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Conserved domains on  [gi|4758796|ref|NP_004138|]
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developmentally-regulated GTP-binding protein 1 [Homo sapiens]

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];
7-367 3.79e-165

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


:

Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 466.20  E-value: 3.79e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796    7 KIAEIEAEMARTQKNKATAHHLGLLKARLAKLRRELITPKGGGGGGPGEgFDVAKTGDARIGFVGFPSVGKSTLLSNLAG 86
Cdd:COG1163   7 KIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEG-FAVKKSGDATVVLVGFPSVGKSTLLNKLTN 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   87 VYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNLILIVLDVLKPlGHKKIIENELE 166
Cdd:COG1163  86 AKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFEL-EQYDVLKEELY 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  167 GFGIRLNSKPPNIGFKKKDKGGINLTATCPQsELDAETVKSILAEYKIHNADVTLRSDATADDLIDVVEGNRVYIPCIYV 246
Cdd:COG1163 165 DAGIRLNKPPPDVTIEKKGKGGIRVNSTGKL-DLDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRVYKPAIVV 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  247 LNKIDQISIEELDIIYK-----VPHcVPISAHHRWNFDDLLEKIWDYLKLVRIYTKPKGQLPDYTSPVVLPySRTTVEDF 321
Cdd:COG1163 244 VNKIDLADEEYVEELKSklpdgVPV-IFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILR-KGSTVGDV 321

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 4758796  322 CMKIHKNLIKEFKYALVWGLSVKHNPQKVGKDHTLEDEDVIQIVKK 367
Cdd:COG1163 322 CEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIK 367
 
Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
7-367 3.79e-165

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 466.20  E-value: 3.79e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796    7 KIAEIEAEMARTQKNKATAHHLGLLKARLAKLRRELITPKGGGGGGPGEgFDVAKTGDARIGFVGFPSVGKSTLLSNLAG 86
Cdd:COG1163   7 KIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEG-FAVKKSGDATVVLVGFPSVGKSTLLNKLTN 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   87 VYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNLILIVLDVLKPlGHKKIIENELE 166
Cdd:COG1163  86 AKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFEL-EQYDVLKEELY 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  167 GFGIRLNSKPPNIGFKKKDKGGINLTATCPQsELDAETVKSILAEYKIHNADVTLRSDATADDLIDVVEGNRVYIPCIYV 246
Cdd:COG1163 165 DAGIRLNKPPPDVTIEKKGKGGIRVNSTGKL-DLDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRVYKPAIVV 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  247 LNKIDQISIEELDIIYK-----VPHcVPISAHHRWNFDDLLEKIWDYLKLVRIYTKPKGQLPDYTSPVVLPySRTTVEDF 321
Cdd:COG1163 244 VNKIDLADEEYVEELKSklpdgVPV-IFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILR-KGSTVGDV 321

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 4758796  322 CMKIHKNLIKEFKYALVWGLSVKHNPQKVGKDHTLEDEDVIQIVKK 367
Cdd:COG1163 322 CEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIK 367
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 65-297 6.52e-157

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: 439.67  E-value: 6.52e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNL 144
Cdd:cd01896   1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  145 ILIVLDVLKPLGHKKIIENELEGFGIRLNSKPPNIGFKKKDKGGINLTATCPQSELDAETVKSILAEYKIHNADVTLRSD 224
Cdd:cd01896  81 ILIVLDATKPEGQREILERELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLTKLDEKTVKAILREYKIHNADVLIRED 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758796  225 ATADDLIDVVEGNRVYIPCIYVLNKIDQISIEELDIIYKVPHCVPISAHHRWNFDDLLEKIWDYLKLVRIYTK 297
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 ...
 187-291 3.93e-63

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: 196.88  E-value: 3.93e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796    187 GGINLTATCPQSELDAETVKSILAEYKIHNADVTLRSDATADDLIDVVEGNRVYIPCIYVLNKIDQISIEELDIIYKVPH 266
Cdd:pfam16897   1 GGINITSTVPLTKLDEETIKAILREYKIHNADVLIREDVTVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDRLAREPD 80

                          90       100
                  ....*....|....*....|....*
gi 4758796    267 CVPISAHHRWNFDDLLEKIWDYLKL 291
Cdd:pfam16897  81 SVPISAEKGLNLDELKERIWEYLGL 105
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 64-217 8.07e-36

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: 128.26  E-value: 8.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796     64 DARIGFVGFPSVGKSTLLSNLAGVY-SEVAAYEFTTLTTVPGVIRYKG--AKIQLLDLPGIIEGAKDGKGRGRQVIAVAR 140
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKgSITEYYPGTTRNYVTTVIEEDGktYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796    141 TCNLILIVLDVLKPL-GHKKIIENELE-GFGIRLNSKPPNIG---FKKKDKGGINLTATCPQSELDAETVKSILAEYKIH 215
Cdd:TIGR00231  81 VFDIVILVLDVEEILeKQTKEIIHHADsGVPIILVGNKIDLKdadLKTHVASEFAKLNGEPIIPLSAETGKNIDSAFKIV 160


                  ..
gi 4758796    216 NA 217
Cdd:TIGR00231 161 EA 162
obgE PRK12299
GTPase CgtA; Reviewed
 65-176 1.75e-20

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 90.90  E-value: 1.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796    65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAK-IQLLDLPGIIEGAKDGKGRGRQVIA-VARtC 142
Cdd:PRK12299 159 ADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKsFVIADIPGLIEGASEGAGLGHRFLKhIER-T 237

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 4758796   143 NLILIVLDV--LKPLGHKKIIENELEGFGIRLNSKP 176
Cdd:PRK12299 238 RLLLHLVDIeaVDPVEDYKTIRNELEKYSPELADKP 273
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 67-150 6.87e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.58  E-value: 6.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796      67 IGFVGFPSVGKSTLLSNLAGvysEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNLIL 146
Cdd:smart00382   5 ILIVGPPGSGKTTLARALAR---ELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDV 81


                   ....
gi 4758796     147 IVLD 150
Cdd:smart00382  82 LILD 85
 
Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
7-367 3.79e-165

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 466.20  E-value: 3.79e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796    7 KIAEIEAEMARTQKNKATAHHLGLLKARLAKLRRELITPKGGGGGGPGEgFDVAKTGDARIGFVGFPSVGKSTLLSNLAG 86
Cdd:COG1163   7 KIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEG-FAVKKSGDATVVLVGFPSVGKSTLLNKLTN 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   87 VYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNLILIVLDVLKPlGHKKIIENELE 166
Cdd:COG1163  86 AKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFEL-EQYDVLKEELY 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  167 GFGIRLNSKPPNIGFKKKDKGGINLTATCPQsELDAETVKSILAEYKIHNADVTLRSDATADDLIDVVEGNRVYIPCIYV 246
Cdd:COG1163 165 DAGIRLNKPPPDVTIEKKGKGGIRVNSTGKL-DLDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRVYKPAIVV 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  247 LNKIDQISIEELDIIYK-----VPHcVPISAHHRWNFDDLLEKIWDYLKLVRIYTKPKGQLPDYTSPVVLPySRTTVEDF 321
Cdd:COG1163 244 VNKIDLADEEYVEELKSklpdgVPV-IFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILR-KGSTVGDV 321

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 4758796  322 CMKIHKNLIKEFKYALVWGLSVKHNPQKVGKDHTLEDEDVIQIVKK 367
Cdd:COG1163 322 CEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIK 367
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 65-297 6.52e-157

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: 439.67  E-value: 6.52e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNL 144
Cdd:cd01896   1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  145 ILIVLDVLKPLGHKKIIENELEGFGIRLNSKPPNIGFKKKDKGGINLTATCPQSELDAETVKSILAEYKIHNADVTLRSD 224
Cdd:cd01896  81 ILIVLDATKPEGQREILERELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLTKLDEKTVKAILREYKIHNADVLIRED 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758796  225 ATADDLIDVVEGNRVYIPCIYVLNKIDQISIEELDIIYKVPHCVPISAHHRWNFDDLLEKIWDYLKLVRIYTK 297
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 ...
 187-291 3.93e-63

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: 196.88  E-value: 3.93e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796    187 GGINLTATCPQSELDAETVKSILAEYKIHNADVTLRSDATADDLIDVVEGNRVYIPCIYVLNKIDQISIEELDIIYKVPH 266
Cdd:pfam16897   1 GGINITSTVPLTKLDEETIKAILREYKIHNADVLIREDVTVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDRLAREPD 80

                          90       100
                  ....*....|....*....|....*
gi 4758796    267 CVPISAHHRWNFDDLLEKIWDYLKL 291
Cdd:pfam16897  81 SVPISAEKGLNLDELKERIWEYLGL 105
TGS_DRG1 cd17230
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 1 ...
 288-367 4.54e-57

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: 180.16  E-value: 4.54e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  288 YLKLVRIYTKPKGQLPDYTSPVVLPYSRTTVEDFCMKIHKNLIKEFKYALVWGLSVKHNPQKVGKDHTLEDEDVIQIVKK 367
Cdd:cd17230   1 YLNLVRIYTKPKGQLPDYEEPVVLRSGKSTVEDFCNKIHKSLIKEFKYALVWGSSVKHNPQRVGKDHVLEDEDVVQIVKK 80
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 64-217 8.07e-36

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: 128.26  E-value: 8.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796     64 DARIGFVGFPSVGKSTLLSNLAGVY-SEVAAYEFTTLTTVPGVIRYKG--AKIQLLDLPGIIEGAKDGKGRGRQVIAVAR 140
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKgSITEYYPGTTRNYVTTVIEEDGktYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796    141 TCNLILIVLDVLKPL-GHKKIIENELE-GFGIRLNSKPPNIG---FKKKDKGGINLTATCPQSELDAETVKSILAEYKIH 215
Cdd:TIGR00231  81 VFDIVILVLDVEEILeKQTKEIIHHADsGVPIILVGNKIDLKdadLKTHVASEFAKLNGEPIIPLSAETGKNIDSAFKIV 160


                  ..
gi 4758796    216 NA 217
Cdd:TIGR00231 161 EA 162
TGS_DRG cd01666
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein ...
 289-366 3.56e-33

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


Pssm-ID: 340457 [Multi-domain]  Cd Length: 77  Bit Score: 118.11  E-value: 3.56e-33
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758796  289 LKLVRIYTKPKGQLPDYTSPVVLPySRTTVEDFCMKIHKNLIKEFKYALVWGLSVKHNPQKVGKDHTLEDEDVIQIVK 366
Cdd:cd01666   1 LGIIRVYTKPPGKKPDFDEPFILR-RGSTVEDVAEKIHKDLAENFKYARVWGKSVKFDGQRVGLDHVLEDGDIVEIHK 77
TGS_DRG2 cd17231
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 2 ...
 288-367 1.12e-31

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: 114.40  E-value: 1.12e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  288 YLKLVRIYTKPKGQLPDYTSPVVLpYSRTTVEDFCMKIHKNLIKEFKYALVWGLSVKHNPQKVGKDHTLEDEDVIQIVKK 367
Cdd:cd17231   1 YLALIRVYTKKRGERPDFGDAIIL-RRGATVEHVCHRIHRTLASQFKYALVWGTSTKYSPQRVGLTHVMEDEDVIQIVKK 79
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 68-187 3.48e-28

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: 108.25  E-value: 3.48e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   68 GFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYK-GAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNLIL 146
Cdd:cd01881   1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGdGVDIQIIDLPGLLDGASEGRGLGEQILAHLYRSDLIL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 4758796  147 IVLDVLK-----PLGHKKIIENELEGFGIRLNSKPPNIGFKKKDKG 187
Cdd:cd01881  81 HVIDASEdcvgdPLEDQKTLNEEVSGSFLFLKNKPEMIVANKIDMA 126
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 66-183 1.91e-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: 1.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796     66 RIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARtCNLI 145
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFLAIIE-ADLI 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 4758796    146 LIVLDVLKPLghkKIIENELEGFGIRLNsKPPNIGFKK 183
Cdd:pfam01926  80 LFVVDSEEGI---TPLDEELLELLRENK-KPIILVLNK 113
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 65-289 1.17e-25

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: 101.35  E-value: 1.17e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYK-GAKIQLLDLPGIIEGAKDGKGRG----RQviaVA 139
Cdd:cd01898   1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDdGRSFVIADIPGLIEGASEGKGLGhrflRH---IE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  140 RtCNLILIVLDV---LKPLGHKKIIENELEGFGIRLNSKppnigfkkkdkgginltatcpqseldaetvksilaeykihn 216
Cdd:cd01898  78 R-TRVLLHVIDLsgeDDPVEDYETIRNELEAYNPGLAEK----------------------------------------- 115

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  217 advtlrsdataddlidvvegnrvyiPCIYVLNKIDQISIEE-LDIIYKVP------HCVPISAHHRWNFDDLLEKIWDYL 289
Cdd:cd01898 116 -------------------------PRIVVLNKIDLLDAEErFEKLKELLkelkgkKVFPISALTGEGLDELLKKLAKLL 170
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
 65-289 2.26e-24

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: 101.73  E-value: 2.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796     65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAK-IQLLDLPGIIEGAKDGKGRGRQVIA-VARtC 142
Cdd:TIGR02729 158 ADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRsFVIADIPGLIEGASEGAGLGHRFLKhIER-T 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796    143 NLILIVLDV-----LKPLGHKKIIENELEGFGIRLNSKPpnigfkkkdkgginltatcpqseldaetvkSILaeykihna 217
Cdd:TIGR02729 237 RVLLHLIDIspedgSDPVEDYEIIRNELKKYSPELAEKP------------------------------RIV-------- 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796    218 dvtlrsdataddlidvvegnrvyipciyVLNKIDQISIEELDII---------YKVphcVPISAHHRWNFDDLLEKIWDY 288
Cdd:TIGR02729 279 ----------------------------VLNKIDLLDEEELEELlkelkkelgKPV---FPISALTGEGLDELLDALAEL 327


                  .
gi 4758796    289 L 289
Cdd:TIGR02729 328 L 328
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
 65-293 5.29e-22

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


Pssm-ID: 440302 [Multi-domain]  Cd Length: 343  Bit Score: 95.43  E-value: 5.29e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAK-IQLLDLPGIIEGAKDGKGRG----RQviaVA 139
Cdd:COG0536 158 ADVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGRsFVIADIPGLIEGASEGAGLGhrflRH---IE 234

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  140 RtCNLILIVLDV-----LKPLGHKKIIENELEGFGIRLNSKppnigfkkkdkgginltatcpqseldaetvksilaeyki 214
Cdd:COG0536 235 R-TRVLLHVVDAapldgRDPVEDYEIIRNELEAYSPELAEK--------------------------------------- 274

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  215 hnadvtlrsdataddlidvvegnrvyiPCIYVLNKIDQISIEELDII--------YKVphcVPISAHHRWNFDDLLEKIW 286
Cdd:COG0536 275 ---------------------------PRIVVLNKIDLLDAEELEELkaeleklgGPV---FPISAVTGEGLDELLYALA 324


                ....*..
gi 4758796  287 DYLKLVR 293
Cdd:COG0536 325 ELLEELR 331
obgE PRK12299
GTPase CgtA; Reviewed
 65-176 1.75e-20

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 90.90  E-value: 1.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796    65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAK-IQLLDLPGIIEGAKDGKGRGRQVIA-VARtC 142
Cdd:PRK12299 159 ADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKsFVIADIPGLIEGASEGAGLGHRFLKhIER-T 237

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 4758796   143 NLILIVLDV--LKPLGHKKIIENELEGFGIRLNSKP 176
Cdd:PRK12299 238 RLLLHLVDIeaVDPVEDYKTIRNELEKYSPELADKP 273
obgE PRK12297
GTPase CgtA; Reviewed
 65-176 1.36e-19

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 89.39  E-value: 1.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796    65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAK-IQLLDLPGIIEGAKDGKGRGRQVIA-VARtC 142
Cdd:PRK12297 159 ADVGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRsFVMADIPGLIEGASEGVGLGHQFLRhIER-T 237

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 4758796   143 NLILIVLDVLK-----PLGHKKIIENELEGFGIRLNSKP 176
Cdd:PRK12297 238 RVIVHVIDMSGsegrdPIEDYEKINKELKLYNPRLLERP 276
TGS pfam02824
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ...
 292-366 1.16e-18

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: 78.74  E-value: 1.16e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4758796    292 VRIYTkPKGQLPDYTSPvvlpysrTTVEDFCMKIHKNLIKEFKYALVWGlsvkhnpQKVGKDHTLEDEDVIQIVK 366
Cdd:pfam02824   1 IRVYT-PDGKVPDLPRG-------ATPEDFAYAIHTSLAKKFIYAKVNG-------QLVGLDHPLEDGDVVEIVT 60
obgE PRK12298
GTPase CgtA; Reviewed
 65-290 5.71e-18

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 84.15  E-value: 5.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796    65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLttVP--GVIRYKGAK-IQLLDLPGIIEGAKDGKGRG-RQVIAVAR 140
Cdd:PRK12298 160 ADVGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTL--VPnlGVVRVDDERsFVVADIPGLIEGASEGAGLGiRFLKHLER 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   141 tCNLILIVLDVL-----KPLGHKKIIENELEGFGIRLNSKPpnigfkkkdkgginltatcpqseldaetvksilaeykih 215
Cdd:PRK12298 238 -CRVLLHLIDIApidgsDPVENARIIINELEKYSPKLAEKP--------------------------------------- 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   216 nadvtlrsdataddlidvvegnRVyipciYVLNKIDQISIEELD---------IIYKVPHCVpISAHHRWNFDDLLEKIW 286
Cdd:PRK12298 278 ----------------------RW-----LVFNKIDLLDEEEAEerakaiveaLGWEGPVYL-ISAASGLGVKELCWDLM 329


                 ....
gi 4758796   287 DYLK 290
Cdd:PRK12298 330 TFIE 333
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 68-285 3.40e-14

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: 69.58  E-value: 3.40e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   68 GFVGFPSVGKSTLLSNLAG-VYSEVAAYEFTTLTTVPGVIR-YKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNLI 145
Cdd:cd00880   1 AIFGRPNVGKSSLLNALLGqNVGIVSPIPGTTRDPVRKEWElLPLGPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  146 LIVLDvlkplghkkiienelegfgirlnskppnigfkkkdkGGINLTatcpqselDAETVKSILAEYKihnadvtlrsda 225
Cdd:cd00880  81 LLVVD------------------------------------SDLTPV--------EEEAKLGLLRERG------------ 104

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758796  226 taddlidvvegnrvyIPCIYVLNKIDQISIEELDIIYKVP--------HCVPISAHHRWNFDDLLEKI 285
Cdd:cd00880 105 ---------------KPVLLVLNKIDLVPESEEEELLRERklellpdlPVIAVSALPGEGIDELRKKI 157
obgE PRK12296
GTPase CgtA; Reviewed
 65-172 2.34e-13

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 71.05  E-value: 2.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796    65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLttVP--GVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIA-VARt 141
Cdd:PRK12296 160 ADVGLVGFPSAGKSSLISALSAAKPKIADYPFTTL--VPnlGVVQAGDTRFTVADVPGLIPGASEGKGLGLDFLRhIER- 236

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 4758796   142 CNLILIVLDVL------KPLGHKKIIENELEGFGIRL 172
Cdd:PRK12296 237 CAVLVHVVDCAtlepgrDPLSDIDALEAELAAYAPAL 273
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 68-285 1.18e-11

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


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 62.47  E-value: 1.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   68 GFVGFPSVGKSTLLSNLAGV-YSEVAAYEFTTLTTVPGVIRYKGA--KIQLLDLPGIIEGakDGKGRGRQVIAVARTCNL 144
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGeVGEVSDVPGTTRDPDVYVKELDKGkvKLVLVDTPGLDEF--GGLGREELARLLLRGADL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  145 ILIVLDvlkplghkkiienelegfgirlnskppnigfkkkdkgginltATCPQSELDAETVksILAEYKIHNadvtlrsd 224
Cdd:cd00882  79 ILLVVD------------------------------------------STDRESEEDAKLL--ILRRLRKEG-------- 106

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4758796  225 ataddlidvvegnrvyIPCIYVLNKIDQISIEELDIIY--------KVPHCVPISAHHRWNFDDLLEKI 285
Cdd:cd00882 107 ----------------IPIILVGNKIDLLEEREVEELLrleelakiLGVPVFEVSAKTGEGVDELFEKL 159
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
 67-273 9.18e-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: 62.25  E-value: 9.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   67 IGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGV--------------------------IRYkgAKIQLLDLPG 120
Cdd:cd01899   1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVgyvrvecpckelgvscnprygkcidgKRY--VPVELIDVAG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  121 IIEGAKDGKGRGRQVIAVARTCNLILIVLDV----------LKPLGHK-----KIIENELEG--FGIrLNSKPPNIgFKK 183
Cdd:cd01899  79 LVPGAHEGKGLGNQFLDDLRDADVLIHVVDAsggtdaegngVETGGYDplediEFLENEIDMwiYGI-LERNWEKI-VRK 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  184 KDKGGINLtatcpqseldAETVKSILA-----EYKIHNADVTLRSDA-----TADDLIDVVEGNRVYI-PCIYVLNKIDQ 252
Cdd:cd01899 157 AKAEKTDI----------VEALSEQLSgfgvnEDVVIEALEELELPAdlskwDDEDLLRLARELRKRRkPMVIAANKADI 226

                       250       260
                ....*....|....*....|....*
gi 4758796  253 IS----IEELDIIYKVPHCVPISAH 273
Cdd:cd01899 227 PDaeenISKLRLKYPDEIVVPTSAE 251
TGS_Obg cd04938
TGS (ThrRS, GTPase and SpoT) domain found in the Obg protein family; The Obg family of GTPases ...
 290-365 2.88e-10

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: 55.91  E-value: 2.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  290 KLVRIYTKPKGQL-------PDYTSPVVLPySRTTVEDFCMKIHKNLIKEFKYALVWGlsvkhNPQKVGKDHTLEDEDVI 362
Cdd:cd04938   1 GLIPVYPVKNIQTftngsgnSVFRDCVLVK-KGTTVKDFANKIHTDLEKGFINAEGIG-----GRRLEGEDYILQDNDVV 74


                ...
gi 4758796  363 QIV 365
Cdd:cd04938  75 KFT 77
PRK09602 PRK09602
translation-associated GTPase; Reviewed
 66-365 4.87e-10

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 60.59  E-value: 4.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796    66 RIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGV--------------------------IRYkgAKIQLLDLP 119
Cdd:PRK09602   3 TIGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVayvrvecpckelgvkcnprngkcidgTRF--IPVELIDVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   120 GIIEGAKDGKGRGRQVIAVARTCNLILIVLDV----------LKPLGHK-----KIIENELEG--FGIRlnskppnigfk 182
Cdd:PRK09602  81 GLVPGAHEGRGLGNQFLDDLRQADALIHVVDAsgstdeegnpVEPGSHDpvediKFLEEELDMwiYGIL----------- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   183 KKDKGGINLTATcpQSELD-AETVKSILAEYKIHNADV--TLR--------SDATADDLIDVVEGNRVYI-PCIYVLNKI 250
Cdd:PRK09602 150 EKNWEKFSRKAQ--AEKFDiEEALAEQLSGLGINEEHVkeALRelglpedpSKWTDEDLLELARELRKISkPMVIAANKA 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   251 DQISIEE-LDIIYKVPH--CVPISAHHRW------------------NF---DDL-------LEKI-------------- 285
Cdd:PRK09602 228 DLPPAEEnIERLKEEKYyiVVPTSAEAELalrraakaglidyipgdsDFeilGELsekqkkaLEYIrevlkkyggtgvqe 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   286 ------WDYLKLVRIY--------TKPKGQ-LPDytsPVVLPYSrTTVEDFCMKIHKNLIKEFKYAlvwgLSVKHNpQKV 350
Cdd:PRK09602 308 aintavFDLLDMIVVYpvedenklTDKKGNvLPD---AFLLPKG-STARDLAYKIHTDIGEGFLYA----IDARTK-RRI 378

                        410
                 ....*....|....*
gi 4758796   351 GKDHTLEDEDVIQIV 365
Cdd:PRK09602 379 GEDYELKDGDVIKIV 393
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 71-216 5.46e-09

Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in eukaryotes ranging from trypanosomes to humans. NOG1 is functionally linked to ribosome biogenesis and found in association with the nuclear pore complexes and identified in many preribosomal complexes. Thus, defects in NOG1 can lead to defects in 60S biogenesis. The S. cerevisiae NOG1 gene is essential for cell viability, and mutations in the predicted G motifs abrogate function. It is a member of the ODN family of GTP-binding proteins that also includes the bacterial Obg and DRG proteins.


Pssm-ID: 206684 [Multi-domain]  Cd Length: 167  Bit Score: 54.87  E-value: 5.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   71 GFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGI----------IEgakdgkgrgRQVI-AVA 139
Cdd:cd01897   7 GYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLRWQVIDTPGIldrpleerntIE---------MQAItALA 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4758796  140 RTCNLILIVLDVLKPLGHKkiIENELEGF-GIR-LNSKPPNIGFKKKDKgginltatCPQSELDAETVKSILAEYKIHN 216
Cdd:cd01897  78 HLRAAVLFFIDPSETCGYS--IEEQLSLFkEIKpLFNKPVIVVLNKIDL--------LTEEDLSEIEKELEKEGEEVIK 146
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 241-315 6.37e-09

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 57.02  E-value: 6.37e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758796  241 IPCIYVLNKIDQISIEELDII-YKVPHCVPISAHHRWNFDDLLEKIWDYLKLVRIYTKpkgqlpdytspVVLPYSR 315
Cdd:COG2262 312 KPIILVFNKIDLLDDEELERLrAGYPDAVFISAKTGEGIDELLEAIEERLPEDRVEVE-----------LLLPYSD 376
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
71-123 3.12e-08

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 54.45  E-value: 3.12e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 4758796   71 GFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIE 123
Cdd:COG1084 167 GYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGRYQVIDTPGLLD 219
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 206-285 6.45e-08

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


Pssm-ID: 206666 [Multi-domain]  Cd Length: 204  Bit Score: 52.46  E-value: 6.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  206 KSILAEykIHNADVTL----RSDATADDLIDVVEgnRVY-------IPCIYVLNKIDQISIEELD--IIYKVPHCVPISA 272
Cdd:cd01878 112 RSTLEE--VAEADLLLhvvdASDPDREEQIETVE--EVLkelgaddIPIILVLNKIDLLDDEELEerLRAGRPDAVFISA 187

                        90
                ....*....|...
gi 4758796  273 HHRWNFDDLLEKI 285
Cdd:cd01878 188 KTGEGLDLLKEAI 200
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 69-121 1.28e-07

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: 50.53  E-value: 1.28e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 4758796   69 FVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGI 121
Cdd:cd01879   2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPGT 54
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
66-121 8.10e-07

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 50.89  E-value: 8.10e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4758796   66 RIGFVGFPSVGKSTLLSNLAGVYSEVAAYefttlttvPGV--------IRYKGAKIQLLDLPGI 121
Cdd:COG0370   5 TIALVGNPNVGKTTLFNALTGSRQKVGNW--------PGVtvekkegkFKLKGKEIELVDLPGT 60
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 70-289 2.52e-06

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


Pssm-ID: 206681 [Multi-domain]  Cd Length: 157  Bit Score: 46.66  E-value: 2.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   70 VGFPSVGKSTLLSNLAGVYSE-VAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAK--DGKGRgRQVIAVARTCNLIL 146
Cdd:cd01894   3 VGRPNVGKSTLFNRLTGRRDAiVSDTPGVTRDRKYGEAEWGGREFILIDTGGIEPDDEgiSKEIR-EQAEIAIEEADVIL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  147 IVLDVlkplghkkiienelegfgirlnskppnigfkkkdKGGInltatcpqSELDAEtvksiLAEYkihnadvtLRsdat 226
Cdd:cd01894  82 FVVDG----------------------------------REGL--------TPADEE-----IAKY--------LR---- 102

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4758796  227 addlidvvegnRVYIPCIYVLNKIDQISIE-ELDIIYK--VPHCVPISAHHRWNFDDLLEKIWDYL 289
Cdd:cd01894 103 -----------KSKKPVILVVNKIDNIKEEeEAAEFYSlgFGEPIPISAEHGRGIGDLLDAILELL 157
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 66-289 3.97e-06

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: 46.30  E-value: 3.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   66 RIGFV---GFPSVGKSTLLSNLAGvySEVAAYEF---TTLTTVPGVIRYKGAKIQLLDLPGIIEG-AKDGKGRGRQVIAV 138
Cdd:cd04163   2 KSGFVaiiGRPNVGKSTLLNALVG--QKISIVSPkpqTTRNRIRGIYTDDDAQIIFVDTPGIHKPkKKLGERMVKAAWSA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  139 ARTCNLILIVLDVLKPLGHkkiienelegfgirlnskppnigfkkkdkgginltatcpqselDAETVKSILAEYKIhnad 218
Cdd:cd04163  80 LKDVDLVLFVVDASEWIGE-------------------------------------------GDEFILELLKKSKT---- 112

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4758796  219 vtlrsdataddlidvvegnrvyiPCIYVLNKIDQIS--------IEELDIIYKVPHCVPISAHHRWNFDDLLEKIWDYL 289
Cdd:cd04163 113 -----------------------PVILVLNKIDLVKdkedllplLEKLKELHPFAEIFPISALKGENVDELLEYIVEYL 168
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 66-162 9.58e-05

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


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 42.42  E-value: 9.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   66 RIGFVGFPSVGKSTLLSNLAG----VYSEVAAyefTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKdgKGRGRQVIAVART 141
Cdd:cd01895   4 KIAIIGRPNVGKSSLLNALLGeervIVSDIAG---TTRDSIDVPFEYDGQKYTLIDTAGIRKKGK--VTEGIEKYSVLRT 78

                        90       100
                ....*....|....*....|....*....
gi 4758796  142 ------CNLILIVLDVLKPLGH--KKIIE 162
Cdd:cd01895  79 lkaierADVVLLVLDASEGITEqdLRIAG 107
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 68-154 1.94e-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: 41.17  E-value: 1.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   68 GFVGFPSVGKSTLLSNLAGvySEVAAYEFTTLTTV---PGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNL 144
Cdd:cd11383   1 GLMGKTGAGKSSLCNALFG--TEVAAVGDRRPTTRaaqAYVWQTGGDGLVLLDLPGVGERGRRDREYEELYRRLLPEADL 78

                        90
                ....*....|
gi 4758796  145 ILIVLDVLKP 154
Cdd:cd11383  79 VLWLLDADDR 88
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 66-220 1.98e-04

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 43.01  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796    66 RIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTL------TTVPG------VIRYKGAKI-----QLLDLPGIIEGAKDG 128
Cdd:PTZ00258  23 KMGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIdpntarVNVPDerfdwlCKHFKPKSIvpaqlDITDIAGLVKGASEG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   129 KGRGRQVIAVARTCNLILIVL------------DVLKPLGHKKIIENEL-----EGFGIRLNSKPPNIGFKKKDKGGinl 191
Cdd:PTZ00258 103 EGLGNAFLSHIRAVDGIYHVVrafededithveGEIDPVRDLEIISSELilkdlEFVEKRLDELTKKRKKKKKKKEE--- 179

                        170       180       190
                 ....*....|....*....|....*....|.
gi 4758796   192 tatcpQSELDA-ETVKSILAEYK-IHNADVT 220
Cdd:PTZ00258 180 -----KVELDVlKKVLEWLEEGKpVRDGDWT 205
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 66-121 4.57e-04

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


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 40.59  E-value: 4.57e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4758796   66 RIGFVGFPSVGKSTLLSNLAGV-YSEVAAyefttlttVPGV------IRYKGaKIQLLDLPGI 121
Cdd:cd01856 117 RAMVVGIPNVGKSTLINRLRGKkVAKVGN--------KPGVtrgqqwIRIGP-NIELLDTPGI 170
TGS_MJ1332_like cd01669
TGS (ThrRS, GTPase and SpoT) domain found in Methanocaldococcus jannaschii uncharacterized ...
 302-365 5.52e-04

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: 38.06  E-value: 5.52e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4758796  302 LPDytspVVLPYSRTTVEDFCMKIHKNLIKEFKYALvwglSVKHNpQKVGKDHTLEDEDVIQIV 365
Cdd:cd01669  23 LPD----AILLKRGSTPRDLAYKIHTDLGKGFLYAI----DARTK-MRLGEDYELKHGDVVKIV 77
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 213-285 5.69e-04

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: 41.31  E-value: 5.69e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4758796    213 KIHNADVTL----RSDATADDLIDVVEGNRVYIPCIYVLNKIDQISIEELDIIYKVPHCVPISAHHRWNFDDLLEKI 285
Cdd:pfam12631 170 AIEEADLVLlvldASRPLDEEDLEILELLKDKKPIIVVLNKSDLLGEIDELEELKGKPVLAISAKTGEGLDELEEAI 246
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
67-289 6.79e-04

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 41.13  E-value: 6.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   67 IGFVGFPSVGKSTLLSNLAG-----VySEVAAyefTTLTTVPGVIRYKGAKIQLLDLPGIIEgAKDGKGRG--RQVIAVA 139
Cdd:COG1159   6 VAIVGRPNVGKSTLLNALVGqkvsiV-SPKPQ---TTRHRIRGIVTREDAQIVFVDTPGIHK-PKRKLGRRmnKAAWSAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  140 RTCNLILIVLDVLKPLGHkkiienelegfgirlnskppnigfkkkdkgginltatcpqselDAETVKSILAEYKIhnadv 219
Cdd:COG1159  81 EDVDVILFVVDATEKIGE-------------------------------------------GDEFILELLKKLKT----- 112

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4758796  220 tlrsdataddlidvvegnrvyiPCIYVLNKIDQIS-------IEELDIIYKVPHCVPISAHHRWNFDDLLEKIWDYL 289
Cdd:COG1159 113 ----------------------PVILVINKIDLVKkeellplLAEYSELLDFAEIVPISALKGDNVDELLDEIAKLL 167
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
242-290 1.34e-03

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 40.39  E-value: 1.34e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 4758796  242 PCIYVLNKIDqiSIEELDIIYK-----VPHCVPISAHHRWNFDDLLEKIWDYLK 290
Cdd:COG1160 113 PVILVVNKVD--GPKREADAAEfyslgLGEPIPISAEHGRGVGDLLDAVLELLP 164
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 210-285 1.38e-03

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


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 39.01  E-value: 1.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796  210 AEYKIHNADVTL-----RSDATADD--LIDVVEGNRVyipcIYVLNKIDQISIEELDIIYKVPHCVPISAHHRWNFDDLL 282
Cdd:cd04164  76 AREAIEEADLVLlvvdaSEGLDEEDleILELPAKKPV----IVVLNKSDLLSDAEGISELNGKPIIAISAKTGEGIDELK 151


                ...
gi 4758796  283 EKI 285
Cdd:cd04164 152 EAL 154
era PRK00089
GTPase Era; Reviewed
 237-289 1.46e-03

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 40.03  E-value: 1.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4758796   237 NRVYIPCIYVLNKIDQIS--------IEELDIIYKVPHCVPISAHHRWNFDDLLEKIWDYL 289
Cdd:PRK00089 110 KKVKTPVILVLNKIDLVKdkeellplLEELSELMDFAEIVPISALKGDNVDELLDVIAKYL 170
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 59-155 3.47e-03

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 39.39  E-value: 3.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796    59 VAKTGDARIGFVGFPSVGKSTLLSNLAG----VYSEVAAyefTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKG---- 130
Cdd:PRK09518 445 LTPSGLRRVALVGRPNVGKSSLLNQLTHeeraVVNDLAG---TTRDPVDEIVEIDGEDWLFIDTAGIKRRQHKLTGaeyy 521

                         90       100
                 ....*....|....*....|....*...
gi 4758796   131 ---RGRQVIavaRTCNLILIVLDVLKPL 155
Cdd:PRK09518 522 sslRTQAAI---ERSELALFLFDASQPI 546
YeeP COG3596
Predicted GTPase [General function prediction only];
66-154 4.26e-03

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 38.59  E-value: 4.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796   66 RIGFVGFPSVGKSTLLSNLAGV-YSEVAAYEFTtlTTVPGVIRYK---GAKIQLLDLPGIIEGAKDGKgRGRQVIAVART 141
Cdd:COG3596  41 VIALVGKTGAGKSSLINALFGAeVAEVGVGRPC--TREIQRYRLEsdgLPGLVLLDTPGLGEVNERDR-EYRELRELLPE 117

                        90
                ....*....|...
gi 4758796  142 CNLILIVLDVLKP 154
Cdd:COG3596 118 ADLILWVVKADDR 130
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
 66-123 4.56e-03

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: 38.52  E-value: 4.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4758796     66 RIGFVGFPSVGKSTLLSNLAG----VYSEVAAyefTTLTTVPGVIRYKGAKIQLLDLPGIIE 123
Cdd:TIGR00436   2 FVAILGRPNVGKSTLLNQLHGqkisITSPKAQ---TTRNRISGIHTTGASQIIFIDTPGFHE 60
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 67-150 6.87e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.58  E-value: 6.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796      67 IGFVGFPSVGKSTLLSNLAGvysEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNLIL 146
Cdd:smart00382   5 ILIVGPPGSGKTTLARALAR---ELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDV 81


                   ....
gi 4758796     147 IVLD 150
Cdd:smart00382  82 LILD 85
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 241-289 7.29e-03

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


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 37.12  E-value: 7.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4758796    241 IPCIYVLNKIDQISIEELDIIYK---------------VPHCVPISAHHRWNFDDLLEKIWDYL 289
Cdd:pfam00009 122 VPIIVFINKMDRVDGAELEEVVEevsrellekygedgeFVPVVPGSALKGEGVQTLLDALDEYL 185
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 63-155 8.96e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 38.03  E-value: 8.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758796    63 GDARIGFVGFPSVGKSTLLSNLAG----VYSEVAAyefTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKG-------R 131
Cdd:PRK03003 210 GPRRVALVGKPNVGKSSLLNKLAGeersVVDDVAG---TTVDPVDSLIELGGKTWRFVDTAGLRRRVKQASGheyyaslR 286

                         90       100
                 ....*....|....*....|....
gi 4758796   132 GRQVIAVARTCnliLIVLDVLKPL 155
Cdd:PRK03003 287 THAAIEAAEVA---VVLIDASEPI 307
 
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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