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Conserved domains on  [gi|530410017|ref|XP_005256557|]
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developmentally-regulated GTP-binding protein 2 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 1-214 2.12e-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: 405.39  E-value: 2.12e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017   1 MTSTASEAASYEFTTLTCIPGVIEYKGANIQLLDLPGIIEGAAQGKGRGRQVIAVARTADVIIMMLDATKGEVQRSLLEK 80
Cdd:cd01896   20 LTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADLILIVLDATKPEGQREILER 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017  81 ELESVGIRLNKHKPNIYFKPKKGGGISFNSTVTLTQCSEKLVQLILHEYKIFNAEVLFREDCSPDEFIDVIVGNRVYMPC 160
Cdd:cd01896  100 ELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLTKLDEKTVKAILREYKIHNADVLIREDITVDDLIDVIEGNRVYIPC 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530410017 161 LYVYNKIDQISMEEVDRLARKPNSVVISCGMKLNLDYLLEMLWEYLALTCIYTK 214
Cdd:cd01896  180 LYVYNKIDLISIEELDRLARIPNSVVISAEKDLNLDELLERIWDYLGLIRIYTK 233
TGS_DRG2 cd17231
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 2 ...
 205-304 4.61e-54

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: 170.64  E-value: 4.61e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017 205 YLALTCIYTKKRGqsqdgsvgpdvwltfspscpaERPDFTDAIILRKGASVEHVCHRIHRSLASQFKYALVWGTSTKYSP 284
Cdd:cd17231    1 YLALIRVYTKKRG---------------------ERPDFGDAIILRRGATVEHVCHRIHRTLASQFKYALVWGTSTKYSP 59

                         90       100
                 ....*....|....*....|
gi 530410017 285 QRVGLTHTMEHEDVIQIVKK 304
Cdd:cd17231   60 QRVGLTHVMEDEDVIQIVKK 79
 
Name Accession Description Interval E-value
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 1-214 2.12e-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: 405.39  E-value: 2.12e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017   1 MTSTASEAASYEFTTLTCIPGVIEYKGANIQLLDLPGIIEGAAQGKGRGRQVIAVARTADVIIMMLDATKGEVQRSLLEK 80
Cdd:cd01896   20 LTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADLILIVLDATKPEGQREILER 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017  81 ELESVGIRLNKHKPNIYFKPKKGGGISFNSTVTLTQCSEKLVQLILHEYKIFNAEVLFREDCSPDEFIDVIVGNRVYMPC 160
Cdd:cd01896  100 ELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLTKLDEKTVKAILREYKIHNADVLIREDITVDDLIDVIEGNRVYIPC 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530410017 161 LYVYNKIDQISMEEVDRLARKPNSVVISCGMKLNLDYLLEMLWEYLALTCIYTK 214
Cdd:cd01896  180 LYVYNKIDLISIEELDRLARIPNSVVISAEKDLNLDELLERIWDYLGLIRIYTK 233
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
1-304 1.20e-116

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 340.24  E-value: 1.20e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017   1 MTSTASEAASYEFTTLTCIPGVIEYKGANIQLLDLPGIIEGAAQGKGRGRQVIAVARTADVIIMMLDATKGEvQRSLLEK 80
Cdd:COG1163   83 LTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELE-QYDVLKE 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017  81 ELESVGIRLNKHKPNIYFKPKKGGGISFNSTVTLTqCSEKLVQLILHEYKIFNAEVLFREDCSPDEFIDVIVGNRVYMPC 160
Cdd:COG1163  162 ELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLD-LDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRVYKPA 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017 161 LYVYNKIDQISMEEVDRLARK----PNSVVISCGMKLNLDYLLEMLWEYLALTCIYTKKRGQSQDgsvgpdvwltfspsc 236
Cdd:COG1163  241 IVVVNKIDLADEEYVEELKSKlpdgVPVIFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKAD--------------- 305

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530410017 237 pAERPdftdaIILRKGASVEHVCHRIHRSLASQFKYALVWGTSTKYSPQRVGLTHTMEHEDVIQIVKK 304
Cdd:COG1163  306 -MEEP-----LILRKGSTVGDVCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIK 367
MMR_HSR1_Xtn pfam16897
C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of ...
 104-208 9.23e-63

C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of the MMR_HSR1 family.


Pssm-ID: 465301 [Multi-domain]  Cd Length: 105  Bit Score: 193.80  E-value: 9.23e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017  104 GGISFNSTVTLTQCSEKLVQLILHEYKIFNAEVLFREDCSPDEFIDVIVGNRVYMPCLYVYNKIDQISMEEVDRLARKPN 183
Cdd:pfam16897   1 GGINITSTVPLTKLDEETIKAILREYKIHNADVLIREDVTVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDRLAREPD 80

                          90       100
                  ....*....|....*....|....*
gi 530410017  184 SVVISCGMKLNLDYLLEMLWEYLAL 208
Cdd:pfam16897  81 SVPISAEKGLNLDELKERIWEYLGL 105
TGS_DRG2 cd17231
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 2 ...
 205-304 4.61e-54

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: 170.64  E-value: 4.61e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017 205 YLALTCIYTKKRGqsqdgsvgpdvwltfspscpaERPDFTDAIILRKGASVEHVCHRIHRSLASQFKYALVWGTSTKYSP 284
Cdd:cd17231    1 YLALIRVYTKKRG---------------------ERPDFGDAIILRRGATVEHVCHRIHRTLASQFKYALVWGTSTKYSP 59

                         90       100
                 ....*....|....*....|
gi 530410017 285 QRVGLTHTMEHEDVIQIVKK 304
Cdd:cd17231   60 QRVGLTHVMEDEDVIQIVKK 79
TGS pfam02824
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ...
 249-303 1.62e-18

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


Pssm-ID: 427005 [Multi-domain]  Cd Length: 60  Bit Score: 77.59  E-value: 1.62e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530410017  249 LRKGASVEHVCHRIHRSLASQFKYALVWGtstkyspQRVGLTHTMEHEDVIQIVK 303
Cdd:pfam02824  13 LPRGATPEDFAYAIHTSLAKKFIYAKVNG-------QLVGLDHPLEDGDVVEIVT 60
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 6-134 5.65e-13

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: 65.47  E-value: 5.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017    6 SEAASYEFTTLTCIPGVIEYKG--ANIQLLDLPGIIEGAAQGKGRGRQVIAVARTADVIIMMLDATKG-EVQRSLLEKEL 82
Cdd:TIGR00231  27 SITEYYPGTTRNYVTTVIEEDGktYKFNLLDTAGQEDYDAIRRLYYPQVERSLRVFDIVILVLDVEEIlEKQTKEIIHHA 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530410017   83 ES-VGIRLNKHKPNI---YFKPKKGGGISFNSTVTLTQCSEKLVQLILHEYKIFNA 134
Cdd:TIGR00231 107 DSgVPIILVGNKIDLkdaDLKTHVASEFAKLNGEPIIPLSAETGKNIDSAFKIVEA 162
obgE PRK12297
GTPase CgtA; Reviewed
 9-181 5.65e-11

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 62.81  E-value: 5.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017   9 ASYEFTTLTCIPGVIEYKGAN-IQLLDLPGIIEGAAQGKGRGRQVIA-VARTAdVIIMMLDATkGEVQRSLLE------K 80
Cdd:PRK12297 186 ANYHFTTLVPNLGVVETDDGRsFVMADIPGLIEGASEGVGLGHQFLRhIERTR-VIVHVIDMS-GSEGRDPIEdyekinK 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017  81 ELESVGIRLNKhKPNI----------------YFKPKKGGGISFNSTVTlTQCSEKLVQLI---LHEYKIFNA------- 134
Cdd:PRK12297 264 ELKLYNPRLLE-RPQIvvankmdlpeaeenleEFKEKLGPKVFPISALT-GQGLDELLYAVaelLEETPEFPLeeeevee 341

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530410017 135 EVLFREDCSPDEF-ID-------VIVGNRVYmpclYVYNKIDQISMEEVDRLARK 181
Cdd:PRK12297 342 EVYYKFEEEEKDFtITrdedgvfVVSGEKIE----RLFKMTNFNRDESLRRFARQ 392
 
Name Accession Description Interval E-value
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 1-214 2.12e-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: 405.39  E-value: 2.12e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017   1 MTSTASEAASYEFTTLTCIPGVIEYKGANIQLLDLPGIIEGAAQGKGRGRQVIAVARTADVIIMMLDATKGEVQRSLLEK 80
Cdd:cd01896   20 LTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADLILIVLDATKPEGQREILER 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017  81 ELESVGIRLNKHKPNIYFKPKKGGGISFNSTVTLTQCSEKLVQLILHEYKIFNAEVLFREDCSPDEFIDVIVGNRVYMPC 160
Cdd:cd01896  100 ELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLTKLDEKTVKAILREYKIHNADVLIREDITVDDLIDVIEGNRVYIPC 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530410017 161 LYVYNKIDQISMEEVDRLARKPNSVVISCGMKLNLDYLLEMLWEYLALTCIYTK 214
Cdd:cd01896  180 LYVYNKIDLISIEELDRLARIPNSVVISAEKDLNLDELLERIWDYLGLIRIYTK 233
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
1-304 1.20e-116

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 340.24  E-value: 1.20e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017   1 MTSTASEAASYEFTTLTCIPGVIEYKGANIQLLDLPGIIEGAAQGKGRGRQVIAVARTADVIIMMLDATKGEvQRSLLEK 80
Cdd:COG1163   83 LTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELE-QYDVLKE 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017  81 ELESVGIRLNKHKPNIYFKPKKGGGISFNSTVTLTqCSEKLVQLILHEYKIFNAEVLFREDCSPDEFIDVIVGNRVYMPC 160
Cdd:COG1163  162 ELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLD-LDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRVYKPA 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017 161 LYVYNKIDQISMEEVDRLARK----PNSVVISCGMKLNLDYLLEMLWEYLALTCIYTKKRGQSQDgsvgpdvwltfspsc 236
Cdd:COG1163  241 IVVVNKIDLADEEYVEELKSKlpdgVPVIFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKAD--------------- 305

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530410017 237 pAERPdftdaIILRKGASVEHVCHRIHRSLASQFKYALVWGTSTKYSPQRVGLTHTMEHEDVIQIVKK 304
Cdd:COG1163  306 -MEEP-----LILRKGSTVGDVCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIK 367
MMR_HSR1_Xtn pfam16897
C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of ...
 104-208 9.23e-63

C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of the MMR_HSR1 family.


Pssm-ID: 465301 [Multi-domain]  Cd Length: 105  Bit Score: 193.80  E-value: 9.23e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017  104 GGISFNSTVTLTQCSEKLVQLILHEYKIFNAEVLFREDCSPDEFIDVIVGNRVYMPCLYVYNKIDQISMEEVDRLARKPN 183
Cdd:pfam16897   1 GGINITSTVPLTKLDEETIKAILREYKIHNADVLIREDVTVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDRLAREPD 80

                          90       100
                  ....*....|....*....|....*
gi 530410017  184 SVVISCGMKLNLDYLLEMLWEYLAL 208
Cdd:pfam16897  81 SVPISAEKGLNLDELKERIWEYLGL 105
TGS_DRG2 cd17231
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 2 ...
 205-304 4.61e-54

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: 170.64  E-value: 4.61e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017 205 YLALTCIYTKKRGqsqdgsvgpdvwltfspscpaERPDFTDAIILRKGASVEHVCHRIHRSLASQFKYALVWGTSTKYSP 284
Cdd:cd17231    1 YLALIRVYTKKRG---------------------ERPDFGDAIILRRGATVEHVCHRIHRTLASQFKYALVWGTSTKYSP 59

                         90       100
                 ....*....|....*....|
gi 530410017 285 QRVGLTHTMEHEDVIQIVKK 304
Cdd:cd17231   60 QRVGLTHVMEDEDVIQIVKK 79
TGS_DRG1 cd17230
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 1 ...
 205-304 6.79e-35

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: 121.22  E-value: 6.79e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017 205 YLALTCIYTKKRGQsqdgsvgpdvwltfspscpaeRPDFTDAIILRKGA-SVEHVCHRIHRSLASQFKYALVWGTSTKYS 283
Cdd:cd17230    1 YLNLVRIYTKPKGQ---------------------LPDYEEPVVLRSGKsTVEDFCNKIHKSLIKEFKYALVWGSSVKHN 59

                         90       100
                 ....*....|....*....|.
gi 530410017 284 PQRVGLTHTMEHEDVIQIVKK 304
Cdd:cd17230   60 PQRVGKDHVLEDEDVVQIVKK 80
TGS_DRG cd01666
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein ...
 206-303 7.04e-35

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: 121.19  E-value: 7.04e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017 206 LALTCIYTKKRGQsqdgsvgpdvwltfspscpaeRPDFTDAIILRKGASVEHVCHRIHRSLASQFKYALVWGTSTKYSPQ 285
Cdd:cd01666    1 LGIIRVYTKPPGK---------------------KPDFDEPFILRRGSTVEDVAEKIHKDLAENFKYARVWGKSVKFDGQ 59

                         90
                 ....*....|....*...
gi 530410017 286 RVGLTHTMEHEDVIQIVK 303
Cdd:cd01666   60 RVGLDHVLEDGDIVEIHK 77
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 1-206 1.09e-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: 105.55  E-value: 1.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017   1 MTSTASEAASYEFTTLTCIPGVIEYK-GANIQLLDLPGIIEGAAQGKGRGRQVIAVARTADVIIMMLDatkgevqrslle 79
Cdd:cd01881   17 LTSAKVEIASYPFTTLEPNVGVFEFGdGVDIQIIDLPGLLDGASEGRGLGEQILAHLYRSDLILHVID------------ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017  80 kelesvgirlnkhkpniyfkpkkgggisfnstvtltqCSEKLVQLILHEYKIFNAEVLFREDcspdefidvivgNRVYMP 159
Cdd:cd01881   85 -------------------------------------ASEDCVGDPLEDQKTLNEEVSGSFL------------FLKNKP 115

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530410017 160 CLYVYNKIDQISMEEV-----DRLARKPNSVVISCGMKLNLDYLLEMLWEYL 206
Cdd:cd01881  116 EMIVANKIDMASENNLkrlklDKLKRGIPVVPTSALTRLGLDRVIRTIRKLL 167
TGS pfam02824
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ...
 249-303 1.62e-18

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


Pssm-ID: 427005 [Multi-domain]  Cd Length: 60  Bit Score: 77.59  E-value: 1.62e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530410017  249 LRKGASVEHVCHRIHRSLASQFKYALVWGtstkyspQRVGLTHTMEHEDVIQIVK 303
Cdd:pfam02824  13 LPRGATPEDFAYAIHTSLAKKFIYAKVNG-------QLVGLDHPLEDGDVVEIVT 60
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 1-91 5.76e-17

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: 74.96  E-value: 5.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017    1 MTSTASEAASYEFTTLTCIPGVIEYKGANIQLLDLPGIIEGAAQGKGRGRQVIAVARtADVIIMMLDATKGevqRSLLEK 80
Cdd:pfam01926  19 LTGAKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFLAIIE-ADLILFVVDSEEG---ITPLDE 94

                          90
                  ....*....|.
gi 530410017   81 ELESVGIRLNK 91
Cdd:pfam01926  95 ELLELLRENKK 105
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 6-134 5.65e-13

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: 65.47  E-value: 5.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017    6 SEAASYEFTTLTCIPGVIEYKG--ANIQLLDLPGIIEGAAQGKGRGRQVIAVARTADVIIMMLDATKG-EVQRSLLEKEL 82
Cdd:TIGR00231  27 SITEYYPGTTRNYVTTVIEEDGktYKFNLLDTAGQEDYDAIRRLYYPQVERSLRVFDIVILVLDVEEIlEKQTKEIIHHA 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530410017   83 ES-VGIRLNKHKPNI---YFKPKKGGGISFNSTVTLTQCSEKLVQLILHEYKIFNA 134
Cdd:TIGR00231 107 DSgVPIILVGNKIDLkdaDLKTHVASEFAKLNGEPIIPLSAETGKNIDSAFKIVEA 162
obgE PRK12297
GTPase CgtA; Reviewed
 9-181 5.65e-11

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 62.81  E-value: 5.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017   9 ASYEFTTLTCIPGVIEYKGAN-IQLLDLPGIIEGAAQGKGRGRQVIA-VARTAdVIIMMLDATkGEVQRSLLE------K 80
Cdd:PRK12297 186 ANYHFTTLVPNLGVVETDDGRsFVMADIPGLIEGASEGVGLGHQFLRhIERTR-VIVHVIDMS-GSEGRDPIEdyekinK 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017  81 ELESVGIRLNKhKPNI----------------YFKPKKGGGISFNSTVTlTQCSEKLVQLI---LHEYKIFNA------- 134
Cdd:PRK12297 264 ELKLYNPRLLE-RPQIvvankmdlpeaeenleEFKEKLGPKVFPISALT-GQGLDELLYAVaelLEETPEFPLeeeevee 341

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530410017 135 EVLFREDCSPDEF-ID-------VIVGNRVYmpclYVYNKIDQISMEEVDRLARK 181
Cdd:PRK12297 342 EVYYKFEEEEKDFtITrdedgvfVVSGEKIE----RLFKMTNFNRDESLRRFARQ 392
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 9-94 1.77e-09

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: 55.89  E-value: 1.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017   9 ASYEFTTLtcIP--GVIEYK-GANIQLLDLPGIIEGAAQGKGRG----RQviaVARTaDVIIMMLDATKGE--VQR-SLL 78
Cdd:cd01898   28 ADYPFTTL--VPnlGVVRVDdGRSFVIADIPGLIEGASEGKGLGhrflRH---IERT-RVLLHVIDLSGEDdpVEDyETI 101

                         90
                 ....*....|....*.
gi 530410017  79 EKELESVGIRLNKhKP 94
Cdd:cd01898  102 RNELEAYNPGLAE-KP 116
TGS_Obg cd04938
TGS (ThrRS, GTPase and SpoT) domain found in the Obg protein family; The Obg family of GTPases ...
 211-302 5.36e-08

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


Pssm-ID: 340517 [Multi-domain]  Cd Length: 77  Bit Score: 49.37  E-value: 5.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017 211 IYTKKRGQSQdgsvgpdvwltfspSCPAERPDFTDAIILRKGASVEHVCHRIHRSLASQFKYALVWGtstkySPQRVGLT 290
Cdd:cd04938    5 VYPVKNIQTF--------------TNGSGNSVFRDCVLVKKGTTVKDFANKIHTDLEKGFINAEGIG-----GRRLEGED 65

                         90
                 ....*....|..
gi 530410017 291 HTMEHEDVIQIV 302
Cdd:cd04938   66 YILQDNDVVKFT 77
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 6-91 8.29e-08

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: 50.71  E-value: 8.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017   6 SEAASYEFTTLTCIPGVIE-YKGANIQLLDLPGIIEGAAQGKGRGRQVIAVARTADVIIMMLDATKGEVQRSLLEKELES 84
Cdd:cd00880   23 GIVSPIPGTTRDPVRKEWElLPLGPVVLIDTPGLDEEGGLGRERVEEARQVADRADLVLLVVDSDLTPVEEEAKLGLLRE 102

                         90
                 ....*....|.
gi 530410017  85 VGIR----LNK 91
Cdd:cd00880  103 RGKPvllvLNK 113
obgE PRK12299
GTPase CgtA; Reviewed
 3-135 3.08e-07

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 50.84  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017   3 STASEA----ASYEFTTLTCIPGVIEYKGAN-IQLLDLPGIIEGAAQGKGRGRQVIA-VARTAdVIIMMLDATKGEVQRS 76
Cdd:PRK12299 176 SAVSAAkpkiADYPFTTLHPNLGVVRVDDYKsFVIADIPGLIEGASEGAGLGHRFLKhIERTR-LLLHLVDIEAVDPVED 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017  77 --LLEKELESVG---------IRLNK----------HKPNIYFKPKKGGGISFNSTVTLTQCsEKLVQLILHEYKIFNAE 135
Cdd:PRK12299 255 ykTIRNELEKYSpeladkpriLVLNKidlldeeeerEKRAALELAALGGPVFLISAVTGEGL-DELLRALWELLEEARRE 333
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 159-207 1.66e-06

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 48.93  E-value: 1.66e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 530410017 159 PCLYVYNKIDQISMEEVDRL-ARKPNSVVISCGMKLNLDYLLEMLWEYLA 207
Cdd:COG2262  313 PIILVFNKIDLLDDEELERLrAGYPDAVFISAKTGEGIDELLEAIEERLP 362
obgE PRK12296
GTPase CgtA; Reviewed
 9-83 8.20e-06

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 47.17  E-value: 8.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017   9 ASYEFTTLtcIP--GVIEYKGANIQLLDLPGIIEGAAQGKGRGRQVIA-VARTAdVIIMMLDATKGEVQRS------LLE 79
Cdd:PRK12296 187 ADYPFTTL--VPnlGVVQAGDTRFTVADVPGLIPGASEGKGLGLDFLRhIERCA-VLVHVVDCATLEPGRDplsdidALE 263


                 ....
gi 530410017  80 KELE 83
Cdd:PRK12296 264 AELA 267
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 159-206 1.23e-05

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


Pssm-ID: 206666 [Multi-domain]  Cd Length: 204  Bit Score: 45.14  E-value: 1.23e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 530410017 159 PCLYVYNKIDQISMEEVDRLARK--PNSVVISCGMKLNLDYLLEMLWEYL 206
Cdd:cd01878  155 PIILVLNKIDLLDDEELEERLRAgrPDAVFISAKTGEGLDLLKEAIEELL 204
GTP_HflX TIGR03156
GTP-binding protein HflX; This protein family is one of a number of homologous small, ...
 159-206 1.29e-05

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


Pssm-ID: 274455 [Multi-domain]  Cd Length: 351  Bit Score: 45.93  E-value: 1.29e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 530410017  159 PCLYVYNKIDQISMEEVDRLAR-KPNSVVISCGMKLNLDYLLEMLWEYL 206
Cdd:TIGR03156 303 PQLLVYNKIDLLDEPRIERLEEgYPEAVFVSAKTGEGLDLLLEAIAERL 351
TGS_MJ1332_like cd01669
TGS (ThrRS, GTPase and SpoT) domain found in Methanocaldococcus jannaschii uncharacterized ...
 245-302 1.76e-05

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


Pssm-ID: 340460 [Multi-domain]  Cd Length: 78  Bit Score: 42.30  E-value: 1.76e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530410017 245 DAIILRKGASVEHVCHRIHRSLASQFKYALvwGTSTKyspQRVGLTHTMEHEDVIQIV 302
Cdd:cd01669   25 DAILLKRGSTPRDLAYKIHTDLGKGFLYAI--DARTK---MRLGEDYELKHGDVVKIV 77
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 23-91 3.24e-05

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: 43.60  E-value: 3.24e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530410017  23 IEYKGANIQLLDLPGIIEGaaQGKGRGRQVIAVARTADVIIMMLDATKGEV---QRSLLEKELESVGIR----LNK 91
Cdd:cd00882   42 LDKGKVKLVLVDTPGLDEF--GGLGREELARLLLRGADLILLVVDSTDRESeedAKLLILRRLRKEGIPiilvGNK 115
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
1-79 3.52e-05

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 44.82  E-value: 3.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017   1 MTSTASEAASYEFTTLTCIPGVIEYKGANIQLLDLPGI----------IEgaaqgkgrgRQ-VIAVARTADVIIMMLDA- 68
Cdd:COG1084  180 VTSAKPEIASYPFTTKGIIVGHFERGHGRYQVIDTPGLldrplserneIE---------RQaILALKHLADVILFLFDPs 250

                         90
                 ....*....|....*
gi 530410017  69 -TKG---EVQRSLLE 79
Cdd:COG1084  251 eTCGyslEEQLNLLE 265
PRK09602 PRK09602
translation-associated GTPase; Reviewed
 7-69 6.25e-05

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 44.03  E-value: 6.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410017   7 EAASYEFTT--------------------LTCIPGVIEYKGAN----IQLLDLPGIIEGAAQGKGRGRQVIAVARTADVI 62
Cdd:PRK09602  27 EIANYPFTTidpnvgvayvrvecpckelgVKCNPRNGKCIDGTrfipVELIDVAGLVPGAHEGRGLGNQFLDDLRQADAL 106


                 ....*..
gi 530410017  63 IMMLDAT 69
Cdd:PRK09602 107 IHVVDAS 113
obgE PRK12298
GTPase CgtA; Reviewed
 9-49 9.04e-05

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 43.70  E-value: 9.04e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 530410017   9 ASYEFTTLtcIP--GVIEY-KGANIQLLDLPGIIEGAAQGKGRG 49
Cdd:PRK12298 187 ADYPFTTL--VPnlGVVRVdDERSFVVADIPGLIEGASEGAGLG 228
EHD cd09913
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ...
 30-91 3.57e-04

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


Pssm-ID: 206740  Cd Length: 241  Bit Score: 41.11  E-value: 3.57e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530410017  30 IQLLDLPGIIEGAAQGKGRGRQVIAVAR----TADVIIMMLDATKGEVQ---RSLLEKEL---ESVGIRLNK 91
Cdd:cd09913   90 VTIVDTPGILSGEKQRQSRGYDFNAVCRwfaeRADLIFLLFDPHKLDISdefRRVIEQLKgheSKIRIVLNK 161
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 3-69 2.45e-03

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: 37.92  E-value: 2.45e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530410017   3 STAS-EAASYEFTTLTCIPGVIEYKGANIQLLDLPGI----------IEgaaqgkgrgRQVI-AVARTADVIIMMLDAT 69
Cdd:cd01897   21 TRAKpEVAPYPFTTKSLFVGHFDYKYLRWQVIDTPGIldrpleerntIE---------MQAItALAHLRAAVLFFIDPS 90
 
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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