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Conserved domains on  [gi|973165464|gb|KUL05237|]
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Small GTP-binding protein [Methanomicrobiales archaeon 53_19]

Protein Classification

OBG GTPase family GTP-binding protein( domain architecture ID 11439361)

OBG GTPase family GTP-binding protein may function as a GTPase, such as Saccharomyces cerevisiae RBG1, which is involved in ribosomal function, and developmentally regulated GTP-binding proteins, which may regulate fundamental cellular processes, perhaps by binding to RNA

EC:  3.6.5.-
Gene Ontology:  GO:0005525|GO:0003924
PubMed:  15827604|11916378

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
1-369 0e+00

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


:

Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 617.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464   1 MNSLEEQIREIEDELRNTKYNKATSLHIGRLKAKIAKLKDEAVSRAMKSSGTGEGYSVKKSGDGTVVLVGFPSVGKSTLL 80
Cdd:COG1163    1 AMTIEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  81 NQLTGTKSETAAYAFTTLTVVPGLMEHRGAKIQILDIPGLIAGAAMGKGRGKEVIAVVRTADLIIILGDVFNDRHIDVLV 160
Cdd:COG1163   81 NKLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELEQYDVLK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 161 KELYDAGIRINTPKPDITIKKSGMGGVRLNTVGSVDLNLEEIRTILSENKIMNAEVLIRGNVTQEDFIDAMIGNRRYTPA 240
Cdd:COG1163  161 EELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLDLDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRVYKPA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 241 FIAINKVDLVDDQSKKEIVKRLTKqfGQAPIMISAHSGYNINALKDAIYEHLGFIQIFMKPLGEPADMEEPLIVREGSTV 320
Cdd:COG1163  241 IVVVNKIDLADEEYVEELKSKLPD--GVPVIFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKGSTV 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 973165464 321 EDVCNRLHRDFVERFRYAKVWGNSVKHDAQRVSLPHVLADGDILTIVTK 369
Cdd:COG1163  319 GDVCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIK 367
 
Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
1-369 0e+00

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 617.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464   1 MNSLEEQIREIEDELRNTKYNKATSLHIGRLKAKIAKLKDEAVSRAMKSSGTGEGYSVKKSGDGTVVLVGFPSVGKSTLL 80
Cdd:COG1163    1 AMTIEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  81 NQLTGTKSETAAYAFTTLTVVPGLMEHRGAKIQILDIPGLIAGAAMGKGRGKEVIAVVRTADLIIILGDVFNDRHIDVLV 160
Cdd:COG1163   81 NKLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELEQYDVLK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 161 KELYDAGIRINTPKPDITIKKSGMGGVRLNTVGSVDLNLEEIRTILSENKIMNAEVLIRGNVTQEDFIDAMIGNRRYTPA 240
Cdd:COG1163  161 EELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLDLDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRVYKPA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 241 FIAINKVDLVDDQSKKEIVKRLTKqfGQAPIMISAHSGYNINALKDAIYEHLGFIQIFMKPLGEPADMEEPLIVREGSTV 320
Cdd:COG1163  241 IVVVNKIDLADEEYVEELKSKLPD--GVPVIFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKGSTV 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 973165464 321 EDVCNRLHRDFVERFRYAKVWGNSVKHDAQRVSLPHVLADGDILTIVTK 369
Cdd:COG1163  319 GDVCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIK 367
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
65-300 7.86e-106

Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding protein (DRG) subfamily is an uncharacterized member of the Obg family, an evolutionary branch of GTPase superfamily proteins. GTPases act as molecular switches regulating diverse cellular processes. DRG2 and DRG1 comprise the DRG subfamily in eukaryotes. In view of their widespread expression in various tissues and high conservation among distantly related species in eukaryotes and archaea, DRG proteins may regulate fundamental cellular processes. It is proposed that the DRG subfamily proteins play their physiological roles through RNA binding.


Pssm-ID: 206683 [Multi-domain]  Cd Length: 233  Bit Score: 310.25  E-value: 7.86e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  65 TVVLVGFPSVGKSTLLNQLTGTKSETAAYAFTTLTVVPGLMEHRGAKIQILDIPGLIAGAAMGKGRGKEVIAVVRTADLI 144
Cdd:cd01896    2 RVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADLI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 145 IILGDVFNDR-HIDVLVKELYDAGIRINTPKPDITIKKSGMGGVRLN-TVGSVDLNLEEIRTILSENKIMNAEVLIRGNV 222
Cdd:cd01896   82 LIVLDATKPEgQREILERELEGVGIRLNKKPPNVTIKKKKKGGINITsTVPLTKLDEKTVKAILREYKIHNADVLIREDI 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 973165464 223 TQEDFIDAMIGNRRYTPAFIAINKVDLVDdqskKEIVKRLTKQFGQAPimISAHSGYNINALKDAIYEHLGFIQIFMK 300
Cdd:cd01896  162 TVDDLIDVIEGNRVYIPCLYVYNKIDLIS----IEELDRLARIPNSVV--ISAEKDLNLDELLERIWDYLGLIRIYTK 233
MMR_HSR1_Xtn pfam16897
C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of ...
185-294 2.61e-35

C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of the MMR_HSR1 family.


Pssm-ID: 465301 [Multi-domain]  Cd Length: 105  Bit Score: 124.85  E-value: 2.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  185 GGVRLN-TVGSVDLNLEEIRTILSENKIMNAEVLIRGNVTQEDFIDAMIGNRRYTPAFIAINKVDLVDDqskkEIVKRLT 263
Cdd:pfam16897   1 GGINITsTVPLTKLDEETIKAILREYKIHNADVLIREDVTVDDLIDVIEGNRVYIPCLYVYNKIDLISI----EELDRLA 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 973165464  264 KQFGqaPIMISAHSGYNINALKDAIYEHLGF 294
Cdd:pfam16897  77 REPD--SVPISAEKGLNLDELKERIWEYLGL 105
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
66-292 3.38e-25

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: 104.04  E-value: 3.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464   66 VVLVGFPSVGKSTLLNQLTGTKSETAAYAFTTLTVVPGLMEHRGAK-IQILDIPGLIAGAAMGKGrgkeviavvrtadli 144
Cdd:TIGR02729 160 VGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRsFVIADIPGLIEGASEGAG--------------- 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  145 iiLGDVFNdRHID---VLVkELYDAGiRINTPKPditikksgmggvrlntvgsvdlnLEEIRTILSENKIMNAEVLIRgn 221
Cdd:TIGR02729 225 --LGHRFL-KHIErtrVLL-HLIDIS-PEDGSDP-----------------------VEDYEIIRNELKKYSPELAEK-- 274
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 973165464  222 vtqedfidamignrrytPAFIAINKVDLVDDQSKKEIVKRLTKQFGQAPIMISAHSGYNINALKDAIYEHL 292
Cdd:TIGR02729 275 -----------------PRIVVLNKIDLLDEEELEELLKELKKELGKPVFPISALTGEGLDELLDALAELL 328
obgE PRK12299
GTPase CgtA; Reviewed
68-293 3.30e-22

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 95.91  E-value: 3.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  68 LVGFPSVGKSTLLNQLTGTKSETAAYAFTTLTVVPGLMEHRGAK-IQILDIPGLIAGAAMGKGrgkeviavvrtadliii 146
Cdd:PRK12299 163 LVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKsFVIADIPGLIEGASEGAG----------------- 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 147 LGDVFNdRHID---VLVkELYDAgirintpkpditikkSGMGGVrlntvgsvdlnlEEIRTILSENKIMNAEVLIRgnvt 223
Cdd:PRK12299 226 LGHRFL-KHIErtrLLL-HLVDI---------------EAVDPV------------EDYKTIRNELEKYSPELADK---- 272
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 973165464 224 qedfidamignrrytPAFIAINKVDLVDDQSKKEIVKRLTKQFGQAPIM-ISAHSGYNINALKDAIYEHLG 293
Cdd:PRK12299 273 ---------------PRILVLNKIDLLDEEEEREKRAALELAALGGPVFlISAVTGEGLDELLRALWELLE 328
 
Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
1-369 0e+00

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 617.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464   1 MNSLEEQIREIEDELRNTKYNKATSLHIGRLKAKIAKLKDEAVSRAMKSSGTGEGYSVKKSGDGTVVLVGFPSVGKSTLL 80
Cdd:COG1163    1 AMTIEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  81 NQLTGTKSETAAYAFTTLTVVPGLMEHRGAKIQILDIPGLIAGAAMGKGRGKEVIAVVRTADLIIILGDVFNDRHIDVLV 160
Cdd:COG1163   81 NKLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELEQYDVLK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 161 KELYDAGIRINTPKPDITIKKSGMGGVRLNTVGSVDLNLEEIRTILSENKIMNAEVLIRGNVTQEDFIDAMIGNRRYTPA 240
Cdd:COG1163  161 EELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLDLDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRVYKPA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 241 FIAINKVDLVDDQSKKEIVKRLTKqfGQAPIMISAHSGYNINALKDAIYEHLGFIQIFMKPLGEPADMEEPLIVREGSTV 320
Cdd:COG1163  241 IVVVNKIDLADEEYVEELKSKLPD--GVPVIFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKGSTV 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 973165464 321 EDVCNRLHRDFVERFRYAKVWGNSVKHDAQRVSLPHVLADGDILTIVTK 369
Cdd:COG1163  319 GDVCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIK 367
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
65-300 7.86e-106

Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding protein (DRG) subfamily is an uncharacterized member of the Obg family, an evolutionary branch of GTPase superfamily proteins. GTPases act as molecular switches regulating diverse cellular processes. DRG2 and DRG1 comprise the DRG subfamily in eukaryotes. In view of their widespread expression in various tissues and high conservation among distantly related species in eukaryotes and archaea, DRG proteins may regulate fundamental cellular processes. It is proposed that the DRG subfamily proteins play their physiological roles through RNA binding.


Pssm-ID: 206683 [Multi-domain]  Cd Length: 233  Bit Score: 310.25  E-value: 7.86e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  65 TVVLVGFPSVGKSTLLNQLTGTKSETAAYAFTTLTVVPGLMEHRGAKIQILDIPGLIAGAAMGKGRGKEVIAVVRTADLI 144
Cdd:cd01896    2 RVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADLI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 145 IILGDVFNDR-HIDVLVKELYDAGIRINTPKPDITIKKSGMGGVRLN-TVGSVDLNLEEIRTILSENKIMNAEVLIRGNV 222
Cdd:cd01896   82 LIVLDATKPEgQREILERELEGVGIRLNKKPPNVTIKKKKKGGINITsTVPLTKLDEKTVKAILREYKIHNADVLIREDI 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 973165464 223 TQEDFIDAMIGNRRYTPAFIAINKVDLVDdqskKEIVKRLTKQFGQAPimISAHSGYNINALKDAIYEHLGFIQIFMK 300
Cdd:cd01896  162 TVDDLIDVIEGNRVYIPCLYVYNKIDLIS----IEELDRLARIPNSVV--ISAEKDLNLDELLERIWDYLGLIRIYTK 233
TGS_DRG cd01666
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein ...
292-368 3.49e-38

TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein (DRG) family; DRG-1 and DRG-2 comprise a highly conserved DRG subfamily of GTP-binding proteins found in archaea, plants, fungi and animals. The exact function of DRG proteins is unknown, although phylogenetic and biochemical fraction studies have linked them to translation, differentiation and growth. Their abnormal expressions may trigger cell transformation or cell cycle arrest. DRG-1 and DRG-2 bind to DFRP1 (DRG family regulatory protein 1) and DFRP2, respectively. Both DRG-1 and DRG-2 contain a domain of characteristic Obg-type G-motifs that may be the core of GTPase activity, as well as the C-terminal TGS (ThrRS, GTPase and SpoT) domain, which has a predominantly beta-grasp ubiquitin-like fold and may be related to RNA binding. DRG subfamily belongs to the Obg family of GTPases.


Pssm-ID: 340457 [Multi-domain]  Cd Length: 77  Bit Score: 131.59  E-value: 3.49e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973165464 292 LGFIQIFMKPLGEPADMEEPLIVREGSTVEDVCNRLHRDFVERFRYAKVWGNSVKHDAQRVSLPHVLADGDILTIVT 368
Cdd:cd01666    1 LGIIRVYTKPPGKKPDFDEPFILRRGSTVEDVAEKIHKDLAENFKYARVWGKSVKFDGQRVGLDHVLEDGDIVEIHK 77
MMR_HSR1_Xtn pfam16897
C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of ...
185-294 2.61e-35

C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of the MMR_HSR1 family.


Pssm-ID: 465301 [Multi-domain]  Cd Length: 105  Bit Score: 124.85  E-value: 2.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  185 GGVRLN-TVGSVDLNLEEIRTILSENKIMNAEVLIRGNVTQEDFIDAMIGNRRYTPAFIAINKVDLVDDqskkEIVKRLT 263
Cdd:pfam16897   1 GGINITsTVPLTKLDEETIKAILREYKIHNADVLIREDVTVDDLIDVIEGNRVYIPCLYVYNKIDLISI----EELDRLA 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 973165464  264 KQFGqaPIMISAHSGYNINALKDAIYEHLGF 294
Cdd:pfam16897  77 REPD--SVPISAEKGLNLDELKERIWEYLGL 105
TGS_DRG2 cd17231
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 2 ...
291-369 1.85e-28

TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 2 (DRG-2); DRG-2 is a member of the DRG family GTP-binding proteins. It has been implicated in cell growth, differentiation and death. DRG-2 plays a critical role in control of the cell cycle and apoptosis in Jurkat T cells. It regulates G2/M progression via the cyclin B1-Cdk1 complex. Moreover, DRG-2 is an endosomal protein and a key regulator of the small GTPase Rab5 deactivation and transferrin recycling. It enhances experimental autoimmune encephalomyelitis (EAE) by suppressing the development of TH17 cells. It is also associated with survival and cytoskeleton organization of osteoclasts under influence of macrophage colony-stimulating factor, and its overexpression leads to elevated bone resorptive activity of osteoclasts, resulting in bone loss. DRG-2 contains a domain of characteristic Obg-type G-motifs that may be the core of GTPase activity, as well as this C-terminal TGS (ThrRS, GTPase and SpoT) domain that has a predominantly beta-grasp ubiquitin-like fold and may be involved in RNA binding.


Pssm-ID: 340751 [Multi-domain]  Cd Length: 79  Bit Score: 105.93  E-value: 1.85e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 973165464 291 HLGFIQIFMKPLGEPADMEEPLIVREGSTVEDVCNRLHRDFVERFRYAKVWGNSVKHDAQRVSLPHVLADGDILTIVTK 369
Cdd:cd17231    1 YLALIRVYTKKRGERPDFGDAIILRRGATVEHVCHRIHRTLASQFKYALVWGTSTKYSPQRVGLTHVMEDEDVIQIVKK 79
TGS_DRG1 cd17230
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 1 ...
291-369 3.92e-28

TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 1 (DRG-1); DRG-1 is a potassium-dependent GTPase that belongs to the DRG family GTP-binding proteins. It plays an important role in regulating cell growth. It functions as a potential oncogene in lung adenocarcinoma and promotes tumor progression via spindle checkpoint signaling regulation. It also plays an important role in melanoma cell growth and transformation, indicating a novel role in CD4(+) T cell-mediated immunotherapy in melanoma. In addition, DRG-1 is regulated by ZC3H15 (zinc finger CCCH-type containing 15, also known as Lerepo4), and displays a high temperature optimum of activity at 42C, suggesting the ability of being active under possible heat stress conditions. DRG-1 contains a domain of characteristic Obg-type G-motifs that may be the core of GTPase activity, as well as this C-terminal TGS (ThrRS, GTPase and SpoT) domain that has a predominantly beta-grasp ubiquitin-like fold and may be related to RNA binding.


Pssm-ID: 340750 [Multi-domain]  Cd Length: 80  Bit Score: 105.05  E-value: 3.92e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 291 HLGFIQIFMKPLGEPADMEEPLIVREG-STVEDVCNRLHRDFVERFRYAKVWGNSVKHDAQRVSLPHVLADGDILTIVTK 369
Cdd:cd17230    1 YLNLVRIYTKPKGQLPDYEEPVVLRSGkSTVEDFCNKIHKSLIKEFKYALVWGSSVKHNPQRVGKDHVLEDEDVVQIVKK 80
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
65-173 4.92e-26

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: 100.77  E-value: 4.92e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464   65 TVVLVGFPSVGKSTLLNQLTGTKSETAAYAFTTLTVVPGLMEHRGAKIQILDIPGLIAGAAMGKGRGKEVIAVVRtADLI 144
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFLAIIE-ADLI 79
                          90       100
                  ....*....|....*....|....*....
gi 973165464  145 IILGDVfnDRHIDVLVKELYDAGIRINTP 173
Cdd:pfam01926  80 LFVVDS--EEGITPLDEELLELLRENKKP 106
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
66-292 3.38e-25

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: 104.04  E-value: 3.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464   66 VVLVGFPSVGKSTLLNQLTGTKSETAAYAFTTLTVVPGLMEHRGAK-IQILDIPGLIAGAAMGKGrgkeviavvrtadli 144
Cdd:TIGR02729 160 VGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRsFVIADIPGLIEGASEGAG--------------- 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  145 iiLGDVFNdRHID---VLVkELYDAGiRINTPKPditikksgmggvrlntvgsvdlnLEEIRTILSENKIMNAEVLIRgn 221
Cdd:TIGR02729 225 --LGHRFL-KHIErtrVLL-HLIDIS-PEDGSDP-----------------------VEDYEIIRNELKKYSPELAEK-- 274
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 973165464  222 vtqedfidamignrrytPAFIAINKVDLVDDQSKKEIVKRLTKQFGQAPIMISAHSGYNINALKDAIYEHL 292
Cdd:TIGR02729 275 -----------------PRIVVLNKIDLLDEEELEELLKELKKELGKPVFPISALTGEGLDELLDALAELL 328
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
68-292 2.03e-24

GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, chromosome partitioning, Replication, recombination, and repair];


Pssm-ID: 440302 [Multi-domain]  Cd Length: 343  Bit Score: 102.37  E-value: 2.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  68 LVGFPSVGKSTLLNQLTGTKSETAAYAFTTLTVVPGLMEHRGAK-IQILDIPGLIAGAAMGKGrgkeviavvrtadliii 146
Cdd:COG0536  162 LVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGRsFVIADIPGLIEGASEGAG----------------- 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 147 LGDVFNdRHID---VLVkELYD-AGIRINTPkpditikksgmggvrlntvgsvdlnLEEIRTILSENKIMNAEVLIRgnv 222
Cdd:COG0536  225 LGHRFL-RHIErtrVLL-HVVDaAPLDGRDP-------------------------VEDYEIIRNELEAYSPELAEK--- 274
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 223 tqedfidamignrrytPAFIAINKVDLVDDQSKKEIVKRLtKQFGQAPIMISAHSGYNINALKDAIYEHL 292
Cdd:COG0536  275 ----------------PRIVVLNKIDLLDAEELEELKAEL-EKLGGPVFPISAVTGEGLDELLYALAELL 327
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
67-292 3.60e-24

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: 97.46  E-value: 3.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  67 VLVGFPSVGKSTLLNQLTGTKSETAAYAFTTLTVVPGLMEH-RGAKIQILDIPGLIAGAAMGKGRGKEVIAVVRTADLII 145
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFgDGVDIQIIDLPGLLDGASEGRGLGEQILAHLYRSDLIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 146 ILGDVFNDRHIDvlvkelydagirintpkpditikksgmggvrlntvgsvdlnleeirtILSENKIMNAEVLIRgnvtqe 225
Cdd:cd01881   81 HVIDASEDCVGD-----------------------------------------------PLEDQKTLNEEVSGS------ 107
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 973165464 226 dfidamIGNRRYTPAFIAINKVDLVDDQSKKEIVKrLTKQFGQAPIMISAHSGYNINALKDAIYEHL 292
Cdd:cd01881  108 ------FLFLKNKPEMIVANKIDMASENNLKRLKL-DKLKRGIPVVPTSALTRLGLDRVIRTIRKLL 167
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
68-292 4.33e-23

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: 94.41  E-value: 4.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  68 LVGFPSVGKSTLLNQLTGTKSETAAYAFTTLT----VVPGLMEHRgakIQILDIPGLIAGAAMGKGrgkeviavvrtadl 143
Cdd:cd01898    5 LVGLPNAGKSTLLSAISNAKPKIADYPFTTLVpnlgVVRVDDGRS---FVIADIPGLIEGASEGKG-------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 144 iiiLGDVFNdRHI---DVLVkELYDAgirinTPKPDItikksgmggvrlntvgsvdlnLEEIRTILSENKIMNAEVLIRg 220
Cdd:cd01898   68 ---LGHRFL-RHIertRVLL-HVIDL-----SGEDDP---------------------VEDYETIRNELEAYNPGLAEK- 115
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973165464 221 nvtqedfidamignrrytPAFIAINKVDLVDDQSKKEIVKRLTKQF-GQAPIMISAHSGYNINALKDAIYEHL 292
Cdd:cd01898  116 ------------------PRIVVLNKIDLLDAEERFEKLKELLKELkGKKVFPISALTGEGLDELLKKLAKLL 170
obgE PRK12299
GTPase CgtA; Reviewed
68-293 3.30e-22

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 95.91  E-value: 3.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  68 LVGFPSVGKSTLLNQLTGTKSETAAYAFTTLTVVPGLMEHRGAK-IQILDIPGLIAGAAMGKGrgkeviavvrtadliii 146
Cdd:PRK12299 163 LVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKsFVIADIPGLIEGASEGAG----------------- 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 147 LGDVFNdRHID---VLVkELYDAgirintpkpditikkSGMGGVrlntvgsvdlnlEEIRTILSENKIMNAEVLIRgnvt 223
Cdd:PRK12299 226 LGHRFL-KHIErtrLLL-HLVDI---------------EAVDPV------------EDYKTIRNELEKYSPELADK---- 272
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 973165464 224 qedfidamignrrytPAFIAINKVDLVDDQSKKEIVKRLTKQFGQAPIM-ISAHSGYNINALKDAIYEHLG 293
Cdd:PRK12299 273 ---------------PRILVLNKIDLLDEEEEREKRAALELAALGGPVFlISAVTGEGLDELLRALWELLE 328
obgE PRK12297
GTPase CgtA; Reviewed
66-316 2.39e-21

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 94.40  E-value: 2.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  66 VVLVGFPSVGKSTLLNQLTGTKSETAAYAFTTLTVVPGLMEHRGAK-IQILDIPGLIAGAAMGKGrgkeviavvrtadli 144
Cdd:PRK12297 161 VGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRsFVMADIPGLIEGASEGVG--------------- 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 145 iiLGDVFNdRHID---VLVkELYDAgirintpkpditikkSGMGGvrlntvgsvDLNLEEIRTILSENKIMNAEVLIRgn 221
Cdd:PRK12297 226 --LGHQFL-RHIErtrVIV-HVIDM---------------SGSEG---------RDPIEDYEKINKELKLYNPRLLER-- 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 222 vtqedfidamignrrytPAFIAINKVDLVDDQskkEIVKRLTKQFGQAPIMISAHSGYNINALKDAIYEHLGFIQIFmkP 301
Cdd:PRK12297 276 -----------------PQIVVANKMDLPEAE---ENLEEFKEKLGPKVFPISALTGQGLDELLYAVAELLEETPEF--P 333
                        250
                 ....*....|....*
gi 973165464 302 LGEPADMEEPLIVRE 316
Cdd:PRK12297 334 LEEEEVEEEVYYKFE 348
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
67-292 3.59e-17

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: 78.06  E-value: 3.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  67 VLVGFPSVGKSTLLNQLTGTK-SETAAYAFTTLTVVPGLMEHRGA-KIQILDIPGLIAGAAMGKGRGKEVIAVVRTADLI 144
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNvGIVSPIPGTTRDPVRKEWELLPLgPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 145 IIlgdvfndrhidvlvkelydagirintpkpditikksgmggvrlntVGSVDLNLEEirtilSENKIMNAEvlirgnvtq 224
Cdd:cd00880   81 LL---------------------------------------------VVDSDLTPVE-----EEAKLGLLR--------- 101
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 225 edfidamignRRYTPAFIAINKVDLVDDQSKKEIVKRLTKQF--GQAPIMISAHSGYNINALKDAIYEHL 292
Cdd:cd00880  102 ----------ERGKPVLLVLNKIDLVPESEEEELLRERKLELlpDLPVIAVSALPGEGIDELRKKIAELL 161
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
63-177 4.96e-17

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: 77.41  E-value: 4.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464   63 DGTVVLVGFPSVGKSTLLNQLTGTK-SETAAYAFTTLTVVPGLMEHRG--AKIQILDIPGLIAGAAMGKGRGKEVIAVVR 139
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKgSITEYYPGTTRNYVTTVIEEDGktYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 973165464  140 TADLIIILGDVFN--DRHIDVLVKEL-YDAGIRINTPKPDI 177
Cdd:TIGR00231  81 VFDIVILVLDVEEilEKQTKEIIHHAdSGVPIILVGNKIDL 121
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
65-293 3.43e-16

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 78.34  E-value: 3.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  65 TVVLVGFPSVGKSTLLNQLTGTKSETAAYAFTTLTVVPGLMEHRGAKIQILDIPGLI-------------Agaamgkgrg 131
Cdd:COG1084  162 TIVVAGYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGRYQVIDTPGLLdrplserneierqA--------- 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 132 keVIAVVRTADLIIILGDvfndrhidvlvkelydagirintpkPDITikkSGMggvrlntvgSVD--LNL-EEIRTILSe 208
Cdd:COG1084  233 --ILALKHLADVILFLFD-------------------------PSET---CGY---------SLEeqLNLlEEIRSLFD- 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 209 nkimnaevlirgnvtqedfidamignrryTPAFIAINKVDLVDDQSKKEIVKRltkqfgqAPIMISAHSGYNINALKDAI 288
Cdd:COG1084  273 -----------------------------VPVIVVINKIDLSDEEELKEAEEE-------ADIKISALTGEGVDELLDEL 316

                 ....*
gi 973165464 289 YEHLG 293
Cdd:COG1084  317 IEALE 321
TGS pfam02824
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ...
314-368 1.85e-15

TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain was detected also at the amino terminus of the uridine kinase from the spirochaete Treponema pallidum (but not any other organizm, including the related spirochaete Borrelia burgdorferi). TGS is a small domain that consists of ~50 amino acid residues and is predicted to possess a predominantly beta-sheet structure. There is no direct information on the functions of the TGS domain, but its presence in two types of regulatory proteins (the GTPases and guanosine polyphosphate phosphohydrolases/synthetases) suggests a ligand (most likely nucleotide)-binding, regulatory role.


Pssm-ID: 427005 [Multi-domain]  Cd Length: 60  Bit Score: 69.88  E-value: 1.85e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 973165464  314 VREGSTVEDVCNRLHRDFVERFRYAKVWGnsvkhdaQRVSLPHVLADGDILTIVT 368
Cdd:pfam02824  13 LPRGATPEDFAYAIHTSLAKKFIYAKVNG-------QLVGLDHPLEDGDVVEIVT 60
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
65-120 8.97e-15

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: 71.44  E-value: 8.97e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 973165464  65 TVVLVGFPSVGKSTLLNQLTGTKSETAAYAFTTLTVVPGLMEHRGAKIQILDIPGL 120
Cdd:cd01897    2 TLVIAGYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLRWQVIDTPGI 57
obgE PRK12298
GTPase CgtA; Reviewed
66-292 3.40e-13

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 70.28  E-value: 3.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  66 VVLVGFPSVGKSTLLNQLTGTKSETAAYAFTTLtvVPGL---MEHRGAKIQILDIPGLIAGAAMGKGrgkeviavvrtad 142
Cdd:PRK12298 162 VGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTL--VPNLgvvRVDDERSFVVADIPGLIEGASEGAG------------- 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 143 liiiLGDVFNdRHID---VLvkelydagirintpkpditikksgmggvrlntvgsvdLNLEEIRTILSENKIMNAEVLIR 219
Cdd:PRK12298 227 ----LGIRFL-KHLErcrVL-------------------------------------LHLIDIAPIDGSDPVENARIIIN 264
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973165464 220 gnvTQEDFIDAMIGNRRYtpafIAINKVDLVDDQSKKEIVKRLTKQFG-QAPIM-ISAHSGYNINALKDAIYEHL 292
Cdd:PRK12298 265 ---ELEKYSPKLAEKPRW----LVFNKIDLLDEEEAEERAKAIVEALGwEGPVYlISAASGLGVKELCWDLMTFI 332
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
64-316 1.52e-11

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 64.24  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  64 GTVVLVGFPSVGKSTLLNQLTGTK-SETAAYAFTTLTVVPGLMEHRGAKIQILDIPGLIAGA-AMGKGRGKEVIAVVRTA 141
Cdd:COG1159    4 GFVAIVGRPNVGKSTLLNALVGQKvSIVSPKPQTTRHRIRGIVTREDAQIVFVDTPGIHKPKrKLGRRMNKAAWSALEDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 142 DLIIILGDVfnDRHIDvlvkelydagirintpkpditikksgmggvrlntvgsvdlnlEEIRTILseNKIMNAEvlirgn 221
Cdd:COG1159   84 DVILFVVDA--TEKIG------------------------------------------EGDEFIL--ELLKKLK------ 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 222 vtqedfidamignrryTPAFIAINKVDLVDDQSKKEIVKRLTKQFGQAPI-MISAHSGYNINALKDAIYEHLgfiqifmk 300
Cdd:COG1159  112 ----------------TPVILVINKIDLVKKEELLPLLAEYSELLDFAEIvPISALKGDNVDELLDEIAKLL-------- 167
                        250       260
                 ....*....|....*....|....*..
gi 973165464 301 PLGE---PADM--EEPL------IVRE 316
Cdd:COG1159  168 PEGPpyyPEDQitDRPErflaaeIIRE 194
era PRK00089
GTPase Era; Reviewed
64-316 2.32e-11

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 63.91  E-value: 2.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  64 GTVVLVGFPSVGKSTLLNQLTGTK-SETAAYAFTTLTVVPGLMEHRGAKIQILDIPGL-IAGAAMGKGRGKEVIAVVRTA 141
Cdd:PRK00089   6 GFVAIVGRPNVGKSTLLNALVGQKiSIVSPKPQTTRHRIRGIVTEDDAQIIFVDTPGIhKPKRALNRAMNKAAWSSLKDV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 142 DLIIILGDVfnDRHIDvlvkelydagirintpkpditikksgmggvrlntvgsvdlnlEEIRTILSENKimnaevlirgn 221
Cdd:PRK00089  86 DLVLFVVDA--DEKIG------------------------------------------PGDEFILEKLK----------- 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 222 vtqedfidamignRRYTPAFIAINKVDLVDDQSK-KEIVKRLTKQFGQAPI-MISAHSGYNINALKDAIYEHLgfiqifm 299
Cdd:PRK00089 111 -------------KVKTPVILVLNKIDLVKDKEElLPLLEELSELMDFAEIvPISALKGDNVDELLDVIAKYL------- 170
                        250       260
                 ....*....|....*....|....*...
gi 973165464 300 kPLGE---PADM--EEPL------IVRE 316
Cdd:PRK00089 171 -PEGPpyyPEDQitDRPErflaaeIIRE 197
obgE PRK12296
GTPase CgtA; Reviewed
66-290 8.54e-11

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 62.96  E-value: 8.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  66 VVLVGFPSVGKSTLLNQLTGTKSETAAYAFTTLtvVP--GLMEHRGAKIQILDIPGLIAGAAMGKGRGKEVIavvrtadl 143
Cdd:PRK12296 162 VGLVGFPSAGKSSLISALSAAKPKIADYPFTTL--VPnlGVVQAGDTRFTVADVPGLIPGASEGKGLGLDFL-------- 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 144 iiilgdvfndRHID---VLVKELyDAGirintpkpditikksgmggvrlntvgsvdlNLEEIRTILSENKIMNAEVLIRG 220
Cdd:PRK12296 232 ----------RHIErcaVLVHVV-DCA------------------------------TLEPGRDPLSDIDALEAELAAYA 270
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 221 NVTQEDFIDAMIGNRrytPAFIAINKVDLVDDQSKKEIVKRLTKQFGQAPIMISAHSGYNINALKDAIYE 290
Cdd:PRK12296 271 PALDGDLGLGDLAER---PRLVVLNKIDVPDARELAEFVRPELEARGWPVFEVSAASREGLRELSFALAE 337
PRK09602 PRK09602
translation-associated GTPase; Reviewed
65-369 1.01e-10

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 62.52  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  65 TVVLVGFPSVGKSTLLNQLTGTKSETAAYAFTTL----------------------TVVPGLMEH--RGAKIQILDIPGL 120
Cdd:PRK09602   3 TIGLVGKPNVGKSTFFNAATLADVEIANYPFTTIdpnvgvayvrvecpckelgvkcNPRNGKCIDgtRFIPVELIDVAGL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 121 IAGAAMGKGRGKEVIAVVRTADLIIILGD-----------VFNDRH-----IDVLVKELYD--AGI----------RINT 172
Cdd:PRK09602  83 VPGAHEGRGLGNQFLDDLRQADALIHVVDasgstdeegnpVEPGSHdpvedIKFLEEELDMwiYGIleknwekfsrKAQA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 173 PKPDITI----KKSGMGgVRLNTVGSV--DLNLEEIRTILSENKIMNAEVLIRgnvtqedfidamignRRYTPAFIAINK 246
Cdd:PRK09602 163 EKFDIEEalaeQLSGLG-INEEHVKEAlrELGLPEDPSKWTDEDLLELARELR---------------KISKPMVIAANK 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 247 VDLVDDQskkEIVKRLTKQFGQAPIMISAH--------------------SGYNI------------------------- 281
Cdd:PRK09602 227 ADLPPAE---ENIERLKEEKYYIVVPTSAEaelalrraakaglidyipgdSDFEIlgelsekqkkaleyirevlkkyggt 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 282 ---NALKDAIYEHLGFIQIFmkPLGEPADMEE------P--LIVREGSTVEDVCNRLHRDFVERFRYAkvwgnsvkHDA- 349
Cdd:PRK09602 304 gvqEAINTAVFDLLDMIVVY--PVEDENKLTDkkgnvlPdaFLLPKGSTARDLAYKIHTDIGEGFLYA--------IDAr 373
                        410       420
                 ....*....|....*....|..
gi 973165464 350 --QRVSLPHVLADGDILTIVTK 369
Cdd:PRK09602 374 tkRRIGEDYELKDGDVIKIVST 395
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
67-290 1.58e-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: 59.01  E-value: 1.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  67 VLVGFPSVGKSTLLNQLTGTK-SETAAYAFTTL--TVVPGLMEHRGAKIQILDIPGLIAGAAMgkGRGKEVIAVVRTADL 143
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEvGEVSDVPGTTRdpDVYVKELDKGKVKLVLVDTPGLDEFGGL--GREELARLLLRGADL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 144 IIIlgdvfndrhidvlvkeLYDAGIRIntpkpditikksgmggvrlntvgSVDLNLEEIRTILSENKImnaevlirgnvt 223
Cdd:cd00882   79 ILL----------------VVDSTDRE-----------------------SEEDAKLLILRRLRKEGI------------ 107
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 973165464 224 qedfidamignrrytPAFIAINKVDLVDDQSKKEIVKRLTKQF--GQAPIMISAHSGYNINALKDAIYE 290
Cdd:cd00882  108 ---------------PIILVGNKIDLLEEREVEELLRLEELAKilGVPVFEVSAKTGEGVDELFEKLIE 161
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
68-119 5.74e-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: 57.47  E-value: 5.74e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 973165464  68 LVGFPSVGKSTLLNQLTGTKSETAAYAFTTLTVVPGLMEHRGAKIQILDIPG 119
Cdd:cd01879    2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPG 53
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
68-260 6.10e-10

Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They are characterized by a distinct glycine-rich motif immediately following the Walker B motif. The Ygr210 and YyaF/YchF subfamilies appear to form one major branch of the Obg-like family. Among eukaryotes, the Ygr210 subfamily is represented only in fungi. These fungal proteins form a tight cluster with their archaeal orthologs, which suggests the possibility of horizontal transfer from archaea to fungi.


Pssm-ID: 206686 [Multi-domain]  Cd Length: 318  Bit Score: 59.93  E-value: 6.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  68 LVGFPSVGKSTLLNQLTGTKSETAAYAFTT------------------LTVVPGLME------HRGAKIQILDIPGLIAG 123
Cdd:cd01899    3 LVGKPNVGKSTFFNAATLADVEIANYPFTTidpnvgvgyvrvecpckeLGVSCNPRYgkcidgKRYVPVELIDVAGLVPG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 124 AAMGKGRGKEVIAVVRTADLIIILGDVFNDRHIDVLVKElydagIRINTPKPDIT---------------------IKKS 182
Cdd:cd01899   83 AHEGKGLGNQFLDDLRDADVLIHVVDASGGTDAEGNGVE-----TGGYDPLEDIEfleneidmwiygilernwekiVRKA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 183 GMGGVRLNTVgsvdlnLEEIRTILSENKIMNAEVLIRGNV-------TQEDFIDAMIGNRRYT-PAFIAINKVDLVDDQS 254
Cdd:cd01899  158 KAEKTDIVEA------LSEQLSGFGVNEDVVIEALEELELpadlskwDDEDLLRLARELRKRRkPMVIAANKADIPDAEE 231

                 ....*.
gi 973165464 255 KKEIVK 260
Cdd:cd01899  232 NISKLR 237
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
65-119 1.23e-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: 56.30  E-value: 1.23e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 973165464   65 TVVLVGFPSVGKSTLLNQLTGTKSETAAYAFTTLTVVPGLMEHRGAKIQILDIPG 119
Cdd:pfam02421   2 TIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFKYKGYEIEIVDLPG 56
PTZ00258 PTZ00258
GTP-binding protein; Provisional
68-163 1.30e-09

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 59.19  E-value: 1.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  68 LVGFPSVGKSTLLNQLTGTKSETAAYAFTT----LTVVP-------GLMEHRGAK------IQILDIPGLIAGAAMGKGR 130
Cdd:PTZ00258  26 IVGLPNVGKSTTFNALCKQQVPAENFPFCTidpnTARVNvpderfdWLCKHFKPKsivpaqLDITDIAGLVKGASEGEGL 105
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 973165464 131 GKEVIAVVRTADLIIILGDVFND-------------RHIDVLVKEL 163
Cdd:PTZ00258 106 GNAFLSHIRAVDGIYHVVRAFEDedithvegeidpvRDLEIISSEL 151
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
64-292 1.52e-09

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: 56.32  E-value: 1.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  64 GTVVLVGFPSVGKSTLLNQLTGTK-SETAAYAFTTLTVVPGLMEHRGAKIQILDIPGLIAG-AAMGKGRGKEVIAVVRTA 141
Cdd:cd04163    4 GFVAIIGRPNVGKSTLLNALVGQKiSIVSPKPQTTRNRIRGIYTDDDAQIIFVDTPGIHKPkKKLGERMVKAAWSALKDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 142 DLIIILGDVFNdrhidvlvkelydagirinTPKPDItikksgmggvrlntvgsvdlnlEEIRTILSENKimnaevlirgn 221
Cdd:cd04163   84 DLVLFVVDASE-------------------WIGEGD----------------------EFILELLKKSK----------- 111
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973165464 222 vtqedfidamignrryTPAFIAINKVDLVDDQSK-KEIVKRLTKQFGQAPI-MISAHSGYNINALKDAIYEHL 292
Cdd:cd04163  112 ----------------TPVILVLNKIDLVKDKEDlLPLLEKLKELHPFAEIfPISALKGENVDELLEYIVEYL 168
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
66-288 1.04e-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: 53.98  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  66 VVLVGFPSVGKSTLLNQLTGTK----SETAAyafTTLTVVPGLMEHRGAKIQILDIPGLiagaamgKGRGK-----EVIA 136
Cdd:cd01895    5 IAIIGRPNVGKSSLLNALLGEErvivSDIAG---TTRDSIDVPFEYDGQKYTLIDTAGI-------RKKGKvtegiEKYS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 137 VVRT------ADLIIILgdvfndrhIDVLVkelydaGIRintpkpditikksgmggvrlntvgSVDLNLeeIRTILSENK 210
Cdd:cd01895   75 VLRTlkaierADVVLLV--------LDASE------GIT------------------------EQDLRI--AGLILEEGK 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 211 imnaevlirgnvtqedfidamignrrytPAFIAINKVDLVDDQSK--KEIVKRLTKQFGQ---APIM-ISAHSGYNINAL 284
Cdd:cd01895  115 ----------------------------ALIIVVNKWDLVEKDEKtmKEFEKELRRKLPFldyAPIVfISALTGQGVDKL 166

                 ....
gi 973165464 285 KDAI 288
Cdd:cd01895  167 FDAI 170
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
65-119 6.35e-08

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 54.36  E-value: 6.35e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 973165464  65 TVVLVGFPSVGKSTLLNQLTGTKSETAAYAFTTLTVVPGLMEHRGAKIQILDIPG 119
Cdd:COG0370    5 TIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKGKEIELVDLPG 59
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
28-309 6.66e-08

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 53.94  E-value: 6.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  28 IGRLKAKIAKL-KDEAVSRAMKssgtgegysvKKSGDGTVVLVGFPSVGKSTLLNQLTGTKSETAAYAFTTL--TVvpgl 104
Cdd:COG2262  173 IARLKRELEKVrKQRELQRKRR----------KRSGIPTVALVGYTNAGKSTLFNRLTGADVLAEDKLFATLdpTT---- 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 105 mehRgakiqILDIPGliagaamgkgrGKEVI-----------------------AVVRTADLIIILGDVFNDRHIDvlvk 161
Cdd:COG2262  239 ---R-----RLELPD-----------GRPVLltdtvgfirklphqlveafrstlEEVREADLLLHVVDASDPDFEE---- 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 162 elydagirintpkpditikksgmggvRLNTVGSV--DLNLEEIRTILsenkimnaeVLirgnvtqedfidamignrrytp 239
Cdd:COG2262  296 --------------------------QIETVNEVleELGADDKPIIL---------VF---------------------- 318
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 240 afiaiNKVDLVDDQSKKEIVKRLTKqfgqaPIMISAHSGYNINALKDAIYEHLGFIQIFMKPLGEPADME 309
Cdd:COG2262  319 -----NKIDLLDDEELERLRAGYPD-----AVFISAKTGEGIDELLEAIEERLPEDRVEVELLLPYSDGD 378
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
29-316 2.37e-07

tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 52.37  E-value: 2.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  29 GRLKAKIAKLKDEaVSRAMKSSGTGEGYSvkksgDG-TVVLVGFPSVGKSTLLNQLTGtkSETA---AYAFTTLTVVPGL 104
Cdd:COG0486  184 EELLERLEELREE-LEALLASARQGELLR-----EGiKVVIVGRPNVGKSSLLNALLG--EERAivtDIAGTTRDVIEER 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 105 MEHRGAKIQILDIPGLIAGA----AMGKGRGKEVIAvvrTADLIIILGDvfndrhidvlvkelydagirintpkpditik 180
Cdd:COG0486  256 INIGGIPVRLIDTAGLRETEdeveKIGIERAREAIE---EADLVLLLLD------------------------------- 301
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 181 ksgmggvrlntvGSVDLNlEEIRTILseNKIMNAEVLirgnvtqedfidamignrrytpafIAINKVDLVDDQSKKeivk 260
Cdd:COG0486  302 ------------ASEPLT-EEDEEIL--EKLKDKPVI------------------------VVLNKIDLPSEADGE---- 338
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 973165464 261 rLTKQFGQAPIMISAHSGYNINALKDAIYEHLGFIQIfmkplgepaDMEEPLIVRE 316
Cdd:COG0486  339 -LKSLPGEPVIAISAKTGEGIDELKEAILELVGEGAL---------EGEGVLLTNA 384
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
66-290 2.67e-07

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 51.97  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  66 VVLVGFPSVGKSTLLNQLTGTK----SETAAyafTTLTVVPGLMEHRGAKIQILDIPGLiagaaMGKGRGKEVI---AVV 138
Cdd:PRK00093 176 IAIIGRPNVGKSSLINALLGEErvivSDIAG---TTRDSIDTPFERDGQKYTLIDTAGI-----RRKGKVTEGVekySVI 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 139 RT------ADLIIILgdvfndrhIDVLvkelydAGIRintpkpditikksgmggvrlntvgSVDLNLeeIRTILSENKim 212
Cdd:PRK00093 248 RTlkaierADVVLLV--------IDAT------EGIT------------------------EQDLRI--AGLALEAGR-- 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 213 naevlirgnvtqedfidAMIgnrrytpafIAINKVDLVDDQSKKEIVKRLTKQFGQ---APIM-ISAHSGYNINALKDAI 288
Cdd:PRK00093 286 -----------------ALV---------IVVNKWDLVDEKTMEEFKKELRRRLPFldyAPIVfISALTGQGVDKLLEAI 339

                 ..
gi 973165464 289 YE 290
Cdd:PRK00093 340 DE 341
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
28-292 3.10e-07

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: 50.54  E-value: 3.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  28 IGRLKAKIAKL-KDEAVSRAmkssgtgegySVKKSGDGTVVLVGFPSVGKSTLLNQLTGTKSETAAYAFTTL--TVvpgl 104
Cdd:cd01878   15 IAKLRKELEKVkKQRELQRA----------RRKRSGVPTVALVGYTNAGKSTLFNALTGADVLAEDQLFATLdpTT---- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 105 meHRgakiqiLDIPGliagaamgkgrGKEVIAV-----------------------VRTADLIIILGDVFNdrhidvlvk 161
Cdd:cd01878   81 --RR------IKLPG-----------GREVLLTdtvgfirdlphqlveafrstleeVAEADLLLHVVDASD--------- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 162 elydagirintPKPDITIKksgmggvrlnTVGSV--DLNLEEIRTIlsenkimnaevlirgnvtqedfidamignrrytp 239
Cdd:cd01878  133 -----------PDREEQIE----------TVEEVlkELGADDIPII---------------------------------- 157
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 973165464 240 afIAINKVDLVDDQskkEIVKRLTKQFGQApIMISAHSGYNINALKDAIYEHL 292
Cdd:cd01878  158 --LVLNKIDLLDDE---ELEERLRAGRPDA-VFISAKTGEGLDLLKEAIEELL 204
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
65-293 3.45e-06

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


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 46.33  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  65 TVVLVGFPSVGKSTLLNQLTGTKSetaayAFTTltvvpglmehrgakiqilDIPGliagaamgkgrgkeviavvRTADLI 144
Cdd:cd04164    5 KVVIAGKPNVGKSSLLNALAGRDR-----AIVS------------------DIAG-------------------TTRDVI 42
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 145 iilgdvfnDRHID---VLVKeLYD-AGIRintpkpditikksgmggvrlNTVGSVDLnlEEIRtiLSENKIMNAEVLI-- 218
Cdd:cd04164   43 --------EEEIDlggIPVR-LIDtAGLR--------------------ETEDEIEK--IGIE--RAREAIEEADLVLlv 89
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 973165464 219 ---RGNVTQEDF-IDAMIGNRRYTpafIAINKVDLVDDQSKKEIVKrltkqfGQAPIMISAHSGYNINALKDAIYEHLG 293
Cdd:cd04164   90 vdaSEGLDEEDLeILELPAKKPVI---VVLNKSDLLSDAEGISELN------GKPIIAISAKTGEGIDELKEALLELAG 159
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
56-121 5.96e-06

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: 45.30  E-value: 5.96e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 973165464  56 YSVKKsgDGTVVLVGFPSVGKSTLLNQLTGTK----SETAAYA--FTTLTVVPGLMehrgakiqILDIPGLI 121
Cdd:cd01857   77 FSALN--EATIGLVGYPNVGKSSLINALVGSKkvsvSSTPGKTkhFQTIFLEPGIT--------LCDCPGLV 138
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
70-119 2.05e-05

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: 46.27  E-value: 2.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 973165464   70 GFPSVGKSTLLNQLTGTKSETAAYAFTTLTVVPGLMEHRGAKIQILDIPG 119
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGFQGEDIEIVDLPG 50
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
66-288 2.63e-05

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 45.79  E-value: 2.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  66 VVLVGFPSVGKSTLLNQLTGTK----SETAAyafTTLTVVPGLMEHRGAKIQILDIPGLiagaamgKGRGK-----EVIA 136
Cdd:COG1160  178 IAIVGRPNVGKSSLINALLGEErvivSDIAG---TTRDSIDTPFERDGKKYTLIDTAGI-------RRKGKvdegiEKYS 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 137 VVRT------ADLIIILgdvfndrhIDVlvkelyDAGIrintpkpditikksgmggvrlntvGSVDLNLeeIRTILSENK 210
Cdd:COG1160  248 VLRTlraierADVVLLV--------IDA------TEGI------------------------TEQDLKI--AGLALEAGK 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 211 imnaevlirgnvtqedfidAMIgnrrytpafIAINKVDLVDDQSK--KEIVKRLTKQFGQ---APIM-ISAHSGYNINAL 284
Cdd:COG1160  288 -------------------ALV---------IVVNKWDLVEKDRKtrEELEKEIRRRLPFldyAPIVfISALTGQGVDKL 339

                 ....
gi 973165464 285 KDAI 288
Cdd:COG1160  340 LEAV 343
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
239-292 2.66e-05

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 44.44  E-value: 2.66e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973165464  239 PAFIAINKVDLVDDQS----KKEIVKRLTKQFGQAP-----IMISAHSGYNINALKDAIYEHL 292
Cdd:pfam00009 123 PIIVFINKMDRVDGAEleevVEEVSRELLEKYGEDGefvpvVPGSALKGEGVQTLLDALDEYL 185
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
26-316 3.07e-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: 45.16  E-value: 3.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464   26 LHIGRLKAKIAKLKDEaVSRAMKSSGTGEGYSvkksgDG-TVVLVGFPSVGKSTLLNQLTGTksETA---AYAFTTLTVV 101
Cdd:pfam12631  62 LTEEELLERLEELLAE-LEKLLATADRGRILR-----EGiKVVIVGKPNVGKSSLLNALLGE--ERAivtDIPGTTRDVI 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  102 PGLMEHRGAKIQILDIPGLIAGA----AMGKGRGKEVIAvvrTADLIIILGDvfndrhidvlvkelydagirintpkpdi 177
Cdd:pfam12631 134 EETINIGGIPLRLIDTAGIRETDdeveKIGIERAREAIE---EADLVLLVLD---------------------------- 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  178 tikksgmggvrlntvGSVDLNlEEIRTILSENKIMNAEVLIrgnvtqedfidamignrrytpafiaINKVDLVDDQSKKE 257
Cdd:pfam12631 183 ---------------ASRPLD-EEDLEILELLKDKKPIIVV-------------------------LNKSDLLGEIDELE 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 973165464  258 IVKrltkqfGQAPIMISAHSGYNINALKDAIYEHLGFIQIFmkplgepadMEEPLIVRE 316
Cdd:pfam12631 222 ELK------GKPVLAISAKTGEGLDELEEAIKELFLAGEIA---------SDGPIITNA 265
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
66-292 3.82e-05

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 43.82  E-value: 3.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  66 VVLVGFPSVGKSTLLNQLTGTKSETAAYAFT---TLTVVPGLMEHRGAKIQILDIPGLIAGAAMGKgrgkEVIAVVRTAD 142
Cdd:COG1100    6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLSTngvTIDKKELKLDGLDVDLVIWDTPGQDEFRETRQ----FYARQLTGAS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 143 LIIILGDVfndRHIDVLVKELYDagirintpkpditikksgmggvrlntvgsvdlnLEEIRTIlsenkimnaevlirgnv 222
Cdd:COG1100   82 LYLFVVDG---TREETLQSLYEL---------------------------------LESLRRL----------------- 108
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973165464 223 tqedfidamignRRYTPAFIAINKVDLVDD---QSKKEIVKRLTKQFGQAPIMISAHSGYNINALKDAIYEHL 292
Cdd:COG1100  109 ------------GKKSPIILVLNKIDLYDEeeiEDEERLKEALSEDNIVEVVATSAKTGEGVEELFAALAEIL 169
TGS_Obg cd04938
TGS (ThrRS, GTPase and SpoT) domain found in the Obg protein family; The Obg family of GTPases ...
295-367 3.84e-05

TGS (ThrRS, GTPase and SpoT) domain found in the Obg protein family; The Obg family of GTPases function has been implicated in cellular processes as diverse as sporulation, stress response, control of DNA replication, and ribosome assembly. It consists of several subfamilies such as DRG and YchF with TGS domain. The TGS domain is named after the various RNA-binding multidomain ThrRS, GTPase, and SpoT/RelA proteins in which this domain occurs. The TGS domain of Obg-like GTPases such as those present in DRG (developmentally regulated GTP-binding protein), and GTP-binding proteins Ygr210 and YchF has a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340517 [Multi-domain]  Cd Length: 77  Bit Score: 41.66  E-value: 3.84e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973165464 295 IQIFMKPLGEPaDMEEPLIVREGSTVEDVCNRLHRDFVERFRYAKVWGNSvkhdaQRVSLPHVLADGDILTIV 367
Cdd:cd04938   11 IQTFTNGSGNS-VFRDCVLVKKGTTVKDFANKIHTDLEKGFINAEGIGGR-----RLEGEDYILQDNDVVKFT 77
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
26-316 6.18e-05

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 44.72  E-value: 6.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  26 LHIGRLKAKIAKLKDEaVSRAMKSSGTGEGYSvkksgDG-TVVLVGFPSVGKSTLLNQLTGTKSetaayAFTTltvvpgl 104
Cdd:PRK05291 183 LSDEKILEKLEELIAE-LEALLASARQGEILR-----EGlKVVIAGRPNVGKSSLLNALLGEER-----AIVT------- 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 105 mehrgakiqilDIPGliagaamgkgrgkeviavvRTADLI---IILGdvfndrhiDVLVKeLYD-AGIRintpKPDITIK 180
Cdd:PRK05291 245 -----------DIAG-------------------TTRDVIeehINLD--------GIPLR-LIDtAGIR----ETDDEVE 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464 181 KSGmggvrlntvgsvdlnleeIRtiLSENKIMNAEVLI------RGNVTQEDFIDAMIGNRRYTpafIAINKVDLVDDQS 254
Cdd:PRK05291 282 KIG------------------IE--RSREAIEEADLVLlvldasEPLTEEDDEILEELKDKPVI---VVLNKADLTGEID 338
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 973165464 255 KKEIVkrltkqfGQAPIMISAHSGYNINALKDAIYEHLGfiqifmkpLGEPADMEEPLIVRE 316
Cdd:PRK05291 339 LEEEN-------GKPVIRISAKTGEGIDELREAIKELAF--------GGFGGNQEGVFLTNA 385
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
64-149 8.89e-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: 43.53  E-value: 8.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464   64 GTVVLVGFPSVGKSTLLNQLTGTK-SETAAYAFTTLTVVPGLMEHRGAKIQILDIPGL-IAGAAMGKGRGKEVIAVVRTA 141
Cdd:TIGR00436   1 GFVAILGRPNVGKSTLLNQLHGQKiSITSPKAQTTRNRISGIHTTGASQIIFIDTPGFhEKKHSLNRLMMKEARSAIGGV 80

                  ....*...
gi 973165464  142 DLIIILGD 149
Cdd:TIGR00436  81 DLILFVVD 88
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
35-149 2.56e-04

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 42.86  E-value: 2.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  35 IAKLKDEAVsRAMKSSGTGEGYsVKKSGDGTVVLVGFPSVGKSTLLNQLTGT-KSETAAYAFTTLTVVPGLMEHRGAKIQ 113
Cdd:PRK09518 424 VGDLLDEAL-DSLKVAEKTSGF-LTPSGLRRVALVGRPNVGKSSLLNQLTHEeRAVVNDLAGTTRDPVDEIVEIDGEDWL 501
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 973165464 114 ILDIPGLiaGAAMGKGRGKEVIAVVRT------ADLIIILGD 149
Cdd:PRK09518 502 FIDTAGI--KRRQHKLTGAEYYSSLRTqaaierSELALFLFD 541
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
239-293 2.79e-04

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: 41.48  E-value: 2.79e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 973165464 239 PAFIAINKVDL----VDDQSKKEIVKRLTKQFGQAP---IMISAHSGYNINALKDAIYEHLG 293
Cdd:cd01855   62 PVILVGNKIDLlpkdVKPNRLKQWVKKRLKIGGLKIkdvILVSAKKGWGVEELIEEIKKLAK 123
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
239-288 3.79e-04

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: 41.23  E-value: 3.79e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 973165464 239 PAFIAINKVDLVDDQSKKEIVKRLtKQFGQAPIMISAHSGYNINALKDAI 288
Cdd:cd01854   35 EPVIVLNKADLVDDEELEELLEIY-EKLGYPVLAVSAKTGEGLDELRELL 83
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
4-119 5.61e-04

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: 39.99  E-value: 5.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464   4 LEEQIREIEDELRNTKYNKATSlHIG--RLKAKIAKLkdeavsramkssgtgegysVKKSGDGTVVLVGFPSVGKSTLLN 81
Cdd:cd01859   58 LEKWKEVFESEGLPVVYVSARE-RLGtrILRRTIKEL-------------------AIDGKPVIVGVVGYPKVGKSSIIN 117
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 973165464  82 QLTGTKSETAAyaftTLTVVPGLMEHR-----GAKIQILDIPG 119
Cdd:cd01859  118 ALKGRHSASTS----PIPGSPGYTKGIqlvriDSKIYLIDTPG 156
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
242-288 6.17e-04

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: 40.22  E-value: 6.17e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 973165464  242 IAINKVDLVDDQSKKEIVKRLTKQFGQAPIMISAHSGYNINALKDAI 288
Cdd:pfam03193  58 IVLNKIDLLDEEEELEELLKIYRAIGYPVLFVSAKTGEGIEALKELL 104
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
65-119 8.32e-04

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 41.24  E-value: 8.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 973165464  65 TVVLVGFPSVGKSTLLNQLTGTKSETAAYAFTTLTVVPGLMEHRGAKIQILDIPG 119
Cdd:PRK09554   5 TIGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQFSTTDHQVTLVDLPG 59
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
228-290 8.52e-04

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: 39.82  E-value: 8.52e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973165464 228 IDAMIGNRrytPAFIAINKVDLVDDQSKKEIVKRLTKQfGQAPIMISAHSGYNINALKDAIYE 290
Cdd:cd01856   40 LDKILGNK---PRLIVLNKADLADPAKTKKWLKYFKSQ-GEPVLFVNAKNGKGVKKLLKKAKK 98
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
65-87 1.65e-03

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 40.01  E-value: 1.65e-03
                         10        20
                 ....*....|....*....|...
gi 973165464  65 TVVLVGFPSVGKSTLLNQLTGTK 87
Cdd:COG1160    4 VVAIVGRPNVGKSTLFNRLTGRR 26
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
66-119 1.74e-03

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: 38.66  E-value: 1.74e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  66 VVLVGFPSVGKSTLLNQLTGTKS-ETAAYAFTT-----LTVVPGlmehrgakIQILDIPG 119
Cdd:cd01856  118 AMVVGIPNVGKSTLINRLRGKKVaKVGNKPGVTrgqqwIRIGPN--------IELLDTPG 169
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
67-150 2.40e-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: 38.19  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  67 VLVGFPSVGKSTLLNQLTGTKSE-TAAYAFTTLTVVPGLMEHRGAKIQILDIPGLIAGAAMGKGRGKE-VIAVVRTADLI 144
Cdd:cd01894    1 AIVGRPNVGKSTLFNRLTGRRDAiVSDTPGVTRDRKYGEAEWGGREFILIDTGGIEPDDEGISKEIREqAEIAIEEADVI 80

                 ....*.
gi 973165464 145 IILGDV 150
Cdd:cd01894   81 LFVVDG 86
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
66-144 4.09e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 39.18  E-value: 4.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  66 VVLVGFPSVGKSTLLNQLTG-TKSETAAYAFTTLTVVPGLMEHRGAKIQILDIPGLiaGAAMGKGRGKEVIAVVRTADLI 144
Cdd:PRK03003 214 VALVGKPNVGKSSLLNKLAGeERSVVDDVAGTTVDPVDSLIELGGKTWRFVDTAGL--RRRVKQASGHEYYASLRTHAAI 291
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
49-85 5.06e-03

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: 37.76  E-value: 5.06e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 973165464  49 SSGTGEGYSVKKS--GDGTVVLVGfPS-VGKSTLLNQLTG 85
Cdd:cd01854   69 SAKTGEGLDELREllKGKTSVLVG-QSgVGKSTLLNALLP 107
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
242-288 5.32e-03

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 38.74  E-value: 5.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 973165464 242 IAINKVDLVDD---QSKKEIVKRLTKQFG--QAPIM-ISAHSGYNINALKDAI 288
Cdd:COG3276  109 VVLTKADLVDEewlELVEEEIRELLAGTFleDAPIVpVSAVTGEGIDELRAAL 161
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
67-149 5.75e-03

YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They 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. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 36.93  E-value: 5.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165464  67 VLVGFPSVGKSTLLNQLTGTK-SETAAYAFTTLTVVPGLMEHRGAKIQILDIPGLIAGAAMGKGRGKEVIAVVRTADLII 145
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTEvAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPGVGERGRRDREYEELYRRLLPEADLVL 80

                 ....
gi 973165464 146 ILGD 149
Cdd:cd11383   81 WLLD 84
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
65-124 7.31e-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: 37.68  E-value: 7.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 973165464  65 TVVLVGFPSVGKSTLLNQLTG-TKSETAAYAFTTLTVVPGLMEHRGAKIQILDIPGLIAGA 124
Cdd:cd01853   33 TILVLGKTGVGKSSTINSIFGeRKVSVSAFQSETLRPREVSRTVDGFKLNIIDTPGLLESQ 93
 
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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