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Conserved domains on  [gi|124506405|ref|XP_001351800|]
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ribosome-interacting GTPase 1, putative [Plasmodium falciparum 3D7]

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

CATH:  3.40.50.300|3.10.20.30
EC:  3.6.5.-
Gene Ontology:  GO:0005525|GO:0003924
PubMed:  15827604|11916378
SCOP:  4004038|4001813|4007676

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];
1-365 3.12e-154

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


:

Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 438.08  E-value: 3.12e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405   1 MSILQKIADIEAEMAKTQKNKATNYHLGLLKAKLSKLKAQLIEGGTKGGGEGEGFDVSKTGDARIGLVGFPSVGKSTLLN 80
Cdd:COG1163    2 MTIEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLLN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  81 KLTGTFSEVASYEFTTLTCVPGIFKYKGAKMQLLDLPGIIEGAKDGKGRGKQVIAVAKSCSLILIVLDVLKPLTYKKIIE 160
Cdd:COG1163   82 KLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELEQYDVLKE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 161 kELEGFGIRLNKKPPNIIFQKKDKGGINITHTVPLnNLDEDMIKSICHEYRIINANISIRCEATVDDIIDVIEGNRLYVP 240
Cdd:COG1163  162 -ELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKL-DLDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRVYKP 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 241 CIYVLNKVDQITMEELN-LVTKLPHNVP---ISAHLEWNLDGLLEAIWNYLDLVRIYTKPKGQIPDYESPVILKKEKcKV 316
Cdd:COG1163  240 AIVVVNKIDLADEEYVEeLKSKLPDGVPvifISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKGS-TV 318

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 124506405 317 ENFCKKIHRSLVQQLKYALVWGKSVKHNPQKVGKDHELNDEDVVQLVKK 365
Cdd:COG1163  319 GDVCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIK 367
 
Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
1-365 3.12e-154

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 438.08  E-value: 3.12e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405   1 MSILQKIADIEAEMAKTQKNKATNYHLGLLKAKLSKLKAQLIEGGTKGGGEGEGFDVSKTGDARIGLVGFPSVGKSTLLN 80
Cdd:COG1163    2 MTIEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLLN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  81 KLTGTFSEVASYEFTTLTCVPGIFKYKGAKMQLLDLPGIIEGAKDGKGRGKQVIAVAKSCSLILIVLDVLKPLTYKKIIE 160
Cdd:COG1163   82 KLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELEQYDVLKE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 161 kELEGFGIRLNKKPPNIIFQKKDKGGINITHTVPLnNLDEDMIKSICHEYRIINANISIRCEATVDDIIDVIEGNRLYVP 240
Cdd:COG1163  162 -ELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKL-DLDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRVYKP 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 241 CIYVLNKVDQITMEELN-LVTKLPHNVP---ISAHLEWNLDGLLEAIWNYLDLVRIYTKPKGQIPDYESPVILKKEKcKV 316
Cdd:COG1163  240 AIVVVNKIDLADEEYVEeLKSKLPDGVPvifISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKGS-TV 318

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 124506405 317 ENFCKKIHRSLVQQLKYALVWGKSVKHNPQKVGKDHELNDEDVVQLVKK 365
Cdd:COG1163  319 GDVCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIK 367
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 63-295 1.84e-149

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: 420.80  E-value: 1.84e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  63 ARIGLVGFPSVGKSTLLNKLTGTFSEVASYEFTTLTCVPGIFKYKGAKMQLLDLPGIIEGAKDGKGRGKQVIAVAKSCSL 142
Cdd:cd01896    1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 143 ILIVLDVLKPLTYKKIIEKELEGFGIRLNKKPPNIIFQKKDKGGINITHTVPLNNLDEDMIKSICHEYRIINANISIRCE 222
Cdd:cd01896   81 ILIVLDATKPEGQREILERELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLTKLDEKTVKAILREYKIHNADVLIRED 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124506405 223 ATVDDIIDVIEGNRLYVPCIYVLNKVDQITMEELNLVTKLPHNVPISAHLEWNLDGLLEAIWNYLDLVRIYTK 295
Cdd:cd01896  161 ITVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDRLARIPNSVVISAEKDLNLDELLERIWDYLGLIRIYTK 233
MMR_HSR1_Xtn pfam16897
C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of ...
 185-289 1.06e-57

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: 182.63  E-value: 1.06e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  185 GGINITHTVPLNNLDEDMIKSICHEYRIINANISIRCEATVDDIIDVIEGNRLYVPCIYVLNKVDQITMEELNLVTKLPH 264
Cdd:pfam16897   1 GGINITSTVPLTKLDEETIKAILREYKIHNADVLIREDVTVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDRLAREPD 80

                          90       100
                  ....*....|....*....|....*
gi 124506405  265 NVPISAHLEWNLDGLLEAIWNYLDL 289
Cdd:pfam16897  81 SVPISAEKGLNLDELKERIWEYLGL 105
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 62-215 2.70e-24

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: 97.44  E-value: 2.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405   62 DARIGLVGFPSVGKSTLLNKLTGT-FSEVASYEFTTLTCVPGIFKYKG--AKMQLLDLPGIIEGAKDGKGRGKQVIAVAK 138
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNkGSITEYYPGTTRNYVTTVIEEDGktYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  139 SCSLILIVLDVLKPLT-YKKIIEKELE-GFGIRLNKKPPNIIFQK---KDKGGINITHTVPLNNLDEDMIKSICHEYRII 213
Cdd:TIGR00231  81 VFDIVILVLDVEEILEkQTKEIIHHADsGVPIILVGNKIDLKDADlktHVASEFAKLNGEPIIPLSAETGKNIDSAFKIV 160


                  ..
gi 124506405  214 NA 215
Cdd:TIGR00231 161 EA 162
obgE PRK12297
GTPase CgtA; Reviewed
 63-183 4.68e-20

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 90.55  E-value: 4.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  63 ARIGLVGFPSVGKSTLLNKLTGTFSEVASYEFTTLTCVPGIFKYKGAK---MQllDLPGIIEGAKDGKGRGKQVIAVAKS 139
Cdd:PRK12297 159 ADVGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRsfvMA--DIPGLIEGASEGVGLGHQFLRHIER 236

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 124506405 140 CSLILIVLDVLK-----PLTYKKIIEKELEGFGIRLNKKPPNIIFQKKD 183
Cdd:PRK12297 237 TRVIVHVIDMSGsegrdPIEDYEKINKELKLYNPRLLERPQIVVANKMD 285
 
Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
1-365 3.12e-154

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 438.08  E-value: 3.12e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405   1 MSILQKIADIEAEMAKTQKNKATNYHLGLLKAKLSKLKAQLIEGGTKGGGEGEGFDVSKTGDARIGLVGFPSVGKSTLLN 80
Cdd:COG1163    2 MTIEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLLN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  81 KLTGTFSEVASYEFTTLTCVPGIFKYKGAKMQLLDLPGIIEGAKDGKGRGKQVIAVAKSCSLILIVLDVLKPLTYKKIIE 160
Cdd:COG1163   82 KLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELEQYDVLKE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 161 kELEGFGIRLNKKPPNIIFQKKDKGGINITHTVPLnNLDEDMIKSICHEYRIINANISIRCEATVDDIIDVIEGNRLYVP 240
Cdd:COG1163  162 -ELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKL-DLDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRVYKP 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 241 CIYVLNKVDQITMEELN-LVTKLPHNVP---ISAHLEWNLDGLLEAIWNYLDLVRIYTKPKGQIPDYESPVILKKEKcKV 316
Cdd:COG1163  240 AIVVVNKIDLADEEYVEeLKSKLPDGVPvifISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKGS-TV 318

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 124506405 317 ENFCKKIHRSLVQQLKYALVWGKSVKHNPQKVGKDHELNDEDVVQLVKK 365
Cdd:COG1163  319 GDVCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIK 367
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 63-295 1.84e-149

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: 420.80  E-value: 1.84e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  63 ARIGLVGFPSVGKSTLLNKLTGTFSEVASYEFTTLTCVPGIFKYKGAKMQLLDLPGIIEGAKDGKGRGKQVIAVAKSCSL 142
Cdd:cd01896    1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 143 ILIVLDVLKPLTYKKIIEKELEGFGIRLNKKPPNIIFQKKDKGGINITHTVPLNNLDEDMIKSICHEYRIINANISIRCE 222
Cdd:cd01896   81 ILIVLDATKPEGQREILERELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLTKLDEKTVKAILREYKIHNADVLIRED 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124506405 223 ATVDDIIDVIEGNRLYVPCIYVLNKVDQITMEELNLVTKLPHNVPISAHLEWNLDGLLEAIWNYLDLVRIYTK 295
Cdd:cd01896  161 ITVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDRLARIPNSVVISAEKDLNLDELLERIWDYLGLIRIYTK 233
MMR_HSR1_Xtn pfam16897
C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of ...
 185-289 1.06e-57

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: 182.63  E-value: 1.06e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  185 GGINITHTVPLNNLDEDMIKSICHEYRIINANISIRCEATVDDIIDVIEGNRLYVPCIYVLNKVDQITMEELNLVTKLPH 264
Cdd:pfam16897   1 GGINITSTVPLTKLDEETIKAILREYKIHNADVLIREDVTVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDRLAREPD 80

                          90       100
                  ....*....|....*....|....*
gi 124506405  265 NVPISAHLEWNLDGLLEAIWNYLDL 289
Cdd:pfam16897  81 SVPISAEKGLNLDELKERIWEYLGL 105
TGS_DRG1 cd17230
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 1 ...
 286-365 3.74e-52

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: 167.45  E-value: 3.74e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 286 YLDLVRIYTKPKGQIPDYESPVILKKEKCKVENFCKKIHRSLVQQLKYALVWGKSVKHNPQKVGKDHELNDEDVVQLVKK 365
Cdd:cd17230    1 YLNLVRIYTKPKGQLPDYEEPVVLRSGKSTVEDFCNKIHKSLIKEFKYALVWGSSVKHNPQRVGKDHVLEDEDVVQIVKK 80
TGS_DRG cd01666
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein ...
 287-364 1.01e-33

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: 119.65  E-value: 1.01e-33
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124506405 287 LDLVRIYTKPKGQIPDYESPVILKKeKCKVENFCKKIHRSLVQQLKYALVWGKSVKHNPQKVGKDHELNDEDVVQLVK 364
Cdd:cd01666    1 LGIIRVYTKPPGKKPDFDEPFILRR-GSTVEDVAEKIHKDLAENFKYARVWGKSVKFDGQRVGLDHVLEDGDIVEIHK 77
TGS_DRG2 cd17231
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 2 ...
 286-365 1.79e-32

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: 116.33  E-value: 1.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 286 YLDLVRIYTKPKGQIPDYESPVILKKeKCKVENFCKKIHRSLVQQLKYALVWGKSVKHNPQKVGKDHELNDEDVVQLVKK 365
Cdd:cd17231    1 YLALIRVYTKKRGERPDFGDAIILRR-GATVEHVCHRIHRTLASQFKYALVWGTSTKYSPQRVGLTHVMEDEDVIQIVKK 79
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 66-185 4.21e-29

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: 110.56  E-value: 4.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  66 GLVGFPSVGKSTLLNKLTGTFSEVASYEFTTLTCVPGIFKYK-GAKMQLLDLPGIIEGAKDGKGRGKQVIAVAKSCSLIL 144
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGdGVDIQIIDLPGLLDGASEGRGLGEQILAHLYRSDLIL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 124506405 145 IVLDVLK-----PLTYKKIIEKELEGFGIRLNKKPPNIIFQKKDKG 185
Cdd:cd01881   81 HVIDASEdcvgdPLEDQKTLNEEVSGSFLFLKNKPEMIVANKIDMA 126
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 64-181 6.31e-29

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: 108.09  E-value: 6.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405   64 RIGLVGFPSVGKSTLLNKLTGTFSEVASYEFTTLTCVPGIFKYKGAKMQLLDLPGIIEGAKDGKGRGKQVIAVAKsCSLI 143
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFLAIIE-ADLI 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 124506405  144 LIVLDVLKPLTykkIIEKELEGFGIRlNKKPPNIIFQK 181
Cdd:pfam01926  80 LFVVDSEEGIT---PLDEELLELLRE-NKKPIILVLNK 113
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 63-183 2.48e-24

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: 97.88  E-value: 2.48e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  63 ARIGLVGFPSVGKSTLLNKLTGTFSEVASYEFTTLTCVPGIFKYK-GAKMQLLDLPGIIEGAKDGKGRG----KQViava 137
Cdd:cd01898    1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDdGRSFVIADIPGLIEGASEGKGLGhrflRHI---- 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 124506405 138 KSCSLILIVLDV---LKPLTYKKIIEKELEGFGIRLNKKPPNIIFQKKD 183
Cdd:cd01898   77 ERTRVLLHVIDLsgeDDPVEDYETIRNELEAYNPGLAEKPRIVVLNKID 125
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 62-215 2.70e-24

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: 97.44  E-value: 2.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405   62 DARIGLVGFPSVGKSTLLNKLTGT-FSEVASYEFTTLTCVPGIFKYKG--AKMQLLDLPGIIEGAKDGKGRGKQVIAVAK 138
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNkGSITEYYPGTTRNYVTTVIEEDGktYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  139 SCSLILIVLDVLKPLT-YKKIIEKELE-GFGIRLNKKPPNIIFQK---KDKGGINITHTVPLNNLDEDMIKSICHEYRII 213
Cdd:TIGR00231  81 VFDIVILVLDVEEILEkQTKEIIHHADsGVPIILVGNKIDLKDADlktHVASEFAKLNGEPIIPLSAETGKNIDSAFKIV 160


                  ..
gi 124506405  214 NA 215
Cdd:TIGR00231 161 EA 162
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
 63-287 8.13e-23

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: 97.49  E-value: 8.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405   63 ARIGLVGFPSVGKSTLLNKLTGTFSEVASYEFTTLTCVPGIFKYKGAK-MQLLDLPGIIEGAKDGKGRGKQVIAVAKSCS 141
Cdd:TIGR02729 158 ADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRsFVIADIPGLIEGASEGAGLGHRFLKHIERTR 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  142 LILIVLDV-----LKPLTYKKIIEKELEGFGIRLNKKPpniifqkkdkgginithtvplnnldedmiksicheyRIInan 216
Cdd:TIGR02729 238 VLLHLIDIspedgSDPVEDYEIIRNELKKYSPELAEKP------------------------------------RIV--- 278

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506405  217 isirceatvddiidviegnrlyvpciyVLNKVDQITMEELN-----LVTKLPHNV-PISAHLEWNLDGLLEAIWNYL 287
Cdd:TIGR02729 279 ---------------------------VLNKIDLLDEEELEellkeLKKELGKPVfPISALTGEGLDELLDALAELL 328
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
 63-291 3.87e-22

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: 95.82  E-value: 3.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  63 ARIGLVGFPSVGKSTLLNKLTGTFSEVASYEFTTLTCVPGIFKYKGAK-MQLLDLPGIIEGAKDGKG----------Rgk 131
Cdd:COG0536  158 ADVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGRsFVIADIPGLIEGASEGAGlghrflrhieR-- 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 132 qviavaksCSLILIVLDV-----LKPLTYKKIIEKELEGFGIRLNKKPpniifqkkdkgginithtvplnnldedmiksi 206
Cdd:COG0536  236 --------TRVLLHVVDAapldgRDPVEDYEIIRNELEAYSPELAEKP-------------------------------- 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 207 cheyRIInanisirceatvddiidviegnrlyvpciyVLNKVDQITMEELNLVTK-LPHN----VPISAHLEWNLDGLLE 281
Cdd:COG0536  276 ----RIV------------------------------VLNKIDLLDAEELEELKAeLEKLggpvFPISAVTGEGLDELLY 321

                        250
                 ....*....|
gi 124506405 282 AIWNYLDLVR 291
Cdd:COG0536  322 ALAELLEELR 331
obgE PRK12297
GTPase CgtA; Reviewed
 63-183 4.68e-20

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 90.55  E-value: 4.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  63 ARIGLVGFPSVGKSTLLNKLTGTFSEVASYEFTTLTCVPGIFKYKGAK---MQllDLPGIIEGAKDGKGRGKQVIAVAKS 139
Cdd:PRK12297 159 ADVGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRsfvMA--DIPGLIEGASEGVGLGHQFLRHIER 236

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 124506405 140 CSLILIVLDVLK-----PLTYKKIIEKELEGFGIRLNKKPPNIIFQKKD 183
Cdd:PRK12297 237 TRVIVHVIDMSGsegrdPIEDYEKINKELKLYNPRLLERPQIVVANKMD 285
obgE PRK12299
GTPase CgtA; Reviewed
 63-183 1.34e-19

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 88.20  E-value: 1.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  63 ARIGLVGFPSVGKSTLLNKLTGTFSEVASYEFTTLTCVPGIFKYKGAK-MQLLDLPGIIEGAKDGKGRGKQVIAVAKSCS 141
Cdd:PRK12299 159 ADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKsFVIADIPGLIEGASEGAGLGHRFLKHIERTR 238

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 124506405 142 LILIVLDV--LKPLTYKKIIEKELEGFGIRLNKKPPNIIFQKKD 183
Cdd:PRK12299 239 LLLHLVDIeaVDPVEDYKTIRNELEKYSPELADKPRILVLNKID 282
obgE PRK12298
GTPase CgtA; Reviewed
 63-288 1.46e-17

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 82.99  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  63 ARIGLVGFPSVGKSTLLNKLTGTFSEVASYEFTTLtcVP--GIFKYKGAKMQLL-DLPGIIEGAKDGKGRGKQVIAVAKS 139
Cdd:PRK12298 160 ADVGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTL--VPnlGVVRVDDERSFVVaDIPGLIEGASEGAGLGIRFLKHLER 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 140 CSLILIVLDVL-----KPLTYKKIIEKELEGFGIRLNKKPpniifqkkdkgginithtvplnnldedmiksicheyRIIn 214
Cdd:PRK12298 238 CRVLLHLIDIApidgsDPVENARIIINELEKYSPKLAEKP------------------------------------RWL- 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 215 anisirceatvddiidviegnrlyvpciyVLNKVDQITMEELN-----LVTKLPHNVP---ISAHLEWNLDGLLEAIWNY 286
Cdd:PRK12298 281 -----------------------------VFNKIDLLDEEEAEerakaIVEALGWEGPvylISAASGLGVKELCWDLMTF 331


                 ..
gi 124506405 287 LD 288
Cdd:PRK12298 332 IE 333
TGS pfam02824
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ...
 290-364 1.89e-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: 1.89e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124506405  290 VRIYTkPKGQIPDYESPVIlkkekckVENFCKKIHRSLVQQLKYALVWGksvkhnpQKVGKDHELNDEDVVQLVK 364
Cdd:pfam02824   1 IRVYT-PDGKVPDLPRGAT-------PEDFAYAIHTSLAKKFIYAKVNG-------QLVGLDHPLEDGDVVEIVT 60
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 66-184 1.01e-13

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: 68.04  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  66 GLVGFPSVGKSTLLNKLTG-TFSEVASYEFTTLTCVPG-IFKYKGAKMQLLDLPGIIEGAKDGKGRGKQVIAVAKSCSLI 143
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGqNVGIVSPIPGTTRDPVRKeWELLPLGPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 124506405 144 LIVLDV-LKPLTYKKIIEKelegfgIRLNKKPPNIIFQKKDK 184
Cdd:cd00880   81 LLVVDSdLTPVEEEAKLGL------LRERGKPVLLVLNKIDL 116
obgE PRK12296
GTPase CgtA; Reviewed
 63-183 1.99e-13

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 71.05  E-value: 1.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  63 ARIGLVGFPSVGKSTLLNKLTGTFSEVASYEFTTLtcVP--GIFKYKGAKMQLLDLPGIIEGAKDGKGRGKQVIAVAKSC 140
Cdd:PRK12296 160 ADVGLVGFPSAGKSSLISALSAAKPKIADYPFTTL--VPnlGVVQAGDTRFTVADVPGLIPGASEGKGLGLDFLRHIERC 237

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 124506405 141 SLILIVLDVL------KPLTYKKIIEKELE---------GFGIRLNKKPPNIIFQKKD 183
Cdd:PRK12296 238 AVLVHVVDCAtlepgrDPLSDIDALEAELAayapaldgdLGLGDLAERPRLVVLNKID 295
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 67-119 4.59e-11

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: 60.65  E-value: 4.59e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 124506405  67 LVGFPSVGKSTLLNKLTGTFSEVASYEFTTLTCVPGIFKYKGAKMQLLDLPGI 119
Cdd:cd01897    5 IAGYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLRWQVIDTPGI 57
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
 65-276 1.43e-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: 61.48  E-value: 1.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  65 IGLVGFPSVGKSTLLNKLTGTFSEVASYEFTT--------------------LTCVPGIFKYKGAK----MQLLDLPGII 120
Cdd:cd01899    1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTidpnvgvgyvrvecpckelgVSCNPRYGKCIDGKryvpVELIDVAGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 121 EGAKDGKGRGKQVI-AVAKSCSLILIV-----------------LDVLKPLT---------YKKIIEKELEGF--GIRLN 171
Cdd:cd01899   81 PGAHEGKGLGNQFLdDLRDADVLIHVVdasggtdaegngvetggYDPLEDIEfleneidmwIYGILERNWEKIvrKAKAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 172 KKPPNIIFQKKDKG-GINITH----------TVPLNNLDEDMIKSICHEYRIINAnisirceatvddiidviegnrlyvP 240
Cdd:cd01899  161 KTDIVEALSEQLSGfGVNEDVviealeelelPADLSKWDDEDLLRLARELRKRRK------------------------P 216

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 124506405 241 CIYVLNKVDQITMEELNLVTKL----PHNVPISAHLEWNL 276
Cdd:cd01899  217 MVIAANKADIPDAEENISKLRLkypdEIVVPTSAEAELAL 256
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 66-184 2.09e-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: 58.62  E-value: 2.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  66 GLVGFPSVGKSTLLNKLTG-TFSEVASYEFTTLTCVPG--IFKYKGAKMQLLDLPGIIEGakDGKGRGKQVIAVAKSCSL 142
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGgEVGEVSDVPGTTRDPDVYvkELDKGKVKLVLVDTPGLDEF--GGLGREELARLLLRGADL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 124506405 143 ILIVLDVLKPLTYKKIIEKELEGFgiRLNKKPPNIIFQKKDK 184
Cdd:cd00882   79 ILLVVDSTDRESEEDAKLLILRRL--RKEGIPIILVGNKIDL 118
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
69-121 3.42e-10

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 60.62  E-value: 3.42e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 124506405  69 GFPSVGKSTLLNKLTGTFSEVASYEFTTLTCVPGIFKYKGAKMQLLDLPGIIE 121
Cdd:COG1084  167 GYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGRYQVIDTPGLLD 219
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 64-119 7.62e-10

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: 57.07  E-value: 7.62e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 124506405   64 RIGLVGFPSVGKSTLLNKLTGTFSEVASYEFTTLTCVPGIFKYKGAKMQLLDLPGI 119
Cdd:pfam02421   2 TIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFKYKGYEIEIVDLPGI 57
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 67-119 4.72e-09

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: 54.77  E-value: 4.72e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 124506405  67 LVGFPSVGKSTLLNKLTGTFSEVASYEFTTLTCVPGIFKYKGAKMQLLDLPGI 119
Cdd:cd01879    2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPGT 54
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
64-119 8.41e-09

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 57.05  E-value: 8.41e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124506405  64 RIGLVGFPSVGKSTLLNKLTGTFSEVASY-----EFTTltcvpGIFKYKGAKMQLLDLPGI 119
Cdd:COG0370    5 TIALVGNPNVGKTTLFNALTGSRQKVGNWpgvtvEKKE-----GKFKLKGKEIELVDLPGT 60
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 59-283 1.25e-08

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: 54.39  E-value: 1.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  59 KTGDARIGLVGFPSVGKSTLLNKLTGTFSEVASYEFTTLTcvpgifkykgAKMQLLDLPGiiegakdgkgrGKQVIAVak 138
Cdd:cd01878   38 RSGVPTVALVGYTNAGKSTLFNALTGADVLAEDQLFATLD----------PTTRRIKLPG-----------GREVLLT-- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 139 scslilivlD-VlkpltykkiiekeleGFgIRlnKKPPNII--FQKkdkgginithTvplnnLDEdmiksicheyrIINA 215
Cdd:cd01878   95 ---------DtV---------------GF-IR--DLPHQLVeaFRS----------T-----LEE-----------VAEA 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 216 NISI-----------RCEATVDDIIDVIEGNRlyVPCIYVLNKVDQITMEEL--NLVTKLPHNVPISAHLEWNLDGLLEA 282
Cdd:cd01878  122 DLLLhvvdasdpdreEQIETVEEVLKELGADD--IPIILVLNKIDLLDDEELeeRLRAGRPDAVFISAKTGEGLDLLKEA 199


                 .
gi 124506405 283 I 283
Cdd:cd01878  200 I 200
PRK09602 PRK09602
translation-associated GTPase; Reviewed
 64-132 8.33e-08

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 53.66  E-value: 8.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  64 RIGLVGFPSVGKSTLLNKLTGTFSEVASYEFTT--------------------LTCVPGIFKYKGAK----MQLLDLPGI 119
Cdd:PRK09602   3 TIGLVGKPNVGKSTFFNAATLADVEIANYPFTTidpnvgvayvrvecpckelgVKCNPRNGKCIDGTrfipVELIDVAGL 82

                         90
                 ....*....|...
gi 124506405 120 IEGAKDGKGRGKQ 132
Cdd:PRK09602  83 VPGAHEGRGLGNQ 95
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 223-287 1.03e-07

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 53.17  E-value: 1.03e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124506405 223 ATVDDIIDVIEGNRlyVPCIYVLNKVDQITMEELN-LVTKLPHNVPISAHLEWNLDGLLEAIWNYL 287
Cdd:COG2262  298 ETVNEVLEELGADD--KPIILVFNKIDLLDDEELErLRAGYPDAVFISAKTGEGIDELLEAIEERL 361
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 64-172 4.09e-07

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: 49.35  E-value: 4.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  64 RIGLVGFPSVGKSTLLNKLTGT----FSEVASyefTTLTCVPGIFKYKGAKMQLLDLPGIIEGAKDGKG-------RGKQ 132
Cdd:cd01895    4 KIAIIGRPNVGKSSLLNALLGEerviVSDIAG---TTRDSIDVPFEYDGQKYTLIDTAGIRKKGKVTEGiekysvlRTLK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 124506405 133 VIavaKSCSLILIVLDVLKPLTY--KKI---IEKELEGFGIRLNK 172
Cdd:cd01895   81 AI---ERADVVLLVLDASEGITEqdLRIaglILEEGKALIIVVNK 122
TGS_Obg cd04938
TGS (ThrRS, GTPase and SpoT) domain found in the Obg protein family; The Obg family of GTPases ...
 289-363 4.39e-07

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: 47.06  E-value: 4.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 289 LVRIYTKPKGQIPDYESP------VILKKEKCKVENFCKKIHRSLVQQLKYALVWGksvkhNPQKVGKDHELNDEDVVQL 362
Cdd:cd04938    2 LIPVYPVKNIQTFTNGSGnsvfrdCVLVKKGTTVKDFANKIHTDLEKGFINAEGIG-----GRRLEGEDYILQDNDVVKF 76


                 .
gi 124506405 363 V 363
Cdd:cd04938   77 T 77
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 67-149 8.17e-07

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: 48.20  E-value: 8.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  67 LVGFPSVGKSTLLNKLTGT-FSEVASYEFTTLTCVPGIFKYKGAKMQLLDLPGIIEGAK--DGKGRgKQVIAVAKSCSLI 143
Cdd:cd01894    2 IVGRPNVGKSTLFNRLTGRrDAIVSDTPGVTRDRKYGEAEWGGREFILIDTGGIEPDDEgiSKEIR-EQAEIAIEEADVI 80


                 ....*.
gi 124506405 144 LIVLDV 149
Cdd:cd01894   81 LFVVDG 86
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 64-163 4.91e-06

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 48.02  E-value: 4.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  64 RIGLVGFPSVGKSTLLNKLTGTFSEVASYEFTTL------TCVP--------GIFKYK---GAKMQLLDLPGIIEGAKDG 126
Cdd:PTZ00258  23 KMGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIdpntarVNVPderfdwlcKHFKPKsivPAQLDITDIAGLVKGASEG 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 124506405 127 KGRGKQVIAVAKSCSLILIVL------------DVLKPLTYKKIIEKEL 163
Cdd:PTZ00258 103 EGLGNAFLSHIRAVDGIYHVVrafededithveGEIDPVRDLEIISSEL 151
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
 69-119 7.29e-06

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: 47.81  E-value: 7.29e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 124506405   69 GFPSVGKSTLLNKLTGTFSEVASYEFTTLTCVPGIFKYKGAKMQLLDLPGI 119
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGFQGEDIEIVDLPGI 51
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
65-119 1.76e-05

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 46.63  E-value: 1.76e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 124506405  65 IGLVGFPSVGKSTLLNKLTGTFSEVASYEFTTLTCVPGIFKYKGAKMQLLDLPGI 119
Cdd:PRK09554   6 IGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQFSTTDHQVTLVDLPGT 60
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 65-184 2.53e-05

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 43.99  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  65 IGLVGFPSVGKSTLLNKLTGT-FSEVASYEFTTLTCVPGIFKYKGAKMQLLDLPGIIEG-AKDGKGRGKQVIAVAKSCSL 142
Cdd:cd04163    6 VAIIGRPNVGKSTLLNALVGQkISIVSPKPQTTRNRIRGIYTDDDAQIIFVDTPGIHKPkKKLGERMVKAAWSALKDVDL 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 124506405 143 ILIVLDVLKPLTY--KKIIEKelegfgIRLNKKPPNIIFQKKDK 184
Cdd:cd04163   86 VLFVVDASEWIGEgdEFILEL------LKKSKTPVILVLNKIDL 123
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
 64-148 1.17e-04

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: 43.15  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405   64 RIGLVGFPSVGKSTLLNKLTG-TFSEVASYEFTTLTCVPGIFKYKGAKMQLLDLPGI-IEGAKDGKGRGKQVIAVAKSCS 141
Cdd:TIGR00436   2 FVAILGRPNVGKSTLLNQLHGqKISITSPKAQTTRNRISGIHTTGASQIIFIDTPGFhEKKHSLNRLMMKEARSAIGGVD 81


                  ....*..
gi 124506405  142 LILIVLD 148
Cdd:TIGR00436  82 LILFVVD 88
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
65-287 1.47e-04

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 43.05  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  65 IGLVGFPSVGKSTLLNKLTGT----FSEVASyefTTLTCVPGIFKYKGAKMQLLDLPGIIEgAKDGKGRG--KQVIAVAK 138
Cdd:COG1159    6 VAIVGRPNVGKSTLLNALVGQkvsiVSPKPQ---TTRHRIRGIVTREDAQIVFVDTPGIHK-PKRKLGRRmnKAAWSALE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 139 SCSLILIVLDVLKPLTykkiiekelegfgirlnkkppniifqkkdkgginithtvplnnlDEDmiksicheyriinanis 218
Cdd:COG1159   82 DVDVILFVVDATEKIG--------------------------------------------EGD----------------- 100

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124506405 219 irceatvDDIIDVIEGNRlyVPCIYVLNKVDQITMEEL----NLVTKLPHN---VPISAHLEWNLDGLLEAIWNYL 287
Cdd:COG1159  101 -------EFILELLKKLK--TPVILVINKIDLVKKEELlpllAEYSELLDFaeiVPISALKGDNVDELLDEIAKLL 167
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
61-183 2.34e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 41.51  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  61 GDARIGLVGFPSVGKSTLLNKLTGTFSEVASYEfTTLtcvpGI------FKYKGAKMQLL--DLPGIIEGAKDgkgrGKQ 132
Cdd:COG1100    2 GEKKIVVVGTGGVGKTSLVNRLVGDIFSLEKYL-STN----GVtidkkeLKLDGLDVDLViwDTPGQDEFRET----RQF 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 124506405 133 VIAVAKSCSLILIVLDVLKPLTYKKIIE--KELEgfgiRLNKKPPNIIFQ-KKD 183
Cdd:COG1100   73 YARQLTGASLYLFVVDGTREETLQSLYEllESLR----RLGKKSPIILVLnKID 122
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 62-119 2.58e-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: 41.15  E-value: 2.58e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124506405  62 DARIGLVGFPSVGKSTLLNKLTG-----TFSEVASYEFTTltcvpGIFKYKGA-KMQLLDLPGI 119
Cdd:cd01859   99 PVIVGVVGYPKVGKSSIINALKGrhsasTSPIPGSPGYTK-----GIQLVRIDsKIYLIDTPGV 157
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 61-154 2.75e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 42.65  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  61 GDARIGLVGFPSVGKSTLLNKLTG----TFSEVASyefTTLTCVPGIFKYKGAKMQLLDLPGIIEGAKDGKG-------R 129
Cdd:PRK03003 210 GPRRVALVGKPNVGKSSLLNKLAGeersVVDDVAG---TTVDPVDSLIELGGKTWRFVDTAGLRRRVKQASGheyyaslR 286

                         90       100
                 ....*....|....*....|....*
gi 124506405 130 GKQVIAVAKSCsliLIVLDVLKPLT 154
Cdd:PRK03003 287 THAAIEAAEVA---VVLIDASEPIS 308
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 58-120 3.58e-04

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: 40.29  E-value: 3.58e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124506405  58 SKTGDARIGLVGFPSVGKSTLLNKLTGtfSEVASY--------EFTTLTCVPGIfkykgakmQLLDLPGII 120
Cdd:cd01857   78 SALNEATIGLVGYPNVGKSSLINALVG--SKKVSVsstpgktkHFQTIFLEPGI--------TLCDCPGLV 138
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 57-154 3.86e-04

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 42.47  E-value: 3.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  57 VSKTGDARIGLVGFPSVGKSTLLNKLTGT-FSEVASYEFTTLTCVPGIFKYKGAKMQLLDLPGIIEGAKDGKGR----GK 131
Cdd:PRK09518 445 LTPSGLRRVALVGRPNVGKSSLLNQLTHEeRAVVNDLAGTTRDPVDEIVEIDGEDWLFIDTAGIKRRQHKLTGAeyysSL 524

                         90       100
                 ....*....|....*....|...
gi 124506405 132 QVIAVAKSCSLILIVLDVLKPLT 154
Cdd:PRK09518 525 RTQAAIERSELALFLFDASQPIS 547
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 64-119 4.09e-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: 40.59  E-value: 4.09e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124506405  64 RIGLVGFPSVGKSTLLNKLTGTFS-EVASyefttltcVPGI------FKYKGaKMQLLDLPGI 119
Cdd:cd01856  117 RAMVVGIPNVGKSTLINRLRGKKVaKVGN--------KPGVtrgqqwIRIGP-NIELLDTPGI 170
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 66-152 1.12e-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: 38.86  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  66 GLVGFPSVGKSTLLNKLTGT-FSEVASYEFTTLTCVPGIFKYKGAKMQLLDLPGIIEGAKDGKGRGKQVIAVAKSCSLIL 144
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTeVAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPGVGERGRRDREYEELYRRLLPEADLVL 80


                 ....*...
gi 124506405 145 IVLDVLKP 152
Cdd:cd11383   81 WLLDADDR 88
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 64-172 1.17e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 40.80  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  64 RIGLVGFPSVGKSTLLNKLTGT----FSEVASyefTTLTCVPGIFKYKGAKMQLLDLPGIIEgakdgKGRGKQVI---AV 136
Cdd:PRK00093 175 KIAIIGRPNVGKSSLINALLGEerviVSDIAG---TTRDSIDTPFERDGQKYTLIDTAGIRR-----KGKVTEGVekySV 246

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 124506405 137 AKS------CSLILIVLDVLKPLTY--KKI---IEKELEGFGIRLNK 172
Cdd:PRK00093 247 IRTlkaierADVVLLVIDATEGITEqdLRIaglALEAGRALVIVVNK 293
YeeP COG3596
Predicted GTPase [General function prediction only];
64-152 1.21e-03

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 40.52  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  64 RIGLVGFPSVGKSTLLNKLTG-TFSEVASYEFTTLTcvPGIFKYK---GAKMQLLDLPGIIEGAKDGKgRGKQVIAVAKS 139
Cdd:COG3596   41 VIALVGKTGAGKSSLINALFGaEVAEVGVGRPCTRE--IQRYRLEsdgLPGLVLLDTPGLGEVNERDR-EYRELRELLPE 117

                         90
                 ....*....|...
gi 124506405 140 CSLILIVLDVLKP 152
Cdd:COG3596  118 ADLILWVVKADDR 130
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 239-283 1.45e-03

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


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 39.01  E-value: 1.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 124506405 239 VPCIYVLNKVDQITMEELNLVTKLPHNVPISAHLEWNLDGLLEAI 283
Cdd:cd04164  110 KPVIVVLNKSDLLSDAEGISELNGKPIIAISAKTGEGIDELKEAL 154
era PRK00089
GTPase Era; Reviewed
 65-184 1.59e-03

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 40.03  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  65 IGLVGFPSVGKSTLLNKLTGT-FSEVASYEFTTLTCVPGIFKYKGAKMQLLDLPGIIEgAKDGKGRG--KQVIAVAKSCS 141
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQkISIVSPKPQTTRHRIRGIVTEDDAQIIFVDTPGIHK-PKRALNRAmnKAAWSSLKDVD 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 124506405 142 LILIVLDVLKPLT--YKKIIEKelegfgIRLNKKPPNIIFQKKDK 184
Cdd:PRK00089  87 LVLFVVDADEKIGpgDEFILEK------LKKVKTPVILVLNKIDL 125
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
64-119 4.43e-03

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 38.85  E-value: 4.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  64 RIGLVGFPSVGKSTLLNKLTGT----FSEVASyefTTLTCVPGIFKYKGAKMQLLDLPGI 119
Cdd:COG1160  177 KIAIVGRPNVGKSSLINALLGEerviVSDIAG---TTRDSIDTPFERDGKKYTLIDTAGI 233
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
59-127 5.27e-03

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 38.17  E-value: 5.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124506405  59 KTGDARIGLVGFPSVGKSTLLNKLTGTFSEVASYEfttltcvPGIFKYK-----GAKMQLLDLPGI----IEGAKDGK 127
Cdd:COG1161  110 KRRPIRVMIVGIPNVGKSTLINRLAGKKVAKTGNK-------PGVTKGQqwiklDDGLELLDTPGIlwpkFEDPEVGY 180
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
65-154 5.62e-03

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 38.47  E-value: 5.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  65 IGLVGFPSVGKSTLLNKLTGT-FSEVASYEFTTLTCVPGIFKYKGAKMQLLDLPGIIEGAKDG--KGRGKQVIAVAKSCS 141
Cdd:COG1160    5 VAIVGRPNVGKSTLFNRLTGRrDAIVDDTPGVTRDRIYGEAEWGGREFTLIDTGGIEPDDDDGleAEIREQAELAIEEAD 84

                         90
                 ....*....|...
gi 124506405 142 LILIVLDVLKPLT 154
Cdd:COG1160   85 VILFVVDGRAGLT 97
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 65-199 9.66e-03

Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.


Pssm-ID: 206650  Cd Length: 224  Bit Score: 36.92  E-value: 9.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405  65 IGLVGFPSVGKSTLLNKLTGT---FSEVASYEFTT----LTCVPgiFKYKGAKMQ---LLDLpgiiEGAkDGKGRGKQV- 133
Cdd:cd01851   10 VSVFGSQSSGKSFLLNHLFGTsdgFDVMDTSQQTTkgiwMWSDP--FKDTDGKKHavlLLDT----EGT-DGRERGEFEn 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506405 134 ------IAVAKSCSLILIV--------LDVLKPLTyKKIIEKELEGFGIRLNKKPPNIIFQKKDkgginITHTVPLNNLD 199
Cdd:cd01851   83 darlfaLATLLSSVLIYNMwqtilgddLDKLMGLL-KTALETLGLAGLHNFSKPKPLLLFVVRD-----FTGPTPLEGLD 156
 
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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