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Conserved domains on  [gi|353238676|emb|CCA70615|]
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probable RBG1-ribosome interacting GTPase [Serendipita indica DSM 11827]

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 super family cl34153
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
15-373 4.64e-144

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


The actual alignment was detected with superfamily member COG1163:

Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 412.65  E-value: 4.64e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  15 HLGLLKAKLAKLRRELlaGPSGGGGGGGGPGFDVARTGVASVGFVGFPSVGKSTLMSKLTGTHSEVAAYEFTTLTSVPGT 94
Cdd:COG1163   27 HIGRLKAKLAELKEEL--EKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGM 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  95 LRLHGSPIQIIDLPGIIEGAKDGRGRGRQVIAVARTCNLIFIVLDVLKPLHDKKILEdELEGFGIRLNKKPPNITVKKKE 174
Cdd:COG1163  105 LEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELEQYDVLKE-ELYDAGIRLNKPPPDVTIEKKG 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 175 KGgepshlsricwltrlGIAITNTVPLTnIDHEEIKAVLSEYRLANCDVAIREpGCTADDLVDVIEGNRVYIPCIYVLNK 254
Cdd:COG1163  184 KG---------------GIRVNSTGKLD-LDEEDIKKILREYGIVNADVLIRE-DVTLDDLIDALMGNRVYKPAIVVVNK 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 255 IDAISIEEL-DLLYKIPHSVP---ISSKEWLNIDELLDALWNALNLVRVYTKPRGLAPDYSAPVVLKRNkATVEDFCNAI 330
Cdd:COG1163  247 IDLADEEYVeELKSKLPDGVPvifISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKG-STVGDVCEKI 325

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 353238676 331 HKEIAKQLKYAIVWGTSAKHsRGQKVGLDHELQDEDVVHIVKK 373
Cdd:COG1163  326 HRDFVERFRYARVWGKSAKH-PGQRVGLDHVLEDGDIVEIIIK 367
 
Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
15-373 4.64e-144

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 412.65  E-value: 4.64e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  15 HLGLLKAKLAKLRRELlaGPSGGGGGGGGPGFDVARTGVASVGFVGFPSVGKSTLMSKLTGTHSEVAAYEFTTLTSVPGT 94
Cdd:COG1163   27 HIGRLKAKLAELKEEL--EKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGM 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  95 LRLHGSPIQIIDLPGIIEGAKDGRGRGRQVIAVARTCNLIFIVLDVLKPLHDKKILEdELEGFGIRLNKKPPNITVKKKE 174
Cdd:COG1163  105 LEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELEQYDVLKE-ELYDAGIRLNKPPPDVTIEKKG 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 175 KGgepshlsricwltrlGIAITNTVPLTnIDHEEIKAVLSEYRLANCDVAIREpGCTADDLVDVIEGNRVYIPCIYVLNK 254
Cdd:COG1163  184 KG---------------GIRVNSTGKLD-LDEEDIKKILREYGIVNADVLIRE-DVTLDDLIDALMGNRVYKPAIVVVNK 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 255 IDAISIEEL-DLLYKIPHSVP---ISSKEWLNIDELLDALWNALNLVRVYTKPRGLAPDYSAPVVLKRNkATVEDFCNAI 330
Cdd:COG1163  247 IDLADEEYVeELKSKLPDGVPvifISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKG-STVGDVCEKI 325

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 353238676 331 HKEIAKQLKYAIVWGTSAKHsRGQKVGLDHELQDEDVVHIVKK 373
Cdd:COG1163  326 HRDFVERFRYARVWGKSAKH-PGQRVGLDHVLEDGDIVEIIIK 367
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 54-302 2.21e-143

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: 405.78  E-value: 2.21e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  54 ASVGFVGFPSVGKSTLMSKLTGTHSEVAAYEFTTLTSVPGTLRLHGSPIQIIDLPGIIEGAKDGRGRGRQVIAVARTCNL 133
Cdd:cd01896    1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 134 IFIVLDVLKPLHDKKILEDELEGFGIRLNKKPPNITVKKKEKGgepshlsricwltrlGIAITNTVPLTNIDHEEIKAVL 213
Cdd:cd01896   81 ILIVLDATKPEGQREILERELEGVGIRLNKKPPNVTIKKKKKG---------------GINITSTVPLTKLDEKTVKAIL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 214 SEYRLANCDVAIREPgCTADDLVDVIEGNRVYIPCIYVLNKIDAISIEELDLLYKIPHSVPISSKEWLNIDELLDALWNA 293
Cdd:cd01896  146 REYKIHNADVLIRED-ITVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDRLARIPNSVVISAEKDLNLDELLERIWDY 224


                 ....*....
gi 353238676 294 LNLVRVYTK 302
Cdd:cd01896  225 LGLIRIYTK 233
MMR_HSR1_Xtn pfam16897
C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of ...
 192-296 5.69e-56

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: 178.39  E-value: 5.69e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  192 GIAITNTVPLTNIDHEEIKAVLSEYRLANCDVAIREPgCTADDLVDVIEGNRVYIPCIYVLNKIDAISIEELDLLYKIPH 271
Cdd:pfam16897   2 GINITSTVPLTKLDEETIKAILREYKIHNADVLIRED-VTVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDRLAREPD 80

                          90       100
                  ....*....|....*....|....*
gi 353238676  272 SVPISSKEWLNIDELLDALWNALNL 296
Cdd:pfam16897  81 SVPISAEKGLNLDELKERIWEYLGL 105
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
 53-165 1.07e-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: 105.58  E-value: 1.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676   53 VASVGFVGFPSVGKSTLMSKLTGTHSEVAAYEFTTLTSVPGTLRLH-GSPIQIIDLPGIIEGAKDGRGRGRQVIA-VART 130
Cdd:TIGR02729 157 LADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDdGRSFVIADIPGLIEGASEGAGLGHRFLKhIERT 236

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 353238676  131 CNLIFIV----LDVLKPLHDKKILEDELEGFGIRLNKKP 165
Cdd:TIGR02729 237 RVLLHLIdispEDGSDPVEDYEIIRNELKKYSPELAEKP 275
obgE PRK12299
GTPase CgtA; Reviewed
 54-165 1.67e-23

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 99.37  E-value: 1.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  54 ASVGFVGFPSVGKSTLMSKLTGTHSEVAAYEFTTLTSVPGTLRL-HGSPIQIIDLPGIIEGAKDGRGRGRQVIA-VARTC 131
Cdd:PRK12299 159 ADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVdDYKSFVIADIPGLIEGASEGAGLGHRFLKhIERTR 238

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 353238676 132 NLIFIV-LDVLKPLHDKKILEDELEGFGIRLNKKP 165
Cdd:PRK12299 239 LLLHLVdIEAVDPVEDYKTIRNELEKYSPELADKP 273
 
Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
15-373 4.64e-144

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 412.65  E-value: 4.64e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  15 HLGLLKAKLAKLRRELlaGPSGGGGGGGGPGFDVARTGVASVGFVGFPSVGKSTLMSKLTGTHSEVAAYEFTTLTSVPGT 94
Cdd:COG1163   27 HIGRLKAKLAELKEEL--EKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGM 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  95 LRLHGSPIQIIDLPGIIEGAKDGRGRGRQVIAVARTCNLIFIVLDVLKPLHDKKILEdELEGFGIRLNKKPPNITVKKKE 174
Cdd:COG1163  105 LEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELEQYDVLKE-ELYDAGIRLNKPPPDVTIEKKG 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 175 KGgepshlsricwltrlGIAITNTVPLTnIDHEEIKAVLSEYRLANCDVAIREpGCTADDLVDVIEGNRVYIPCIYVLNK 254
Cdd:COG1163  184 KG---------------GIRVNSTGKLD-LDEEDIKKILREYGIVNADVLIRE-DVTLDDLIDALMGNRVYKPAIVVVNK 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 255 IDAISIEEL-DLLYKIPHSVP---ISSKEWLNIDELLDALWNALNLVRVYTKPRGLAPDYSAPVVLKRNkATVEDFCNAI 330
Cdd:COG1163  247 IDLADEEYVeELKSKLPDGVPvifISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKG-STVGDVCEKI 325

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 353238676 331 HKEIAKQLKYAIVWGTSAKHsRGQKVGLDHELQDEDVVHIVKK 373
Cdd:COG1163  326 HRDFVERFRYARVWGKSAKH-PGQRVGLDHVLEDGDIVEIIIK 367
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 54-302 2.21e-143

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: 405.78  E-value: 2.21e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  54 ASVGFVGFPSVGKSTLMSKLTGTHSEVAAYEFTTLTSVPGTLRLHGSPIQIIDLPGIIEGAKDGRGRGRQVIAVARTCNL 133
Cdd:cd01896    1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 134 IFIVLDVLKPLHDKKILEDELEGFGIRLNKKPPNITVKKKEKGgepshlsricwltrlGIAITNTVPLTNIDHEEIKAVL 213
Cdd:cd01896   81 ILIVLDATKPEGQREILERELEGVGIRLNKKPPNVTIKKKKKG---------------GINITSTVPLTKLDEKTVKAIL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 214 SEYRLANCDVAIREPgCTADDLVDVIEGNRVYIPCIYVLNKIDAISIEELDLLYKIPHSVPISSKEWLNIDELLDALWNA 293
Cdd:cd01896  146 REYKIHNADVLIRED-ITVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDRLARIPNSVVISAEKDLNLDELLERIWDY 224


                 ....*....
gi 353238676 294 LNLVRVYTK 302
Cdd:cd01896  225 LGLIRIYTK 233
MMR_HSR1_Xtn pfam16897
C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of ...
 192-296 5.69e-56

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: 178.39  E-value: 5.69e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  192 GIAITNTVPLTNIDHEEIKAVLSEYRLANCDVAIREPgCTADDLVDVIEGNRVYIPCIYVLNKIDAISIEELDLLYKIPH 271
Cdd:pfam16897   2 GINITSTVPLTKLDEETIKAILREYKIHNADVLIRED-VTVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDRLAREPD 80

                          90       100
                  ....*....|....*....|....*
gi 353238676  272 SVPISSKEWLNIDELLDALWNALNL 296
Cdd:pfam16897  81 SVPISAEKGLNLDELKERIWEYLGL 105
TGS_DRG1 cd17230
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 1 ...
 294-373 3.29e-46

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: 152.43  E-value: 3.29e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 294 LNLVRVYTKPRGLAPDYSAPVVLKRNKATVEDFCNAIHKEIAKQLKYAIVWGTSAKHsRGQKVGLDHELQDEDVVHIVKK 373
Cdd:cd17230    2 LNLVRIYTKPKGQLPDYEEPVVLRSGKSTVEDFCNKIHKSLIKEFKYALVWGSSVKH-NPQRVGKDHVLEDEDVVQIVKK 80
TGS_DRG2 cd17231
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 2 ...
 294-373 1.82e-33

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: 119.41  E-value: 1.82e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 294 LNLVRVYTKPRGLAPDYSAPVVLKRNkATVEDFCNAIHKEIAKQLKYAIVWGTSAKHSRgQKVGLDHELQDEDVVHIVKK 373
Cdd:cd17231    2 LALIRVYTKKRGERPDFGDAIILRRG-ATVEHVCHRIHRTLASQFKYALVWGTSTKYSP-QRVGLTHVMEDEDVIQIVKK 79
TGS_DRG cd01666
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein ...
 294-372 4.20e-32

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: 115.41  E-value: 4.20e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 353238676 294 LNLVRVYTKPRGLAPDYSAPVVLKRNkATVEDFCNAIHKEIAKQLKYAIVWGTSAKHSrGQKVGLDHELQDEDVVHIVK 372
Cdd:cd01666    1 LGIIRVYTKPPGKKPDFDEPFILRRG-STVEDVAEKIHKDLAENFKYARVWGKSVKFD-GQRVGLDHVLEDGDIVEIHK 77
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 57-193 6.79e-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: 110.18  E-value: 6.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  57 GFVGFPSVGKSTLMSKLTGTHSEVAAYEFTTLTSVPGTLR-LHGSPIQIIDLPGIIEGAKDGRGRGRQVIAVARTCNLIF 135
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEfGDGVDIQIIDLPGLLDGASEGRGLGEQILAHLYRSDLIL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 353238676 136 IVLDVLK-----PLHDKKILEDELEGFGIRLNKKP-------------PNITVKKKEKGGEPSHLSRICWLTRLGI 193
Cdd:cd01881   81 HVIDASEdcvgdPLEDQKTLNEEVSGSFLFLKNKPemivankidmaseNNLKRLKLDKLKRGIPVVPTSALTRLGL 156
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 56-172 2.84e-28

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: 106.55  E-value: 2.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676   56 VGFVGFPSVGKSTLMSKLTGTHSEVAAYEFTTLTSVPGTLRLHGSPIQIIDLPGIIEGAKDGRGRGRQVIAVARtCNLIF 135
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFLAIIE-ADLIL 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 353238676  136 IVLDVLKPLhdkKILEDELEGFGIRlNKKPPNITVKK 172
Cdd:pfam01926  81 FVVDSEEGI---TPLDEELLELLRE-NKKPIILVLNK 113
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 54-165 1.47e-26

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: 104.04  E-value: 1.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  54 ASVGFVGFPSVGKSTLMSKLTGTHSEVAAYEFTTLTSVPGTLRL-HGSPIQIIDLPGIIEGAKDGRGRG----RQviaVA 128
Cdd:cd01898    1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVdDGRSFVIADIPGLIEGASEGKGLGhrflRH---IE 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 353238676 129 RtCNLIFIVLDV---LKPLHDKKILEDELEGFGIRLNKKP 165
Cdd:cd01898   78 R-TRVLLHVIDLsgeDDPVEDYETIRNELEAYNPGLAEKP 116
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
 53-165 1.07e-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: 105.58  E-value: 1.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676   53 VASVGFVGFPSVGKSTLMSKLTGTHSEVAAYEFTTLTSVPGTLRLH-GSPIQIIDLPGIIEGAKDGRGRGRQVIA-VART 130
Cdd:TIGR02729 157 LADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDdGRSFVIADIPGLIEGASEGAGLGHRFLKhIERT 236

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 353238676  131 CNLIFIV----LDVLKPLHDKKILEDELEGFGIRLNKKP 165
Cdd:TIGR02729 237 RVLLHLIdispEDGSDPVEDYEIIRNELKKYSPELAEKP 275
obgE PRK12299
GTPase CgtA; Reviewed
 54-165 1.67e-23

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 99.37  E-value: 1.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  54 ASVGFVGFPSVGKSTLMSKLTGTHSEVAAYEFTTLTSVPGTLRL-HGSPIQIIDLPGIIEGAKDGRGRGRQVIA-VARTC 131
Cdd:PRK12299 159 ADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVdDYKSFVIADIPGLIEGASEGAGLGHRFLKhIERTR 238

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 353238676 132 NLIFIV-LDVLKPLHDKKILEDELEGFGIRLNKKP 165
Cdd:PRK12299 239 LLLHLVdIEAVDPVEDYKTIRNELEKYSPELADKP 273
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
 53-298 2.52e-23

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: 99.28  E-value: 2.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  53 VASVGFVGFPSVGKSTLMSKLTGTHSEVAAYEFTTLTSVPGTLRL-HGSPIQIIDLPGIIEGAKDGRGRG----RQviaV 127
Cdd:COG0536  157 LADVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVgDGRSFVIADIPGLIEGASEGAGLGhrflRH---I 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 128 ARTCNLIFIV----LDVLKPLHDKKILEDELEGFGIRLNKKPpnitvkkkekggepshlsriCWLtrlgiaitntvpltn 203
Cdd:COG0536  234 ERTRVLLHVVdaapLDGRDPVEDYEIIRNELEAYSPELAEKP--------------------RIV--------------- 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 204 idheeikavlseyrlancdvairepgctaddlvdviegnrvyipciyVLNKIDAISIEELDLL------YKIPHsVPISS 277
Cdd:COG0536  279 -----------------------------------------------VLNKIDLLDAEELEELkaelekLGGPV-FPISA 310

                        250       260
                 ....*....|....*....|.
gi 353238676 278 KEWLNIDELLDALWNALNLVR 298
Cdd:COG0536  311 VTGEGLDELLYALAELLEELR 331
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 56-221 2.58e-22

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: 92.05  E-value: 2.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676   56 VGFVGFPSVGKSTLMSKLTGTH-SEVAAYEFTTLTSVPGTLRLHGSP--IQIIDLPGIIEGAKDGRGRGRQVIAVARTCN 132
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKgSITEYYPGTTRNYVTTVIEEDGKTykFNLLDTAGQEDYDAIRRLYYPQVERSLRVFD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  133 LIFIVLDVLKPLH-DKKILEDELE-GFGIRLN-KKPPNITVKKKEKggepshlsricwlTRLGIAITNTVPLTNIDHEEI 209
Cdd:TIGR00231  84 IVILVLDVEEILEkQTKEIIHHADsGVPIILVgNKIDLKDADLKTH-------------VASEFAKLNGEPIIPLSAETG 150

                         170
                  ....*....|..
gi 353238676  210 KAVLSEYRLANC 221
Cdd:TIGR00231 151 KNIDSAFKIVEA 162
obgE PRK12297
GTPase CgtA; Reviewed
 54-165 8.99e-21

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 92.86  E-value: 8.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  54 ASVGFVGFPSVGKSTLMSKLTGTHSEVAAYEFTTLTSVPGTLRL-HGSPIQIIDLPGIIEGAKDGRGRGRQVIA-VARTC 131
Cdd:PRK12297 159 ADVGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETdDGRSFVMADIPGLIEGASEGVGLGHQFLRhIERTR 238

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 353238676 132 NLIFIV----LDVLKPLHDKKILEDELEGFGIRLNKKP 165
Cdd:PRK12297 239 VIVHVIdmsgSEGRDPIEDYEKINKELKLYNPRLLERP 276
TGS pfam02824
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ...
 297-372 2.98e-19

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: 80.67  E-value: 2.98e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 353238676  297 VRVYTkPRGLAPDYsapvvlkRNKATVEDFCNAIHKEIAKQLKYAIVWgtsakhsrGQKVGLDHELQDEDVVHIVK 372
Cdd:pfam02824   1 IRVYT-PDGKVPDL-------PRGATPEDFAYAIHTSLAKKFIYAKVN--------GQLVGLDHPLEDGDVVEIVT 60
obgE PRK12298
GTPase CgtA; Reviewed
 53-165 4.80e-17

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 81.84  E-value: 4.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  53 VASVGFVGFPSVGKSTLMSKLTGTHSEVAAYEFTTLtsVP--GTLRL-HGSPIQIIDLPGIIEGAKDGRGRG-RQVIAVA 128
Cdd:PRK12298 159 LADVGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTL--VPnlGVVRVdDERSFVVADIPGLIEGASEGAGLGiRFLKHLE 236

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 353238676 129 RTCNLIFIV----LDVLKPLHDKKILEDELEGFGIRLNKKP 165
Cdd:PRK12298 237 RCRVLLHLIdiapIDGSDPVENARIIINELEKYSPKLAEKP 277
PRK09602 PRK09602
translation-associated GTPase; Reviewed
 55-371 1.18e-15

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 77.54  E-value: 1.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  55 SVGFVGFPSVGKSTLMSKLTGTHSEVAAYEFTT--------------------LTSVPGTLRLHGS----PIQIIDLPGI 110
Cdd:PRK09602   3 TIGLVGKPNVGKSTFFNAATLADVEIANYPFTTidpnvgvayvrvecpckelgVKCNPRNGKCIDGtrfiPVELIDVAGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 111 IEGAKDGRGRGRQVIAVARTCNLIFIVLDVL---------------KPLHDKKILEDELEG--FGIrLNKkppNItvKKK 173
Cdd:PRK09602  83 VPGAHEGRGLGNQFLDDLRQADALIHVVDASgstdeegnpvepgshDPVEDIKFLEEELDMwiYGI-LEK---NW--EKF 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 174 EKGGEPSHLsricwltRLGIAITNTVPLTNIDHEEIKAVLSEyrlanCDVAIREPGCTADDLVDVIEGNRVYI-PCIYVL 252
Cdd:PRK09602 157 SRKAQAEKF-------DIEEALAEQLSGLGINEEHVKEALRE-----LGLPEDPSKWTDEDLLELARELRKISkPMVIAA 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 253 NKIDAISIEE-LDLLYKIPHS--VPISS-----------------------------------------KEWLN------ 282
Cdd:PRK09602 225 NKADLPPAEEnIERLKEEKYYivVPTSAeaelalrraakaglidyipgdsdfeilgelsekqkkaleyiREVLKkyggtg 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 283 IDELLD-ALWNALNLVRVY--------TKPRG-LAPDysaPVVLKRNkATVEDFCNAIHKEIAKQLKYAIvwgtSAKhsR 352
Cdd:PRK09602 305 VQEAINtAVFDLLDMIVVYpvedenklTDKKGnVLPD---AFLLPKG-STARDLAYKIHTDIGEGFLYAI----DAR--T 374

                        410
                 ....*....|....*....
gi 353238676 353 GQKVGLDHELQDEDVVHIV 371
Cdd:PRK09602 375 KRRIGEDYELKDGDVIKIV 393
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 57-163 2.80e-15

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: 72.66  E-value: 2.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  57 GFVGFPSVGKSTLMSKLTGTH-SEVAAYEFTTLTSVPGTLRLHGS-PIQIIDLPGIIEGAKDGRGRGRQVIAVARTCNLI 134
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNvGIVSPIPGTTRDPVRKEWELLPLgPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 353238676 135 FIVLDVLKPLHDKKILEDELEGFGIR----LNK 163
Cdd:cd00880   81 LLVVDSDLTPVEEEAKLGLLRERGKPvllvLNK 113
obgE PRK12296
GTPase CgtA; Reviewed
 53-161 7.10e-14

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 72.59  E-value: 7.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  53 VASVGFVGFPSVGKSTLMSKLTGTHSEVAAYEFTTLtsVP--GTLRLHGSPIQIIDLPGIIEGAKDGRGRGRQVIAVART 130
Cdd:PRK12296 159 VADVGLVGFPSAGKSSLISALSAAKPKIADYPFTTL--VPnlGVVQAGDTRFTVADVPGLIPGASEGKGLGLDFLRHIER 236

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 353238676 131 CNLIFIVLDVL------KPLHDKKILEDELEGFGIRL 161
Cdd:PRK12296 237 CAVLVHVVDCAtlepgrDPLSDIDALEAELAAYAPAL 273
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
 56-277 8.26e-12

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: 65.33  E-value: 8.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  56 VGFVGFPSVGKSTLMSKLTGTHSEVAAYEFTT--------------------LTSVPGT------LRLHgsPIQIIDLPG 109
Cdd:cd01899    1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTidpnvgvgyvrvecpckelgVSCNPRYgkcidgKRYV--PVELIDVAG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 110 IIEGAKDGRGRGRQVIAVARTCNLIFIVLDVL---------------KPLHDKKILEDELEG--FGIrLNKKPPNItVKK 172
Cdd:cd01899   79 LVPGAHEGKGLGNQFLDDLRDADVLIHVVDASggtdaegngvetggyDPLEDIEFLENEIDMwiYGI-LERNWEKI-VRK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 173 KEKGGepshlsricwlTRLGIAITNTVPLTNIDHEEIKAVLSEYRLancdvAIREPGCTADDLVDVIEGNRVYI-PCIYV 251
Cdd:cd01899  157 AKAEK-----------TDIVEALSEQLSGFGVNEDVVIEALEELEL-----PADLSKWDDEDLLRLARELRKRRkPMVIA 220

                        250       260       270
                 ....*....|....*....|....*....|
gi 353238676 252 LNKIDAIS----IEELDLLYKIPHSVPISS 277
Cdd:cd01899  221 ANKADIPDaeenISKLRLKYPDEIVVPTSA 250
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 57-215 9.52e-11

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: 59.78  E-value: 9.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  57 GFVGFPSVGKSTLMSKLTG-THSEVAAYEFTTLTSVPGTLRLHGS--PIQIIDLPGIIEGakDGRGRGRQVIAVARTCNL 133
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGgEVGEVSDVPGTTRDPDVYVKELDKGkvKLVLVDTPGLDEF--GGLGREELARLLLRGADL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 134 IFIVLDVLKPLHDKKI---LEDELEGFGIR----LNK--KPPNITVKKKEKGGEpshlsricwltRLGIAITNTVPLTNI 204
Cdd:cd00882   79 ILLVVDSTDRESEEDAkllILRRLRKEGIPiilvGNKidLLEEREVEELLRLEE-----------LAKILGVPVFEVSAK 147

                        170
                 ....*....|.
gi 353238676 205 DHEEIKAVLSE 215
Cdd:cd00882  148 TGEGVDELFEK 158
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
60-112 1.37e-10

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 61.77  E-value: 1.37e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 353238676  60 GFPSVGKSTLMSKLTGTHSEVAAYEFTTLTSVPGTLRLHGSPIQIIDLPGIIE 112
Cdd:COG1084  167 GYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGRYQVIDTPGLLD 219
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 58-110 1.48e-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: 56.31  E-value: 1.48e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 353238676  58 FVGFPSVGKSTLMSKLTGTHSEVAAYEFTTLTSVPGTLRLHGSPIQIIDLPGI 110
Cdd:cd01879    2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPGT 54
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 60-110 2.36e-09

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: 56.03  E-value: 2.36e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 353238676  60 GFPSVGKSTLMSKLTGTHSEVAAYEFTTLTSVPGTLRLHGSPIQIIDLPGI 110
Cdd:cd01897    7 GYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLRWQVIDTPGI 57
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 56-110 3.78e-09

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


Pssm-ID: 460552 [Multi-domain]  Cd Length: 156  Bit Score: 55.15  E-value: 3.78e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 353238676   56 VGFVGFPSVGKSTLMSKLTGTHSEVAAYEFTTLTSVPGTLRLHGSPIQIIDLPGI 110
Cdd:pfam02421   3 IALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFKYKGYEIEIVDLPGI 57
TGS_Obg cd04938
TGS (ThrRS, GTPase and SpoT) domain found in the Obg protein family; The Obg family of GTPases ...
 295-371 7.44e-09

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: 52.06  E-value: 7.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 295 NLVRVYTKPRG-------LAPDYSAPVVLKrNKATVEDFCNAIHKEIAKQLKYAIVWGTSakhsrgQKVGLDHELQDEDV 367
Cdd:cd04938    1 GLIPVYPVKNIqtftngsGNSVFRDCVLVK-KGTTVKDFANKIHTDLEKGFINAEGIGGR------RLEGEDYILQDNDV 73


                 ....
gi 353238676 368 VHIV 371
Cdd:cd04938   74 VKFT 77
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 246-294 1.28e-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: 1.28e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 353238676 246 IPCIYVLNKIDAISIEELD-LLYKIPHSVPISSKEWLNIDELLDALWNAL 294
Cdd:COG2262  312 KPIILVFNKIDLLDDEELErLRAGYPDAVFISAKTGEGIDELLEAIEERL 361
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
56-110 1.56e-07

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 53.20  E-value: 1.56e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 353238676  56 VGFVGFPSVGKSTLMSKLTGTHSEVAAYEFTTLTSVPGTLRLHGSPIQIIDLPGI 110
Cdd:COG0370    6 IALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKGKEIELVDLPGT 60
TGS_MJ1332_like cd01669
TGS (ThrRS, GTPase and SpoT) domain found in Methanocaldococcus jannaschii uncharacterized ...
 314-371 4.27e-07

TGS (ThrRS, GTPase and SpoT) domain found in Methanocaldococcus jannaschii uncharacterized GTP-binding protein MJ1332 and similar proteins; This family includes a group of uncharacterized GTP-binding proteins from archaea, which belong to the Obg family of GTPases. The family members contain a domain of characteristic Obg-type G-motifs that may be the core of GTPase activity, as well as a C-terminal TGS (ThrRS, GTPase and SpoT) domain that has a predominantly beta-grasp ubiquitin-like fold.


Pssm-ID: 340460 [Multi-domain]  Cd Length: 78  Bit Score: 46.92  E-value: 4.27e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 353238676 314 VVLKRNkATVEDFCNAIHKEIAKQLKYAIvwgtSAKhsRGQKVGLDHELQDEDVVHIV 371
Cdd:cd01669   27 ILLKRG-STPRDLAYKIHTDLGKGFLYAI----DAR--TKMRLGEDYELKHGDVVKIV 77
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 246-290 8.10e-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: 48.99  E-value: 8.10e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 353238676 246 IPCIYVLNKIDAISIEELD--LLYKIPHSVPISSKEWLNIDELLDAL 290
Cdd:cd01878  154 IPIILVLNKIDLLDDEELEerLRAGRPDAVFISAKTGEGLDLLKEAI 200
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 55-154 5.12e-06

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 48.02  E-value: 5.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  55 SVGFVGFPSVGKSTLMSKLTGTHSEVAAYEFTTL------TSVP-----------GTLRLHGSPIQIIDLPGIIEGAKDG 117
Cdd:PTZ00258  23 KMGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIdpntarVNVPderfdwlckhfKPKSIVPAQLDITDIAGLVKGASEG 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 353238676 118 RGRGRQVIAVARTCNLIFIVL------------DVLKPLHDKKILEDEL 154
Cdd:PTZ00258 103 EGLGNAFLSHIRAVDGIYHVVrafededithveGEIDPVRDLEIISSEL 151
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 59-140 8.88e-06

EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206681 [Multi-domain]  Cd Length: 157  Bit Score: 45.12  E-value: 8.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  59 VGFPSVGKSTLMSKLTGTHSE-VAAYEFTTLTSVPGTLRLHGSPIQIIDLPGIIEGAK--DGRGRgRQVIAVARTCNLIF 135
Cdd:cd01894    3 VGRPNVGKSTLFNRLTGRRDAiVSDTPGVTRDRKYGEAEWGGREFILIDTGGIEPDDEgiSKEIR-EQAEIAIEEADVIL 81


                 ....*
gi 353238676 136 IVLDV 140
Cdd:cd01894   82 FVVDG 86
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
 60-110 1.94e-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: 46.66  E-value: 1.94e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 353238676   60 GFPSVGKSTLMSKLTGTHSEVAAYEFTTLTSVPGTLRLHGSPIQIIDLPGI 110
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGFQGEDIEIVDLPGI 51
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 56-163 2.69e-05

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: 44.35  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  56 VGFVGFPSVGKSTLMSKLTGTH----SEVAAyefTTLTSVPGTLRLHGSPIQIIDLPGIiegakdgRGRGRQV-----IA 126
Cdd:cd01895    5 IAIIGRPNVGKSSLLNALLGEErvivSDIAG---TTRDSIDVPFEYDGQKYTLIDTAGI-------RKKGKVTegiekYS 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 353238676 127 VART------CNLIFIVLDVLKPLH--DKKIL---EDELEGFGIRLNK 163
Cdd:cd01895   75 VLRTlkaierADVVLLVLDASEGITeqDLRIAgliLEEGKALIIVVNK 122
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 57-143 6.03e-05

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: 42.71  E-value: 6.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  57 GFVGFPSVGKSTLMSKLTGTH-SEVAAYEFTTLTSVPGTLRLHGSPIQIIDLPGIIEGAKDGRGRGRQVIAVARTCNLIF 135
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTEvAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPGVGERGRRDREYEELYRRLLPEADLVL 80


                 ....*...
gi 353238676 136 IVLDVLKP 143
Cdd:cd11383   81 WLLDADDR 88
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 246-290 2.61e-04

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


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 41.29  E-value: 2.61e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 353238676 246 IPCIYVLNKIDAIS--------IEELDLLYKIPHSVPISSKEWLNIDELLDAL 290
Cdd:cd04163  112 TPVILVLNKIDLVKdkedllplLEKLKELHPFAEIFPISALKGENVDELLEYI 164
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 56-216 3.73e-04

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


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 40.91  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  56 VGFVGFPSVGKSTLMSKLTGTHseVAAyefttLTSVPGTLR------LHGSPIQII--DLPGIIEG-AKDGRGRGRQVIA 126
Cdd:cd04163    6 VAIIGRPNVGKSTLLNALVGQK--ISI-----VSPKPQTTRnrirgiYTDDDAQIIfvDTPGIHKPkKKLGERMVKAAWS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676 127 VARTCNLIFIVLDVLKPL--HDKKILEdelegfGIRLNKKPPNITVKKKEKGGEPSHLSRICWLTRLGIAITNTVP---L 201
Cdd:cd04163   79 ALKDVDLVLFVVDASEWIgeGDEFILE------LLKKSKTPVILVLNKIDLVKDKEDLLPLLEKLKELHPFAEIFPisaL 152

                        170
                 ....*....|....*
gi 353238676 202 TNIDHEEIKAVLSEY 216
Cdd:cd04163  153 KGENVDELLEYIVEY 167
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
 56-112 4.06e-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: 41.61  E-value: 4.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 353238676   56 VGFVGFPSVGKSTLMSKLTGTH-SEVAAYEFTTLTSVPGTLRLHGSPIQIIDLPGIIE 112
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHGQKiSITSPKAQTTRNRISGIHTTGASQIIFIDTPGFHE 60
EHD cd09913
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ...
 102-143 4.75e-04

Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain (EHD) proteins regulate endocytic events; they have been linked to a number of Rab proteins through their association with mutual effectors, suggesting a coordinate role in endocytic regulation. Eukaryotic EHDs comprise four members (EHD1-4) in mammals and single members in Caenorhabditis elegans (Rme-1), Drosophila melanogaster (Past1) as well as several eukaryotic parasites. EHD1 regulates trafficking of multiple receptors from the endocytic recycling compartment (ERC) to the plasma membrane; EHD2 regulates trafficking from the plasma membrane by controlling Rac1 activity; EHD3 regulates endosome-to-Golgi transport, and preserves Golgi morphology; EHD4 is involved in the control of trafficking at the early endosome and regulates exit of cargo toward the recycling compartment as well as late endocytic pathway. Rme-1, an ortholog of human EHD1, controls the recycling of internalized receptors from the endocytic recycling compartment to the plasma membrane. In D. melanogaster, deletion of the Past1 gene leads to infertility as well as premature death of adult flies. Arabidopsis thaliana also has homologs of EHD proteins (AtEHD1 and AtEHD2), possibly involved in regulating endocytosis and signaling.


Pssm-ID: 206740  Cd Length: 241  Bit Score: 41.11  E-value: 4.75e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 353238676 102 IQIIDLPGIIEGAKDGRGRGRQVIAVAR----TCNLIFIVLDVLKP 143
Cdd:cd09913   90 VTIVDTPGILSGEKQRQSRGYDFNAVCRwfaeRADLIFLLFDPHKL 135
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
246-290 8.26e-04

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 40.74  E-value: 8.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 353238676 246 IPCIYVLNKIDAIS-------IEELDLLYKIPHSVPISSKEWLNIDELLDAL 290
Cdd:COG1159  112 TPVILVINKIDLVKkeellplLAEYSELLDFAEIVPISALKGDNVDELLDEI 163
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 59-152 9.55e-04

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: 39.40  E-value: 9.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  59 VGFPSVGKSTLMSKLTGthSEVAayeftTLTSVPGTLR--------LHGSPIQIIDLPGI------IEgaKDGRGRGRQV 124
Cdd:cd04164    9 AGKPNVGKSSLLNALAG--RDRA-----IVSDIAGTTRdvieeeidLGGIPVRLIDTAGLretedeIE--KIGIERAREA 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 353238676 125 IAVArtcNLIFIVLDVLKPL--HDKKILED 152
Cdd:cd04164   80 IEEA---DLVLLVVDASEGLdeEDLEILEL 106
TGS_RSH cd01668
TGS (ThrRS, GTPase and SpoT) domain found in the RelA/SpoT homolog (RSH) family; The RelA/SpoT ...
 321-371 9.59e-04

TGS (ThrRS, GTPase and SpoT) domain found in the RelA/SpoT homolog (RSH) family; The RelA/SpoT homolog (RSH) family consists of long RSH proteins and short RSH proteins. Long RSH proteins have been characterized as containing an N-terminal region and a C-terminal region. The N-terminal region contains a pseudo-hydrolase (inactive-hydrolase) domain and a (p)ppGpp synthetase domain. The C-terminal region contains a ubiquitin-like TGS (ThrRS, GTPase and SpoT) domain, a conserved cysteine domain (CC), helical and ACT (aspartate kinase, chorismate mutase, TyrA domain) domains connected by a linker region. Short RSH proteins have a truncated C-terminal region without ACT domain. The RSH family includes two classes of enzyme: i) monofunctional (p)ppGpp synthetase I, RelA, and ii) bifunctional (p)ppGpp synthetase II/hydrolase, SpoT (also called Rel). Both classes are capable of synthesizing (p)ppGpp but only bifunctional enzymes are capable of (p)ppGpp hydrolysis. SpoT is a ribosome-associated protein that is activated during amino acid starvation and thought to mediate the stringent response. The function of the TGS domain of SpoT is in transcription of survival and virulence genes in respond to environmental stress. RelA is an ATP:GTP(GDP) pyrophosphate transferase that is recruited to stalled ribosomes and activated to synthesize (p)ppGpp, which acts as a pleiotropic secondary messenger.


Pssm-ID: 340459 [Multi-domain]  Cd Length: 59  Bit Score: 37.12  E-value: 9.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 353238676 321 ATVEDFCNAIHKEIAKQLKYAIVwgtsakhsRGQKVGLDHELQDEDVVHIV 371
Cdd:cd01668   16 ATPIDFAYAIHTDVGNKCVGAKV--------NGKIVPLDYVLKNGDVVEII 58
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 247-290 1.13e-03

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: 40.54  E-value: 1.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 353238676  247 PCIYVLNKIDAISIEELDLLYKIPHSVPISSKEWLNIDELLDAL 290
Cdd:pfam12631 203 PIIVVLNKSDLLGEIDELEELKGKPVLAISAKTGEGLDELEEAI 246
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
56-150 1.43e-03

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 40.39  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  56 VGFVGFPSVGKSTLMSKLTGthsevaaYEFTTLTSVPGTLR--------LHGSPIQIIDLPGIiegakdgRGRGRQV--- 124
Cdd:COG1160  178 IAIVGRPNVGKSSLINALLG-------EERVIVSDIAGTTRdsidtpfeRDGKKYTLIDTAGI-------RRKGKVDegi 243

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 353238676 125 --IAVART------CNLIFIVLDVLKPLH--DKKIL 150
Cdd:COG1160  244 ekYSVLRTlraierADVVLLVIDATEGITeqDLKIA 279
era PRK00089
GTPase Era; Reviewed
 242-290 1.47e-03

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 40.03  E-value: 1.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 353238676 242 NRVYIPCIYVLNKIDAIS--------IEELDLLYKIPHSVPISSKEWLNIDELLDAL 290
Cdd:PRK00089 110 KKVKTPVILVLNKIDLVKdkeellplLEELSELMDFAEIVPISALKGDNVDELLDVI 166
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 50-183 1.51e-03

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: 40.16  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676   50 RTGVaSVGFVGFPSVGKSTLMSKLTGThsEVAayeftTLTSVPGT--------LRLHGSPIQIIDLPGI------IEgaK 115
Cdd:pfam12631  92 REGI-KVVIVGKPNVGKSSLLNALLGE--ERA-----IVTDIPGTtrdvieetINIGGIPLRLIDTAGIretddeVE--K 161

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 353238676  116 DGRGRGRQVIAvarTCNLIFIVLDVLKPLH--DKKILEDELEGFGIR--LNKK--PPNITVKKKEKGGEPSHLS 183
Cdd:pfam12631 162 IGIERAREAIE---EADLVLLVLDASRPLDeeDLEILELLKDKKPIIvvLNKSdlLGEIDELEELKGKPVLAIS 232
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 247-290 1.53e-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: 38.63  E-value: 1.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 353238676 247 PCIYVLNKIDAISIEELDLLYKIPHSVPISSKEWLNIDELLDAL 290
Cdd:cd04164  111 PVIVVLNKSDLLSDAEGISELNGKPIIAISAKTGEGIDELKEAL 154
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
56-151 2.55e-03

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 39.20  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  56 VGFVGFPSVGKSTLMSKLTGTHseVAAyefttLTSVPGTLR------LHGSPIQII--DLPGIIEgAKDGRGRG--RQVI 125
Cdd:COG1159    6 VAIVGRPNVGKSTLLNALVGQK--VSI-----VSPKPQTTRhrirgiVTREDAQIVfvDTPGIHK-PKRKLGRRmnKAAW 77

                         90       100
                 ....*....|....*....|....*...
gi 353238676 126 AVARTCNLIFIVLDVLKPLH--DKKILE 151
Cdd:COG1159   78 SALEDVDVILFVVDATEKIGegDEFILE 105
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 54-110 2.75e-03

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: 38.07  E-value: 2.75e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 353238676  54 ASVGFVGFPSVGKSTLMSKLTGTHS-------EVAAYefttlTSVPGTLRLhGSPIQIIDLPGI 110
Cdd:cd01859  100 VIVGVVGYPKVGKSSIINALKGRHSastspipGSPGY-----TKGIQLVRI-DSKIYLIDTPGV 157
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 56-150 4.53e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 38.88  E-value: 4.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  56 VGFVGFPSVGKSTLMSKLTGthSEVAayefttLTS-VPGTLR--------LHGSPIQIIDLPGIiegakdgRGRGR---- 122
Cdd:PRK00093 176 IAIIGRPNVGKSSLINALLG--EERV------IVSdIAGTTRdsidtpfeRDGQKYTLIDTAGI-------RRKGKvteg 240

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 353238676 123 -QVIAVART------CNLIFIVLDVLKPL--HDKKIL 150
Cdd:PRK00093 241 vEKYSVIRTlkaierADVVLLVIDATEGIteQDLRIA 277
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 58-110 5.40e-03

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: 37.63  E-value: 5.40e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 353238676  58 FVGFPSVGKSTLMSKL--TGTHSEVAAYEFTTLT--SVPG-TLRLHGSPIQ----IIDLPGI 110
Cdd:cd01855  130 VVGATNVGKSTLINALlkSNGGKVQAQALVQRLTvsPIPGtTLGLIKIPLGegkkLYDTPGI 191
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 246-290 5.95e-03

YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 37.10  E-value: 5.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 353238676 246 IPCIYVLNKIDAISI-----------EELDLLYKIPHSVPISSKEWLNIDELLDAL 290
Cdd:cd01876  111 IPFLIVLTKADKLKKselakvlkkikEELNLFNILPPVILFSSKKGTGIDELRALI 166
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 246-290 6.79e-03

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: 37.12  E-value: 6.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 353238676  246 IPCIYVLNKIDAISIEELD---------LLYKIPHS------VPISSKEWLNIDELLDAL 290
Cdd:pfam00009 122 VPIIVFINKMDRVDGAELEevveevsreLLEKYGEDgefvpvVPGSALKGEGVQTLLDAL 181
 
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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