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Conserved domains on  [gi|672708772|dbj|GAK74146|]
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GTP-binding protein ['Chrysanthemum coronarium' phytoplasma]

Protein Classification

YlqF/YawG family GTPase( domain architecture ID 11497227)

YlqF/YawG family GTPase such as bacterial ribosome biogenesis GTPase YlqF, an essential protein that is required for a late step of 50S ribosomal subunit assembly

CATH:  3.40.50.300
Gene Ontology:  GO:0005525|GO:0003924
PubMed:  11916378

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
 4-284 9.50e-118

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: 339.49  E-value: 9.50e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772    4 FNWFPGHMKKTFDQIKNNLSLVDIVLVILDARIPLSSLNSQIFSLINQrqKPLLILLNKFSLTDPCKINNFIANYHKKQI 83
Cdd:TIGR03596   1 IQWFPGHMAKARREIKENLKLVDVVIEVLDARIPLSSRNPMIDEIRGN--KPRLIVLNKADLADPAVTKQWLKYFEEKGI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772   84 PVLTIDAIKSPKLQEIYQKALTTIKAKNPLFKSRRIatQTPNIKAMIVGTPNVGKSTLINSFAQKKVLKTANLAGTTKRI 163
Cdd:TIGR03596  79 KALAVNAKKGAGVKKIIKAAKKLLKEKNEKLKAKGL--KNRPIRAMIVGIPNVGKSTLINRLAGKKVAKVGNRPGVTKGQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  164 QWIDIAKpNIQFLDTPGVLWHNFSDPRISLALALAGCFKDSILPLEKLGIHALCYLIKHYGTNLQKRFNLDQNDLSNPNL 243
Cdd:TIGR03596 157 QWIKLSD-NLELLDTPGILWPKFEDQEVGLKLAATGAIKDEALDLEDVALFLLEYLLEHYPELLKERYKLDELPEDPVEL 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 672708772  244 VDIIGQKRNIYTKNQKVDQSRVYQMLLQEIRQGNLGKLNFD 284
Cdd:TIGR03596 236 LEAIAKKRGCLLKGGELDLDRAAEILLNDFRKGKLGRISLE 276
 
Name Accession Description Interval E-value
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
 4-284 9.50e-118

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: 339.49  E-value: 9.50e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772    4 FNWFPGHMKKTFDQIKNNLSLVDIVLVILDARIPLSSLNSQIFSLINQrqKPLLILLNKFSLTDPCKINNFIANYHKKQI 83
Cdd:TIGR03596   1 IQWFPGHMAKARREIKENLKLVDVVIEVLDARIPLSSRNPMIDEIRGN--KPRLIVLNKADLADPAVTKQWLKYFEEKGI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772   84 PVLTIDAIKSPKLQEIYQKALTTIKAKNPLFKSRRIatQTPNIKAMIVGTPNVGKSTLINSFAQKKVLKTANLAGTTKRI 163
Cdd:TIGR03596  79 KALAVNAKKGAGVKKIIKAAKKLLKEKNEKLKAKGL--KNRPIRAMIVGIPNVGKSTLINRLAGKKVAKVGNRPGVTKGQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  164 QWIDIAKpNIQFLDTPGVLWHNFSDPRISLALALAGCFKDSILPLEKLGIHALCYLIKHYGTNLQKRFNLDQNDLSNPNL 243
Cdd:TIGR03596 157 QWIKLSD-NLELLDTPGILWPKFEDQEVGLKLAATGAIKDEALDLEDVALFLLEYLLEHYPELLKERYKLDELPEDPVEL 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 672708772  244 VDIIGQKRNIYTKNQKVDQSRVYQMLLQEIRQGNLGKLNFD 284
Cdd:TIGR03596 236 LEAIAKKRGCLLKGGELDLDRAAEILLNDFRKGKLGRISLE 276
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
3-284 3.93e-102

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 299.72  E-value: 3.93e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772   3 TFNWFPGHMKKTFDQIKNNLSLVDIVLVILDARIPLSSLNSQIFSLInqRQKPLLILLNKFSLTDPCKINNFIANYHKKQ 82
Cdd:COG1161    2 QIQWFPGHMAKARRQIKEILKLVDLVIEVVDARIPLSSRNPMLDELV--GNKPRLLVLNKADLADPSVTKQWLKYFEKQG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  83 IPVLTIDAIKSPKLQEIYQKALTTIKAKNPLFKSRRiatqtpnikAMIVGTPNVGKSTLINSFAQKKVLKTANLAGTTKR 162
Cdd:COG1161   80 VDALAISAKKGKGIKELIEAIRELAPEKGIKRRPIR---------VMIVGIPNVGKSTLINRLAGKKVAKTGNKPGVTKG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772 163 IQWIDIAKpNIQFLDTPGVLWHNFSDPRISLALALAGCFKDSILPLEKLGIHALCYLIKHYGTNLQKRFNLDQNDLSNPN 242
Cdd:COG1161  151 QQWIKLDD-GLELLDTPGILWPKFEDPEVGYKLAATGAIKDEVLDLEEVALFLLGYLARRYPELLKERYKLDELPRTKLE 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 672708772 243 LVDIIGQKRNIYTKNQKVDQSRVYQMLLQEIRQGNLGKLNFD 284
Cdd:COG1161  230 LLEAIGRKRGCLLSGGEVDLEKAAEILLTDFRSGKLGRITLE 271
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 6-182 3.35e-69

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: 212.00  E-value: 3.35e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772   6 WFPGHMKKTFDQIKNNLSLVDIVLVILDARIPLSSLNSQIFSLInqRQKPLLILLNKFSLTDPCKINNFIANYHKKQIPV 85
Cdd:cd01856    1 WFPGHMAKALRQIKEKLKLVDVVIEVRDARIPLSSRNPDLDKIL--GNKPRLIVLNKADLADPAKTKKWLKYFKSQGEPV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  86 LTIDAIKSPKLQEIYQKALTTIKAKNplfKSRRIATQTPNIKAMIVGTPNVGKSTLINSFAQKKVLKTANLAGTTKRIQW 165
Cdd:cd01856   79 LFVNAKNGKGVKKLLKKAKKLLKENE---KLKAKGLLPRPLRAMVVGIPNVGKSTLINRLRGKKVAKVGNKPGVTRGQQW 155

                        170
                 ....*....|....*..
gi 672708772 166 IDIaKPNIQFLDTPGVL 182
Cdd:cd01856  156 IRI-GPNIELLDTPGIL 171
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 127-182 1.20e-13

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: 66.10  E-value: 1.20e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 672708772  127 KAMIVGTPNVGKSTLINSFAQKKVlKTANLAGTTKRIQW--IDIAKPNIQFLDTPGVL 182
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKA-IVSDYPGTTRDPNEgrLELKGKQIILVDTPGLI 57
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 26-160 1.17e-08

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 55.44  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  26 DIVLVILDARIPLSSLNSQIFSLINQRQKPLLILLNKfslTDPCKINNFIANYHKKQIP-VLTIDAIKSPKLQEIYQKAL 104
Cdd:PRK00093  82 DVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNK---VDGPDEEADAYEFYSLGLGePYPISAEHGRGIGDLLDAIL 158

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 672708772 105 ttikakNPLFKSRRIATQTPNIKAMIVGTPNVGKSTLINSFAQKKVLKTANLAGTT 160
Cdd:PRK00093 159 ------EELPEEEEEDEEDEPIKIAIIGRPNVGKSSLINALLGEERVIVSDIAGTT 208
 
Name Accession Description Interval E-value
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
 4-284 9.50e-118

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: 339.49  E-value: 9.50e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772    4 FNWFPGHMKKTFDQIKNNLSLVDIVLVILDARIPLSSLNSQIFSLINQrqKPLLILLNKFSLTDPCKINNFIANYHKKQI 83
Cdd:TIGR03596   1 IQWFPGHMAKARREIKENLKLVDVVIEVLDARIPLSSRNPMIDEIRGN--KPRLIVLNKADLADPAVTKQWLKYFEEKGI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772   84 PVLTIDAIKSPKLQEIYQKALTTIKAKNPLFKSRRIatQTPNIKAMIVGTPNVGKSTLINSFAQKKVLKTANLAGTTKRI 163
Cdd:TIGR03596  79 KALAVNAKKGAGVKKIIKAAKKLLKEKNEKLKAKGL--KNRPIRAMIVGIPNVGKSTLINRLAGKKVAKVGNRPGVTKGQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  164 QWIDIAKpNIQFLDTPGVLWHNFSDPRISLALALAGCFKDSILPLEKLGIHALCYLIKHYGTNLQKRFNLDQNDLSNPNL 243
Cdd:TIGR03596 157 QWIKLSD-NLELLDTPGILWPKFEDQEVGLKLAATGAIKDEALDLEDVALFLLEYLLEHYPELLKERYKLDELPEDPVEL 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 672708772  244 VDIIGQKRNIYTKNQKVDQSRVYQMLLQEIRQGNLGKLNFD 284
Cdd:TIGR03596 236 LEAIAKKRGCLLKGGELDLDRAAEILLNDFRKGKLGRISLE 276
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
3-284 3.93e-102

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 299.72  E-value: 3.93e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772   3 TFNWFPGHMKKTFDQIKNNLSLVDIVLVILDARIPLSSLNSQIFSLInqRQKPLLILLNKFSLTDPCKINNFIANYHKKQ 82
Cdd:COG1161    2 QIQWFPGHMAKARRQIKEILKLVDLVIEVVDARIPLSSRNPMLDELV--GNKPRLLVLNKADLADPSVTKQWLKYFEKQG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  83 IPVLTIDAIKSPKLQEIYQKALTTIKAKNPLFKSRRiatqtpnikAMIVGTPNVGKSTLINSFAQKKVLKTANLAGTTKR 162
Cdd:COG1161   80 VDALAISAKKGKGIKELIEAIRELAPEKGIKRRPIR---------VMIVGIPNVGKSTLINRLAGKKVAKTGNKPGVTKG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772 163 IQWIDIAKpNIQFLDTPGVLWHNFSDPRISLALALAGCFKDSILPLEKLGIHALCYLIKHYGTNLQKRFNLDQNDLSNPN 242
Cdd:COG1161  151 QQWIKLDD-GLELLDTPGILWPKFEDPEVGYKLAATGAIKDEVLDLEEVALFLLGYLARRYPELLKERYKLDELPRTKLE 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 672708772 243 LVDIIGQKRNIYTKNQKVDQSRVYQMLLQEIRQGNLGKLNFD 284
Cdd:COG1161  230 LLEAIGRKRGCLLSGGEVDLEKAAEILLTDFRSGKLGRITLE 271
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 6-182 3.35e-69

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: 212.00  E-value: 3.35e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772   6 WFPGHMKKTFDQIKNNLSLVDIVLVILDARIPLSSLNSQIFSLInqRQKPLLILLNKFSLTDPCKINNFIANYHKKQIPV 85
Cdd:cd01856    1 WFPGHMAKALRQIKEKLKLVDVVIEVRDARIPLSSRNPDLDKIL--GNKPRLIVLNKADLADPAKTKKWLKYFKSQGEPV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  86 LTIDAIKSPKLQEIYQKALTTIKAKNplfKSRRIATQTPNIKAMIVGTPNVGKSTLINSFAQKKVLKTANLAGTTKRIQW 165
Cdd:cd01856   79 LFVNAKNGKGVKKLLKKAKKLLKENE---KLKAKGLLPRPLRAMVVGIPNVGKSTLINRLRGKKVAKVGNKPGVTRGQQW 155

                        170
                 ....*....|....*..
gi 672708772 166 IDIaKPNIQFLDTPGVL 182
Cdd:cd01856  156 IRI-GPNIELLDTPGIL 171
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 26-181 1.67e-20

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: 85.51  E-value: 1.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  26 DIVLVILDARIPLSSLNSQIFSLINQRQKPLLILLNKFSLTDPCKINNFIANYHKKQIPvlTIDAIKSPKLQEIYQKALT 105
Cdd:cd01849    1 DVVVEVVDARDPLSSRNPDIEVLINEKNKKLIMVLNKADLVPKEVLRKWVAELSELYGT--KTFFISATNGQGILKLKAE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672708772 106 TIKAKNPLFKSRriatqtpNIKAMIVGTPNVGKSTLINSFAQKKVLKTANLAGTTKRIQWIDIAKpNIQFLDTPGV 181
Cdd:cd01849   79 ITKQKLKLKYKK-------GIRVGVVGLPNVGKSSFINALLNKFKLKVGSIPGTTKLQQDVKLDK-EIYLYDTPGI 146
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 25-181 1.04e-19

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: 83.52  E-value: 1.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  25 VDIVLVILDARIPLSSLNSQIFSLINQRQKPLLILLNKFSLTDPCKINNFIANYHKKQIPVLTIDAikspKLQEIYQKAL 104
Cdd:cd01859   12 ADVVLEVVDARDPELTRSRKLERMALELGKKLIIVLNKADLVPREVLEKWKEVFESEGLPVVYVSA----RERLGTRILR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772 105 TTIKaknplfksrRIATQTPNIKAMIVGTPNVGKSTLINSFAQKKVLKTANL---AGTTKRIQWIDIAKpNIQFLDTPGV 181
Cdd:cd01859   88 RTIK---------ELAIDGKPVIVGVVGYPKVGKSSIINALKGRHSASTSPIpgsPGYTKGIQLVRIDS-KIYLIDTPGV 157
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
 26-181 3.50e-15

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: 71.84  E-value: 3.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  26 DIVLVILDARIPLSSLNSQI--FSLINQRQKPLLILLNKFSLTDPCKINNFIaNYHKKQIPVLTIDA-----------IK 92
Cdd:cd04178    1 DVILEVLDARDPLGCRCPQVerAVLVLGPNKKLVLVLNKIDLVPKENVEKWL-KYLRNEFPTVAFKAstqqqkknlsrKS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  93 SPKLQEIYQKALTTIKAKNPLFK-----SRRIATQTPnIKAMIVGTPNVGKSTLINSFAQKKVLKTANLAGTTKRIQWID 167
Cdd:cd04178   80 KKVKASDDLLSSSACLGADALLKllknyARNKGIKTS-ITVGVVGYPNVGKSSVINSLKRSRACNVGATPGVTKSMQEVH 158

                        170
                 ....*....|....
gi 672708772 168 IAKpNIQFLDTPGV 181
Cdd:cd04178  159 LDK-HVKLLDSPGV 171
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 127-182 1.20e-13

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: 66.10  E-value: 1.20e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 672708772  127 KAMIVGTPNVGKSTLINSFAQKKVlKTANLAGTTKRIQW--IDIAKPNIQFLDTPGVL 182
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKA-IVSDYPGTTRDPNEgrLELKGKQIILVDTPGLI 57
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 130-182 5.62e-12

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: 62.65  E-value: 5.62e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 672708772 130 IVGTPNVGKSTLINSFAQKKVLKTANLAGTTKRIQ---WIDIAKPNIQFLDTPGVL 182
Cdd:cd00880    2 IFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVrkeWELLPLGPVVLIDTPGLD 57
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 26-180 8.31e-12

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: 61.48  E-value: 8.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  26 DIVLVILDARIPLSSLNSQIFSLINQ--RQKPLLILLNKFSLTDPcKINNFIANYHKKQIPVLtidaikspklqeiyqka 103
Cdd:cd01857   13 DVVVQIVDARNPLFFRCPDLEKYVKEvdPSKENVLLLNKADLVTE-EQRKAWARYFKKEGIVV----------------- 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672708772 104 lttikaknpLFKSRRIATQTPnikamIVGTPNVGKSTLINSFAQKKVLKTANLAGTTKRIQWIDIaKPNIQFLDTPG 180
Cdd:cd01857   75 ---------LFFSALNEATIG-----LVGYPNVGKSSLINALVGSKKVSVSSTPGKTKHFQTIFL-EPGITLCDCPG 136
NGP_1 cd01858
A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; ...
 26-181 1.45e-10

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: 58.46  E-value: 1.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  26 DIVLVILDARIPLSSLNSQIFSLI--NQRQKPLLILLNKFSLtdpckINNFIAnyhKKQIPVLTIDaikSPKLqeIYQKA 103
Cdd:cd01858   10 DVIIQVLDARDPMGTRCKHVEKYLrkEKPHKHLIFVLNKCDL-----VPTWVT---KRWVKVLSKE---YPTL--AFHAS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772 104 LTTIKAKNPLFKSRR----IATQTPNIKAMIVGTPNVGKSTLINSFAQKKVLKTANLAGTTKRIQWIDIAKpNIQFLDTP 179
Cdd:cd01858   77 ITNPFGKGALINLLRqfakLHSDKKQISVGFIGYPNVGKSSVINTLRSKKVCKVAPIPGETKVWQYITLMK-RIYLIDCP 155


                 ..
gi 672708772 180 GV 181
Cdd:cd01858  156 GV 157
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 130-180 4.42e-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: 4.42e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 672708772 130 IVGTPNVGKSTLINSFAQKKVLKTANLAGTTKRIQ----WIDIAKPNIQFLDTPG 180
Cdd:cd00882    2 VVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDvyvkELDKGKVKLVLVDTPG 56
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 12-181 1.02e-08

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: 54.19  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  12 KKTFDQIKNNLSLVDIVLVILDarIPLSsLNSQIFSLINQrqKPLLILLNKFSLTDPCKINNFIANYHKKQIpvltidAI 91
Cdd:cd01855   24 LEILSTLLNDNALVVHVVDIFD--FPGS-LIPGLAELIGA--KPVILVGNKIDLLPKDVKPNRLKQWVKKRL------KI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  92 KSPKLQEIYqkaLTTIKaKNPLFKS--RRIATQT-PNIKAMIVGTPNVGKSTLINSFAQKKVLK-----------TANLA 157
Cdd:cd01855   93 GGLKIKDVI---LVSAK-KGWGVEEliEEIKKLAkYRGDVYVVGATNVGKSTLINALLKSNGGKvqaqalvqrltVSPIP 168

                        170       180
                 ....*....|....*....|....
gi 672708772 158 GTTKRIQWIDIaKPNIQFLDTPGV 181
Cdd:cd01855  169 GTTLGLIKIPL-GEGKKLYDTPGI 191
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 26-160 1.17e-08

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 55.44  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  26 DIVLVILDARIPLSSLNSQIFSLINQRQKPLLILLNKfslTDPCKINNFIANYHKKQIP-VLTIDAIKSPKLQEIYQKAL 104
Cdd:PRK00093  82 DVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNK---VDGPDEEADAYEFYSLGLGePYPISAEHGRGIGDLLDAIL 158

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 672708772 105 ttikakNPLFKSRRIATQTPNIKAMIVGTPNVGKSTLINSFAQKKVLKTANLAGTT 160
Cdd:PRK00093 159 ------EELPEEEEEDEEDEPIKIAIIGRPNVGKSSLINALLGEERVIVSDIAGTT 208
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
7-160 1.24e-08

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 55.42  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772   7 FPGHMKKtfdQIKNNLSLVDIVLVILDARIPLSSLNSQIFSLINQRQKPLLILLNK-------------FSL--TDPCki 71
Cdd:COG1160   68 LEAEIRE---QAELAIEEADVILFVVDGRAGLTPLDEEIAKLLRRSGKPVILVVNKvdgpkreadaaefYSLglGEPI-- 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  72 nnFIANYHKKQIPVLtIDAIkspklqeiyQKALTTIKAKNPLFKSRRIAtqtpnikamIVGTPNVGKSTLINSFAQKKVL 151
Cdd:COG1160  143 --PISAEHGRGVGDL-LDAV---------LELLPEEEEEEEEDDPIKIA---------IVGRPNVGKSSLINALLGEERV 201


                 ....*....
gi 672708772 152 KTANLAGTT 160
Cdd:COG1160  202 IVSDIAGTT 210
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 130-181 6.72e-08

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: 51.31  E-value: 6.72e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 672708772 130 IVGTPNVGKSTLINSFAQKKVLKTANLAGTT-KRIQWIDIaKPNIQ--FLDTPGV 181
Cdd:cd04163    8 IIGRPNVGKSTLLNALVGQKISIVSPKPQTTrNRIRGIYT-DDDAQiiFVDTPGI 61
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 130-188 1.10e-07

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: 50.64  E-value: 1.10e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672708772 130 IVGTPNVGKSTLINSFAQKKVlKTANLAGTTKRIQ--WIDIAKPNIQFLDTPGVLWHNFSD 188
Cdd:cd01897    5 IAGYPNVGKSSLVNKLTRAKP-EVAPYPFTTKSLFvgHFDYKYLRWQVIDTPGILDRPLEE 64
YeeP COG3596
Predicted GTPase [General function prediction only];
117-181 1.14e-07

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 52.08  E-value: 1.14e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672708772 117 RRIATQTPNIkaMIVGTPNVGKSTLINSFAQKKVLKTANLAGTTKRIQWIDI---AKPNIQFLDTPGV 181
Cdd:COG3596   33 LLVELPPPVI--ALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLesdGLPGLVLLDTPGL 98
era PRK00089
GTPase Era; Reviewed
 130-181 1.37e-07

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 51.59  E-value: 1.37e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 672708772 130 IVGTPNVGKSTLINSFAQKKVLKTANLAGTT-KRIQWIDIAKPN-IQFLDTPGV 181
Cdd:PRK00089  10 IVGRPNVGKSTLLNALVGQKISIVSPKPQTTrHRIRGIVTEDDAqIIFVDTPGI 63
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
130-181 2.06e-07

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 51.14  E-value: 2.06e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 672708772 130 IVGTPNVGKSTLINSFAQKKVLKTANLAGTT-KRIQWIDIaKPNIQ--FLDTPGV 181
Cdd:COG1159    8 IVGRPNVGKSTLLNALVGQKVSIVSPKPQTTrHRIRGIVT-REDAQivFVDTPGI 61
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 126-180 2.34e-06

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: 46.72  E-value: 2.34e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 672708772 126 IKAMIVGTPNVGKSTLINSFAQKKVLKTANLAGTTKRI--QWIDIAKPNIQFLDTPG 180
Cdd:cd04164    4 IKVVIAGKPNVGKSSLLNALAGRDRAIVSDIAGTTRDVieEEIDLGGIPVRLIDTAG 60
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 124-181 3.25e-06

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: 46.27  E-value: 3.25e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772 124 PNIKAMIVGTPNVGKSTLINSFAQKKVLKTANLAGTTKRIQWIDIAKPNIQFL--DTPGV 181
Cdd:cd01895    1 DPIKIAIIGRPNVGKSSLLNALLGEERVIVSDIAGTTRDSIDVPFEYDGQKYTliDTAGI 60
GTPase_YqeH TIGR03597
ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of ...
 52-185 4.09e-06

ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of GTPases involved in ribosome biogenesis. Like YqlF, it shows a cyclical permutation relative to GTPases EngA (in which the GTPase domain is duplicated), Era, and others. Members of this protein family are found in a relatively small number of bacterial species, including Bacillus subtilis but not Escherichia coli. [Protein synthesis, Other]


Pssm-ID: 213834 [Multi-domain]  Cd Length: 360  Bit Score: 47.61  E-value: 4.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772   52 RQKPLLILLNKFSL----TDPCKINNFIANYHKKQ----IPVLTIDAIKSPKLQEIYQKalttikaknplfksrrIATQT 123
Cdd:TIGR03597  89 GGNPVLLVGNKIDLlpksVNLSKIKEWMKKRAKELglkpVDIILVSAKKGNGIDELLDK----------------IKKAR 152

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672708772  124 PNIKAMIVGTPNVGKSTLINSFAQ-----KKVLKTANLAGTTkrIQWIDIA-KPNIQFLDTPGVLWHN 185
Cdd:TIGR03597 153 NKKDVYVVGVTNVGKSSLINKLLKqnngdKDVITTSPFPGTT--LDLIEIPlDDGHSLYDTPGIINSH 218
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 57-203 4.35e-06

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


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 46.62  E-value: 4.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  57 LILLNKFSLTDPCKINNFIANYHKKQIPVLTIDAIKSPKLQEIYqkalttikaknPLFKSRRIAtqtpnikamIVGTPNV 136
Cdd:cd01854   37 VIVLNKADLVDDEELEELLEIYEKLGYPVLAVSAKTGEGLDELR-----------ELLKGKTSV---------LVGQSGV 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672708772 137 GKSTLINSFAQKKVLKTANL-----AG--TTKRIQWIDIAKpNIQFLDTPGV----LWHNFSDprislalALAGCFKD 203
Cdd:cd01854   97 GKSTLLNALLPELVLATGEIseklgRGrhTTTHRELFPLPG-GGLIIDTPGFrelgLLHIDPE-------ELAEYFPE 166
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 126-180 4.42e-06

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: 45.83  E-value: 4.42e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 672708772  126 IKAMIVGTPNVGKSTLINSFAQKKVLKTANLAGTT----KRIQWIDIAKPNIQFLDTPG 180
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTrnyvTTVIEEDGKTYKFNLLDTAG 60
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 17-181 6.37e-06

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 47.48  E-value: 6.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  17 QIKNNLSLVDIVLVILDARIPLSSLNSQIFSLINQRQKPLLILLNKFsltdpckiNNFIANYHKKQIPVLTID------A 90
Cdd:PRK09518 347 QAQIAVSLADAVVFVVDGQVGLTSTDERIVRMLRRAGKPVVLAVNKI--------DDQASEYDAAEFWKLGLGepypisA 418

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  91 IKSPKLQEIYQKALTTIKAKNPLFK------SRRIAtqtpnikamIVGTPNVGKSTLINSFAQKKVLKTANLAGTTKRI- 163
Cdd:PRK09518 419 MHGRGVGDLLDEALDSLKVAEKTSGfltpsgLRRVA---------LVGRPNVGKSSLLNQLTHEERAVVNDLAGTTRDPv 489

                        170
                 ....*....|....*....
gi 672708772 164 -QWIDIAKPNIQFLDTPGV 181
Cdd:PRK09518 490 dEIVEIDGEDWLFIDTAGI 508
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
 126-180 6.45e-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: 46.61  E-value: 6.45e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 672708772  126 IKAMIVGTPNVGKSTLINSFAQKKVLKTANLAGTTK-RIQWIDIAKPN-IQFLDTPG 180
Cdd:TIGR00436   1 GFVAILGRPNVGKSTLLNQLHGQKISITSPKAQTTRnRISGIHTTGASqIIFIDTPG 57
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 26-121 1.00e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 46.58  E-value: 1.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  26 DIVLVILDARIPLSSLNSQIFSLINQRQKPLLILLNKFSLTDPCKINNFIAN-----YHKKQIPVLTIDAIKSPKLQEIY 100
Cdd:PRK00093 257 DVVLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKWDLVDEKTMEEFKKElrrrlPFLDYAPIVFISALTGQGVDKLL 336

                         90       100
                 ....*....|....*....|.
gi 672708772 101 QKALTTIKAKNplfksRRIAT 121
Cdd:PRK00093 337 EAIDEAYENAN-----RRIST 352
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 130-182 1.16e-05

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: 44.69  E-value: 1.16e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 672708772 130 IVGTPNVGKSTLINSFAQKKVlKTANLAGTTKR-----IQWIDIAKpnIQFLDTPGVL 182
Cdd:cd01881    2 LVGLPNVGKSTLLSALTSAKV-EIASYPFTTLEpnvgvFEFGDGVD--IQIIDLPGLL 56
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
107-182 1.33e-05

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 45.98  E-value: 1.33e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672708772 107 IKAKNPLfksRRIATQTPNIKAMIV-GTPNVGKSTLINSFAQKKVlKTANLAGTTKRIQ--WIDIAKPNIQFLDTPGVL 182
Cdd:COG1084  144 NEARNKL---RKLPDIDPDLPTIVVaGYPNVGKSSLVSKVTSAKP-EIASYPFTTKGIIvgHFERGHGRYQVIDTPGLL 218
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 130-180 1.56e-05

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: 44.42  E-value: 1.56e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 672708772 130 IVGTPNVGKSTLINS-FAQKKVLKTANLAGTTKRIQWIDIAkPNIQFLDTPG 180
Cdd:cd01876    4 FAGRSNVGKSSLINAlTNRKKLARTSKTPGRTQLINFFNVG-DKFRLVDLPG 54
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
83-180 1.95e-05

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 45.49  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  83 IPVLTIDAIKSpKLQEIYQKALTTIKAknplFKSRRIATQTpnIKAMIVGTPNVGKSTLINSFAQKKVLKTANLAGTTkR 162
Cdd:PRK05291 180 IEFLSDEKILE-KLEELIAELEALLAS----ARQGEILREG--LKVVIAGRPNVGKSSLLNALLGEERAIVTDIAGTT-R 251

                         90       100
                 ....*....|....*....|.
gi 672708772 163 --IQW-IDIAKPNIQFLDTPG 180
Cdd:PRK05291 252 dvIEEhINLDGIPLRLIDTAG 272
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
125-180 2.26e-05

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 44.20  E-value: 2.26e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772 125 NIKAMIVGTPNVGKSTLINSFAQKKVLKTANLA--GTT-KRIQW-IDIAKPNIQFLDTPG 180
Cdd:COG1100    3 EKKIVVVGTGGVGKTSLVNRLVGDIFSLEKYLStnGVTiDKKELkLDGLDVDLVIWDTPG 62
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 130-181 2.42e-05

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: 43.58  E-value: 2.42e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 672708772 130 IVGTPNVGKSTLINSFAQKKVLKTANLAGTTK-----RIQWIDiaKPnIQFLDTPGV 181
Cdd:cd01894    2 IVGRPNVGKSTLFNRLTGRRDAIVSDTPGVTRdrkygEAEWGG--RE-FILIDTGGI 55
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 83-180 2.63e-05

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: 45.44  E-value: 2.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  83 IPVLTIDAIKSpKLQEIyQKALTTIKAKnplFKSRRIATQtpNIKAMIVGTPNVGKSTLINSFAQKKVlktA---NLAGT 159
Cdd:COG0486  178 VEFLDREELLE-RLEEL-REELEALLAS---ARQGELLRE--GIKVVIVGRPNVGKSSLLNALLGEER---AivtDIAGT 247

                         90       100
                 ....*....|....*....|....
gi 672708772 160 TkR--I-QWIDIAKPNIQFLDTPG 180
Cdd:COG0486  248 T-RdvIeERINIGGIPVRLIDTAG 270
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
26-124 3.17e-05

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 45.01  E-value: 3.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  26 DIVLVILDARIPLSSLNSQIFSLINQRQKPLLILLNKFSLTDpcKINNFIANYhKKQI----------PVLTIDAIKS-- 93
Cdd:COG1160  259 DVVLLVIDATEGITEQDLKIAGLALEAGKALVIVVNKWDLVE--KDRKTREEL-EKEIrrrlpfldyaPIVFISALTGqg 335

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 672708772  94 -----PKLQEIYQKALTTIK------------AKN--PLFKSRRI----ATQTP 124
Cdd:COG1160  336 vdkllEAVDEVYESANKRIStsklnrvleeavERHppPAVKGRRLkiyyATQVG 389
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 26-106 7.35e-05

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: 42.42  E-value: 7.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  26 DIVLVILDARIPLSSLNSQIFSLINQRQKPLLILLNKFSLTDpcKINNFIANYhKKQI----------PVLTIDAIKSPK 95
Cdd:cd01895   86 DVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVE--KDEKTMKEF-EKELrrklpfldyaPIVFISALTGQG 162

                         90
                 ....*....|.
gi 672708772  96 LQEIYQKALTT 106
Cdd:cd01895  163 VDKLFDAIKEV 173
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
131-182 1.29e-04

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 42.86  E-value: 1.29e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772 131 VGTPNVGKSTLINSFAQKKVlKTANLAGTTKRIQwidiakP--------NIQFLDTPGVL 182
Cdd:COG1163   69 VGFPSVGKSTLLNKLTNAKS-EVGAYEFTTLDVV------PgmleykgaKIQILDVPGLI 121
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 130-180 3.19e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 41.96  E-value: 3.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 672708772 130 IVGTPNVGKSTLINSFAQKKVLKTANLAGTTK-----RIQWIDIakpNIQFLDTPG 180
Cdd:PRK00093   6 IVGRPNVGKSTLFNRLTGKRDAIVADTPGVTRdriygEAEWLGR---EFILIDTGG 58
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 130-181 3.65e-04

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: 40.13  E-value: 3.65e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 672708772 130 IVGTPNVGKSTLINSFAQKKVlKTANLAGTT--KRIQWIDIAKPNIQFLDTPGV 181
Cdd:cd01879    2 LVGNPNVGKTTLFNALTGARQ-KVGNWPGVTveKKEGEFKLGGKEIEIVDLPGT 54
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 130-181 4.21e-04

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: 40.22  E-value: 4.21e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 672708772 130 IVGTPNVGKSTLINSFAQKKVLKTANLAgTTKRIQWIDIA-KPNIQFLDTPGV 181
Cdd:cd09912    5 VVGEFSAGKSTLLNALLGEEVLPTGVTP-TTAVITVLRYGlLKGVVLVDTPGL 56
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 83-160 4.53e-04

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: 41.31  E-value: 4.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772   83 IPVLTIDAIKSpKLQEIYQKALTTIKAknplFKSRRIATQtpNIKAMIVGTPNVGKSTLINSFAQKKVlktA---NLAGT 159
Cdd:pfam12631  59 IEELTEEELLE-RLEELLAELEKLLAT----ADRGRILRE--GIKVVIVGKPNVGKSSLLNALLGEER---AivtDIPGT 128


                  .
gi 672708772  160 T 160
Cdd:pfam12631 129 T 129
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
130-160 5.61e-04

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 41.16  E-value: 5.61e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 672708772 130 IVGTPNVGKSTLINSFAQKKVLKTANLAGTT 160
Cdd:COG1160    7 IVGRPNVGKSTLFNRLTGRRDAIVDDTPGVT 37
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 117-181 9.30e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 40.34  E-value: 9.30e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672708772 117 RRIAtqtpnikamIVGTPNVGKSTLINSFAQKKVLKTANLAGTTKRI--QWIDIAKPNIQFLDTPGV 181
Cdd:PRK03003 212 RRVA---------LVGKPNVGKSSLLNKLAGEERSVVDDVAGTTVDPvdSLIELGGKTWRFVDTAGL 269
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 25-102 1.01e-03

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: 39.15  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772  25 VDIVLVILDARIPLSSLNSQIfSLINQRQKPLLILLNKFSLTDPC---KINNFIANYHKKQIPVLTIDAIKSPKLQEIYQ 101
Cdd:cd00880   77 ADLVLLVVDSDLTPVEEEAKL-GLLRERGKPVLLVLNKIDLVPESeeeELLRERKLELLPDLPVIAVSALPGEGIDELRK 155


                 .
gi 672708772 102 K 102
Cdd:cd00880  156 K 156
PRK04213 PRK04213
GTP-binding protein EngB;
124-180 1.04e-03

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 39.51  E-value: 1.04e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 672708772 124 PNIKAMIV--GTPNVGKSTLINSFAQKKVlKTANLAGTTKRIQWIDIAkpNIQFLDTPG 180
Cdd:PRK04213   6 PDRKPEIVfvGRSNVGKSTLVRELTGKKV-RVGKRPGVTRKPNHYDWG--DFILTDLPG 61
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
115-181 1.10e-03

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 40.49  E-value: 1.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672708772 115 KSRRIAtqtpnikamIVGTPNVGKSTLINSFAQKKVlKTANLAGTT--KRIQWIDIAKPNIQFLDTPGV 181
Cdd:COG0370    2 KMITIA---------LVGNPNVGKTTLFNALTGSRQ-KVGNWPGVTveKKEGKFKLKGKEIELVDLPGT 60
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 126-181 1.20e-03

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: 38.59  E-value: 1.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 672708772  126 IKAMIVGTPNVGKSTLINSFAQKKvLKTANLAGTT--KRIQWIDIAKPNIQFLDTPGV 181
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTGAN-QHVGNWPGVTveKKEGKFKYKGYEIEIVDLPGI 57
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
 130-180 1.55e-03

Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 39.62  E-value: 1.55e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672708772 130 IVGTPNVGKSTLINSFAQKKVLkTANLAGTT------------KRIQWI-DIAKPN------IQFLDTPG 180
Cdd:COG0012    5 IVGLPNVGKSTLFNALTKAGAE-AANYPFCTiepnvgvvpvpdERLDKLaEIVKPKkivpatIEFVDIAG 73
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 11-79 2.88e-03

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: 37.47  E-value: 2.88e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672708772  11 MKKTFDQIKNnlslVDIVLVILDARIPLSSLNSQIFSLINqrQKPLLILLNKFSLTDPCKINNFIANYH 79
Cdd:cd04164   73 IERAREAIEE----ADLVLLVVDASEGLDEEDLEILELPA--KKPVIVVLNKSDLLSDAEGISELNGKP 135
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
25-81 8.46e-03

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 37.28  E-value: 8.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 672708772  25 VDIVLVILDARIPLSSLNSQIFSLINQRQKPLLILLNKFSLTDPCKINNFIANYHKK 81
Cdd:COG1159   83 VDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLVKKEELLPLLAEYSEL 139
 
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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