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Conserved domains on  [gi|892236348|emb|CMY13194|]
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GTP-binding protein [Streptococcus pneumoniae]

Protein Classification

YlqF/YawG family GTPase( domain architecture ID 11497227)

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

CATH:  3.40.50.300
Gene Ontology:  GO:0005525|GO:0003924
PubMed:  11916378
SCOP:  4004041|4007669

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
4-274 7.90e-147

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: 412.29  E-value: 7.90e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348    4 IQWFPGHMSKARRQVQENLKFVDFVTILVDARLPLSSQNPMLTKIVGDKPKLLILNKADLADPAMTKEWRQYFESQGIQT 83
Cdd:TIGR03596   1 IQWFPGHMAKARREIKENLKLVDVVIEVLDARIPLSSRNPMIDEIRGNKPRLIVLNKADLADPAVTKQWLKYFEEKGIKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348   84 LAINSKEQVTVKVVTDAAKKLMADKIARQKERGIQIETLRTMIIGIPNAGKSTLMNRLAGKKIAVVGNKPGVTKGQQWLK 163
Cdd:TIGR03596  81 LAVNAKKGAGVKKIIKAAKKLLKEKNEKLKAKGLKNRPIRAMIVGIPNVGKSTLINRLAGKKVAKVGNRPGVTKGQQWIK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  164 TNKDLEILDTPGILWPKFEDETVALKLALTGAIKDQLLPMDEVTIFGINYFKEHYPEKLAERFKQMKIEEEPSVIIMDMT 243
Cdd:TIGR03596 161 LSDNLELLDTPGILWPKFEDQEVGLKLAATGAIKDEALDLEDVALFLLEYLLEHYPELLKERYKLDELPEDPVELLEAIA 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 892236348  244 RALGF-----RDDYDRFYSLFVKEVRDGKLGNYTLD 274
Cdd:TIGR03596 241 KKRGCllkggELDLDRAAEILLNDFRKGKLGRISLE 276
 
Name Accession Description Interval E-value
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
4-274 7.90e-147

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: 412.29  E-value: 7.90e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348    4 IQWFPGHMSKARRQVQENLKFVDFVTILVDARLPLSSQNPMLTKIVGDKPKLLILNKADLADPAMTKEWRQYFESQGIQT 83
Cdd:TIGR03596   1 IQWFPGHMAKARREIKENLKLVDVVIEVLDARIPLSSRNPMIDEIRGNKPRLIVLNKADLADPAVTKQWLKYFEEKGIKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348   84 LAINSKEQVTVKVVTDAAKKLMADKIARQKERGIQIETLRTMIIGIPNAGKSTLMNRLAGKKIAVVGNKPGVTKGQQWLK 163
Cdd:TIGR03596  81 LAVNAKKGAGVKKIIKAAKKLLKEKNEKLKAKGLKNRPIRAMIVGIPNVGKSTLINRLAGKKVAKVGNRPGVTKGQQWIK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  164 TNKDLEILDTPGILWPKFEDETVALKLALTGAIKDQLLPMDEVTIFGINYFKEHYPEKLAERFKQMKIEEEPSVIIMDMT 243
Cdd:TIGR03596 161 LSDNLELLDTPGILWPKFEDQEVGLKLAATGAIKDEALDLEDVALFLLEYLLEHYPELLKERYKLDELPEDPVELLEAIA 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 892236348  244 RALGF-----RDDYDRFYSLFVKEVRDGKLGNYTLD 274
Cdd:TIGR03596 241 KKRGCllkggELDLDRAAEILLNDFRKGKLGRISLE 276
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
3-278 2.13e-139

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 393.70  E-value: 2.13e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348   3 TIQWFPGHMSKARRQVQENLKFVDFVTILVDARLPLSSQNPMLTKIVGDKPKLLILNKADLADPAMTKEWRQYFESQGIQ 82
Cdd:COG1161    2 QIQWFPGHMAKARRQIKEILKLVDLVIEVVDARIPLSSRNPMLDELVGNKPRLLVLNKADLADPSVTKQWLKYFEKQGVD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  83 TLAINSKEQVTVKVVTDAAKKLMadkiarqKERGIQIETLRTMIIGIPNAGKSTLMNRLAGKKIAVVGNKPGVTKGQQWL 162
Cdd:COG1161   82 ALAISAKKGKGIKELIEAIRELA-------PEKGIKRRPIRVMIVGIPNVGKSTLINRLAGKKVAKTGNKPGVTKGQQWI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348 163 KTNKDLEILDTPGILWPKFEDETVALKLALTGAIKDQLLPMDEVTIFGINYFKEHYPEKLAERFKQMKIEEEPSVIIMDM 242
Cdd:COG1161  155 KLDDGLELLDTPGILWPKFEDPEVGYKLAATGAIKDEVLDLEEVALFLLGYLARRYPELLKERYKLDELPRTKLELLEAI 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 892236348 243 TRALGF-----RDDYDRFYSLFVKEVRDGKLGNYTLDTLED 278
Cdd:COG1161  235 GRKRGCllsggEVDLEKAAEILLTDFRSGKLGRITLETPEE 275
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
6-177 8.00e-87

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: 256.30  E-value: 8.00e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348   6 WFPGHMSKARRQVQENLKFVDFVTILVDARLPLSSQNPMLTKIVGDKPKLLILNKADLADPAMTKEWRQYFESQGIQTLA 85
Cdd:cd01856    1 WFPGHMAKALRQIKEKLKLVDVVIEVRDARIPLSSRNPDLDKILGNKPRLIVLNKADLADPAKTKKWLKYFKSQGEPVLF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  86 INSKEQVTVKVVTDAAKKLMADKIARQKeRGIQIETLRTMIIGIPNAGKSTLMNRLAGKKIAVVGNKPGVTKGQQWLKTN 165
Cdd:cd01856   81 VNAKNGKGVKKLLKKAKKLLKENEKLKA-KGLLPRPLRAMVVGIPNVGKSTLINRLRGKKVAKVGNKPGVTRGQQWIRIG 159
                        170
                 ....*....|..
gi 892236348 166 KDLEILDTPGIL 177
Cdd:cd01856  160 PNIELLDTPGIL 171
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
123-186 7.74e-16

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 71.88  E-value: 7.74e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 892236348  123 RTMIIGIPNAGKSTLMNRLAGKKiAVVGNKPGVTKGQQ---WLKTNKDLEILDTPGILWPKFEDETV 186
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK-AIVSDYPGTTRDPNegrLELKGKQIILVDTPGLIEGASEGEGL 66
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
126-209 1.28e-11

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 64.30  E-value: 1.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348 126 IIGIPNAGKSTLMNRLAGKKIAVVGNKPGVT----KGQ-QWLktNKDLEILDTPGIlwpKFEDETvalklaLTGAIKDQ- 199
Cdd:PRK00093   6 IVGRPNVGKSTLFNRLTGKRDAIVADTPGVTrdriYGEaEWL--GREFILIDTGGI---EPDDDG------FEKQIREQa 74
                         90
                 ....*....|..
gi 892236348 200 LLPMDE--VTIF 209
Cdd:PRK00093  75 ELAIEEadVILF 86
 
Name Accession Description Interval E-value
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
4-274 7.90e-147

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: 412.29  E-value: 7.90e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348    4 IQWFPGHMSKARRQVQENLKFVDFVTILVDARLPLSSQNPMLTKIVGDKPKLLILNKADLADPAMTKEWRQYFESQGIQT 83
Cdd:TIGR03596   1 IQWFPGHMAKARREIKENLKLVDVVIEVLDARIPLSSRNPMIDEIRGNKPRLIVLNKADLADPAVTKQWLKYFEEKGIKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348   84 LAINSKEQVTVKVVTDAAKKLMADKIARQKERGIQIETLRTMIIGIPNAGKSTLMNRLAGKKIAVVGNKPGVTKGQQWLK 163
Cdd:TIGR03596  81 LAVNAKKGAGVKKIIKAAKKLLKEKNEKLKAKGLKNRPIRAMIVGIPNVGKSTLINRLAGKKVAKVGNRPGVTKGQQWIK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  164 TNKDLEILDTPGILWPKFEDETVALKLALTGAIKDQLLPMDEVTIFGINYFKEHYPEKLAERFKQMKIEEEPSVIIMDMT 243
Cdd:TIGR03596 161 LSDNLELLDTPGILWPKFEDQEVGLKLAATGAIKDEALDLEDVALFLLEYLLEHYPELLKERYKLDELPEDPVELLEAIA 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 892236348  244 RALGF-----RDDYDRFYSLFVKEVRDGKLGNYTLD 274
Cdd:TIGR03596 241 KKRGCllkggELDLDRAAEILLNDFRKGKLGRISLE 276
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
3-278 2.13e-139

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 393.70  E-value: 2.13e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348   3 TIQWFPGHMSKARRQVQENLKFVDFVTILVDARLPLSSQNPMLTKIVGDKPKLLILNKADLADPAMTKEWRQYFESQGIQ 82
Cdd:COG1161    2 QIQWFPGHMAKARRQIKEILKLVDLVIEVVDARIPLSSRNPMLDELVGNKPRLLVLNKADLADPSVTKQWLKYFEKQGVD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  83 TLAINSKEQVTVKVVTDAAKKLMadkiarqKERGIQIETLRTMIIGIPNAGKSTLMNRLAGKKIAVVGNKPGVTKGQQWL 162
Cdd:COG1161   82 ALAISAKKGKGIKELIEAIRELA-------PEKGIKRRPIRVMIVGIPNVGKSTLINRLAGKKVAKTGNKPGVTKGQQWI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348 163 KTNKDLEILDTPGILWPKFEDETVALKLALTGAIKDQLLPMDEVTIFGINYFKEHYPEKLAERFKQMKIEEEPSVIIMDM 242
Cdd:COG1161  155 KLDDGLELLDTPGILWPKFEDPEVGYKLAATGAIKDEVLDLEEVALFLLGYLARRYPELLKERYKLDELPRTKLELLEAI 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 892236348 243 TRALGF-----RDDYDRFYSLFVKEVRDGKLGNYTLDTLED 278
Cdd:COG1161  235 GRKRGCllsggEVDLEKAAEILLTDFRSGKLGRITLETPEE 275
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
6-177 8.00e-87

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: 256.30  E-value: 8.00e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348   6 WFPGHMSKARRQVQENLKFVDFVTILVDARLPLSSQNPMLTKIVGDKPKLLILNKADLADPAMTKEWRQYFESQGIQTLA 85
Cdd:cd01856    1 WFPGHMAKALRQIKEKLKLVDVVIEVRDARIPLSSRNPDLDKILGNKPRLIVLNKADLADPAKTKKWLKYFKSQGEPVLF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  86 INSKEQVTVKVVTDAAKKLMADKIARQKeRGIQIETLRTMIIGIPNAGKSTLMNRLAGKKIAVVGNKPGVTKGQQWLKTN 165
Cdd:cd01856   81 VNAKNGKGVKKLLKKAKKLLKENEKLKA-KGLLPRPLRAMVVGIPNVGKSTLINRLRGKKVAKVGNKPGVTRGQQWIRIG 159
                        170
                 ....*....|..
gi 892236348 166 KDLEILDTPGIL 177
Cdd:cd01856  160 PNIELLDTPGIL 171
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
26-176 9.06e-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: 109.78  E-value: 9.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  26 DFVTILVDARLPLSSQNPMLTKIV--GDKPKLLILNKADLADPAMTKEWRQY-FESQGIQTLAINSKEQVTVKVVTDAAK 102
Cdd:cd01849    1 DVVVEVVDARDPLSSRNPDIEVLIneKNKKLIMVLNKADLVPKEVLRKWVAElSELYGTKTFFISATNGQGILKLKAEIT 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 892236348 103 KLMADKIARQKergiqietLRTMIIGIPNAGKSTLMNRLAGKKIAVVGNKPGVTKGQQWLKTNKDLEILDTPGI 176
Cdd:cd01849   81 KQKLKLKYKKG--------IRVGVVGLPNVGKSSFINALLNKFKLKVGSIPGTTKLQQDVKLDKEIYLYDTPGI 146
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
15-176 4.50e-28

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: 105.48  E-value: 4.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  15 RRQVQENLKFVDFVTILVDARLPLSSQNPMLTKIV--GDKPKLLILNKADLADPAMTKEWRQYFESQGIQTLAINSKEQV 92
Cdd:cd01859    2 KRLVRRIIKEADVVLEVVDARDPELTRSRKLERMAleLGKKLIIVLNKADLVPREVLEKWKEVFESEGLPVVYVSARERL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  93 TVKVVTDAAKKLMADKiarqkergiqiETLRTMIIGIPNAGKSTLMNRLAGKKIAV---VGNKPGVTKGQQWLKTNKDLE 169
Cdd:cd01859   82 GTRILRRTIKELAIDG-----------KPVIVGVVGYPKVGKSSIINALKGRHSAStspIPGSPGYTKGIQLVRIDSKIY 150

                 ....*..
gi 892236348 170 ILDTPGI 176
Cdd:cd01859  151 LIDTPGV 157
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
16-179 5.34e-21

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: 86.52  E-value: 5.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  16 RQVQENLKFVDFVTILVDARLPLSSQNPML----TKIVGDKPKLLILNKADLADPAMTKEWRQYFESQGIQTLAINSKEQ 91
Cdd:cd01857    3 RQLWRVIERSDVVVQIVDARNPLFFRCPDLekyvKEVDPSKENVLLLNKADLVTEEQRKAWARYFKKEGIVVLFFSALNE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  92 VTVKVVtdaakklmadkiarqkergiqietlrtmiiGIPNAGKSTLMNRLAGKKIAVVGNKPGVTKGQQWLKTNKDLEIL 171
Cdd:cd01857   83 ATIGLV------------------------------GYPNVGKSSLINALVGSKKVSVSSTPGKTKHFQTIFLEPGITLC 132

                 ....*...
gi 892236348 172 DTPGILWP 179
Cdd:cd01857  133 DCPGLVFP 140
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
26-176 1.94e-20

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: 85.70  E-value: 1.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  26 DFVTILVDARLPLSSQNPMLTKIV----GDKPKLLILNKADLADPAMTKEWRQYFES------------QGIQTLAINSK 89
Cdd:cd04178    1 DVILEVLDARDPLGCRCPQVERAVlvlgPNKKLVLVLNKIDLVPKENVEKWLKYLRNefptvafkastqQQKKNLSRKSK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  90 EQVTVKVVTDAAKKLMAD---KIARQKERGIQIETLRTM-IIGIPNAGKSTLMNRLAGKKIAVVGNKPGVTKGQQWLKTN 165
Cdd:cd04178   81 KVKASDDLLSSSACLGADallKLLKNYARNKGIKTSITVgVVGYPNVGKSSVINSLKRSRACNVGATPGVTKSMQEVHLD 160
                        170
                 ....*....|.
gi 892236348 166 KDLEILDTPGI 176
Cdd:cd04178  161 KHVKLLDSPGV 171
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
123-186 7.74e-16

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 71.88  E-value: 7.74e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 892236348  123 RTMIIGIPNAGKSTLMNRLAGKKiAVVGNKPGVTKGQQ---WLKTNKDLEILDTPGILWPKFEDETV 186
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK-AIVSDYPGTTRDPNegrLELKGKQIILVDTPGLIEGASEGEGL 66
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
126-177 8.45e-14

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: 67.66  E-value: 8.45e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 892236348 126 IIGIPNAGKSTLMNRLAGKKIAVVGNKPGVTKGQQ----WLKTNKDLEILDTPGIL 177
Cdd:cd00880    2 IFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVrkewELLPLGPVVLIDTPGLD 57
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
126-176 1.13e-12

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: 64.38  E-value: 1.13e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 892236348 126 IIGIPNAGKSTLMNRLAGKKIAVVGNKPGVT----KGQ-QWLktNKDLEILDTPGI 176
Cdd:cd01894    2 IVGRPNVGKSTLFNRLTGRRDAIVSDTPGVTrdrkYGEaEWG--GREFILIDTGGI 55
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
126-209 1.07e-11

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 64.66  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348 126 IIGIPNAGKSTLMNRLAGKKIAVVGNKPGVT----KGQ-QWLktNKDLEILDTPGIlWPKFEDEtvalklaLTGAIKDQ- 199
Cdd:COG1160    7 IVGRPNVGKSTLFNRLTGRRDAIVDDTPGVTrdriYGEaEWG--GREFTLIDTGGI-EPDDDDG-------LEAEIREQa 76
                         90
                 ....*....|..
gi 892236348 200 LLPMDE--VTIF 209
Cdd:COG1160   77 ELAIEEadVILF 88
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
126-209 1.28e-11

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 64.30  E-value: 1.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348 126 IIGIPNAGKSTLMNRLAGKKIAVVGNKPGVT----KGQ-QWLktNKDLEILDTPGIlwpKFEDETvalklaLTGAIKDQ- 199
Cdd:PRK00093   6 IVGRPNVGKSTLFNRLTGKRDAIVADTPGVTrdriYGEaEWL--GREFILIDTGGI---EPDDDG------FEKQIREQa 74
                         90
                 ....*....|..
gi 892236348 200 LLPMDE--VTIF 209
Cdd:PRK00093  75 ELAIEEadVILF 86
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
55-176 2.17e-11

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: 62.03  E-value: 2.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  55 LLILNKADLADPAMTKEWRQYFESQGIQTLAINSKEQVTVkvvtDAAKKLMADKIarqkergiqietlrTMIIGIPNAGK 134
Cdd:cd01854   37 VIVLNKADLVDDEELEELLEIYEKLGYPVLAVSAKTGEGL----DELRELLKGKT--------------SVLVGQSGVGK 98
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 892236348 135 STLMNRLAGKKIAVVG---NKPGvtKGQ------QWLKTNKDLEILDTPGI 176
Cdd:cd01854   99 STLLNALLPELVLATGeisEKLG--RGRhttthrELFPLPGGGLIIDTPGF 147
NGP_1 cd01858
A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; ...
26-176 7.33e-11

A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; Autoantigen NGP-1 (Nucleolar G-protein gene 1) has been shown to localize in the nucleolus and nucleolar organizers in all cell types analyzed, which is indicative of a function in ribosomal assembly. NGP-1 and its homologs show a circular permutation of the GTPase signature motifs so that the C-terminal strands 5, 6, and 7 (strand 6 contains the G4 box with NKXD motif) are relocated to the N terminus.


Pssm-ID: 206751 [Multi-domain]  Cd Length: 157  Bit Score: 59.23  E-value: 7.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  26 DFVTILVDARLPLSSQNPMLTK-IVGDKPK---LLILNKADLADPAMTKEWRQYFeSQGIQTLAINSKeqvtvkvVTDAA 101
Cdd:cd01858   10 DVIIQVLDARDPMGTRCKHVEKyLRKEKPHkhlIFVLNKCDLVPTWVTKRWVKVL-SKEYPTLAFHAS-------ITNPF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348 102 KKLMADKIARQ-----KERgiqiETLRTMIIGIPNAGKSTLMNRLAGKKIAVVGNKPGVTKGQQWLKTNKDLEILDTPGI 176
Cdd:cd01858   82 GKGALINLLRQfaklhSDK----KQISVGFIGYPNVGKSSVINTLRSKKVCKVAPIPGETKVWQYITLMKRIYLIDCPGV 157
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
126-187 1.10e-10

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: 59.01  E-value: 1.10e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 892236348 126 IIGIPNAGKSTLMNRLAGKKiAVVGNKPGVT---KGQQWLKTNKDLEILDTPGI--LWPKFEDETVA 187
Cdd:cd01879    2 LVGNPNVGKTTLFNALTGAR-QKVGNWPGVTvekKEGEFKLGGKEIEIVDLPGTysLTPYSEDEKVA 67
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
126-180 1.38e-10

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: 58.63  E-value: 1.38e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 892236348 126 IIGIPNAGKSTLMNRLAGKKIAVVGNKPGVT----KGqqwLKTNKDLEI--LDTPGILWPK 180
Cdd:cd04163    8 IIGRPNVGKSTLLNALVGQKISIVSPKPQTTrnriRG---IYTDDDAQIifVDTPGIHKPK 65
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
126-180 1.69e-10

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 60.39  E-value: 1.69e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 892236348 126 IIGIPNAGKSTLMNRLAGKKIAVVGNKPGVT----KGqqwLKTNKDLEI--LDTPGILWPK 180
Cdd:COG1159    8 IVGRPNVGKSTLLNALVGQKVSIVSPKPQTTrhriRG---IVTREDAQIvfVDTPGIHKPK 65
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
126-176 2.87e-10

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: 57.85  E-value: 2.87e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 892236348 126 IIGIPNAGKSTLMNRLAGKKIAVVGNKPGVTKGQ-----QWLKTNKDLEILDTPGI 176
Cdd:cd00882    2 VVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPdvyvkELDKGKVKLVLVDTPGL 57
era PRK00089
GTPase Era; Reviewed
126-180 7.89e-10

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 58.14  E-value: 7.89e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 892236348 126 IIGIPNAGKSTLMNRLAGKKIAVVGNKPGVT----KGqqwLKTNKDLEI--LDTPGILWPK 180
Cdd:PRK00089  10 IVGRPNVGKSTLLNALVGQKISIVSPKPQTTrhriRG---IVTEDDAQIifVDTPGIHKPK 67
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
40-176 1.10e-09

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: 56.50  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  40 SQNPMLTKIVGDKPKLLILNKADL----ADPAMTKEW-RQYFESQGIQTLAInskeqvtvkVVTDAAK-----KLMaDKI 109
Cdd:cd01855   49 SLIPGLAELIGAKPVILVGNKIDLlpkdVKPNRLKQWvKKRLKIGGLKIKDV---------ILVSAKKgwgveELI-EEI 118
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 892236348 110 ARQKERGIQIetlrtMIIGIPNAGKSTLMNRLAGKKIAVVGNK-----------PGVTKGQQWLKTNKDLEILDTPGI 176
Cdd:cd01855  119 KKLAKYRGDV-----YVVGATNVGKSTLINALLKSNGGKVQAQalvqrltvspiPGTTLGLIKIPLGEGKKLYDTPGI 191
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
126-187 1.22e-09

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 58.59  E-value: 1.22e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 892236348 126 IIGIPNAGKSTLMNRLAGKKiAVVGNKPGVT---KGQQWLKTNKDLEILDTPGI--LWPKFEDETVA 187
Cdd:COG0370    8 LVGNPNVGKTTLFNALTGSR-QKVGNWPGVTvekKEGKFKLKGKEIELVDLPGTysLSAYSPDEKVA 73
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
127-187 1.49e-09

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: 55.53  E-value: 1.49e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 892236348  127 IGIPNAGKSTLMNRLAGKKiAVVGNKPGVT--KGQQWLKT-NKDLEILDTPGI--LWPKFEDETVA 187
Cdd:pfam02421   6 VGNPNVGKTTLFNALTGAN-QHVGNWPGVTveKKEGKFKYkGYEIEIVDLPGIysLSPYSEEERVA 70
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
7-176 5.29e-09

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 56.60  E-value: 5.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348   7 FPGHMskaRRQVQENLKFVDFVTILVDARLPLSSQNPMLTKIV--GDKPKLLILNKAD-LADPAMTKEwrqyFESQGIQT 83
Cdd:PRK00093  66 FEKQI---REQAELAIEEADVILFVVDGRAGLTPADEEIAKILrkSNKPVILVVNKVDgPDEEADAYE----FYSLGLGE 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  84 -LAInSKE--QVTVKVVTDAAKKLMADKIARQKERGIQIEtlrtmIIGIPNAGKSTLMNRLAGKKIAVVGNKPGVT---- 156
Cdd:PRK00093 139 pYPI-SAEhgRGIGDLLDAILEELPEEEEEDEEDEPIKIA-----IIGRPNVGKSSLINALLGEERVIVSDIAGTTrdsi 212
                        170       180
                 ....*....|....*....|....*.
gi 892236348 157 ------KGQQWlktnkdlEILDTPGI 176
Cdd:PRK00093 213 dtpferDGQKY-------TLIDTAGI 231
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
120-176 9.21e-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: 53.27  E-value: 9.21e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 892236348 120 ETLRTMIIGIPNAGKSTLMNRLAGKKIAVVGNKPGVTKgqQWLKTNKDLE-----ILDTPGI 176
Cdd:cd04164    2 EGIKVVIAGKPNVGKSSLLNALAGRDRAIVSDIAGTTR--DVIEEEIDLGgipvrLIDTAGL 61
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
120-176 2.26e-08

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: 52.43  E-value: 2.26e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 892236348 120 ETLRTMIIGIPNAGKSTLMNRLAGKKIAVVGNKPGVT----------KGQQWLktnkdleILDTPGI 176
Cdd:cd01895    1 DPIKIAIIGRPNVGKSSLLNALLGEERVIVSDIAGTTrdsidvpfeyDGQKYT-------LIDTAGI 60
YeeP COG3596
Predicted GTPase [General function prediction only];
93-176 4.06e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 53.23  E-value: 4.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  93 TVKVVTDAAKKLMADKIARQKergIQIETLRTMIIGIPNAGKSTLMNRLAGKKIAVVGNKPGVTKGQQWLK----TNKDL 168
Cdd:COG3596   14 ALKRLPQVLRELLAEALERLL---VELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRlesdGLPGL 90

                 ....*...
gi 892236348 169 EILDTPGI 176
Cdd:COG3596   91 VLLDTPGL 98
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
99-156 5.29e-08

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 53.58  E-value: 5.29e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 892236348  99 DAAKKLMADKIARQKERGIQIETLRTMIIGIPNAGKSTLMNRLAGKKIAVVGNKPGVT 156
Cdd:PRK05291 193 EELIAELEALLASARQGEILREGLKVVIAGRPNVGKSSLLNALLGEERAIVTDIAGTT 250
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
11-176 5.48e-08

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 53.49  E-value: 5.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  11 MSKARRQVQENLKFVDFVTILVDARLPLSSQNPMLTKIV--GDKPKLLILNKADlaDPAMTKEWRQYFE----------- 77
Cdd:COG1160   69 EAEIREQAELAIEEADVILFVVDGRAGLTPLDEEIAKLLrrSGKPVILVVNKVD--GPKREADAAEFYSlglgepipisa 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  78 --SQGIQTLAinskeqvtvkvvtDAAKKLMADKIARQKERGIqietLRTMIIGIPNAGKSTLMNRLAGKKIAVVGNKPGV 155
Cdd:COG1160  147 ehGRGVGDLL-------------DAVLELLPEEEEEEEEDDP----IKIAIVGRPNVGKSSLINALLGEERVIVSDIAGT 209
                        170       180       190
                 ....*....|....*....|....*....|.
gi 892236348 156 T----------KGQQWLktnkdleILDTPGI 176
Cdd:COG1160  210 TrdsidtpferDGKKYT-------LIDTAGI 233
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
99-156 7.18e-08

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: 53.14  E-value: 7.18e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 892236348  99 DAAKKLMADKIARQKERGIQIETLRTMIIGIPNAGKSTLMNRLAGKKIAVVGNKPGVT 156
Cdd:COG0486  191 EELREELEALLASARQGELLREGIKVVIVGRPNVGKSSLLNALLGEERAIVTDIAGTT 248
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
16-176 1.26e-07

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 52.49  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  16 RQVQENLKFVDFVTILVDARLPLSSQNPMLTKIV--GDKPKLLILNKADLADP-AMTKEwrqyFESQGI-QTLAINSKEQ 91
Cdd:PRK09518 346 SQAQIAVSLADAVVFVVDGQVGLTSTDERIVRMLrrAGKPVVLAVNKIDDQASeYDAAE----FWKLGLgEPYPISAMHG 421
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  92 VTVKVVTDAAKKLMADKiarQKERGIQIET--LRTMIIGIPNAGKSTLMNRLAGKKIAVVGNKPGVTK----------GQ 159
Cdd:PRK09518 422 RGVGDLLDEALDSLKVA---EKTSGFLTPSglRRVALVGRPNVGKSSLLNQLTHEERAVVNDLAGTTRdpvdeiveidGE 498
                        170
                 ....*....|....*..
gi 892236348 160 QWLktnkdleILDTPGI 176
Cdd:PRK09518 499 DWL-------FIDTAGI 508
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
128-187 1.31e-07

ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane protein required for iron(II) update, is encoded in an operon with FeoA (75 amino acids), which is also required, and is regulated by Fur. There appear to be two copies in Archaeoglobus fulgidus and Clostridium acetobutylicum. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273077 [Multi-domain]  Cd Length: 591  Bit Score: 52.44  E-value: 1.31e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 892236348  128 GIPNAGKSTLMNRLAGKKiAVVGNKPGVT--KGQQWLKTN-KDLEILDTPGI--LWPKFEDETVA 187
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGAN-QTVGNWPGVTveKKEGKLGFQgEDIEIVDLPGIysLTTFSLEEEVA 64
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
126-180 3.32e-07

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: 50.46  E-value: 3.32e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 892236348  126 IIGIPNAGKSTLMNRLAGKKIAVVGNKPGVTKGQ-QWLKTNKDLEI--LDTPGILWPK 180
Cdd:TIGR00436   5 ILGRPNVGKSTLLNQLHGQKISITSPKAQTTRNRiSGIHTTGASQIifIDTPGFHEKK 62
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
90-156 4.06e-07

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: 50.56  E-value: 4.06e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348   90 EQVTVKVVTDAAKKLMA--DKIARQKERGIQI-ETLRTMIIGIPNAGKSTLMNRLAGKKIAVVGNKPGVT 156
Cdd:pfam12631  60 EELTEEELLERLEELLAelEKLLATADRGRILrEGIKVVIVGKPNVGKSSLLNALLGEERAIVTDIPGTT 129
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
126-175 6.07e-07

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 50.56  E-value: 6.07e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 892236348 126 IIGIPNAGKSTLMNRLAGKKIAVVGNKPGVTKGQ-----QWLKTnkDLEILDTPG 175
Cdd:PRK09518 280 IVGRPNVGKSTLVNRILGRREAVVEDTPGVTRDRvsydaEWAGT--DFKLVDTGG 332
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
126-157 6.83e-07

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 49.97  E-value: 6.83e-07
                         10        20        30
                 ....*....|....*....|....*....|..
gi 892236348 126 IIGIPNAGKSTLMNRLAGKKIAVVGNKPGVTK 157
Cdd:PRK03003  43 VVGRPNVGKSTLVNRILGRREAVVEDVPGVTR 74
PRK00098 PRK00098
GTPase RsgA; Reviewed
55-144 5.92e-06

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 46.74  E-value: 5.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  55 LLILNKADLADpaMTKEWRQY---FESQGIQTLAINSKEQVTVkvvtDAAKKLMADKIarqkergiqietlrTMIIGIPN 131
Cdd:PRK00098 115 IIVLNKIDLLD--DLEEARELlalYRAIGYDVLELSAKEGEGL----DELKPLLAGKV--------------TVLAGQSG 174
                         90
                 ....*....|...
gi 892236348 132 AGKSTLMNRLAGK 144
Cdd:PRK00098 175 VGKSTLLNALAPD 187
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
126-176 9.50e-06

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 44.67  E-value: 9.50e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 892236348  126 IIGIPNAGKSTLMNRLAGKKIAVVGNKPGVT----------KGQQWLktnkdLEILDTPGI 176
Cdd:TIGR00231   6 IVGHPNVGKSTLLNSLLGNKGSITEYYPGTTrnyvttvieeDGKTYK-----FNLLDTAGQ 61
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
55-150 1.12e-05

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: 44.84  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348   55 LLILNKADLADPAMT-KEWRQYFESQGIQTLAINSKEQVTVkvvtDAAKKLMADKIarqkergiqietlrTMIIGIPNAG 133
Cdd:pfam03193  57 VIVLNKIDLLDEEEElEELLKIYRAIGYPVLFVSAKTGEGI----EALKELLKGKT--------------TVLAGQSGVG 118
                          90
                  ....*....|....*..
gi 892236348  134 KSTLMNRLAGKKIAVVG 150
Cdd:pfam03193 119 KSTLLNALLPELDLRTG 135
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
126-175 1.67e-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: 44.04  E-value: 1.67e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 892236348 126 IIGIPNAGKSTLMNRLAG-KKIAVVGNKPGVTKGQQWLKTNKDLEILDTPG 175
Cdd:cd01876    4 FAGRSNVGKSSLINALTNrKKLARTSKTPGRTQLINFFNVGDKFRLVDLPG 54
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
126-195 3.94e-05

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 43.43  E-value: 3.94e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 892236348 126 IIGIPNAGKSTLMNRLAGKKIAVvgNKPGVTKG-QQWLK------TNKDLEILDTPGILwpKFEDETVALKLALTGA 195
Cdd:COG1100    8 VVGTGGVGKTSLVNRLVGDIFSL--EKYLSTNGvTIDKKelkldgLDVDLVIWDTPGQD--EFRETRQFYARQLTGA 80
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
126-176 4.33e-05

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 44.71  E-value: 4.33e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 892236348 126 IIGIPNAGKSTLMNRLAGKKiAVVGNKPGVT---KGQQWLKTNKDLEILDTPGI 176
Cdd:PRK09554   8 LIGNPNSGKTTLFNQLTGAR-QRVGNWAGVTverKEGQFSTTDHQVTLVDLPGT 60
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
126-240 1.36e-04

Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; The Obg-like subfamily consists of five well-delimited, ancient subfamilies, namely Obg, DRG, YyaF/YchF, Ygr210, and NOG1. Four of these groups (Obg, DRG, YyaF/YchF, and Ygr210) are characterized by a distinct glycine-rich motif immediately following the Walker B motif (G3 box). Obg/CgtA is an essential gene that is involved in the initiation of sporulation and DNA replication in the bacteria Caulobacter and Bacillus, but its exact molecular role is unknown. Furthermore, several OBG family members possess a C-terminal RNA-binding domain, the TGS domain, which is also present in threonyl-tRNA synthetase and in bacterial guanosine polyphosphatase SpoT. Nog1 is a nucleolar protein that might function in ribosome assembly. The DRG and Nog1 subfamilies are ubiquitous in archaea and eukaryotes, the Ygr210 subfamily is present in archaea and fungi, and the Obg and YyaF/YchF subfamilies are ubiquitous in bacteria and eukaryotes. The Obg/Nog1 and DRG subfamilies appear to form one major branch of the Obg family and the Ygr210 and YchF subfamilies form another branch. No GEFs, GAPs, or GDIs for Obg have been identified.


Pssm-ID: 206668 [Multi-domain]  Cd Length: 167  Bit Score: 41.61  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348 126 IIGIPNAGKSTLMNRLAGKKIAvVGNKPGVTK----GQQWLKTNKDLEILDTPGILWPKFED----ETVALKLALTGAI- 196
Cdd:cd01881    2 LVGLPNVGKSTLLSALTSAKVE-IASYPFTTLepnvGVFEFGDGVDIQIIDLPGLLDGASEGrglgEQILAHLYRSDLIl 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 892236348 197 -------KDQLLPMDEVtifginyfkEHYPEKLAERFKQMKieEEPSVIIM 240
Cdd:cd01881   81 hvidaseDCVGDPLEDQ---------KTLNEEVSGSFLFLK--NKPEMIVA 120
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
126-176 2.32e-04

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


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 40.99  E-value: 2.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 892236348 126 IIGIPNAGKSTLMNRLAGKKIAVVGNKPgVTKGQQWLK--TNKDLEILDTPGI 176
Cdd:cd09912    5 VVGEFSAGKSTLLNALLGEEVLPTGVTP-TTAVITVLRygLLKGVVLVDTPGL 56
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
123-156 2.48e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 42.26  E-value: 2.48e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 892236348 123 RTMIIGIPNAGKSTLMNRLAGKKIAVVGNKPGVT 156
Cdd:PRK03003 213 RVALVGKPNVGKSSLLNKLAGEERSVVDDVAGTT 246
PRK04213 PRK04213
GTP-binding protein EngB;
126-175 3.22e-04

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 40.67  E-value: 3.22e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 892236348 126 IIGIPNAGKSTLMNRLAGKKIAvVGNKPGVTkgqqwLKTN----KDLEILDTPG 175
Cdd:PRK04213  14 FVGRSNVGKSTLVRELTGKKVR-VGKRPGVT-----RKPNhydwGDFILTDLPG 61
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
123-177 4.45e-04

Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in eukaryotes ranging from trypanosomes to humans. NOG1 is functionally linked to ribosome biogenesis and found in association with the nuclear pore complexes and identified in many preribosomal complexes. Thus, defects in NOG1 can lead to defects in 60S biogenesis. The S. cerevisiae NOG1 gene is essential for cell viability, and mutations in the predicted G motifs abrogate function. It is a member of the ODN family of GTP-binding proteins that also includes the bacterial Obg and DRG proteins.


Pssm-ID: 206684 [Multi-domain]  Cd Length: 167  Bit Score: 39.85  E-value: 4.45e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 892236348 123 RTMII-GIPNAGKSTLMNRLAGKKIAvVGNKPGVTKG----------QQWlktnkdlEILDTPGIL 177
Cdd:cd01897    1 RTLVIaGYPNVGKSSLVNKLTRAKPE-VAPYPFTTKSlfvghfdykyLRW-------QVIDTPGIL 58
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
131-157 8.99e-04

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 439988 [Multi-domain]  Cd Length: 194  Bit Score: 39.28  E-value: 8.99e-04
                         10        20
                 ....*....|....*....|....*...
gi 892236348 131 NAGKSTLMNRLAG-KKIAVVGNKPGVTK 157
Cdd:COG0218   33 NVGKSSLINALTNrKKLARTSKTPGKTQ 60
PRK12289 PRK12289
small ribosomal subunit biogenesis GTPase RsgA;
53-141 2.53e-03

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237040 [Multi-domain]  Cd Length: 352  Bit Score: 38.84  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 892236348  53 PKLLILNKADLADPAMTKEWRQYFESQGIQTLAINSKEQVTVKVVTDAakklMADKIarqkergiqietlrTMIIGIPNA 132
Cdd:PRK12289 122 EIVLCLNKADLVSPTEQQQWQDRLQQWGYQPLFISVETGIGLEALLEQ----LRNKI--------------TVVAGPSGV 183

                 ....*....
gi 892236348 133 GKSTLMNRL 141
Cdd:PRK12289 184 GKSSLINRL 192
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
107-143 3.35e-03

HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.


Pssm-ID: 206666 [Multi-domain]  Cd Length: 204  Bit Score: 37.82  E-value: 3.35e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 892236348 107 DKIARQKERGIQ----IETLRTMIIGIPNAGKSTLMNRLAG 143
Cdd:cd01878   23 EKVKKQRELQRArrkrSGVPTVALVGYTNAGKSTLFNALTG 63
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
114-147 3.91e-03

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


Pssm-ID: 274271 [Multi-domain]  Cd Length: 328  Bit Score: 38.17  E-value: 3.91e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 892236348  114 ERGIQIEtLRTM----IIGIPNAGKSTLMNRL-AGK-KIA 147
Cdd:TIGR02729 147 ERWLRLE-LKLLadvgLVGLPNAGKSTLISAVsAAKpKIA 185
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
13-90 5.44e-03

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: 38.12  E-value: 5.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 892236348  13 KARRQVQEnlkfVDFVTILVDARLPLSSQNPMLTKIVGDKPKLLILNKADLADpamtKEWRQYFESQGIQTLAINSKE 90
Cdd:COG0486  285 RAREAIEE----ADLVLLLLDASEPLTEEDEEILEKLKDKPVIVVLNKIDLPS----EADGELKSLPGEPVIAISAKT 354
obgE PRK12299
GTPase CgtA; Reviewed
126-147 7.12e-03

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 37.36  E-value: 7.12e-03
                         10        20
                 ....*....|....*....|....
gi 892236348 126 IIGIPNAGKSTLMNRL-AGK-KIA 147
Cdd:PRK12299 163 LVGLPNAGKSTLISAVsAAKpKIA 186
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
126-147 7.66e-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: 36.25  E-value: 7.66e-03
                         10        20
                 ....*....|....*....|....
gi 892236348 126 IIGIPNAGKSTLMNRL--AGKKIA 147
Cdd:cd01898    5 LVGLPNAGKSTLLSAIsnAKPKIA 28
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
11-67 9.27e-03

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 35.93  E-value: 9.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 892236348  11 MSKARRQVQEnlkfVDFVTILVDARLPLSSQNPMLTKIVGDKPKLLILNKADLADPA 67
Cdd:cd04164   73 IERAREAIEE----ADLVLLVVDASEGLDEEDLEILELPAKKPVIVVLNKSDLLSDA 125
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
131-148 9.53e-03

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 36.99  E-value: 9.53e-03
                         10
                 ....*....|....*...
gi 892236348 131 NAGKSTLMNRLAGKKIAV 148
Cdd:COG2262  209 NAGKSTLFNRLTGADVLA 226
 
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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