAD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  91 LVIFVVEGTNW-TADDEMVLTKLSSLRCPVILAINKIDNVTDKTVLLPhigmiSQKMNFLDVVPISAEKGVGVDT-IAKI 168
Cdd:PRK00093   83 VILFVVDGRAGlTPADEEIAKILRKSNKPVILVVNKVDGPDEEADAYE-----FYSLGLGEPYPISAEHGRGIGDlLDAI 157
                         170
                  ....*....|....*..
gi 1327839087 169 VKQHIPEAVHHFPEDYI 185
Cdd:PRK00093  158 LEELPEEEEEDEEDEPI 174
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
10-125 1.30e-29

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 108.48  E-value: 1.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  10 FVAIVGRPNVGKSTLLNQLLGQKvSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLhIEEkrAINRLMNRAASSSIGDV 89
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK-AIVSDYPGTTRDPNEGRLELKGKQIILVDTPGL-IEG--ASEGEGLGRAFLAIIEA 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1327839087  90 ELVIFVVEGTN-WTADDEMVLTKLSSLRCPVILAINK 125
Cdd:pfam01926  77 DLILFVVDSEEgITPLDEELLELLRENKKPIILVLNK 113
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
12-165 4.83e-28

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 106.00  E-value: 4.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  12 AIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRH--RIMGIHTEDNYQIIYVDTPGlhIEEKRAINRLmnRAASSSIGDV 89
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDpdVYVKELDKGKVKLVLVDTPG--LDEFGGLGRE--ELARLLLRGA 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327839087  90 ELVIFVVEGTNWTADDEMVLTKLSSLRC---PVILAINKIDNVTDKTVLLPHIGMISQKMNFLDVVPISAEKGVGVDTI 165
Cdd:cd00882    77 DLILLVVDSTDRESEEDAKLLILRRLRKegiPIILVGNKIDLLEEREVEELLRLEELAKILGVPVFEVSAKTGEGVDEL 155
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
11-191 2.86e-23

tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 98.98  E-value: 2.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRImgihTE----DNYQIIYVDTPGLH-----IEE---KRAINRlM 78
Cdd:COG0486   216 VVIVGRPNVGKSSLLNALLGEERAIVTDIAGTTRDVI----EEriniGGIPVRLIDTAGLRetedeVEKigiERAREA-I 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  79 NRAasssigdvELVIFVVEGTN-WTADDEMVLTKLSSLrcPVILAINKIDnvtdktvLLPHIGMISQKMNFLDVVPISAE 157
Cdd:COG0486   291 EEA--------DLVLLLLDASEpLTEEDEEILEKLKDK--PVIVVLNKID-------LPSEADGELKSLPGEPVIAISAK 353
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1327839087 158 KGVGVDTIAKIVKQHIPEAVHHFPEDYITDRSQR 191
Cdd:COG0486   354 TGEGIDELKEAILELVGEGALEGEGVLLTNARHR 387
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
11-163 3.04e-23

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 93.33  E-value: 3.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLHIE----EKRAINRLMNRAASSsi 86
Cdd:cd04164     6 VVIAGKPNVGKSSLLNALAGRDRAIVSDIAGTTRDVIEEEIDLGGIPVRLIDTAGLRETedeiEKIGIERAREAIEEA-- 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327839087  87 gdvELVIFVVEGTN-WTADDEMVLTKLSSLrcPVILAINKIDnvtdktvLLPHIGMISQKmNFLDVVPISAEKGVGVD 163
Cdd:cd04164    84 ---DLVLLVVDASEgLDEEDLEILELPAKK--PVIVVLNKSD-------LLSDAEGISEL-NGKPIIAISAKTGEGID 148
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
11-171 4.86e-23

Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 98.17  E-value: 4.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHrimGIHTE---DNYQIIYVDTPGL----HIE---EKRAINRlmnr 80
Cdd:COG1160   178 IAIVGRPNVGKSSLINALLGEERVIVSDIAGTTRD---SIDTPferDGKKYTLIDTAGIrrkgKVDegiEKYSVLR---- 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  81 aASSSIGDVELVIFVVEGT-NWTADDemvlTKLSSL----RCPVILAINKIDNVTDKTVLLPHI-GMISQKMNFLD---V 151
Cdd:COG1160   251 -TLRAIERADVVLLVIDATeGITEQD----LKIAGLaleaGKALVIVVNKWDLVEKDRKTREELeKEIRRRLPFLDyapI 325
                         170       180
                  ....*....|....*....|
gi 1327839087 152 VPISAEKGVGVDTIAKIVKQ 171
Cdd:COG1160   326 VFISALTGQGVDKLLEAVDE 345
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
11-171 1.75e-22

EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 91.73  E-value: 1.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGL----HIE---EKRAINRlmnraAS 83
Cdd:cd01895     5 IAIIGRPNVGKSSLLNALLGEERVIVSDIAGTTRDSIDVPFEYDGQKYTLIDTAGIrkkgKVTegiEKYSVLR-----TL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  84 SSIGDVELVIFVVEGT-NWTADDEMVLTKLSSLRCPVILAINKIDNVTDKTVLLPHI-GMISQKMNFLD---VVPISAEK 158
Cdd:cd01895    80 KAIERADVVLLVLDASeGITEQDLRIAGLILEEGKALIIVVNKWDLVEKDEKTMKEFeKELRRKLPFLDyapIVFISALT 159
                         170
                  ....*....|...
gi 1327839087 159 GVGVDTIAKIVKQ 171
Cdd:cd01895   160 GQGVDKLFDAIKE 172
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
11-171 2.31e-21

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 93.19  E-value: 2.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHrimGIHTE---DNYQIIYVDTPGL----HIE---EKRAINRLMNr 80
Cdd:PRK00093  176 IAIIGRPNVGKSSLINALLGEERVIVSDIAGTTRD---SIDTPferDGQKYTLIDTAGIrrkgKVTegvEKYSVIRTLK- 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  81 aassSIGDVELVIFVVEGTN-WTADDEmvltKLSSL----RCPVILAINKIDNVTDKTVLLpHIGMISQKMNFLD---VV 152
Cdd:PRK00093  252 ----AIERADVVLLVIDATEgITEQDL----RIAGLaleaGRALVIVVNKWDLVDEKTMEE-FKKELRRRLPFLDyapIV 322
                         170
                  ....*....|....*....
gi 1327839087 153 PISAEKGVGVDTIAKIVKQ 171
Cdd:PRK00093  323 FISALTGQGVDKLLEAIDE 341
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
11-191 7.73e-21

MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.


Pssm-ID: 463649 [Multi-domain]  Cd Length: 326  Bit Score: 90.62  E-value: 7.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRImgihtE-----DNYQIIYVDTPGLHIE----EKRAINRLMNRA 81
Cdd:pfam12631  97 VVIVGKPNVGKSSLLNALLGEERAIVTDIPGTTRDVI-----EetiniGGIPLRLIDTAGIRETddevEKIGIERAREAI 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  82 ASSsigdvELVIFVVEGTN-WTADDEMVLTKLSSlRCPVILAINKIDnvtdktvlLPHIGMISQKMNFLDVVPISAEKGV 160
Cdd:pfam12631 172 EEA-----DLVLLVLDASRpLDEEDLEILELLKD-KKPIIVVLNKSD--------LLGEIDELEELKGKPVLAISAKTGE 237
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1327839087 161 GVDTIAKIVKQHIPEAVHHFPEDYITDRSQR 191
Cdd:pfam12631 238 GLDELEEAIKELFLAGEIASDGPIITNARHK 268
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
11-191 3.19e-20

tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 90.17  E-value: 3.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRImgihtE-----DNYQIIYVDTPGLH-----IEE---KRAINRl 77
Cdd:PRK05291  218 VVIAGRPNVGKSSLLNALLGEERAIVTDIAGTTRDVI-----EehinlDGIPLRLIDTAGIRetddeVEKigiERSREA- 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  78 MNRAasssigdvELVIFVVEGTN-WTADDEMVLTKLSSLrcPVILAINKIDnvtdktvLLPHIGMISQkmNFLDVVPISA 156
Cdd:PRK05291  292 IEEA--------DLVLLVLDASEpLTEEDDEILEELKDK--PVIVVLNKAD-------LTGEIDLEEE--NGKPVIRISA 352
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1327839087 157 EKGVGVDTIAKIVKQHIPEAVHHFPED-YITdrSQR 191
Cdd:PRK05291  353 KTGEGIDELREAIKELAFGGFGGNQEGvFLT--NAR 386
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
11-173 1.17e-19

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 84.26  E-value: 1.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRKP----QTTRHRImgIHTEDNYQIIYVDTPGlhIEEKRAINRLMNRaassSI 86
Cdd:COG1100     6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLStngvTIDKKEL--KLDGLDVDLVIWDTPG--QDEFRETRQFYAR----QL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  87 GDVELVIFVVEGTNwTADDEMVLTKLSSLR-----CPVILAINKIDNVTDKTVLLPH--IGMISQKmNFLDVVPISAEKG 159
Cdd:COG1100    78 TGASLYLFVVDGTR-EETLQSLYELLESLRrlgkkSPIILVLNKIDLYDEEEIEDEErlKEALSED-NIVEVVATSAKTG 155
                         170
                  ....*....|....
gi 1327839087 160 VGVDTIAKIVKQHI 173
Cdd:COG1100   156 EGVEELFAALAEIL 169
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
9-176 4.62e-18

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 84.46  E-value: 4.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087   9 GFVAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLHIEEKrAINRLMNRAASSSIGD 88
Cdd:PRK09518  276 GVVAIVGRPNVGKSTLVNRILGRREAVVEDTPGVTRDRVSYDAEWAGTDFKLVDTGGWEADVE-GIDSAIASQAQIAVSL 354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  89 VELVIFVVEG-TNWTADDEMVLTKLSSLRCPVILAINKIDNVTDKtvllphiGMISQ--KMNFLDVVPISAEKGVGVDTI 165
Cdd:PRK09518  355 ADAVVFVVDGqVGLTSTDERIVRMLRRAGKPVVLAVNKIDDQASE-------YDAAEfwKLGLGEPYPISAMHGRGVGDL 427
                         170
                  ....*....|.
gi 1327839087 166 AKIVKQHIPEA 176
Cdd:PRK09518  428 LDEALDSLKVA 438
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
11-182 6.73e-18

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 83.48  E-value: 6.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLHIEEKrAINRLMNRAASSSIGDVE 90
Cdd:PRK03003   41 VAVVGRPNVGKSTLVNRILGRREAVVEDVPGVTRDRVSYDAEWNGRRFTVVDTGGWEPDAK-GLQASVAEQAEVAMRTAD 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  91 LVIFVVEGT-NWTADDEMVLTKLSSLRCPVILAINKIDNVT---DKTVLL------PHigmisqkmnfldvvPISAEKGV 160
Cdd:PRK03003  120 AVLFVVDATvGATATDEAVARVLRRSGKPVILAANKVDDERgeaDAAALWslglgePH--------------PVSALHGR 185
                         170       180
                  ....*....|....*....|...
gi 1327839087 161 GV-DTIAKIVKQhIPEAVHHFPE 182
Cdd:PRK03003  186 GVgDLLDAVLAA-LPEVPRVGSA 207
mnmE_trmE_thdF TIGR00450
tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF ...
11-206 2.53e-17

tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF (thiophene and furan oxidation protein), is a GTPase involved in tRNA modification to create 5-methylaminomethyl-2-thiouridine in the wobble position of some tRNAs. This protein and GidA form an alpha2/beta2 heterotetramer. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273083 [Multi-domain]  Cd Length: 442  Bit Score: 81.76  E-value: 2.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLHiEEKRAINRLMNRAASSSIGDVE 90
Cdd:TIGR00450 206 LAIVGSPNVGKSSLLNALLKQDRAIVSDIKGTTRDVVEGDFELNGILIKLLDTAGIR-EHADFVERLGIEKSFKAIKQAD 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  91 LVIFVVEGT-NWTADDEMVLTkLSSLRCPVILAINKIDNVTDKTVLLPHigmiSQKMNFLDVVPISAEKGVGVDTIAKIV 169
Cdd:TIGR00450 285 LVIYVLDASqPLTKDDFLIID-LNKSKKPFILVLNKIDLKINSLEFFVS----SKVLNSSNLSAKQLKIKALVDLLTQKI 359
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1327839087 170 KQHIPEAVHHFpEDYITDRSQRFMASEIIREKLMRFL 206
Cdd:TIGR00450 360 NAFYSKERVEL-DDYLISSWQAMILLEKAIAQLQQFL 395
KH_2 pfam07650
KH domain;
209-286 6.44e-17

KH domain;


Pssm-ID: 429574 [Multi-domain]  Cd Length: 78  Bit Score: 73.74  E-value: 6.44e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327839087 209 ELPYSVTVEIEQFKVTDVGI-YHINGLILVEREGQKKMVIGNKGSKLKTIGTEARIDMERMFDNKVHLELWvKVKSGWA 286
Cdd:pfam07650   1 EIPYSLAVELKFAGVSKVEIeRTPNAVIVVIRASQPGIVIGKGGSRIKKIGKELRKDIEKLLGKKVYLNIV-KVKKPWL 78
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
11-173 2.34e-16

YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 75.24  E-value: 2.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQK-VSITSRKPQTTRHrimgIHT-EDNYQIIYVDTPG-----LHIEEKRAINRLMNR--A 81
Cdd:cd01876     2 VAFAGRSNVGKSSLINALTNRKkLARTSKTPGRTQL----INFfNVGDKFRLVDLPGygyakVSKEVREKWGKLIEEylE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  82 ASSSIgdvELVIFVVEGTN-WTADDEMVLTKLSSLRCPVILAINKIDNVTDKTVLLpHIGMISQKMN----FLDVVPISA 156
Cdd:cd01876    78 NRENL---KGVVLLIDARHgPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAK-VLKKIKEELNlfniLPPVILFSS 153
                         170
                  ....*....|....*..
gi 1327839087 157 EKGVGVDTIAKIVKQHI 173
Cdd:cd01876   154 KKGTGIDELRALIAEWL 170
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
11-167 8.08e-16

Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.


Pssm-ID: 460552 [Multi-domain]  Cd Length: 156  Bit Score: 73.25  E-value: 8.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLG--QKVsitSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLH------IEEKRAINRLMNraa 82
Cdd:pfam02421   3 IALVGNPNVGKTTLFNALTGanQHV---GNWPGVTVEKKEGKFKYKGYEIEIVDLPGIYslspysEEERVARDYLLN--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  83 sssiGDVELVIFVVEGTNwtADDEMVLT-KLSSLRCPVILAINKIDNVTDKTVLLpHIGMISQKMNfLDVVPISAEKGVG 161
Cdd:pfam02421  77 ----EKPDVIVNVVDATN--LERNLYLTlQLLELGLPVVLALNMMDEAEKKGIKI-DIKKLSELLG-VPVVPTSARKGEG 148

                  ....*.
gi 1327839087 162 VDTIAK 167
Cdd:pfam02421 149 IDELLD 154
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
11-262 2.04e-14

Fe2+ transporter FeoB [Inorganic ion transport and metabolism];


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 73.23  E-value: 2.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLG--QKVS----IT-SRKpqttrhriMGIHTEDNYQIIYVDTPG---LH---IEEKRAINRL 77
Cdd:COG0370     6 IALVGNPNVGKTTLFNALTGsrQKVGnwpgVTvEKK--------EGKFKLKGKEIELVDLPGtysLSaysPDEKVARDFL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  78 MNraasssiGDVELVIFVVEGTNwtaddemvL-------TKLSSLRCPVILAINKIDNVTDKTVLLpHIGMISQKMNfLD 150
Cdd:COG0370    78 LE-------EKPDVVVNVVDATN--------LernlyltLQLLELGIPVVLALNMMDEAEKKGIKI-DVEKLSKLLG-VP 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087 151 VVPISAEKGVGVDT-IAKIVKQHIPEAVHHFPEDYITDRSQRFmaseiirEKLMRFLGDELPYSVTVEIEQFKVTDVGIY 229
Cdd:COG0370   141 VVPTSARKGKGIDElKEAIIEAAEGKKPRPLRIDYPEEIEEAI-------EELEELLEEDGPYPSRWLAIKLLEGDEEVL 213
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1327839087 230 HINGLILVEREGQKKMVIGNKGSKLKTIGTEAR 262
Cdd:COG0370   214 ELLSELLELLEEIREELEEELGEDLESIIADAR 246
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
11-182 7.89e-14

GTP-binding protein, GTP1/Obg family [General function prediction only];


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 70.63  E-value: 7.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNqllgqkvSITSRKPQ------TTRHRIMGIHTEDN--YQIIyvDTPGL----HIE----EKRAI 74
Cdd:COG1084   163 IVVAGYPNVGKSSLVS-------KVTSAKPEiasypfTTKGIIVGHFERGHgrYQVI--DTPGLldrpLSErneiERQAI 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  75 NRLMNraasssIGDVelVIFVVEGTN---WTADDEMVLTK--LSSLRCPVILAINKIDNVTDKTVllphigmisQKMNFL 149
Cdd:COG1084   234 LALKH------LADV--ILFLFDPSEtcgYSLEEQLNLLEeiRSLFDVPVIVVINKIDLSDEEEL---------KEAEEE 296
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1327839087 150 DVVPISAEKGVGVDTiakiVKQHIPEAVHHFPE 182
Cdd:COG1084   297 ADIKISALTGEGVDE----LLDELIEALEEEPE 325
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
11-88 1.43e-13

Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 69.37  E-value: 1.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMgIHTEDNYQIIyvDTPGL---HIEEKRAINRLmnrAASSSIG 87
Cdd:COG1161   116 VMIVGIPNVGKSTLINRLAGKKVAKTGNKPGVTKGQQW-IKLDDGLELL--DTPGIlwpKFEDPEVGYKL---AATGAIK 189

                  .
gi 1327839087  88 D 88
Cdd:COG1161   190 D 190
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
12-170 3.10e-13

Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) subfamily. E. coli has an iron(II) transport system, known as feo, which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.


Pssm-ID: 206667 [Multi-domain]  Cd Length: 159  Bit Score: 66.33  E-value: 3.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  12 AIVGRPNVGKSTLLNQLLG--QKVsitSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLH------IEEKRAINRLMNraas 83
Cdd:cd01879     1 ALVGNPNVGKTTLFNALTGarQKV---GNWPGVTVEKKEGEFKLGGKEIEIVDLPGTYsltpysEDEKVARDFLLG---- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  84 ssiGDVELVIFVVEGTNwtADDEMVLT-KLSSLRCPVILAINKIDNVTDKTVLLpHIGMISQKMNfLDVVPISAEKGVGV 162
Cdd:cd01879    74 ---EEPDLIVNVVDATN--LERNLYLTlQLLELGLPVVVALNMIDEAEKRGIKI-DLDKLSELLG-VPVVPTSARKGEGI 146
                         170
                  ....*....|..
gi 1327839087 163 D----TIAKIVK 170
Cdd:cd01879   147 DelldAIAKLAE 158
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
11-171 8.57e-13

Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in eukaryotes ranging from trypanosomes to humans. NOG1 is functionally linked to ribosome biogenesis and found in association with the nuclear pore complexes and identified in many preribosomal complexes. Thus, defects in NOG1 can lead to defects in 60S biogenesis. The S. cerevisiae NOG1 gene is essential for cell viability, and mutations in the predicted G motifs abrogate function. It is a member of the ODN family of GTP-binding proteins that also includes the bacterial Obg and DRG proteins.


Pssm-ID: 206684 [Multi-domain]  Cd Length: 167  Bit Score: 65.27  E-value: 8.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRkPQTTRHRIMGiHTEDNY---QIIyvDTPGL--------HIEEKRAINRLMN 79
Cdd:cd01897     3 LVIAGYPNVGKSSLVNKLTRAKPEVAPY-PFTTKSLFVG-HFDYKYlrwQVI--DTPGIldrpleerNTIEMQAITALAH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  80 RAAsssigdveLVIFVVEGTN---WTADDEMVLtkLSSLR----CPVILAINKIDNVTDKtvLLPHIGMISQKMNFlDVV 152
Cdd:cd01897    79 LRA--------AVLFFIDPSEtcgYSIEEQLSL--FKEIKplfnKPVIVVLNKIDLLTEE--DLSEIEKELEKEGE-EVI 145
                         170
                  ....*....|....*....
gi 1327839087 153 PISAEKGVGVDTIAKIVKQ 171
Cdd:cd01897   146 KISTLTEEGVDELKNKACE 164
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
11-174 2.33e-12

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: 64.47  E-value: 2.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLL---GQKVSITSRKPQTTRH-------RIMGI-----HTE---DNYQIIYVDTPGlHIEekr 72
Cdd:pfam00009   6 IGIIGHVDHGKTTLTDRLLyytGAISKRGEVKGEGEAGldnlpeeRERGItiksaAVSfetKDYLINLIDTPG-HVD--- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  73 aINRLMNRAASSSIGDVeLVIFVVEGTNWTAddEMVLTKLSSLRCPVILAINKIDNVTDKTVLLPhIGMISQK------- 145
Cdd:pfam00009  82 -FVKEVIRGLAQADGAI-LVVDAVEGVMPQT--REHLRLARQLGVPIIVFINKMDRVDGAELEEV-VEEVSREllekyge 156
                         170       180       190
                  ....*....|....*....|....*....|
gi 1327839087 146 -MNFLDVVPISAEKGVGVDTIAKIVKQHIP 174
Cdd:pfam00009 157 dGEFVPVVPGSALKGEGVQTLLDALDEYLP 186
YeeP COG3596
Predicted GTPase [General function prediction only];
11-179 3.12e-12

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 65.94  E-value: 3.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITS-RKPQT---TRHRimgIHTEDNYQIIYVDTPGLH-IEEKRAINRLMNRAASss 85
Cdd:COG3596    42 IALVGKTGAGKSSLINALFGAEVAEVGvGRPCTreiQRYR---LESDGLPGLVLLDTPGLGeVNERDREYRELRELLP-- 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  86 igDVELVIFVVEGTNwtADDEMVLTKLSSLR-----CPVILAINKID--------NVTDKTVLLPHIGMISQKMNFL--- 149
Cdd:COG3596   117 --EADLILWVVKADD--RALATDEEFLQALRaqypdPPVLVVLTQVDrleperewDPPYNWPSPPKEQNIRRALEAIaeq 192
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1327839087 150 ------DVVPISAEKGV---GVDTIAKIVKQHIPEAVHH 179
Cdd:COG3596   193 lgvpidRVIPVSAAEDRtgyGLEELVDALAEALPEAKRS 231
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
11-65 7.63e-12

Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. The YlqF subfamily is represented in all eukaryotes as well as a phylogenetically diverse array of bacteria (including gram-positive bacteria, proteobacteria, Synechocystis, Borrelia, and Thermotoga).


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 62.55  E-value: 7.63e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHrIMGIHTEDNYQIIyvDTPG 65
Cdd:cd01856   118 AMVVGIPNVGKSTLINRLRGKKVAKVGNKPGVTRG-QQWIRIGPNIELL--DTPG 169
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
11-173 8.47e-12

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 439988 [Multi-domain]  Cd Length: 194  Bit Score: 62.78  E-value: 8.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKvSI--TSRKPQTTRHrImgihtedNY-----QIIYVDTPG-----LHIEEKRAINRLM 78
Cdd:COG0218    26 IAFAGRSNVGKSSLINALTNRK-KLarTSKTPGKTQL-I-------NFflindKFYLVDLPGygyakVSKAEKEKWQKLI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  79 -----NRaasssigdVELVIFVV------EgtnWTADDEMVLTKLSSLRCPVILAINKIDNVTdKTVLLPHIGMISQKMN 147
Cdd:COG0218    97 edyleGR--------ENLKGVVLlidirhP---PKELDLEMLEWLDEAGIPFLIVLTKADKLK-KSELAKQLKAIKKALG 164
                         170       180       190
                  ....*....|....*....|....*....|
gi 1327839087 148 FL----DVVPISAEKGVGVDTIAKIVKQHI 173
Cdd:COG0218   165 KDpaapEVILFSSLKKEGIDELRAAIEEWL 194
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
15-220 2.68e-11

ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane protein required for iron(II) update, is encoded in an operon with FeoA (75 amino acids), which is also required, and is regulated by Fur. There appear to be two copies in Archaeoglobus fulgidus and Clostridium acetobutylicum. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273077 [Multi-domain]  Cd Length: 591  Bit Score: 63.99  E-value: 2.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  15 GRPNVGKSTLLNQLLGQKVSItSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLH------IEEKRAINRLMNraasssiGD 88
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTV-GNWPGVTVEKKEGKLGFQGEDIEIVDLPGIYslttfsLEEEVARDYLLN-------EK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  89 VELVIFVVEGTNwtADDEMVLT-KLSSLRCPVILAINKIDNVTDKTVLLpHIGMISQKMNfLDVVPISAEKGVGV-DTIA 166
Cdd:TIGR00437  73 PDLVVNVVDASN--LERNLYLTlQLLELGIPMILALNLVDEAEKKGIRI-DEEKLEERLG-VPVVPTSATEGRGIeRLKD 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327839087 167 KIVKQHIPE-----AVHHFPEDYiTDRSQRFMASEIIREKLMRFLGDELP--YSVTVEIEQ 220
Cdd:TIGR00437 149 AIRKAIGLKelkkrAIEIVPEAY-QVVEVVEGLIEIIYSISKRGLEILLGllEDLSLEIEK 208
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
6-127 8.62e-11

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 62.50  E-value: 8.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087   6 SHCGFVAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLHIEEKRAINR-----LMNR 80
Cdd:PRK09518  448 SGLRRVALVGRPNVGKSSLLNQLTHEERAVVNDLAGTTRDPVDEIVEIDGEDWLFIDTAGIKRRQHKLTGAeyyssLRTQ 527
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1327839087  81 AAsssIGDVELVIFVVEGTNWTAD-DEMVL-TKLSSLRCpVILAINKID 127
Cdd:PRK09518  528 AA---IERSELALFLFDASQPISEqDLKVMsMAVDAGRA-LVLVFNKWD 572
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
11-173 1.70e-10

Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain.


Pssm-ID: 206685 [Multi-domain]  Cd Length: 170  Bit Score: 58.59  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNqllgqkvSITSRKPQ------TTRHRIMG-IHTEDNYQIIYVDTPGL----------------H 67
Cdd:cd01898     3 VGLVGLPNAGKSTLLS-------AISNAKPKiadypfTTLVPNLGvVRVDDGRSFVIADIPGLiegasegkglghrflrH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  68 IEekrainrlmnRAAsssigdveLVIFVVEGTNwtADD-----EMVLTKLSS-----LRCPVILAINKIDNVTDKTvLLP 137
Cdd:cd01898    76 IE----------RTR--------VLLHVIDLSG--EDDpvedyETIRNELEAynpglAEKPRIVVLNKIDLLDAEE-RFE 134
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1327839087 138 HIGMISQKMNFLDVVPISAEKGVGVDTIAKIVKQHI 173
Cdd:cd01898   135 KLKELLKELKGKKVFPISALTGEGLDELLKKLAKLL 170
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
11-97 1.86e-10

ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding proteins involved in ribosome biogenesis, including the essential YlqF protein of Bacillus subtilis, which is an essential protein. They are related to Era, EngA, and other GTPases of ribosome biogenesis, but are circularly permuted. This family is not universal, and is not present in Escherichia coli, and so is not as well studied as some other GTPases. This model is built for bacterial members. [Protein synthesis, Other]


Pssm-ID: 274669 [Multi-domain]  Cd Length: 276  Bit Score: 60.22  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRhRIMGIHTEDNYQIIyvDTPGL---HIEEKRAINRLmnrAASSSIG 87
Cdd:TIGR03596 121 AMIVGIPNVGKSTLINRLAGKKVAKVGNRPGVTK-GQQWIKLSDNLELL--DTPGIlwpKFEDQEVGLKL---AATGAIK 194
                          90
                  ....*....|....*
gi 1327839087  88 DV-----ELVIFVVE 97
Cdd:TIGR03596 195 DEaldleDVALFLLE 209
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
11-173 3.71e-10

HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.


Pssm-ID: 206666 [Multi-domain]  Cd Length: 204  Bit Score: 58.24  E-value: 3.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSItsrKPQ------TTRHRimgIHTEDNYQIIYVDTPGLhieekraINRLMN----- 79
Cdd:cd01878    44 VALVGYTNAGKSTLFNALTGADVLA---EDQlfatldPTTRR---IKLPGGREVLLTDTVGF-------IRDLPHqlvea 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  80 -RAASSSIGDVELVIFVVEGTNWTADDEM-----VLTKLSSLRCPVILAINKIDNVTDKTVLlphigmISQKMNFLDVVP 153
Cdd:cd01878   111 fRSTLEEVAEADLLLHVVDASDPDREEQIetveeVLKELGADDIPIILVLNKIDLLDDEELE------ERLRAGRPDAVF 184
                         170       180
                  ....*....|....*....|
gi 1327839087 154 ISAEKGVGVDTIAKIVKQHI 173
Cdd:cd01878   185 ISAKTGEGLDLLKEAIEELL 204
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
12-163 2.88e-09

Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; The Obg-like subfamily consists of five well-delimited, ancient subfamilies, namely Obg, DRG, YyaF/YchF, Ygr210, and NOG1. Four of these groups (Obg, DRG, YyaF/YchF, and Ygr210) are characterized by a distinct glycine-rich motif immediately following the Walker B motif (G3 box). Obg/CgtA is an essential gene that is involved in the initiation of sporulation and DNA replication in the bacteria Caulobacter and Bacillus, but its exact molecular role is unknown. Furthermore, several OBG family members possess a C-terminal RNA-binding domain, the TGS domain, which is also present in threonyl-tRNA synthetase and in bacterial guanosine polyphosphatase SpoT. Nog1 is a nucleolar protein that might function in ribosome assembly. The DRG and Nog1 subfamilies are ubiquitous in archaea and eukaryotes, the Ygr210 subfamily is present in archaea and fungi, and the Obg and YyaF/YchF subfamilies are ubiquitous in bacteria and eukaryotes. The Obg/Nog1 and DRG subfamilies appear to form one major branch of the Obg family and the Ygr210 and YchF subfamilies form another branch. No GEFs, GAPs, or GDIs for Obg have been identified.


Pssm-ID: 206668 [Multi-domain]  Cd Length: 167  Bit Score: 55.09  E-value: 2.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  12 AIVGRPNVGKSTLLNQLLGQKVSITSrKPQTTRHRIMG-IHTEDNYQIIYVDTPGL---HIEEKRAINRLMNRAASSSig 87
Cdd:cd01881     1 GLVGLPNVGKSTLLSALTSAKVEIAS-YPFTTLEPNVGvFEFGDGVDIQIIDLPGLldgASEGRGLGEQILAHLYRSD-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  88 dveLVIFVVEGTNWTADDEMvlTKLSSLRC------------PVILAINKIDNVTDKTvllPHIGMISQKMNFLDVVPIS 155
Cdd:cd01881    78 ---LILHVIDASEDCVGDPL--EDQKTLNEevsgsflflknkPEMIVANKIDMASENN---LKRLKLDKLKRGIPVVPTS 149

                  ....*...
gi 1327839087 156 AEKGVGVD 163
Cdd:cd01881   150 ALTRLGLD 157
PRK04213 PRK04213
GTP-binding protein EngB;
11-176 3.90e-09

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 55.31  E-value: 3.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSiTSRKPQTTRhRIMGIHTEDnyqIIYVDTPG------LHIEEKRAINRLMNRAASS 84
Cdd:PRK04213   12 IVFVGRSNVGKSTLVRELTGKKVR-VGKRPGVTR-KPNHYDWGD---FILTDLPGfgfmsgVPKEVQEKIKDEIVRYIED 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  85 SIGDVELVIFVVEGTN-------WTADDEM-----VLTKLSSLRCPVILAINKIDNVTDKTVLLPHI----GMISQKMNF 148
Cdd:PRK04213   87 NADRILAAVLVVDGKSfieiierWEGRGEIpidveMFDFLRELGIPPIVAVNKMDKIKNRDEVLDEIaerlGLYPPWRQW 166
                         170       180
                  ....*....|....*....|....*....
gi 1327839087 149 LDV-VPISAEKGvGVDTIAKIVKQHIPEA 176
Cdd:PRK04213  167 QDIiAPISAKKG-GIEELKEAIRKRLHEA 194
obgE PRK12299
GTPase CgtA; Reviewed
11-176 7.96e-09

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 55.85  E-value: 7.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNqllgqkvSITSRKPQ------TTRHRIMGI-HTEDNYQIIYVDTPGL----------------H 67
Cdd:PRK12299  161 VGLVGLPNAGKSTLIS-------AVSAAKPKiadypfTTLHPNLGVvRVDDYKSFVIADIPGLiegasegaglghrflkH 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  68 IEEKRAINRLMNRAASSSIGDVELVIFVVEgtnwtADDEMVLTKlsslrcPVILAINKIDNVTDKTVLLPHIGMISQKMN 147
Cdd:PRK12299  234 IERTRLLLHLVDIEAVDPVEDYKTIRNELE-----KYSPELADK------PRILVLNKIDLLDEEEEREKRAALELAALG 302
                         170       180
                  ....*....|....*....|....*....
gi 1327839087 148 fLDVVPISAEKGVGVDTIAKIVKQHIPEA 176
Cdd:PRK12299  303 -GPVFLISAVTGEGLDELLRALWELLEEA 330
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
11-66 1.68e-08

A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC class I region and is highly homologous to a putative GTP-binding protein, MMR1 from mouse. These proteins represent a new subfamily of GTP-binding proteins that has only eukaryote members. This subfamily shows a circular permutation of the GTPase signature motifs so that the C-terminal strands 5, 6, and 7 (strand 6 contains the G4 box with sequence NKXD) are relocated to the N-terminus.


Pssm-ID: 206750 [Multi-domain]  Cd Length: 140  Bit Score: 52.23  E-value: 1.68e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHrIMGIHTEDNyqIIYVDTPGL 66
Cdd:cd01857    85 IGLVGYPNVGKSSLINALVGSKKVSVSSTPGKTKH-FQTIFLEPG--ITLCDCPGL 137
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
11-180 2.26e-08

50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 54.71  E-value: 2.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSI----------TSRKpqttrhrimgIHTEDNYQIIYVDTPG----L-H-------- 67
Cdd:COG2262   202 VALVGYTNAGKSTLFNRLTGADVLAedklfatldpTTRR----------LELPDGRPVLLTDTVGfirkLpHqlveafrs 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  68 -IEEkrainrlmnraasssIGDVELVIFVVEGTNWTADDEM-----VLTKLSSLRCPVILAINKIDnvtdktvLLPHIGM 141
Cdd:COG2262   272 tLEE---------------VREADLLLHVVDASDPDFEEQIetvneVLEELGADDKPIILVFNKID-------LLDDEEL 329
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1327839087 142 ISQKMNFLDVVPISAEKGVGVDTIAKIVKQHIPEAVHHF 180
Cdd:COG2262   330 ERLRAGYPDAVFISAKTGEGIDELLEAIEERLPEDRVEV 368
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
11-174 3.12e-08

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: 52.68  E-value: 3.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRK----PQTTRH---RIMGIHTE--------DNYQIIYVDTPGlHieekraIN 75
Cdd:cd00881     2 VGVIGHVDHGKTTLTGSLLYQTGAIDRRGtrkeTFLDTLkeeRERGITIKtgvvefewPKRRINFIDTPG-H------ED 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  76 RLMNRAASSSIGDVELVIF-VVEGTnwTADDEMVLTKLSSLRCPVILAINKIDNVTDKTV---------LLPHIGMISQK 145
Cdd:cd00881    75 FSKETVRGLAQADGALLVVdANEGV--EPQTREHLNIALAGGLPIIVAVNKIDRVGEEDFdevlreikeLLKLIGFTFLK 152
                         170       180
                  ....*....|....*....|....*....
gi 1327839087 146 MNFLDVVPISAEKGVGVDTIAKIVKQHIP 174
Cdd:cd00881   153 GKDVPIIPISALTGEGIEELLDAIVEHLP 181
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
11-179 6.04e-08

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 53.95  E-value: 6.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLG--QKVsitSRKPQTTRHRIMGIHTEDNYQIIYVDTPGLH----IEEKRAINRlmnRAASS 84
Cdd:PRK09554    6 IGLIGNPNSGKTTLFNQLTGarQRV---GNWAGVTVERKEGQFSTTDHQVTLVDLPGTYslttISSQTSLDE---QIACH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  85 SI--GDVELVIFVVEGTNwtADDEMVLT-KLSSLRCPVILAINKIDnVTDKTVLLPHIGMISQKMNfLDVVPISAEKGVG 161
Cdd:PRK09554   80 YIlsGDADLLINVVDASN--LERNLYLTlQLLELGIPCIVALNMLD-IAEKQNIRIDIDALSARLG-CPVIPLVSTRGRG 155
                         170       180
                  ....*....|....*....|..
gi 1327839087 162 VDTIAKIVKQH----IPEAVHH 179
Cdd:PRK09554  156 IEALKLAIDRHqaneNVELVHY 177
EutP COG4917
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ...
11-127 8.16e-08

Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];


Pssm-ID: 443945 [Multi-domain]  Cd Length: 145  Bit Score: 50.57  E-value: 8.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKvsITSRKPQTtrhrimgihtednyqIIY----VDTPGLHIEekraiNRLMNRAASSSI 86
Cdd:COG4917     4 IMLIGRSGAGKTTLTQALNGEE--LEYRKTQA---------------VEYydniIDTPGEYIE-----NPRFYKALIATA 61
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1327839087  87 GDVELVIFVvegtnWTADDEMVL---TKLSSLRCPVILAINKID 127
Cdd:COG4917    62 QDADVIVLV-----QDATEPRSVfppGFAKAFNKPVIGVITKID 100
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
11-132 9.75e-08

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 51.01  E-value: 9.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDNyqIIYVDTPGLHieekrAINRLMNRAASSSIGDVE 90
Cdd:cd09912     3 LAVVGEFSAGKSTLLNALLGEEVLPTGVTPTTAVITVLRYGLLKG--VVLVDTPGLN-----STIEHHTEITESFLPRAD 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1327839087  91 LVIFVVEGTN-WTADDEMVLTKLSS-LRCPVILAINKIDNVTDK 132
Cdd:cd09912    76 AVIFVLSADQpLTESEREFLKEILKwSGKKIFFVLNKIDLLSEE 119
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
12-166 2.90e-07

YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 48.88  E-value: 2.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  12 AIVGRPNVGKSTLLNQLLGQKVSITS-RKPQTTRHRIMGIHTEDNYQIIyVDTPGlhIEEKRAINRLMNRAASSSIGDVE 90
Cdd:cd11383     1 GLMGKTGAGKSSLCNALFGTEVAAVGdRRPTTRAAQAYVWQTGGDGLVL-LDLPG--VGERGRRDREYEELYRRLLPEAD 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327839087  91 LVIFVVEGTNW--TADDEMVLTKLSSLRCPVILAINKIDNvtdktvllphigmisqkmnfldVVPISAEKGVGVDTIA 166
Cdd:cd11383    78 LVLWLLDADDRalAADHDFYLLPLAGHDAPLLFVLNQVDP----------------------VLAVSARTGWGLDELA 133
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
11-100 7.68e-07

Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 49.80  E-value: 7.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRkPQTTRHRIMGIHTEDNYQIIYVDTPGLhIEEKrAINRLMNRAASSSIGDVE 90
Cdd:COG1163    66 VVLVGFPSVGKSTLLNKLTNAKSEVGAY-EFTTLDVVPGMLEYKGAKIQILDVPGL-IEGA-ASGKGRGKEVLSVVRNAD 142
                          90
                  ....*....|
gi 1327839087  91 LVIFVVEGTN 100
Cdd:COG1163   143 LILIVLDVFE 152
infB CHL00189
translation initiation factor 2; Provisional
11-163 1.14e-06

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 49.83  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLlgqkvsitsRKPQTTRHRIMGI------------HTEDNYQIIYVDTPGlHieekRAINRLM 78
Cdd:CHL00189  247 VTILGHVDHGKTTLLDKI---------RKTQIAQKEAGGItqkigayevefeYKDENQKIVFLDTPG-H----EAFSSMR 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  79 NRAASSSigdvELVIFVVegtnwTADDEM------VLTKLSSLRCPVILAINKIDNVTDKTVLLPH----IGMISQKMNF 148
Cdd:CHL00189  313 SRGANVT----DIAILII-----AADDGVkpqtieAINYIQAANVPIIVAINKIDKANANTERIKQqlakYNLIPEKWGG 383
                         170
                  ....*....|....*.
gi 1327839087 149 -LDVVPISAEKGVGVD 163
Cdd:CHL00189  384 dTPMIPISASQGTNID 399
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
11-66 1.58e-06

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 49.20  E-value: 1.58e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRIMGIHTEDNYQIIYVDTPGL 66
Cdd:PRK03003  214 VALVGKPNVGKSSLLNKLAGEERSVVDDVAGTTVDPVDSLIELGGKTWRFVDTAGL 269
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
19-70 6.40e-06

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 46.24  E-value: 6.40e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327839087  19 VGKSTLLNQLLG---QKVSITSRKPQ----TTRHRIMgIHTEDNYQIIyvDTPG------LHIEE 70
Cdd:cd01854    96 VGKSTLLNALLPelvLATGEISEKLGrgrhTTTHREL-FPLPGGGLII--DTPGfrelglLHIDP 157
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
1-65 3.19e-05

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 43.68  E-value: 3.19e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327839087   1 MSELQSHC--GFVAIVGRPNVGKSTLLNQLLG------QKVSITSRKPQ-TTRHRIMgIHTEDNYQIIyvDTPG 65
Cdd:pfam03193  97 IEALKELLkgKTTVLAGQSGVGKSTLLNALLPeldlrtGEISEKLGRGRhTTTHVEL-FPLPGGGLLI--DTPG 167
obgE PRK12297
GTPase CgtA; Reviewed
11-183 6.29e-05

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 43.94  E-value: 6.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNqllgqkvSITSRKPQ------TTRHRIMG-IHTEDNYQIIYVDTPGLhIEekrainrlmnrAAS 83
Cdd:PRK12297  161 VGLVGFPNVGKSTLLS-------VVSNAKPKianyhfTTLVPNLGvVETDDGRSFVMADIPGL-IE-----------GAS 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  84 SSIG-------DVE---LVIFVV-----EGTNWTADDEMVLTKLSS-----LRCPVILAINKID------NVTDktvLLP 137
Cdd:PRK12297  222 EGVGlghqflrHIErtrVIVHVIdmsgsEGRDPIEDYEKINKELKLynprlLERPQIVVANKMDlpeaeeNLEE---FKE 298
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1327839087 138 HIGmisqkmnfLDVVPISAEKGVGVD----TIAKIVKQHIPEAVHHFPED 183
Cdd:PRK12297  299 KLG--------PKVFPISALTGQGLDellyAVAELLEETPEFPLEEEEVE 340
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
9-65 7.81e-05

An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents archaeal GTPase typified by the protein MJ1464 from Methanococcus jannaschii. The members of this family show a circular permutation of the GTPase signature motifs so that C-terminal strands 5, 6, and 7 (strands 6 contain the NKxD motif) are relocated to the N terminus.


Pssm-ID: 206752 [Multi-domain]  Cd Length: 157  Bit Score: 42.31  E-value: 7.81e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327839087   9 GFVAIVGRPNVGKSTLLNQLLGQKVSITSRKPQT---TRH----RIMGihtednyQIIYVDTPG 65
Cdd:cd01859   100 VIVGVVGYPKVGKSSIINALKGRHSASTSPIPGSpgyTKGiqlvRIDS-------KIYLIDTPG 156
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
11-100 7.89e-05

Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding protein (DRG) subfamily is an uncharacterized member of the Obg family, an evolutionary branch of GTPase superfamily proteins. GTPases act as molecular switches regulating diverse cellular processes. DRG2 and DRG1 comprise the DRG subfamily in eukaryotes. In view of their widespread expression in various tissues and high conservation among distantly related species in eukaryotes and archaea, DRG proteins may regulate fundamental cellular processes. It is proposed that the DRG subfamily proteins play their physiological roles through RNA binding.


Pssm-ID: 206683 [Multi-domain]  Cd Length: 233  Bit Score: 42.92  E-value: 7.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRkPQTTRHRIMGIHTEDNYQIIYVDTPGlhIEEKRAINRLMNRAASSSIGDVE 90
Cdd:cd01896     3 VALVGFPSVGKSTLLSKLTNTKSEVAAY-EFTTLTCVPGVMEYKGAKIQLLDLPG--IIEGASDGKGRGRQVIAVARTAD 79
                          90
                  ....*....|
gi 1327839087  91 LVIFVVEGTN 100
Cdd:cd01896    80 LILIVLDATK 89
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
11-127 8.73e-05

Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.


Pssm-ID: 206678 [Multi-domain]  Cd Length: 194  Bit Score: 42.58  E-value: 8.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQkvSITSRKPQTTRHRIM---------GI-----HTEDNYQ---IIYVDTPGlHIEEKRA 73
Cdd:cd01891     5 IAIIAHVDHGKTTLVDALLKQ--SGTFRENEEVGERVMdsndlererGItilakNTAITYKdtkINIIDTPG-HADFGGE 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1327839087  74 INRLMNRAASssigdVELVIFVVEG----TNWtaddemVLTKLSSLRCPVILAINKID 127
Cdd:cd01891    82 VERVLSMVDG-----VLLLVDASEGpmpqTRF------VLKKALEAGLKPIVVINKID 128
PRK01889 PRK01889
GTPase RsgA; Reviewed
1-66 1.13e-04

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 43.38  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087   1 MSELQSHCG---FVAIVGRPNVGKSTLLNQLLGQKVSIT-------SRKPQTTRHRIM------GIhtednyqIIyvDTP 64
Cdd:PRK01889  185 LDVLAAWLSggkTVALLGSSGVGKSTLVNALLGEEVQKTgavreddSKGRHTTTHRELhplpsgGL-------LI--DTP 255

                  ..
gi 1327839087  65 GL 66
Cdd:PRK01889  256 GM 257
RsgA COG1162
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
19-70 1.98e-04

Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440776 [Multi-domain]  Cd Length: 300  Bit Score: 42.41  E-value: 1.98e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327839087  19 VGKSTLLNQLLG---QKVSITSRKPQ----TTRHRIMgIHTEDNYQIIyvDTPGL------HIEE 70
Cdd:COG1162   177 VGKSTLINALLPdadLATGEISEKLGrgrhTTTHAEL-YPLPGGGWLI--DTPGFrefglwHIEP 238
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
3-86 2.50e-04

Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like (Translocon at the Outer-envelope membrane of Chloroplasts) family contains several Toc proteins, including Toc34, Toc33, Toc120, Toc159, Toc86, Toc125, and Toc90. The Toc complex at the outer envelope membrane of chloroplasts is a molecular machine of ~500 kDa that contains a single Toc159 protein, four Toc75 molecules, and four or five copies of Toc34. Toc64 and Toc12 are associated with the translocon, but do not appear to be part of the core complex. The Toc translocon initiates the import of nuclear-encoded preproteins from the cytosol into the organelle. Toc34 and Toc159 are both GTPases, while Toc75 is a beta-barrel integral membrane protein. Toc159 is equally distributed between a soluble cytoplasmic form and a membrane-inserted form, suggesting that assembly of the Toc complex is dynamic. Toc34 and Toc75 act sequentially to mediate docking and insertion of Toc159 resulting in assembly of the functional translocon.


Pssm-ID: 206652  Cd Length: 248  Bit Score: 41.53  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087   3 ELQSHCGfVAIVGRPNVGKSTLLNQLLG-QKVSITSRKPQTTR-HRIMGihTEDNYQIIYVDTPGLHieekRAINRLMNR 80
Cdd:cd01853    27 ELDFSLT-ILVLGKTGVGKSSTINSIFGeRKVSVSAFQSETLRpREVSR--TVDGFKLNIIDTPGLL----ESQDQRVNR 99

                  ....*.
gi 1327839087  81 AASSSI 86
Cdd:cd01853   100 KILSII 105
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
13-66 4.30e-04

Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 40.33  E-value: 4.30e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327839087  13 IVGRPNVGKSTLLNQLLGQKVS-----------ITSRKPQTTRH--RIMGIhtedNYQIIYvDTPGL 66
Cdd:cd01855   130 VVGATNVGKSTLINALLKSNGGkvqaqalvqrlTVSPIPGTTLGliKIPLG----EGKKLY-DTPGI 191
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
11-134 1.01e-03

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 39.61  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKV--SITSRKP-QTTRHRimgiHTEDNYQIIYVDTPGlHieeKRAINRLMNRAASSSIG 87
Cdd:cd04105     3 VLLLGPSDSGKTALFTKLTTGKVrsTVTSIEPnVASFYS----NSSKGKKLTLVDVPG-H---EKLRDKLLEYLKASLKA 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327839087  88 dvelVIFVVEGT----NWTADDEMVLTKLSSLR-----CPVILAINKIDNVTDKTV 134
Cdd:cd04105    75 ----IVFVVDSAtfqkNIRDVAEFLYDILTDLEkiknkIPILIACNKQDLFTAKPA 126
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
11-66 2.28e-03

Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, and archaea. They all exhibit a circular permutation of the GTPase signature motifs so that the order of the conserved G box motifs is G4-G5-G1-G2-G3, with G4 and G5 being permuted from the C-terminal region of proteins in the Ras superfamily to the N-terminus of YlqF-related GTPases.


Pssm-ID: 206746 [Multi-domain]  Cd Length: 146  Bit Score: 37.75  E-value: 2.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHRimgIHTEDNYQIIYVDTPGL 66
Cdd:cd01849    94 VGVVGLPNVGKSSFINALLNKFKLKVGSIPGTTKLQ---QDVKLDKEIYLYDTPGI 146
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
11-128 2.30e-03

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 38.73  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLgQKVSITSRK-------------PQTTRHRiMGIHTE------DNYQIIYVDTPGLHIEEK 71
Cdd:cd04170     2 IALVGHSGSGKTTLAEALL-YATGAIDRLgrvedgntvsdydPEEKKRK-MSIETSvaplewNGHKINLIDTPGYADFVG 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327839087  72 RAINRLMNraasssigdVELVIFVVEgtnwtADD------EMVLTKLSSLRCPVILAINKIDN 128
Cdd:cd04170    80 ETLSALRA---------VDAALIVVE-----AQSgvevgtEKVWEFLDDAKLPRIIFINKMDR 128
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
11-163 3.56e-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: 37.45  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  11 VAIVGRPNVGKSTLLNQLlgQKVSITSRKPQ-TTRHriMG----IHTEDNYQIIYVDTPGlHieekRAINRLMNRAASss 85
Cdd:cd01887     3 VTVMGHVDHGKTTLLDKI--RKTNVAAGEAGgITQH--IGayqvPIDVKIPGITFIDTPG-H----EAFTNMRARGAS-- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839087  86 IGDVelVIFVVEgtnwtADDE-MVLTK-----LSSLRCPVILAINKIDNVTDKTVL-------LPHIGMISQKM-NFLDV 151
Cdd:cd01887    72 VTDI--AILVVA-----ADDGvMPQTIeainhAKAANVPIIVAINKIDKPYGTEADpervkneLSELGLVGEEWgGDVSI 144
                         170
                  ....*....|..
gi 1327839087 152 VPISAEKGVGVD 163
Cdd:cd01887   145 VPISAKTGEGID 156
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
10-47 6.77e-03

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 37.13  E-value: 6.77e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1327839087  10 FVAIVGrPN-VGKSTLLNQLLGQ------KVSITSRKPQTTRHRI 47
Cdd:cd03235    27 FLAIVG-PNgAGKSTLLKAILGLlkptsgSIRVFGKPLEKERKRI 70
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
14-66 7.60e-03

AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 36.82  E-value: 7.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1327839087  14 VGRPNVGKSTLLNQLLGQKVSITSRKPQT-TRHRIMGIHTEDNYQIIYVDTPGL 66
Cdd:pfam04548   6 VGKTGNGKSATGNSILGRKAFESKLRAQGvTKTCQLVSRTWDGRIINVIDTPGL 59
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
11-65 7.71e-03

A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein that functions as a regulator of cell growth and proliferation in stem cells and in several types of cancer cells, but is not expressed in the differentiated cells of most mammalian adult tissues. NS shuttles between the nucleolus and nucleoplasm bidirectionally at a rate that is fast and independent of cell type. Lowering GTP levels decreases the nucleolar retention of NS, and expression of NS is abruptly down-regulated during differentiation prior to terminal cell division. Found only in eukaryotes, NS consists of an N-terminal basic domain, a coiled-coil domain, a GTP-binding domain, an intermediate domain, and a C-terminal acidic domain. Experimental evidence indicates that NS uses its GTP-binding property as a molecular switch to control the transition between the nucleolus and nucleoplasm, and this process involves interaction between the basic, GTP-binding, and intermediate domains of the protein.


Pssm-ID: 206753 [Multi-domain]  Cd Length: 171  Bit Score: 36.40  E-value: 7.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1327839087  11 VAIVGRPNVGKSTLLNQLLGQKVSITSRKPQTTRHrIMGIHTEDNYQIIyvDTPG 65
Cdd:cd04178   119 VGVVGYPNVGKSSVINSLKRSRACNVGATPGVTKS-MQEVHLDKHVKLL--DSPG 170
PRK00098 PRK00098
GTPase RsgA; Reviewed
19-70 8.22e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 37.11  E-value: 8.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327839087  19 VGKSTLLNQLLGQ---KVSITSRKPQ----TTRHRIMgIHTEDNYQIIyvDTPGL------HIEE 70
Cdd:PRK00098  175 VGKSTLLNALAPDlelKTGEISEALGrgkhTTTHVEL-YDLPGGGLLI--DTPGFssfglhDLEA 236
 
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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