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Conserved domains on  [gi|752704354|ref|WP_041351696|]
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MULTISPECIES: ribosome biogenesis GTPase YqeH [Bacillus]

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 ...
 6-366 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: 613.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354    6 CIGCGVTIQTEDKTGLGYAPPASLTKENVICQRCFRLKNYNEIQDVSLTDDDFLNILHGIGETDSLVVKIVDIFDFNGSW 85
Cdd:TIGR03597   1 CIGCGAAIQTTDPKKPGYTPKSALEKEEVYCQRCFRLKHYNEIQDVELNDDDFLNLLNSLGDSNALIVYVVDIFDFEGSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354   86 INGLQRLVGGNPILLVGNKADILPKSLKRERLIQWMKREAKELGLKPVDVFLVSAGRGQGIREVIDAIEHYRNGKDVYVV 165
Cdd:TIGR03597  81 IPELKRFVGGNPVLLVGNKIDLLPKSVNLSKIKEWMKKRAKELGLKPVDIILVSAKKGNGIDELLDKIKKARNKKDVYVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  166 GCTNVGKSTFINRIIKEVSGEEDIITTSQFPGTTLDAIEIPLDDGSSLYDTPGIINNHQMAHYVNKKDLKILSPKKELKP 245
Cdd:TIGR03597 161 GVTNVGKSSLINKLLKQNNGDKDVITTSPFPGTTLDLIEIPLDDGHSLYDTPGIINSHQMAHYLDKKDLKYITPKKEIKP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  246 RTFQLNDQQTLYFGGLARFDYVSGERSPFICYMPNELMIHRTKLENADALYEKHAGELLTPPGKDEMDQFPELVAHTFTI 325
Cdd:TIGR03597 241 KTYQLNPNQTLFLGGLARFDYLKGEKTSFTFYVSNELNIHRTKLENADELYNKHLGNLLSPPCLDDKFNLPELVFHTFTI 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 752704354  326 KdKKTDIVFSGLGWVTVHDADKKVTAYAPKGVHVFVRRSLI 366
Cdd:TIGR03597 321 K-EKTDIVFSGLGWITVKRGGAKVKVYAPKGVGVSLRKALI 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 ...
 6-366 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: 613.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354    6 CIGCGVTIQTEDKTGLGYAPPASLTKENVICQRCFRLKNYNEIQDVSLTDDDFLNILHGIGETDSLVVKIVDIFDFNGSW 85
Cdd:TIGR03597   1 CIGCGAAIQTTDPKKPGYTPKSALEKEEVYCQRCFRLKHYNEIQDVELNDDDFLNLLNSLGDSNALIVYVVDIFDFEGSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354   86 INGLQRLVGGNPILLVGNKADILPKSLKRERLIQWMKREAKELGLKPVDVFLVSAGRGQGIREVIDAIEHYRNGKDVYVV 165
Cdd:TIGR03597  81 IPELKRFVGGNPVLLVGNKIDLLPKSVNLSKIKEWMKKRAKELGLKPVDIILVSAKKGNGIDELLDKIKKARNKKDVYVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  166 GCTNVGKSTFINRIIKEVSGEEDIITTSQFPGTTLDAIEIPLDDGSSLYDTPGIINNHQMAHYVNKKDLKILSPKKELKP 245
Cdd:TIGR03597 161 GVTNVGKSSLINKLLKQNNGDKDVITTSPFPGTTLDLIEIPLDDGHSLYDTPGIINSHQMAHYLDKKDLKYITPKKEIKP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  246 RTFQLNDQQTLYFGGLARFDYVSGERSPFICYMPNELMIHRTKLENADALYEKHAGELLTPPGKDEMDQFPELVAHTFTI 325
Cdd:TIGR03597 241 KTYQLNPNQTLFLGGLARFDYLKGEKTSFTFYVSNELNIHRTKLENADELYNKHLGNLLSPPCLDDKFNLPELVFHTFTI 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 752704354  326 KdKKTDIVFSGLGWVTVHDADKKVTAYAPKGVHVFVRRSLI 366
Cdd:TIGR03597 321 K-EKTDIVFSGLGWITVKRGGAKVKVYAPKGVGVSLRKALI 360
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 36-219 6.34e-81

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: 245.25  E-value: 6.34e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  36 CQRCFRLKNYNEIQDVSLTDDDFLNILHGIGETDSLVVKIVDIFDFNGSWINGLQRLVGGNPILLVGNKADILPKSLKRE 115
Cdd:cd01855    1 CQRCFKLKHYNKLLDVEIPDEDFLEILSTLLNDNALVVHVVDIFDFPGSLIPGLAELIGAKPVILVGNKIDLLPKDVKPN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354 116 RLIQWMKREAKELGLKPVDVFLVSAGRGQGIREVIDAIEHYRN-GKDVYVVGCTNVGKSTFINRIIKEVSG------EED 188
Cdd:cd01855   81 RLKQWVKKRLKIGGLKIKDVILVSAKKGWGVEELIEEIKKLAKyRGDVYVVGATNVGKSTLINALLKSNGGkvqaqaLVQ 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 752704354 189 IITTSQFPGTTLDAIEIPLDDGSSLYDTPGI 219
Cdd:cd01855  161 RLTVSPIPGTTLGLIKIPLGEGKKLYDTPGI 191
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
59-342 2.50e-79

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 244.25  E-value: 2.50e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  59 LNILHGIGETDSLVVKIVDIFDFNGSWINGLQRLVGGNPILLVGNKADILPKSLKRerliQWMKREAKElGlkpVDVFLV 138
Cdd:COG1161   14 RRQIKEILKLVDLVIEVVDARIPLSSRNPMLDELVGNKPRLLVLNKADLADPSVTK----QWLKYFEKQ-G---VDALAI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354 139 SAGRGQGIREVIDAIEHY-------RNGKDVYVVGCTNVGKSTFINRIIKevsgeEDIITTSQFPGTTLDAIEIPLDDGS 211
Cdd:COG1161   86 SAKKGKGIKELIEAIRELapekgikRRPIRVMIVGIPNVGKSTLINRLAG-----KKVAKTGNKPGVTKGQQWIKLDDGL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354 212 SLYDTPGIINnhqmAHYVNKKDLKILSPKKELKPRTFQLNDQQTLYFGGLARFdYVSGERSPFicympNELMIHRTKLEN 291
Cdd:COG1161  161 ELLDTPGILW----PKFEDPEVGYKLAATGAIKDEVLDLEEVALFLLGYLARR-YPELLKERY-----KLDELPRTKLEL 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 752704354 292 ADALYEKhAGELLtPPGKDEMDQFPELVahtftikdkKTDIVFSGLGWVTV 342
Cdd:COG1161  231 LEAIGRK-RGCLL-SGGEVDLEKAAEIL---------LTDFRSGKLGRITL 270
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 89-219 9.86e-16

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 77.78  E-value: 9.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  89 LQRLvgGNPILLVGNKADilpkSLKRERLIQwmkrEAKELGLKpvDVFLVSAGRGQGIREVIDAIEHYRNGKDVY----- 163
Cdd:PRK00093 105 LRKS--NKPVILVVNKVD----GPDEEADAY----EFYSLGLG--EPYPISAEHGRGIGDLLDAILEELPEEEEEdeede 172

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 752704354 164 -----VVGCTNVGKSTFINRIIkevsGEEDIITTSQfPGTTLDAIEIPLDDGSSLY---DTPGI 219
Cdd:PRK00093 173 pikiaIIGRPNVGKSSLINALL----GEERVIVSDI-AGTTRDSIDTPFERDGQKYtliDTAGI 231
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 161-236 2.97e-14

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: 68.41  E-value: 2.97e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752704354  161 DVYVVGCTNVGKSTFINRIIKEVSgeediiTTSQFPGTTLDAIEIPLDDGSS---LYDTPGIINNHQMAHYVNKKDLKI 236
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKA------IVSDYPGTTRDPNEGRLELKGKqiiLVDTPGLIEGASEGEGLGRAFLAI 73
 
Name Accession Description Interval E-value
GTPase_YqeH TIGR03597
ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of ...
 6-366 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: 613.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354    6 CIGCGVTIQTEDKTGLGYAPPASLTKENVICQRCFRLKNYNEIQDVSLTDDDFLNILHGIGETDSLVVKIVDIFDFNGSW 85
Cdd:TIGR03597   1 CIGCGAAIQTTDPKKPGYTPKSALEKEEVYCQRCFRLKHYNEIQDVELNDDDFLNLLNSLGDSNALIVYVVDIFDFEGSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354   86 INGLQRLVGGNPILLVGNKADILPKSLKRERLIQWMKREAKELGLKPVDVFLVSAGRGQGIREVIDAIEHYRNGKDVYVV 165
Cdd:TIGR03597  81 IPELKRFVGGNPVLLVGNKIDLLPKSVNLSKIKEWMKKRAKELGLKPVDIILVSAKKGNGIDELLDKIKKARNKKDVYVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  166 GCTNVGKSTFINRIIKEVSGEEDIITTSQFPGTTLDAIEIPLDDGSSLYDTPGIINNHQMAHYVNKKDLKILSPKKELKP 245
Cdd:TIGR03597 161 GVTNVGKSSLINKLLKQNNGDKDVITTSPFPGTTLDLIEIPLDDGHSLYDTPGIINSHQMAHYLDKKDLKYITPKKEIKP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  246 RTFQLNDQQTLYFGGLARFDYVSGERSPFICYMPNELMIHRTKLENADALYEKHAGELLTPPGKDEMDQFPELVAHTFTI 325
Cdd:TIGR03597 241 KTYQLNPNQTLFLGGLARFDYLKGEKTSFTFYVSNELNIHRTKLENADELYNKHLGNLLSPPCLDDKFNLPELVFHTFTI 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 752704354  326 KdKKTDIVFSGLGWVTVHDADKKVTAYAPKGVHVFVRRSLI 366
Cdd:TIGR03597 321 K-EKTDIVFSGLGWITVKRGGAKVKVYAPKGVGVSLRKALI 360
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 36-219 6.34e-81

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: 245.25  E-value: 6.34e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  36 CQRCFRLKNYNEIQDVSLTDDDFLNILHGIGETDSLVVKIVDIFDFNGSWINGLQRLVGGNPILLVGNKADILPKSLKRE 115
Cdd:cd01855    1 CQRCFKLKHYNKLLDVEIPDEDFLEILSTLLNDNALVVHVVDIFDFPGSLIPGLAELIGAKPVILVGNKIDLLPKDVKPN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354 116 RLIQWMKREAKELGLKPVDVFLVSAGRGQGIREVIDAIEHYRN-GKDVYVVGCTNVGKSTFINRIIKEVSG------EED 188
Cdd:cd01855   81 RLKQWVKKRLKIGGLKIKDVILVSAKKGWGVEELIEEIKKLAKyRGDVYVVGATNVGKSTLINALLKSNGGkvqaqaLVQ 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 752704354 189 IITTSQFPGTTLDAIEIPLDDGSSLYDTPGI 219
Cdd:cd01855  161 RLTVSPIPGTTLGLIKIPLGEGKKLYDTPGI 191
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
59-342 2.50e-79

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 244.25  E-value: 2.50e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  59 LNILHGIGETDSLVVKIVDIFDFNGSWINGLQRLVGGNPILLVGNKADILPKSLKRerliQWMKREAKElGlkpVDVFLV 138
Cdd:COG1161   14 RRQIKEILKLVDLVIEVVDARIPLSSRNPMLDELVGNKPRLLVLNKADLADPSVTK----QWLKYFEKQ-G---VDALAI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354 139 SAGRGQGIREVIDAIEHY-------RNGKDVYVVGCTNVGKSTFINRIIKevsgeEDIITTSQFPGTTLDAIEIPLDDGS 211
Cdd:COG1161   86 SAKKGKGIKELIEAIRELapekgikRRPIRVMIVGIPNVGKSTLINRLAG-----KKVAKTGNKPGVTKGQQWIKLDDGL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354 212 SLYDTPGIINnhqmAHYVNKKDLKILSPKKELKPRTFQLNDQQTLYFGGLARFdYVSGERSPFicympNELMIHRTKLEN 291
Cdd:COG1161  161 ELLDTPGILW----PKFEDPEVGYKLAATGAIKDEVLDLEEVALFLLGYLARR-YPELLKERY-----KLDELPRTKLEL 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 752704354 292 ADALYEKhAGELLtPPGKDEMDQFPELVahtftikdkKTDIVFSGLGWVTV 342
Cdd:COG1161  231 LEAIGRK-RGCLL-SGGEVDLEKAAEIL---------LTDFRSGKLGRITL 270
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 71-219 3.63e-30

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: 112.48  E-value: 3.63e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  71 LVVKIVDIFDFNGSWINGLQRLV--GGNPILLVGNKADILPKSLKRerliQWMkreAKELGLKPVDVFLVSAGRGQGIRE 148
Cdd:cd01849    2 VVVEVVDARDPLSSRNPDIEVLIneKNKKLIMVLNKADLVPKEVLR----KWV---AELSELYGTKTFFISATNGQGILK 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752704354 149 VIDAI------EHYRNGKDVYVVGCTNVGKSTFINRIIKEVSGEediitTSQFPGTTLDAIEIPLDDGSSLYDTPGI 219
Cdd:cd01849   75 LKAEItkqklkLKYKKGIRVGVVGLPNVGKSSFINALLNKFKLK-----VGSIPGTTKLQQDVKLDKEIYLYDTPGI 146
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
97-219 3.61e-17

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 82.38  E-value: 3.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  97 PILLVGNKADilpkSLKRERLIQwmkrEAKELGLKpvDVFLVSAGRGQGIREVIDAI-EHYRNGKD---------VYVVG 166
Cdd:COG1160  113 PVILVVNKVD----GPKREADAA----EFYSLGLG--EPIPISAEHGRGVGDLLDAVlELLPEEEEeeeeddpikIAIVG 182

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 752704354 167 CTNVGKSTFINRIIkevsGEEDIITTSQfPGTTLDAIEIPLD-DGSS--LYDTPGI 219
Cdd:COG1160  183 RPNVGKSSLINALL----GEERVIVSDI-AGTTRDSIDTPFErDGKKytLIDTAGI 233
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 89-219 9.86e-16

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 77.78  E-value: 9.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  89 LQRLvgGNPILLVGNKADilpkSLKRERLIQwmkrEAKELGLKpvDVFLVSAGRGQGIREVIDAIEHYRNGKDVY----- 163
Cdd:PRK00093 105 LRKS--NKPVILVVNKVD----GPDEEADAY----EFYSLGLG--EPYPISAEHGRGIGDLLDAILEELPEEEEEdeede 172

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 752704354 164 -----VVGCTNVGKSTFINRIIkevsGEEDIITTSQfPGTTLDAIEIPLDDGSSLY---DTPGI 219
Cdd:PRK00093 173 pikiaIIGRPNVGKSSLINALL----GEERVIVSDI-AGTTRDSIDTPFERDGQKYtliDTAGI 231
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 161-236 2.97e-14

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: 68.41  E-value: 2.97e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752704354  161 DVYVVGCTNVGKSTFINRIIKEVSgeediiTTSQFPGTTLDAIEIPLDDGSS---LYDTPGIINNHQMAHYVNKKDLKI 236
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKA------IVSDYPGTTRDPNEGRLELKGKqiiLVDTPGLIEGASEGEGLGRAFLAI 73
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 89-219 5.45e-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: 63.70  E-value: 5.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  89 LQRLVGGNPILLVGNKADILPKSLKRerliQWMKreakELGLKPVDVFLVSAGRGQGIREVIDAIEHYRNGKD------- 161
Cdd:cd01856   40 LDKILGNKPRLIVLNKADLADPAKTK----KWLK----YFKSQGEPVLFVNAKNGKGVKKLLKKAKKLLKENEklkakgl 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752704354 162 ------VYVVGCTNVGKSTFINRIIK---EVSGEEdiittsqfPGTTLDAIEIPLDDGSSLYDTPGI 219
Cdd:cd01856  112 lprplrAMVVGIPNVGKSTLINRLRGkkvAKVGNK--------PGVTRGQQWIRIGPNIELLDTPGI 170
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
 89-220 9.16e-11

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: 61.76  E-value: 9.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354   89 LQRLVGGNPILLVGNKADILPKslkrERLIQWMKReakeLGLKPVDVFLVSAGRGQGIREVIDAI-EHY--RNGKD---- 161
Cdd:TIGR03596  42 IDEIRGNKPRLIVLNKADLADP----AVTKQWLKY----FEEKGIKALAVNAKKGAGVKKIIKAAkKLLkeKNEKLkakg 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752704354  162 -------VYVVGCTNVGKSTFINRIIKEVSGEediitTSQFPGTTLDAIEIPLDDGSSLYDTPGII 220
Cdd:TIGR03596 114 lknrpirAMIVGIPNVGKSTLINRLAGKKVAK-----VGNRPGVTKGQQWIKLSDNLELLDTPGIL 174
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 94-219 1.38e-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: 59.48  E-value: 1.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354   94 GGNPILLVgNKADILPKslkRERLIQWMKReAKELGlkpVDVFLVSAGRGQGIREVIDAIEhyrnGKDVYVVGCTNVGKS 173
Cdd:pfam03193  53 GIEPVIVL-NKIDLLDE---EEELEELLKI-YRAIG---YPVLFVSAKTGEGIEALKELLK----GKTTVLAGQSGVGKS 120

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 752704354  174 TFINRIIkevsGEEDIIT--TSQFPG----TTLDAIEIPLDDGSSLYDTPGI 219
Cdd:pfam03193 121 TLLNALL----PELDLRTgeISEKLGrgrhTTTHVELFPLPGGGLLIDTPGF 168
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 65-219 5.55e-10

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: 57.33  E-value: 5.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  65 IGETDsLVVKIVDIFDFNGSWINGLQRLV--GGNPILLVGNKADILPkslkRERLIQWmkreAKELGLKPVDVFLVSAGR 142
Cdd:cd01859    9 IKEAD-VVLEVVDARDPELTRSRKLERMAleLGKKLIIVLNKADLVP----REVLEKW----KEVFESEGLPVVYVSARE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354 143 GQGIREVIDAIEHY-RNGKD--VYVVGCTNVGKSTFINRIIKEVSGEEDIITTSqfPGTTLDAIEIPLDDGSSLYDTPGI 219
Cdd:cd01859   80 RLGTRILRRTIKELaIDGKPviVGVVGYPKVGKSSIINALKGRHSASTSPIPGS--PGYTKGIQLVRIDSKIYLIDTPGV 157
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 97-219 8.31e-10

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: 58.18  E-value: 8.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  97 PILLVgNKADILPKSLKRERLIQWmkreaKELGlkpVDVFLVSAGRGQGIREVIDAIEhyrnGKDVYVVGCTNVGKSTFI 176
Cdd:cd01854   36 PVIVL-NKADLVDDEELEELLEIY-----EKLG---YPVLAVSAKTGEGLDELRELLK----GKTSVLVGQSGVGKSTLL 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 752704354 177 NRIIkevsGEEDIIT--TSQFPG----TTLDAIEIPLDDGSSLYDTPGI 219
Cdd:cd01854  103 NALL----PELVLATgeISEKLGrgrhTTTHRELFPLPGGGLIIDTPGF 147
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 162-219 3.60e-09

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: 55.52  E-value: 3.60e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 752704354 162 VYVVGCTNVGKSTFINRIIkevsGEEDIITTSQfPGTTLDAIEIPLDDGSSLY---DTPGI 219
Cdd:cd01895    5 IAIIGRPNVGKSSLLNALL----GEERVIVSDI-AGTTRDSIDVPFEYDGQKYtliDTAGI 60
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 157-219 1.05e-08

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: 53.65  E-value: 1.05e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752704354 157 RNGKDVYVVGCTNVGKSTFINRIikevSGEEDIITTSQfPGTTLDAIEIPLD-DGSS--LYDTPGI 219
Cdd:cd04164    1 REGIKVVIAGKPNVGKSSLLNAL----AGRDRAIVSDI-AGTTRDVIEEEIDlGGIPvrLIDTAGL 61
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 164-219 7.50e-08

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: 51.48  E-value: 7.50e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354 164 VVGCTNVGKSTFINRIIKEVSGEediitTSQFPGTTLDAI--EIPLDDGSS--LYDTPGI 219
Cdd:cd00880    2 IFGRPNVGKSSLLNALLGQNVGI-----VSPIPGTTRDPVrkEWELLPLGPvvLIDTPGL 56
PRK00098 PRK00098
GTPase RsgA; Reviewed
 97-219 4.63e-07

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 50.97  E-value: 4.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  97 PILLVGNKADILpkslkrERLIQWMKREA--KELGlkpVDVFLVSAGRGQGIREVIDAIEhyrnGKDVYVVGCTNVGKST 174
Cdd:PRK00098 113 KPIIVLNKIDLL------DDLEEARELLAlyRAIG---YDVLELSAKEGEGLDELKPLLA----GKVTVLAGQSGVGKST 179

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 752704354 175 FINRIIKEVSGEEDIITTSQFPG--TTLDAIEIPLDDGSSLYDTPGI 219
Cdd:PRK00098 180 LLNALAPDLELKTGEISEALGRGkhTTTHVELYDLPGGGLLIDTPGF 226
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 144-219 1.67e-06

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: 49.67  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354 144 QGIREVIDAI-------EHYRNGKDVYVVGCTNVGKSTFINRIikevSGEEDIITTSQfPGTTLDAIEIPLD-DGSS--L 213
Cdd:COG0486  191 EELREELEALlasarqgELLREGIKVVIVGRPNVGKSSLLNAL----LGEERAIVTDI-AGTTRDVIEERINiGGIPvrL 265


                 ....*.
gi 752704354 214 YDTPGI 219
Cdd:COG0486  266 IDTAGL 271
PRK12289 PRK12289
small ribosomal subunit biogenesis GTPase RsgA;
95-228 2.08e-06

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237040 [Multi-domain]  Cd Length: 352  Bit Score: 49.24  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  95 GNPILLVGNKADIL-PKSLK--RERLIQWmkreakelGLKPvdvFLVSAGRGQGIreviDAIEHYRNGKDVYVVGCTNVG 171
Cdd:PRK12289 120 GLEIVLCLNKADLVsPTEQQqwQDRLQQW--------GYQP---LFISVETGIGL----EALLEQLRNKITVVAGPSGVG 184

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354 172 KSTFINRII-------KEVSGEediitTSQFPGTTLDAIEIPLDDGSSLYDTPG------IINNHQMAHY 228
Cdd:PRK12289 185 KSSLINRLIpdvelrvGKVSGK-----LGRGRHTTRHVELFELPNGGLLADTPGfnqpdlDCSPRELAHY 249
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
134-219 2.09e-06

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 49.34  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354 134 DVFLVSAGRGQGIREVIDAIEH----------YRNGKDVYVVGCTNVGKSTFINRIIKE----VSgeeDIittsqfPGTT 199
Cdd:PRK05291 180 IEFLSDEKILEKLEELIAELEAllasarqgeiLREGLKVVIAGRPNVGKSSLLNALLGEeraiVT---DI------AGTT 250

                         90       100
                 ....*....|....*....|...
gi 752704354 200 LDAIEIPLD-DGSS--LYDTPGI 219
Cdd:PRK05291 251 RDVIEEHINlDGIPlrLIDTAGI 273
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 62-219 2.61e-06

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 49.41  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  62 LHGIGETDSLVVKIvdifdfngswingLQRlvGGNPILLVGNKADilpkslkrERLIQWMKREAKELGL-KPvdvFLVSA 140
Cdd:PRK09518 365 QVGLTSTDERIVRM-------------LRR--AGKPVVLAVNKID--------DQASEYDAAEFWKLGLgEP---YPISA 418

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354 141 GRGQGIREVIDAI-----EHYRNG--------KDVYVVGCTNVGKSTFINRIikevSGEEDIItTSQFPGTTLDAIE--I 205
Cdd:PRK09518 419 MHGRGVGDLLDEAldslkVAEKTSgfltpsglRRVALVGRPNVGKSSLLNQL----THEERAV-VNDLAGTTRDPVDeiV 493

                        170
                 ....*....|....*
gi 752704354 206 PLDDGSSLY-DTPGI 219
Cdd:PRK09518 494 EIDGEDWLFiDTAGI 508
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 164-237 3.01e-06

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: 46.68  E-value: 3.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354 164 VVGCTNVGKSTFINRIIKEVSGEediitTSQFPGTTLDAIEIPLDDGSS-----LYDTPGII------NNHQMAHYVNKK 232
Cdd:cd00882    2 VVGRGGVGKSSLLNALLGGEVGE-----VSDVPGTTRDPDVYVKELDKGkvklvLVDTPGLDefgglgREELARLLLRGA 76


                 ....*
gi 752704354 233 DLKIL 237
Cdd:cd00882   77 DLILL 81
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 95-156 4.72e-06

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: 46.08  E-value: 4.72e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 752704354  95 GNPILLVGNKADILPKSLKRERLiqwmkREAKELGLKPVDVFLVSAGRGQGIREVIDAIEHY 156
Cdd:cd00880  104 GKPVLLVLNKIDLVPESEEEELL-----RERKLELLPDLPVIAVSALPGEGIDELRKKIAEL 160
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
162-220 8.48e-06

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 45.74  E-value: 8.48e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 752704354 162 VYVVGCTNVGKSTFINRIIKEVSGEEDIITTSqfpGTTLDAIEIPLDDGSS---LYDTPGII 220
Cdd:COG1100    6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLSTN---GVTIDKKELKLDGLDVdlvIWDTPGQD 64
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
 162-219 1.00e-05

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: 1.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 752704354  162 VYVVGCTNVGKSTFINRIIKevsgeEDIITTSQFPGTTLDAIEIPLDDGSS---LYDTPGI 219
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHG-----QKISITSPKAQTTRNRISGIHTTGASqiiFIDTPGF 58
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 130-219 2.91e-05

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: 45.55  E-value: 2.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  130 LKPVDVFLVSAGRGQGIREVID-AIehyrngkdvyvVGCTNVGKSTFINRIikevSGEEDIITTSQfPGTTLDAIEIPLD 208
Cdd:pfam12631  75 LAELEKLLATADRGRILREGIKvVI-----------VGKPNVGKSSLLNAL----LGEERAIVTDI-PGTTRDVIEETIN 138

                          90
                  ....*....|....
gi 752704354  209 -DGSS--LYDTPGI 219
Cdd:pfam12631 139 iGGIPlrLIDTAGI 152
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 95-153 2.95e-05

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: 43.98  E-value: 2.95e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 752704354  95 GNPILLVGNKADILPkslkrERLIQWMKREAKELGLKPVDVFLVSAGRGQGIREVIDAI 153
Cdd:cd00882  106 GIPIILVGNKIDLLE-----EREVEELLRLEELAKILGVPVFEVSAKTGEGVDELFEKL 159
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
 94-219 7.09e-05

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: 42.95  E-value: 7.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  94 GGNPILLVGNKADILPKslkrERLIQWMK--------------------REAKELGLKPVDVFLVSAGRGQGIREVIDAI 153
Cdd:cd04178   29 PNKKLVLVLNKIDLVPK----ENVEKWLKylrnefptvafkastqqqkkNLSRKSKKVKASDDLLSSSACLGADALLKLL 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752704354 154 EHYRNGKD------VYVVGCTNVGKSTFINRIIKE----VSGEediittsqfPGTTLDAIEIPLDDGSSLYDTPGI 219
Cdd:cd04178  105 KNYARNKGiktsitVGVVGYPNVGKSSVINSLKRSracnVGAT---------PGVTKSMQEVHLDKHVKLLDSPGV 171
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 162-227 7.11e-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: 42.83  E-value: 7.11e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354 162 VYVVGCTNVGKSTFINRIIKE-VSgeediITTSQfPGTTLDAI-EIPLDDGSSL--YDTPGIINNHQMAH 227
Cdd:cd04163    6 VAIIGRPNVGKSTLLNALVGQkIS-----IVSPK-PQTTRNRIrGIYTDDDAQIifVDTPGIHKPKKKLG 69
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 64-219 8.75e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 44.19  E-value: 8.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  64 GIGETDSLVVKIvdifdfngswingLQRlvGGNPILLVGNKADilpkslkRERliQWMkrEAKE---LGLKpvDVFLVSA 140
Cdd:PRK03003 130 GATATDEAVARV-------------LRR--SGKPVILAANKVD-------DER--GEA--DAAAlwsLGLG--EPHPVSA 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354 141 GRGQGIREVIDAI-----EHYRNG------KDVYVVGCTNVGKSTFINRiikeVSGEEDIItTSQFPGTTLDAIE--IPL 207
Cdd:PRK03003 182 LHGRGVGDLLDAVlaalpEVPRVGsasggpRRVALVGKPNVGKSSLLNK----LAGEERSV-VDDVAGTTVDPVDslIEL 256

                        170
                 ....*....|...
gi 752704354 208 DDGS-SLYDTPGI 219
Cdd:PRK03003 257 GGKTwRFVDTAGL 269
TIGR00157 TIGR00157
ribosome small subunit-dependent GTPase A; Members of this protein were designated YjeQ and ...
 134-219 1.13e-04

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


Pssm-ID: 272934 [Multi-domain]  Cd Length: 245  Bit Score: 43.17  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  134 DVFLVSAGRGQGIREVIdaiEHYRNGKDVYVvGCTNVGKSTFINRIIKEVSGE-EDIITTSQF-PGTTLDAIEIPLDDGs 211
Cdd:TIGR00157  99 QVLMTSSKNQDGLKELI---EALQNRISVFA-GQSGVGKSSLINALDPSVKQQvNDISSKLGLgKHTTTHVELFHFHGG- 173


                  ....*...
gi 752704354  212 SLYDTPGI 219
Cdd:TIGR00157 174 LIADTPGF 181
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 60-156 1.44e-04

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: 42.06  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  60 NILHGIGETDsLVVKIVDIFDFNGS---WI-NGLQRLvgGNPILLVGNKADILPKSLKRERLIQWMKreakeLGLKPVDV 135
Cdd:cd04163   75 AAWSALKDVD-LVLFVVDASEWIGEgdeFIlELLKKS--KTPVILVLNKIDLVKDKEDLLPLLEKLK-----ELHPFAEI 146

                         90       100
                 ....*....|....*....|.
gi 752704354 136 FLVSAGRGQGIREVIDAIEHY 156
Cdd:cd04163  147 FPISALKGENVDELLEYIVEY 167
obgE PRK12299
GTPase CgtA; Reviewed
 97-153 1.89e-04

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 42.75  E-value: 1.89e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 752704354  97 PILLVGNKADILPKSLKRErliqwmKREAKELGLKPVDVFLVSAGRGQGIREVIDAI 153
Cdd:PRK12299 273 PRILVLNKIDLLDEEEERE------KRAALELAALGGPVFLISAVTGEGLDELLRAL 323
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
85-164 2.14e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 41.51  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  85 WINGLQRLVGGNPILLVGNKADILP--KSLKRERLIQWMKREakelglKPVDVFLVSAGRGQGIREVIDAI-EHYRNGKD 161
Cdd:COG1100  101 LLESLRRLGKKSPIILVLNKIDLYDeeEIEDEERLKEALSED------NIVEVVATSAKTGEGVEELFAALaEILRGEGD 174


                 ...
gi 752704354 162 VYV 164
Cdd:COG1100  175 SLD 177
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 97-153 6.30e-04

Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain.


Pssm-ID: 206685 [Multi-domain]  Cd Length: 170  Bit Score: 40.10  E-value: 6.30e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 752704354  97 PILLVGNKADILPKSLKRERLiqwmkrEAKELGLKPVDVFLVSAGRGQGIREVIDAI 153
Cdd:cd01898  116 PRIVVLNKIDLLDAEERFEKL------KELLKELKGKKVFPISALTGEGLDELLKKL 166
Rab21 cd04123
Rab GTPase family 21 (Rab21); The localization and function of Rab21 are not clearly defined, ...
 85-153 6.42e-04

Rab GTPase family 21 (Rab21); The localization and function of Rab21 are not clearly defined, with conflicting data reported. Rab21 has been reported to localize in the ER in human intestinal epithelial cells, with partial colocalization with alpha-glucosidase, a late endosomal/lysosomal marker. More recently, Rab21 was shown to colocalize with and affect the morphology of early endosomes. In Dictyostelium, GTP-bound Rab21, together with two novel LIM domain proteins, LimF and ChLim, has been shown to regulate phagocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133323 [Multi-domain]  Cd Length: 162  Bit Score: 39.90  E-value: 6.42e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 752704354  85 WINGLQRLVGGN-PILLVGNKADilpksLKRERLIQWMKRE--AKELGLKpvdVFLVSAGRGQGIREVIDAI 153
Cdd:cd04123   94 WIKELKQMRGNNiSLVIVGNKID-----LERQRVVSKSEAEeyAKSVGAK---HFETSAKTGKGIEELFLSL 157
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
164-220 7.46e-04

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 40.74  E-value: 7.46e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 752704354 164 VVGCTNVGKSTFINRIIKE-VSgeediITTSQfPGTTLDAIEIPLDDGSS---LYDTPGII 220
Cdd:COG1159    8 IVGRPNVGKSTLLNALVGQkVS-----IVSPK-PQTTRHRIRGIVTREDAqivFVDTPGIH 62
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
97-156 7.66e-04

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 40.74  E-value: 7.66e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  97 PILLVGNKADILPKSLKRERLIQWMKReakelgLKPVDVFLVSAGRGQGIREVIDAIEHY 156
Cdd:COG1159  113 PVILVINKIDLVKKEELLPLLAEYSEL------LDFAEIVPISALKGDNVDELLDEIAKL 166
era PRK00089
GTPase Era; Reviewed
 162-219 8.55e-04

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 40.80  E-value: 8.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 752704354 162 VYVVGCTNVGKSTFINRIIKE-VSgeediITTSQfPGTTLDAIE-IPLDDGSS--LYDTPGI 219
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQkIS-----IVSPK-PQTTRHRIRgIVTEDDAQiiFVDTPGI 63
Rab5_related cd01860
Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion; The ...
 84-153 1.02e-03

Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion; The Rab5-related subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206653 [Multi-domain]  Cd Length: 163  Bit Score: 39.46  E-value: 1.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 752704354  84 SWINGLQRLVGGNPIL-LVGNKADILPkslKRERLIQWMKREAKELGLkpvDVFLVSAGRGQGIREVIDAI 153
Cdd:cd01860   94 SWVKELQEHGPPNIVIaLAGNKADLES---KRQVSTEEAQEYADENGL---LFMETSAKTGENVNELFTEI 158
Sar1 cd00879
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ...
 97-156 1.25e-03

Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII vesicle coats involved in export of cargo from the ER. The GTPase activity of Sar1 functions as a molecular switch to control protein-protein and protein-lipid interactions that direct vesicle budding from the ER. Activation of the GDP to the GTP-bound form of Sar1 involves the membrane-associated guanine nucleotide exchange factor (GEF) Sec12. Sar1 is unlike all Ras superfamily GTPases that use either myristoyl or prenyl groups to direct membrane association and function, in that Sar1 lacks such modification. Instead, Sar1 contains a unique nine-amino-acid N-terminal extension. This extension contains an evolutionarily conserved cluster of bulky hydrophobic amino acids, referred to as the Sar1-N-terminal activation recruitment (STAR) motif. The STAR motif mediates the recruitment of Sar1 to ER membranes and facilitates its interaction with mammalian Sec12 GEF leading to activation.


Pssm-ID: 206645 [Multi-domain]  Cd Length: 191  Bit Score: 39.57  E-value: 1.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  97 PILLVGNKADIlPKSLKRERLIQWM----------KREAKELGLKPVDVFLVSAGRGQGIREVIDAIEHY 156
Cdd:cd00879  122 PILILGNKIDK-PGAVSEEELREALglygtttgkgGVSLKVSNIRPVEVFMCSVVKRQGYGEGFRWLSQY 190
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 97-156 1.27e-03

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: 39.03  E-value: 1.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  97 PILLVGNKADILPKSLKRERLIQWMKREAKELGLKPVdvFLVSAGRGQGIREVIDAIEHY 156
Cdd:cd01876  112 PFLIVLTKADKLKKSELAKVLKKIKEELNLFNILPPV--ILFSSKKGTGIDELRALIAEW 169
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
 152-247 1.65e-03

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


Pssm-ID: 206652  Cd Length: 248  Bit Score: 39.61  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354 152 AIEHYRNGKD-------VYVVGCTNVGKSTFINRIIkevsgEEDIITTSQFPGTTLDAIEIpldDGS------SLYDTPG 218
Cdd:cd01853   17 LHELEAKLKKeldfsltILVLGKTGVGKSSTINSIF-----GERKVSVSAFQSETLRPREV---SRTvdgfklNIIDTPG 88

                         90       100
                 ....*....|....*....|....*....
gi 752704354 219 IINNHQmaHYVNKKDLKILspKKELKPRT 247
Cdd:cd01853   89 LLESQD--QRVNRKILSII--KRFLKKKT 113
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 164-234 2.94e-03

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


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 38.30  E-value: 2.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752704354 164 VVGCTNVGKSTFINRII-KEVSGEEDIITTSQfpgTTLdaIEIPLDDGSSLYDTPGI---INNHQMA--HYVNKKDL 234
Cdd:cd09912    5 VVGEFSAGKSTLLNALLgEEVLPTGVTPTTAV---ITV--LRYGLLKGVVLVDTPGLnstIEHHTEIteSFLPRADA 76
MeaB pfam03308
Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ...
 64-157 3.07e-03

Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ArgK proteins acting as ATPase enzymes and kinases. They are now believed to be methylmalonyl Co-A mutase-associated GTPase MeaB. Structural studies of MeaB and the human ortholog (methylmalonyl associated protein A) MMAA, reveal alpha-helical domains at the N- and C-termini as well as a Ras-like GTPase domain. Mutational analysis of MeaB, show prohibited growth in Methylobacterium due to the inability to convert methylmalonyl-CoA to succinyl-CoA caused by an inactive form of methylmalonyl-CoA mutatase (mcm). In humans, mutations in (MMAA) are associated with the fatal disease methylmalonyl aciduria.


Pssm-ID: 281323 [Multi-domain]  Cd Length: 272  Bit Score: 38.96  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354   64 GIGETDSLVVKIVDIFDF-----NGSWINGLQRLVGGNPILLVGNKADI-LPKSLKRERLIQWMKR--EAKELGLKPvDV 135
Cdd:pfam03308 135 GVGQSEVDVANMVDTFVLltmpgGGDELQGIKAGIMEIADIYVVNKADGnLPGAERAARELRAALHllTPFEAGWRP-PV 213

                          90       100
                  ....*....|....*....|..
gi 752704354  136 FLVSAGRGQGIREVIDAIEHYR 157
Cdd:pfam03308 214 LTTSAVRGEGIDELWDAIEEHR 235
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 165-219 3.80e-03

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: 37.41  E-value: 3.80e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 752704354 165 VGCTNVGKSTFINRIIkevsGEEDIItTSQFPGTTLDAIE--IPLDDGS-SLYDTPGI 219
Cdd:cd01894    3 VGRPNVGKSTLFNRLT----GRRDAI-VSDTPGVTRDRKYgeAEWGGREfILIDTGGI 55
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
164-219 5.26e-03

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 38.47  E-value: 5.26e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 752704354 164 VVGCTNVGKSTFINRIIkevsGEEDIITTSQfPGTTLDAI--EIPLDDGS-SLYDTPGI 219
Cdd:COG1160    7 IVGRPNVGKSTLFNRLT----GRRDAIVDDT-PGVTRDRIygEAEWGGREfTLIDTGGI 60
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 165-219 7.31e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 38.11  E-value: 7.31e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 752704354 165 VGCTNVGKSTFINRIIkevsGEEDIItTSQFPGTTLDAI--EIPLDDGS-SLYDTPGI 219
Cdd:PRK00093   7 VGRPNVGKSTLFNRLT----GKRDAI-VADTPGVTRDRIygEAEWLGREfILIDTGGI 59
Arl10_like cd04159
Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from ...
 70-151 7.47e-03

Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from a human cancer-derived EST dataset. No functional information about the subfamily is available at the current time, but crystal structures of human Arl10b and Arl10c have been solved.


Pssm-ID: 206724 [Multi-domain]  Cd Length: 159  Bit Score: 36.91  E-value: 7.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752704354  70 SLVVKIVDIFDFnGSW---INGLQRLVG-----GNPILLVGNKADiLPKSLKRERLIQWMKreAKELGLKPVDVFLVSAG 141
Cdd:cd04159   69 NAIVYVVDAADR-EKLevaKNELHDLLEkpsleGIPLLVLGNKND-LPGALSVDELIEQMN--LKSITDREVSCYSISAK 144

                         90
                 ....*....|
gi 752704354 142 RGQGIREVID 151
Cdd:cd04159  145 EKTNIDIVLD 154
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
 84-153 9.75e-03

Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible.


Pssm-ID: 206640 [Multi-domain]  Cd Length: 159  Bit Score: 36.28  E-value: 9.75e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 752704354  84 SWINGLQRLVGGN-PILLVGNKADILPKSL-KRERLIQWmkreAKELGLKpvdVFLVSAGRGQGIREVIDAI 153
Cdd:cd00154   93 KWLNELKEYAPPNiPIILVGNKSDLEDERQvSTEEAQQF----AKENGLL---FFETSAKTGENVDEAFESL 157
 
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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