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Conserved domains on  [gi|690757820|gb|KGF06534|]
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GTPase Era [Arcanobacterium sp. S3PF19]

Protein Classification

GTPase Era( domain architecture ID 11439328)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
9-306 6.07e-159

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


:

Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 444.43  E-value: 6.07e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   9 YRAGFVAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQLILTDTPGLHKPRTLLGQRLNDLVRESL 88
Cdd:COG1159    1 FRSGFVAIVGRPNVGKSTLLNALVGQKVSIVSPKPQTTRHRIRGIVTREDAQIVFVDTPGIHKPKRKLGRRMNKAAWSAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  89 SDLDAVVLCLPADEKIGPGDRFLLNLVRQTKAPIVAAVTKTDKTGREKLAAKLAELGELADFAQIVPVSAVRGEQIGLLT 168
Cdd:COG1159   81 EDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLVKKEELLPLLAEYSELLDFAEIVPISALKGDNVDELL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820 169 DLLLEMMPLSVPLYPTDTLTDETEGELVAEYIREAALEGVREELPHSIAVVVEEIAQRPvkegeknrPLTDVHASIYVER 248
Cdd:COG1159  161 DEIAKLLPEGPPYYPEDQITDRPERFLAAEIIREKILRLLRDELPYSVAVEIEEFEERE--------GLLRIRATIYVER 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 690757820 249 ESQKGIVIGRGGSRLKDVGRRARIPIEELLESRVYLDLRVKVAKDWQRDPKLLGRLGF 306
Cdd:COG1159  233 DSQKGIIIGKGGSMLKKIGTEARKDIEKLLGKKVFLELWVKVKKNWRDDERALRELGY 290
 
Name Accession Description Interval E-value
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
9-306 6.07e-159

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 444.43  E-value: 6.07e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   9 YRAGFVAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQLILTDTPGLHKPRTLLGQRLNDLVRESL 88
Cdd:COG1159    1 FRSGFVAIVGRPNVGKSTLLNALVGQKVSIVSPKPQTTRHRIRGIVTREDAQIVFVDTPGIHKPKRKLGRRMNKAAWSAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  89 SDLDAVVLCLPADEKIGPGDRFLLNLVRQTKAPIVAAVTKTDKTGREKLAAKLAELGELADFAQIVPVSAVRGEQIGLLT 168
Cdd:COG1159   81 EDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLVKKEELLPLLAEYSELLDFAEIVPISALKGDNVDELL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820 169 DLLLEMMPLSVPLYPTDTLTDETEGELVAEYIREAALEGVREELPHSIAVVVEEIAQRPvkegeknrPLTDVHASIYVER 248
Cdd:COG1159  161 DEIAKLLPEGPPYYPEDQITDRPERFLAAEIIREKILRLLRDELPYSVAVEIEEFEERE--------GLLRIRATIYVER 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 690757820 249 ESQKGIVIGRGGSRLKDVGRRARIPIEELLESRVYLDLRVKVAKDWQRDPKLLGRLGF 306
Cdd:COG1159  233 DSQKGIIIGKGGSMLKKIGTEARKDIEKLLGKKVFLELWVKVKKNWRDDERALRELGY 290
era PRK00089
GTPase Era; Reviewed
7-306 3.70e-151

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 424.85  E-value: 3.70e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   7 PDYRAGFVAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQLILTDTPGLHKPRTLLGQRLNDLVRE 86
Cdd:PRK00089   1 MGFKSGFVAIVGRPNVGKSTLLNALVGQKISIVSPKPQTTRHRIRGIVTEDDAQIIFVDTPGIHKPKRALNRAMNKAAWS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  87 SLSDLDAVVLCLPADEKIGPGDRFLLNLVRQTKAPIVAAVTKTDKTG-REKLAAKLAELGELADFAQIVPVSAVRGEQIG 165
Cdd:PRK00089  81 SLKDVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVKdKEELLPLLEELSELMDFAEIVPISALKGDNVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820 166 LLTDLLLEMMPLSVPLYPTDTLTDETEGELVAEYIREAALEGVREELPHSIAVVVEEIaqrpvkegeKNRPLTDVHASIY 245
Cdd:PRK00089 161 ELLDVIAKYLPEGPPYYPEDQITDRPERFLAAEIIREKLLRLLGDELPYSVAVEIEKF---------EERGLVRIEATIY 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 690757820 246 VERESQKGIVIGRGGSRLKDVGRRARIPIEELLESRVYLDLRVKVAKDWQRDPKLLGRLGF 306
Cdd:PRK00089 232 VERDSQKGIIIGKGGAMLKKIGTEARKDIEKLLGKKVFLELWVKVKKGWRDDEKALRELGY 292
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
12-289 1.24e-79

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: 242.68  E-value: 1.24e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   12 GFVAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQLILTDTPGLHKPRTLLGQRLNDLVRESLSDL 91
Cdd:TIGR00436   1 GFVAILGRPNVGKSTLLNQLHGQKISITSPKAQTTRNRISGIHTTGASQIIFIDTPGFHEKKHSLNRLMMKEARSAIGGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   92 DAVVLCLPADEKIGPgDRFLLNLVRQTKAPIVAAVTKTDKTGREKLAAKLAELGELADFAQIVPVSAVRGEQIGLLTDLL 171
Cdd:TIGR00436  81 DLILFVVDSDQWNGD-GEFVLTKLQNLKRPVVLTRNKLDNKFKDKLLPLIDKYAILEDFKDIVPISALTGDNTSFLAAFI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  172 LEMMPLSVPLYPTDTLTDETEGELVAEYIREAALEGVREELPHSIAVVVEEIaqrpvKEGEKNrpLTDVHASIYVERESQ 251
Cdd:TIGR00436 160 EVHLPEGPFRYPEDYVTDQPDRFKISEIIREKIIRYTKEEIPHSVRVEIERK-----SFNEKG--LLKIHALISVERESQ 232
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 690757820  252 KGIVIGRGGSRLKDVGRRARIPIEELLESRVYLDLRVK 289
Cdd:TIGR00436 233 KKIIIGKNGSMIKAIGIAARKDILELFDCDVFLELFVK 270
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
9-175 7.22e-72

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: 219.26  E-value: 7.22e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   9 YRAGFVAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQLILTDTPGLHKPRTLLGQRLNDLVRESL 88
Cdd:cd04163    1 FKSGFVAIIGRPNVGKSTLLNALVGQKISIVSPKPQTTRNRIRGIYTDDDAQIIFVDTPGIHKPKKKLGERMVKAAWSAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  89 SDLDAVVLCLPADEKIGPGDRFLLNLVRQTKAPIVAAVTKTDKTG-REKLAAKLAELGELADFAQIVPVSAVRGEQIGLL 167
Cdd:cd04163   81 KDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLVKdKEDLLPLLEKLKELHPFAEIFPISALKGENVDEL 160

                 ....*...
gi 690757820 168 TDLLLEMM 175
Cdd:cd04163  161 LEYIVEYL 168
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
13-128 1.92e-25

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: 97.69  E-value: 1.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   13 FVAVVGRPNAGKSTLTNALVGKKiAITANQPETTRKAIRAIVSRPAGQLILTDTPGLhkPRTLLGQRLNDLVRESLSDLD 92
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK-AIVSDYPGTTRDPNEGRLELKGKQIILVDTPGL--IEGASEGEGLGRAFLAIIEAD 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 690757820   93 AVVLCLPADEKIGPGDRFLLNLVRQTKAPIVAAVTK 128
Cdd:pfam01926  78 LILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
 
Name Accession Description Interval E-value
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
9-306 6.07e-159

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 444.43  E-value: 6.07e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   9 YRAGFVAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQLILTDTPGLHKPRTLLGQRLNDLVRESL 88
Cdd:COG1159    1 FRSGFVAIVGRPNVGKSTLLNALVGQKVSIVSPKPQTTRHRIRGIVTREDAQIVFVDTPGIHKPKRKLGRRMNKAAWSAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  89 SDLDAVVLCLPADEKIGPGDRFLLNLVRQTKAPIVAAVTKTDKTGREKLAAKLAELGELADFAQIVPVSAVRGEQIGLLT 168
Cdd:COG1159   81 EDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLVKKEELLPLLAEYSELLDFAEIVPISALKGDNVDELL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820 169 DLLLEMMPLSVPLYPTDTLTDETEGELVAEYIREAALEGVREELPHSIAVVVEEIAQRPvkegeknrPLTDVHASIYVER 248
Cdd:COG1159  161 DEIAKLLPEGPPYYPEDQITDRPERFLAAEIIREKILRLLRDELPYSVAVEIEEFEERE--------GLLRIRATIYVER 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 690757820 249 ESQKGIVIGRGGSRLKDVGRRARIPIEELLESRVYLDLRVKVAKDWQRDPKLLGRLGF 306
Cdd:COG1159  233 DSQKGIIIGKGGSMLKKIGTEARKDIEKLLGKKVFLELWVKVKKNWRDDERALRELGY 290
era PRK00089
GTPase Era; Reviewed
7-306 3.70e-151

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 424.85  E-value: 3.70e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   7 PDYRAGFVAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQLILTDTPGLHKPRTLLGQRLNDLVRE 86
Cdd:PRK00089   1 MGFKSGFVAIVGRPNVGKSTLLNALVGQKISIVSPKPQTTRHRIRGIVTEDDAQIIFVDTPGIHKPKRALNRAMNKAAWS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  87 SLSDLDAVVLCLPADEKIGPGDRFLLNLVRQTKAPIVAAVTKTDKTG-REKLAAKLAELGELADFAQIVPVSAVRGEQIG 165
Cdd:PRK00089  81 SLKDVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVKdKEELLPLLEELSELMDFAEIVPISALKGDNVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820 166 LLTDLLLEMMPLSVPLYPTDTLTDETEGELVAEYIREAALEGVREELPHSIAVVVEEIaqrpvkegeKNRPLTDVHASIY 245
Cdd:PRK00089 161 ELLDVIAKYLPEGPPYYPEDQITDRPERFLAAEIIREKLLRLLGDELPYSVAVEIEKF---------EERGLVRIEATIY 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 690757820 246 VERESQKGIVIGRGGSRLKDVGRRARIPIEELLESRVYLDLRVKVAKDWQRDPKLLGRLGF 306
Cdd:PRK00089 232 VERDSQKGIIIGKGGAMLKKIGTEARKDIEKLLGKKVFLELWVKVKKGWRDDEKALRELGY 292
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
12-289 1.24e-79

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: 242.68  E-value: 1.24e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   12 GFVAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQLILTDTPGLHKPRTLLGQRLNDLVRESLSDL 91
Cdd:TIGR00436   1 GFVAILGRPNVGKSTLLNQLHGQKISITSPKAQTTRNRISGIHTTGASQIIFIDTPGFHEKKHSLNRLMMKEARSAIGGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   92 DAVVLCLPADEKIGPgDRFLLNLVRQTKAPIVAAVTKTDKTGREKLAAKLAELGELADFAQIVPVSAVRGEQIGLLTDLL 171
Cdd:TIGR00436  81 DLILFVVDSDQWNGD-GEFVLTKLQNLKRPVVLTRNKLDNKFKDKLLPLIDKYAILEDFKDIVPISALTGDNTSFLAAFI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  172 LEMMPLSVPLYPTDTLTDETEGELVAEYIREAALEGVREELPHSIAVVVEEIaqrpvKEGEKNrpLTDVHASIYVERESQ 251
Cdd:TIGR00436 160 EVHLPEGPFRYPEDYVTDQPDRFKISEIIREKIIRYTKEEIPHSVRVEIERK-----SFNEKG--LLKIHALISVERESQ 232
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 690757820  252 KGIVIGRGGSRLKDVGRRARIPIEELLESRVYLDLRVK 289
Cdd:TIGR00436 233 KKIIIGKNGSMIKAIGIAARKDILELFDCDVFLELFVK 270
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
9-175 7.22e-72

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: 219.26  E-value: 7.22e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   9 YRAGFVAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQLILTDTPGLHKPRTLLGQRLNDLVRESL 88
Cdd:cd04163    1 FKSGFVAIIGRPNVGKSTLLNALVGQKISIVSPKPQTTRNRIRGIYTDDDAQIIFVDTPGIHKPKKKLGERMVKAAWSAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  89 SDLDAVVLCLPADEKIGPGDRFLLNLVRQTKAPIVAAVTKTDKTG-REKLAAKLAELGELADFAQIVPVSAVRGEQIGLL 167
Cdd:cd04163   81 KDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLVKdKEDLLPLLEKLKELHPFAEIFPISALKGENVDEL 160

                 ....*...
gi 690757820 168 TDLLLEMM 175
Cdd:cd04163  161 LEYIVEYL 168
KH-II_Era cd22534
type II K-homology (KH) RNA-binding domain found in GTPase Era and similar proteins; GTPase ...
197-290 6.93e-29

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: 105.99  E-value: 6.93e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820 197 AEYIREAALEGVREELPHSIAVVVEEIaqrpvKEGEKNrpLTDVHASIYVERESQKGIVIGRGGSRLKDVGRRARIPIEE 276
Cdd:cd22534    1 AEIIREKLLELLRQELPYSVAVEIEEW-----EEREDG--SLRIEAEIIVEKESQKKIIIGKGGATIKKIGIEARKDLEK 73
                         90
                 ....*....|....
gi 690757820 277 LLESRVYLDLRVKV 290
Cdd:cd22534   74 LFGRKVYLKLWVKV 87
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
15-174 1.18e-28

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: 107.72  E-value: 1.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  15 AVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIR-AIVSRPAGQLILTDTPGLHKPRTlLGQRLNDLVRESLSDLDA 93
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRkEWELLPLGPVVLIDTPGLDEEGG-LGRERVEEARQVADRADL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  94 VVLCLPADEKIGPGDRFLLNLVRQTKaPIVAAVTKTDK-TGREKLAAKLAELGELADFAQIVPVSAVRGEQIGLLTDLLL 172
Cdd:cd00880   80 VLLVVDSDLTPVEEEAKLGLLRERGK-PVLLVLNKIDLvPESEEEELLRERKLELLPDLPVIAVSALPGEGIDELRKKIA 158

                 ..
gi 690757820 173 EM 174
Cdd:cd00880  159 EL 160
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
15-175 6.00e-27

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: 103.28  E-value: 6.00e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  15 AVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQLILTDTPGLHKPRTLLGQRLNDLVRESLSDLDAV 94
Cdd:cd01894    1 AIVGRPNVGKSTLFNRLTGRRDAIVSDTPGVTRDRKYGEAEWGGREFILIDTGGIEPDDEGISKEIREQAEIAIEEADVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  95 VLCLPADEKIGPGDRFLLNLVRQTKAPIVAAVTKTDKTGREKLAAKLAELGeladFAQIVPVSAVRGEQIGLLTDLLLEM 174
Cdd:cd01894   81 LFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNIKEEEEAAEFYSLG----FGEPIPISAEHGRGIGDLLDAILEL 156

                 .
gi 690757820 175 M 175
Cdd:cd01894  157 L 157
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
13-128 1.92e-25

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: 97.69  E-value: 1.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   13 FVAVVGRPNAGKSTLTNALVGKKiAITANQPETTRKAIRAIVSRPAGQLILTDTPGLhkPRTLLGQRLNDLVRESLSDLD 92
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK-AIVSDYPGTTRDPNEGRLELKGKQIILVDTPGL--IEGASEGEGLGRAFLAIIEAD 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 690757820   93 AVVLCLPADEKIGPGDRFLLNLVRQTKAPIVAAVTK 128
Cdd:pfam01926  78 LILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
14-176 8.64e-25

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 103.21  E-value: 8.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQLILTDTPGLHKPRTLLGQRLNDLVRESLSDLDA 93
Cdd:PRK00093   4 VAIVGRPNVGKSTLFNRLTGKRDAIVADTPGVTRDRIYGEAEWLGREFILIDTGGIEPDDDGFEKQIREQAELAIEEADV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  94 VVLCLPADEKIGPGDRFLLNLVRQTKAPIVAAVTKTDKTGREKLAAKLAELGeladFAQIVPVSAVRGEQIGLLTDLLLE 173
Cdd:PRK00093  84 ILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDGPDEEADAYEFYSLG----LGEPYPISAEHGRGIGDLLDAILE 159

                 ...
gi 690757820 174 MMP 176
Cdd:PRK00093 160 ELP 162
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
14-176 2.85e-24

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 101.64  E-value: 2.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQLILTDTPGL-HKPRTLLGQRLNDLVRESLSDLD 92
Cdd:COG1160    5 VAIVGRPNVGKSTLFNRLTGRRDAIVDDTPGVTRDRIYGEAEWGGREFTLIDTGGIePDDDDGLEAEIREQAELAIEEAD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  93 AVVLCLPADEKIGPGDRFLLNLVRQTKAPIVAAVTKTDKTGREKLAAKLAELGeladFAQIVPVSAVRGEQIGLLTDLLL 172
Cdd:COG1160   85 VILFVVDGRAGLTPLDEEIAKLLRRSGKPVILVVNKVDGPKREADAAEFYSLG----LGEPIPISAEHGRGVGDLLDAVL 160

                 ....
gi 690757820 173 EMMP 176
Cdd:COG1160  161 ELLP 164
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
15-173 3.00e-20

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: 85.59  E-value: 3.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  15 AVVGRPNAGKSTLTNALVGKKIAITANQPETTR--KAIRAIVSRPAGQLILTDTPGLHKPRtllGQRLNDLVRESLSDLD 92
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRdpDVYVKELDKGKVKLVLVDTPGLDEFG---GLGREELARLLLRGAD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  93 AVVLCLPADEKIGPGD--RFLLNLVRQTKAPIVAAVTKTDK-TGREKLAAKLAELGELADFAQIVPVSAVRGEQIGLLTD 169
Cdd:cd00882   78 LILLVVDSTDRESEEDakLLILRRLRKEGIPIILVGNKIDLlEEREVEELLRLEELAKILGVPVFEVSAKTGEGVDELFE 157

                 ....
gi 690757820 170 LLLE 173
Cdd:cd00882  158 KLIE 161
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
14-173 2.40e-19

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: 83.25  E-value: 2.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQLILTDTPGLHKP-------------RTLlgqrl 80
Cdd:cd01895    5 IAIIGRPNVGKSSLLNALLGEERVIVSDIAGTTRDSIDVPFEYDGQKYTLIDTAGIRKKgkvtegiekysvlRTL----- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  81 ndlvrESLSDLDAVVLCLPADEKIGPGDRFLLNLVRQTKAPIVAAVTKTD---------KTGREKLAAKLAELgelaDFA 151
Cdd:cd01895   80 -----KAIERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDlvekdektmKEFEKELRRKLPFL----DYA 150
                        170       180
                 ....*....|....*....|..
gi 690757820 152 QIVPVSAVRGEQIGLLTDLLLE 173
Cdd:cd01895  151 PIVFISALTGQGVDKLFDAIKE 172
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
14-173 2.07e-18

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 84.69  E-value: 2.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQLILTDTPGLHKP-------------RTLlgqrl 80
Cdd:COG1160  178 IAIVGRPNVGKSSLINALLGEERVIVSDIAGTTRDSIDTPFERDGKKYTLIDTAGIRRKgkvdegiekysvlRTL----- 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  81 ndlvrESLSDLDAVVLCLPADEKIGPGDRFLLNLV-RQTKAPIVA-----AVTKTDKTgREKLAAKLAElgELA--DFAQ 152
Cdd:COG1160  253 -----RAIERADVVLLVIDATEGITEQDLKIAGLAlEAGKALVIVvnkwdLVEKDRKT-REELEKEIRR--RLPflDYAP 324
                        170       180
                 ....*....|....*....|.
gi 690757820 153 IVPVSAVRGEQIGLLTDLLLE 173
Cdd:COG1160  325 IVFISALTGQGVDKLLEAVDE 345
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
10-175 3.32e-18

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: 79.85  E-value: 3.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  10 RAGF-VAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVsrpagQL-----ILTDTPGLHKprTllgqrlNDL 83
Cdd:cd04164    1 REGIkVVIAGKPNVGKSSLLNALAGRDRAIVSDIAGTTRDVIEEEI-----DLggipvRLIDTAGLRE--T------EDE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  84 V--------RESLSDLDAVVLCLPADEKIGPGDrfLLNLVRQTKAPIVAAVTKTDKTGREKLAAKLAELgeladfaQIVP 155
Cdd:cd04164   68 IekigieraREAIEEADLVLLVVDASEGLDEED--LEILELPAKKPVIVVLNKSDLLSDAEGISELNGK-------PIIA 138
                        170       180
                 ....*....|....*....|
gi 690757820 156 VSAVRGEQIGLLTDLLLEMM 175
Cdd:cd04164  139 ISAKTGEGIDELKEALLELA 158
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
14-173 1.20e-17

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 82.79  E-value: 1.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQLILTDTPGLHKP-------------RTLlgqrl 80
Cdd:PRK00093 176 IAIIGRPNVGKSSLINALLGEERVIVSDIAGTTRDSIDTPFERDGQKYTLIDTAGIRRKgkvtegvekysviRTL----- 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  81 ndlvrESLSDLDAVVLCLPADEKIGPGDRFLLNLVRQTKAPIVAAVTKTD-------KTGREKLAAKLAELgelaDFAQI 153
Cdd:PRK00093 251 -----KAIERADVVLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKWDlvdektmEEFKKELRRRLPFL----DYAPI 321
                        170       180
                 ....*....|....*....|
gi 690757820 154 VPVSAVRGEQIGLLTDLLLE 173
Cdd:PRK00093 322 VFISALTGQGVDKLLEAIDE 341
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
9-204 3.42e-17

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: 81.26  E-value: 3.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   9 YRAGF-VAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRpAGQLI-LTDTPGLHKPrtllgqrlNDLV-- 84
Cdd:COG0486  210 LREGIkVVIVGRPNVGKSSLLNALLGEERAIVTDIAGTTRDVIEERINI-GGIPVrLIDTAGLRET--------EDEVek 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  85 ------RESLSDLDAVVLCLPADEKIGPGDRFLLNLVRQTKAPIVAavTKTDktgrekLAAKLAELGELADFAQIVPVSA 158
Cdd:COG0486  281 igieraREAIEEADLVLLLLDASEPLTEEDEEILEKLKDKPVIVVL--NKID------LPSEADGELKSLPGEPVIAISA 352
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 690757820 159 VRGEQIGLLTDLLLEMM----PLSVPLYPT-------------------DTLTDETEGELVAEYIREAA 204
Cdd:COG0486  353 KTGEGIDELKEAILELVgegaLEGEGVLLTnarhrealeralealeralEALESGLPLELLAEDLRLAL 421
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
9-204 1.47e-16

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: 78.68  E-value: 1.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820    9 YRAGF-VAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVS---RPagqLILTDTPGLHKPrtllgqrlNDLV 84
Cdd:pfam12631  91 LREGIkVVIVGKPNVGKSSLLNALLGEERAIVTDIPGTTRDVIEETINiggIP---LRLIDTAGIRET--------DDEV 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   85 --------RESLSDLDAVVLCLPADEKIGPGDRFLLNLVRQTKaPIVAAVTKTDKTGREklaaklaELGELADFAQIVPV 156
Cdd:pfam12631 160 ekigieraREAIEEADLVLLVLDASRPLDEEDLEILELLKDKK-PIIVVLNKSDLLGEI-------DELEELKGKPVLAI 231
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 690757820  157 SAVRGEQIGLLTDLLLEMM----PLSVPLYPT-------------------DTLTDETEGELVAEYIREAA 204
Cdd:pfam12631 232 SAKTGEGLDELEEAIKELFlageIASDGPIITnarhkealeralealeealEALEGGMPLDLVAEDLREAL 302
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
14-175 3.76e-16

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


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 74.47  E-value: 3.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  14 VAVVGRPNAGKSTLTNALVG-KKIAITANQPETTRKAIRAIVsrpAGQLILTDTP--GLHKPRTLLGQRLNDLVRESLSD 90
Cdd:cd01876    2 VAFAGRSNVGKSSLINALTNrKKLARTSKTPGRTQLINFFNV---GDKFRLVDLPgyGYAKVSKEVREKWGKLIEEYLEN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  91 ---LDAVVLCLPADEKIGPGDRFLLNLVRQTKAPIVAAVTKTDKTGREKLAAKLAE----LGELADFAQIVPVSAVRGEQ 163
Cdd:cd01876   79 renLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKikeeLNLFNILPPVILFSSKKGTG 158
                        170
                 ....*....|..
gi 690757820 164 IGLLTDLLLEMM 175
Cdd:cd01876  159 IDELRALIAEWL 170
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
14-203 9.16e-16

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 77.07  E-value: 9.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVS---RPagqLILTDTPGLHKPrtllgqrlNDLV------ 84
Cdd:PRK05291 218 VVIAGRPNVGKSSLLNALLGEERAIVTDIAGTTRDVIEEHINldgIP---LRLIDTAGIRET--------DDEVekigie 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  85 --RESLSDLDAVVLCLPADEKIGPGDRFLLNLVRQTKAPIVAavTKTDKTGREKLaaklaelgELADFAQIVPVSAVRGE 162
Cdd:PRK05291 287 rsREAIEEADLVLLVLDASEPLTEEDDEILEELKDKPVIVVL--NKADLTGEIDL--------EEENGKPVIRISAKTGE 356
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 690757820 163 QIGLLTDLLLEMMPLSVP-----LYPT-------------------DTLTDETEGELVAEYIREA 203
Cdd:PRK05291 357 GIDELREAIKELAFGGFGgnqegVFLTnarhlealeralehleralEGLESGLPLELLAEDLRLA 421
KH_2 pfam07650
KH domain;
211-295 2.18e-15

KH domain;


Pssm-ID: 429574 [Multi-domain]  Cd Length: 78  Bit Score: 69.89  E-value: 2.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  211 ELPHSIAVVVEEiaqrpvKEGEKNRPLTDVHASIYVERESQKGIVIGRGGSRLKDVGRRARIPIEELLESRVYLDLrVKV 290
Cdd:pfam07650   1 EIPYSLAVELKF------AGVSKVEIERTPNAVIVVIRASQPGIVIGKGGSRIKKIGKELRKDIEKLLGKKVYLNI-VKV 73

                  ....*
gi 690757820  291 AKDWQ 295
Cdd:pfam07650  74 KKPWL 78
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
12-172 3.31e-15

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: 71.63  E-value: 3.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   12 GFVAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSR--PAGQLILTDTPGLHKPRTLLGQRLNDLVReSLS 89
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEdgKTYKFNLLDTAGQEDYDAIRRLYYPQVER-SLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   90 DLDAVVLCLPADEKIGPgDRFLLNLVRQTKAPIVAAVTKTDKTGR---EKLAAKLAELGeladFAQIVPVSAVRGEQIGL 166
Cdd:TIGR00231  81 VFDIVILVLDVEEILEK-QTKEIIHHADSGVPIILVGNKIDLKDAdlkTHVASEFAKLN----GEPIIPLSAETGKNIDS 155

                  ....*.
gi 690757820  167 LTDLLL 172
Cdd:TIGR00231 156 AFKIVE 161
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
14-176 1.46e-14

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: 70.40  E-value: 1.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIAITANQPE-----TTRKAIRA----IVSRPAG------QLILTDTPGlHKprtllgq 78
Cdd:cd00881    2 VGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRketflDTLKEERErgitIKTGVVEfewpkrRINFIDTPG-HE------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  79 rlnDLVRE---SLSDLDAVVLCLPADEKIGPGDRFLLNLVRQTKAPIVAAVTKTDKTGREKLAAKLAELGEL-------- 147
Cdd:cd00881   74 ---DFSKEtvrGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGEEDFDEVLREIKELlkligftf 150
                        170       180       190
                 ....*....|....*....|....*....|.
gi 690757820 148 --ADFAQIVPVSAVRGEQIGLLTDLLLEMMP 176
Cdd:cd00881  151 lkGKDVPIIPISALTGEGIEELLDAIVEHLP 181
YeeP COG3596
Predicted GTPase [General function prediction only];
14-176 1.46e-13

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 69.79  E-value: 1.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQ-LILTDTPGLH--KPRTLLGQRLNDLVREslsd 90
Cdd:COG3596   42 IALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLESDGLPgLVLLDTPGLGevNERDREYRELRELLPE---- 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  91 LDAVVLCLPADEkigPGD----RFLLNLVRQ-TKAPIVAAVTKTDKTG--------------------REKLAAKLAELG 145
Cdd:COG3596  118 ADLILWVVKADD---RALatdeEFLQALRAQyPDPPVLVVLTQVDRLEperewdppynwpsppkeqniRRALEAIAEQLG 194
                        170       180       190
                 ....*....|....*....|....*....|....
gi 690757820 146 ELADfaQIVPVSA---VRGEQIGLLTDLLLEMMP 176
Cdd:COG3596  195 VPID--RVIPVSAaedRTGYGLEELVDALAEALP 226
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
15-173 8.01e-13

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: 64.67  E-value: 8.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  15 AVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQLILTDTPGlHKPRTLLGQRLNDLVRESLSDLDAV 94
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPG-VGERGRRDREYEELYRRLLPEADLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  95 VLCLPADEKIGPGDR-FLLNLVRQTKAPIVAAVTKTDktgreklaaklaelgeladfaQIVPVSAVRGEQIGLLTDLLLE 173
Cdd:cd11383   80 LWLLDADDRALAADHdFYLLPLAGHDAPLLFVLNQVD---------------------PVLAVSARTGWGLDELAEALIT 138
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
14-158 1.11e-12

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: 65.26  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIAITANQPETtrkAIRAIVS-RPAGQLILTDTPGLHkprtLLGQRLNDLVRESLSDLD 92
Cdd:cd09912    3 LAVVGEFSAGKSTLLNALLGEEVLPTGVTPTT---AVITVLRyGLLKGVVLVDTPGLN----STIEHHTEITESFLPRAD 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 690757820  93 AVVLCLPADEKIGPGDR-FLLNLVRQTKAPIVAAVTKTDKTGREKLAA-------KLAELGELADFAQIVPVSA 158
Cdd:cd09912   76 AVIFVLSADQPLTESEReFLKEILKWSGKKIFFVLNKIDLLSEEELEEvleysreELGVLELGGGEPRIFPVSA 149
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
12-207 2.47e-12

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 67.13  E-value: 2.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  12 GFVAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQLILTDTPGLHKPRTLLGQRLNDLVRESLSDL 91
Cdd:PRK09518 276 GVVAIVGRPNVGKSTLVNRILGRREAVVEDTPGVTRDRVSYDAEWAGTDFKLVDTGGWEADVEGIDSAIASQAQIAVSLA 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  92 DAVVLCLpaDEKIGP--GDRFLLNLVRQTKAPIVAAVTKTDKTGREKLAAKLAELGeladFAQIVPVSAVRGEQIGLLTD 169
Cdd:PRK09518 356 DAVVFVV--DGQVGLtsTDERIVRMLRRAGKPVVLAVNKIDDQASEYDAAEFWKLG----LGEPYPISAMHGRGVGDLLD 429
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 690757820 170 LLLEMMPLSVPlyptdtltdeTEGELVAEYIREAALEG 207
Cdd:PRK09518 430 EALDSLKVAEK----------TSGFLTPSGLRRVALVG 457
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
14-176 6.84e-12

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 65.76  E-value: 6.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAiraiVSRPAG----QLILTDTPGLHKPRTLLGQRLNDLVRESLS 89
Cdd:PRK03003  41 VAVVGRPNVGKSTLVNRILGRREAVVEDVPGVTRDR----VSYDAEwngrRFTVVDTGGWEPDAKGLQASVAEQAEVAMR 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  90 DLDAVVLCLPADEKIGPGDRFLLNLVRQTKAPIVAAVTKTDKTGREKLAAKLAELGeladFAQIVPVSAVRGEQIGLLTD 169
Cdd:PRK03003 117 TADAVLFVVDATVGATATDEAVARVLRRSGKPVILAANKVDDERGEADAAALWSLG----LGEPHPVSALHGRGVGDLLD 192

                 ....*..
gi 690757820 170 LLLEMMP 176
Cdd:PRK03003 193 AVLAALP 199
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
2-68 7.02e-12

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


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 62.55  E-value: 7.02e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 690757820   2 KNTENPDYRagfVAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSrpaGQLILTDTPG 68
Cdd:cd01856  109 KGLLPRPLR---AMVVGIPNVGKSTLINRLRGKKVAKVGNKPGVTRGQQWIRIG---PNIELLDTPG 169
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
14-68 7.86e-11

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 61.28  E-value: 7.86e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSrpaGQLILTDTPG 68
Cdd:COG1161  116 VMIVGIPNVGKSTLINRLAGKKVAKTGNKPGVTKGQQWIKLD---DGLELLDTPG 167
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
14-175 6.87e-10

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: 57.39  E-value: 6.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  14 VAVVGRPNAGKSTLTNALVG-KKIAITANQPETTRK----AIRaivsrpaGQLILTDTPG----------LHKPRTLLGQ 78
Cdd:COG0218   26 IAFAGRSNVGKSSLINALTNrKKLARTSKTPGKTQLinffLIN-------DKFYLVDLPGygyakvskaeKEKWQKLIED 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  79 RLNDlvRESLSDLdaVVLClpaDEKIGPG--DRFLLNLVRQTKAPIVAAVTKTDKTGREKLAAKLA----ELGELADFAQ 152
Cdd:COG0218   99 YLEG--RENLKGV--VLLI---DIRHPPKelDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKaikkALGKDPAAPE 171
                        170       180
                 ....*....|....*....|...
gi 690757820 153 IVPVSAVRGEQIGLLTDLLLEMM 175
Cdd:COG0218  172 VILFSSLKKEGIDELRAAIEEWL 194
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
14-175 4.96e-09

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 54.60  E-value: 4.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKiaITANQPETTRKA--IRAIVSRPAG--QLILTDTPGL---HKPRTLLGQRLND---- 82
Cdd:COG1100    6 IVVVGTGGVGKTSLVNRLVGDI--FSLEKYLSTNGVtiDKKELKLDGLdvDLVIWDTPGQdefRETRQFYARQLTGasly 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  83 --LVRESLSDLDAVVLclpadekigpgdrFLLNLVRQT--KAPIVAAVTKTDKTGREKL--AAKLAELGELADFAQIVPV 156
Cdd:COG1100   84 lfVVDGTREETLQSLY-------------ELLESLRRLgkKSPIILVLNKIDLYDEEEIedEERLKEALSEDNIVEVVAT 150
                        170
                 ....*....|....*....
gi 690757820 157 SAVRGEQIGLLTDLLLEMM 175
Cdd:COG1100  151 SAKTGEGVEELFAALAEIL 169
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
14-174 6.83e-09

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: 54.02  E-value: 6.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIA------ITANqpettrkaIRA-IVSRP-AGQLIL-TDTPGlHKPRTLL---GQRLN 81
Cdd:cd01887    3 VTVMGHVDHGKTTLLDKIRKTNVAageaggITQH--------IGAyQVPIDvKIPGITfIDTPG-HEAFTNMrarGASVT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  82 DLVreslsdldavVLCLPADEKIGPGDRFLLNLVRQTKAPIVAAVTKTDKTGR-----EKLAAKLAELGELA-DFA---Q 152
Cdd:cd01887   74 DIA----------ILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPYGteadpERVKNELSELGLVGeEWGgdvS 143
                        170       180
                 ....*....|....*....|..
gi 690757820 153 IVPVSAVRGEQIGLLTDLLLEM 174
Cdd:cd01887  144 IVPISAKTGEGIDDLLEAILLL 165
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
15-174 1.63e-08

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: 52.84  E-value: 1.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  15 AVVGRPNAGKSTLTNALVGKKiAITANQPETTRKAIRAIVSRPAGQLILTDTPGLHkprtllgqrlndlvreSLSDLDav 94
Cdd:cd01879    1 ALVGNPNVGKTTLFNALTGAR-QKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPGTY----------------SLTPYS-- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  95 vlclpADEKI-------GPGDRFL-----------LNLVRQ---TKAPIVAAVTKTDKTGREKL---AAKLAE-LGelad 149
Cdd:cd01879   62 -----EDEKVardfllgEEPDLIVnvvdatnlernLYLTLQlleLGLPVVVALNMIDEAEKRGIkidLDKLSElLG---- 132
                        170       180
                 ....*....|....*....|....*
gi 690757820 150 fAQIVPVSAVRGEQIGLLTDLLLEM 174
Cdd:cd01879  133 -VPVVPTSARKGEGIDELLDAIAKL 156
infB CHL00189
translation initiation factor 2; Provisional
2-177 7.17e-08

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 53.68  E-value: 7.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   2 KNTENPDYRAGFVAVVGRPNAGKSTLTNALVGKKIA------ITANQpettrKAIRAIVSRPAG--QLILTDTPGlHKPR 73
Cdd:CHL00189 235 AFTENSINRPPIVTILGHVDHGKTTLLDKIRKTQIAqkeaggITQKI-----GAYEVEFEYKDEnqKIVFLDTPG-HEAF 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  74 TLLGQRlndlvreSLSDLDAVVLCLPADEKIGPGDRFLLNLVRQTKAPIVAAVTKTDKTGR--EKLAAKLAELG----EL 147
Cdd:CHL00189 309 SSMRSR-------GANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANAntERIKQQLAKYNlipeKW 381
                        170       180       190
                 ....*....|....*....|....*....|
gi 690757820 148 ADFAQIVPVSAVRGEQIglltDLLLEMMPL 177
Cdd:CHL00189 382 GGDTPMIPISASQGTNI----DKLLETILL 407
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
15-164 1.25e-07

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: 50.47  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  15 AVVGRPNAGKSTLTNALVGKKIAItANQPETTRKAIRAIVSRPAGQLI-LTDTPGL----HKPRTLLGQRLNDLVRESL- 88
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAKVEI-ASYPFTTLEPNVGVFEFGDGVDIqIIDLPGLldgaSEGRGLGEQILAHLYRSDLi 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 690757820  89 -SDLDAVVLC--LPADEKIGPGDRFLLNLVRQTKAPIVAAVTKTDKTGREKLaaKLAELGELADFAQIVPVSAVRGEQI 164
Cdd:cd01881   80 lHVIDASEDCvgDPLEDQKTLNEEVSGSFLFLKNKPEMIVANKIDMASENNL--KRLKLDKLKRGIPVVPTSALTRLGL 156
mnmE_trmE_thdF TIGR00450
tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF ...
14-130 1.27e-06

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: 49.41  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   14 VAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQLILTDTPGLHKPRTLLGQRLNDLVRESLSDLDA 93
Cdd:TIGR00450 206 LAIVGSPNVGKSSLLNALLKQDRAIVSDIKGTTRDVVEGDFELNGILIKLLDTAGIREHADFVERLGIEKSFKAIKQADL 285
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 690757820   94 VVLCLPADEKIGPGDrFLLNLVRQTKAPIVAAVTKTD 130
Cdd:TIGR00450 286 VIYVLDASQPLTKDD-FLIIDLNKSKKPFILVLNKID 321
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
14-209 3.77e-06

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 48.19  E-value: 3.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKiAITANQPETT--RKaiRAIVSRPAGQLILTDTPG---LHkPRTLlgqrlnD--LVRE 86
Cdd:COG0370    6 IALVGNPNVGKTTLFNALTGSR-QKVGNWPGVTveKK--EGKFKLKGKEIELVDLPGtysLS-AYSP------DekVARD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  87 SL--SDLDAVVL-----CLpadekigpgDR--FLLNLVRQTKAPIVAAVTKTD---KTGREKLAAKLAE-LGeladfAQI 153
Cdd:COG0370   76 FLleEKPDVVVNvvdatNL---------ERnlYLTLQLLELGIPVVLALNMMDeaeKKGIKIDVEKLSKlLG-----VPV 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 690757820 154 VPVSAVRGEQIGLLTDLLLEMMPLSVPLYPTDTLTDETEGEL--VAEYIREAALEGVR 209
Cdd:COG0370  142 VPTSARKGKGIDELKEAIIEAAEGKKPRPLRIDYPEEIEEAIeeLEELLEEDGPYPSR 199
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
14-173 8.26e-06

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: 45.11  E-value: 8.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIAItANQPETTRKAIRAIVSRPAG-QLILTDTPGL----------------HKPRT-- 74
Cdd:cd01898    3 VGLVGLPNAGKSTLLSAISNAKPKI-ADYPFTTLVPNLGVVRVDDGrSFVIADIPGLiegasegkglghrflrHIERTrv 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  75 LL----GQRLNDLVreslSDLDAVVLCLpadEKIGPGdrfLLNlvrqtKAPIVAAvTKTDKTGREKLAAKLAELGELADF 150
Cdd:cd01898   82 LLhvidLSGEDDPV----EDYETIRNEL---EAYNPG---LAE-----KPRIVVL-NKIDLLDAEERFEKLKELLKELKG 145
                        170       180
                 ....*....|....*....|...
gi 690757820 151 AQIVPVSAVRGEQIGLLTDLLLE 173
Cdd:cd01898  146 KKVFPISALTGEGLDELLKKLAK 168
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
7-68 3.86e-05

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


Pssm-ID: 206752 [Multi-domain]  Cd Length: 157  Bit Score: 43.08  E-value: 3.86e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 690757820   7 PDYRAGFVAVVGRPNAGKSTLTNALVGKKIAITANQPETT--RKAIRAIvsRPAGQLILTDTPG 68
Cdd:cd01859   95 IDGKPVIVGVVGYPKVGKSSIINALKGRHSASTSPIPGSPgyTKGIQLV--RIDSKIYLIDTPG 156
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
14-68 6.70e-05

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: 42.44  E-value: 6.70e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 690757820   14 VAVVGRPNAGKSTLTNALVGKKiAITANQPETTRKAIRAIVSRPAGQLILTDTPG 68
Cdd:pfam02421   3 IALVGNPNVGKTTLFNALTGAN-QHVGNWPGVTVEKKEGKFKYKGYEIEIVDLPG 56
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
14-71 8.78e-05

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 44.01  E-value: 8.78e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQLILTDTPGLHK 71
Cdd:PRK09518 453 VALVGRPNVGKSSLLNQLTHEERAVVNDLAGTTRDPVDEIVEIDGEDWLFIDTAGIKR 510
PRK04213 PRK04213
GTP-binding protein EngB;
3-68 1.06e-04

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 42.60  E-value: 1.06e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 690757820   3 NTENPDYRAGFVAVVGRPNAGKSTLTNALVGKKIAiTANQPETTRKairaIVSRPAGQLILTDTPG 68
Cdd:PRK04213   1 MFETRPDRKPEIVFVGRSNVGKSTLVRELTGKKVR-VGKRPGVTRK----PNHYDWGDFILTDLPG 61
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
14-69 1.19e-04

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: 41.45  E-value: 1.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIAITANQPETTrKAIRAIVSRPagQLILTDTPGL 69
Cdd:cd01857   85 IGLVGYPNVGKSSLINALVGSKKVSVSSTPGKT-KHFQTIFLEP--GITLCDCPGL 137
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
16-69 1.99e-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: 41.48  E-value: 1.99e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 690757820  16 VVGRPNAGKSTLTNAL----VGKKIAITANQ-------PETTRKAIRAIVSRpagQLILTDTPGL 69
Cdd:cd01855  130 VVGATNVGKSTLINALlksnGGKVQAQALVQrltvspiPGTTLGLIKIPLGE---GKKLYDTPGI 191
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
14-175 2.71e-04

Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome GTP-binding protein that associates with ribosomal subunits and appears to play a role in ribosomal RNA maturation. This GTPase, related to the nucleolar protein Obg, is designated CgtA in bacteria. Mutations in this gene are pleiotropic, but it appears that effects on cellular functions such as chromosome partition may be secondary to the effect on ribosome structure. Recent work done in Vibrio cholerae shows an essential role in the stringent response, in which RelA-dependent ability to synthesize the alarmone ppGpp is required for deletion of this GTPase to be lethal. [Protein synthesis, Other]


Pssm-ID: 274271 [Multi-domain]  Cd Length: 328  Bit Score: 42.02  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   14 VAVVGRPNAGKSTLTNALVGKKIAItANQPETTRKAIRAIVSRPAGQ-LILTDTPGL----------------HKPRTll 76
Cdd:TIGR02729 160 VGLVGLPNAGKSTLISAVSAAKPKI-ADYPFTTLVPNLGVVRVDDGRsFVIADIPGLiegasegaglghrflkHIERT-- 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   77 gqRL--------NDLVRESLSDLDAVVLCLpadEKIGPGdrfLLNLvrqtkaPIVAAVTKTDKTGREKLAAKLAELGELA 148
Cdd:TIGR02729 237 --RVllhlidisPEDGSDPVEDYEIIRNEL---KKYSPE---LAEK------PRIVVLNKIDLLDEEELEELLKELKKEL 302
                         170       180
                  ....*....|....*....|....*..
gi 690757820  149 DfAQIVPVSAVRGEQIGLLTDLLLEMM 175
Cdd:TIGR02729 303 G-KPVFPISALTGEGLDELLDALAELL 328
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
14-82 4.89e-04

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


Pssm-ID: 206652  Cd Length: 248  Bit Score: 40.76  E-value: 4.89e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 690757820  14 VAVVGRPNAGKSTLTNALVG-KKIAITANQPETTRkaIRAIVSRPAG-QLILTDTPGLHkprTLLGQRLND 82
Cdd:cd01853   34 ILVLGKTGVGKSSTINSIFGeRKVSVSAFQSETLR--PREVSRTVDGfKLNIIDTPGLL---ESQDQRVNR 99
PduV-EutP pfam10662
Ethanolamine utilization - propanediol utilization; Members of this family function in ...
14-167 6.17e-04

Ethanolamine utilization - propanediol utilization; Members of this family function in ethanolamine and propanediol degradation pathways. PduV may be involved in the association of the bacterial microcompartments (BMCs) to filaments.


Pssm-ID: 402341 [Multi-domain]  Cd Length: 137  Bit Score: 39.19  E-value: 6.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820   14 VAVVGRPNAGKSTLTNALVGKKIAITANQpettrkairAIVSRPAgqliLTDTPGLHkprtLLGQRLNDLVRESLSDLDA 93
Cdd:pfam10662   4 IMLIGPTGCGKTTLCQALSGEELKYKKTQ---------AIEFYDN----AIDTPGEY----LENRRYYSALIVTSADADV 66
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 690757820   94 VVLCLPADEkigPGDRFLLNLVRQTKAPIVAAVTKTDKTGREKLAAKLAELGELADFAQIVPVSAVRGEQIGLL 167
Cdd:pfam10662  67 IALVQDATE---PESTFPPGFASMFNKPVIGIITKIDLAKDEANIEIAEEWLSLAGAQKIFRISAVEKIGIEEL 137
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
10-68 6.24e-04

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: 40.14  E-value: 6.24e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 690757820  10 RAGF--VAVVGRPNAGKSTLTNALVGKKIAiTANQP----ETTRkaiRAIVSRPAGQLILTDTPG 68
Cdd:cd01878   38 RSGVptVALVGYTNAGKSTLFNALTGADVL-AEDQLfatlDPTT---RRIKLPGGREVLLTDTVG 98
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
14-174 7.77e-04

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: 39.47  E-value: 7.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIAItANQPETTRKAIRAIVSRPAGQLILTDTPG-LHKPrtlLGQRlNDLVRES---LS 89
Cdd:cd01897    3 LVIAGYPNVGKSSLVNKLTRAKPEV-APYPFTTKSLFVGHFDYKYLRWQVIDTPGiLDRP---LEER-NTIEMQAitaLA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  90 DLDAVVL--------C-LPADEKIgpgdrfllNLVRQTK----APIVAAVTKTDKTGREKLAAKLAELgeLADFAQIVPV 156
Cdd:cd01897   78 HLRAAVLffidpsetCgYSIEEQL--------SLFKEIKplfnKPVIVVLNKIDLLTEEDLSEIEKEL--EKEGEEVIKI 147
                        170
                 ....*....|....*...
gi 690757820 157 SAVRGEQIGLLTDLLLEM 174
Cdd:cd01897  148 STLTEEGVDELKNKACEL 165
PRK01889 PRK01889
GTPase RsgA; Reviewed
14-69 1.02e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 40.30  E-value: 1.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIAITANQPE--------TTRkaiRAIVSRPAGQLILtDTPGL 69
Cdd:PRK01889 198 VALLGSSGVGKSTLVNALLGEEVQKTGAVREddskgrhtTTH---RELHPLPSGGLLI-DTPGM 257
GTP_HflX TIGR03156
GTP-binding protein HflX; This protein family is one of a number of homologous small, ...
14-68 1.51e-03

GTP-binding protein HflX; This protein family is one of a number of homologous small, well-conserved GTP-binding proteins with pleiotropic effects. Bacterial members are designated HflX, following the naming convention in Escherichia coli where HflX is encoded immediately downstream of the RNA chaperone Hfq, and immediately upstream of HflKC, a membrane-associated protease pair with an important housekeeping function. Over large numbers of other bacterial genomes, the pairing with hfq is more significant than with hflK and hlfC. The gene from Homo sapiens in this family has been named PGPL (pseudoautosomal GTP-binding protein-like). [Unknown function, General]


Pssm-ID: 274455 [Multi-domain]  Cd Length: 351  Bit Score: 39.76  E-value: 1.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 690757820   14 VAVVGRPNAGKSTLTNALVGKKIaITANQ------PeTTRKairaIVSRPAGQLILTDTPG 68
Cdd:TIGR03156 192 VALVGYTNAGKSTLFNALTGADV-YAADQlfatldP-TTRR----LDLPDGGEVLLTDTVG 246
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
14-69 1.70e-03

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


Pssm-ID: 206746 [Multi-domain]  Cd Length: 146  Bit Score: 38.13  E-value: 1.70e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRpagQLILTDTPGL 69
Cdd:cd01849   94 VGVVGLPNVGKSSFINALLNKFKLKVGSIPGTTKLQQDVKLDK---EIYLYDTPGI 146
Dynamin_N pfam00350
Dynamin family;
14-50 2.01e-03

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 38.37  E-value: 2.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 690757820   14 VAVVGRPNAGKSTLTNALVGKKIAITANQPeTTRKAI 50
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGP-TTRRPT 36
obgE PRK12299
GTPase CgtA; Reviewed
14-174 2.40e-03

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 38.90  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  14 VAVVGRPNAGKSTL----TNAlvgK-KIaitANQPETTRKAIRAIVSRPAGQ-LILTDTPGL----------------HK 71
Cdd:PRK12299 161 VGLVGLPNAGKSTLisavSAA---KpKI---ADYPFTTLHPNLGVVRVDDYKsFVIADIPGLiegasegaglghrflkHI 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  72 PRT--LLgqRLNDLVRES-LSDLDAVVLCLpadEKIGPGdrfLLNlvrqtKaPIVAAVTKTDKTGREKLAAKLAELGELA 148
Cdd:PRK12299 235 ERTrlLL--HLVDIEAVDpVEDYKTIRNEL---EKYSPE---LAD-----K-PRILVLNKIDLLDEEEEREKRAALELAA 300
                        170       180
                 ....*....|....*....|....*.
gi 690757820 149 DFAQIVPVSAVRGEQIGLLTDLLLEM 174
Cdd:PRK12299 301 LGGPVFLISAVTGEGLDELLRALWEL 326
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
14-211 2.75e-03

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 38.91  E-value: 2.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIaITANQ------PeTTRKairaiVSRPAGQ-LILTDTPG------------------ 68
Cdd:COG2262  202 VALVGYTNAGKSTLFNRLTGADV-LAEDKlfatldP-TTRR-----LELPDGRpVLLTDTVGfirklphqlveafrstle 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  69 --------LH-----KPRTLlgQRLNDlVRESLSDLDavvlclpADEKigpgdrfllnlvrqtkaPIVAAVTKTDKTGRE 135
Cdd:COG2262  275 evreadllLHvvdasDPDFE--EQIET-VNEVLEELG-------ADDK-----------------PIILVFNKIDLLDDE 327
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 690757820 136 klaaKLAELGELADFAqiVPVSAVRGEQIGLLTDLLLEMmpLSVPLYPTDTLTDETEGELVAEYIREAALEGVREE 211
Cdd:COG2262  328 ----ELERLRAGYPDA--VFISAKTGEGIDELLEAIEER--LPEDRVEVELLLPYSDGDLVAWLHEHGEVLSEEYD 395
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
14-47 2.94e-03

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


Pssm-ID: 206753 [Multi-domain]  Cd Length: 171  Bit Score: 37.94  E-value: 2.94e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIAITANQPETTR 47
Cdd:cd04178  119 VGVVGYPNVGKSSVINSLKRSRACNVGATPGVTK 152
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
14-71 3.83e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 38.80  E-value: 3.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIAITANQPETTRKAIRAIVSRPAGQLILTDTPGLHK 71
Cdd:PRK03003 214 VALVGKPNVGKSSLLNKLAGEERSVVDDVAGTTVDPVDSLIELGGKTWRFVDTAGLRR 271
PRK09866 PRK09866
clamp-binding protein CrfC;
14-90 9.04e-03

clamp-binding protein CrfC;


Pssm-ID: 182123 [Multi-domain]  Cd Length: 741  Bit Score: 37.51  E-value: 9.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690757820  14 VAVVGRPNAGKSTLTNALVGKKIAITANQPETtrkAIRAIVSRPAGQliltDTPGLHKPRT--------LLGQRLNDLVR 85
Cdd:PRK09866  72 LAIVGTMKAGKSTTINAIVGTEVLPNRNRPMT---ALPTLIRHTPGQ----KEPVLHFSHVapidcliqQLQQRLRDCDI 144

                 ....*
gi 690757820  86 ESLSD 90
Cdd:PRK09866 145 KHLTD 149
 
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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