NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|119187731|ref|XP_001244472|]
View 

ribosome-interacting GTPase 1 [Coccidioides immitis RS]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
1-367 2.04e-157

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


:

Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 446.55  E-value: 2.04e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731   1 MATTVDKIKEIEAEMARTQKNKATSFHLGQLKAKLAKLKRELLTPSGGGGGGGAGFDVARTGVASVGFIGFPSVGKSTLM 80
Cdd:COG1163    1 AMTIEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  81 SKLTGQHSEAAAYEFTTLTTVPGQVLYNGAKIQILDLPGIIQGAKDGKGRGRQVIAVAKTCHLIFIVLDVNKPLTDKRII 160
Cdd:COG1163   81 NKLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELEQYDVLK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 161 EaELEGFGIRINKSPPNIVFKKKDKGGISITSTVPLThIDHDEIKAVMSEYRISSADIAIRCDATIDDLIDVLeAKSRSY 240
Cdd:COG1163  161 E-ELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLD-LDEEDIKKILREYGIVNADVLIREDVTLDDLIDAL-MGNRVY 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 241 IPVIYALNKIDSISIEEL-DLLYRIPN---ACPISAEHGWNVDELLEQMWEKLNLKRIYTKPKGKAPDYTAPVVLKSNNc 316
Cdd:COG1163  238 KPAIVVVNKIDLADEEYVeELKSKLPDgvpVIFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKGS- 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119187731 317 TVEDFCNAIHKSIVEQFKHAIVYGRSVKHQPQRVGLSHQLEDEDIITIIKR 367
Cdd:COG1163  317 TVGDVCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIK 367
 
Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
1-367 2.04e-157

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 446.55  E-value: 2.04e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731   1 MATTVDKIKEIEAEMARTQKNKATSFHLGQLKAKLAKLKRELLTPSGGGGGGGAGFDVARTGVASVGFIGFPSVGKSTLM 80
Cdd:COG1163    1 AMTIEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  81 SKLTGQHSEAAAYEFTTLTTVPGQVLYNGAKIQILDLPGIIQGAKDGKGRGRQVIAVAKTCHLIFIVLDVNKPLTDKRII 160
Cdd:COG1163   81 NKLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELEQYDVLK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 161 EaELEGFGIRINKSPPNIVFKKKDKGGISITSTVPLThIDHDEIKAVMSEYRISSADIAIRCDATIDDLIDVLeAKSRSY 240
Cdd:COG1163  161 E-ELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLD-LDEEDIKKILREYGIVNADVLIREDVTLDDLIDAL-MGNRVY 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 241 IPVIYALNKIDSISIEEL-DLLYRIPN---ACPISAEHGWNVDELLEQMWEKLNLKRIYTKPKGKAPDYTAPVVLKSNNc 316
Cdd:COG1163  238 KPAIVVVNKIDLADEEYVeELKSKLPDgvpVIFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKGS- 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119187731 317 TVEDFCNAIHKSIVEQFKHAIVYGRSVKHQPQRVGLSHQLEDEDIITIIKR 367
Cdd:COG1163  317 TVGDVCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIK 367
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 64-297 2.03e-144

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: 408.09  E-value: 2.03e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  64 ASVGFIGFPSVGKSTLMSKLTGQHSEAAAYEFTTLTTVPGQVLYNGAKIQILDLPGIIQGAKDGKGRGRQVIAVAKTCHL 143
Cdd:cd01896    1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 144 IFIVLDVNKPLTDKRIIEAELEGFGIRINKSPPNIVFKKKDKGGISITSTVPLTHIDHDEIKAVMSEYRISSADIAIRCD 223
Cdd:cd01896   81 ILIVLDATKPEGQREILERELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLTKLDEKTVKAILREYKIHNADVLIRED 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119187731 224 ATIDDLIDVLEaKSRSYIPVIYALNKIDSISIEELDLLYRIPNACPISAEHGWNVDELLEQMWEKLNLKRIYTK 297
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 ...
 186-291 1.67e-57

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: 182.24  E-value: 1.67e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  186 GGISITSTVPLTHIDHDEIKAVMSEYRISSADIAIRCDATIDDLIDVLEaKSRSYIPVIYALNKIDSISIEELDLLYRIP 265
Cdd:pfam16897   1 GGINITSTVPLTKLDEETIKAILREYKIHNADVLIREDVTVDDLIDVIE-GNRVYIPCLYVYNKIDLISIEELDRLAREP 79

                          90       100
                  ....*....|....*....|....*.
gi 119187731  266 NACPISAEHGWNVDELLEQMWEKLNL 291
Cdd:pfam16897  80 DSVPISAEKGLNLDELKERIWEYLGL 105
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 66-200 3.49e-22

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 91.66  E-value: 3.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731   66 VGFIGFPSVGKSTLMSKLTGQH-SEAAAYEFTTLTTVPGQVLYNG--AKIQILDLPGIIQGAKDGKGRGRQVIAVAKTCH 142
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKgSITEYYPGTTRNYVTTVIEEDGktYKFNLLDTAGQEDYDAIRRLYYPQVERSLRVFD 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119187731  143 LIFIVLDVNKPLT-DKRIIEAELE-GFGIRINKSPPNIV---FKKKDKGGISITSTVPLTHID 200
Cdd:TIGR00231  84 IVILVLDVEEILEkQTKEIIHHADsGVPIILVGNKIDLKdadLKTHVASEFAKLNGEPIIPLS 146
obgE PRK12297
GTPase CgtA; Reviewed
 64-184 1.85e-18

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 85.92  E-value: 1.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  64 ASVGFIGFPSVGKSTLMSKLTGQHSEAAAYEFTTLTTVPGQVLYNGAK-IQILDLPGIIQGAKDGKGRG----RQViava 138
Cdd:PRK12297 159 ADVGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRsFVMADIPGLIEGASEGVGLGhqflRHI---- 234

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119187731 139 KTCHLIFIVLDVNK-----PLTDKRIIEAELEGFGIRINKSPPNIVFKKKD 184
Cdd:PRK12297 235 ERTRVIVHVIDMSGsegrdPIEDYEKINKELKLYNPRLLERPQIVVANKMD 285
 
Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
1-367 2.04e-157

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 446.55  E-value: 2.04e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731   1 MATTVDKIKEIEAEMARTQKNKATSFHLGQLKAKLAKLKRELLTPSGGGGGGGAGFDVARTGVASVGFIGFPSVGKSTLM 80
Cdd:COG1163    1 AMTIEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  81 SKLTGQHSEAAAYEFTTLTTVPGQVLYNGAKIQILDLPGIIQGAKDGKGRGRQVIAVAKTCHLIFIVLDVNKPLTDKRII 160
Cdd:COG1163   81 NKLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELEQYDVLK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 161 EaELEGFGIRINKSPPNIVFKKKDKGGISITSTVPLThIDHDEIKAVMSEYRISSADIAIRCDATIDDLIDVLeAKSRSY 240
Cdd:COG1163  161 E-ELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLD-LDEEDIKKILREYGIVNADVLIREDVTLDDLIDAL-MGNRVY 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 241 IPVIYALNKIDSISIEEL-DLLYRIPN---ACPISAEHGWNVDELLEQMWEKLNLKRIYTKPKGKAPDYTAPVVLKSNNc 316
Cdd:COG1163  238 KPAIVVVNKIDLADEEYVeELKSKLPDgvpVIFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKGS- 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119187731 317 TVEDFCNAIHKSIVEQFKHAIVYGRSVKHQPQRVGLSHQLEDEDIITIIKR 367
Cdd:COG1163  317 TVGDVCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIK 367
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 64-297 2.03e-144

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: 408.09  E-value: 2.03e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  64 ASVGFIGFPSVGKSTLMSKLTGQHSEAAAYEFTTLTTVPGQVLYNGAKIQILDLPGIIQGAKDGKGRGRQVIAVAKTCHL 143
Cdd:cd01896    1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 144 IFIVLDVNKPLTDKRIIEAELEGFGIRINKSPPNIVFKKKDKGGISITSTVPLTHIDHDEIKAVMSEYRISSADIAIRCD 223
Cdd:cd01896   81 ILIVLDATKPEGQREILERELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLTKLDEKTVKAILREYKIHNADVLIRED 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119187731 224 ATIDDLIDVLEaKSRSYIPVIYALNKIDSISIEELDLLYRIPNACPISAEHGWNVDELLEQMWEKLNLKRIYTK 297
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 ...
 186-291 1.67e-57

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: 182.24  E-value: 1.67e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  186 GGISITSTVPLTHIDHDEIKAVMSEYRISSADIAIRCDATIDDLIDVLEaKSRSYIPVIYALNKIDSISIEELDLLYRIP 265
Cdd:pfam16897   1 GGINITSTVPLTKLDEETIKAILREYKIHNADVLIREDVTVDDLIDVIE-GNRVYIPCLYVYNKIDLISIEELDRLAREP 79

                          90       100
                  ....*....|....*....|....*.
gi 119187731  266 NACPISAEHGWNVDELLEQMWEKLNL 291
Cdd:pfam16897  80 DSVPISAEKGLNLDELKERIWEYLGL 105
TGS_DRG1 cd17230
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 1 ...
 289-367 6.02e-47

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: 154.35  E-value: 6.02e-47
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119187731 289 LNLKRIYTKPKGKAPDYTAPVVLKSNNCTVEDFCNAIHKSIVEQFKHAIVYGRSVKHQPQRVGLSHQLEDEDIITIIKR 367
Cdd:cd17230    2 LNLVRIYTKPKGQLPDYEEPVVLRSGKSTVEDFCNKIHKSLIKEFKYALVWGSSVKHNPQRVGKDHVLEDEDVVQIVKK 80
TGS_DRG cd01666
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein ...
 289-366 1.05e-34

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: 122.34  E-value: 1.05e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119187731 289 LNLKRIYTKPKGKAPDYTAPVVLKSNnCTVEDFCNAIHKSIVEQFKHAIVYGRSVKHQPQRVGLSHQLEDEDIITIIK 366
Cdd:cd01666    1 LGIIRVYTKPPGKKPDFDEPFILRRG-STVEDVAEKIHKDLAENFKYARVWGKSVKFDGQRVGLDHVLEDGDIVEIHK 77
TGS_DRG2 cd17231
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 2 ...
 289-367 1.49e-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: 114.02  E-value: 1.49e-31
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119187731 289 LNLKRIYTKPKGKAPDYTAPVVLKsNNCTVEDFCNAIHKSIVEQFKHAIVYGRSVKHQPQRVGLSHQLEDEDIITIIKR 367
Cdd:cd17231    2 LALIRVYTKKRGERPDFGDAIILR-RGATVEHVCHRIHRTLASQFKYALVWGTSTKYSPQRVGLTHVMEDEDVIQIVKK 79
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 66-182 3.96e-28

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


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 106.16  E-value: 3.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731   66 VGFIGFPSVGKSTLMSKLTGQHSEAAAYEFTTLTTVPGQVLYNGAKIQILDLPGIIQGAKDGKGRGRQVIAVAKtCHLIF 145
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFLAIIE-ADLIL 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 119187731  146 IVLDVNKPLTDkriIEAELEGFGIRINKsPPNIVFKK 182
Cdd:pfam01926  81 FVVDSEEGITP---LDEELLELLRENKK-PIILVLNK 113
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 67-289 2.03e-27

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: 105.94  E-value: 2.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  67 GFIGFPSVGKSTLMSKLTGQHSEAAAYEFTTLTTVPGQVLY-NGAKIQILDLPGIIQGAKDGKGRGRQVIAVAKTCHLIF 145
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFgDGVDIQIIDLPGLLDGASEGRGLGEQILAHLYRSDLIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 146 IVLDVNKpltdkriieaelegfgirinksppnivfkkkdkggisitstvpLTHIDH-DEIKAVmsEYRISSADIaircda 224
Cdd:cd01881   81 HVIDASE-------------------------------------------DCVGDPlEDQKTL--NEEVSGSFL------ 109

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 225 tiddlidvleakSRSYIPVIYALNKIDSISIEELDLLYRI-----PNACPISAEHGWNVDELLEQMWEKL 289
Cdd:cd01881  110 ------------FLKNKPEMIVANKIDMASENNLKRLKLDklkrgIPVVPTSALTRLGLDRVIRTIRKLL 167
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 66-200 3.49e-22

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 91.66  E-value: 3.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731   66 VGFIGFPSVGKSTLMSKLTGQH-SEAAAYEFTTLTTVPGQVLYNG--AKIQILDLPGIIQGAKDGKGRGRQVIAVAKTCH 142
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKgSITEYYPGTTRNYVTTVIEEDGktYKFNLLDTAGQEDYDAIRRLYYPQVERSLRVFD 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119187731  143 LIFIVLDVNKPLT-DKRIIEAELE-GFGIRINKSPPNIV---FKKKDKGGISITSTVPLTHID 200
Cdd:TIGR00231  84 IVILVLDVEEILEkQTKEIIHHADsGVPIILVGNKIDLKdadLKTHVASEFAKLNGEPIIPLS 146
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 64-289 5.71e-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: 91.33  E-value: 5.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  64 ASVGFIGFPSVGKSTLMSKLTGQHSEAAAYEFTTLTTVPGQV-LYNGAKIQILDLPGIIQGAKDGKGRG----RQViava 138
Cdd:cd01898    1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVrVDDGRSFVIADIPGLIEGASEGKGLGhrflRHI---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 139 KTCHLIFIVLDVNK---PLTDKRIIEAELEGFGIRinksppnivfkkkdkggisitstvplthidhdeikavmseyriss 215
Cdd:cd01898   77 ERTRVLLHVIDLSGeddPVEDYETIRNELEAYNPG--------------------------------------------- 111

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 216 adiaircdatiddlidvLEAKsrsyiPVIYALNKIDSISIEE-LDLLYRIPNAC------PISAEHGWNVDELLEQMWEK 288
Cdd:cd01898  112 -----------------LAEK-----PRIVVLNKIDLLDAEErFEKLKELLKELkgkkvfPISALTGEGLDELLKKLAKL 169


                 .
gi 119187731 289 L 289
Cdd:cd01898  170 L 170
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
 63-289 1.33e-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: 94.03  E-value: 1.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731   63 VASVGFIGFPSVGKSTLMSKLTGQHSEAAAYEFTTLTTVPGQVLYNGAK-IQILDLPGIIQGAKDGKGRGRQVIA-VAKT 140
Cdd:TIGR02729 157 LADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRsFVIADIPGLIEGASEGAGLGHRFLKhIERT 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  141 CHLIFIV----LDVNKPLTDKRIIEAELEGFGirinksppnivfkkkdkggisitstvplthidhdeikavmseyrissa 216
Cdd:TIGR02729 237 RVLLHLIdispEDGSDPVEDYEIIRNELKKYS------------------------------------------------ 268

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119187731  217 diaircdatiddliDVLEAKsrsyiPVIYALNKIDSISIEELD-LLYRIPNAC-----PISAEHGWNVDELLEQMWEKL 289
Cdd:TIGR02729 269 --------------PELAEK-----PRIVVLNKIDLLDEEELEeLLKELKKELgkpvfPISALTGEGLDELLDALAELL 328
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
 63-290 1.36e-18

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


Pssm-ID: 440302 [Multi-domain]  Cd Length: 343  Bit Score: 85.42  E-value: 1.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  63 VASVGFIGFPSVGKSTLMSKLTGQHSEAAAYEFTTLTTVPGQVLYNGAK-IQILDLPGIIQGAKDGKGRG----RQviaV 137
Cdd:COG0536  157 LADVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGRsFVIADIPGLIEGASEGAGLGhrflRH---I 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 138 AKTCHLIFIV----LDVNKPLTDKRIIEAELEGFGirinksppnivfkkkdkggisitstvplthidhdeikavmseyri 213
Cdd:COG0536  234 ERTRVLLHVVdaapLDGRDPVEDYEIIRNELEAYS--------------------------------------------- 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 214 ssadiaircdatiddliDVLEAKSRsyipvIYALNKIDSISIEELDLLYRIPNAC-----PISAEHGWNVDELLEQMWEK 288
Cdd:COG0536  269 -----------------PELAEKPR-----IVVLNKIDLLDAEELEELKAELEKLggpvfPISAVTGEGLDELLYALAEL 326


                 ..
gi 119187731 289 LN 290
Cdd:COG0536  327 LE 328
obgE PRK12297
GTPase CgtA; Reviewed
 64-184 1.85e-18

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 85.92  E-value: 1.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  64 ASVGFIGFPSVGKSTLMSKLTGQHSEAAAYEFTTLTTVPGQVLYNGAK-IQILDLPGIIQGAKDGKGRG----RQViava 138
Cdd:PRK12297 159 ADVGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRsFVMADIPGLIEGASEGVGLGhqflRHI---- 234

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119187731 139 KTCHLIFIVLDVNK-----PLTDKRIIEAELEGFGIRINKSPPNIVFKKKD 184
Cdd:PRK12297 235 ERTRVIVHVIDMSGsegrdPIEDYEKINKELKLYNPRLLERPQIVVANKMD 285
obgE PRK12299
GTPase CgtA; Reviewed
 64-293 2.48e-18

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 84.74  E-value: 2.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  64 ASVGFIGFPSVGKSTLMSKLTGQHSEAAAYEFTTLTTVPGQVLYNGAK-IQILDLPGIIQGAKDGKGRGRQVIA-VAKTC 141
Cdd:PRK12299 159 ADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKsFVIADIPGLIEGASEGAGLGHRFLKhIERTR 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 142 HLIFIV-LDVNKPLTDKRIIEAELEGFGirinksppnivfkkkdkggisitstvplthidhdeikavmseyrissadiai 220
Cdd:PRK12299 239 LLLHLVdIEAVDPVEDYKTIRNELEKYS---------------------------------------------------- 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 221 rcdatiDDLIDvleaKSRsyipvIYALNKIDSISiEELDLLYRIPNAC--------PISAEHGWNVDELLEQMWEKLNLK 292
Cdd:PRK12299 267 ------PELAD----KPR-----ILVLNKIDLLD-EEEEREKRAALELaalggpvfLISAVTGEGLDELLRALWELLEEA 330


                 .
gi 119187731 293 R 293
Cdd:PRK12299 331 R 331
TGS pfam02824
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ...
 293-366 1.02e-17

TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain was detected also at the amino terminus of the uridine kinase from the spirochaete Treponema pallidum (but not any other organizm, including the related spirochaete Borrelia burgdorferi). TGS is a small domain that consists of ~50 amino acid residues and is predicted to possess a predominantly beta-sheet structure. There is no direct information on the functions of the TGS domain, but its presence in two types of regulatory proteins (the GTPases and guanosine polyphosphate phosphohydrolases/synthetases) suggests a ligand (most likely nucleotide)-binding, regulatory role.


Pssm-ID: 427005 [Multi-domain]  Cd Length: 60  Bit Score: 76.43  E-value: 1.02e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119187731  293 RIYTkPKGKAPDYTAPVvlksnncTVEDFCNAIHKSIVEQFKHAIVYGrsvkhqpQRVGLSHQLEDEDIITIIK 366
Cdd:pfam02824   2 RVYT-PDGKVPDLPRGA-------TPEDFAYAIHTSLAKKFIYAKVNG-------QLVGLDHPLEDGDVVEIVT 60
obgE PRK12296
GTPase CgtA; Reviewed
 63-168 2.66e-14

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 73.75  E-value: 2.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  63 VASVGFIGFPSVGKSTLMSKLTGQHSEAAAYEFTTLttVP--GQVLYNGAKIQILDLPGIIQGAKDGKGRGRQVIAVAKT 140
Cdd:PRK12296 159 VADVGLVGFPSAGKSSLISALSAAKPKIADYPFTTL--VPnlGVVQAGDTRFTVADVPGLIPGASEGKGLGLDFLRHIER 236

                         90       100       110
                 ....*....|....*....|....*....|....
gi 119187731 141 CHLIFIVLDV------NKPLTDKRIIEAELEGFG 168
Cdd:PRK12296 237 CAVLVHVVDCatlepgRDPLSDIDALEAELAAYA 270
obgE PRK12298
GTPase CgtA; Reviewed
 63-294 4.06e-14

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 72.98  E-value: 4.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  63 VASVGFIGFPSVGKSTLMSKLTGQHSEAAAYEFTTLttVP--GQVLY-NGAKIQILDLPGIIQGAKDGKGRG-RQVIAVA 138
Cdd:PRK12298 159 LADVGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTL--VPnlGVVRVdDERSFVVADIPGLIEGASEGAGLGiRFLKHLE 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 139 KTCHLIFIV----LDVNKPLTDKRIIEAELEGFGIRINKSPPNIVFKKKDKggisitstvplthIDHDEIKAVmseyris 214
Cdd:PRK12298 237 RCRVLLHLIdiapIDGSDPVENARIIINELEKYSPKLAEKPRWLVFNKIDL-------------LDEEEAEER------- 296

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 215 sadiaircdatIDDLIDVLEAKSRSYipVIYALNK--IDSISIEELDLLYRIPNACPISAEHgwnvDELLEQMWEKLNLK 292
Cdd:PRK12298 297 -----------AKAIVEALGWEGPVY--LISAASGlgVKELCWDLMTFIEENPREEAEEAEA----PEKVEFMWDDYHRE 359


                 ..
gi 119187731 293 RI 294
Cdd:PRK12298 360 QL 361
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 67-289 6.03e-13

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


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 66.12  E-value: 6.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  67 GFIGFPSVGKSTLMSKLTGQH-SEAAAYEFTTLTTVPGQV-LYNGAKIQILDLPGIIQGAKDGKGRGRQVIAVAKTCHLI 144
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNvGIVSPIPGTTRDPVRKEWeLLPLGPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 145 FIVLDvnkpltdkriieaelegfgirinksppnivfkkkdkggisitstvplthidhdeikavmseyrissadiairCDA 224
Cdd:cd00880   81 LLVVD------------------------------------------------------------------------SDL 88

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119187731 225 TIDDLIDVLEAKSRSYIPVIYALNKIDSISIEELDLLYRIP--------NACPISAEHGWNVDELLEQMWEKL 289
Cdd:cd00880   89 TPVEEEAKLGLLRERGKPVLLVLNKIDLVPESEEEELLRERklellpdlPVIAVSALPGEGIDELRKKIAELL 161
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 70-289 6.14e-12

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: 63.35  E-value: 6.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  70 GFPSVGKSTLMSKLTGQHSEAAAYEFTTLTTVPGQVLYNGAKIQILDLPGIiqgakdgkgrgrqviavaktchlifivLD 149
Cdd:cd01897    7 GYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLRWQVIDTPGI---------------------------LD 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 150 vnKPLTDKRIIEaelegfgirinksppnivfkkkdkggisITSTVPLTHIdHDEIKAVMseyrissaDIAIRCDATIDDL 229
Cdd:cd01897   60 --RPLEERNTIE----------------------------MQAITALAHL-RAAVLFFI--------DPSETCGYSIEEQ 100

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119187731 230 IDVL-EAKSRSYIPVIYALNKIDSISIEELDLLYRIPNACP-----ISAEHGWNVDELLEQMWEKL 289
Cdd:cd01897  101 LSLFkEIKPLFNKPVIVVLNKIDLLTEEDLSEIEKELEKEGeevikISTLTEEGVDELKNKACELL 166
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 67-285 1.84e-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: 61.70  E-value: 1.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  67 GFIGFPSVGKSTLMSKLTGQH-SEAAAYEFTTL--TTVPGQVLYNGAKIQILDLPGIIQGakDGKGRGRQVIAVAKTCHL 143
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEvGEVSDVPGTTRdpDVYVKELDKGKVKLVLVDTPGLDEF--GGLGREELARLLLRGADL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 144 IFIVLDVNKPLTDKRI---IEAELEGFGIRInksppnIVFkkkdkggisitstvpLTHIDHDEikavmseyrissadiai 220
Cdd:cd00882   79 ILLVVDSTDRESEEDAkllILRRLRKEGIPI------ILV---------------GNKIDLLE----------------- 120

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119187731 221 rcDATIDDLIDVLEAKSRSYIPVIyalnkidsisieeldllyripnacPISAEHGWNVDELLEQM 285
Cdd:cd00882  121 --EREVEELLRLEELAKILGVPVF------------------------EVSAKTGEGVDELFEKL 159
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
70-289 2.09e-11

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 64.08  E-value: 2.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  70 GFPSVGKSTLMSKLTGQHSEAAAYEFTTLTTVPGQVLYNGAKIQILDLPGIiqgakdgkgrgrqviavaktchlifivLD 149
Cdd:COG1084  167 GYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGRYQVIDTPGL---------------------------LD 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 150 vnKPLTDKRIIEaelegfgirinksppnivfKKkdkggisitSTVPLTHIDhDEIKAVMseyrissaDIAIRCDATIDDL 229
Cdd:COG1084  220 --RPLSERNEIE-------------------RQ---------AILALKHLA-DVILFLF--------DPSETCGYSLEEQ 260

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119187731 230 IDVLEA-KSRSYIPVIYALNKIDSISIEELDLLYRIPNACpISAEHGWNVDELLEQMWEKL 289
Cdd:COG1084  261 LNLLEEiRSLFDVPVIVVINKIDLSDEEELKEAEEEADIK-ISALTGEGVDELLDELIEAL 320
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 184-289 1.31e-09

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: 56.29  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 184 DKGGISITSTVPLTHIdhdeikAVMSEYRISSADIAI-----RCDATIDD--LIDVLEaksRSYIPVIYALNKIDSISIE 256
Cdd:cd01894   51 DTGGIEPDDEGISKEI------REQAEIAIEEADVILfvvdgREGLTPADeeIAKYLR---KSKKPVILVVNKIDNIKEE 121

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 119187731 257 -ELDLLYR--IPNACPISAEHGWNVDELLEQMWEKL 289
Cdd:cd01894  122 eEAAEFYSlgFGEPIPISAEHGRGIGDLLDAILELL 157
TGS_Obg cd04938
TGS (ThrRS, GTPase and SpoT) domain found in the Obg protein family; The Obg family of GTPases ...
 290-364 2.61e-09

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


Pssm-ID: 340517 [Multi-domain]  Cd Length: 77  Bit Score: 53.22  E-value: 2.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 290 NLKRIYTKPKGK-------APDYTAPVVLKsNNCTVEDFCNAIHKSIVEQFKHAIVYGrsvkhQPQRVGLSHQLEDEDII 362
Cdd:cd04938    1 GLIPVYPVKNIQtftngsgNSVFRDCVLVK-KGTTVKDFANKIHTDLEKGFINAEGIG-----GRRLEGEDYILQDNDVV 74


                 ..
gi 119187731 363 TI 364
Cdd:cd04938   75 KF 76
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 59-289 1.24e-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: 54.39  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  59 ARTGVASVGFIGFPSVGKSTLMSKLTGQHSEAAAYEFTTLTTvpgqvlyngaKIQILDLPGiiqgakdgkgrGRQVIava 138
Cdd:cd01878   37 KRSGVPTVALVGYTNAGKSTLFNALTGADVLAEDQLFATLDP----------TTRRIKLPG-----------GREVL--- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 139 ktchlifivldvnkpLTDKriieaelEGFgirINKSPPNIV--FKkkdkggisitSTVP-------LTH-IDhdeikavm 208
Cdd:cd01878   93 ---------------LTDT-------VGF---IRDLPHQLVeaFR----------STLEevaeadlLLHvVD-------- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 209 seyrISSADIAIRCDATIDDL--IDVLEaksrsyIPVIYALNKIDSISIEELD--LLYRIPNACPISAEHGWNVDELLEQ 284
Cdd:cd01878  130 ----ASDPDREEQIETVEEVLkeLGADD------IPIILVLNKIDLLDDEELEerLRAGRPDAVFISAKTGEGLDLLKEA 199


                 ....*
gi 119187731 285 MWEKL 289
Cdd:cd01878  200 IEELL 204
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
 66-273 4.49e-08

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: 54.16  E-value: 4.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  66 VGFIGFPSVGKSTLMSKLTGQHSEAAAYEFTTL----------TTVPGQVL--------------YNGAKIQILDLPGII 121
Cdd:cd01899    1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIdpnvgvgyvrVECPCKELgvscnprygkcidgKRYVPVELIDVAGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 122 QGAKDGKGRGRQ--------------VIAVAKT-CHLIFIVLDVNKPLTDKRIIEAELEG--FGIrINKSPPNIVfKKKD 184
Cdd:cd01899   81 PGAHEGKGLGNQflddlrdadvlihvVDASGGTdAEGNGVETGGYDPLEDIEFLENEIDMwiYGI-LERNWEKIV-RKAK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 185 KGGISITSTV--PLTHIdhdeikaVMSEYRISSADIAIRCDA-----TIDDLIDVLEAKSRSYIPVIYALNKIDSIS--- 254
Cdd:cd01899  159 AEKTDIVEALseQLSGF-------GVNEDVVIEALEELELPAdlskwDDEDLLRLARELRKRRKPMVIAANKADIPDaee 231

                        250       260
                 ....*....|....*....|
gi 119187731 255 -IEELDLLYRIPNACPISAE 273
Cdd:cd01899  232 nISKLRLKYPDEIVVPTSAE 251
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 65-164 5.67e-07

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 51.10  E-value: 5.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  65 SVGFIGFPSVGKSTLMSKLTGQHSEAAAYEFTTL------TTVPGQVL-----YNGAK------IQILDLPGIIQGAKDG 127
Cdd:PTZ00258  23 KMGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIdpntarVNVPDERFdwlckHFKPKsivpaqLDITDIAGLVKGASEG 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 119187731 128 KGRGRQVIAVAKTCHLIFIVL-------------DVNkPLTDKRIIEAEL 164
Cdd:PTZ00258 103 EGLGNAFLSHIRAVDGIYHVVrafededithvegEID-PVRDLEIISSEL 151
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 68-120 3.75e-06

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


Pssm-ID: 206667 [Multi-domain]  Cd Length: 159  Bit Score: 46.30  E-value: 3.75e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119187731  68 FIGFPSVGKSTLMSKLTGQHSEAAAYEFTTLTTVPGQVLYNGAKIQILDLPGI 120
Cdd:cd01879    2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPGT 54
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
184-289 4.71e-06

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 48.10  E-value: 4.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 184 DKGGISITSTvplthidhDEIKAVM---SEYRISSADIAI-----RCDATIDD--LIDVLeakSRSYIPVIYALNKIDSI 253
Cdd:COG1160   56 DTGGIEPDDD--------DGLEAEIreqAELAIEEADVILfvvdgRAGLTPLDeeIAKLL---RRSGKPVILVVNKVDGP 124

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 119187731 254 SIEELDL-LYR--IPNACPISAEHGWNVDELLEQMWEKL 289
Cdd:COG1160  125 KREADAAeFYSlgLGEPIPISAEHGRGVGDLLDAVLELL 163
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 66-120 8.64e-06

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: 45.13  E-value: 8.64e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119187731   66 VGFIGFPSVGKSTLMSKLTGQHSEAAAYEFTTLTTVPGQVLYNGAKIQILDLPGI 120
Cdd:pfam02421   3 IALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFKYKGYEIEIVDLPGI 57
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
 70-120 2.72e-05

ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane protein required for iron(II) update, is encoded in an operon with FeoA (75 amino acids), which is also required, and is regulated by Fur. There appear to be two copies in Archaeoglobus fulgidus and Clostridium acetobutylicum. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273077 [Multi-domain]  Cd Length: 591  Bit Score: 45.89  E-value: 2.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 119187731   70 GFPSVGKSTLMSKLTGQHSEAAAYEFTTLTTVPGQVLYNGAKIQILDLPGI 120
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGFQGEDIEIVDLPGI 51
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 242-289 4.54e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 45.04  E-value: 4.54e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119187731 242 PVIYALNKIDSISIEELDL-LYR--IPNACPISAEHGWNVDELLEQMWEKL 289
Cdd:PRK00093 111 PVILVVNKVDGPDEEADAYeFYSlgLGEPYPISAEHGRGIGDLLDAILEEL 161
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 66-173 5.34e-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: 43.19  E-value: 5.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  66 VGFIGFPSVGKSTLMSKLTGQH----SEAAAyefTTLTTVPGQVLYNGAKIQILDLPGIIQGAKDGKG-------RGRQV 134
Cdd:cd01895    5 IAIIGRPNVGKSSLLNALLGEErvivSDIAG---TTRDSIDVPFEYDGQKYTLIDTAGIRKKGKVTEGiekysvlRTLKA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 119187731 135 IavaKTCHLIFIVLDVNKPLT--DKRIIEAELE---GFGIRINK 173
Cdd:cd01895   82 I---ERADVVLLVLDASEGITeqDLRIAGLILEegkALIIVVNK 122
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
66-120 1.44e-04

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 43.57  E-value: 1.44e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119187731  66 VGFIGFPSVGKSTLMSKLTGQHSEAAAYEFTTLTTVPGQVLYNGAKIQILDLPGI 120
Cdd:COG0370    6 IALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKGKEIELVDLPGT 60
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 232-289 1.72e-04

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


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 41.68  E-value: 1.72e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119187731 232 VLEAKSRSYIPVIYALNKIDSIS--------IEELDLLYRIPNACPISAEHGWNVDELLEQMWEKL 289
Cdd:cd04163  103 ILELLKKSKTPVILVLNKIDLVKdkedllplLEKLKELHPFAEIFPISALKGENVDELLEYIVEYL 168
EHD cd09913
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ...
 100-174 1.76e-04

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


Pssm-ID: 206740  Cd Length: 241  Bit Score: 42.65  E-value: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 100 TVPGQVLYngaKIQILDLPGIIQGAKDGKGRGRQVIAV----AKTCHLIFIVLDVNKP-LTD--KRIIEAeLEGF--GIR 170
Cdd:cd09913   81 TLPHPLLE---SVTIVDTPGILSGEKQRQSRGYDFNAVcrwfAERADLIFLLFDPHKLdISDefRRVIEQ-LKGHesKIR 156


                 ....*.
gi 119187731 171 I--NKS 174
Cdd:cd09913  157 IvlNKA 162
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 209-285 4.03e-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: 40.56  E-value: 4.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119187731 209 SEYRISSADIAIR-CDAT-IDDLIDVLEAKSRSYIPVIYALNKIDSISIEELDLLYRIPNACPISAEHGWNVDELLEQM 285
Cdd:cd04164   76 AREAIEEADLVLLvVDASeGLDEEDLEILELPAKKPVIVVLNKSDLLSDAEGISELNGKPIIAISAKTGEGIDELKEAL 154
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 64-120 4.47e-04

An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents archaeal GTPase typified by the protein MJ1464 from Methanococcus jannaschii. The members of this family show a circular permutation of the GTPase signature motifs so that C-terminal strands 5, 6, and 7 (strands 6 contain the NKxD motif) are relocated to the N terminus.


Pssm-ID: 206752 [Multi-domain]  Cd Length: 157  Bit Score: 40.38  E-value: 4.47e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119187731  64 ASVGFIGFPSVGKSTLMSKLTGQHSEAAAyeftTLTTVPG-----QVLYNGAKIQILDLPGI 120
Cdd:cd01859  100 VIVGVVGYPKVGKSSIINALKGRHSASTS----PIPGSPGytkgiQLVRIDSKIYLIDTPGV 157
PRK09602 PRK09602
translation-associated GTPase; Reviewed
 65-365 6.28e-04

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 41.33  E-value: 6.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  65 SVGFIGFPSVGKSTLMSKLTGQHSEAAAYEFTTLTTVPGqVLY-----------------NG--------AKIQILDLPG 119
Cdd:PRK09602   3 TIGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVG-VAYvrvecpckelgvkcnprNGkcidgtrfIPVELIDVAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 120 IIQGAKDGKGRG-------RQVIAvaktchlIFIVLDV---------------NKPLTDKRIIEAELEG--FGIrinksp 175
Cdd:PRK09602  82 LVPGAHEGRGLGnqflddlRQADA-------LIHVVDAsgstdeegnpvepgsHDPVEDIKFLEEELDMwiYGI------ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 176 pniVFKKKDKggisITSTVPLTHID-HDEIKAVMSEYRISSADI--AIR--------CDATIDDLID-VLEAKSRSYiPV 243
Cdd:PRK09602 149 ---LEKNWEK----FSRKAQAEKFDiEEALAEQLSGLGINEEHVkeALRelglpedpSKWTDEDLLElARELRKISK-PM 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 244 IYALNKIDSISIEE-LDLLYRI--PNACPISAEH-----------------GWN----VDEL-------LEQMWEKLN-- 290
Cdd:PRK09602 221 VIAANKADLPPAEEnIERLKEEkyYIVVPTSAEAelalrraakaglidyipGDSdfeiLGELsekqkkaLEYIREVLKky 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 291 ----------------LKRI----------YTKPKGKA-PDytapVVLKSNNCTVEDFCNAIHKSIVEQFKHAIvYGRSv 343
Cdd:PRK09602 301 ggtgvqeaintavfdlLDMIvvypvedenkLTDKKGNVlPD----AFLLPKGSTARDLAYKIHTDIGEGFLYAI-DART- 374

                        410       420
                 ....*....|....*....|..
gi 119187731 344 khqPQRVGLSHQLEDEDIITII 365
Cdd:PRK09602 375 ---KRRIGEDYELKDGDVIKIV 393
era PRK00089
GTPase Era; Reviewed
 232-289 6.33e-04

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 41.19  E-value: 6.33e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119187731 232 VLEAKSRSYIPVIYALNKIDSIS--------IEELDLLYRIPNACPISAEHGWNVDELLEQMWEKL 289
Cdd:PRK00089 105 ILEKLKKVKTPVILVLNKIDLVKdkeellplLEELSELMDFAEIVPISALKGDNVDELLDVIAKYL 170
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 241-285 1.11e-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: 39.43  E-value: 1.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  241 IPVIYALNKIDSISIEELDLLYR---------------IPNACPISAEHGWNVDELLEQM 285
Cdd:pfam00009 122 VPIIVFINKMDRVDGAELEEVVEevsrellekygedgeFVPVVPGSALKGEGVQTLLDAL 181
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 241-283 1.16e-03

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 39.59  E-value: 1.16e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 241 IPVIYALNKIDSISIEELDLLYR-----------------IPNACPISAEHGWNVDELLE 283
Cdd:cd00881  115 LPIIVAVNKIDRVGEEDFDEVLReikellkligftflkgkDVPIIPISALTGEGIEELLD 174
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
66-289 1.53e-03

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 39.97  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  66 VGFIGFPSVGKSTLMSKLTGQH----SEAAAyefTT-------LTTVPGQVLYngakiqiLDLPGIIQgAKDGKGRG--R 132
Cdd:COG1159    6 VAIVGRPNVGKSTLLNALVGQKvsivSPKPQ---TTrhrirgiVTREDAQIVF-------VDTPGIHK-PKRKLGRRmnK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 133 QVIAVAKTCHLIFIVLDVNKPLT--DKRIIEaelegfgiRINKSPpnivfkkkdkggisitstvplthidhdeikavmse 210
Cdd:COG1159   75 AAWSALEDVDVILFVVDATEKIGegDEFILE--------LLKKLK----------------------------------- 111

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731 211 yrissadiaircdatiddlidvleaksrsyIPVIYALNKIDSIS-------IEELDLLYRIPNACPISAEHGWNVDELLE 283
Cdd:COG1159  112 ------------------------------TPVILVINKIDLVKkeellplLAEYSELLDFAEIVPISALKGDNVDELLD 161


                 ....*.
gi 119187731 284 QMWEKL 289
Cdd:COG1159  162 EIAKLL 167
TGS_MJ1332_like cd01669
TGS (ThrRS, GTPase and SpoT) domain found in Methanocaldococcus jannaschii uncharacterized ...
 317-365 3.10e-03

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


Pssm-ID: 340460 [Multi-domain]  Cd Length: 78  Bit Score: 36.14  E-value: 3.10e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 119187731 317 TVEDFCNAIHKSIVEQFKHAIvygrSVKHQpQRVGLSHQLEDEDIITII 365
Cdd:cd01669   34 TPRDLAYKIHTDLGKGFLYAI----DARTK-MRLGEDYELKHGDVVKIV 77
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 212-296 4.62e-03

MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.


Pssm-ID: 463649 [Multi-domain]  Cd Length: 326  Bit Score: 38.62  E-value: 4.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  212 RISSADIAIRC-DAT--IDDLIDVLEAKSRSYIPVIYALNKIDSISIEELDLLYRIPNACPISAEHGWNVDELLEQMWEK 288
Cdd:pfam12631 170 AIEEADLVLLVlDASrpLDEEDLEILELLKDKKPIIVVLNKSDLLGEIDELEELKGKPVLAISAKTGEGLDELEEAIKEL 249


                  ....*...
gi 119187731  289 LNLKRIYT 296
Cdd:pfam12631 250 FLAGEIAS 257
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 64-121 5.68e-03

A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC class I region and is highly homologous to a putative GTP-binding protein, MMR1 from mouse. These proteins represent a new subfamily of GTP-binding proteins that has only eukaryote members. This subfamily shows a circular permutation of the GTPase signature motifs so that the C-terminal strands 5, 6, and 7 (strand 6 contains the G4 box with sequence NKXD) are relocated to the N-terminus.


Pssm-ID: 206750 [Multi-domain]  Cd Length: 140  Bit Score: 36.83  E-value: 5.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119187731  64 ASVGFIGFPSVGKSTLMSKLTGQhseaaayEFTTLTTVPG-----QVLYNGAKIQILDLPGII 121
Cdd:cd01857   83 ATIGLVGYPNVGKSSLINALVGS-------KKVSVSSTPGktkhfQTIFLEPGITLCDCPGLV 138
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
241-290 7.80e-03

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 36.88  E-value: 7.80e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119187731 241 IPVIYALNKIDSISIEELDLLYRIPNAC---------PISAEHGWNVDELLEQMWEKLN 290
Cdd:COG1100  112 SPIILVLNKIDLYDEEEIEDEERLKEALsednivevvATSAKTGEGVEELFAALAEILR 170
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
62-184 8.64e-03

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 36.88  E-value: 8.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119187731  62 GVASVGFIGFPSVGKSTLMSKLTGQHSEAAAYEFT---TLTTVPGQVLYNGAKIQILDLPGIiqgakDGKGRGRQVIAVA 138
Cdd:COG1100    2 GEKKIVVVGTGGVGKTSLVNRLVGDIFSLEKYLSTngvTIDKKELKLDGLDVDLVIWDTPGQ-----DEFRETRQFYARQ 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 119187731 139 -KTCHLIFIVLDVNKPLTDKRIIEAeLEGFgIRINKSPPNI-VFKKKD 184
Cdd:COG1100   77 lTGASLYLFVVDGTREETLQSLYEL-LESL-RRLGKKSPIIlVLNKID 122
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
65-120 9.45e-03

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 38.16  E-value: 9.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119187731  65 SVGFIGFPSVGKSTLMSKLTGQHSEAAAYEFTTLTTVPGQVLYNGAKIQILDLPGI 120
Cdd:PRK09554   5 TIGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQFSTTDHQVTLVDLPGT 60
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH