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Conserved domains on  [gi|1570043770|gb|RYP42347|]
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hypothetical protein DL767_000269 [Monosporascus sp. MG133]

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];
4-367 6.18e-150

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


:

Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 427.68  E-value: 6.18e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770   4 ITDKIKEIEDEMRRTQKNKATEYHLGLLKGKLARLRAQLlEPGPGSGSGGGAGFDVSKSGDARIALVGFPSVGKSTFLSK 83
Cdd:COG1163     4 IEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEEL-EKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLLNK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  84 VTKTRSEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGIIEGAAEGKGRGRQVISAAKTSDLILMVLDATKRaEQRTLLEA 163
Cdd:COG1163    83 LTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFEL-EQYDVLKE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770 164 ELEAVGIRLNREPPNIYLKQKKAGGMKITFQSPPKnLDEKMVFNILRDYKLLNVEVLVRDDeATVDDLIDVIMKDhRKYI 243
Cdd:COG1163   162 ELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLD-LDEEDIKKILREYGIVNADVLIRED-VTLDDLIDALMGN-RVYK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770 244 KCLYVYNKIDSVSIEFLD----KLAREPNTAVMSCEMDLGIQDVVDRCWKELQLIRIYTKRKGSDPDFSEALIVRNNSTI 319
Cdd:COG1163   239 PAIVVVNKIDLADEEYVEelksKLPDGVPVIFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKGSTV 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1570043770 320 EDVCDRIHRTLKDTYKYALVWGASARHVPQRVGLSHVVADEDVVYIVS 367
Cdd:COG1163   319 GDVCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIII 366
 
Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
4-367 6.18e-150

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 427.68  E-value: 6.18e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770   4 ITDKIKEIEDEMRRTQKNKATEYHLGLLKGKLARLRAQLlEPGPGSGSGGGAGFDVSKSGDARIALVGFPSVGKSTFLSK 83
Cdd:COG1163     4 IEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEEL-EKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLLNK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  84 VTKTRSEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGIIEGAAEGKGRGRQVISAAKTSDLILMVLDATKRaEQRTLLEA 163
Cdd:COG1163    83 LTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFEL-EQYDVLKE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770 164 ELEAVGIRLNREPPNIYLKQKKAGGMKITFQSPPKnLDEKMVFNILRDYKLLNVEVLVRDDeATVDDLIDVIMKDhRKYI 243
Cdd:COG1163   162 ELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLD-LDEEDIKKILREYGIVNADVLIRED-VTLDDLIDALMGN-RVYK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770 244 KCLYVYNKIDSVSIEFLD----KLAREPNTAVMSCEMDLGIQDVVDRCWKELQLIRIYTKRKGSDPDFSEALIVRNNSTI 319
Cdd:COG1163   239 PAIVVVNKIDLADEEYVEelksKLPDGVPVIFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKGSTV 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1570043770 320 EDVCDRIHRTLKDTYKYALVWGASARHVPQRVGLSHVVADEDVVYIVS 367
Cdd:COG1163   319 GDVCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIII 366
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 65-299 8.75e-133

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: 378.81  E-value: 8.75e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  65 ARIALVGFPSVGKSTFLSKVTKTRSEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGIIEGAAEGKGRGRQVISAAKTSDL 144
Cdd:cd01896     1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770 145 ILMVLDATKRAEQRTLLEAELEAVGIRLNREPPNIYLKQKKAGGMKITFQSPPKNLDEKMVFNILRDYKLLNVEVLVRDD 224
Cdd:cd01896    81 ILIVLDATKPEGQREILERELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLTKLDEKTVKAILREYKIHNADVLIRED 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1570043770 225 eATVDDLIDVIMkDHRKYIKCLYVYNKIDSVSIEFLDKLAREPNTAVMSCEMDLGIQDVVDRCWKELQLIRIYTK 299
Cdd:cd01896   161 -ITVDDLIDVIE-GNRVYIPCLYVYNKIDLISIEELDRLARIPNSVVISAEKDLNLDELLERIWDYLGLIRIYTK 233
MMR_HSR1_Xtn pfam16897
C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of ...
 187-293 2.63e-46

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: 153.35  E-value: 2.63e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770 187 GGMKITFQSPPKNLDEKMVFNILRDYKLLNVEVLVRDDeATVDDLIDVIMkDHRKYIKCLYVYNKIDSVSIEFLDKLARE 266
Cdd:pfam16897   1 GGINITSTVPLTKLDEETIKAILREYKIHNADVLIRED-VTVDDLIDVIE-GNRVYIPCLYVYNKIDLISIEELDRLARE 78

                          90       100
                  ....*....|....*....|....*..
gi 1570043770 267 PNTAVMSCEMDLGIQDVVDRCWKELQL 293
Cdd:pfam16897  79 PDSVPISAEKGLNLDELKERIWEYLGL 105
obgE PRK12297
GTPase CgtA; Reviewed
 65-134 2.93e-21

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 94.40  E-value: 2.93e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1570043770  65 ARIALVGFPSVGKSTFLSKVTKTRSEVASYAFTTLTAIPGVLEYGGAE-IQLLDLPGIIEGAAEGKGRGRQ 134
Cdd:PRK12297  159 ADVGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRsFVMADIPGLIEGASEGVGLGHQ 229
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
 65-132 6.93e-21

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: 92.10  E-value: 6.93e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1570043770  65 ARIALVGFPSVGKSTFLSKVTKTRSEVASYAFTTLTAIPGVLEYGGA-EIQLLDLPGIIEGAAEGKGRG 132
Cdd:TIGR02729 158 ADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGrSFVIADIPGLIEGASEGAGLG 226
 
Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
4-367 6.18e-150

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 427.68  E-value: 6.18e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770   4 ITDKIKEIEDEMRRTQKNKATEYHLGLLKGKLARLRAQLlEPGPGSGSGGGAGFDVSKSGDARIALVGFPSVGKSTFLSK 83
Cdd:COG1163     4 IEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEEL-EKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLLNK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  84 VTKTRSEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGIIEGAAEGKGRGRQVISAAKTSDLILMVLDATKRaEQRTLLEA 163
Cdd:COG1163    83 LTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFEL-EQYDVLKE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770 164 ELEAVGIRLNREPPNIYLKQKKAGGMKITFQSPPKnLDEKMVFNILRDYKLLNVEVLVRDDeATVDDLIDVIMKDhRKYI 243
Cdd:COG1163   162 ELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLD-LDEEDIKKILREYGIVNADVLIRED-VTLDDLIDALMGN-RVYK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770 244 KCLYVYNKIDSVSIEFLD----KLAREPNTAVMSCEMDLGIQDVVDRCWKELQLIRIYTKRKGSDPDFSEALIVRNNSTI 319
Cdd:COG1163   239 PAIVVVNKIDLADEEYVEelksKLPDGVPVIFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKGSTV 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1570043770 320 EDVCDRIHRTLKDTYKYALVWGASARHVPQRVGLSHVVADEDVVYIVS 367
Cdd:COG1163   319 GDVCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIII 366
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 65-299 8.75e-133

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: 378.81  E-value: 8.75e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  65 ARIALVGFPSVGKSTFLSKVTKTRSEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGIIEGAAEGKGRGRQVISAAKTSDL 144
Cdd:cd01896     1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770 145 ILMVLDATKRAEQRTLLEAELEAVGIRLNREPPNIYLKQKKAGGMKITFQSPPKNLDEKMVFNILRDYKLLNVEVLVRDD 224
Cdd:cd01896    81 ILIVLDATKPEGQREILERELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLTKLDEKTVKAILREYKIHNADVLIRED 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1570043770 225 eATVDDLIDVIMkDHRKYIKCLYVYNKIDSVSIEFLDKLAREPNTAVMSCEMDLGIQDVVDRCWKELQLIRIYTK 299
Cdd:cd01896   161 -ITVDDLIDVIE-GNRVYIPCLYVYNKIDLISIEELDRLARIPNSVVISAEKDLNLDELLERIWDYLGLIRIYTK 233
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 68-291 3.21e-50

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: 166.03  E-value: 3.21e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  68 ALVGFPSVGKSTFLSKVTKTRSEVASYAFTTLTAIPGVLEYG-GAEIQLLDLPGIIEGAAEGKGRGRQVISAAKTSDLIL 146
Cdd:cd01881     1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGdGVDIQIIDLPGLLDGASEGRGLGEQILAHLYRSDLIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770 147 MVLDATKRAeqrtlleaeleavgirlnreppniylkqkkaggmkitfqsppknldekmVFNILRDYKLLNVEVLVRDDEa 226
Cdd:cd01881    81 HVIDASEDC-------------------------------------------------VGDPLEDQKTLNEEVSGSFLF- 110

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770 227 tvddlidvimkdhRKYIKCLYVYNKIDSVSIEFL-----DKLAREPNTAVMSCEMDLGIQDVVDRCWKEL 291
Cdd:cd01881   111 -------------LKNKPEMIVANKIDMASENNLkrlklDKLKRGIPVVPTSALTRLGLDRVIRTIRKLL 167
MMR_HSR1_Xtn pfam16897
C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of ...
 187-293 2.63e-46

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: 153.35  E-value: 2.63e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770 187 GGMKITFQSPPKNLDEKMVFNILRDYKLLNVEVLVRDDeATVDDLIDVIMkDHRKYIKCLYVYNKIDSVSIEFLDKLARE 266
Cdd:pfam16897   1 GGINITSTVPLTKLDEETIKAILREYKIHNADVLIRED-VTVDDLIDVIE-GNRVYIPCLYVYNKIDLISIEELDRLARE 78

                          90       100
                  ....*....|....*....|....*..
gi 1570043770 267 PNTAVMSCEMDLGIQDVVDRCWKELQL 293
Cdd:pfam16897  79 PDSVPISAEKGLNLDELKERIWEYLGL 105
TGS_DRG2 cd17231
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 2 ...
 290-368 9.64e-45

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: 148.69  E-value: 9.64e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1570043770 290 ELQLIRIYTKRKGSDPDFSEALIVRNNSTIEDVCDRIHRTLKDTYKYALVWGASARHVPQRVGLSHVVADEDVVYIVSG 368
Cdd:cd17231     1 YLALIRVYTKKRGERPDFGDAIILRRGATVEHVCHRIHRTLASQFKYALVWGTSTKYSPQRVGLTHVMEDEDVIQIVKK 79
TGS_DRG1 cd17230
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 1 ...
 291-366 1.46e-34

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: 122.00  E-value: 1.46e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1570043770 291 LQLIRIYTKRKGSDPDFSEALIVRNN-STIEDVCDRIHRTLKDTYKYALVWGASARHVPQRVGLSHVVADEDVVYIV 366
Cdd:cd17230     2 LNLVRIYTKPKGQLPDYEEPVVLRSGkSTVEDFCNKIHKSLIKEFKYALVWGSSVKHNPQRVGKDHVLEDEDVVQIV 78
TGS_DRG cd01666
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein ...
 291-366 1.05e-32

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


Pssm-ID: 340457 [Multi-domain]  Cd Length: 77  Bit Score: 116.95  E-value: 1.05e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1570043770 291 LQLIRIYTKRKGSDPDFSEALIVRNNSTIEDVCDRIHRTLKDTYKYALVWGASARHVPQRVGLSHVVADEDVVYIV 366
Cdd:cd01666     1 LGIIRVYTKPPGKKPDFDEPFILRRGSTVEDVAEKIHKDLAENFKYARVWGKSVKFDGQRVGLDHVLEDGDIVEIH 76
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 66-174 1.29e-28

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 107.32  E-value: 1.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  66 RIALVGFPSVGKSTFLSKVTKTRSEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGIIEGAAEGKGRGRQVISAAKtSDLI 145
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFLAIIE-ADLI 79

                          90       100
                  ....*....|....*....|....*....
gi 1570043770 146 LMVLDATkraEQRTLLEAELEAVGIRLNR 174
Cdd:pfam01926  80 LFVVDSE---EGITPLDEELLELLRENKK 105
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 65-176 5.10e-22

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: 91.72  E-value: 5.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  65 ARIALVGFPSVGKSTFLSKVTKTRSEVASYAFTTLTAIPGVLEYG-GAEIQLLDLPGIIEGAAEGKGRG----RQVisaa 139
Cdd:cd01898     1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDdGRSFVIADIPGLIEGASEGKGLGhrflRHI---- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1570043770 140 KTSDLILMVLDATKRA---EQRTLLEAELEAVGIRLNREP 176
Cdd:cd01898    77 ERTRVLLHVIDLSGEDdpvEDYETIRNELEAYNPGLAEKP 116
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
 65-167 1.02e-21

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: 94.66  E-value: 1.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  65 ARIALVGFPSVGKSTFLSKVTKTRSEVASYAFTTLTAIPGVLEYG-GAEIQLLDLPGIIEGAAEGKGRG----RQVisaA 139
Cdd:COG0536   158 ADVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGdGRSFVIADIPGLIEGASEGAGLGhrflRHI---E 234

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1570043770 140 KTSdLILMVLDATkRAEQRTLLEA------ELEA 167
Cdd:COG0536   235 RTR-VLLHVVDAA-PLDGRDPVEDyeiirnELEA 266
obgE PRK12297
GTPase CgtA; Reviewed
 65-134 2.93e-21

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 94.40  E-value: 2.93e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1570043770  65 ARIALVGFPSVGKSTFLSKVTKTRSEVASYAFTTLTAIPGVLEYGGAE-IQLLDLPGIIEGAAEGKGRGRQ 134
Cdd:PRK12297  159 ADVGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRsFVMADIPGLIEGASEGVGLGHQ 229
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
 65-132 6.93e-21

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: 92.10  E-value: 6.93e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1570043770  65 ARIALVGFPSVGKSTFLSKVTKTRSEVASYAFTTLTAIPGVLEYGGA-EIQLLDLPGIIEGAAEGKGRG 132
Cdd:TIGR02729 158 ADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGrSFVIADIPGLIEGASEGAGLG 226
obgE PRK12299
GTPase CgtA; Reviewed
 65-167 3.30e-20

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 90.13  E-value: 3.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  65 ARIALVGFPSVGKSTFLSKVTKTRSEVASYAFTTLTAIPGVLEYG-GAEIQLLDLPGIIEGAAEGKGRG----RQVisaA 139
Cdd:PRK12299  159 ADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDdYKSFVIADIPGLIEGASEGAGLGhrflKHI---E 235

                          90       100       110
                  ....*....|....*....|....*....|
gi 1570043770 140 KTSdLILMVLDATKRA--EQRTLLEAELEA 167
Cdd:PRK12299  236 RTR-LLLHLVDIEAVDpvEDYKTIRNELEK 264
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 68-172 1.86e-16

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: 76.13  E-value: 1.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  68 ALVGFPSVGKSTFLSKVT-KTRSEVASYAFTTLTAIPGVLE-YGGAEIQLLDLPGIIEGAAEGKGRGRQVISAAKTSDLI 145
Cdd:cd00880     1 AIFGRPNVGKSSLLNALLgQNVGIVSPIPGTTRDPVRKEWElLPLGPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80

                          90       100
                  ....*....|....*....|....*..
gi 1570043770 146 LMVLDATKRAEQRTLLEAELEAVGIRL 172
Cdd:cd00880    81 LLVVDSDLTPVEEEAKLGLLRERGKPV 107
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 64-179 2.33e-16

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: 75.87  E-value: 2.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  64 DARIALVGFPSVGKSTFLSKVTKT-RSEVASYAFTTLTAIPGVLEYGG--AEIQLLDLPGIIEGAAEGKGRGRQVISAAK 140
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNkGSITEYYPGTTRNYVTTVIEEDGktYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1570043770 141 TSDLILMVLDATK-RAEQRTLLEAELEA-VGIRLNREPPNI 179
Cdd:TIGR00231  81 VFDIVILVLDVEEiLEKQTKEIIHHADSgVPIILVGNKIDL 121
obgE PRK12298
GTPase CgtA; Reviewed
 65-132 7.78e-16

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 77.99  E-value: 7.78e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1570043770  65 ARIALVGFPSVGKSTFLSKVTKTRSEVASYAFTTLtaIP--GVLEYG-GAEIQLLDLPGIIEGAAEGKGRG 132
Cdd:PRK12298  160 ADVGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTL--VPnlGVVRVDdERSFVVADIPGLIEGASEGAGLG 228
obgE PRK12296
GTPase CgtA; Reviewed
 65-167 2.21e-15

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 77.22  E-value: 2.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  65 ARIALVGFPSVGKSTFLSKVTKTRSEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGIIEGAAEGKGRGRQVISAAKTSDL 144
Cdd:PRK12296  160 ADVGLVGFPSAGKSSLISALSAAKPKIADYPFTTLVPNLGVVQAGDTRFTVADVPGLIPGASEGKGLGLDFLRHIERCAV 239

                          90       100
                  ....*....|....*....|....*....
gi 1570043770 145 ILMVLD-ATKRAEQRTL-----LEAELEA 167
Cdd:PRK12296  240 LVHVVDcATLEPGRDPLsdidaLEAELAA 268
TGS pfam02824
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ...
 294-366 1.55e-14

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: 67.57  E-value: 1.55e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1570043770 294 IRIYTKrKGSDPDFsealivRNNSTIEDVCDRIHRTLKDTYKYALVWGasarhvpQRVGLSHVVADEDVVYIV 366
Cdd:pfam02824   1 IRVYTP-DGKVPDL------PRGATPEDFAYAIHTSLAKKFIYAKVNG-------QLVGLDHPLEDGDVVEIV 59
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
71-152 1.87e-14

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 73.33  E-value: 1.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  71 GFPSVGKSTFLSKVTKTRSEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGI----------IEgaaegkgrgRQVISAAK 140
Cdd:COG1084   167 GYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGRYQVIDTPGLldrplserneIE---------RQAILALK 237

                          90
                  ....*....|...
gi 1570043770 141 T-SDLILMVLDAT 152
Cdd:COG1084   238 HlADVILFLFDPS 250
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 67-162 4.17e-14

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: 69.51  E-value: 4.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  67 IALVGFPSVGKSTFLSKVTKTRSEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGI----------IEgaaegkgrgRQVI 136
Cdd:cd01897     3 LVIAGYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLRWQVIDTPGIldrpleerntIE---------MQAI 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1570043770 137 SA-AKTSDLILMVLDATKR-----AEQRTLLE 162
Cdd:cd01897    74 TAlAHLRAAVLFFIDPSETcgysiEEQLSLFK 105
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
 67-152 1.13e-13

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: 71.11  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  67 IALVGFPSVGKSTFLSKVTKTRSEVASYAFTTLTAIPGV---------LEYGGAE---------------IQLLDLPGII 122
Cdd:cd01899     1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVgyvrvecpcKELGVSCnprygkcidgkryvpVELIDVAGLV 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1570043770 123 EGAAEGKGRGRQVISAAKTSDLILMVLDAT 152
Cdd:cd01899    81 PGAHEGKGLGNQFLDDLRDADVLIHVVDAS 110
PRK09602 PRK09602
translation-associated GTPase; Reviewed
 66-367 6.56e-13

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 69.45  E-value: 6.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  66 RIALVGFPSVGKSTFLSKVTKTRSEVASYAFTTLTAIPGV---------LEYGG---------------AEIQLLDLPGI 121
Cdd:PRK09602    3 TIGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVayvrvecpcKELGVkcnprngkcidgtrfIPVELIDVAGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770 122 IEGAAEGKGRGRQVISAAKTSDLILMVLDATKraeqRTLLEAELEAVGIR--------LNRE---------PPNI--YLK 182
Cdd:PRK09602   83 VPGAHEGRGLGNQFLDDLRQADALIHVVDASG----STDEEGNPVEPGSHdpvedikfLEEEldmwiygilEKNWekFSR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770 183 QKKAGGMKITfqsppKNLDEKMV-FNILRD---YKLLNVEVLVRDDEATVDDLIDVImKDHRKYIK-CLYVYNKIDSVSI 257
Cdd:PRK09602  159 KAQAEKFDIE-----EALAEQLSgLGINEEhvkEALRELGLPEDPSKWTDEDLLELA-RELRKISKpMVIAANKADLPPA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770 258 -EFLDKLAREPNTAVMSC----EMDL---------------------------------------------GIQDVVDRC 287
Cdd:PRK09602  233 eENIERLKEEKYYIVVPTsaeaELALrraakaglidyipgdsdfeilgelsekqkkaleyirevlkkyggtGVQEAINTA 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770 288 -WKELQLIRIY---TKRKGSD------PDfseALIVRNNSTIEDVCDRIHRTLKDTYKYALvwgaSARhVPQRVGLSHVV 357
Cdd:PRK09602  313 vFDLLDMIVVYpveDENKLTDkkgnvlPD---AFLLPKGSTARDLAYKIHTDIGEGFLYAI----DAR-TKRRIGEDYEL 384

                         410
                  ....*....|
gi 1570043770 358 ADEDVVYIVS 367
Cdd:PRK09602  385 KDGDVIKIVS 394
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 68-172 6.60e-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: 60.16  E-value: 6.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  68 ALVGFPSVGKSTFLSK-VTKTRSEVASYAFTTLTAIPGVLEYGGAE--IQLLDLPGIIEGaaEGKGRGRQVISAAKTSDL 144
Cdd:cd00882     1 VVVGRGGVGKSSLLNAlLGGEVGEVSDVPGTTRDPDVYVKELDKGKvkLVLVDTPGLDEF--GGLGREELARLLLRGADL 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1570043770 145 ILMVLDATKR---AEQRTLLEAELEAVGIRL 172
Cdd:cd00882    79 ILLVVDSTDReseEDAKLLILRRLRKEGIPI 109
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 68-152 8.29e-11

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: 59.78  E-value: 8.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  68 ALVGFPSVGKSTFLSKVTKTRSEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGI--IEGAAEGKGRGRQVISAAKtSDLI 145
Cdd:cd01879     1 ALVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPGTysLTPYSEDEKVARDFLLGEE-PDLI 79


                  ....*..
gi 1570043770 146 LMVLDAT 152
Cdd:cd01879    80 VNVVDAT 86
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 66-152 2.29e-10

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


Pssm-ID: 460552 [Multi-domain]  Cd Length: 156  Bit Score: 58.62  E-value: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  66 RIALVGFPSVGKSTFLSKVTKTRSEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGI--IEGAAEGKGRGRQVISAAKtSD 143
Cdd:pfam02421   2 TIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFKYKGYEIEIVDLPGIysLSPYSEEERVARDYLLNEK-PD 80


                  ....*....
gi 1570043770 144 LILMVLDAT 152
Cdd:pfam02421  81 VIVNVVDAT 89
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
66-152 4.38e-08

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 54.74  E-value: 4.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  66 RIALVGFPSVGKSTFLSKVTKTRSEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGII--------EGAAegkgrgRQVIS 137
Cdd:COG0370     5 TIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKGKEIELVDLPGTYslsayspdEKVA------RDFLL 78

                          90
                  ....*....|....*
gi 1570043770 138 AAKTsDLILMVLDAT 152
Cdd:COG0370    79 EEKP-DVVVNVVDAT 92
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 61-154 9.85e-08

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: 51.31  E-value: 9.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  61 KSGdaRIALVGFPSVGKSTFLSKVTKTR-SEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGIIEgaaEGKGRG----RQV 135
Cdd:cd04163     2 KSG--FVAIIGRPNVGKSTLLNALVGQKiSIVSPKPQTTRNRIRGIYTDDDAQIIFVDTPGIHK---PKKKLGermvKAA 76

                          90
                  ....*....|....*....
gi 1570043770 136 ISAAKTSDLILMVLDATKR 154
Cdd:cd04163    77 WSALKDVDLVLFVVDASEW 95
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 68-158 1.56e-07

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: 50.03  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  68 ALVGFPSVGKSTFLSKVTKTR-SEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGIIEGAAEGKGRGRQVISAAKTSDLIL 146
Cdd:cd11383     1 GLMGKTGAGKSSLCNALFGTEvAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPGVGERGRRDREYEELYRRLLPEADLVL 80

                          90
                  ....*....|..
gi 1570043770 147 MVLDATKRAEQR 158
Cdd:cd11383    81 WLLDADDRALAA 92
TGS_Obg cd04938
TGS (ThrRS, GTPase and SpoT) domain found in the Obg protein family; The Obg family of GTPases ...
 293-366 2.08e-07

TGS (ThrRS, GTPase and SpoT) domain found in the Obg protein family; The Obg family of GTPases function has been implicated in cellular processes as diverse as sporulation, stress response, control of DNA replication, and ribosome assembly. It consists of several subfamilies such as DRG and YchF with TGS domain. The TGS domain is named after the various RNA-binding multidomain ThrRS, GTPase, and SpoT/RelA proteins in which this domain occurs. The TGS domain of Obg-like GTPases such as those present in DRG (developmentally regulated GTP-binding protein), and GTP-binding proteins Ygr210 and YchF has a beta-grasp ubiquitin-like fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340517 [Multi-domain]  Cd Length: 77  Bit Score: 47.83  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770 293 LIRIYTKRKG-------SDPDFSEALIVRNNSTIEDVCDRIHRTLKDTYKYALVWGAsarhvPQRVGLSHVVADEDVVYI 365
Cdd:cd04938     2 LIPVYPVKNIqtftngsGNSVFRDCVLVKKGTTVKDFANKIHTDLEKGFINAEGIGG-----RRLEGEDYILQDNDVVKF 76


                  .
gi 1570043770 366 V 366
Cdd:cd04938    77 T 77
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 68-152 3.93e-07

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


Pssm-ID: 206681 [Multi-domain]  Cd Length: 157  Bit Score: 49.36  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  68 ALVGFPSVGKSTFLSKVTKTRSE-VASYAFTTLTAIPGVLEYGGAEIQLLDLPGIIEGAAEGKGRGR-QVISAAKTSDLI 145
Cdd:cd01894     1 AIVGRPNVGKSTLFNRLTGRRDAiVSDTPGVTRDRKYGEAEWGGREFILIDTGGIEPDDEGISKEIReQAEIAIEEADVI 80


                  ....*..
gi 1570043770 146 LMVLDAT 152
Cdd:cd01894    81 LFVVDGR 87
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
61-154 5.29e-07

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 50.76  E-value: 5.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  61 KSGdaRIALVGFPSVGKSTFL-----SKVtktrSEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGIIEGAAE-GKGRGRQ 134
Cdd:COG1159     2 RSG--FVAIVGRPNVGKSTLLnalvgQKV----SIVSPKPQTTRHRIRGIVTREDAQIVFVDTPGIHKPKRKlGRRMNKA 75

                          90       100
                  ....*....|....*....|
gi 1570043770 135 VISAAKTSDLILMVLDATKR 154
Cdd:COG1159    76 AWSALEDVDVILFVVDATEK 95
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
67-152 1.39e-06

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 50.02  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  67 IALVGFPSVGKSTFLSKVTKTR-SEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGIIEGAAEG--KGRGRQVISAAKTSD 143
Cdd:COG1160     5 VAIVGRPNVGKSTLFNRLTGRRdAIVDDTPGVTRDRIYGEAEWGGREFTLIDTGGIEPDDDDGleAEIREQAELAIEEAD 84


                  ....*....
gi 1570043770 144 LILMVLDAT 152
Cdd:COG1160    85 VILFVVDGR 93
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 66-151 2.77e-06

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 48.89  E-value: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  66 RIALVGFPSVGKSTFLSKVTKTR-SEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGIIEGAA--EGKGRgRQVISAAKTS 142
Cdd:PRK00093    3 VVAIVGRPNVGKSTLFNRLTGKRdAIVADTPGVTRDRIYGEAEWLGREFILIDTGGIEPDDDgfEKQIR-EQAELAIEEA 81


                  ....*....
gi 1570043770 143 DLILMVLDA 151
Cdd:PRK00093   82 DVILFVVDG 90
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 66-152 2.84e-06

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: 47.04  E-value: 2.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  66 RIALVGFPSVGKSTFLSKVTK-TRSEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGI-----IEGAAE--GKGRGRQVIS 137
Cdd:cd01895     4 KIAIIGRPNVGKSSLLNALLGeERVIVSDIAGTTRDSIDVPFEYDGQKYTLIDTAGIrkkgkVTEGIEkySVLRTLKAIE 83

                          90
                  ....*....|....*
gi 1570043770 138 AAktsDLILMVLDAT 152
Cdd:cd01895    84 RA---DVVLLVLDAS 95
era PRK00089
GTPase Era; Reviewed
 67-153 4.16e-06

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 47.73  E-value: 4.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  67 IALVGFPSVGKSTFLSKVTKTR-SEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGIIEgaAEGK-GRG--RQVISAAKTS 142
Cdd:PRK00089    8 VAIVGRPNVGKSTLLNALVGQKiSIVSPKPQTTRHRIRGIVTEDDAQIIFVDTPGIHK--PKRAlNRAmnKAAWSSLKDV 85

                          90
                  ....*....|.
gi 1570043770 143 DLILMVLDATK 153
Cdd:PRK00089   86 DLVLFVVDADE 96
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 66-148 1.58e-05

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 46.48  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  66 RIALVGFPSVGKSTFLSKVTKTRSEVASYAFTTL---TAIPGV----LEY----------GGAEIQLLDLPGIIEGAAEG 128
Cdd:PTZ00258   23 KMGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIdpnTARVNVpderFDWlckhfkpksiVPAQLDITDIAGLVKGASEG 102

                          90       100
                  ....*....|....*....|
gi 1570043770 129 KGRGRQVISAAKTSDLILMV 148
Cdd:PTZ00258  103 EGLGNAFLSHIRAVDGIYHV 122
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 59-157 3.94e-05

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 45.56  E-value: 3.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  59 VSKSGDARIALVGFPSVGKSTFLSKVT-KTRSEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGIIEGAAEGKG------- 130
Cdd:PRK09518  445 LTPSGLRRVALVGRPNVGKSSLLNQLThEERAVVNDLAGTTRDPVDEIVEIDGEDWLFIDTAGIKRRQHKLTGaeyyssl 524

                          90       100
                  ....*....|....*....|....*...
gi 1570043770 131 RGRQVISAaktSDLILMVLDATKR-AEQ 157
Cdd:PRK09518  525 RTQAAIER---SELALFLFDASQPiSEQ 549
YeeP COG3596
Predicted GTPase [General function prediction only];
66-157 4.07e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 45.14  E-value: 4.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  66 RIALVGFPSVGKSTFLSKVTK-TRSEVASYAFTTLTAIPGVLEYGGAE-IQLLDLPGIIEGAAEGKgRGRQVISAAKTSD 143
Cdd:COG3596    41 VIALVGKTGAGKSSLINALFGaEVAEVGVGRPCTREIQRYRLESDGLPgLVLLDTPGLGEVNERDR-EYRELRELLPEAD 119

                          90
                  ....*....|....
gi 1570043770 144 LILMVLDATKRAEQ 157
Cdd:COG3596   120 LILWVVKADDRALA 133
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 58-121 9.28e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 44.19  E-value: 9.28e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  58 DVSKSGDA-----RIALVGFPSVGKSTFLSKVT-KTRSEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGI 121
Cdd:PRK03003  200 EVPRVGSAsggprRVALVGKPNVGKSSLLNKLAgEERSVVDDVAGTTVDPVDSLIELGGKTWRFVDTAGL 269
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
66-152 1.14e-04

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 43.86  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  66 RIALVGFPSVGKSTFLSKVTKT-RSEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGI-----IEGAAEgK---GRGRQVI 136
Cdd:COG1160   177 KIAIVGRPNVGKSSLINALLGEeRVIVSDIAGTTRDSIDTPFERDGKKYTLIDTAGIrrkgkVDEGIE-KysvLRTLRAI 255

                          90
                  ....*....|....*.
gi 1570043770 137 SAAktsDLILMVLDAT 152
Cdd:COG1160   256 ERA---DVVLLVIDAT 268
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 66-153 1.41e-04

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


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 41.71  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  66 RIALVGFPSVGKSTFLSKVTKT-RSEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGI------IEgaAEGKGRGRQvisA 138
Cdd:cd04164     5 KVVIAGKPNVGKSSLLNALAGRdRAIVSDIAGTTRDVIEEEIDLGGIPVRLIDTAGLretedeIE--KIGIERARE---A 79

                          90
                  ....*....|....*
gi 1570043770 139 AKTSDLILMVLDATK 153
Cdd:cd04164    80 IEEADLVLLVVDASE 94
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 66-152 1.66e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 43.50  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  66 RIALVGFPSVGKSTFLSKVTKT-RSEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGI-----IEGAAE--GKGRGRQVIS 137
Cdd:PRK00093  175 KIAIIGRPNVGKSSLINALLGEeRVIVSDIAGTTRDSIDTPFERDGQKYTLIDTAGIrrkgkVTEGVEkySVIRTLKAIE 254

                          90
                  ....*....|....*
gi 1570043770 138 AAktsDLILMVLDAT 152
Cdd:PRK00093  255 RA---DVVLLVIDAT 266
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
66-153 1.14e-03

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 40.86  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  66 RIALVGFPSVGKST---FLSKvtKTRSEVASYAFTTLTAIPGVLEYGGAEIQLLDLPGI------IEgaAEGKGRGRQvi 136
Cdd:PRK05291  217 KVVIAGRPNVGKSSllnALLG--EERAIVTDIAGTTRDVIEEHINLDGIPLRLIDTAGIretddeVE--KIGIERSRE-- 290

                          90
                  ....*....|....*..
gi 1570043770 137 sAAKTSDLILMVLDATK 153
Cdd:PRK05291  291 -AIEEADLVLLVLDASE 306
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 66-153 4.03e-03

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


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 38.89  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  66 RIALVGFPSVGKSTFLSKVtkTRSEVAsyaftTLTAIPG----VLE----YGGAEIQLLDLPGI------IEgaAEGKGR 131
Cdd:COG0486   215 KVVIVGRPNVGKSSLLNAL--LGEERA-----IVTDIAGttrdVIEerinIGGIPVRLIDTAGLretedeVE--KIGIER 285

                          90       100
                  ....*....|....*....|..
gi 1570043770 132 GRQvisAAKTSDLILMVLDATK 153
Cdd:COG0486   286 ARE---AIEEADLVLLLLDASE 304
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
63-177 5.66e-03

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 37.27  E-value: 5.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570043770  63 GDARIALVGFPSVGKSTFLSK----------------VTKTRSEVAsyafttltaipgvLEYGGAEIQLLDLPGIIEGAA 126
Cdd:COG1100     2 GEKKIVVVGTGGVGKTSLVNRlvgdifslekylstngVTIDKKELK-------------LDGLDVDLVIWDTPGQDEFRE 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1570043770 127 EGKGRGRQVISAaktsDLILMVLDATKRAEQRTLLEAeLEAVgIRLNREPP 177
Cdd:COG1100    69 TRQFYARQLTGA----SLYLFVVDGTREETLQSLYEL-LESL-RRLGKKSP 113
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 66-121 8.65e-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: 36.74  E-value: 8.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1570043770  66 RIALVGFPSVGKSTFLSKVTKTRSEVASyafttltAIPGV------LEYGGaEIQLLDLPGI 121
Cdd:cd01856   117 RAMVVGIPNVGKSTLINRLRGKKVAKVG-------NKPGVtrgqqwIRIGP-NIELLDTPGI 170
 
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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