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Conserved domains on  [gi|1493836038|ref|WP_121510263|]
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MULTISPECIES: ribosome biogenesis GTPase YlqF [Mesotoga]

Protein Classification

RbgA family protein( domain architecture ID 11439330)

RbgA family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
3-269 3.58e-103

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


:

Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 301.64  E-value: 3.58e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038   3 YPGHIQKAKRQIQNYIKSVDGIVELLDARIPLSSRAYEAEKLFQKKQRIVVLNKSDLADPKITSMWRDYFKSEGSDVVEA 82
Cdd:COG1161     6 FPGHMAKARRQIKEILKLVDLVIEVVDARIPLSSRNPMLDELVGNKPRLLVLNKADLADPSVTKQWLKYFEKQGVDALAI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  83 SLRSTDAKQFIIREIVPLLKSR---FYEKRFMVVGMPNVGKSTFINRLKGKKSLAVGNRPGITRGVQWINVSESIAVLDT 159
Cdd:COG1161    86 SAKKGKGIKELIEAIRELAPEKgikRRPIRVMIVGIPNVGKSTLINRLAGKKVAKTGNKPGVTKGQQWIKLDDGLELLDT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038 160 PGILYSDLRSPHITTKLLAVGSLPYEKFDPLDAFERVLALIVERYGKGLLEDY-LGEEFSNQEEFVEKFCRRRNYLAKQG 238
Cdd:COG1161   166 PGILWPKFEDPEVGYKLAATGAIKDEVLDLEEVALFLLGYLARRYPELLKERYkLDELPRTKLELLEAIGRKRGCLLSGG 245

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1493836038 239 ALDTTRGAHTFLREVAAGKAGRLSFEDPESF 269
Cdd:COG1161   246 EVDLEKAAEILLTDFRSGKLGRITLETPEEV 276
 
Name Accession Description Interval E-value
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
3-269 3.58e-103

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 301.64  E-value: 3.58e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038   3 YPGHIQKAKRQIQNYIKSVDGIVELLDARIPLSSRAYEAEKLFQKKQRIVVLNKSDLADPKITSMWRDYFKSEGSDVVEA 82
Cdd:COG1161     6 FPGHMAKARRQIKEILKLVDLVIEVVDARIPLSSRNPMLDELVGNKPRLLVLNKADLADPSVTKQWLKYFEKQGVDALAI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  83 SLRSTDAKQFIIREIVPLLKSR---FYEKRFMVVGMPNVGKSTFINRLKGKKSLAVGNRPGITRGVQWINVSESIAVLDT 159
Cdd:COG1161    86 SAKKGKGIKELIEAIRELAPEKgikRRPIRVMIVGIPNVGKSTLINRLAGKKVAKTGNKPGVTKGQQWIKLDDGLELLDT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038 160 PGILYSDLRSPHITTKLLAVGSLPYEKFDPLDAFERVLALIVERYGKGLLEDY-LGEEFSNQEEFVEKFCRRRNYLAKQG 238
Cdd:COG1161   166 PGILWPKFEDPEVGYKLAATGAIKDEVLDLEEVALFLLGYLARRYPELLKERYkLDELPRTKLELLEAIGRKRGCLLSGG 245

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1493836038 239 ALDTTRGAHTFLREVAAGKAGRLSFEDPESF 269
Cdd:COG1161   246 EVDLEKAAEILLTDFRSGKLGRITLETPEEV 276
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
 3-264 8.09e-93

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: 275.16  E-value: 8.09e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038   3 YPGHIQKAKRQIQNYIKSVDGIVELLDARIPLSSRAYEAEKLFQKKQRIVVLNKSDLADPKITSMWRDYFKSEGSDVVEA 82
Cdd:TIGR03596   4 FPGHMAKARREIKENLKLVDVVIEVLDARIPLSSRNPMIDEIRGNKPRLIVLNKADLADPAVTKQWLKYFEEKGIKALAV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  83 SLRSTDAKQFI---IREIVPLLKSRFYEK-------RFMVVGMPNVGKSTFINRLKGKKSLAVGNRPGITRGVQWINVSE 152
Cdd:TIGR03596  84 NAKKGAGVKKIikaAKKLLKEKNEKLKAKglknrpiRAMIVGIPNVGKSTLINRLAGKKVAKVGNRPGVTKGQQWIKLSD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038 153 SIAVLDTPGILYSDLRSPHITTKLLAVGSLPYEKFDPLDAFERVLALIVERYGKGLLEDY-LGEEFSNQEEFVEKFCRRR 231
Cdd:TIGR03596 164 NLELLDTPGILWPKFEDQEVGLKLAATGAIKDEALDLEDVALFLLEYLLEHYPELLKERYkLDELPEDPVELLEAIAKKR 243

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1493836038 232 NYLAKQGALDTTRGAHTFLREVAAGKAGRLSFE 264
Cdd:TIGR03596 244 GCLLKGGELDLDRAAEILLNDFRKGKLGRISLE 276
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 3-163 6.90e-77

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: 230.88  E-value: 6.90e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038   3 YPGHIQKAKRQIQNYIKSVDGIVELLDARIPLSSRAYEAEKLFQKKQRIVVLNKSDLADPKITSMWRDYFKSEGSDVVEA 82
Cdd:cd01856     2 FPGHMAKALRQIKEKLKLVDVVIEVRDARIPLSSRNPDLDKILGNKPRLIVLNKADLADPAKTKKWLKYFKSQGEPVLFV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  83 SLRSTDAKQFIIREIVPLLKSRFYEK---------RFMVVGMPNVGKSTFINRLKGKKSLAVGNRPGITRGVQWINVSES 153
Cdd:cd01856    82 NAKNGKGVKKLLKKAKKLLKENEKLKakgllprplRAMVVGIPNVGKSTLINRLRGKKVAKVGNKPGVTRGQQWIRIGPN 161

                         170
                  ....*....|
gi 1493836038 154 IAVLDTPGIL 163
Cdd:cd01856   162 IELLDTPGIL 171
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 109-179 4.06e-16

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: 72.27  E-value: 4.06e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1493836038 109 RFMVVGMPNVGKSTFINRLKGKKSLaVGNRPGITRGVQWINVS---ESIAVLDTPGILYSDLRSPHITTKLLAV 179
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAI-VSDYPGTTRDPNEGRLElkgKQIILVDTPGLIEGASEGEGLGRAFLAI 73
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 11-143 4.91e-09

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 56.60  E-value: 4.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  11 KRQIQNYIKSVDGIVELLDARIPLSSRAYE-AEKLFQ-KKQRIVVLNKSDlaDPKITSMWRDYFK-------------SE 75
Cdd:PRK00093   71 REQAELAIEEADVILFVVDGRAGLTPADEEiAKILRKsNKPVILVVNKVD--GPDEEADAYEFYSlglgepypisaehGR 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1493836038  76 G-SDVVEAslrstdakqfiIREIVPLLKSRFYEK---RFMVVGMPNVGKSTFINRLKGKKSLAVGNRPGITR 143
Cdd:PRK00093  149 GiGDLLDA-----------ILEELPEEEEEDEEDepiKIAIIGRPNVGKSSLINALLGEERVIVSDIAGTTR 209
 
Name Accession Description Interval E-value
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
3-269 3.58e-103

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 301.64  E-value: 3.58e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038   3 YPGHIQKAKRQIQNYIKSVDGIVELLDARIPLSSRAYEAEKLFQKKQRIVVLNKSDLADPKITSMWRDYFKSEGSDVVEA 82
Cdd:COG1161     6 FPGHMAKARRQIKEILKLVDLVIEVVDARIPLSSRNPMLDELVGNKPRLLVLNKADLADPSVTKQWLKYFEKQGVDALAI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  83 SLRSTDAKQFIIREIVPLLKSR---FYEKRFMVVGMPNVGKSTFINRLKGKKSLAVGNRPGITRGVQWINVSESIAVLDT 159
Cdd:COG1161    86 SAKKGKGIKELIEAIRELAPEKgikRRPIRVMIVGIPNVGKSTLINRLAGKKVAKTGNKPGVTKGQQWIKLDDGLELLDT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038 160 PGILYSDLRSPHITTKLLAVGSLPYEKFDPLDAFERVLALIVERYGKGLLEDY-LGEEFSNQEEFVEKFCRRRNYLAKQG 238
Cdd:COG1161   166 PGILWPKFEDPEVGYKLAATGAIKDEVLDLEEVALFLLGYLARRYPELLKERYkLDELPRTKLELLEAIGRKRGCLLSGG 245

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1493836038 239 ALDTTRGAHTFLREVAAGKAGRLSFEDPESF 269
Cdd:COG1161   246 EVDLEKAAEILLTDFRSGKLGRITLETPEEV 276
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
 3-264 8.09e-93

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: 275.16  E-value: 8.09e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038   3 YPGHIQKAKRQIQNYIKSVDGIVELLDARIPLSSRAYEAEKLFQKKQRIVVLNKSDLADPKITSMWRDYFKSEGSDVVEA 82
Cdd:TIGR03596   4 FPGHMAKARREIKENLKLVDVVIEVLDARIPLSSRNPMIDEIRGNKPRLIVLNKADLADPAVTKQWLKYFEEKGIKALAV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  83 SLRSTDAKQFI---IREIVPLLKSRFYEK-------RFMVVGMPNVGKSTFINRLKGKKSLAVGNRPGITRGVQWINVSE 152
Cdd:TIGR03596  84 NAKKGAGVKKIikaAKKLLKEKNEKLKAKglknrpiRAMIVGIPNVGKSTLINRLAGKKVAKVGNRPGVTKGQQWIKLSD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038 153 SIAVLDTPGILYSDLRSPHITTKLLAVGSLPYEKFDPLDAFERVLALIVERYGKGLLEDY-LGEEFSNQEEFVEKFCRRR 231
Cdd:TIGR03596 164 NLELLDTPGILWPKFEDQEVGLKLAATGAIKDEALDLEDVALFLLEYLLEHYPELLKERYkLDELPEDPVELLEAIAKKR 243

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1493836038 232 NYLAKQGALDTTRGAHTFLREVAAGKAGRLSFE 264
Cdd:TIGR03596 244 GCLLKGGELDLDRAAEILLNDFRKGKLGRISLE 276
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 3-163 6.90e-77

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: 230.88  E-value: 6.90e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038   3 YPGHIQKAKRQIQNYIKSVDGIVELLDARIPLSSRAYEAEKLFQKKQRIVVLNKSDLADPKITSMWRDYFKSEGSDVVEA 82
Cdd:cd01856     2 FPGHMAKALRQIKEKLKLVDVVIEVRDARIPLSSRNPDLDKILGNKPRLIVLNKADLADPAKTKKWLKYFKSQGEPVLFV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  83 SLRSTDAKQFIIREIVPLLKSRFYEK---------RFMVVGMPNVGKSTFINRLKGKKSLAVGNRPGITRGVQWINVSES 153
Cdd:cd01856    82 NAKNGKGVKKLLKKAKKLLKENEKLKakgllprplRAMVVGIPNVGKSTLINRLRGKKVAKVGNKPGVTRGQQWIRIGPN 161

                         170
                  ....*....|
gi 1493836038 154 IAVLDTPGIL 163
Cdd:cd01856   162 IELLDTPGIL 171
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 22-162 1.92e-34

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: 121.72  E-value: 1.92e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  22 DGIVELLDARIPLSSRAYEAEKLF--QKKQRIVVLNKSDLADPKITSMWRDYFK-SEGSDVVEASLRSTDAKQFIIREIV 98
Cdd:cd01849     1 DVVVEVVDARDPLSSRNPDIEVLIneKNKKLIMVLNKADLVPKEVLRKWVAELSeLYGTKTFFISATNGQGILKLKAEIT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1493836038  99 PLLKSRFYEK--RFMVVGMPNVGKSTFINRLKGKKSLAVGNRPGITRGVQWINVSESIAVLDTPGI 162
Cdd:cd01849    81 KQKLKLKYKKgiRVGVVGLPNVGKSSFINALLNKFKLKVGSIPGTTKLQQDVKLDKEIYLYDTPGI 146
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 11-162 1.01e-32

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: 117.42  E-value: 1.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  11 KRQIQNYIKSVDGIVELLDARIPLSSRAYEAEKLFQK--KQRIVVLNKSDLADPKITSMWRDYFKSEGSDVVEASLRSTD 88
Cdd:cd01859     2 KRLVRRIIKEADVVLEVVDARDPELTRSRKLERMALElgKKLIIVLNKADLVPREVLEKWKEVFESEGLPVVYVSARERL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1493836038  89 AKQFIIREIVPLLKSRFyEKRFMVVGMPNVGKSTFINRLKGKKSL---AVGNRPGITRGVQWINVSESIAVLDTPGI 162
Cdd:cd01859    82 GTRILRRTIKELAIDGK-PVIVGVVGYPKVGKSSIINALKGRHSAstsPIPGSPGYTKGIQLVRIDSKIYLIDTPGV 157
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
 22-162 1.03e-24

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: 96.88  E-value: 1.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  22 DGIVELLDARIPLSSRAYEAEK---LFQKKQRIV-VLNKSDLADPKITSMWRDYFKSE---------------------- 75
Cdd:cd04178     1 DVILEVLDARDPLGCRCPQVERavlVLGPNKKLVlVLNKIDLVPKENVEKWLKYLRNEfptvafkastqqqkknlsrksk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  76 GSDVVEASLRSTDAkqFIIREIVPLLK--SRFYEKRFM----VVGMPNVGKSTFINRLKGKKSLAVGNRPGITRGVQWIN 149
Cdd:cd04178    81 KVKASDDLLSSSAC--LGADALLKLLKnyARNKGIKTSitvgVVGYPNVGKSSVINSLKRSRACNVGATPGVTKSMQEVH 158

                         170
                  ....*....|...
gi 1493836038 150 VSESIAVLDTPGI 162
Cdd:cd04178   159 LDKHVKLLDSPGV 171
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 12-161 1.51e-23

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: 93.07  E-value: 1.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  12 RQIQNYIKSVDGIVELLDARIPLSSRAYEAEKLFQKKQR----IVVLNKSDLADPKITSMWRDYFKSEGSDVVEASlrst 87
Cdd:cd01857     3 RQLWRVIERSDVVVQIVDARNPLFFRCPDLEKYVKEVDPskenVLLLNKADLVTEEQRKAWARYFKKEGIVVLFFS---- 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1493836038  88 dakqFIIREIVPLlksrfyekrfmvVGMPNVGKSTFINRLKGKKSLAVGNRPGITRGVQWINVSESIAVLDTPG 161
Cdd:cd01857    79 ----ALNEATIGL------------VGYPNVGKSSLINALVGSKKVSVSSTPGKTKHFQTIFLEPGITLCDCPG 136
NGP_1 cd01858
A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; ...
 18-162 7.82e-19

A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; Autoantigen NGP-1 (Nucleolar G-protein gene 1) has been shown to localize in the nucleolus and nucleolar organizers in all cell types analyzed, which is indicative of a function in ribosomal assembly. NGP-1 and its homologs show 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 NKXD motif) are relocated to the N terminus.


Pssm-ID: 206751 [Multi-domain]  Cd Length: 157  Bit Score: 81.19  E-value: 7.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  18 IKSVDGIVELLDARIPLSSRAYEAEKLFQK----KQRIVVLNKSDLADPKITSMWRDYFKSEGSDVV-EASLRSTDAKQF 92
Cdd:cd01858     6 IDSSDVIIQVLDARDPMGTRCKHVEKYLRKekphKHLIFVLNKCDLVPTWVTKRWVKVLSKEYPTLAfHASITNPFGKGA 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1493836038  93 II---REIVPLLksrfYEKRFMVVGM---PNVGKSTFINRLKGKKSLAVGNRPGITRGVQWINVSESIAVLDTPGI 162
Cdd:cd01858    86 LInllRQFAKLH----SDKKQISVGFigyPNVGKSSVINTLRSKKVCKVAPIPGETKVWQYITLMKRIYLIDCPGV 157
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 109-179 4.06e-16

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: 72.27  E-value: 4.06e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1493836038 109 RFMVVGMPNVGKSTFINRLKGKKSLaVGNRPGITRGVQWINVS---ESIAVLDTPGILYSDLRSPHITTKLLAV 179
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAI-VSDYPGTTRDPNEGRLElkgKQIILVDTPGLIEGASEGEGLGRAFLAI 73
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 24-162 6.43e-15

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: 71.14  E-value: 6.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  24 IVELLDarIPLSsRAYEAEKLFQKKQRIVVLNKSDLAdPKITSMWR------DYFKSEGSDVVEASLRSTDAKQFI---I 94
Cdd:cd01855    40 VVDIFD--FPGS-LIPGLAELIGAKPVILVGNKIDLL-PKDVKPNRlkqwvkKRLKIGGLKIKDVILVSAKKGWGVeelI 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1493836038  95 REIVPLLKSRfyeKRFMVVGMPNVGKSTFINRL-----KGKKSLAVGNR------PGITRGVQWINVSESIAVLDTPGI 162
Cdd:cd01855   116 EEIKKLAKYR---GDVYVVGATNVGKSTLINALlksngGKVQAQALVQRltvspiPGTTLGLIKIPLGEGKKLYDTPGI 191
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 51-178 1.34e-13

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: 67.81  E-value: 1.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  51 IVVLNKSDLADPKITSMWRDYFKSEGSDVVEASlrstdAKQfiiREIVPLLKSRFYEKRFMVVGMPNVGKSTFINRLKGK 130
Cdd:cd01854    37 VIVLNKADLVDDEELEELLEIYEKLGYPVLAVS-----AKT---GEGLDELRELLKGKTSVLVGQSGVGKSTLLNALLPE 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1493836038 131 KSLAVGnrpGI----------TRGVQWINVSESIAVLDTPGIlySDLRSPHITTKLLA 178
Cdd:cd01854   109 LVLATG---EIseklgrgrhtTTHRELFPLPGGGLIIDTPGF--RELGLLHIDPEELA 161
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 112-166 3.21e-10

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: 57.64  E-value: 3.21e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1493836038 112 VVGMPNVGKSTFINRLKGKKSLAVGNRPGITRGVQ----WINVSESIAVLDTPGILYSD 166
Cdd:cd00880     2 IFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVrkewELLPLGPVVLIDTPGLDEEG 60
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 112-177 4.01e-09

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: 54.38  E-value: 4.01e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1493836038 112 VVGMPNVGKSTFINRLKGKKSLAVGNRPGITRG-----VQWINVSESIAVLDTPGIL-YSDLRSPHITTKLL 177
Cdd:cd00882     2 VVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDpdvyvKELDKGKVKLVLVDTPGLDeFGGLGREELARLLL 73
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 11-143 4.91e-09

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 56.60  E-value: 4.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  11 KRQIQNYIKSVDGIVELLDARIPLSSRAYE-AEKLFQ-KKQRIVVLNKSDlaDPKITSMWRDYFK-------------SE 75
Cdd:PRK00093   71 REQAELAIEEADVILFVVDGRAGLTPADEEiAKILRKsNKPVILVVNKVD--GPDEEADAYEFYSlglgepypisaehGR 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1493836038  76 G-SDVVEAslrstdakqfiIREIVPLLKSRFYEK---RFMVVGMPNVGKSTFINRLKGKKSLAVGNRPGITR 143
Cdd:PRK00093  149 GiGDLLDA-----------ILEELPEEEEEDEEDepiKIAIIGRPNVGKSSLINALLGEERVIVSDIAGTTR 209
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 112-165 9.47e-09

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: 53.23  E-value: 9.47e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1493836038 112 VVGMPNVGKSTFINRLKGKKsLAVGNRPGIT----RGVQWINvSESIAVLDTPGIlYS 165
Cdd:cd01879     2 LVGNPNVGKTTLFNALTGAR-QKVGNWPGVTvekkEGEFKLG-GKEIEIVDLPGT-YS 56
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 51-162 1.01e-08

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: 53.70  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  51 IVVLNKSDLADPKIT-SMWRDYFKSEGSDVVEASLRSTDAkqfiIREIVPLLKSRFYekrfMVVGMPNVGKSTFINRLKG 129
Cdd:pfam03193  57 VIVLNKIDLLDEEEElEELLKIYRAIGYPVLFVSAKTGEG----IEALKELLKGKTT----VLAGQSGVGKSTLLNALLP 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1493836038 130 KKSLAVGnrpGI----------TRGVQWINVSESIAVLDTPGI 162
Cdd:pfam03193 129 ELDLRTG---EIseklgrgrhtTTHVELFPLPGGGLLIDTPGF 168
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
11-162 1.69e-08

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 54.64  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  11 KRQIQNYIKSVDGIVELLDARIPLSSRAYE-AEKLFQ-KKQRIVVLNKSDlaDPKITSMWRDYFK-----------SEGS 77
Cdd:COG1160    73 REQAELAIEEADVILFVVDGRAGLTPLDEEiAKLLRRsGKPVILVVNKVD--GPKREADAAEFYSlglgepipisaEHGR 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  78 DVVEaslrstdakqfIIREIVPLLKSRFYEK------RFMVVGMPNVGKSTFINRLKGKKSLAVGNRPGITRgvqwinvs 151
Cdd:COG1160   151 GVGD-----------LLDAVLELLPEEEEEEeeddpiKIAIVGRPNVGKSSLINALLGEERVIVSDIAGTTR-------- 211

                         170       180
                  ....*....|....*....|..
gi 1493836038 152 ESIAVL-----------DTPGI 162
Cdd:COG1160   212 DSIDTPferdgkkytliDTAGI 233
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 113-161 3.82e-08

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: 51.74  E-value: 3.82e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1493836038 113 VGMPNVGKSTFINRLKGKKSLA-VGNRPGITRGVQWINVSESIAVLDTPG 161
Cdd:cd01876     5 AGRSNVGKSSLINALTNRKKLArTSKTPGRTQLINFFNVGDKFRLVDLPG 54
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 108-165 5.28e-08

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: 51.30  E-value: 5.28e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1493836038 108 KRFMVVGMPNVGKSTFINRLKGKKsLAVGNRPGITrgvqwINVSE--------SIAVLDTPGIlYS 165
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTGAN-QHVGNWPGVT-----VEKKEgkfkykgyEIEIVDLPGI-YS 59
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 113-162 8.16e-08

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: 50.51  E-value: 8.16e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1493836038 113 VGMPNVGKSTFINRLKGKKSLAVGNRPGITRG-----VQWINVseSIAVLDTPGI 162
Cdd:cd01894     3 VGRPNVGKSTLFNRLTGRRDAIVSDTPGVTRDrkygeAEWGGR--EFILIDTGGI 55
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 109-234 1.75e-07

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: 50.12  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038 109 RFMVVGMPNVGKSTFINRLKGKKSLAVGNRPGITRgvqwinvsESIAVL-----------DTPGI-----------LYSD 166
Cdd:cd01895     4 KIAIIGRPNVGKSSLLNALLGEERVIVSDIAGTTR--------DSIDVPfeydgqkytliDTAGIrkkgkvtegieKYSV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038 167 LRS------PHITtkLLAV-GSLPYEKFDpldafERVLALIVERyGKGLL-----EDYLGEEFSNQEEFVEKFCRRRNYL 234
Cdd:cd01895    76 LRTlkaierADVV--LLVLdASEGITEQD-----LRIAGLILEE-GKALIivvnkWDLVEKDEKTMKEFEKELRRKLPFL 147
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 112-162 1.77e-07

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: 49.77  E-value: 1.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1493836038 112 VVGMPNVGKSTFINRLKGKKSLAVGNRPGITR----GVqwinVSES---IAVLDTPGI 162
Cdd:cd04163     8 IIGRPNVGKSTLLNALVGQKISIVSPKPQTTRnrirGI----YTDDdaqIIFVDTPGI 61
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 113-162 2.01e-07

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 51.59  E-value: 2.01e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1493836038 113 VGMPNVGKSTFINRLKGKKSLAVGNRPGITR----G-VQWINVseSIAVLDTPGI 162
Cdd:PRK00093    7 VGRPNVGKSTLFNRLTGKRDAIVADTPGVTRdriyGeAEWLGR--EFILIDTGGI 59
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
107-165 2.27e-07

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 51.66  E-value: 2.27e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1493836038 107 EKRFMVVGMPNVGKSTFINRLKGKKsLAVGNRPGIT----RGVqWINVSESIAVLDTPGIlYS 165
Cdd:COG0370     3 MITIALVGNPNVGKTTLFNALTGSR-QKVGNWPGVTvekkEGK-FKLKGKEIELVDLPGT-YS 62
PRK00098 PRK00098
GTPase RsgA; Reviewed
 51-162 3.24e-07

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 50.59  E-value: 3.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  51 IVVLNKSDLAD--PKITSMWRDYfKSEGSDVVEASLRSTDAkqfiIREIVPLLKsrfyEKRFMVVGMPNVGKSTFINRLK 128
Cdd:PRK00098  115 IIVLNKIDLLDdlEEARELLALY-RAIGYDVLELSAKEGEG----LDELKPLLA----GKVTVLAGQSGVGKSTLLNALA 185

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1493836038 129 GKKSLAVGNrpgI----------TRGVQWINVSESIAVLDTPGI 162
Cdd:PRK00098  186 PDLELKTGE---IsealgrgkhtTTHVELYDLPGGGLLIDTPGF 226
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
112-162 5.09e-07

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 50.41  E-value: 5.09e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1493836038 112 VVGMPNVGKSTFINRLKGKKSLAVGNRPGITR----G-VQWINVseSIAVLDTPGI 162
Cdd:COG1160     7 IVGRPNVGKSTLFNRLTGRRDAIVDDTPGVTRdriyGeAEWGGR--EFTLIDTGGI 60
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 112-163 1.02e-06

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: 47.55  E-value: 1.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1493836038 112 VVGMPNVGKSTFINRLKGKKsLAVGNRPGITRGvqwINV------SESIAVLDTPGIL 163
Cdd:cd01897     5 IAGYPNVGKSSLVNKLTRAK-PEVAPYPFTTKS---LFVghfdykYLRWQVIDTPGIL 58
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
112-162 1.42e-06

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 48.45  E-value: 1.42e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1493836038 112 VVGMPNVGKSTFINRLKGKKSLAVGNRPGITR----GVqwINVSES-IAVLDTPGI 162
Cdd:COG1159     8 IVGRPNVGKSTLLNALVGQKVSIVSPKPQTTRhrirGI--VTREDAqIVFVDTPGI 61
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 112-143 2.62e-06

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 48.25  E-value: 2.62e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1493836038 112 VVGMPNVGKSTFINRLKGKKSLAVGNRPGITR 143
Cdd:PRK09518  280 IVGRPNVGKSTLVNRILGRREAVVEDTPGVTR 311
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
 112-162 2.79e-06

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: 47.38  E-value: 2.79e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1493836038 112 VVGMPNVGKSTFINRLKGKKSLAVGNRPGITR----GVQwINVSESIAVLDTPGI 162
Cdd:TIGR00436   5 ILGRPNVGKSTLLNQLHGQKISITSPKAQTTRnrisGIH-TTGASQIIFIDTPGF 58
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
63-163 2.91e-06

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 47.91  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  63 KITSMWRDY-FKSEGSDVVEAS-LRstdaKQF------IIREIVPLLKS--------------RFYEKRFMVVGMPNVGK 120
Cdd:COG1084    98 KIKEISREYiRKIRRADSDEARkLR----KEAfgriasVVRRIDDDLLFlnearnklrklpdiDPDLPTIVVAGYPNVGK 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1493836038 121 STFINRLKGKKSlAVGNRPGITRGvqwINV------SESIAVLDTPGIL 163
Cdd:COG1084   174 SSLVSKVTSAKP-EIASYPFTTKG---IIVghfergHGRYQVIDTPGLL 218
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
 114-165 4.33e-06

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: 47.81  E-value: 4.33e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1493836038 114 GMPNVGKSTFINRLKGkKSLAVGNRPGIT---RGVQWINVSESIAVLDTPGIlYS 165
Cdd:TIGR00437   1 GNPNVGKSTLFNALTG-ANQTVGNWPGVTvekKEGKLGFQGEDIEIVDLPGI-YS 53
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 112-143 4.54e-06

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 47.66  E-value: 4.54e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1493836038 112 VVGMPNVGKSTFINRLKGKKSLAVGNRPGITR 143
Cdd:PRK03003   43 VVGRPNVGKSTLVNRILGRREAVVEDVPGVTR 74
era PRK00089
GTPase Era; Reviewed
 112-162 9.38e-06

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 46.19  E-value: 9.38e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1493836038 112 VVGMPNVGKSTFINRLKGKKSLAVGNRPGITR----GVqwINVSES-IAVLDTPGI 162
Cdd:PRK00089   10 IVGRPNVGKSTLLNALVGQKISIVSPKPQTTRhrirGI--VTEDDAqIIFVDTPGI 63
PRK04213 PRK04213
GTP-binding protein EngB;
112-161 1.67e-05

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 44.52  E-value: 1.67e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1493836038 112 VVGMPNVGKSTFINRLKGKKsLAVGNRPGITRGVQWINVSESIaVLDTPG 161
Cdd:PRK04213   14 FVGRSNVGKSTLVRELTGKK-VRVGKRPGVTRKPNHYDWGDFI-LTDLPG 61
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 117-161 1.90e-05

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: 44.29  E-value: 1.90e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1493836038 117 NVGKSTFINRLKGKKSLA-VGNRPGITRGvqwIN---VSESIAVLDTPG 161
Cdd:COG0218    33 NVGKSSLINALTNRKKLArTSKTPGKTQL---INfflINDKFYLVDLPG 78
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 107-212 2.99e-05

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: 43.51  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038 107 EKRFMVVGMPNVGKSTFINRLKGKKSLAVGNRPGITR-----GVQWINVSESIAVLDTPG-ILYSDLRSPHITTkllAVG 180
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRnyvttVIEEDGKTYKFNLLDTAGqEDYDAIRRLYYPQ---VER 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1493836038 181 SLpyEKFDpldafervLALIVERYGKGLLEDY 212
Cdd:TIGR00231  78 SL--RVFD--------IVILVLDVEEILEKQT 99
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
112-163 8.09e-05

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 43.25  E-value: 8.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1493836038 112 VVGMPNVGKSTFINRLKGKKSlAVGNRPGIT----------RGVQwinvsesIAVLDTPGIL 163
Cdd:COG1163    68 LVGFPSVGKSTLLNKLTNAKS-EVGAYEFTTldvvpgmleyKGAK-------IQILDVPGLI 121
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 7-66 1.63e-04

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: 40.94  E-value: 1.63e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038   7 IQKAKRQIQNyiksVDGIVELLDARIPLSSRAYEAEKLFQKKQRIVVLNKSDLADPKITS 66
Cdd:cd04164    73 IERAREAIEE----ADLVLLVVDASEGLDEEDLEILELPAKKPVIVVLNKSDLLSDAEGI 128
TIGR00157 TIGR00157
ribosome small subunit-dependent GTPase A; Members of this protein were designated YjeQ and ...
 49-162 3.42e-04

ribosome small subunit-dependent GTPase A; Members of this protein were designated YjeQ and are now designated RsgA (ribosome small subunit-dependent GTPase A). The strongest motif in the alignment of these proteins is GXSGVGKS[ST], a classic P-loop for nucleotide binding. This protein has been shown to cleave GTP and remain bound to GDP. A role as a regulator of translation has been suggested. The Aquifex aeolicus ortholog is split into consecutive open reading frames. Consequently, this model was build in fragment mode (-f option). [Protein synthesis, Translation factors]


Pssm-ID: 272934 [Multi-domain]  Cd Length: 245  Bit Score: 41.25  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  49 QRIVVLNKSD-LADPKITSMWRDYFKSEGSDVVEASLRSTDAkqfiIREIVPLLKSRFYekrfMVVGMPNVGKSTFINRL 127
Cdd:TIGR00157  69 EPIIVLNKIDlLDDEDMEKEQLDIYRNIGYQVLMTSSKNQDG----LKELIEALQNRIS----VFAGQSGVGKSSLINAL 140

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1493836038 128 KGKKSLAVGNRPG-------ITRGVQWINVSESIaVLDTPGI 162
Cdd:TIGR00157 141 DPSVKQQVNDISSklglgkhTTTHVELFHFHGGL-IADTPGF 181
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 113-162 3.87e-04

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: 40.17  E-value: 3.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1493836038 113 VGMPNVGKSTFINRLKGKKSLAVGNRPGITRGVqwinVSESIA-------VLDTPGI 162
Cdd:cd04164     9 AGKPNVGKSSLLNALAGRDRAIVSDIAGTTRDV----IEEEIDlggipvrLIDTAGL 61
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 7-86 4.60e-04

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: 41.20  E-value: 4.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038   7 IQKAKRQIqnyiKSVDGIVELLDARIPLSSRAYEAEKLFQKKQRIVVLNKSDLADPKitsmWRDYFKSEGSDVVEASLRS 86
Cdd:COG0486   283 IERAREAI----EEADLVLLLLDASEPLTEEDEEILEKLKDKPVIVVLNKIDLPSEA----DGELKSLPGEPVIAISAKT 354
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 112-163 5.43e-04

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: 39.68  E-value: 5.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1493836038 112 VVGMPNVGKSTFINRLKGKKSlAVGNRPGITR----GVQWINVSESIAVLDTPGIL 163
Cdd:cd01881     2 LVGLPNVGKSTLLSALTSAKV-EIASYPFTTLepnvGVFEFGDGVDIQIIDLPGLL 56
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 112-163 6.31e-04

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: 40.22  E-value: 6.31e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1493836038 112 VVGMPNVGKSTFINRLKGKKSlAVGNR--------PGIT--RGVQwinvsesIAVLDTPGIL 163
Cdd:cd01896     5 LVGFPSVGKSTLLSKLTNTKS-EVAAYefttltcvPGVMeyKGAK-------IQLLDLPGII 58
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 113-210 8.34e-04

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: 39.33  E-value: 8.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038 113 VGMPNVGKSTFINRLKGKKSlAVGNRPGITR----GVQWINVSESIAVLDTPGIL----------YSDLRspHIT-TKLL 177
Cdd:cd01898     6 VGLPNAGKSTLLSAISNAKP-KIADYPFTTLvpnlGVVRVDDGRSFVIADIPGLIegasegkglgHRFLR--HIErTRVL 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1493836038 178 A-VGSLpYEKFDPLDAFErvlALI--VERYGKGLLE 210
Cdd:cd01898    83 LhVIDL-SGEDDPVEDYE---TIRneLEAYNPGLAE 114
PRK12289 PRK12289
small ribosomal subunit biogenesis GTPase RsgA;
51-161 9.21e-04

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237040 [Multi-domain]  Cd Length: 352  Bit Score: 40.00  E-value: 9.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  51 IVVLNKSDLADPKITSMWRDYFKSEGSDVVEASLRSTDAkqfiireiVPLLKSRFYEKRFMVVGMPNVGKSTFINRLKGK 130
Cdd:PRK12289  124 VLCLNKADLVSPTEQQQWQDRLQQWGYQPLFISVETGIG--------LEALLEQLRNKITVVAGPSGVGKSSLINRLIPD 195

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1493836038 131 KSLAVGNRPG-------ITRGVQWINVSESIAVLDTPG 161
Cdd:PRK12289  196 VELRVGKVSGklgrgrhTTRHVELFELPNGGLLADTPG 233
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 112-139 1.30e-03

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 39.93  E-value: 1.30e-03
                          10        20
                  ....*....|....*....|....*...
gi 1493836038 112 VVGMPNVGKSTFINRLkGKKSLAVGNRP 139
Cdd:PTZ00258   26 IVGLPNVGKSTTFNAL-CKQQVPAENFP 52
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
106-163 1.31e-03

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 38.81  E-value: 1.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1493836038 106 YEKRFMVVGMPNVGKSTFINRLKGKKslaVGNRP-GITRGVQ-------WINVSESIAVLDTPGIL 163
Cdd:COG1100     2 GEKKIVVVGTGGVGKTSLVNRLVGDI---FSLEKyLSTNGVTidkkelkLDGLDVDLVIWDTPGQD 64
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
7-71 3.09e-03

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 38.55  E-value: 3.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1493836038   7 IQKAKRQIqnyiKSVDGIVELLDARIPLSSRAYEAEKLFQKKQRIVVLNKSDLADPKITSMWRDY 71
Cdd:PRK05291  285 IERSREAI----EEADLVLLVLDASEPLTEEDDEILEELKDKPVIVVLNKADLTGEIDLEEENGK 345
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 7-63 3.53e-03

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: 38.23  E-value: 3.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1493836038   7 IQKAKRQIQNyiksVDGIVELLDARIPLSSRAYEAEKLFQKKQRIV-VLNKSDLADPK 63
Cdd:pfam12631 164 IERAREAIEE----ADLVLLVLDASRPLDEEDLEILELLKDKKPIIvVLNKSDLLGEI 217
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 14-77 4.44e-03

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: 37.14  E-value: 4.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1493836038  14 IQNYIKSVDGIVELLDARIPLSsrayEAEKLFQKKQR-------IVVLNKSDLADPKITSMWRDYFKSEGS 77
Cdd:cd09912    67 TESFLPRADAVIFVLSADQPLT----ESEREFLKEILkwsgkkiFFVLNKIDLLSEEELEEVLEYSREELG 133
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 12-143 6.45e-03

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 37.85  E-value: 6.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1493836038  12 RQIQNYIKSVDGIVELLDARI-PLSSRAYEAEKL-FQKKQRIVVLNKSDlaDPKITSMWRDYFK-------------SEG 76
Cdd:PRK09518  346 SQAQIAVSLADAVVFVVDGQVgLTSTDERIVRMLrRAGKPVVLAVNKID--DQASEYDAAEFWKlglgepypisamhGRG 423

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1493836038  77 -SDVVEASLRSTDAKQfiiREIVPLLKSRFyeKRFMVVGMPNVGKSTFINRLKGKKSLAVGNRPGITR 143
Cdd:PRK09518  424 vGDLLDEALDSLKVAE---KTSGFLTPSGL--RRVALVGRPNVGKSSLLNQLTHEERAVVNDLAGTTR 486
obgE PRK12299
GTPase CgtA; Reviewed
 113-127 7.75e-03

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 37.36  E-value: 7.75e-03
                          10
                  ....*....|....*
gi 1493836038 113 VGMPNVGKSTFINRL 127
Cdd:PRK12299  164 VGLPNAGKSTLISAV 178
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 108-143 8.81e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 37.26  E-value: 8.81e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1493836038 108 KRFMVVGMPNVGKSTFINRLKGKKSLAVGNRPGITR 143
Cdd:PRK03003  212 RRVALVGKPNVGKSSLLNKLAGEERSVVDDVAGTTV 247
 
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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