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Conserved domains on  [gi|495777602|ref|WP_008502181|]
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MULTISPECIES: GTPase Era [Enterobacter]

Protein Classification

GTPase Era( domain architecture ID 11477992)

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 PRK00089
GTPase Era; Reviewed
4-297 2.07e-179

GTPase Era; Reviewed


:

Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 496.11  E-value: 2.07e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   4 EKTYCGFIAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLHmEEKRAINRLMNKAAS 83
Cdd:PRK00089   1 MGFKSGFVAIVGRPNVGKSTLLNALVGQKISIVSPKPQTTRHRIRGIVTEDDAQIIFVDTPGIH-KPKRALNRAMNKAAW 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  84 SSIGDVELVIFVVEGTR-WTPDDEMVLNKLRDGKTPVILAVNKVDNVQEKADLLPHLQWLGSQMNFLDIVPLSAETGLNV 162
Cdd:PRK00089  80 SSLKDVDLVLFVVDADEkIGPGDEFILEKLKKVKTPVILVLNKIDLVKDKEELLPLLEELSELMDFAEIVPISALKGDNV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602 163 DTIAGIVRKHLPEAIHHFPEEYITDRSQRFMASEIIREKLMRFLGAELPYSVTVEIERFQsnERGGYDINGLILVEREGQ 242
Cdd:PRK00089 160 DELLDVIAKYLPEGPPYYPEDQITDRPERFLAAEIIREKLLRLLGDELPYSVAVEIEKFE--ERGLVRIEATIYVERDSQ 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495777602 243 KKMVIGNKGAKIKTIGIEARKDMQEMFEAPVHLELWVKVKSGWADDERALRSLGY 297
Cdd:PRK00089 238 KGIIIGKGGAMLKKIGTEARKDIEKLLGKKVFLELWVKVKKGWRDDEKALRELGY 292
 
Name Accession Description Interval E-value
era PRK00089
GTPase Era; Reviewed
4-297 2.07e-179

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 496.11  E-value: 2.07e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   4 EKTYCGFIAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLHmEEKRAINRLMNKAAS 83
Cdd:PRK00089   1 MGFKSGFVAIVGRPNVGKSTLLNALVGQKISIVSPKPQTTRHRIRGIVTEDDAQIIFVDTPGIH-KPKRALNRAMNKAAW 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  84 SSIGDVELVIFVVEGTR-WTPDDEMVLNKLRDGKTPVILAVNKVDNVQEKADLLPHLQWLGSQMNFLDIVPLSAETGLNV 162
Cdd:PRK00089  80 SSLKDVDLVLFVVDADEkIGPGDEFILEKLKKVKTPVILVLNKIDLVKDKEELLPLLEELSELMDFAEIVPISALKGDNV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602 163 DTIAGIVRKHLPEAIHHFPEEYITDRSQRFMASEIIREKLMRFLGAELPYSVTVEIERFQsnERGGYDINGLILVEREGQ 242
Cdd:PRK00089 160 DELLDVIAKYLPEGPPYYPEDQITDRPERFLAAEIIREKLLRLLGDELPYSVAVEIEKFE--ERGLVRIEATIYVERDSQ 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495777602 243 KKMVIGNKGAKIKTIGIEARKDMQEMFEAPVHLELWVKVKSGWADDERALRSLGY 297
Cdd:PRK00089 238 KGIIIGKGGAMLKKIGTEARKDIEKLLGKKVFLELWVKVKKGWRDDEKALRELGY 292
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
6-297 1.55e-175

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 486.42  E-value: 1.55e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   6 TYCGFIAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLHmEEKRAINRLMNKAASSS 85
Cdd:COG1159    1 FRSGFVAIVGRPNVGKSTLLNALVGQKVSIVSPKPQTTRHRIRGIVTREDAQIVFVDTPGIH-KPKRKLGRRMNKAAWSA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  86 IGDVELVIFVVEGTR-WTPDDEMVLNKLRDGKTPVILAVNKVDNVqEKADLLPHLQWLGSQMNFLDIVPLSAETGLNVDT 164
Cdd:COG1159   80 LEDVDVILFVVDATEkIGEGDEFILELLKKLKTPVILVINKIDLV-KKEELLPLLAEYSELLDFAEIVPISALKGDNVDE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602 165 IAGIVRKHLPEAIHHFPEEYITDRSQRFMASEIIREKLMRFLGAELPYSVTVEIERFQsnERGG-YDINGLILVEREGQK 243
Cdd:COG1159  159 LLDEIAKLLPEGPPYYPEDQITDRPERFLAAEIIREKILRLLRDELPYSVAVEIEEFE--EREGlLRIRATIYVERDSQK 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 495777602 244 KMVIGNKGAKIKTIGIEARKDMQEMFEAPVHLELWVKVKSGWADDERALRSLGY 297
Cdd:COG1159  237 GIIIGKGGSMLKKIGTEARKDIEKLLGKKVFLELWVKVKKNWRDDERALRELGY 290
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
9-280 2.04e-149

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: 419.49  E-value: 2.04e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602    9 GFIAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLHmEEKRAINRLMNKAASSSIGD 88
Cdd:TIGR00436   1 GFVAILGRPNVGKSTLLNQLHGQKISITSPKAQTTRNRISGIHTTGASQIIFIDTPGFH-EKKHSLNRLMMKEARSAIGG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   89 VELVIFVVEGTRWTPDDEMVLNKLRDGKTPVILAVNKVDNvQEKADLLPHLQWLGSQMNFLDIVPLSAETGLNVDTIAGI 168
Cdd:TIGR00436  80 VDLILFVVDSDQWNGDGEFVLTKLQNLKRPVVLTRNKLDN-KFKDKLLPLIDKYAILEDFKDIVPISALTGDNTSFLAAF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  169 VRKHLPEAIHHFPEEYITDRSQRFMASEIIREKLMRFLGAELPYSVTVEIERFQSNERGGYDINGLILVEREGQKKMVIG 248
Cdd:TIGR00436 159 IEVHLPEGPFRYPEDYVTDQPDRFKISEIIREKIIRYTKEEIPHSVRVEIERKSFNEKGLLKIHALISVERESQKKIIIG 238
                         250       260       270
                  ....*....|....*....|....*....|..
gi 495777602  249 NKGAKIKTIGIEARKDMQEMFEAPVHLELWVK 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 ...
6-173 2.58e-87

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: 258.16  E-value: 2.58e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   6 TYCGFIAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLHMEEKRAINRlMNKAASSS 85
Cdd:cd04163    1 FKSGFVAIIGRPNVGKSTLLNALVGQKISIVSPKPQTTRNRIRGIYTDDDAQIIFVDTPGIHKPKKKLGER-MVKAAWSA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  86 IGDVELVIFVVEGTRW-TPDDEMVLNKLRDGKTPVILAVNKVDNVQEKADLLPHLQWLGSQMNFLDIVPLSAETGLNVDT 164
Cdd:cd04163   80 LKDVDLVLFVVDASEWiGEGDEFILELLKKSKTPVILVLNKIDLVKDKEDLLPLLEKLKELHPFAEIFPISALKGENVDE 159

                 ....*....
gi 495777602 165 IAGIVRKHL 173
Cdd:cd04163  160 LLEYIVEYL 168
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
10-125 9.36e-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: 106.55  E-value: 9.36e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   10 FIAIVGRPNVGKSTLLNNLLGQKiSITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLHmeeKRAINRLMNKAASSSIGDV 89
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK-AIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLI---EGASEGEGLGRAFLAIIEA 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 495777602   90 ELVIFVVEGTR-WTPDDEMVLNKLRDGKTPVILAVNK 125
Cdd:pfam01926  77 DLILFVVDSEEgITPLDEELLELLRENKKPIILVLNK 113
 
Name Accession Description Interval E-value
era PRK00089
GTPase Era; Reviewed
4-297 2.07e-179

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 496.11  E-value: 2.07e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   4 EKTYCGFIAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLHmEEKRAINRLMNKAAS 83
Cdd:PRK00089   1 MGFKSGFVAIVGRPNVGKSTLLNALVGQKISIVSPKPQTTRHRIRGIVTEDDAQIIFVDTPGIH-KPKRALNRAMNKAAW 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  84 SSIGDVELVIFVVEGTR-WTPDDEMVLNKLRDGKTPVILAVNKVDNVQEKADLLPHLQWLGSQMNFLDIVPLSAETGLNV 162
Cdd:PRK00089  80 SSLKDVDLVLFVVDADEkIGPGDEFILEKLKKVKTPVILVLNKIDLVKDKEELLPLLEELSELMDFAEIVPISALKGDNV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602 163 DTIAGIVRKHLPEAIHHFPEEYITDRSQRFMASEIIREKLMRFLGAELPYSVTVEIERFQsnERGGYDINGLILVEREGQ 242
Cdd:PRK00089 160 DELLDVIAKYLPEGPPYYPEDQITDRPERFLAAEIIREKLLRLLGDELPYSVAVEIEKFE--ERGLVRIEATIYVERDSQ 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495777602 243 KKMVIGNKGAKIKTIGIEARKDMQEMFEAPVHLELWVKVKSGWADDERALRSLGY 297
Cdd:PRK00089 238 KGIIIGKGGAMLKKIGTEARKDIEKLLGKKVFLELWVKVKKGWRDDEKALRELGY 292
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
6-297 1.55e-175

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 486.42  E-value: 1.55e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   6 TYCGFIAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLHmEEKRAINRLMNKAASSS 85
Cdd:COG1159    1 FRSGFVAIVGRPNVGKSTLLNALVGQKVSIVSPKPQTTRHRIRGIVTREDAQIVFVDTPGIH-KPKRKLGRRMNKAAWSA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  86 IGDVELVIFVVEGTR-WTPDDEMVLNKLRDGKTPVILAVNKVDNVqEKADLLPHLQWLGSQMNFLDIVPLSAETGLNVDT 164
Cdd:COG1159   80 LEDVDVILFVVDATEkIGEGDEFILELLKKLKTPVILVINKIDLV-KKEELLPLLAEYSELLDFAEIVPISALKGDNVDE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602 165 IAGIVRKHLPEAIHHFPEEYITDRSQRFMASEIIREKLMRFLGAELPYSVTVEIERFQsnERGG-YDINGLILVEREGQK 243
Cdd:COG1159  159 LLDEIAKLLPEGPPYYPEDQITDRPERFLAAEIIREKILRLLRDELPYSVAVEIEEFE--EREGlLRIRATIYVERDSQK 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 495777602 244 KMVIGNKGAKIKTIGIEARKDMQEMFEAPVHLELWVKVKSGWADDERALRSLGY 297
Cdd:COG1159  237 GIIIGKGGSMLKKIGTEARKDIEKLLGKKVFLELWVKVKKNWRDDERALRELGY 290
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
9-280 2.04e-149

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: 419.49  E-value: 2.04e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602    9 GFIAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLHmEEKRAINRLMNKAASSSIGD 88
Cdd:TIGR00436   1 GFVAILGRPNVGKSTLLNQLHGQKISITSPKAQTTRNRISGIHTTGASQIIFIDTPGFH-EKKHSLNRLMMKEARSAIGG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   89 VELVIFVVEGTRWTPDDEMVLNKLRDGKTPVILAVNKVDNvQEKADLLPHLQWLGSQMNFLDIVPLSAETGLNVDTIAGI 168
Cdd:TIGR00436  80 VDLILFVVDSDQWNGDGEFVLTKLQNLKRPVVLTRNKLDN-KFKDKLLPLIDKYAILEDFKDIVPISALTGDNTSFLAAF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  169 VRKHLPEAIHHFPEEYITDRSQRFMASEIIREKLMRFLGAELPYSVTVEIERFQSNERGGYDINGLILVEREGQKKMVIG 248
Cdd:TIGR00436 159 IEVHLPEGPFRYPEDYVTDQPDRFKISEIIREKIIRYTKEEIPHSVRVEIERKSFNEKGLLKIHALISVERESQKKIIIG 238
                         250       260       270
                  ....*....|....*....|....*....|..
gi 495777602  249 NKGAKIKTIGIEARKDMQEMFEAPVHLELWVK 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 ...
6-173 2.58e-87

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: 258.16  E-value: 2.58e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   6 TYCGFIAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLHMEEKRAINRlMNKAASSS 85
Cdd:cd04163    1 FKSGFVAIIGRPNVGKSTLLNALVGQKISIVSPKPQTTRNRIRGIYTDDDAQIIFVDTPGIHKPKKKLGER-MVKAAWSA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  86 IGDVELVIFVVEGTRW-TPDDEMVLNKLRDGKTPVILAVNKVDNVQEKADLLPHLQWLGSQMNFLDIVPLSAETGLNVDT 164
Cdd:cd04163   80 LKDVDLVLFVVDASEWiGEGDEFILELLKKSKTPVILVLNKIDLVKDKEDLLPLLEKLKELHPFAEIFPISALKGENVDE 159

                 ....*....
gi 495777602 165 IAGIVRKHL 173
Cdd:cd04163  160 LLEYIVEYL 168
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
8-171 2.98e-42

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: 142.90  E-value: 2.98e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602    8 CGFIAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVGIHTEG--AYQAIYVDTPGlhMEEKRAINRLMNKAASSS 85
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEDgkTYKFNLLDTAG--QEDYDAIRRLYYPQVERS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   86 IGDVELVIFVVeGTRWTP-DDEMVLNKLRDGKTPVILAVNKVDNVQekADLLPHLQWLGSQMNFLDIVPLSAETGLNVDT 164
Cdd:TIGR00231  79 LRVFDIVILVL-DVEEILeKQTKEIIHHADSGVPIILVGNKIDLKD--ADLKTHVASEFAKLNGEPIIPLSAETGKNIDS 155

                  ....*..
gi 495777602  165 IAGIVRK 171
Cdd:TIGR00231 156 AFKIVEA 162
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
12-165 6.69e-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: 142.00  E-value: 6.69e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  12 AIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVG-IHTEGAYQAIYVDTPGLHmeEKRAINRLMNKAASSSIGDVE 90
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRKeWELLPLGPVVLIDTPGLD--EEGGLGRERVEEARQVADRAD 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495777602  91 LVIFVVEGTRWTPDDEMVLNKLRDGKTPVILAVNKVDNVQEKADLLPHLQWLGSQMNFLDIVPLSAETGLNVDTI 165
Cdd:cd00880   79 LVLLVVDSDLTPVEEEAKLGLLRERGKPVLLVLNKIDLVPESEEEELLRERKLELLPDLPVIAVSALPGEGIDEL 153
KH-II_Era cd22534
type II K-homology (KH) RNA-binding domain found in GTPase Era and similar proteins; GTPase ...
195-281 3.21e-35

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: 122.17  E-value: 3.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602 195 SEIIREKLMRFLGAELPYSVTVEIERFQSNERGGYDINGLILVEREGQKKMVIGNKGAKIKTIGIEARKDMQEMFEAPVH 274
Cdd:cd22534    1 AEIIREKLLELLRQELPYSVAVEIEEWEEREDGSLRIEAEIIVEKESQKKIIIGKGGATIKKIGIEARKDLEKLFGRKVY 80

                 ....*..
gi 495777602 275 LELWVKV 281
Cdd:cd22534   81 LKLWVKV 87
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
11-176 2.00e-34

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 129.76  E-value: 2.00e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLHMEEKRAINRLMNKAASSSIGDVE 90
Cdd:COG1160    5 VAIVGRPNVGKSTLFNRLTGRRDAIVDDTPGVTRDRIYGEAEWGGREFTLIDTGGIEPDDDDGLEAEIREQAELAIEEAD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  91 LVIFVVEG-TRWTPDDEMVLNKLRDGKTPVILAVNKVDNVQEKADLLPHLQwLGsqmnFLDIVPLSAETGLNVDTIAGIV 169
Cdd:COG1160   85 VILFVVDGrAGLTPLDEEIAKLLRRSGKPVILVVNKVDGPKREADAAEFYS-LG----LGEPIPISAEHGRGVGDLLDAV 159

                 ....*..
gi 495777602 170 RKHLPEA 176
Cdd:COG1160  160 LELLPEE 166
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
12-173 1.14e-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: 120.62  E-value: 1.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  12 AIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLHMEEKRaINRLMNKAASSSIGDVEL 91
Cdd:cd01894    1 AIVGRPNVGKSTLFNRLTGRRDAIVSDTPGVTRDRKYGEAEWGGREFILIDTGGIEPDDEG-ISKEIREQAEIAIEEADV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  92 VIFVV---EGTrwTPDDEMVLNKLRDGKTPVILAVNKVDNVQEKADLLPhLQWLGsqmnFLDIVPLSAETGLNVDTIAGI 168
Cdd:cd01894   80 ILFVVdgrEGL--TPADEEIAKYLRKSKKPVILVVNKIDNIKEEEEAAE-FYSLG----FGEPIPISAEHGRGIGDLLDA 152

                 ....*
gi 495777602 169 VRKHL 173
Cdd:cd01894  153 ILELL 157
GTPase_EngA TIGR03594
ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase ...
11-187 2.63e-33

ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase with a duplication of its GTP-binding domain. It is broadly to universally distributed among bacteria. It appears to function in ribosome biogenesis or stability. [Protein synthesis, Other]


Pssm-ID: 274667 [Multi-domain]  Cd Length: 428  Bit Score: 126.41  E-value: 2.63e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   11 IAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLhMEEKRAINRLMNKAASSSIGDVE 90
Cdd:TIGR03594   1 VAIVGRPNVGKSTLFNRLTGKRDAIVDDTPGVTRDRIYGDAEWGGREFILIDTGGI-EEDDDGIDAQIREQAEIAIEEAD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   91 LVIFVVEG-TRWTPDDEMVLNKLRDGKTPVILAVNKVDNVQEKADLLPhLQWLGsqmnFLDIVPLSAETGLNVDTIAGIV 169
Cdd:TIGR03594  80 VILFVVDGrEGLTPEDEEIAKWLRKSGKPVILVANKIDGPKEDADAAE-FYSLG----FGEPIPISAEHGRGIGDLLDAI 154
                         170
                  ....*....|....*...
gi 495777602  170 RKHLPEAihHFPEEYITD 187
Cdd:TIGR03594 155 LELLPEE--EEEEEEEED 170
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
11-183 8.00e-32

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 122.47  E-value: 8.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLhMEEKRAINRLMNKAASSSIGDVE 90
Cdd:PRK00093   4 VAIVGRPNVGKSTLFNRLTGKRDAIVADTPGVTRDRIYGEAEWLGREFILIDTGGI-EPDDDGFEKQIREQAELAIEEAD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  91 LVIFVVEG-TRWTPDDEMVLNKLRDGKTPVILAVNKVDNVQEKADLLPHLQwLGsqmnFLDIVPLSAETGLNVDTIAGIV 169
Cdd:PRK00093  83 VILFVVDGrAGLTPADEEIAKILRKSNKPVILVVNKVDGPDEEADAYEFYS-LG----LGEPYPISAEHGRGIGDLLDAI 157
                        170
                 ....*....|....
gi 495777602 170 RKHLPEAIHHFPEE 183
Cdd:PRK00093 158 LEELPEEEEEDEED 171
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
10-125 9.36e-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: 106.55  E-value: 9.36e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   10 FIAIVGRPNVGKSTLLNNLLGQKiSITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLHmeeKRAINRLMNKAASSSIGDV 89
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK-AIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLI---EGASEGEGLGRAFLAIIEA 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 495777602   90 ELVIFVVEGTR-WTPDDEMVLNKLRDGKTPVILAVNK 125
Cdd:pfam01926  77 DLILFVVDSEEgITPLDEELLELLRENKKPIILVLNK 113
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
12-165 8.83e-25

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: 97.53  E-value: 8.83e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  12 AIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVG--IHTEGAYQAIYVDTPGLhmEEKRAINRLmnKAASSSIGDV 89
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYvkELDKGKVKLVLVDTPGL--DEFGGLGRE--ELARLLLRGA 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495777602  90 ELVIFVVEGTRWTPDDEM---VLNKLRDGKTPVILAVNKVDNVQEKADLLPHLQWLGSQMNFLDIVPLSAETGLNVDTI 165
Cdd:cd00882   77 DLILLVVDSTDRESEEDAkllILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAKILGVPVFEVSAKTGEGVDEL 155
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
11-163 5.56e-22

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: 89.86  E-value: 5.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRI-VGIHTEGaYQAIYVDTPGLHME----EKRAINRLMNKAASSs 85
Cdd:cd04164    6 VVIAGKPNVGKSSLLNALAGRDRAIVSDIAGTTRDVIeEEIDLGG-IPVRLIDTAGLRETedeiEKIGIERAREAIEEA- 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495777602  86 igdvELVIFVVEGTR-WTPDDEMVLNKLRdgKTPVILAVNkvdnvqeKADLLPHlQWLGSQMNFLDIVPLSAETGLNVD 163
Cdd:cd04164   84 ----DLVLLVVDASEgLDEEDLEILELPA--KKPVIVVLN-------KSDLLSD-AEGISELNGKPIIAISAKTGEGID 148
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
11-165 1.89e-21

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: 89.03  E-value: 1.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGL----HME---EKRAINRlmnkaAS 83
Cdd:cd01895    5 IAIIGRPNVGKSSLLNALLGEERVIVSDIAGTTRDSIDVPFEYDGQKYTLIDTAGIrkkgKVTegiEKYSVLR-----TL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  84 SSIGDVELVIFVVEGTRWTPD-DEMVLNKLRDGKTPVILAVNKVDNVQEKADLLPHL-QWLGSQMNFLD---IVPLSAET 158
Cdd:cd01895   80 KAIERADVVLLVLDASEGITEqDLRIAGLILEEGKALIIVVNKWDLVEKDEKTMKEFeKELRRKLPFLDyapIVFISALT 159

                 ....*..
gi 495777602 159 GLNVDTI 165
Cdd:cd01895  160 GQGVDKL 166
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
11-163 5.41e-21

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: 92.43  E-value: 5.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRI-VGIHTEGayqaIYV---DTPGLHmE-----EKRAINRLMNKA 81
Cdd:COG0486  216 VVIVGRPNVGKSSLLNALLGEERAIVTDIAGTTRDVIeERINIGG----IPVrliDTAGLR-EtedevEKIGIERAREAI 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  82 ASSsigdvELVIFVVEGTR-WTPDDEMVLNKLRDgkTPVILAVNkvdnvqeKADLLPHLQWLGSQMNFLDIVPLSAETGL 160
Cdd:COG0486  291 EEA-----DLVLLLLDASEpLTEEDEEILEKLKD--KPVIVVLN-------KIDLPSEADGELKSLPGEPVIAISAKTGE 356

                 ...
gi 495777602 161 NVD 163
Cdd:COG0486  357 GID 359
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
11-163 4.74e-19

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: 85.61  E-value: 4.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   11 IAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRI-VGIHTEGaYQAIYVDTPGLHME----EKRAINRLMNKAASSs 85
Cdd:pfam12631  97 VVIVGKPNVGKSSLLNALLGEERAIVTDIPGTTRDVIeETINIGG-IPLRLIDTAGIRETddevEKIGIERAREAIEEA- 174
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495777602   86 igdvELVIFVVEGTR-WTPDDEMVLNKLRDGKtPVILAVNKVDNVQEKADLLPHlqwlgsqmNFLDIVPLSAETGLNVD 163
Cdd:pfam12631 175 ----DLVLLVLDASRpLDEEDLEILELLKDKK-PIIVVLNKSDLLGEIDELEEL--------KGKPVLAISAKTGEGLD 240
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
11-191 1.22e-18

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 85.55  E-value: 1.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRI-VGIHTEGaYQAIYVDTPGLHmE-----EKRAINRLMNKAASS 84
Cdd:PRK05291 218 VVIAGRPNVGKSSLLNALLGEERAIVTDIAGTTRDVIeEHINLDG-IPLRLIDTAGIR-EtddevEKIGIERSREAIEEA 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  85 sigdvELVIFVVEGTR-WTPDDEMVLNKLRDgkTPVILAVNkvdnvqeKADLLPhlQWLGSQMNFLDIVPLSAETGLNVD 163
Cdd:PRK05291 296 -----DLVLLVLDASEpLTEEDDEILEELKD--KPVIVVLN-------KADLTG--EIDLEEENGKPVIRISAKTGEGID 359
                        170       180
                 ....*....|....*....|....*....
gi 495777602 164 TIAGIVRKHLPEAIHHFPEE-YITdrSQR 191
Cdd:PRK05291 360 ELREAIKELAFGGFGGNQEGvFLT--NAR 386
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
11-165 1.31e-18

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 85.46  E-value: 1.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRI-VGIHTEGaYQAIYVDTPGL----HME---EKRAINRlmnkaA 82
Cdd:COG1160  178 IAIVGRPNVGKSSLINALLGEERVIVSDIAGTTRDSIdTPFERDG-KKYTLIDTAGIrrkgKVDegiEKYSVLR-----T 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  83 SSSIGDVELVIFVVEGTR-WTPDDEMVLNK-LRDGKtPVILAVNKVDNVQEKADLLPHL-----QWLGsQMNFLDIVPLS 155
Cdd:COG1160  252 LRAIERADVVLLVIDATEgITEQDLKIAGLaLEAGK-ALVIVVNKWDLVEKDRKTREELekeirRRLP-FLDYAPIVFIS 329
                        170
                 ....*....|
gi 495777602 156 AETGLNVDTI 165
Cdd:COG1160  330 ALTGQGVDKL 339
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
11-134 9.28e-18

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 83.10  E-value: 9.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIvgihtegAYQAIY-------VDTPGLHMEEKrAINRLMNKAAS 83
Cdd:PRK03003  41 VAVVGRPNVGKSTLVNRILGRREAVVEDVPGVTRDRV-------SYDAEWngrrftvVDTGGWEPDAK-GLQASVAEQAE 112
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495777602  84 SSIGDVELVIFVVEGT-RWTPDDEMVLNKLRDGKTPVILAVNKVDNVQEKAD 134
Cdd:PRK03003 113 VAMRTADAVLFVVDATvGATATDEAVARVLRRSGKPVILAANKVDDERGEAD 164
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
11-165 1.42e-17

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 82.41  E-value: 1.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRI-VGIHTEGaYQAIYVDTPGL-------HMEEKRAINRLMNkaa 82
Cdd:PRK00093 176 IAIIGRPNVGKSSLINALLGEERVIVSDIAGTTRDSIdTPFERDG-QKYTLIDTAGIrrkgkvtEGVEKYSVIRTLK--- 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  83 ssSIGDVELVIFVVEGTR-WTPDDEMVLNK-LRDGKtPVILAVNKVDNVQE------KADLLPHLQwlgsQMNFLDIVPL 154
Cdd:PRK00093 252 --AIERADVVLLVIDATEgITEQDLRIAGLaLEAGR-ALVIVVNKWDLVDEktmeefKKELRRRLP----FLDYAPIVFI 324
                        170
                 ....*....|.
gi 495777602 155 SAETGLNVDTI 165
Cdd:PRK00093 325 SALTGQGVDKL 335
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
11-173 1.20e-16

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 76.17  E-value: 1.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISI----TSRKAQTTRHRIvgIHTEGAYQAIYVDTPGLhmEEKRAINRLMnkaaSSSI 86
Cdd:COG1100    6 IVVVGTGGVGKTSLVNRLVGDIFSLekylSTNGVTIDKKEL--KLDGLDVDLVIWDTPGQ--DEFRETRQFY----ARQL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  87 GDVELVIFVVEGTRWTPDDEMV--LNKLRD--GKTPVILAVNKVDNVQEKaDLLPH--LQWLGSQMNFLDIVPLSAETGL 160
Cdd:COG1100   78 TGASLYLFVVDGTREETLQSLYelLESLRRlgKKSPIILVLNKIDLYDEE-EIEDEerLKEALSEDNIVEVVATSAKTGE 156
                        170
                 ....*....|...
gi 495777602 161 NVDTIAGIVRKHL 173
Cdd:COG1100  157 GVEELFAALAEIL 169
KH_2 pfam07650
KH domain;
209-286 3.15e-16

KH domain;


Pssm-ID: 429574 [Multi-domain]  Cd Length: 78  Bit Score: 71.81  E-value: 3.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  209 ELPYSVTVEIERFqsnERGGYDI----NGLILVEREGQKKMVIGNKGAKIKTIGIEARKDMQEMFEAPVHLELWvKVKSG 284
Cdd:pfam07650   1 EIPYSLAVELKFA---GVSKVEIertpNAVIVVIRASQPGIVIGKGGSRIKKIGKELRKDIEKLLGKKVYLNIV-KVKKP 76

                  ..
gi 495777602  285 WA 286
Cdd:pfam07650  77 WL 78
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
9-135 7.34e-16

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 77.91  E-value: 7.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   9 GFIAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLHMEEKrAINRLMNKAASSSIGD 88
Cdd:PRK09518 276 GVVAIVGRPNVGKSTLVNRILGRREAVVEDTPGVTRDRVSYDAEWAGTDFKLVDTGGWEADVE-GIDSAIASQAQIAVSL 354
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 495777602  89 VELVIFVVEG-TRWTPDDEMVLNKLRDGKTPVILAVNKVDNVQEKADL 135
Cdd:PRK09518 355 ADAVVFVVDGqVGLTSTDERIVRMLRRAGKPVVLAVNKIDDQASEYDA 402
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
11-173 1.64e-15

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: 72.54  E-value: 1.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQK-ISITSRKAQTTRH----RIVGihtegayQAIYVDTPG-----LHMEEKRAINRLMNK 80
Cdd:cd01876    2 VAFAGRSNVGKSSLINALTNRKkLARTSKTPGRTQLinffNVGD-------KFRLVDLPGygyakVSKEVREKWGKLIEE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  81 --AASSSIgdvELVIFVVEGTR-WTPDDEMVLNKLRDGKTPVILAVNKVDNV--QEKADLLPHL-QWLGSQMNFLDIVPL 154
Cdd:cd01876   75 ylENRENL---KGVVLLIDARHgPTPIDLEMLEFLEELGIPFLIVLTKADKLkkSELAKVLKKIkEELNLFNILPPVILF 151
                        170
                 ....*....|....*....
gi 495777602 155 SAETGLNVDTIAGIVRKHL 173
Cdd:cd01876  152 SSKKGTGIDELRALIAEWL 170
YeeP COG3596
Predicted GTPase [General function prediction only];
11-176 9.14e-13

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 67.48  E-value: 9.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRH--RIVgIHTEGAYQAIYVDTPGLH--MEEKRAINRLMNKAAsssi 86
Cdd:COG3596   42 IALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREiqRYR-LESDGLPGLVLLDTPGLGevNERDREYRELRELLP---- 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  87 gDVELVIFVVEGTRwtPDDEMVLNKLRDGKT-----PVILAVNKVDNVQEKADLLPHLQWLGS-QMNFL----------- 149
Cdd:COG3596  117 -EADLILWVVKADD--RALATDEEFLQALRAqypdpPVLVVLTQVDRLEPEREWDPPYNWPSPpKEQNIrraleaiaeql 193
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 495777602 150 -----DIVPLSAE---TGLNVDTIAGIVRKHLPEA 176
Cdd:COG3596  194 gvpidRVIPVSAAedrTGYGLEELVDALAEALPEA 228
mnmE_trmE_thdF TIGR00450
tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF ...
11-127 1.49e-12

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: 67.51  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   11 IAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLHmEEKRAINRLMNKAASSSIGDVE 90
Cdd:TIGR00450 206 LAIVGSPNVGKSSLLNALLKQDRAIVSDIKGTTRDVVEGDFELNGILIKLLDTAGIR-EHADFVERLGIEKSFKAIKQAD 284
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 495777602   91 LVIFVVEGTR-WTPDDEMV--LNKLrdgKTPVILAVNKVD 127
Cdd:TIGR00450 285 LVIYVLDASQpLTKDDFLIidLNKS---KKPFILVLNKID 321
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
11-183 1.46e-11

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 64.08  E-value: 1.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNnllgqkiSITSRKAQ------TTRHRIVGiHTEGAYQAIY-VDTPGL---HME-----EKRAIN 75
Cdd:COG1084  163 IVVAGYPNVGKSSLVS-------KVTSAKPEiasypfTTKGIIVG-HFERGHGRYQvIDTPGLldrPLSerneiERQAIL 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  76 RLMNkaasssIGDVELVIFVVEGTR-WTPDDEM-VLNKLRDG-KTPVILAVNKVDNVQEKadllphlqwLGSQMNFLDIV 152
Cdd:COG1084  235 ALKH------LADVILFLFDPSETCgYSLEEQLnLLEEIRSLfDVPVIVVINKIDLSDEE---------ELKEAEEEADI 299
                        170       180       190
                 ....*....|....*....|....*....|.
gi 495777602 153 PLSAETGLNVDTiagiVRKHLPEAIHHFPEE 183
Cdd:COG1084  300 KISALTGEGVDE----LLDELIEALEEEPEL 326
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
11-173 3.82e-10

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 60.58  E-value: 3.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLHMEEKRAINR-----LMNKAAsss 85
Cdd:PRK09518 453 VALVGRPNVGKSSLLNQLTHEERAVVNDLAGTTRDPVDEIVEIDGEDWLFIDTAGIKRRQHKLTGAeyyssLRTQAA--- 529
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  86 IGDVELVIFVVEGTRWTPD-DEMVLNKLRDGKTPVILAVNKVDNVQEKADllphlQWLGSQMNF-LDIVP------LSAE 157
Cdd:PRK09518 530 IERSELALFLFDASQPISEqDLKVMSMAVDAGRALVLVFNKWDLMDEFRR-----QRLERLWKTeFDRVTwarrvnLSAK 604
                        170
                 ....*....|....*.
gi 495777602 158 TGLNVDTIAGIVRKHL 173
Cdd:PRK09518 605 TGWHTNRLAPAMQEAL 620
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
12-167 1.08e-09

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: 55.81  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  12 AIVGRPNVGKSTLLNNLLGQKISITSRKAQTTR--HRIV-GIHTEGayqAIYVDTPGLhmEEKRAINRLMNKAASSSIGD 88
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRaaQAYVwQTGGDG---LVLLDLPGV--GERGRRDREYEELYRRLLPE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  89 VELVIFVVEgtrwtPDD-------EMVLNKLRDGKTPVILAVNKVDNVqekadllphlqwlgsqmnfldiVPLSAETGLN 161
Cdd:cd11383   76 ADLVLWLLD-----ADDralaadhDFYLLPLAGHDAPLLFVLNQVDPV----------------------LAVSARTGWG 128

                 ....*.
gi 495777602 162 VDTIAG 167
Cdd:cd11383  129 LDELAE 134
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
13-88 6.18e-09

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 55.88  E-value: 6.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  13 IVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRI---VGIHTEgayqaIYvDTPGL---HMEEKRAINRLmnkAASSSI 86
Cdd:COG1161  118 IVGIPNVGKSTLINRLAGKKVAKTGNKPGVTKGQQwikLDDGLE-----LL-DTPGIlwpKFEDPEVGYKL---AATGAI 188

                 ..
gi 495777602  87 GD 88
Cdd:COG1161  189 KD 190
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
11-165 6.40e-09

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: 53.99  E-value: 6.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   11 IAIVGRPNVGKSTLLNNLLG--QKISITSRkaqTTRHRIVGIHTEGAYQAIYVDTPGLH------MEEKRAINRLMNkaa 82
Cdd:pfam02421   3 IALVGNPNVGKTTLFNALTGanQHVGNWPG---VTVEKKEGKFKYKGYEIEIVDLPGIYslspysEEERVARDYLLN--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   83 sssiGDVELVIFVVEGTRwtpddemvLNK-------LRDGKTPVILAVNKVDNVQEK-----ADLLPHLqwLGsqmnfLD 150
Cdd:pfam02421  77 ----EKPDVIVNVVDATN--------LERnlyltlqLLELGLPVVLALNMMDEAEKKgikidIKKLSEL--LG-----VP 137
                         170
                  ....*....|....*
gi 495777602  151 IVPLSAETGLNVDTI 165
Cdd:pfam02421 138 VVPTSARKGEGIDEL 152
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
11-163 1.03e-08

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: 53.72  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISITSRkAQTTRHRIVGiHTEGAYQAIYV-DTPGL---HME-----EKRAINRLMNKA 81
Cdd:cd01897    3 LVIAGYPNVGKSSLVNKLTRAKPEVAPY-PFTTKSLFVG-HFDYKYLRWQViDTPGIldrPLEerntiEMQAITALAHLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  82 AsssigdveLVIFVVEGTR---WTPDDEMVL----NKLRDgkTPVILAVNKVDNVQEkaDLLPHLQWLGSQMNFlDIVPL 154
Cdd:cd01897   81 A--------AVLFFIDPSEtcgYSIEEQLSLfkeiKPLFN--KPVIVVLNKIDLLTE--EDLSEIEKELEKEGE-EVIKI 147

                 ....*....
gi 495777602 155 SAETGLNVD 163
Cdd:cd01897  148 STLTEEGVD 156
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
11-173 1.10e-08

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 55.75  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLHMEEKRA-----INRLMNKAAsss 85
Cdd:PRK03003 214 VALVGKPNVGKSSLLNKLAGEERSVVDDVAGTTVDPVDSLIELGGKTWRFVDTAGLRRRVKQAsgheyYASLRTHAA--- 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  86 IGDVELVIFVVEGTR-WTPDDEMVLNKLRDGKTPVILAVNKVDNVQE--------KADL-LPHLQWLGSqmnfldiVPLS 155
Cdd:PRK03003 291 IEAAEVAVVLIDASEpISEQDQRVLSMVIEAGRALVLAFNKWDLVDEdrryylerEIDReLAQVPWAPR-------VNIS 363
                        170
                 ....*....|....*...
gi 495777602 156 AETGLNVDTIAGIVRKHL 173
Cdd:PRK03003 364 AKTGRAVDKLVPALETAL 381
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
11-174 2.26e-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: 53.07  E-value: 2.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISITSRKA---------QTTRHRIVGIHTE------GAYQAIYVDTPGlHmeekraIN 75
Cdd:cd00881    2 VGVIGHVDHGKTTLTGSLLYQTGAIDRRGTrketfldtlKEERERGITIKTGvvefewPKRRINFIDTPG-H------ED 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  76 RLMNKAASSSIGDVELVIF-VVEGTrwTPDDEMVLNKLRDGKTPVILAVNKVDNV-QEKAD--------LLPHLQWLgsQ 145
Cdd:cd00881   75 FSKETVRGLAQADGALLVVdANEGV--EPQTREHLNIALAGGLPIIVAVNKIDRVgEEDFDevlreikeLLKLIGFT--F 150
                        170       180       190
                 ....*....|....*....|....*....|.
gi 495777602 146 MNFLD--IVPLSAETGLNVDTIAGIVRKHLP 174
Cdd:cd00881  151 LKGKDvpIIPISALTGEGIEELLDAIVEHLP 181
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
11-173 2.77e-08

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: 52.77  E-value: 2.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQK-ISITSRKAQTTRH----RIVGihtegayQAIYVDTPG-----LHMEEKRAINRLMNK 80
Cdd:COG0218   26 IAFAGRSNVGKSSLINALTNRKkLARTSKTPGKTQLinffLIND-------KFYLVDLPGygyakVSKAEKEKWQKLIED 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  81 --AASSSIgdvELVIFVVEGTR-WTPDDEMVLNKLRDGKTPVILAVNKVDNVQeKADLLPHL----QWLGSQMNFLDIVP 153
Cdd:COG0218   99 ylEGRENL---KGVVLLIDIRHpPKELDLEMLEWLDEAGIPFLIVLTKADKLK-KSELAKQLkaikKALGKDPAAPEVIL 174
                        170       180
                 ....*....|....*....|
gi 495777602 154 LSAETGLNVDTIAGIVRKHL 173
Cdd:COG0218  175 FSSLKKEGIDELRAAIEEWL 194
PRK04213 PRK04213
GTP-binding protein EngB;
11-176 5.81e-08

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 51.84  E-value: 5.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISiTSRKAQTTRhRIvgIHTEGAyQAIYVDTPGL-HME--EKRAINRLMNK------- 80
Cdd:PRK04213  12 IVFVGRSNVGKSTLVRELTGKKVR-VGKRPGVTR-KP--NHYDWG-DFILTDLPGFgFMSgvPKEVQEKIKDEivryied 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  81 -----AASSSIGDVELVIFVVEgtRWTPDDEM-----VLNKLRDGKTPVILAVNKVDNVQEKADLL-----------PHL 139
Cdd:PRK04213  87 nadriLAAVLVVDGKSFIEIIE--RWEGRGEIpidveMFDFLRELGIPPIVAVNKMDKIKNRDEVLdeiaerlglypPWR 164
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 495777602 140 QWLGSqmnfldIVPLSAETGlNVDTIAGIVRKHLPEA 176
Cdd:PRK04213 165 QWQDI------IAPISAKKG-GIEELKEAIRKRLHEA 194
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
11-65 7.90e-08

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: 50.99  E-value: 7.90e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRH-RIVGIHTEgayqaIYV-DTPG 65
Cdd:cd01856  118 AMVVGIPNVGKSTLINRLRGKKVAKVGNKPGVTRGqQWIRIGPN-----IELlDTPG 169
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
15-224 3.61e-07

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: 51.28  E-value: 3.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   15 GRPNVGKSTLLNNLLGQKISItSRKAQTTRHRIVGIHTEGAYQAIYVDTPGLH------MEEKRAINRLMNkaasssiGD 88
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTV-GNWPGVTVEKKEGKLGFQGEDIEIVDLPGIYslttfsLEEEVARDYLLN-------EK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   89 VELVIFVVEGTRWTPDDEMVLNKLRDGKtPVILAVNKVDNVQEK-----ADLLPHLqwLGsqmnfLDIVPLSAETGLNVD 163
Cdd:TIGR00437  73 PDLVVNVVDASNLERNLYLTLQLLELGI-PMILALNLVDEAEKKgiridEEKLEER--LG-----VPVVPTSATEGRGIE 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495777602  164 TIAGIVRK------HLPEAIHHFPEEYiTDRSQRFMASEIIREKLMRFLGAELP--YSVTVEIERFQSN 224
Cdd:TIGR00437 145 RLKDAIRKaiglkeLKKRAIEIVPEAY-QVVEVVEGLIEIIYSISKRGLEILLGllEDLSLEIEKIERN 212
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
11-174 4.22e-07

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: 49.45  E-value: 4.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   11 IAIVGRPNVGKSTLLNNLL---GQKISITSRKAQTTRH-------RIVGI---------HTEGAYQAIyVDTPGlHmeek 71
Cdd:pfam00009   6 IGIIGHVDHGKTTLTDRLLyytGAISKRGEVKGEGEAGldnlpeeRERGItiksaavsfETKDYLINL-IDTPG-H---- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   72 RAINRLMNKAASSSIGDVeLVIFVVEGTrwTPDDEMVLNKLRDGKTPVILAVNKVDNV----------QEKADLlphLQW 141
Cdd:pfam00009  80 VDFVKEVIRGLAQADGAI-LVVDAVEGV--MPQTREHLRLARQLGVPIIVFINKMDRVdgaeleevveEVSREL---LEK 153
                         170       180       190
                  ....*....|....*....|....*....|...
gi 495777602  142 LGSQMNFLDIVPLSAETGLNVDTIAGIVRKHLP 174
Cdd:pfam00009 154 YGEDGEFVPVVPGSALKGEGVQTLLDALDEYLP 186
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
12-163 7.84e-07

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: 47.84  E-value: 7.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  12 AIVGRPNVGKSTLLNNLLG--QKISITSRkaqTTRHRIVGIHTEGAYQAIYVDTPGLH------MEEKRAINRLMNkaas 83
Cdd:cd01879    1 ALVGNPNVGKTTLFNALTGarQKVGNWPG---VTVEKKEGEFKLGGKEIEIVDLPGTYsltpysEDEKVARDFLLG---- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  84 ssiGDVELVIFVVEGTRwtpddemvLNK--------LRDGKtPVILAVNKVDNVQEK-----ADLLPHLqwLGSQmnfld 150
Cdd:cd01879   74 ---EEPDLIVNVVDATN--------LERnlyltlqlLELGL-PVVVALNMIDEAEKRgikidLDKLSEL--LGVP----- 134
                        170
                 ....*....|...
gi 495777602 151 IVPLSAETGLNVD 163
Cdd:cd01879  135 VVPTSARKGEGID 147
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
11-183 9.40e-07

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 50.12  E-value: 9.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLG--QKIS----IT-SRKaqttrhriVGIHTEGAYQAIYVDTPG---LH---MEEKRAINRL 77
Cdd:COG0370    6 IALVGNPNVGKTTLFNALTGsrQKVGnwpgVTvEKK--------EGKFKLKGKEIELVDLPGtysLSaysPDEKVARDFL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  78 MNkaasssiGDVELVIFVVEGTRwtpddemvLNK-------LRDGKTPVILAVNKVDNVQEK-----ADLLPHLqwLGsq 145
Cdd:COG0370   78 LE-------EKPDVVVNVVDATN--------LERnlyltlqLLELGIPVVLALNMMDEAEKKgikidVEKLSKL--LG-- 138
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 495777602 146 mnfLDIVPLSAETGLNVD----TIAGIVR-KHLPEAIHHFPEE 183
Cdd:COG0370  139 ---VPVVPTSARKGKGIDelkeAIIEAAEgKKPRPLRIDYPEE 178
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
12-173 1.55e-06

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: 47.39  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  12 AIVGRPNVGKSTLLNNLLGQKISITSrKAQTTRHRIVGIHTEGAYQAI-YVDTPGL------HMEEKRAINRLMNKAass 84
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAKVEIAS-YPFTTLEPNVGVFEFGDGVDIqIIDLPGLldgaseGRGLGEQILAHLYRS--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  85 sigdvELVIFVVEGT----RWTPDDEMVLN------KLRDGKTPVILAVNKVDNVQEkaDLLPHLQWLGSQmNFLDIVPL 154
Cdd:cd01881   77 -----DLILHVIDASedcvGDPLEDQKTLNeevsgsFLFLKNKPEMIVANKIDMASE--NNLKRLKLDKLK-RGIPVVPT 148
                        170
                 ....*....|....*....
gi 495777602 155 SAETGLNVDTIAGIVRKHL 173
Cdd:cd01881  149 SALTRLGLDRVIRTIRKLL 167
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
11-97 1.78e-06

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: 48.27  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   11 IAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRH-RIVGIHTEgayqaIYV-DTPGL---HMEEKRAINRLmnkAASSS 85
Cdd:TIGR03596 121 AMIVGIPNVGKSTLINRLAGKKVAKVGNRPGVTKGqQWIKLSDN-----LELlDTPGIlwpKFEDQEVGLKL---AATGA 192
                          90
                  ....*....|....*..
gi 495777602   86 IGDV-----ELVIFVVE 97
Cdd:TIGR03596 193 IKDEaldleDVALFLLE 209
infB CHL00189
translation initiation factor 2; Provisional
11-163 1.84e-06

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 49.06  E-value: 1.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNnllgqKIsitsRKAQTTRHRIVGIHTE-GAY-----------QAIYVDTPGlHmeekRAINRLM 78
Cdd:CHL00189 247 VTILGHVDHGKTTLLD-----KI----RKTQIAQKEAGGITQKiGAYevefeykdenqKIVFLDTPG-H----EAFSSMR 312
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  79 NKAASSSigdvELVIFVV---EGTRwtPDDEMVLNKLRDGKTPVILAVNKVD-------NVQE---KADLLPHlQWLGSq 145
Cdd:CHL00189 313 SRGANVT----DIAILIIaadDGVK--PQTIEAINYIQAANVPIIVAINKIDkananteRIKQqlaKYNLIPE-KWGGD- 384
                        170
                 ....*....|....*...
gi 495777602 146 mnfLDIVPLSAETGLNVD 163
Cdd:CHL00189 385 ---TPMIPISASQGTNID 399
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
11-161 2.54e-06

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: 46.77  E-value: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKI---SI--TSRKAQTTRHRI---VGIhtegayqaiyVDTPGLHmeekrAINRLMNKAA 82
Cdd:cd09912    3 LAVVGEFSAGKSTLLNALLGEEVlptGVtpTTAVITVLRYGLlkgVVL----------VDTPGLN-----STIEHHTEIT 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  83 SSSIGDVELVIFVVE----GTRwtpDDEMVLNKLRD-GKTPVILAVNKVDNVQEKADL---------LPHLQWLGsqmNF 148
Cdd:cd09912   68 ESFLPRADAVIFVLSadqpLTE---SEREFLKEILKwSGKKIFFVLNKIDLLSEEELEevleysreeLGVLELGG---GE 141
                        170
                 ....*....|...
gi 495777602 149 LDIVPLSAETGLN 161
Cdd:cd09912  142 PRIFPVSAKEALE 154
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
11-66 1.54e-05

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: 43.76  E-value: 1.54e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISITSRKAQTTRHrivgihtegaYQAIYV-------DTPGL 66
Cdd:cd01857   85 IGLVGYPNVGKSSLINALVGSKKVSVSSTPGKTKH----------FQTIFLepgitlcDCPGL 137
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
11-173 2.46e-05

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: 44.37  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGqkisiTSRKAQ--------TTRHRivgIHTEGAYQAIYVDTPGL-----H---------M 68
Cdd:cd01878   44 VALVGYTNAGKSTLFNALTG-----ADVLAEdqlfatldPTTRR---IKLPGGREVLLTDTVGFirdlpHqlveafrstL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  69 EEkrainrlmnkaasssIGDVELVIFVVEGTRWTPDDEM-----VLNKLRDGKTPVILAVNKVDNVQEKAdllphlQWLG 143
Cdd:cd01878  116 EE---------------VAEADLLLHVVDASDPDREEQIetveeVLKELGADDIPIILVLNKIDLLDDEE------LEER 174
                        170       180       190
                 ....*....|....*....|....*....|
gi 495777602 144 SQMNFLDIVPLSAETGLNVDTIAGIVRKHL 173
Cdd:cd01878  175 LRAGRPDAVFISAKTGEGLDLLKEAIEELL 204
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
11-163 2.85e-05

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: 43.61  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLlgQKISITSRKAQ-TTRHrivgIhteGAYQAIY---------VDTPGlHmeekRAINRLMNK 80
Cdd:cd01887    3 VTVMGHVDHGKTTLLDKI--RKTNVAAGEAGgITQH----I---GAYQVPIdvkipgitfIDTPG-H----EAFTNMRAR 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  81 AASssIGD-VELVIFVVEGTRwtPDDEMVLNKLRDGKTPVILAVNKVD-------NVQE-KADLLPH----LQWLGSQMn 147
Cdd:cd01887   69 GAS--VTDiAILVVAADDGVM--PQTIEAINHAKAANVPIIVAINKIDkpygteaDPERvKNELSELglvgEEWGGDVS- 143
                        170
                 ....*....|....*.
gi 495777602 148 fldIVPLSAETGLNVD 163
Cdd:cd01887  144 ---IVPISAKTGEGID 156
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
11-96 3.20e-05

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 44.79  E-value: 3.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKiSITSRKAQTTRHRIVGI-HTEGAYQAIyVDTPGLhmEEKRAINRLMNKAASSSIGDV 89
Cdd:COG1163   66 VVLVGFPSVGKSTLLNKLTNAK-SEVGAYEFTTLDVVPGMlEYKGAKIQI-LDVPGL--IEGAASGKGRGKEVLSVVRNA 141

                 ....*..
gi 495777602  90 ELVIFVV 96
Cdd:COG1163  142 DLILIVL 148
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
11-173 4.57e-05

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: 43.18  E-value: 4.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNnllgqkiSITSRKAQ------TTRHRIVG-IHTEGAYQAIYVDTPGLhmeekraInrlmnKAAS 83
Cdd:cd01898    3 VGLVGLPNAGKSTLLS-------AISNAKPKiadypfTTLVPNLGvVRVDDGRSFVIADIPGL-------I-----EGAS 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  84 SSIG-------DVE---LVIFVVEGTrwTPDD-----EMVLNKLR------DGKtPVILAVNKVD--NVQEKADLLPHLQ 140
Cdd:cd01898   64 EGKGlghrflrHIErtrVLLHVIDLS--GEDDpvedyETIRNELEaynpglAEK-PRIVVLNKIDllDAEERFEKLKELL 140
                        170       180       190
                 ....*....|....*....|....*....|...
gi 495777602 141 wlgSQMNFLDIVPLSAETGLNVDTIAGIVRKHL 173
Cdd:cd01898  141 ---KELKGKKVFPISALTGEGLDELLKKLAKLL 170
PRK01889 PRK01889
GTPase RsgA; Reviewed
11-66 4.16e-04

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 41.46  E-value: 4.16e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISIT-------SRKAQTTRHRIVGIHTEGayqAIYVDTPGL 66
Cdd:PRK01889 198 VALLGSSGVGKSTLVNALLGEEVQKTgavreddSKGRHTTTHRELHPLPSG---GLLIDTPGM 257
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
19-70 5.50e-04

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: 40.46  E-value: 5.50e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495777602  19 VGKSTLLNNLLG---QKISITSRKAQ----TTRHRIvgIHT--EGAYqaIyVDTPG------LHMEE 70
Cdd:cd01854   96 VGKSTLLNALLPelvLATGEISEKLGrgrhTTTHRE--LFPlpGGGL--I-IDTPGfrelglLHIDP 157
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
11-127 7.48e-04

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: 39.88  E-value: 7.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQkiSITSRKAQTTRHRIV---------GI-----HTEGAYQAIY---VDTPGlHMEEKRA 73
Cdd:cd01891    5 IAIIAHVDHGKTTLVDALLKQ--SGTFRENEEVGERVMdsndlererGItilakNTAITYKDTKiniIDTPG-HADFGGE 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 495777602  74 INRLMNKAASssigdVELVIFVVEGTRwtPDDEMVLNKLRDGKTPVILAVNKVD 127
Cdd:cd01891   82 VERVLSMVDG-----VLLLVDASEGPM--PQTRFVLKKALEAGLKPIVVINKID 128
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
3-66 8.53e-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: 39.56  E-value: 8.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495777602   3 EEKTYCGFIAIVGRPNVGKSTLLNNLLGQKISITSRKAQ----TTRHrIVG-----IHTEGAYQAIYVDTPGL 66
Cdd:cd01855  120 KLAKYRGDVYVVGATNVGKSTLINALLKSNGGKVQAQALvqrlTVSP-IPGttlglIKIPLGEGKKLYDTPGI 191
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
11-113 1.26e-03

AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 (avrRpt2-induced gene 1) that appears to be involved in plant resistance to bacteria. The Arabidopsis disease resistance gene RPS2 is involved in recognition of bacterial pathogens carrying the avirulence gene avrRpt2. AIG1 exhibits RPS2- and avrRpt1-dependent induction early after infection with Pseudomonas syringae carrying avrRpt2. This subfamily also includes IAN-4 protein, which has GTP-binding activity and shares sequence homology with a novel family of putative GTP-binding proteins: the immuno-associated nucleotide (IAN) family. The evolutionary conservation of the IAN family provides a unique example of a plant pathogen response gene conserved in animals. The IAN/IMAP subfamily has been proposed to regulate apoptosis in vertebrates and angiosperm plants, particularly in relation to cancer, diabetes, and infections. The human IAN genes were renamed GIMAP (GTPase of the immunity associated proteins).


Pssm-ID: 206651 [Multi-domain]  Cd Length: 201  Bit Score: 39.06  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISITSRKAQ-----------TTRHRIVGIhtegayqaiyVDTPGLHM------EEKRA 73
Cdd:cd01852    3 LVLVGKTGNGKSATGNTILGRKVFESKLSASgvtktcqkesaVWDGRRVNV----------IDTPGLFDtsvspeQLSKE 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 495777602  74 INRLMNKAAsssiGDVELVIFVVEGTRWTPDDEMVLNKLR 113
Cdd:cd01852   73 IIRCLSLSA----PGPHAFLLVVPLGRFTEEEEQAVEELQ 108
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
11-183 3.19e-03

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 38.93  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGqkisitSRK-----AQTTRHRIVGIHTEGAYQAIYVDTPGLH----------MEEKRAIN 75
Cdd:PRK09554   6 IGLIGNPNSGKTTLFNQLTG------ARQrvgnwAGVTVERKEGQFSTTDHQVTLVDLPGTYslttissqtsLDEQIACH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  76 RLMNkaasssiGDVELVIFVVEGTRWTPDDEMVLNKLRDGkTPVILAVNKVDNVQekadllphlqwlgSQMNFLDIVPLS 155
Cdd:PRK09554  80 YILS-------GDADLLINVVDASNLERNLYLTLQLLELG-IPCIVALNMLDIAE-------------KQNIRIDIDALS 138
                        170       180       190
                 ....*....|....*....|....*....|...
gi 495777602 156 AETGLNVDTIA-----GIvrKHLPEAIHHFPEE 183
Cdd:PRK09554 139 ARLGCPVIPLVstrgrGI--EALKLAIDRHQAN 169
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
9-65 3.65e-03

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: 37.30  E-value: 3.65e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495777602   9 GFIAIVGRPNVGKSTLLNNLLGQKisitsrKAQTTRHRIVGIHTEG-----AYQAIY-VDTPG 65
Cdd:cd01859  100 VIVGVVGYPKVGKSSIINALKGRH------SASTSPIPGSPGYTKGiqlvrIDSKIYlIDTPG 156
Dynamin_N pfam00350
Dynamin family;
11-37 4.71e-03

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 37.21  E-value: 4.71e-03
                          10        20
                  ....*....|....*....|....*..
gi 495777602   11 IAIVGRPNVGKSTLLNNLLGQKISITS 37
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRG 27
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
10-47 5.98e-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: 5.98e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 495777602  10 FIAIVGrPN-VGKSTLLNNLLGQ------KISITSRKAQTTRHRI 47
Cdd:cd03235   27 FLAIVG-PNgAGKSTLLKAILGLlkptsgSIRVFGKPLEKERKRI 70
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
11-100 6.40e-03

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: 37.14  E-value: 6.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKisitSRKAQ---TTRHRIVG-IHTEGAYQAIyVDTPGLHmeEKRAINRLMNKAASSSI 86
Cdd:cd01896    3 VALVGFPSVGKSTLLSKLTNTK----SEVAAyefTTLTCVPGvMEYKGAKIQL-LDLPGII--EGASDGKGRGRQVIAVA 75
                         90
                 ....*....|....
gi 495777602  87 GDVELVIFVVEGTR 100
Cdd:cd01896   76 RTADLILIVLDATK 89
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
11-76 7.20e-03

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: 37.30  E-value: 7.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495777602  11 IAIVGRPNVGKSTLLNNLLGQKISITS--RKAQTTRHRIVGihTEGAYQAIYVDTPGLHMEEKRAINR 76
Cdd:cd01853   34 ILVLGKTGVGKSSTINSIFGERKVSVSafQSETLRPREVSR--TVDGFKLNIIDTPGLLESQDQRVNR 99
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
11-65 8.15e-03

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: 36.37  E-value: 8.15e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495777602   11 IAIVGRPNVGKSTLLNNLLG------QKISITSRKAQ-TTRHRIVgIHT-EGAYqaiYVDTPG 65
Cdd:pfam03193 109 TVLAGQSGVGKSTLLNALLPeldlrtGEISEKLGRGRhTTTHVEL-FPLpGGGL---LIDTPG 167
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
11-114 9.18e-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: 36.43  E-value: 9.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777602   11 IAIVGRPNVGKSTLLNNLLGQKISITSRKAQT-TRHRIVGIHTEGAYQAIYVDTPGL-----HMEEK-RAINRLMNKAAs 83
Cdd:pfam04548   3 IVLVGKTGNGKSATGNSILGRKAFESKLRAQGvTKTCQLVSRTWDGRIINVIDTPGLfdlsvSNDFIsKEIIRCLLLAE- 81
                          90       100       110
                  ....*....|....*....|....*....|.
gi 495777602   84 ssiGDVELVIFVVEGTRWTPDDEMVLNKLRD 114
Cdd:pfam04548  82 ---PGPHAVLLVLSLGRFTEEEEQALRTLQE 109
 
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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