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Conserved domains on  [gi|71981008|ref|NP_498808|]
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putative GTP-binding protein C02F5.3 [Caenorhabditis elegans]

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];
1-366 1.64e-161

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


:

Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 456.95  E-value: 1.64e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008   1 MGILEKIAEIEHEISRTQKNKATEYHLGLLKAKLAKYRQQLLEPTGKGGAKGEGFDVMKSGDARVAMVGFPSVGKSTLLS 80
Cdd:COG1163   2 MTIEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLLN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  81 SMTSTHSEAAGYEFTTLTCIPGVISYNGANIQLLDLPGIIEGASQGKGRGRQVISVAKTADLILMMLDAGKSDQQKMLLe 160
Cdd:COG1163  82 KLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELEQYDVLK- 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008 161 RELEAVGIRLNKKPPNIYVKQKKVGGVKFTNTVPLThCNEKLIMTVLHEYKIFNADVIFREDCTVDEFIDVIQGNRVYMT 240
Cdd:COG1163 161 EELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLD-LDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRVYKP 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008 241 CLYVYNKVDQISIEEIDRL-ARMPH---HVVISCEMNLNMDYLLEKMWEYLALVRVYTKKPGNAPDLgpEDGIILRGGAT 316
Cdd:COG1163 240 AIVVVNKIDLADEEYVEELkSKLPDgvpVIFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADM--EEPLILRKGST 317

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 71981008 317 IEHCCHALHRSIAAQLRYAIVWGTSTKFSPQRVGLHHKLDHEDVIQIVKK 366
Cdd:COG1163 318 VGDVCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIK 367
 
Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
1-366 1.64e-161

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 456.95  E-value: 1.64e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008   1 MGILEKIAEIEHEISRTQKNKATEYHLGLLKAKLAKYRQQLLEPTGKGGAKGEGFDVMKSGDARVAMVGFPSVGKSTLLS 80
Cdd:COG1163   2 MTIEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLLN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  81 SMTSTHSEAAGYEFTTLTCIPGVISYNGANIQLLDLPGIIEGASQGKGRGRQVISVAKTADLILMMLDAGKSDQQKMLLe 160
Cdd:COG1163  82 KLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELEQYDVLK- 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008 161 RELEAVGIRLNKKPPNIYVKQKKVGGVKFTNTVPLThCNEKLIMTVLHEYKIFNADVIFREDCTVDEFIDVIQGNRVYMT 240
Cdd:COG1163 161 EELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLD-LDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRVYKP 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008 241 CLYVYNKVDQISIEEIDRL-ARMPH---HVVISCEMNLNMDYLLEKMWEYLALVRVYTKKPGNAPDLgpEDGIILRGGAT 316
Cdd:COG1163 240 AIVVVNKIDLADEEYVEELkSKLPDgvpVIFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADM--EEPLILRKGST 317

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 71981008 317 IEHCCHALHRSIAAQLRYAIVWGTSTKFSPQRVGLHHKLDHEDVIQIVKK 366
Cdd:COG1163 318 VGDVCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIK 367
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 63-295 1.47e-158

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: 443.91  E-value: 1.47e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  63 ARVAMVGFPSVGKSTLLSSMTSTHSEAAGYEFTTLTCIPGVISYNGANIQLLDLPGIIEGASQGKGRGRQVISVAKTADL 142
Cdd:cd01896   1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008 143 ILMMLDAGKSDQQKMLLERELEAVGIRLNKKPPNIYVKQKKVGGVKFTNTVPLTHCNEKLIMTVLHEYKIFNADVIFRED 222
Cdd:cd01896  81 ILIVLDATKPEGQREILERELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLTKLDEKTVKAILREYKIHNADVLIRED 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71981008 223 CTVDEFIDVIQGNRVYMTCLYVYNKVDQISIEEIDRLARMPHHVVISCEMNLNMDYLLEKMWEYLALVRVYTK 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 3.84e-64

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: 199.19  E-value: 3.84e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008   185 GGVKFTNTVPLTHCNEKLIMTVLHEYKIFNADVIFREDCTVDEFIDVIQGNRVYMTCLYVYNKVDQISIEEIDRLARMPH 264
Cdd:pfam16897   1 GGINITSTVPLTKLDEETIKAILREYKIHNADVLIREDVTVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDRLAREPD 80

                          90       100
                  ....*....|....*....|....*
gi 71981008   265 HVVISCEMNLNMDYLLEKMWEYLAL 289
Cdd:pfam16897  81 SVPISAEKGLNLDELKERIWEYLGL 105
obgE PRK12297
GTPase CgtA; Reviewed
 63-174 5.02e-20

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 90.55  E-value: 5.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008   63 ARVAMVGFPSVGKSTLLSSMTSTHSEAAGYEFTTLTCIPGVISYNGAN-IQLLDLPGIIEGASQGKGRGRQVIS-VAKTA 140
Cdd:PRK12297 159 ADVGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRsFVMADIPGLIEGASEGVGLGHQFLRhIERTR 238

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 71981008  141 dLILMMLDAGKSD-----QQKMLLERELEAVGIRLNKKP 174
Cdd:PRK12297 239 -VIVHVIDMSGSEgrdpiEDYEKINKELKLYNPRLLERP 276
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
 63-174 1.72e-19

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: 87.86  E-value: 1.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008    63 ARVAMVGFPSVGKSTLLSSMTSTHSEAAGYEFTTLTCIPGVISYNGAN-IQLLDLPGIIEGASQGKGRGRQVIS-VAKTA 140
Cdd:TIGR02729 158 ADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRsFVIADIPGLIEGASEGAGLGHRFLKhIERTR 237

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 71981008   141 dLILMMLDAGKSDQQKML-----LERELEAVGIRLNKKP 174
Cdd:TIGR02729 238 -VLLHLIDISPEDGSDPVedyeiIRNELKKYSPELAEKP 275
 
Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
1-366 1.64e-161

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 456.95  E-value: 1.64e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008   1 MGILEKIAEIEHEISRTQKNKATEYHLGLLKAKLAKYRQQLLEPTGKGGAKGEGFDVMKSGDARVAMVGFPSVGKSTLLS 80
Cdd:COG1163   2 MTIEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLLN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  81 SMTSTHSEAAGYEFTTLTCIPGVISYNGANIQLLDLPGIIEGASQGKGRGRQVISVAKTADLILMMLDAGKSDQQKMLLe 160
Cdd:COG1163  82 KLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELEQYDVLK- 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008 161 RELEAVGIRLNKKPPNIYVKQKKVGGVKFTNTVPLThCNEKLIMTVLHEYKIFNADVIFREDCTVDEFIDVIQGNRVYMT 240
Cdd:COG1163 161 EELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLD-LDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRVYKP 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008 241 CLYVYNKVDQISIEEIDRL-ARMPH---HVVISCEMNLNMDYLLEKMWEYLALVRVYTKKPGNAPDLgpEDGIILRGGAT 316
Cdd:COG1163 240 AIVVVNKIDLADEEYVEELkSKLPDgvpVIFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADM--EEPLILRKGST 317

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 71981008 317 IEHCCHALHRSIAAQLRYAIVWGTSTKFSPQRVGLHHKLDHEDVIQIVKK 366
Cdd:COG1163 318 VGDVCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIK 367
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 63-295 1.47e-158

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: 443.91  E-value: 1.47e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  63 ARVAMVGFPSVGKSTLLSSMTSTHSEAAGYEFTTLTCIPGVISYNGANIQLLDLPGIIEGASQGKGRGRQVISVAKTADL 142
Cdd:cd01896   1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008 143 ILMMLDAGKSDQQKMLLERELEAVGIRLNKKPPNIYVKQKKVGGVKFTNTVPLTHCNEKLIMTVLHEYKIFNADVIFRED 222
Cdd:cd01896  81 ILIVLDATKPEGQREILERELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLTKLDEKTVKAILREYKIHNADVLIRED 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71981008 223 CTVDEFIDVIQGNRVYMTCLYVYNKVDQISIEEIDRLARMPHHVVISCEMNLNMDYLLEKMWEYLALVRVYTK 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 3.84e-64

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: 199.19  E-value: 3.84e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008   185 GGVKFTNTVPLTHCNEKLIMTVLHEYKIFNADVIFREDCTVDEFIDVIQGNRVYMTCLYVYNKVDQISIEEIDRLARMPH 264
Cdd:pfam16897   1 GGINITSTVPLTKLDEETIKAILREYKIHNADVLIREDVTVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDRLAREPD 80

                          90       100
                  ....*....|....*....|....*
gi 71981008   265 HVVISCEMNLNMDYLLEKMWEYLAL 289
Cdd:pfam16897  81 SVPISAEKGLNLDELKERIWEYLGL 105
TGS_DRG2 cd17231
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 2 ...
 286-366 8.75e-49

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: 159.09  E-value: 8.75e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008 286 YLALVRVYTKKPGNAPDLGpeDGIILRGGATIEHCCHALHRSIAAQLRYAIVWGTSTKFSPQRVGLHHKLDHEDVIQIVK 365
Cdd:cd17231   1 YLALIRVYTKKRGERPDFG--DAIILRRGATVEHVCHRIHRTLASQFKYALVWGTSTKYSPQRVGLTHVMEDEDVIQIVK 78


                .
gi 71981008 366 K 366
Cdd:cd17231  79 K 79
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 66-287 5.54e-31

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: 115.57  E-value: 5.54e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  66 AMVGFPSVGKSTLLSSMTSTHSEAAGYEFTTLTCIPGVISY-NGANIQLLDLPGIIEGASQGKGRGRQVISVAKTADLIL 144
Cdd:cd01881   1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFgDGVDIQIIDLPGLLDGASEGRGLGEQILAHLYRSDLIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008 145 MMLDagksdqqkmllereleavgirlnkkppniyvkqkkvggvkftntvplthCNEKLIMTVLHEYKIfnadvIFREdct 224
Cdd:cd01881  81 HVID-------------------------------------------------ASEDCVGDPLEDQKT-----LNEE--- 103

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71981008 225 vdefIDVIQGNRVYMTCLYVYNKVDQISIEEI-----DRLARMPHHVVISCEMNLNMDYLLEKMWEYL 287
Cdd:cd01881 104 ----VSGSFLFLKNKPEMIVANKIDMASENNLkrlklDKLKRGIPVVPTSALTRLGLDRVIRTIRKLL 167
TGS_DRG1 cd17230
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 1 ...
 286-366 1.60e-30

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: 111.21  E-value: 1.60e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008 286 YLALVRVYTKKPGNAPDLgpEDGIILR-GGATIEHCCHALHRSIAAQLRYAIVWGTSTKFSPQRVGLHHKLDHEDVIQIV 364
Cdd:cd17230   1 YLNLVRIYTKPKGQLPDY--EEPVVLRsGKSTVEDFCNKIHKSLIKEFKYALVWGSSVKHNPQRVGKDHVLEDEDVVQIV 78


                ..
gi 71981008 365 KK 366
Cdd:cd17230  79 KK 80
TGS_DRG cd01666
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein ...
 287-365 6.61e-30

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: 109.63  E-value: 6.61e-30
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71981008 287 LALVRVYTKKPGNAPDLgpEDGIILRGGATIEHCCHALHRSIAAQLRYAIVWGTSTKFSPQRVGLHHKLDHEDVIQIVK 365
Cdd:cd01666   1 LGIIRVYTKPPGKKPDF--DEPFILRRGSTVEDVAEKIHKDLAENFKYARVWGKSVKFDGQRVGLDHVLEDGDIVEIHK 77
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 64-173 2.78e-27

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: 103.85  E-value: 2.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008    64 RVAMVGFPSVGKSTLLSSMTSTHSEAAGYEFTTLTCIPGVISYNGANIQLLDLPGIIEGASQGKGRGRQVISVAKtADLI 143
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFLAIIE-ADLI 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 71981008   144 LMMLDagkSDQQKMLLERELEAVGIRLNKK 173
Cdd:pfam01926  80 LFVVD---SEEGITPLDEELLELLRENKKP 106
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 63-174 8.87e-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: 96.34  E-value: 8.87e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  63 ARVAMVGFPSVGKSTLLSSMTSTHSEAAGYEFTTLtcIP--GVISY-NGANIQLLDLPGIIEGASQGKGRG----RQVis 135
Cdd:cd01898   1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTL--VPnlGVVRVdDGRSFVIADIPGLIEGASEGKGLGhrflRHI-- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 71981008 136 vaKTADLILMMLDAGKSD---QQKMLLERELEAVGIRLNKKP 174
Cdd:cd01898  77 --ERTRVLLHVIDLSGEDdpvEDYETIRNELEAYNPGLAEKP 116
obgE PRK12297
GTPase CgtA; Reviewed
 63-174 5.02e-20

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 90.55  E-value: 5.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008   63 ARVAMVGFPSVGKSTLLSSMTSTHSEAAGYEFTTLTCIPGVISYNGAN-IQLLDLPGIIEGASQGKGRGRQVIS-VAKTA 140
Cdd:PRK12297 159 ADVGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRsFVMADIPGLIEGASEGVGLGHQFLRhIERTR 238

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 71981008  141 dLILMMLDAGKSD-----QQKMLLERELEAVGIRLNKKP 174
Cdd:PRK12297 239 -VIVHVIDMSGSEgrdpiEDYEKINKELKLYNPRLLERP 276
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
 63-174 7.58e-20

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: 89.27  E-value: 7.58e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  63 ARVAMVGFPSVGKSTLLSSMTSTHSEAAGYEFTTLTciP--GVISYNGAN-IQLLDLPGIIEGASQGKGRG----RQvis 135
Cdd:COG0536 158 ADVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLV--PnlGVVRVGDGRsFVIADIPGLIEGASEGAGLGhrflRH--- 232

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 71981008 136 VAKTAdLILMMLDAGKSDQQKML-----LERELEAVGIRLNKKP 174
Cdd:COG0536 233 IERTR-VLLHVVDAAPLDGRDPVedyeiIRNELEAYSPELAEKP 275
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
 63-174 1.72e-19

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: 87.86  E-value: 1.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008    63 ARVAMVGFPSVGKSTLLSSMTSTHSEAAGYEFTTLTCIPGVISYNGAN-IQLLDLPGIIEGASQGKGRGRQVIS-VAKTA 140
Cdd:TIGR02729 158 ADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRsFVIADIPGLIEGASEGAGLGHRFLKhIERTR 237

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 71981008   141 dLILMMLDAGKSDQQKML-----LERELEAVGIRLNKKP 174
Cdd:TIGR02729 238 -VLLHLIDISPEDGSDPVedyeiIRNELKKYSPELAEKP 275
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 62-177 1.74e-17

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 78.95  E-value: 1.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008    62 DARVAMVGFPSVGKSTLLSSMTSTH-SEAAGYEFTTLTCIPGVISYNG--ANIQLLDLPGIIEGASQGKGRGRQVISVAK 138
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKgSITEYYPGTTRNYVTTVIEEDGktYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 71981008   139 TADLILMMLDAGKSDQ-QKMLLERELEA-VGIRLNKKPPNI 177
Cdd:TIGR00231  81 VFDIVILVLDVEEILEkQTKEIIHHADSgVPIILVGNKIDL 121
TGS pfam02824
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ...
 290-365 5.19e-17

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: 74.12  E-value: 5.19e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71981008   290 VRVYTKKpGNAPDLgpedgiilRGGATIEHCCHALHRSIAAQLRYAIVWGtstkfspQRVGLHHKLDHEDVIQIVK 365
Cdd:pfam02824   1 IRVYTPD-GKVPDL--------PRGATPEDFAYAIHTSLAKKFIYAKVNG-------QLVGLDHPLEDGDVVEIVT 60
obgE PRK12299
GTPase CgtA; Reviewed
 63-174 1.07e-16

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 80.11  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008   63 ARVAMVGFPSVGKSTLLSSMTSTHSEAAGYEFTTLTCIPGVISY-NGANIQLLDLPGIIEGASQGKGRGRQVIS-VAKTA 140
Cdd:PRK12299 159 ADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVdDYKSFVIADIPGLIEGASEGAGLGHRFLKhIERTR 238

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 71981008  141 dLILMMLDAGKSD--QQKMLLERELEAVGIRLNKKP 174
Cdd:PRK12299 239 -LLLHLVDIEAVDpvEDYKTIRNELEKYSPELADKP 273
obgE PRK12296
GTPase CgtA; Reviewed
 49-130 7.77e-16

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 78.37  E-value: 7.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008   49 GAKGEGFDV---MKSgDARVAMVGFPSVGKSTLLSSMTSTHSEAAGYEFTTLtcIP--GVISYNGANIQLLDLPGIIEGA 123
Cdd:PRK12296 144 GEPGEERDLvleLKS-VADVGLVGFPSAGKSSLISALSAAKPKIADYPFTTL--VPnlGVVQAGDTRFTVADVPGLIPGA 220


                 ....*..
gi 71981008  124 SQGKGRG 130
Cdd:PRK12296 221 SEGKGLG 227
obgE PRK12298
GTPase CgtA; Reviewed
 63-130 2.59e-14

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 73.36  E-value: 2.59e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71981008   63 ARVAMVGFPSVGKSTLLSSMTSTHSEAAGYEFTTLtcIP--GVISY-NGANIQLLDLPGIIEGASQGKGRG 130
Cdd:PRK12298 160 ADVGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTL--VPnlGVVRVdDERSFVVADIPGLIEGASEGAGLG 228
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 66-172 6.90e-12

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: 63.03  E-value: 6.90e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  66 AMVGFPSVGKSTLLSSMTSTH-SEAAGYEFTTLTcipgVISYN-----GANIQLLDLPGIIEGASQGKGRGRQVISVAKT 139
Cdd:cd00880   1 AIFGRPNVGKSSLLNALLGQNvGIVSPIPGTTRD----PVRKEwellpLGPVVLIDTPGLDEEGGLGRERVEEARQVADR 76

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 71981008 140 ADLILMMLDAGKSDQQKMLLERELEAVGIR----LNK 172
Cdd:cd00880  77 ADLVLLVVDSDLTPVEEEAKLGLLRERGKPvllvLNK 113
PRK09602 PRK09602
translation-associated GTPase; Reviewed
 64-364 1.84e-11

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 64.83  E-value: 1.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008   64 RVAMVGFPSVGKSTLLSSMTSTHSEAAGYEFTT--------------------LTCIPGVISYNGAN----IQLLDLPGI 119
Cdd:PRK09602   3 TIGLVGKPNVGKSTFFNAATLADVEIANYPFTTidpnvgvayvrvecpckelgVKCNPRNGKCIDGTrfipVELIDVAGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  120 IEGASQGKGRGRQVISVAKTADLILMMLDA-GKSDQQ---------------KMlLERELE--------------AVGIR 169
Cdd:PRK09602  83 VPGAHEGRGLGNQFLDDLRQADALIHVVDAsGSTDEEgnpvepgshdpvediKF-LEEELDmwiygileknwekfSRKAQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  170 LNKKPPNIYVKQKKVG-GVkftntvplthcNEKLIMTVLHEYKIFNADVIFREDcTVDEFIDVIQgnRVYMTCLYVYNKV 248
Cdd:PRK09602 162 AEKFDIEEALAEQLSGlGI-----------NEEHVKEALRELGLPEDPSKWTDE-DLLELARELR--KISKPMVIAANKA 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  249 DQISIEE-IDRLARMPHHVVISC----EMNLNM-------DYL-------------------LEKMWEYLA--------- 288
Cdd:PRK09602 228 DLPPAEEnIERLKEEKYYIVVPTsaeaELALRRaakagliDYIpgdsdfeilgelsekqkkaLEYIREVLKkyggtgvqe 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  289 -----------LVRVY--------TKKPGNA-PDLgpedgIILRGGATIEHCCHALHRSIAAQLRYAIvwGTSTKfspQR 348
Cdd:PRK09602 308 aintavfdlldMIVVYpvedenklTDKKGNVlPDA-----FLLPKGSTARDLAYKIHTDIGEGFLYAI--DARTK---RR 377

                        410
                 ....*....|....*.
gi 71981008  349 VGLHHKLDHEDVIQIV 364
Cdd:PRK09602 378 IGEDYELKDGDVIKIV 393
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
 65-268 1.93e-11

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: 64.17  E-value: 1.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  65 VAMVGFPSVGKSTLLSSMTSTHSEAAGYEFTT------------------LTCIPGVISYNGAN------IQLLDLPGII 120
Cdd:cd01899   1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTidpnvgvgyvrvecpckeLGVSCNPRYGKCIDgkryvpVELIDVAGLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008 121 EGASQGKGRGRQVISVAKTADLILMMLDA-GKSDQQK--------------MLLERELEA-VGIRLNKKPPNIyVKQKKV 184
Cdd:cd01899  81 PGAHEGKGLGNQFLDDLRDADVLIHVVDAsGGTDAEGngvetggydplediEFLENEIDMwIYGILERNWEKI-VRKAKA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008 185 GGVKFTNTV--PLT--HCNEKLIMTVLHEyKIFNADVIFREDCTVDEFIDVIQgnRVYMTCLYVYNKVDQISIEEIDRLA 260
Cdd:cd01899 160 EKTDIVEALseQLSgfGVNEDVVIEALEE-LELPADLSKWDDEDLLRLARELR--KRRKPMVIAANKADIPDAEENISKL 236

                       250
                ....*....|
gi 71981008 261 RM--PHHVVI 268
Cdd:cd01899 237 RLkyPDEIVV 246
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
52-160 2.06e-10

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 61.39  E-value: 2.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  52 GEGFDVMK-----SGDARVAMV-GFPSVGKSTLLSSMTSTHSEAAGYEFTTLTCIPGVISYNGANIQLLDLPGI------ 119
Cdd:COG1084 144 NEARNKLRklpdiDPDLPTIVVaGYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGRYQVIDTPGLldrpls 223

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 71981008 120 ----IEgasqgkgrgRQVISVAKT-ADLILMMLDAGKS-----DQQKMLLE 160
Cdd:COG1084 224 erneIE---------RQAILALKHlADVILFLFDPSETcgyslEEQLNLLE 265
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 66-172 5.39e-10

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 57.47  E-value: 5.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  66 AMVGFPSVGKSTLLSSMT-STHSEAAGYEFTTLTCIPGVISYNGA--NIQLLDLPGIIEGasQGKGRGRQVISVAKTADL 142
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLgGEVGEVSDVPGTTRDPDVYVKELDKGkvKLVLVDTPGLDEF--GGLGREELARLLLRGADL 78

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 71981008 143 ILMMLDAGK---SDQQKMLLERELEAVGIR----LNK 172
Cdd:cd00882  79 ILLVVDSTDresEEDAKLLILRRLRKEGIPiilvGNK 115
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 64-172 6.01e-08

EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 52.05  E-value: 6.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  64 RVAMVGFPSVGKSTLLSSMT----STHSEAAGyefTTLTCIPGVISYNGANIQLLDLPGIIEgasqgKGRGRQVI---SV 136
Cdd:cd01895   4 KIAIIGRPNVGKSSLLNALLgeerVIVSDIAG---TTRDSIDVPFEYDGQKYTLIDTAGIRK-----KGKVTEGIekySV 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 71981008 137 AKT------ADLILMMLDA--GKSDQQKMLLERELE---AVGIRLNK 172
Cdd:cd01895  76 LRTlkaierADVVLLVLDAseGITEQDLRIAGLILEegkALIIVVNK 122
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 69-119 2.81e-07

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: 49.87  E-value: 2.81e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 71981008  69 GFPSVGKSTLLSSMTSTHSEAAGYEFTTLTCIPGVISYNGANIQLLDLPGI 119
Cdd:cd01897   7 GYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLRWQVIDTPGI 57
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
58-172 4.89e-07

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 50.76  E-value: 4.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  58 MKSGdaRVAMVGFPSVGKSTLLS-------SMTSTHSEaagyefTTLTCIPGVISYNGANIQLLDLPGIIEGASQ-GKGR 129
Cdd:COG1159   1 FRSG--FVAIVGRPNVGKSTLLNalvgqkvSIVSPKPQ------TTRHRIRGIVTREDAQIVFVDTPGIHKPKRKlGRRM 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 71981008 130 GRQVISVAKTADLILMMLDAGK--SDQQKMLLEReLEAVGIR----LNK 172
Cdd:COG1159  73 NKAAWSALEDVDVILFVVDATEkiGEGDEFILEL-LKKLKTPvilvINK 120
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 66-119 2.55e-06

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: 46.68  E-value: 2.55e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 71981008  66 AMVGFPSVGKSTLLSSMTSTHSEAAGYEFTTLTCIPGVISYNGANIQLLDLPGI 119
Cdd:cd01879   1 ALVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPGT 54
era PRK00089
GTPase Era; Reviewed
 58-174 5.52e-06

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 47.35  E-value: 5.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008   58 MKSGdaRVAMVGFPSVGKSTLLS-------SMTSTHSEaagyefTTLTCIPGVISYNGANIQLLDLPGIIEGASQ-GKGR 129
Cdd:PRK00089   3 FKSG--FVAIVGRPNVGKSTLLNalvgqkiSIVSPKPQ------TTRHRIRGIVTEDDAQIIFVDTPGIHKPKRAlNRAM 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 71981008  130 GRQVISVAKTADLILMMLDAGK--SDQQKMLLEReleavgIRLNKKP 174
Cdd:PRK00089  75 NKAAWSSLKDVDLVLFVVDADEkiGPGDEFILEK------LKKVKTP 115
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 58-151 1.21e-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: 45.14  E-value: 1.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  58 MKSGdaRVAMVGFPSVGKSTLL-------SSMTSTHSEaagyefTTLTCIPGVISYNGANIQLLDLPGIIEGASQ-GKGR 129
Cdd:cd04163   1 FKSG--FVAIIGRPNVGKSTLLnalvgqkISIVSPKPQ------TTRNRIRGIYTDDDAQIIFVDTPGIHKPKKKlGERM 72

                        90       100
                ....*....|....*....|..
gi 71981008 130 GRQVISVAKTADLILMMLDAGK 151
Cdd:cd04163  73 VKAAWSALKDVDLVLFVVDASE 94
BMS1 cd01882
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ...
 65-149 1.88e-05

Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is an essential, evolutionarily conserved, nucleolar protein. Its depletion interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. Bms1, the putative endonuclease Rc11, and the essential U3 small nucleolar RNA form a stable subcomplex that is believed to control an early step in the formation of the 40S subumit. The C-terminal domain of Bms1 contains a GTPase-activating protein (GAP) that functions intramolecularly. It is believed that Rc11 activates Bms1 by acting as a guanine-nucleotide exchange factor (GEF) to promote GDP/GTP exchange, and that activated (GTP-bound) Bms1 delivers Rc11 to the preribosomes.


Pssm-ID: 206669 [Multi-domain]  Cd Length: 231  Bit Score: 45.41  E-value: 1.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  65 VAMVGFPSVGKSTLLSSMTSTHSEaagyefTTLTCIPG---VISYNGANIQLLDLPGIIEGasqgkgrgrqVISVAKTAD 141
Cdd:cd01882  42 VVVVGPPGVGKSTLIRSLIKRYTK------QNLSDIKGpitIVTGKKRRLTFIECPNDINS----------MIDVAKIAD 105


                ....*...
gi 71981008 142 LILMMLDA 149
Cdd:cd01882 106 LVLLLIDG 113
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 64-119 2.85e-05

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: 44.06  E-value: 2.85e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71981008  64 RVAMVGFPSVGKSTLLSSMTSTHSEAAGYEfttltciPGV------ISYNGaNIQLLDLPGI 119
Cdd:cd01856 117 RAMVVGIPNVGKSTLINRLRGKKVAKVGNK-------PGVtrgqqwIRIGP-NIELLDTPGI 170
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
64-119 3.51e-05

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 45.50  E-value: 3.51e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71981008  64 RVAMVGFPSVGKSTLLSSMTSTHSEAAGYefttltciPGV--------ISYNGANIQLLDLPGI 119
Cdd:COG0370   5 TIALVGNPNVGKTTLFNALTGSRQKVGNW--------PGVtvekkegkFKLKGKEIELVDLPGT 60
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 66-149 3.72e-05

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: 43.58  E-value: 3.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  66 AMVGFPSVGKSTLLSSMTSTH----SEAAGyefTTLTCIPGVISYNGANIQLLDLPGIIEGAS--QGKGRgRQVISVAKT 139
Cdd:cd01894   1 AIVGRPNVGKSTLFNRLTGRRdaivSDTPG---VTRDRKYGEAEWGGREFILIDTGGIEPDDEgiSKEIR-EQAEIAIEE 76

                        90
                ....*....|
gi 71981008 140 ADLILMMLDA 149
Cdd:cd01894  77 ADVILFVVDG 86
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 242-288 4.39e-05

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 45.08  E-value: 4.39e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 71981008 242 LYVYNKVDQISIEEIDRLARM-PHHVVISCEMNLNMDYLLEKMWEYLA 288
Cdd:COG2262 315 ILVFNKIDLLDDEELERLRAGyPDAVFISAKTGEGIDELLEAIEERLP 362
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 66-151 1.24e-04

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: 41.56  E-value: 1.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  66 AMVGFPSVGKSTLLSSMTSTH-SEAAGYEFTTLTCIPGVISYNGANIQLLDLPGIIEGASQGKGRGRQVISVAKTADLIL 144
Cdd:cd11383   1 GLMGKTGAGKSSLCNALFGTEvAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPGVGERGRRDREYEELYRRLLPEADLVL 80


                ....*..
gi 71981008 145 MMLDAGK 151
Cdd:cd11383  81 WLLDADD 87
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 64-172 1.60e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 43.50  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008   64 RVAMVGFPSVGKSTLLSSMTSTH----SEAAGyefTTLTCIPGVISYNGANIQLLDLPGIIEgasqgKGRGRQVI---SV 136
Cdd:PRK00093 175 KIAIIGRPNVGKSSLINALLGEErvivSDIAG---TTRDSIDTPFERDGQKYTLIDTAGIRR-----KGKVTEGVekySV 246

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 71981008  137 AKT------ADLILMMLDA--GKSDQQKMLLERELE---AVGIRLNK 172
Cdd:PRK00093 247 IRTlkaierADVVLLVIDAteGITEQDLRIAGLALEagrALVIVVNK 293
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
 64-160 1.90e-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: 42.76  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008    64 RVAMVGFPSVGKSTLL-------SSMTSTHSEaagyefTTLTCIPGVISYNGANIQLLDLPGI-IEGASQGKGRGRQVIS 135
Cdd:TIGR00436   2 FVAILGRPNVGKSTLLnqlhgqkISITSPKAQ------TTRNRISGIHTTGASQIIFIDTPGFhEKKHSLNRLMMKEARS 75

                          90       100
                  ....*....|....*....|....*...
gi 71981008   136 VAKTADLILMMLDAgkSDQQK---MLLE 160
Cdd:TIGR00436  76 AIGGVDLILFVVDS--DQWNGdgeFVLT 101
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 51-165 1.96e-04

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 43.24  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008   51 KGEGFdVMKSGDARVAMVGFPSVGKSTLLSSMT----STHSEAAGyefTTLTCIPGVISYNGANIQLLDLPGIIEGASQG 126
Cdd:PRK09518 440 KTSGF-LTPSGLRRVALVGRPNVGKSSLLNQLTheerAVVNDLAG---TTRDPVDEIVEIDGEDWLFIDTAGIKRRQHKL 515

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 71981008  127 KG-------RGRQVIsvaKTADLILMMLDAGK--SDQQKMLLERELEA 165
Cdd:PRK09518 516 TGaeyysslRTQAAI---ERSELALFLFDASQpiSEQDLKVMSMAVDA 560
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
64-154 5.50e-04

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 41.55  E-value: 5.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  64 RVAMVGFPSVGKSTLLSSMT----STHSEAAGyefTTLTCIPGVISYNGANIQLLDLPGIiegasqgKGRGRQV-----I 134
Cdd:COG1160 177 KIAIVGRPNVGKSSLINALLgeerVIVSDIAG---TTRDSIDTPFERDGKKYTLIDTAGI-------RRKGKVDegiekY 246

                        90       100
                ....*....|....*....|....*...
gi 71981008 135 SVAKT------ADLILMMLDA--GKSDQ 154
Cdd:COG1160 247 SVLRTlraierADVVLLVIDAteGITEQ 274
EHD cd09913
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ...
 111-172 6.23e-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: 40.72  E-value: 6.23e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71981008 111 IQLLDLPGIIEGASQGKGRGRQVISV----AKTADLILMMLDAGK---SDQQKMLLEREL---EAVGIRLNK 172
Cdd:cd09913  90 VTIVDTPGILSGEKQRQSRGYDFNAVcrwfAERADLIFLLFDPHKldiSDEFRRVIEQLKgheSKIRIVLNK 161
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 64-182 2.81e-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: 37.86  E-value: 2.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  64 RVAMVGFPSVGKSTLLSSMtsTHSEAAgyeftTLTCIPG--------VISYNGANIQLLDLPGI------IEgaSQGKGR 129
Cdd:cd04164   5 KVVIAGKPNVGKSSLLNAL--AGRDRA-----IVSDIAGttrdvieeEIDLGGIPVRLIDTAGLretedeIE--KIGIER 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 71981008 130 GRQVIsvaKTADLILMMLDAGKSDQqkmllerELEAVGIRLNKKPPNIYVKQK 182
Cdd:cd04164  76 AREAI---EEADLVLLVVDASEGLD-------EEDLEILELPAKKPVIVVLNK 118
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 241-287 3.82e-03

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


Pssm-ID: 206666 [Multi-domain]  Cd Length: 204  Bit Score: 38.21  E-value: 3.82e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 71981008 241 CLYVYNKVDQISIEEIDRLAR--MPHHVVISCEMNLNMDYLLEKMWEYL 287
Cdd:cd01878 156 IILVLNKIDLLDDEELEERLRagRPDAVFISAKTGEGLDLLKEAIEELL 204
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
58-120 4.27e-03

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 38.55  E-value: 4.27e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71981008  58 MKSGDARVAMVGFPSVGKSTLLSSMTSTHSEAAGYEfttltciPGV------ISYNGaNIQLLDLPGII 120
Cdd:COG1161 109 IKRRPIRVMIVGIPNVGKSTLINRLAGKKVAKTGNK-------PGVtkgqqwIKLDD-GLELLDTPGIL 169
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 58-119 4.52e-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: 37.30  E-value: 4.52e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  58 MKSGDARVAMVGFPSVGKSTLLSSMTSTHSeaagyefTTLTCIPGVISYN--------GANIQLLDLPGI 119
Cdd:cd01859  95 IDGKPVIVGVVGYPKVGKSSIINALKGRHS-------ASTSPIPGSPGYTkgiqlvriDSKIYLIDTPGV 157
TGS_MJ1332_like cd01669
TGS (ThrRS, GTPase and SpoT) domain found in Methanocaldococcus jannaschii uncharacterized ...
 293-364 5.92e-03

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: 35.37  E-value: 5.92e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71981008 293 YTKKPGNA-PDLgpedgIILRGGATIEHCCHALHRSIAAQLRYAIvwGTSTKfspQRVGLHHKLDHEDVIQIV 364
Cdd:cd01669  15 LTDKKGNVlPDA-----ILLKRGSTPRDLAYKIHTDLGKGFLYAI--DARTK---MRLGEDYELKHGDVVKIV 77
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 3-172 5.96e-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: 38.23  E-value: 5.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008     3 ILEKIAEIEHEISRTqknkateyhlgllkakLAKYRQqlleptGKggakgegfdVMKSGdARVAMVGFPSVGKSTLLSSM 82
Cdd:pfam12631  67 LLERLEELLAELEKL----------------LATADR------GR---------ILREG-IKVVIVGKPNVGKSSLLNAL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008    83 tsTHSEAAgyeftTLTCIPG--------VISYNGANIQLLDLPGI------IEgaSQGKGRGRQVIsvaKTADLILMMLD 148
Cdd:pfam12631 115 --LGEERA-----IVTDIPGttrdvieeTINIGGIPLRLIDTAGIretddeVE--KIGIERAREAI---EEADLVLLVLD 182

                         170       180
                  ....*....|....*....|....*...
gi 71981008   149 A--GKSDQQKMLLERELEAVGIR--LNK 172
Cdd:pfam12631 183 AsrPLDEEDLEILELLKDKKPIIvvLNK 210
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
64-172 5.96e-03

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 38.55  E-value: 5.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008   64 RVAMVGFPSVGKSTLLSSMtsTHSEAAgyeftTLTCIPG--------VISYNGANIQLLDLPGI------IEgaSQGKGR 129
Cdd:PRK05291 217 KVVIAGRPNVGKSSLLNAL--LGEERA-----IVTDIAGttrdvieeHINLDGIPLRLIDTAGIretddeVE--KIGIER 287

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 71981008  130 GRQVIsvaKTADLILMMLDAGK---SDQQKMLLERELEAVGIRLNK 172
Cdd:PRK05291 288 SREAI---EEADLVLLVLDASEpltEEDDEILEELKDKPVIVVLNK 330
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 57-161 6.61e-03

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


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 38.12  E-value: 6.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71981008  57 VMKSGdARVAMVGFPSVGKSTLLSSMtsTHSEAAgyeftTLTCIPG--------VISYNGANIQLLDLPGI------IEg 122
Cdd:COG0486 209 LLREG-IKVVIVGRPNVGKSSLLNAL--LGEERA-----IVTDIAGttrdvieeRINIGGIPVRLIDTAGLretedeVE- 279

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 71981008 123 aSQGKGRGRQVIsvaKTADLILMMLDAGK--SDQQKMLLER 161
Cdd:COG0486 280 -KIGIERAREAI---EEADLVLLLLDASEplTEEDEEILEK 316
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
 64-119 7.35e-03

A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein that functions as a regulator of cell growth and proliferation in stem cells and in several types of cancer cells, but is not expressed in the differentiated cells of most mammalian adult tissues. NS shuttles between the nucleolus and nucleoplasm bidirectionally at a rate that is fast and independent of cell type. Lowering GTP levels decreases the nucleolar retention of NS, and expression of NS is abruptly down-regulated during differentiation prior to terminal cell division. Found only in eukaryotes, NS consists of an N-terminal basic domain, a coiled-coil domain, a GTP-binding domain, an intermediate domain, and a C-terminal acidic domain. Experimental evidence indicates that NS uses its GTP-binding property as a molecular switch to control the transition between the nucleolus and nucleoplasm, and this process involves interaction between the basic, GTP-binding, and intermediate domains of the protein.


Pssm-ID: 206753 [Multi-domain]  Cd Length: 171  Bit Score: 36.78  E-value: 7.35e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71981008  64 RVAMVGFPSVGKSTLLSSMTSTHSEAAGyefttltCIPGVISYN-----GANIQLLDLPGI 119
Cdd:cd04178 118 TVGVVGYPNVGKSSVINSLKRSRACNVG-------ATPGVTKSMqevhlDKHVKLLDSPGV 171
 
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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