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Conserved domains on  [gi|1250756189|gb|PCY51024|]
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ribosome biogenesis GTPase YqeH [Listeria monocytogenes]

Protein Classification

GTPase_YqeH family protein( domain architecture ID 11497231)

GTPase_YqeH family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GTPase_YqeH TIGR03597
ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of ...
7-366 0e+00

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: 589.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189   7 CIGCGAVIQTEDPDKIGYAPKSSLNNEQVICKRCFRLKHYNEIQDVALTDDDFLRILNQISSKQALIVYVVDIFDFDGSW 86
Cdd:TIGR03597   1 CIGCGAAIQTTDPKKPGYTPKSALEKEEVYCQRCFRLKHYNEIQDVELNDDDFLNLLNSLGDSNALIVYVVDIFDFEGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  87 LPGLPRFAGSNPVLLVGNKEDVLPKSLKRDKLTRWMRTRAKEQGLAATDVVLVSAEKGHGFDTLLEKIDELRNGQDVYVV 166
Cdd:TIGR03597  81 IPELKRFVGGNPVLLVGNKIDLLPKSVNLSKIKEWMKKRAKELGLKPVDIILVSAKKGNGIDELLDKIKKARNKKDVYVV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 167 GCTNVGKSTLINRIIKQASGENNVITTSQFPGTTLDKIEIPLADGNVLVDTPGIINHHQMAHFIDTTTLKAITPKKEVKP 246
Cdd:TIGR03597 161 GVTNVGKSSLINKLLKQNNGDKDVITTSPFPGTTLDLIEIPLDDGHSLYDTPGIINSHQMAHYLDKKDLKYITPKKEIKP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 247 AVFQLNEEQTLFLGALARLDYVSGGRKSLVVYVSNNLPIHRTKLEKAEALYEKQAGLVLQPPTEEDMKTLPKLVPYSFTV 326
Cdd:TIGR03597 241 KTYQLNPNQTLFLGGLARFDYLKGEKTSFTFYVSNELNIHRTKLENADELYNKHLGNLLSPPCLDDKFNLPELVFHTFTI 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1250756189 327 KEKADIVFSGLGWVTIPEGGAKVTAWVPEGVSATIRTSLV 366
Cdd:TIGR03597 321 KEKTDIVFSGLGWITVKRGGAKVKVYAPKGVGVSLRKALI 360
 
Name Accession Description Interval E-value
GTPase_YqeH TIGR03597
ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of ...
7-366 0e+00

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: 589.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189   7 CIGCGAVIQTEDPDKIGYAPKSSLNNEQVICKRCFRLKHYNEIQDVALTDDDFLRILNQISSKQALIVYVVDIFDFDGSW 86
Cdd:TIGR03597   1 CIGCGAAIQTTDPKKPGYTPKSALEKEEVYCQRCFRLKHYNEIQDVELNDDDFLNLLNSLGDSNALIVYVVDIFDFEGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  87 LPGLPRFAGSNPVLLVGNKEDVLPKSLKRDKLTRWMRTRAKEQGLAATDVVLVSAEKGHGFDTLLEKIDELRNGQDVYVV 166
Cdd:TIGR03597  81 IPELKRFVGGNPVLLVGNKIDLLPKSVNLSKIKEWMKKRAKELGLKPVDIILVSAKKGNGIDELLDKIKKARNKKDVYVV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 167 GCTNVGKSTLINRIIKQASGENNVITTSQFPGTTLDKIEIPLADGNVLVDTPGIINHHQMAHFIDTTTLKAITPKKEVKP 246
Cdd:TIGR03597 161 GVTNVGKSSLINKLLKQNNGDKDVITTSPFPGTTLDLIEIPLDDGHSLYDTPGIINSHQMAHYLDKKDLKYITPKKEIKP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 247 AVFQLNEEQTLFLGALARLDYVSGGRKSLVVYVSNNLPIHRTKLEKAEALYEKQAGLVLQPPTEEDMKTLPKLVPYSFTV 326
Cdd:TIGR03597 241 KTYQLNPNQTLFLGGLARFDYLKGEKTSFTFYVSNELNIHRTKLENADELYNKHLGNLLSPPCLDDKFNLPELVFHTFTI 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1250756189 327 KEKADIVFSGLGWVTIPEGGAKVTAWVPEGVSATIRTSLV 366
Cdd:TIGR03597 321 KEKTDIVFSGLGWITVKRGGAKVKVYAPKGVGVSLRKALI 360
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
37-220 4.20e-80

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: 243.33  E-value: 4.20e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  37 CKRCFRLKHYNEIQDVALTDDDFLRILNQISSKQALIVYVVDIFDFDGSWLPGLPRFAGSNPVLLVGNKEDVLPKSLKRD 116
Cdd:cd01855     1 CQRCFKLKHYNKLLDVEIPDEDFLEILSTLLNDNALVVHVVDIFDFPGSLIPGLAELIGAKPVILVGNKIDLLPKDVKPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 117 KLTRWMRTRAKEQGLAATDVVLVSAEKGHGFDTLLEKIDELRN-GQDVYVVGCTNVGKSTLINRIIK------QASGENN 189
Cdd:cd01855    81 RLKQWVKKRLKIGGLKIKDVILVSAKKGWGVEELIEEIKKLAKyRGDVYVVGATNVGKSTLINALLKsnggkvQAQALVQ 160
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1250756189 190 VITTSQFPGTTLDKIEIPLADGNVLVDTPGI 220
Cdd:cd01855   161 RLTVSPIPGTTLGLIKIPLGEGKKLYDTPGI 191
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
60-342 2.25e-72

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 226.53  E-value: 2.25e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  60 LRILNQISSKQALIVYVVDIFDFDGSWLPGLPRFAGSNPVLLVGNKEDVLPKSLKRdkltRWMRtRAKEQGlaaTDVVLV 139
Cdd:COG1161    14 RRQIKEILKLVDLVIEVVDARIPLSSRNPMLDELVGNKPRLLVLNKADLADPSVTK----QWLK-YFEKQG---VDALAI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 140 SAEKGHGFDTLLEKIDEL-------RNGQDVYVVGCTNVGKSTLINRIIKQasgenNVITTSQFPGTTLDKIEIPLADGN 212
Cdd:COG1161    86 SAKKGKGIKELIEAIRELapekgikRRPIRVMIVGIPNVGKSTLINRLAGK-----KVAKTGNKPGVTKGQQWIKLDDGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 213 VLVDTPGIINHhqmaHFIDTTTLKAITPKKEVKPAVFQLNEEQTLFLGALARLdYVSGGRKSLvvyvsnNLP-IHRTKLE 291
Cdd:COG1161   161 ELLDTPGILWP----KFEDPEVGYKLAATGAIKDEVLDLEEVALFLLGYLARR-YPELLKERY------KLDeLPRTKLE 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1250756189 292 KAEALYEKqAGLvLQPPTEEDMKTLPKLVpysftvkeKADIVFSGLGWVTI 342
Cdd:COG1161   230 LLEAIGRK-RGC-LLSGGEVDLEKAAEIL--------LTDFRSGKLGRITL 270
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
55-220 1.71e-16

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 80.09  E-value: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  55 TDDDFL-RILNQisSKQAL-----IVYVVD----IFDFD---GSWLpglpRFAGSnPVLLVGNKEDvlpkslkrdklTRW 121
Cdd:PRK00093   62 DDDGFEkQIREQ--AELAIeeadvILFVVDgragLTPADeeiAKIL----RKSNK-PVILVVNKVD-----------GPD 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 122 MRTRAKE-QGLAATDVVLVSAEKGHGFDTLLEKI------DELRNGQDVY----VVGCTNVGKSTLINRIIkqasGENNV 190
Cdd:PRK00093  124 EEADAYEfYSLGLGEPYPISAEHGRGIGDLLDAIleelpeEEEEDEEDEPikiaIIGRPNVGKSSLINALL----GEERV 199
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1250756189 191 ITTSQfPGTTLDKIEIPLADGN---VLVDTPGI 220
Cdd:PRK00093  200 IVSDI-AGTTRDSIDTPFERDGqkyTLIDTAGI 231
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
162-221 7.80e-15

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: 69.96  E-value: 7.80e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1250756189 162 DVYVVGCTNVGKSTLINRIIKQASgennviTTSQFPGTTLDKIEIPLADGN---VLVDTPGII 221
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKA------IVSDYPGTTRDPNEGRLELKGkqiILVDTPGLI 57
 
Name Accession Description Interval E-value
GTPase_YqeH TIGR03597
ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of ...
7-366 0e+00

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: 589.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189   7 CIGCGAVIQTEDPDKIGYAPKSSLNNEQVICKRCFRLKHYNEIQDVALTDDDFLRILNQISSKQALIVYVVDIFDFDGSW 86
Cdd:TIGR03597   1 CIGCGAAIQTTDPKKPGYTPKSALEKEEVYCQRCFRLKHYNEIQDVELNDDDFLNLLNSLGDSNALIVYVVDIFDFEGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  87 LPGLPRFAGSNPVLLVGNKEDVLPKSLKRDKLTRWMRTRAKEQGLAATDVVLVSAEKGHGFDTLLEKIDELRNGQDVYVV 166
Cdd:TIGR03597  81 IPELKRFVGGNPVLLVGNKIDLLPKSVNLSKIKEWMKKRAKELGLKPVDIILVSAKKGNGIDELLDKIKKARNKKDVYVV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 167 GCTNVGKSTLINRIIKQASGENNVITTSQFPGTTLDKIEIPLADGNVLVDTPGIINHHQMAHFIDTTTLKAITPKKEVKP 246
Cdd:TIGR03597 161 GVTNVGKSSLINKLLKQNNGDKDVITTSPFPGTTLDLIEIPLDDGHSLYDTPGIINSHQMAHYLDKKDLKYITPKKEIKP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 247 AVFQLNEEQTLFLGALARLDYVSGGRKSLVVYVSNNLPIHRTKLEKAEALYEKQAGLVLQPPTEEDMKTLPKLVPYSFTV 326
Cdd:TIGR03597 241 KTYQLNPNQTLFLGGLARFDYLKGEKTSFTFYVSNELNIHRTKLENADELYNKHLGNLLSPPCLDDKFNLPELVFHTFTI 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1250756189 327 KEKADIVFSGLGWVTIPEGGAKVTAWVPEGVSATIRTSLV 366
Cdd:TIGR03597 321 KEKTDIVFSGLGWITVKRGGAKVKVYAPKGVGVSLRKALI 360
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
37-220 4.20e-80

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: 243.33  E-value: 4.20e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  37 CKRCFRLKHYNEIQDVALTDDDFLRILNQISSKQALIVYVVDIFDFDGSWLPGLPRFAGSNPVLLVGNKEDVLPKSLKRD 116
Cdd:cd01855     1 CQRCFKLKHYNKLLDVEIPDEDFLEILSTLLNDNALVVHVVDIFDFPGSLIPGLAELIGAKPVILVGNKIDLLPKDVKPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 117 KLTRWMRTRAKEQGLAATDVVLVSAEKGHGFDTLLEKIDELRN-GQDVYVVGCTNVGKSTLINRIIK------QASGENN 189
Cdd:cd01855    81 RLKQWVKKRLKIGGLKIKDVILVSAKKGWGVEELIEEIKKLAKyRGDVYVVGATNVGKSTLINALLKsnggkvQAQALVQ 160
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1250756189 190 VITTSQFPGTTLDKIEIPLADGNVLVDTPGI 220
Cdd:cd01855   161 RLTVSPIPGTTLGLIKIPLGEGKKLYDTPGI 191
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
60-342 2.25e-72

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 226.53  E-value: 2.25e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  60 LRILNQISSKQALIVYVVDIFDFDGSWLPGLPRFAGSNPVLLVGNKEDVLPKSLKRdkltRWMRtRAKEQGlaaTDVVLV 139
Cdd:COG1161    14 RRQIKEILKLVDLVIEVVDARIPLSSRNPMLDELVGNKPRLLVLNKADLADPSVTK----QWLK-YFEKQG---VDALAI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 140 SAEKGHGFDTLLEKIDEL-------RNGQDVYVVGCTNVGKSTLINRIIKQasgenNVITTSQFPGTTLDKIEIPLADGN 212
Cdd:COG1161    86 SAKKGKGIKELIEAIRELapekgikRRPIRVMIVGIPNVGKSTLINRLAGK-----KVAKTGNKPGVTKGQQWIKLDDGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 213 VLVDTPGIINHhqmaHFIDTTTLKAITPKKEVKPAVFQLNEEQTLFLGALARLdYVSGGRKSLvvyvsnNLP-IHRTKLE 291
Cdd:COG1161   161 ELLDTPGILWP----KFEDPEVGYKLAATGAIKDEVLDLEEVALFLLGYLARR-YPELLKERY------KLDeLPRTKLE 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1250756189 292 KAEALYEKqAGLvLQPPTEEDMKTLPKLVpysftvkeKADIVFSGLGWVTI 342
Cdd:COG1161   230 LLEAIGRK-RGC-LLSGGEVDLEKAAEIL--------LTDFRSGKLGRITL 270
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
72-220 1.77e-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: 86.67  E-value: 1.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  72 LIVYVVDIFDFDGSWLPGLPRFA--GSNPVLLVGNKEDVLPKSLKRdkltRWmrtRAKEQGLAATDVVLVSAEKGHG--- 146
Cdd:cd01849     2 VVVEVVDARDPLSSRNPDIEVLIneKNKKLIMVLNKADLVPKEVLR----KW---VAELSELYGTKTFFISATNGQGilk 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1250756189 147 ---FDTLLEKIDELRNGQDVYVVGCTNVGKSTLINRIIKQasgenNVITTSQFPGTTLDKIEIPLADGNVLVDTPGI 220
Cdd:cd01849    75 lkaEITKQKLKLKYKKGIRVGVVGLPNVGKSSFINALLNK-----FKLKVGSIPGTTKLQQDVKLDKEIYLYDTPGI 146
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
55-220 1.71e-16

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 80.09  E-value: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  55 TDDDFL-RILNQisSKQAL-----IVYVVD----IFDFD---GSWLpglpRFAGSnPVLLVGNKEDvlpkslkrdklTRW 121
Cdd:PRK00093   62 DDDGFEkQIREQ--AELAIeeadvILFVVDgragLTPADeeiAKIL----RKSNK-PVILVVNKVD-----------GPD 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 122 MRTRAKE-QGLAATDVVLVSAEKGHGFDTLLEKI------DELRNGQDVY----VVGCTNVGKSTLINRIIkqasGENNV 190
Cdd:PRK00093  124 EEADAYEfYSLGLGEPYPISAEHGRGIGDLLDAIleelpeEEEEDEEDEPikiaIIGRPNVGKSSLINALL----GEERV 199
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1250756189 191 ITTSQfPGTTLDKIEIPLADGN---VLVDTPGI 220
Cdd:PRK00093  200 IVSDI-AGTTRDSIDTPFERDGqkyTLIDTAGI 231
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
98-220 6.17e-16

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 78.53  E-value: 6.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  98 PVLLVGNKEDvlpkSLKRDkltrwmrTRAKE-QGLAATDVVLVSAEKGHGFDTLLEKI--------------DELRngqd 162
Cdd:COG1160   113 PVILVVNKVD----GPKRE-------ADAAEfYSLGLGEPIPISAEHGRGVGDLLDAVlellpeeeeeeeedDPIK---- 177
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1250756189 163 VYVVGCTNVGKSTLINRIIkqasGENNVITTSQfPGTTLDKIEIPL-ADGN--VLVDTPGI 220
Cdd:COG1160   178 IAIVGRPNVGKSSLINALL----GEERVIVSDI-AGTTRDSIDTPFeRDGKkyTLIDTAGI 233
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
162-221 7.80e-15

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: 69.96  E-value: 7.80e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1250756189 162 DVYVVGCTNVGKSTLINRIIKQASgennviTTSQFPGTTLDKIEIPLADGN---VLVDTPGII 221
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKA------IVSDYPGTTRDPNEGRLELKGkqiILVDTPGLI 57
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
60-220 1.59e-13

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: 67.73  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  60 LRILNQISSKQALIVYVVDIFDFDGSWLPGLPRFAGSN--PVLLVGNKEDVLPkslkRDKLTRWMRtRAKEQGLaatDVV 137
Cdd:cd01859     2 KRLVRRIIKEADVVLEVVDARDPELTRSRKLERMALELgkKLIIVLNKADLVP----REVLEKWKE-VFESEGL---PVV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 138 LVSAEKGHGFDTLLEKIDEL-RNGQD--VYVVGCTNVGKSTLINRIIKQASGENNVITTSqfPGTTLDKIEIPLADGNVL 214
Cdd:cd01859    74 YVSARERLGTRILRRTIKELaIDGKPviVGVVGYPKVGKSSIINALKGRHSASTSPIPGS--PGYTKGIQLVRIDSKIYL 151

                  ....*.
gi 1250756189 215 VDTPGI 220
Cdd:cd01859   152 IDTPGV 157
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
88-220 9.38e-12

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


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 62.93  E-value: 9.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  88 PGLPRFAGSNPVLLVGNKEDVLPKslkrDKLTRWMRtRAKEQGlaaTDVVLVSAEKGHGFDTLLEKIDELRNGQD----- 162
Cdd:cd01856    38 PDLDKILGNKPRLIVLNKADLADP----AKTKKWLK-YFKSQG---EPVLFVNAKNGKGVKKLLKKAKKLLKENEklkak 109
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1250756189 163 --------VYVVGCTNVGKSTLINRIIKQasgenNVITTSQFPGTTLDKIEIPLADGNVLVDTPGI 220
Cdd:cd01856   110 gllprplrAMVVGIPNVGKSTLINRLRGK-----KVAKVGNKPGVTRGQQWIRIGPNIELLDTPGI 170
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
163-220 5.97e-11

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: 60.52  E-value: 5.97e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1250756189 163 VYVVGCTNVGKSTLINRIIkqasGENNVITTSQfPGTTLDKIEIPLADGN---VLVDTPGI 220
Cdd:cd01895     5 IAIIGRPNVGKSSLLNALL----GEERVIVSDI-AGTTRDSIDVPFEYDGqkyTLIDTAGI 60
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
88-221 2.59e-10

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


Pssm-ID: 274669 [Multi-domain]  Cd Length: 276  Bit Score: 60.60  E-value: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  88 PGLPRFAGSNPVLLVGNKEDVLPKSlKRDKLTRWMRtrakEQGlaaTDVVLVSAEKGHGFDTLLEKIDEL---RNGQD-- 162
Cdd:TIGR03596  40 PMIDEIRGNKPRLIVLNKADLADPA-VTKQWLKYFE----EKG---IKALAVNAKKGAGVKKIIKAAKKLlkeKNEKLka 111
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1250756189 163 ---------VYVVGCTNVGKSTLINRIIKqasgeNNVITTSQFPGTTLDKIEIPLADGNVLVDTPGII 221
Cdd:TIGR03596 112 kglknrpirAMIVGIPNVGKSTLINRLAG-----KKVAKVGNRPGVTKGQQWIKLSDNLELLDTPGIL 174
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
70-220 7.85e-10

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: 57.55  E-value: 7.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  70 QALIVYVVDIFDFDgSWLpgLPRF------AGSNPVLLVgNKEDVLPKslkRDKLTRWMrTRAKEQGLaatDVVLVSAEK 143
Cdd:pfam03193  25 QAVIVFSLKEPDFN-LNL--LDRFlvlaeaSGIEPVIVL-NKIDLLDE---EEELEELL-KIYRAIGY---PVLFVSAKT 93
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1250756189 144 GHGFDTLLEKIDelrnGQDVYVVGCTNVGKSTLINRIIKQASGENNVITTSQFPG--TTLDKIEIPLADGNVLVDTPGI 220
Cdd:pfam03193  94 GEGIEALKELLK----GKTTVLAGQSGVGKSTLLNALLPELDLRTGEISEKLGRGrhTTTHVELFPLPGGGLLIDTPGF 168
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
165-220 2.94e-09

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: 55.33  E-value: 2.94e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 165 VVGCTNVGKSTLINRIIKQASGEnnvitTSQFPGTTLD----KIEIPLADGNVLVDTPGI 220
Cdd:cd00880     2 IFGRPNVGKSSLLNALLGQNVGI-----VSPIPGTTRDpvrkEWELLPLGPVVLIDTPGL 56
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
94-220 3.40e-09

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: 56.25  E-value: 3.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  94 AGSNPVLLVgNKEDVLPKSLKRDKLTRWmrtraKEQGLaatDVVLVSAEKGHGFDTLLEkidELRNGQDVyVVGCTNVGK 173
Cdd:cd01854    32 SGIEPVIVL-NKADLVDDEELEELLEIY-----EKLGY---PVLAVSAKTGEGLDELRE---LLKGKTSV-LVGQSGVGK 98
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1250756189 174 STLINRIIKQASGENNVI---------TTSQfpgTTLdkieIPLADGNVLVDTPGI 220
Cdd:cd01854    99 STLLNALLPELVLATGEIseklgrgrhTTTH---REL----FPLPGGGLIIDTPGF 147
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
158-220 7.90e-09

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: 54.04  E-value: 7.90e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1250756189 158 RNGQDVYVVGCTNVGKSTLINRIikqaSGENNVITTSQfPGTTLDKIEIPLADGNV---LVDTPGI 220
Cdd:cd04164     1 REGIKVVIAGKPNVGKSSLLNAL----AGRDRAIVSDI-AGTTRDVIEEEIDLGGIpvrLIDTAGL 61
RsgA COG1162
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
94-220 8.89e-09

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


Pssm-ID: 440776 [Multi-domain]  Cd Length: 300  Bit Score: 55.89  E-value: 8.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  94 AGSNPVLLVgNKEDVLPKSLKRDKLTRwmrtrAKEQGLaatDVVLVSAEKGHGFDTLLEKIDelrnGQDVYVVGCTNVGK 173
Cdd:COG1162   113 AGIEPVIVL-NKADLADDEELEELLAI-----YEALGY---PVLAVSAKTGEGLDELRELLK----GKTSVLVGQSGVGK 179
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1250756189 174 STLINRII---KQASGE-NNVI-----TTSQfpgTTLdkieIPLADGNVLVDTPGI 220
Cdd:COG1162   180 STLINALLpdaDLATGEiSEKLgrgrhTTTH---AEL----YPLPGGGWLIDTPGF 228
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
163-257 5.91e-08

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: 53.16  E-value: 5.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 163 VYVVGCTNVGKSTLINRIIKQasgenNVITTSQFPGTTLDKIEIPLADGN---VLVDTPGI-INHHQMAHFIDTTTLKAI 238
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHGQ-----KISITSPKAQTTRNRISGIHTTGAsqiIFIDTPGFhEKKHSLNRLMMKEARSAI 77
                          90
                  ....*....|....*....
gi 1250756189 239 tpkKEVKPAVFQLNEEQTL 257
Cdd:TIGR00436  78 ---GGVDLILFVVDSDQWN 93
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
165-238 1.03e-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: 50.92  E-value: 1.03e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1250756189 165 VVGCTNVGKSTLINRIIkqasGENNVITTSQfPGTTLDKIEIPLADGN---VLVDTPGII-NHHQMAHFIDTTTLKAI 238
Cdd:cd04163     8 IIGRPNVGKSTLLNALV----GQKISIVSPK-PQTTRNRIRGIYTDDDaqiIFVDTPGIHkPKKKLGERMVKAAWSAL 80
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
163-221 1.25e-07

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 51.14  E-value: 1.25e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1250756189 163 VYVVGCTNVGKSTLINRIIKQASGENNVITTSqfpGTTLDKIEIPLADGN---VLVDTPGII 221
Cdd:COG1100     6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLSTN---GVTIDKKELKLDGLDvdlVIWDTPGQD 64
PRK00098 PRK00098
GTPase RsgA; Reviewed
98-220 1.53e-07

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 52.13  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  98 PVLLVGNKEDVLpkslkrDKLTRWMRTRAKEQGLAaTDVVLVSAEKGHGFDTLLEKIDelrnGQDVYVVGCTNVGKSTLI 177
Cdd:PRK00098  113 KPIIVLNKIDLL------DDLEEARELLALYRAIG-YDVLELSAKEGEGLDELKPLLA----GKVTVLAGQSGVGKSTLL 181
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1250756189 178 NRIIKQASGENNVITTSQFPG--TT----LdkieIPLADGNVLVDTPGI 220
Cdd:PRK00098  182 NALAPDLELKTGEISEALGRGkhTTthveL----YDLPGGGLLIDTPGF 226
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
165-220 3.08e-07

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: 49.76  E-value: 3.08e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1250756189 165 VVGCTNVGKSTLINRIIKQasgenNVITTSQFPGTTL--DKIEIPLADGN---VLVDTPGI 220
Cdd:cd00882     2 VVGRGGVGKSSLLNALLGG-----EVGEVSDVPGTTRdpDVYVKELDKGKvklVLVDTPGL 57
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
157-220 3.61e-07

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: 51.60  E-value: 3.61e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1250756189 157 LRNGQDVYVVGCTNVGKSTLINRIikqaSGENNVITTSQfPGTTLDKIE-------IPLadgnVLVDTPGI 220
Cdd:COG0486   210 LREGIKVVIVGRPNVGKSSLLNAL----LGEERAIVTDI-AGTTRDVIEeriniggIPV----RLIDTAGL 271
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
165-224 5.46e-07

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 50.37  E-value: 5.46e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1250756189 165 VVGCTNVGKSTLINRIIkqasGENNVITTSQfPGTTLDKIEIPLADGN---VLVDTPGIINHH 224
Cdd:COG1159     8 IVGRPNVGKSTLLNALV----GQKVSIVSPK-PQTTRHRIRGIVTREDaqiVFVDTPGIHKPK 65
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
157-220 7.43e-07

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 50.88  E-value: 7.43e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1250756189 157 LRNGQDVYVVGCTNVGKSTLINRIikqaSGENNVITTSQfPGTTLDKIE-------IPLadgnVLVDTPGI 220
Cdd:PRK05291  212 LREGLKVVIAGRPNVGKSSLLNAL----LGEERAIVTDI-AGTTRDVIEehinldgIPL----RLIDTAGI 273
era PRK00089
GTPase Era; Reviewed
163-220 8.11e-07

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 50.05  E-value: 8.11e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1250756189 163 VYVVGCTNVGKSTLINRIIkqasGENNVITTSQfPGTTLDKIEIPLADGN---VLVDTPGI 220
Cdd:PRK00089    8 VAIVGRPNVGKSTLLNALV----GQKISIVSPK-PQTTRHRIRGIVTEDDaqiIFVDTPGI 63
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
148-220 1.43e-06

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: 49.40  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 148 DTLLEKIDE---LRNGQDVYVVGCTNVGKSTLINRIikqaSGENNVITTSQfPGTTLDKIE-------IPLadgnVLVDT 217
Cdd:pfam12631  79 EKLLATADRgriLREGIKVVIVGKPNVGKSSLLNAL----LGEERAIVTDI-PGTTRDVIEetiniggIPL----RLIDT 149

                  ...
gi 1250756189 218 PGI 220
Cdd:pfam12631 150 AGI 152
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
166-220 2.44e-06

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: 47.04  E-value: 2.44e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1250756189 166 VGCTNVGKSTLINRIIkqasGENNVItTSQFPGTTLDKIEiplADGNV------LVDTPGI 220
Cdd:cd01894     3 VGRPNVGKSTLFNRLT----GRRDAI-VSDTPGVTRDRKY---GEAEWggrefiLIDTGGI 55
TIGR00157 TIGR00157
ribosome small subunit-dependent GTPase A; Members of this protein were designated YjeQ and ...
135-220 5.82e-06

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: 47.02  E-value: 5.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 135 DVVLVSAEKGhgfDTLLEKIDELRNGQDVYVvGCTNVGKSTLINRIIKQASGE-NNVITTSQFPGTTLDKIEIPLADGNV 213
Cdd:TIGR00157  99 QVLMTSSKNQ---DGLKELIEALQNRISVFA-GQSGVGKSSLINALDPSVKQQvNDISSKLGLGKHTTTHVELFHFHGGL 174

                  ....*..
gi 1250756189 214 LVDTPGI 220
Cdd:TIGR00157 175 IADTPGF 181
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
165-312 6.07e-06

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


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 46.00  E-value: 6.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 165 VVGCTNVGKSTLINRII-KQASGENNVITTSqfpgtTLDKIEIPLADGNVLVDTPGI---INHHQMahfidtTTLKAItp 240
Cdd:cd09912     5 VVGEFSAGKSTLLNALLgEEVLPTGVTPTTA-----VITVLRYGLLKGVVLVDTPGLnstIEHHTE------ITESFL-- 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1250756189 241 kKEVKPAVFQLNEEQTLFLGALARLDYVSGGRKSLVVYVSNNLPIHRTKLEKAEALYEKQAGLVLQPPTEED 312
Cdd:cd09912    72 -PRADAVIFVLSADQPLTESEREFLKEILKWSGKKIFFVLNKIDLLSEEELEEVLEYSREELGVLELGGGEP 142
PRK01889 PRK01889
GTPase RsgA; Reviewed
94-220 8.62e-06

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 47.24  E-value: 8.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  94 AGSNPVLlVGNKEDVLPKSlkrDKLTRwmRTRAKEQGLaatDVVLVSAEKGHGFDTLLEKideLRNGQDVYVVGCTNVGK 173
Cdd:PRK01889  141 SGAEPVI-VLTKADLCEDA---EEKIA--EVEALAPGV---PVLAVSALDGEGLDVLAAW---LSGGKTVALLGSSGVGK 208
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1250756189 174 STLINRIIKQASGENNVITTSQFPG--TTLDKIEIPLADGNVLVDTPGI 220
Cdd:PRK01889  209 STLVNALLGEEVQKTGAVREDDSKGrhTTTHRELHPLPSGGLLIDTPGM 257
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
166-219 2.25e-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: 2.25e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1250756189 166 VGCTNVGKSTLINRIIKQasgeNNVITTSQFPGTTLDKIEIPLADGNVLVDTPG 219
Cdd:cd01876     5 AGRSNVGKSSLINALTNR----KKLARTSKTPGRTQLINFFNVGDKFRLVDLPG 54
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
95-221 2.63e-05

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


Pssm-ID: 206750 [Multi-domain]  Cd Length: 140  Bit Score: 43.37  E-value: 2.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  95 GSNPVLLVGNKEDVLPKSLkRDKLTRWMRTRAKeqglaatDVVLVSAekghgfdtllekidelRNGQDVYVVGCTNVGKS 174
Cdd:cd01857    41 PSKENVLLLNKADLVTEEQ-RKAWARYFKKEGI-------VVLFFSA----------------LNEATIGLVGYPNVGKS 96
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1250756189 175 TLINRIIkqasgENNVITTSQFPGTTLDKIEIPLADGNVLVDTPGII 221
Cdd:cd01857    97 SLINALV-----GSKKVSVSSTPGKTKHFQTIFLEPGITLCDCPGLV 138
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
166-220 3.93e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 45.43  E-value: 3.93e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1250756189 166 VGCTNVGKSTLINRIIkqasGENNVItTSQFPGTTLDKIEiplADGNV------LVDTPGI 220
Cdd:PRK00093    7 VGRPNVGKSTLFNRLT----GKRDAI-VADTPGVTRDRIY---GEAEWlgrefiLIDTGGI 59
PRK12289 PRK12289
small ribosomal subunit biogenesis GTPase RsgA;
98-219 4.57e-05

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237040 [Multi-domain]  Cd Length: 352  Bit Score: 45.01  E-value: 4.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  98 PVLLVGNKEDVL-PKSLK--RDKLTRWmrtrakeqglaATDVVLVSAEKGHGFDTLLEKideLRNGQDVyVVGCTNVGKS 174
Cdd:PRK12289  122 EIVLCLNKADLVsPTEQQqwQDRLQQW-----------GYQPLFISVETGIGLEALLEQ---LRNKITV-VAGPSGVGKS 186
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1250756189 175 TLINRIIKQASgennvITTSQFPGT------TLDKIEI-PLADGNVLVDTPG 219
Cdd:PRK12289  187 SLINRLIPDVE-----LRVGKVSGKlgrgrhTTRHVELfELPNGGLLADTPG 233
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
72-157 4.60e-05

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: 43.22  E-value: 4.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  72 LIVYVVDIFDFDGS---WLpgLPRFAGSN-PVLLVGNKEDVLPKSLKRDKLTRWMrtrakEQGLAATDVVLVSAEKGHGF 147
Cdd:cd04163    85 LVLFVVDASEWIGEgdeFI--LELLKKSKtPVILVLNKIDLVKDKEDLLPLLEKL-----KELHPFAEIFPISALKGENV 157
                          90
                  ....*....|
gi 1250756189 148 DTLLEKIDEL 157
Cdd:cd04163   158 DELLEYIVEY 167
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
163-220 4.60e-05

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


Pssm-ID: 460552 [Multi-domain]  Cd Length: 156  Bit Score: 43.21  E-value: 4.60e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1250756189 163 VYVVGCTNVGKSTLINRIikqaSGENNVIttSQFPGTTLDKIEIPLADGN---VLVDTPGI 220
Cdd:pfam02421   3 IALVGNPNVGKTTLFNAL----TGANQHV--GNWPGVTVEKKEGKFKYKGyeiEIVDLPGI 57
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
163-219 6.54e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 44.58  E-value: 6.54e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1250756189 163 VYVVGCTNVGKSTLINRII--KQASGENnvittsqFPGTTLDKIEIPlADGN----VLVDTPG 219
Cdd:PRK03003   41 VAVVGRPNVGKSTLVNRILgrREAVVED-------VPGVTRDRVSYD-AEWNgrrfTVVDTGG 95
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
165-220 8.72e-05

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 44.24  E-value: 8.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1250756189 165 VVGCTNVGKSTLINRIIkqasGENNVITTSQfPGTTLDKI--EIPLADGN-VLVDTPGI 220
Cdd:COG1160     7 IVGRPNVGKSTLFNRLT----GRRDAIVDDT-PGVTRDRIygEAEWGGREfTLIDTGGI 60
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
165-220 1.58e-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: 41.67  E-value: 1.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1250756189 165 VVGCTNVGKSTLINRIikqaSGENNviTTSQFPGTTLDKIE--IPLADGNV-LVDTPGI 220
Cdd:cd01879     2 LVGNPNVGKTTLFNAL----TGARQ--KVGNWPGVTVEKKEgeFKLGGKEIeIVDLPGT 54
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
98-220 2.97e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 42.65  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  98 PVLLVGNKEDvlPKSLKRDKLTRWmrtrakeqGLAATDVVLVSAEKGHGFDTLLEKI-----------DELRNGQDVYVV 166
Cdd:PRK03003  148 PVILAANKVD--DERGEADAAALW--------SLGLGEPHPVSALHGRGVGDLLDAVlaalpevprvgSASGGPRRVALV 217
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1250756189 167 GCTNVGKSTLINRIikqaSGENNVItTSQFPGTTLDKI-EIPLADGNV--LVDTPGI 220
Cdd:PRK03003  218 GKPNVGKSSLLNKL----AGEERSV-VDDVAGTTVDPVdSLIELGGKTwrFVDTAGL 269
PRK11058 PRK11058
GTPase HflX; Provisional
163-223 5.94e-04

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 41.63  E-value: 5.94e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1250756189 163 VYVVGCTNVGKSTLINRIIkqasgENNVITTSQFPGT---TLDKIEIPLADGNVLVDTPGIINH 223
Cdd:PRK11058  200 VSLVGYTNAGKSTLFNRIT-----EARVYAADQLFATldpTLRRIDVADVGETVLADTVGFIRH 258
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
73-220 1.01e-03

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


Pssm-ID: 206753 [Multi-domain]  Cd Length: 171  Bit Score: 39.48  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  73 IVYVVDIFDFDGSWLPGLPRF----AGSNPVLLVGNKEDVLPKslkrDKLTRWM--------------------RTRAKE 128
Cdd:cd04178     3 ILEVLDARDPLGCRCPQVERAvlvlGPNKKLVLVLNKIDLVPK----ENVEKWLkylrnefptvafkastqqqkKNLSRK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189 129 QGLAATDVVLVSAEKGHGFDTLLEKIDELRNGQD------VYVVGCTNVGKSTLINRiIKQAsgenNVITTSQFPGTTLD 202
Cdd:cd04178    79 SKKVKASDDLLSSSACLGADALLKLLKNYARNKGiktsitVGVVGYPNVGKSSVINS-LKRS----RACNVGATPGVTKS 153
                         170
                  ....*....|....*....
gi 1250756189 203 KIEIPLaDGNV-LVDTPGI 220
Cdd:cd04178   154 MQEVHL-DKHVkLLDSPGV 171
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
166-219 1.02e-03

ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other]


Pssm-ID: 274670 [Multi-domain]  Cd Length: 179  Bit Score: 39.76  E-value: 1.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1250756189 166 VGCTNVGKSTLINRIIKQasgeNNVITTSQFPGTTldkIEI---PLADGNVLVDTPG 219
Cdd:TIGR03598  24 AGRSNVGKSSLINALTNR----KKLARTSKTPGRT---QLInffEVNDGFRLVDLPG 73
PRK04213 PRK04213
GTP-binding protein EngB;
163-219 1.12e-03

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 39.90  E-value: 1.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1250756189 163 VYVVGCTNVGKSTLINRIikqaSGENnvITTSQFPGTTLDKIEIPLADgNVLVDTPG 219
Cdd:PRK04213   12 IVFVGRSNVGKSTLVREL----TGKK--VRVGKRPGVTRKPNHYDWGD-FILTDLPG 61
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
155-219 1.30e-03

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 40.93  E-value: 1.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1250756189 155 DELRNGQD----VYVVGCTNVGKSTLINRII--KQASGENnvittsqFPGTTLDKIEIPlADGN----VLVDTPG 219
Cdd:PRK09518  266 GDEKAGPKavgvVAIVGRPNVGKSTLVNRILgrREAVVED-------TPGVTRDRVSYD-AEWAgtdfKLVDTGG 332
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
72-157 2.06e-03

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: 38.56  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  72 LIVYVVDIFDFD-------------GSWLPGLPRfagsNPVLLVGNKEDVLPKSLKRDKLtrwmrtRAKEQGLAATDVVL 138
Cdd:cd01898    81 VLLHVIDLSGEDdpvedyetirnelEAYNPGLAE----KPRIVVLNKIDLLDAEERFEKL------KELLKELKGKKVFP 150
                          90
                  ....*....|....*....
gi 1250756189 139 VSAEKGHGFDTLLEKIDEL 157
Cdd:cd01898   151 ISALTGEGLDELLKKLAKL 169
era PRK00089
GTPase Era; Reviewed
72-154 2.17e-03

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 39.26  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250756189  72 LIVYVVDIFDfdgSWLPG----LPRFAGSN-PVLLVGNKEDVLPKSLKRDKLTRWMRtrakeQGLAATDVVLVSAEKGHG 146
Cdd:PRK00089   87 LVLFVVDADE---KIGPGdefiLEKLKKVKtPVILVLNKIDLVKDKEELLPLLEELS-----ELMDFAEIVPISALKGDN 158

                  ....*...
gi 1250756189 147 FDTLLEKI 154
Cdd:PRK00089  159 VDELLDVI 166
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
165-221 3.05e-03

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: 38.12  E-value: 3.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1250756189 165 VVGCTNVGKSTLINRIIKqasgeNNVITTSQFPGTTLD----KIEIplaDGNV----LVDTPGII 221
Cdd:TIGR00231   6 IVGHPNVGKSTLLNSLLG-----NKGSITEYYPGTTRNyvttVIEE---DGKTykfnLLDTAGQE 62
 
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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