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Conserved domains on  [gi|10946678|ref|NP_067329|]
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developmentally-regulated GTP-binding protein 2 [Mus musculus]

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];
1-364 3.08e-166

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


:

Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 468.51  E-value: 3.08e-166
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678   1 MGILEKISEIEKEIARTQKNKATEYHLGLLKAKLAKYRAQLLEPSKSASSKGEGFDVMKSGDARVALIGFPSVGKSTFLS 80
Cdd:COG1163   2 MTIEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLLN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  81 LMTSTASEAASYEFTTLTCIPGVIEYKGANIQLLDLPGIIEGAAQGRGRGRQVIAVARTADVVVMMLDATKGDvQRSLLE 160
Cdd:COG1163  82 KLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELE-QYDVLK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678 161 KELESVGIRLNKHKPNIYFKPKKGGGISFNSTVTLTqCSEKLVQLILHEYKIFNAEVLFREDCSPDDFIDVIVGNRVYMP 240
Cdd:COG1163 161 EELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLD-LDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRVYKP 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678 241 CLYVYNKIDQISMEEVDRLARK----PNSVVISCGMKLNLDYLLEMLWEYLALTCIYTKKRGQRPDFTDAIILRKGASVE 316
Cdd:COG1163 240 AIVVVNKIDLADEEYVEELKSKlpdgVPVIFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKGSTVG 319

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 10946678 317 HVCHRIHRSLASQFKYALVWGTSTKYSPQRVGLTHTMEHEDVIQIVKK 364
Cdd:COG1163 320 DVCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIK 367
 
Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
1-364 3.08e-166

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 468.51  E-value: 3.08e-166
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678   1 MGILEKISEIEKEIARTQKNKATEYHLGLLKAKLAKYRAQLLEPSKSASSKGEGFDVMKSGDARVALIGFPSVGKSTFLS 80
Cdd:COG1163   2 MTIEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLLN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  81 LMTSTASEAASYEFTTLTCIPGVIEYKGANIQLLDLPGIIEGAAQGRGRGRQVIAVARTADVVVMMLDATKGDvQRSLLE 160
Cdd:COG1163  82 KLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELE-QYDVLK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678 161 KELESVGIRLNKHKPNIYFKPKKGGGISFNSTVTLTqCSEKLVQLILHEYKIFNAEVLFREDCSPDDFIDVIVGNRVYMP 240
Cdd:COG1163 161 EELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLD-LDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRVYKP 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678 241 CLYVYNKIDQISMEEVDRLARK----PNSVVISCGMKLNLDYLLEMLWEYLALTCIYTKKRGQRPDFTDAIILRKGASVE 316
Cdd:COG1163 240 AIVVVNKIDLADEEYVEELKSKlpdgVPVIFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKGSTVG 319

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 10946678 317 HVCHRIHRSLASQFKYALVWGTSTKYSPQRVGLTHTMEHEDVIQIVKK 364
Cdd:COG1163 320 DVCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIK 367
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 63-295 6.81e-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: 442.37  E-value: 6.81e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  63 ARVALIGFPSVGKSTFLSLMTSTASEAASYEFTTLTCIPGVIEYKGANIQLLDLPGIIEGAAQGRGRGRQVIAVARTADV 142
Cdd:cd01896   1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678 143 VVMMLDATKGDVQRSLLEKELESVGIRLNKHKPNIYFKPKKGGGISFNSTVTLTQCSEKLVQLILHEYKIFNAEVLFRED 222
Cdd:cd01896  81 ILIVLDATKPEGQREILERELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLTKLDEKTVKAILREYKIHNADVLIRED 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10946678 223 CSPDDFIDVIVGNRVYMPCLYVYNKIDQISMEEVDRLARKPNSVVISCGMKLNLDYLLEMLWEYLALTCIYTK 295
Cdd:cd01896 161 ITVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDRLARIPNSVVISAEKDLNLDELLERIWDYLGLIRIYTK 233
MMR_HSR1_Xtn pfam16897
C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of ...
 185-289 1.44e-62

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: 195.34  E-value: 1.44e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678   185 GGISFNSTVTLTQCSEKLVQLILHEYKIFNAEVLFREDCSPDDFIDVIVGNRVYMPCLYVYNKIDQISMEEVDRLARKPN 264
Cdd:pfam16897   1 GGINITSTVPLTKLDEETIKAILREYKIHNADVLIREDVTVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDRLAREPD 80

                          90       100
                  ....*....|....*....|....*
gi 10946678   265 SVVISCGMKLNLDYLLEMLWEYLAL 289
Cdd:pfam16897  81 SVPISAEKGLNLDELKERIWEYLGL 105
obgE PRK12297
GTPase CgtA; Reviewed
 63-262 2.39e-21

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 94.40  E-value: 2.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678   63 ARVALIGFPSVGKSTFLSLMTSTASEAASYEFTTLTCIPGVIEYKGAN-IQLLDLPGIIEGAAQGRGRGRQVIA-VARTA 140
Cdd:PRK12297 159 ADVGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRsFVMADIPGLIEGASEGVGLGHQFLRhIERTR 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  141 dVVVMMLDATkGDVQRSLLE------KELESVGIRLNKhKPNI----------------YFKPKKGGGISFNSTVTlTQC 198
Cdd:PRK12297 239 -VIVHVIDMS-GSEGRDPIEdyekinKELKLYNPRLLE-RPQIvvankmdlpeaeenleEFKEKLGPKVFPISALT-GQG 314

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  199 SEKLVQLI---LHEYKIFNA-------EVLFREDCSPDDF-ID-------VIVGNRVYmpclYVYNKIDQISMEEVDRLA 260
Cdd:PRK12297 315 LDELLYAVaelLEETPEFPLeeeeveeEVYYKFEEEEKDFtITrdedgvfVVSGEKIE----RLFKMTNFNRDESLRRFA 390


                 ..
gi 10946678  261 RK 262
Cdd:PRK12297 391 RQ 392
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 62-215 7.89e-19

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: 82.42  E-value: 7.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678    62 DARVALIGFPSVGKSTFL-SLMTSTASEAASYEFTTLTCIPGVIEYKG--ANIQLLDLPGIIEGAAQGRGRGRQVIAVAR 138
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLnSLLGNKGSITEYYPGTTRNYVTTVIEEDGktYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678   139 TADVVVMMLDATKGDV-QRSLLEKELES-VGIRLNKHKPNI---YFKPKKGGGISFNSTVTLTQCSEKLVQLILHEYKIF 213
Cdd:TIGR00231  81 VFDIVILVLDVEEILEkQTKEIIHHADSgVPIILVGNKIDLkdaDLKTHVASEFAKLNGEPIIPLSAETGKNIDSAFKIV 160


                  ..
gi 10946678   214 NA 215
Cdd:TIGR00231 161 EA 162
 
Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
1-364 3.08e-166

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 468.51  E-value: 3.08e-166
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678   1 MGILEKISEIEKEIARTQKNKATEYHLGLLKAKLAKYRAQLLEPSKSASSKGEGFDVMKSGDARVALIGFPSVGKSTFLS 80
Cdd:COG1163   2 MTIEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLLN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  81 LMTSTASEAASYEFTTLTCIPGVIEYKGANIQLLDLPGIIEGAAQGRGRGRQVIAVARTADVVVMMLDATKGDvQRSLLE 160
Cdd:COG1163  82 KLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELE-QYDVLK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678 161 KELESVGIRLNKHKPNIYFKPKKGGGISFNSTVTLTqCSEKLVQLILHEYKIFNAEVLFREDCSPDDFIDVIVGNRVYMP 240
Cdd:COG1163 161 EELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLD-LDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRVYKP 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678 241 CLYVYNKIDQISMEEVDRLARK----PNSVVISCGMKLNLDYLLEMLWEYLALTCIYTKKRGQRPDFTDAIILRKGASVE 316
Cdd:COG1163 240 AIVVVNKIDLADEEYVEELKSKlpdgVPVIFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKGSTVG 319

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 10946678 317 HVCHRIHRSLASQFKYALVWGTSTKYSPQRVGLTHTMEHEDVIQIVKK 364
Cdd:COG1163 320 DVCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIK 367
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 63-295 6.81e-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: 442.37  E-value: 6.81e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  63 ARVALIGFPSVGKSTFLSLMTSTASEAASYEFTTLTCIPGVIEYKGANIQLLDLPGIIEGAAQGRGRGRQVIAVARTADV 142
Cdd:cd01896   1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678 143 VVMMLDATKGDVQRSLLEKELESVGIRLNKHKPNIYFKPKKGGGISFNSTVTLTQCSEKLVQLILHEYKIFNAEVLFRED 222
Cdd:cd01896  81 ILIVLDATKPEGQREILERELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLTKLDEKTVKAILREYKIHNADVLIRED 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10946678 223 CSPDDFIDVIVGNRVYMPCLYVYNKIDQISMEEVDRLARKPNSVVISCGMKLNLDYLLEMLWEYLALTCIYTK 295
Cdd:cd01896 161 ITVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDRLARIPNSVVISAEKDLNLDELLERIWDYLGLIRIYTK 233
MMR_HSR1_Xtn pfam16897
C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of ...
 185-289 1.44e-62

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: 195.34  E-value: 1.44e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678   185 GGISFNSTVTLTQCSEKLVQLILHEYKIFNAEVLFREDCSPDDFIDVIVGNRVYMPCLYVYNKIDQISMEEVDRLARKPN 264
Cdd:pfam16897   1 GGINITSTVPLTKLDEETIKAILREYKIHNADVLIREDVTVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDRLAREPD 80

                          90       100
                  ....*....|....*....|....*
gi 10946678   265 SVVISCGMKLNLDYLLEMLWEYLAL 289
Cdd:pfam16897  81 SVPISAEKGLNLDELKERIWEYLGL 105
TGS_DRG2 cd17231
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 2 ...
 286-364 1.48e-57

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: 181.43  E-value: 1.48e-57
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10946678 286 YLALTCIYTKKRGQRPDFTDAIILRKGASVEHVCHRIHRSLASQFKYALVWGTSTKYSPQRVGLTHTMEHEDVIQIVKK 364
Cdd:cd17231   1 YLALIRVYTKKRGERPDFGDAIILRRGATVEHVCHRIHRTLASQFKYALVWGTSTKYSPQRVGLTHVMEDEDVIQIVKK 79
TGS_DRG1 cd17230
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 1 ...
 286-364 5.71e-39

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: 133.55  E-value: 5.71e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678 286 YLALTCIYTKKRGQRPDFTDAIILRKGA-SVEHVCHRIHRSLASQFKYALVWGTSTKYSPQRVGLTHTMEHEDVIQIVKK 364
Cdd:cd17230   1 YLNLVRIYTKPKGQLPDYEEPVVLRSGKsTVEDFCNKIHKSLIKEFKYALVWGSSVKHNPQRVGKDHVLEDEDVVQIVKK 80
TGS_DRG cd01666
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein ...
 287-363 9.74e-39

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: 132.74  E-value: 9.74e-39
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10946678 287 LALTCIYTKKRGQRPDFTDAIILRKGASVEHVCHRIHRSLASQFKYALVWGTSTKYSPQRVGLTHTMEHEDVIQIVK 363
Cdd:cd01666   1 LGIIRVYTKPPGKKPDFDEPFILRRGSTVEDVAEKIHKDLAENFKYARVWGKSVKFDGQRVGLDHVLEDGDIVEIHK 77
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 66-287 3.37e-37

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: 131.75  E-value: 3.37e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  66 ALIGFPSVGKSTFLSLMTSTASEAASYEFTTLTCIPGVIEYK-GANIQLLDLPGIIEGAAQGRGRGRQVIAVARTADVVV 144
Cdd:cd01881   1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGdGVDIQIIDLPGLLDGASEGRGLGEQILAHLYRSDLIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678 145 MMLDatkgdvqrsllekelesvgirlnkhkpniyfkpkkgggisfnstvtltqCSEKLVQLILHEYKIFNAEVLFREDcs 224
Cdd:cd01881  81 HVID-------------------------------------------------ASEDCVGDPLEDQKTLNEEVSGSFL-- 109

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10946678 225 pddfidvivgNRVYMPCLYVYNKIDQISMEEV-----DRLARKPNSVVISCGMKLNLDYLLEMLWEYL 287
Cdd:cd01881 110 ----------FLKNKPEMIVANKIDMASENNLkrlklDKLKRGIPVVPTSALTRLGLDRVIRTIRKLL 167
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 64-172 1.82e-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: 104.24  E-value: 1.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678    64 RVALIGFPSVGKSTFLSLMTSTASEAASYEFTTLTCIPGVIEYKGANIQLLDLPGIIEGAAQGRGRGRQVIAVARtADVV 143
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFLAIIE-ADLI 79

                          90       100
                  ....*....|....*....|....*....
gi 10946678   144 VMMLDATKGdvqRSLLEKELESVGIRLNK 172
Cdd:pfam01926  80 LFVVDSEEG---ITPLDEELLELLRENKK 105
obgE PRK12297
GTPase CgtA; Reviewed
 63-262 2.39e-21

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 94.40  E-value: 2.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678   63 ARVALIGFPSVGKSTFLSLMTSTASEAASYEFTTLTCIPGVIEYKGAN-IQLLDLPGIIEGAAQGRGRGRQVIA-VARTA 140
Cdd:PRK12297 159 ADVGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRsFVMADIPGLIEGASEGVGLGHQFLRhIERTR 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  141 dVVVMMLDATkGDVQRSLLE------KELESVGIRLNKhKPNI----------------YFKPKKGGGISFNSTVTlTQC 198
Cdd:PRK12297 239 -VIVHVIDMS-GSEGRDPIEdyekinKELKLYNPRLLE-RPQIvvankmdlpeaeenleEFKEKLGPKVFPISALT-GQG 314

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  199 SEKLVQLI---LHEYKIFNA-------EVLFREDCSPDDF-ID-------VIVGNRVYmpclYVYNKIDQISMEEVDRLA 260
Cdd:PRK12297 315 LDELLYAVaelLEETPEFPLeeeeveeEVYYKFEEEEKDFtITrdedgvfVVSGEKIE----RLFKMTNFNRDESLRRFA 390


                 ..
gi 10946678  261 RK 262
Cdd:PRK12297 391 RQ 392
TGS pfam02824
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ...
 292-363 7.35e-20

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: 82.21  E-value: 7.35e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10946678   292 IYTKKrGQRPDftdaiiLRKGASVEHVCHRIHRSLASQFKYALVWGtstkyspQRVGLTHTMEHEDVIQIVK 363
Cdd:pfam02824   3 VYTPD-GKVPD------LPRGATPEDFAYAIHTSLAKKFIYAKVNG-------QLVGLDHPLEDGDVVEIVT 60
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 63-175 1.61e-19

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: 84.40  E-value: 1.61e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  63 ARVALIGFPSVGKSTFLSLMTSTASEAASYEFTTLtcIP--GVIEYK-GANIQLLDLPGIIEGAAQGRGRG----RQvia 135
Cdd:cd01898   1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTL--VPnlGVVRVDdGRSFVIADIPGLIEGASEGKGLGhrflRH--- 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 10946678 136 VARTaDVVVMMLDATKG-----DVQrsLLEKELESVGIRLNKhKP 175
Cdd:cd01898  76 IERT-RVLLHVIDLSGEddpveDYE--TIRNELEAYNPGLAE-KP 116
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 62-215 7.89e-19

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: 82.42  E-value: 7.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678    62 DARVALIGFPSVGKSTFL-SLMTSTASEAASYEFTTLTCIPGVIEYKG--ANIQLLDLPGIIEGAAQGRGRGRQVIAVAR 138
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLnSLLGNKGSITEYYPGTTRNYVTTVIEEDGktYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678   139 TADVVVMMLDATKGDV-QRSLLEKELES-VGIRLNKHKPNI---YFKPKKGGGISFNSTVTLTQCSEKLVQLILHEYKIF 213
Cdd:TIGR00231  81 VFDIVILVLDVEEILEkQTKEIIHHADSgVPIILVGNKIDLkdaDLKTHVASEFAKLNGEPIIPLSAETGKNIDSAFKIV 160


                  ..
gi 10946678   214 NA 215
Cdd:TIGR00231 161 EA 162
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
 63-287 7.15e-18

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: 83.49  E-value: 7.15e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  63 ARVALIGFPSVGKSTFLSLMTSTASEAASYEFTTLTciP--GVIEYKGAN-IQLLDLPGIIEGAAQGRGRG----RQvia 135
Cdd:COG0536 158 ADVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLV--PnlGVVRVGDGRsFVIADIPGLIEGASEGAGLGhrflRH--- 232

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678 136 VARTAdVVVMMLDATKGDvQRSLLEKelesvgirlnkhkpniyfkpkkgggisfnstvtltqcseklVQLILHEYKIFNA 215
Cdd:COG0536 233 IERTR-VLLHVVDAAPLD-GRDPVED-----------------------------------------YEIIRNELEAYSP 269

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10946678 216 EVLFRedcspddfidvivgnrvymPCLYVYNKIDQISMEEVDRL-----ARKPNSVVISCGMKLNLDYLLEMLWEYL 287
Cdd:COG0536 270 ELAEK-------------------PRIVVLNKIDLLDAEELEELkaeleKLGGPVFPISAVTGEGLDELLYALAELL 327
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
 63-177 1.50e-17

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: 82.47  E-value: 1.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678    63 ARVALIGFPSVGKSTFLSLMTSTASEAASYEFTTLTCIPGVIEYKGAN-IQLLDLPGIIEGAAQGRGRGRQVIA-VARTA 140
Cdd:TIGR02729 158 ADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRsFVIADIPGLIEGASEGAGLGHRFLKhIERTR 237

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 10946678   141 dVVVMMLDAT---KGDVQRS--LLEKELESVGIRLNKhKPNI 177
Cdd:TIGR02729 238 -VLLHLIDISpedGSDPVEDyeIIRNELKKYSPELAE-KPRI 277
obgE PRK12299
GTPase CgtA; Reviewed
 63-216 1.87e-16

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 79.34  E-value: 1.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678   63 ARVALIGFPSVGKSTFLSLMTSTASEAASYEFTTLTCIPGVIEYKGAN-IQLLDLPGIIEGAAQGRGRGRQVIA-VARTA 140
Cdd:PRK12299 159 ADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKsFVIADIPGLIEGASEGAGLGHRFLKhIERTR 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  141 dVVVMMLDATKGDVQRS--LLEKELESVG---------IRLNK----------HKPNIYFKPKKGGGISFNSTVTLTQCs 199
Cdd:PRK12299 239 -LLLHLVDIEAVDPVEDykTIRNELEKYSpeladkpriLVLNKidlldeeeerEKRAALELAALGGPVFLISAVTGEGL- 316

                        170
                 ....*....|....*..
gi 10946678  200 EKLVQLILHEYKIFNAE 216
Cdd:PRK12299 317 DELLRALWELLEEARRE 333
obgE PRK12296
GTPase CgtA; Reviewed
 28-150 4.19e-15

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 76.44  E-value: 4.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678   28 GLLKAKLAKYR------AQLLEPsksasskGEGFDV---MKSgDARVALIGFPSVGKSTFLSLMTSTASEAASYEFTTLt 98
Cdd:PRK12296 124 GLGNAALASKArkapgfALLGEP-------GEERDLvleLKS-VADVGLVGFPSAGKSSLISALSAAKPKIADYPFTTL- 194

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 10946678   99 cIP--GVIEYKGANIQLLDLPGIIEGAAQGRGRGRQVIA-VARTAdVVVMMLD-AT 150
Cdd:PRK12296 195 -VPnlGVVQAGDTRFTVADVPGLIPGASEGKGLGLDFLRhIERCA-VLVHVVDcAT 248
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
 65-276 6.86e-15

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: 74.57  E-value: 6.86e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  65 VALIGFPSVGKSTFLSLMTSTASEAASYEFTT------------------LTCIPGVIEYKGAN------IQLLDLPGII 120
Cdd:cd01899   1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTidpnvgvgyvrvecpckeLGVSCNPRYGKCIDgkryvpVELIDVAGLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678 121 EGAAQGRGRGRQVIAVARTADVVVMMLDATKG-----------------DVQrsLLEKELES-VGIRLNKHKPNIYFKPK 182
Cdd:cd01899  81 PGAHEGKGLGNQFLDDLRDADVLIHVVDASGGtdaegngvetggydpleDIE--FLENEIDMwIYGILERNWEKIVRKAK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678 183 KGGgisFNSTVTLtqcSEKLVQLILHEYKIFNA--EVLFREDCS---PDDFIDVIVGNRVY-MPCLYVYNKIDQISMEEV 256
Cdd:cd01899 159 AEK---TDIVEAL---SEQLSGFGVNEDVVIEAleELELPADLSkwdDEDLLRLARELRKRrKPMVIAANKADIPDAEEN 232

                       250       260
                ....*....|....*....|....
gi 10946678 257 DRLARK----PNSVVISCGMKLNL 276
Cdd:cd01899 233 ISKLRLkypdEIVVPTSAEAELAL 256
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 66-172 2.72e-13

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 66.89  E-value: 2.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  66 ALIGFPSVGKSTFL-SLMTSTASEAASYEFTTLTCIPGVIE-YKGANIQLLDLPGIIEGAAQGRGRGRQVIAVARTADVV 143
Cdd:cd00880   1 AIFGRPNVGKSSLLnALLGQNVGIVSPIPGTTRDPVRKEWElLPLGPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 10946678 144 VMMLDATKGDVQRSLLEKELESVGIR----LNK 172
Cdd:cd00880  81 LLVVDSDLTPVEEEAKLGLLRERGKPvllvLNK 113
PRK09602 PRK09602
translation-associated GTPase; Reviewed
 64-362 3.13e-13

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 70.22  E-value: 3.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678   64 RVALIGFPSVGKSTFLSLMTSTASEAASYEFTT--------------------LTCIPGVIEYKGAN----IQLLDLPGI 119
Cdd:PRK09602   3 TIGLVGKPNVGKSTFFNAATLADVEIANYPFTTidpnvgvayvrvecpckelgVKCNPRNGKCIDGTrfipVELIDVAGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  120 IEGAAQGRGRGRQVIAVARTADVVVMMLDATKG-----------------DVQrsLLEKELES--VGIrLNKHKPNIyfk 180
Cdd:PRK09602  83 VPGAHEGRGLGNQFLDDLRQADALIHVVDASGStdeegnpvepgshdpveDIK--FLEEELDMwiYGI-LEKNWEKF--- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  181 PKKGGGISFNSTVTLTqcsEKLVQLILHEYKIFNAEVLFREDCSP-----DDFIDVIVGNRVY-MPCLYVYNKIDQISME 254
Cdd:PRK09602 157 SRKAQAEKFDIEEALA---EQLSGLGINEEHVKEALRELGLPEDPskwtdEDLLELARELRKIsKPMVIAANKADLPPAE 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  255 E-VDRLARKPNSVVI--SCGMKLNL---------DYL-------------------LEMLWEYL---------------- 287
Cdd:PRK09602 234 EnIERLKEEKYYIVVptSAEAELALrraakagliDYIpgdsdfeilgelsekqkkaLEYIREVLkkyggtgvqeaintav 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  288 --ALTCI----------YTKKRGQRpdFTDAIILRKGASVEHVCHRIHRSLASQFKYALvwGTSTKyspQRVGLTHTMEH 355
Cdd:PRK09602 314 fdLLDMIvvypvedenkLTDKKGNV--LPDAFLLPKGSTARDLAYKIHTDIGEGFLYAI--DARTK---RRIGEDYELKD 386


                 ....*..
gi 10946678  356 EDVIQIV 362
Cdd:PRK09602 387 GDVIKIV 393
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
69-160 1.04e-12

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 68.32  E-value: 1.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  69 GFPSVGKSTFLSLMTSTASEAASYEFTTLTCIPGVIEYKGANIQLLDLPGI----------IEgaaqgrgrgRQ-VIAVA 137
Cdd:COG1084 167 GYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGRYQVIDTPGLldrplserneIE---------RQaILALK 237

                        90       100
                ....*....|....*....|....*...
gi 10946678 138 RTADVVVMMLDA--TKG---DVQRSLLE 160
Cdd:COG1084 238 HLADVILFLFDPseTCGyslEEQLNLLE 265
obgE PRK12298
GTPase CgtA; Reviewed
 63-182 1.27e-12

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 68.36  E-value: 1.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678   63 ARVALIGFPSVGKSTFLSLMTSTASEAASYEFTTLtcIP--GVIEY-KGANIQLLDLPGIIEGAAQGRGRG-RQVIAVAR 138
Cdd:PRK12298 160 ADVGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTL--VPnlGVVRVdDERSFVVADIPGLIEGASEGAGLGiRFLKHLER 237

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 10946678  139 TAdVVVMMLDATKGDVQR-----SLLEKELEsvgirlnKHKPNIYFKPK 182
Cdd:PRK12298 238 CR-VLLHLIDIAPIDGSDpvenaRIIINELE-------KYSPKLAEKPR 278
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 66-172 2.33e-10

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


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 58.62  E-value: 2.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  66 ALIGFPSVGKSTFL-SLMTSTASEAASYEFTTLTCIPGVIEYKGA--NIQLLDLPGIIEGaaQGRGRGRQVIAVARTADV 142
Cdd:cd00882   1 VVVGRGGVGKSSLLnALLGGEVGEVSDVPGTTRDPDVYVKELDKGkvKLVLVDTPGLDEF--GGLGREELARLLLRGADL 78

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 10946678 143 VVMMLDATKG---DVQRSLLEKELESVGIR----LNK 172
Cdd:cd00882  79 ILLVVDSTDReseEDAKLLILRRLRKEGIPiilvGNK 115
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 69-150 4.66e-10

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: 57.96  E-value: 4.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  69 GFPSVGKSTFLSLMTSTASEAASYEFTTLTCIPGVIEYKGANIQLLDLPGI----------IEgaaqgrgrgRQVI-AVA 137
Cdd:cd01897   7 GYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLRWQVIDTPGIldrpleerntIE---------MQAItALA 77

                        90
                ....*....|...
gi 10946678 138 RTADVVVMMLDAT 150
Cdd:cd01897  78 HLRAAVLFFIDPS 90
TGS_Obg cd04938
TGS (ThrRS, GTPase and SpoT) domain found in the Obg protein family; The Obg family of GTPases ...
 292-362 2.85e-08

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: 50.52  E-value: 2.85e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10946678 292 IYTKKRGQR-------PDFTDAIILRKGASVEHVCHRIHRSLASQFKYALVWGtstkySPQRVGLTHTMEHEDVIQIV 362
Cdd:cd04938   5 VYPVKNIQTftngsgnSVFRDCVLVKKGTTVKDFANKIHTDLEKGFINAEGIG-----GRRLEGEDYILQDNDVVKFT 77
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 64-152 1.29e-07

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


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 50.89  E-value: 1.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  64 RVALIGFPSVGKSTFLSLMT----STASEAASyefTTLTCIPGVIEYKGANIQLLDLPGIiegaaqgRGRGRQV-----I 134
Cdd:cd01895   4 KIAIIGRPNVGKSSLLNALLgeerVIVSDIAG---TTRDSIDVPFEYDGQKYTLIDTAGI-------RKKGKVTegiekY 73

                        90       100
                ....*....|....*....|....
gi 10946678 135 AVART------ADVVVMMLDATKG 152
Cdd:cd01895  74 SVLRTlkaierADVVLLVLDASEG 97
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
64-152 4.96e-07

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 51.18  E-value: 4.96e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  64 RVALIGFPSVGKSTFLSLMT----STASEAASyefTTLTCIPGVIEYKGANIQLLDLPGIiegaaqgRGRGRQV-----I 134
Cdd:COG1160 177 KIAIVGRPNVGKSSLINALLgeerVIVSDIAG---TTRDSIDTPFERDGKKYTLIDTAGI-------RRKGKVDegiekY 246

                        90       100
                ....*....|....*....|....
gi 10946678 135 AVART------ADVVVMMLDATKG 152
Cdd:COG1160 247 SVLRTlraierADVVLLVIDATEG 270
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
58-172 2.94e-06

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 48.45  E-value: 2.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  58 MKSGdaRVALIGFPSVGKSTFL--------SLMTSTASeaasyefTTLTCIPGVIEYKGANIQLLDLPGIIEGA-AQGRG 128
Cdd:COG1159   1 FRSG--FVAIVGRPNVGKSTLLnalvgqkvSIVSPKPQ-------TTRHRIRGIVTREDAQIVFVDTPGIHKPKrKLGRR 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 10946678 129 RGRQVIAVARTADVVVMMLDATK--GDVQRSLLEKeLESVGIR----LNK 172
Cdd:COG1159  72 MNKAAWSALEDVDVILFVVDATEkiGEGDEFILEL-LKKLKTPvilvINK 120
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 240-288 3.81e-06

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 48.54  E-value: 3.81e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 10946678 240 PCLYVYNKIDQISMEEVDRL-ARKPNSVVISCGMKLNLDYLLEMLWEYLA 288
Cdd:COG2262 313 PIILVFNKIDLLDDEELERLrAGYPDAVFISAKTGEGIDELLEAIEERLP 362
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 64-152 4.95e-06

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 48.12  E-value: 4.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678   64 RVALIGFPSVGKSTFLSLMT----STASEAASyefTTLTCIPGVIEYKGANIQLLDLPGIiegaaqgRGRGR-----QVI 134
Cdd:PRK00093 175 KIAIIGRPNVGKSSLINALLgeerVIVSDIAG---TTRDSIDTPFERDGQKYTLIDTAGI-------RRKGKvtegvEKY 244

                         90       100
                 ....*....|....*....|....
gi 10946678  135 AVART------ADVVVMMLDATKG 152
Cdd:PRK00093 245 SVIRTlkaierADVVLLVIDATEG 268
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 66-119 1.19e-05

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: 44.75  E-value: 1.19e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 10946678  66 ALIGFPSVGKSTFLSLMTSTASEAASYEFTTLTCIPGVIEYKGANIQLLDLPGI 119
Cdd:cd01879   1 ALVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPGT 54
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 58-152 1.55e-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: 44.76  E-value: 1.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  58 MKSGdaRVALIGFPSVGKSTFL--------SLMTSTASeaasyefTTLTCIPGVIEYKGANIQLLDLPGIIEgaaQGRGR 129
Cdd:cd04163   1 FKSG--FVAIIGRPNVGKSTLLnalvgqkiSIVSPKPQ-------TTRNRIRGIYTDDDAQIIFVDTPGIHK---PKKKL 68

                        90       100
                ....*....|....*....|....*..
gi 10946678 130 GRQVIAVART----ADVVVMMLDATKG 152
Cdd:cd04163  69 GERMVKAAWSalkdVDLVLFVVDASEW 95
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 240-287 2.71e-05

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: 44.76  E-value: 2.71e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 10946678 240 PCLYVYNKIDQISMEEVDRLARK--PNSVVISCGMKLNLDYLLEMLWEYL 287
Cdd:cd01878 155 PIILVLNKIDLLDDEELEERLRAgrPDAVFISAKTGEGLDLLKEAIEELL 204
GTP_HflX TIGR03156
GTP-binding protein HflX; This protein family is one of a number of homologous small, ...
 240-287 2.99e-05

GTP-binding protein HflX; This protein family is one of a number of homologous small, well-conserved GTP-binding proteins with pleiotropic effects. Bacterial members are designated HflX, following the naming convention in Escherichia coli where HflX is encoded immediately downstream of the RNA chaperone Hfq, and immediately upstream of HflKC, a membrane-associated protease pair with an important housekeeping function. Over large numbers of other bacterial genomes, the pairing with hfq is more significant than with hflK and hlfC. The gene from Homo sapiens in this family has been named PGPL (pseudoautosomal GTP-binding protein-like). [Unknown function, General]


Pssm-ID: 274455 [Multi-domain]  Cd Length: 351  Bit Score: 45.54  E-value: 2.99e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 10946678   240 PCLYVYNKIDQISMEEVDRLAR-KPNSVVISCGMKLNLDYLLEMLWEYL 287
Cdd:TIGR03156 303 PQLLVYNKIDLLDEPRIERLEEgYPEAVFVSAKTGEGLDLLLEAIAERL 351
TGS_MJ1332_like cd01669
TGS (ThrRS, GTPase and SpoT) domain found in Methanocaldococcus jannaschii uncharacterized ...
 305-362 3.73e-05

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: 41.53  E-value: 3.73e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 10946678 305 DAIILRKGASVEHVCHRIHRSLASQFKYALvwGTSTKyspQRVGLTHTMEHEDVIQIV 362
Cdd:cd01669  25 DAILLKRGSTPRDLAYKIHTDLGKGFLYAI--DARTK---MRLGEDYELKHGDVVKIV 77
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
64-150 7.43e-05

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 44.73  E-value: 7.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  64 RVALIGFPSVGKSTFLSLMTSTASEAASYefttltciPGV--------IEYKGANIQLLDLPGII--------EGAAqgr 127
Cdd:COG0370   5 TIALVGNPNVGKTTLFNALTGSRQKVGNW--------PGVtvekkegkFKLKGKEIELVDLPGTYslsayspdEKVA--- 73

                        90       100
                ....*....|....*....|...
gi 10946678 128 grgRQVIAVARtADVVVMMLDAT 150
Cdd:COG0370  74 ---RDFLLEEK-PDVVVNVVDAT 92
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 66-151 2.58e-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: 40.79  E-value: 2.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  66 ALIGFPSVGKSTFLS-LMTSTASEAASYEFTTLTCIPGVIEYKGANIQLLDLPGIIEGAAQGRGRGRQVIAVARTADVVV 144
Cdd:cd11383   1 GLMGKTGAGKSSLCNaLFGTEVAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPGVGERGRRDREYEELYRRLLPEADLVL 80


                ....*..
gi 10946678 145 MMLDATK 151
Cdd:cd11383  81 WLLDADD 87
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 64-146 2.63e-04

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 42.63  E-value: 2.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678   64 RVALIGFPSVGKSTFLSLMTSTASEAASYEFTTLTCIPGVIE------------YK-----GANIQLLDLPGIIEGAAQG 126
Cdd:PTZ00258  23 KMGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNvpderfdwlckhFKpksivPAQLDITDIAGLVKGASEG 102

                         90       100
                 ....*....|....*....|
gi 10946678  127 RGRGRQVIAVARTADVVVMM 146
Cdd:PTZ00258 103 EGLGNAFLSHIRAVDGIYHV 122
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 66-152 2.82e-04

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: 40.88  E-value: 2.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  66 ALIGFPSVGKSTFLSLMTSTaSEA--ASYEFTTLTCIPGVIEYKGANIQLLDLPGIIEGAA--QGRGRgRQVIAVARTAD 141
Cdd:cd01894   1 AIVGRPNVGKSTLFNRLTGR-RDAivSDTPGVTRDRKYGEAEWGGREFILIDTGGIEPDDEgiSKEIR-EQAEIAIEEAD 78

                        90
                ....*....|.
gi 10946678 142 VVVMMLDATKG 152
Cdd:cd01894  79 VILFVVDGREG 89
era PRK00089
GTPase Era; Reviewed
 58-152 3.00e-04

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 41.96  E-value: 3.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678   58 MKSGdaRVALIGFPSVGKSTFL--------SLMTSTASeaasyefTTLTCIPGVIEYKGANIQLLDLPGI-IEGAAQGRG 128
Cdd:PRK00089   3 FKSG--FVAIVGRPNVGKSTLLnalvgqkiSIVSPKPQ-------TTRHRIRGIVTEDDAQIIFVDTPGIhKPKRALNRA 73

                         90       100
                 ....*....|....*....|....
gi 10946678  129 RGRQVIAVARTADVVVMMLDATKG 152
Cdd:PRK00089  74 MNKAAWSSLKDVDLVLFVVDADEK 97
EHD cd09913
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ...
 111-172 4.25e-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: 41.49  E-value: 4.25e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10946678 111 IQLLDLPGIIEGAAQGRGRGRQVIAVAR----TADVVVMMLDATKGDVQ---RSLLEKEL---ESVGIRLNK 172
Cdd:cd09913  90 VTIVDTPGILSGEKQRQSRGYDFNAVCRwfaeRADLIFLLFDPHKLDISdefRRVIEQLKgheSKIRIVLNK 161
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 3-119 6.59e-04

Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, and archaea. They all exhibit a circular permutation of the GTPase signature motifs so that the order of the conserved G box motifs is G4-G5-G1-G2-G3, with G4 and G5 being permuted from the C-terminal region of proteins in the Ras superfamily to the N-terminus of YlqF-related GTPases.


Pssm-ID: 206746 [Multi-domain]  Cd Length: 146  Bit Score: 39.68  E-value: 6.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678   3 ILEKISEIEKEIarTQKNKATEYHLGLLKAKLAKYRAQLLEPSKSASSKGEGFDVMKSGDARVALIGFPSVGKSTFL-SL 81
Cdd:cd01849  34 VLNKADLVPKEV--LRKWVAELSELYGTKTFFISATNGQGILKLKAEITKQKLKLKYKKGIRVGVVGLPNVGKSSFInAL 111

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 10946678  82 MTSTASEAASYEFTTLTCIpgVIEYkGANIQLLDLPGI 119
Cdd:cd01849 112 LNKFKLKVGSIPGTTKLQQ--DVKL-DKEIYLYDTPGI 146
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 29-149 2.76e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 39.57  E-value: 2.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678   29 LLKAKLAKYraqllePSKSASSKGEGfdvmksGDARVALIGFPSVGKSTFLSLMT----STASEAASyefTTLTCIPGVI 104
Cdd:PRK03003 190 LLDAVLAAL------PEVPRVGSASG------GPRRVALVGKPNVGKSSLLNKLAgeerSVVDDVAG---TTVDPVDSLI 254

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 10946678  105 EYKGANIQLLDLPGIIE--GAAQgrgrGRQVIAVART------ADVVVMMLDA 149
Cdd:PRK03003 255 ELGGKTWRFVDTAGLRRrvKQAS----GHEYYASLRThaaieaAEVAVVLIDA 303
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 51-150 4.77e-03

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 39.01  E-value: 4.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678   51 KGEGFdVMKSGDARVALIGFPSVGKSTFLSLMT----STASEAASyefTTLTCIPGVIEYKGANIQLLDLPGIIEGAAQG 126
Cdd:PRK09518 440 KTSGF-LTPSGLRRVALVGRPNVGKSSLLNQLTheerAVVNDLAG---TTRDPVDEIVEIDGEDWLFIDTAGIKRRQHKL 515

                         90       100       110
                 ....*....|....*....|....*....|.
gi 10946678  127 RG-------RGRQVIavaRTADVVVMMLDAT 150
Cdd:PRK09518 516 TGaeyysslRTQAAI---ERSELALFLFDAS 543
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 58-119 5.36e-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: 5.36e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10946678  58 MKSGDARVALIGFPSVGKSTFLSLMT-----STASEAASYEFTTltcipGVIEYKGA-NIQLLDLPGI 119
Cdd:cd01859  95 IDGKPVIVGVVGYPKVGKSSIINALKgrhsaSTSPIPGSPGYTK-----GIQLVRIDsKIYLIDTPGV 157
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 64-119 5.97e-03

Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. The YlqF subfamily is represented in all eukaryotes as well as a phylogenetically diverse array of bacteria (including gram-positive bacteria, proteobacteria, Synechocystis, Borrelia, and Thermotoga).


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 37.12  E-value: 5.97e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10946678  64 RVALIGFPSVGKSTFLSLMTSTASEAASYEfttltciPGV------IEYKGaNIQLLDLPGI 119
Cdd:cd01856 117 RAMVVGIPNVGKSTLINRLRGKKVAKVGNK-------PGVtrgqqwIRIGP-NIELLDTPGI 170
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 64-152 7.59e-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: 36.70  E-value: 7.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  64 RVALIGFPSVGKSTFLSLMTStaSEAAsyeftTLTCIPG----VIE----YKGANIQLLDLPGI------IEGAAQGRGR 129
Cdd:cd04164   5 KVVIAGKPNVGKSSLLNALAG--RDRA-----IVSDIAGttrdVIEeeidLGGIPVRLIDTAGLretedeIEKIGIERAR 77

                        90       100
                ....*....|....*....|...
gi 10946678 130 GRqviavARTADVVVMMLDATKG 152
Cdd:cd04164  78 EA-----IEEADLVLLVVDASEG 95
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 30-153 8.91e-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: 37.73  E-value: 8.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946678  30 LKAKLAKYRAQLLEPSKSASsKGEgfdVMKSGdARVALIGFPSVGKSTFLSLMtsTASEAAsyeftTLTCIPG----VIE 105
Cdd:COG0486 186 LLERLEELREELEALLASAR-QGE---LLREG-IKVVIVGRPNVGKSSLLNAL--LGEERA-----IVTDIAGttrdVIE 253

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 10946678 106 ----YKGANIQLLDLPGI------IEgaAQGRGRGRQVIAvarTADVVVMMLDATKGD 153
Cdd:COG0486 254 erinIGGIPVRLIDTAGLretedeVE--KIGIERAREAIE---EADLVLLLLDASEPL 306
 
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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