NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|20129659|ref|NP_610055|]
View 

nucleostemin 4 [Drosophila melanogaster]

Protein Classification

HSR1_MMR1 and RbgA domain-containing protein( domain architecture ID 12923183)

HSR1_MMR1 and RbgA domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
163-390 1.12e-64

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: 207.85  E-value: 1.12e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 163 TWRQLWRVLEFSDILLIIVDVRYATLMFPPSLYDYIINTLK-KHAIVVFNKVDLVEPHAVVAWRQYFRDRYPqlpVVLFA 241
Cdd:cd01857   1 VWRQLWRVIERSDVVVQIVDARNPLFFRCPDLEKYVKEVDPsKENVLLLNKADLVTEEQRKAWARYFKKEGI---VVLFF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 242 SFLPRSrkgsqrgpqahrrsmegvyniykecqryvqgevdlttweqkiredmrsdqldildeistavegelkisssidtt 321
Cdd:cd01857  78 SALNEA-------------------------------------------------------------------------- 83
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20129659 322 phehvkyhsgvlTIGCIGFPNVGKSSLINALKGRKVVSVSRTPGHTKHFQTIFLTPLVRLCDCPGLVFP 390
Cdd:cd01857  84 ------------TIGLVGYPNVGKSSLINALVGSKKVSVSSTPGKTKHFQTIFLEPGITLCDCPGLVFP 140
RbgA super family cl34151
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
204-474 4.92e-18

Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG1161:

Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 84.39  E-value: 4.92e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 204 KHAIVVFNKVDLVEPHAVVAWRQYFRDRypQLPVVLFASflprsRKGSqrgpqahrrsmeGVYNIYKECQRYVQGEvdlt 283
Cdd:COG1161  51 KPRLLVLNKADLADPSVTKQWLKYFEKQ--GVDALAISA-----KKGK------------GIKELIEAIRELAPEK---- 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 284 tweQKIREDMRsdqldildeistavegelkisssidttphehvkyhsgVLTIGCigfPNVGKSSLINALKGRKVVSVSRT 363
Cdd:COG1161 108 ---GIKRRPIR-------------------------------------VMIVGI---PNVGKSTLINRLAGKKVAKTGNK 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 364 PGHTKHFQTIFLTPLVRLCDCPGLVFPS-STPKSLQVLLGSFPISQLAVPYRSL-KFLGEHL--NLPQLL--RLHLPEdy 437
Cdd:COG1161 145 PGVTKGQQWIKLDDGLELLDTPGILWPKfEDPEVGYKLAATGAIKDEVLDLEEVaLFLLGYLarRYPELLkeRYKLDE-- 222
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 20129659 438 DEWSAVAISDAWAYKRGFLTAKaARPDRYRAANHILR 474
Cdd:COG1161 223 LPRTKLELLEAIGRKRGCLLSG-GEVDLEKAAEILLT 258
 
Name Accession Description Interval E-value
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
163-390 1.12e-64

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: 207.85  E-value: 1.12e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 163 TWRQLWRVLEFSDILLIIVDVRYATLMFPPSLYDYIINTLK-KHAIVVFNKVDLVEPHAVVAWRQYFRDRYPqlpVVLFA 241
Cdd:cd01857   1 VWRQLWRVIERSDVVVQIVDARNPLFFRCPDLEKYVKEVDPsKENVLLLNKADLVTEEQRKAWARYFKKEGI---VVLFF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 242 SFLPRSrkgsqrgpqahrrsmegvyniykecqryvqgevdlttweqkiredmrsdqldildeistavegelkisssidtt 321
Cdd:cd01857  78 SALNEA-------------------------------------------------------------------------- 83
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20129659 322 phehvkyhsgvlTIGCIGFPNVGKSSLINALKGRKVVSVSRTPGHTKHFQTIFLTPLVRLCDCPGLVFP 390
Cdd:cd01857  84 ------------TIGLVGYPNVGKSSLINALVGSKKVSVSSTPGKTKHFQTIFLEPGITLCDCPGLVFP 140
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
204-474 4.92e-18

Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 84.39  E-value: 4.92e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 204 KHAIVVFNKVDLVEPHAVVAWRQYFRDRypQLPVVLFASflprsRKGSqrgpqahrrsmeGVYNIYKECQRYVQGEvdlt 283
Cdd:COG1161  51 KPRLLVLNKADLADPSVTKQWLKYFEKQ--GVDALAISA-----KKGK------------GIKELIEAIRELAPEK---- 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 284 tweQKIREDMRsdqldildeistavegelkisssidttphehvkyhsgVLTIGCigfPNVGKSSLINALKGRKVVSVSRT 363
Cdd:COG1161 108 ---GIKRRPIR-------------------------------------VMIVGI---PNVGKSTLINRLAGKKVAKTGNK 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 364 PGHTKHFQTIFLTPLVRLCDCPGLVFPS-STPKSLQVLLGSFPISQLAVPYRSL-KFLGEHL--NLPQLL--RLHLPEdy 437
Cdd:COG1161 145 PGVTKGQQWIKLDDGLELLDTPGILWPKfEDPEVGYKLAATGAIKDEVLDLEEVaLFLLGYLarRYPELLkeRYKLDE-- 222
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 20129659 438 DEWSAVAISDAWAYKRGFLTAKaARPDRYRAANHILR 474
Cdd:COG1161 223 LPRTKLELLEAIGRKRGCLLSG-GEVDLEKAAEILLT 258
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
165-474 2.26e-17

ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding proteins involved in ribosome biogenesis, including the essential YlqF protein of Bacillus subtilis, which is an essential protein. They are related to Era, EngA, and other GTPases of ribosome biogenesis, but are circularly permuted. This family is not universal, and is not present in Escherichia coli, and so is not as well studied as some other GTPases. This model is built for bacterial members. [Protein synthesis, Other]


Pssm-ID: 274669 [Multi-domain]  Cd Length: 276  Bit Score: 82.56  E-value: 2.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659   165 RQLWRVLEFSDILLIIVDVRYATLMFPPSLYDYIINtlKKHaIVVFNKVDLVEPHAVVAWRQYFRDrypQLPVVLFASfl 244
Cdd:TIGR03596  13 REIKENLKLVDVVIEVLDARIPLSSRNPMIDEIRGN--KPR-LIVLNKADLADPAVTKQWLKYFEE---KGIKALAVN-- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659   245 prSRKGSqrgpqahrrsmeGVYNIYKECQRyvqgevdlttweqkiredMRSDQLDILDEistavEGELKISssidttphe 324
Cdd:TIGR03596  85 --AKKGA------------GVKKIIKAAKK------------------LLKEKNEKLKA-----KGLKNRP--------- 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659   325 hvkyhsgvLTIGCIGFPNVGKSSLINALKGRKVVSVSRTPGHTKHFQTIFLTPLVRLCDCPGLVFPSSTPKSLQVLL--- 401
Cdd:TIGR03596 119 --------IRAMIVGIPNVGKSTLINRLAGKKVAKVGNRPGVTKGQQWIKLSDNLELLDTPGILWPKFEDQEVGLKLaat 190
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20129659   402 GSfpISQLAVPYRSL-KFLGEHL--NLPQLLRLHLPEDYDEWSAVAISDAWAYKRGFLTaKAARPDRYRAANHILR 474
Cdd:TIGR03596 191 GA--IKDEALDLEDVaLFLLEYLleHYPELLKERYKLDELPEDPVELLEAIAKKRGCLL-KGGELDLDRAAEILLN 263
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
334-397 6.79e-16

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: 73.81  E-value: 6.79e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20129659   334 TIGCIGFPNVGKSSLINALKGRKVVsVSRTPGHTKHFQTIFLTPL---VRLCDCPGLVFPSSTPKSL 397
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAI-VSDYPGTTRDPNEGRLELKgkqIILVDTPGLIEGASEGEGL 66
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
342-386 1.13e-07

ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other]


Pssm-ID: 274670 [Multi-domain]  Cd Length: 179  Bit Score: 52.09  E-value: 1.13e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 20129659   342 NVGKSSLINALKGRK-VVSVSRTPGHTkhfQTI---FLTPLVRLCDCPG 386
Cdd:TIGR03598  28 NVGKSSLINALTNRKkLARTSKTPGRT---QLInffEVNDGFRLVDLPG 73
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
342-386 1.34e-07

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 439988 [Multi-domain]  Cd Length: 194  Bit Score: 52.00  E-value: 1.34e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 20129659 342 NVGKSSLINALKGRK-VVSVSRTPGHTkhfQTI--F-LTPLVRLCDCPG 386
Cdd:COG0218  33 NVGKSSLINALTNRKkLARTSKTPGKT---QLInfFlINDKFYLVDLPG 78
era PRK00089
GTPase Era; Reviewed
327-377 4.27e-07

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 51.97  E-value: 4.27e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20129659  327 KYHSGVLTIgcIGFPNVGKSSLINALKGRKVVSVSRTPG----------HTKHFQTIFL-TP 377
Cdd:PRK00089   2 GFKSGFVAI--VGRPNVGKSTLLNALVGQKISIVSPKPQttrhrirgivTEDDAQIIFVdTP 61
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
287-367 3.76e-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: 39.77  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659   287 QKIREdMRSDQLDIL-----------DEISTAVEGEL-----KISSSIDT---TPHEHVKYHSGVLT-IgcIGFPNVGKS 346
Cdd:pfam12631  32 RKIEE-LREKLLELLalieaaidfpeDDIEELTEEELlerleELLAELEKllaTADRGRILREGIKVvI--VGKPNVGKS 108
                          90       100
                  ....*....|....*....|.
gi 20129659   347 SLINALKGRKVVSVSRTPGHT 367
Cdd:pfam12631 109 SLLNALLGEERAIVTDIPGTT 129
 
Name Accession Description Interval E-value
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
163-390 1.12e-64

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: 207.85  E-value: 1.12e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 163 TWRQLWRVLEFSDILLIIVDVRYATLMFPPSLYDYIINTLK-KHAIVVFNKVDLVEPHAVVAWRQYFRDRYPqlpVVLFA 241
Cdd:cd01857   1 VWRQLWRVIERSDVVVQIVDARNPLFFRCPDLEKYVKEVDPsKENVLLLNKADLVTEEQRKAWARYFKKEGI---VVLFF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 242 SFLPRSrkgsqrgpqahrrsmegvyniykecqryvqgevdlttweqkiredmrsdqldildeistavegelkisssidtt 321
Cdd:cd01857  78 SALNEA-------------------------------------------------------------------------- 83
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20129659 322 phehvkyhsgvlTIGCIGFPNVGKSSLINALKGRKVVSVSRTPGHTKHFQTIFLTPLVRLCDCPGLVFP 390
Cdd:cd01857  84 ------------TIGLVGYPNVGKSSLINALVGSKKVSVSSTPGKTKHFQTIFLEPGITLCDCPGLVFP 140
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
203-386 2.86e-22

A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein that functions as a regulator of cell growth and proliferation in stem cells and in several types of cancer cells, but is not expressed in the differentiated cells of most mammalian adult tissues. NS shuttles between the nucleolus and nucleoplasm bidirectionally at a rate that is fast and independent of cell type. Lowering GTP levels decreases the nucleolar retention of NS, and expression of NS is abruptly down-regulated during differentiation prior to terminal cell division. Found only in eukaryotes, NS consists of an N-terminal basic domain, a coiled-coil domain, a GTP-binding domain, an intermediate domain, and a C-terminal acidic domain. Experimental evidence indicates that NS uses its GTP-binding property as a molecular switch to control the transition between the nucleolus and nucleoplasm, and this process involves interaction between the basic, GTP-binding, and intermediate domains of the protein.


Pssm-ID: 206753 [Multi-domain]  Cd Length: 171  Bit Score: 93.79  E-value: 2.86e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 203 KKHAIVVFNKVDLVEPHAVVAWRQYFRDrypQLPVVLF-ASFLPRSRKGSQRGPQAhrrsmegvyniyKECQRYVQGEVD 281
Cdd:cd04178  30 NKKLVLVLNKIDLVPKENVEKWLKYLRN---EFPTVAFkASTQQQKKNLSRKSKKV------------KASDDLLSSSAC 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 282 LTTweqkiredmrsdqlDILDEISTAVEGELKISSSIdttphehvkyhsgvlTIGCIGFPNVGKSSLINALKGRKVVSVS 361
Cdd:cd04178  95 LGA--------------DALLKLLKNYARNKGIKTSI---------------TVGVVGYPNVGKSSVINSLKRSRACNVG 145
                       170       180
                ....*....|....*....|....*
gi 20129659 362 RTPGHTKHFQTIFLTPLVRLCDCPG 386
Cdd:cd04178 146 ATPGVTKSMQEVHLDKHVKLLDSPG 170
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
164-386 2.74e-19

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: 85.06  E-value: 2.74e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 164 WRQLWRVLEFSDILLIIVDVRYATLMFPPSLYDYIINtLKKHAIVVFNKVDLVEPHAVVAWRQYFRDRypQLPVVLFASf 243
Cdd:cd01859   2 KRLVRRIIKEADVVLEVVDARDPELTRSRKLERMALE-LGKKLIIVLNKADLVPREVLEKWKEVFESE--GLPVVYVSA- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 244 lpRSRKGSQrgpqahrrsmegvyniykecqryvqgevdlttweqKIREDMRSdqldildeistavegelkisSSIDTTPh 323
Cdd:cd01859  78 --RERLGTR-----------------------------------ILRRTIKE--------------------LAIDGKP- 99
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20129659 324 ehvkyhsgvLTIGCIGFPNVGKSSLINALKGRKVVSVSRT---PGHTKHFQTIFLTPLVRLCDCPG 386
Cdd:cd01859 100 ---------VIVGVVGYPKVGKSSIINALKGRHSASTSPIpgsPGYTKGIQLVRIDSKIYLIDTPG 156
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
204-474 4.92e-18

Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 84.39  E-value: 4.92e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 204 KHAIVVFNKVDLVEPHAVVAWRQYFRDRypQLPVVLFASflprsRKGSqrgpqahrrsmeGVYNIYKECQRYVQGEvdlt 283
Cdd:COG1161  51 KPRLLVLNKADLADPSVTKQWLKYFEKQ--GVDALAISA-----KKGK------------GIKELIEAIRELAPEK---- 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 284 tweQKIREDMRsdqldildeistavegelkisssidttphehvkyhsgVLTIGCigfPNVGKSSLINALKGRKVVSVSRT 363
Cdd:COG1161 108 ---GIKRRPIR-------------------------------------VMIVGI---PNVGKSTLINRLAGKKVAKTGNK 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 364 PGHTKHFQTIFLTPLVRLCDCPGLVFPS-STPKSLQVLLGSFPISQLAVPYRSL-KFLGEHL--NLPQLL--RLHLPEdy 437
Cdd:COG1161 145 PGVTKGQQWIKLDDGLELLDTPGILWPKfEDPEVGYKLAATGAIKDEVLDLEEVaLFLLGYLarRYPELLkeRYKLDE-- 222
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 20129659 438 DEWSAVAISDAWAYKRGFLTAKaARPDRYRAANHILR 474
Cdd:COG1161 223 LPRTKLELLEAIGRKRGCLLSG-GEVDLEKAAEILLT 258
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
175-387 1.34e-17

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


Pssm-ID: 206746 [Multi-domain]  Cd Length: 146  Bit Score: 79.74  E-value: 1.34e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 175 DILLIIVDVRyATLMFPPSLYDYIINTLKKHAIVVFNKVDLVEPHAVVAWRQYFRDRYPqlPVVLFASFLPrsrkgsqrg 254
Cdd:cd01849   1 DVVVEVVDAR-DPLSSRNPDIEVLINEKNKKLIMVLNKADLVPKEVLRKWVAELSELYG--TKTFFISATN--------- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 255 pqahrrsmegvyniykecqryvqgevdlttweqkiredmrsdqldildeistaVEGELKISSSIdtTPHEHVKYHSGVLT 334
Cdd:cd01849  69 -----------------------------------------------------GQGILKLKAEI--TKQKLKLKYKKGIR 93
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 20129659 335 IGCIGFPNVGKSSLINALKGRKVVSVSRTPGHTKHFQTIFLTPLVRLCDCPGL 387
Cdd:cd01849  94 VGVVGLPNVGKSSFINALLNKFKLKVGSIPGTTKLQQDVKLDKEIYLYDTPGI 146
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
165-474 2.26e-17

ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding proteins involved in ribosome biogenesis, including the essential YlqF protein of Bacillus subtilis, which is an essential protein. They are related to Era, EngA, and other GTPases of ribosome biogenesis, but are circularly permuted. This family is not universal, and is not present in Escherichia coli, and so is not as well studied as some other GTPases. This model is built for bacterial members. [Protein synthesis, Other]


Pssm-ID: 274669 [Multi-domain]  Cd Length: 276  Bit Score: 82.56  E-value: 2.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659   165 RQLWRVLEFSDILLIIVDVRYATLMFPPSLYDYIINtlKKHaIVVFNKVDLVEPHAVVAWRQYFRDrypQLPVVLFASfl 244
Cdd:TIGR03596  13 REIKENLKLVDVVIEVLDARIPLSSRNPMIDEIRGN--KPR-LIVLNKADLADPAVTKQWLKYFEE---KGIKALAVN-- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659   245 prSRKGSqrgpqahrrsmeGVYNIYKECQRyvqgevdlttweqkiredMRSDQLDILDEistavEGELKISssidttphe 324
Cdd:TIGR03596  85 --AKKGA------------GVKKIIKAAKK------------------LLKEKNEKLKA-----KGLKNRP--------- 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659   325 hvkyhsgvLTIGCIGFPNVGKSSLINALKGRKVVSVSRTPGHTKHFQTIFLTPLVRLCDCPGLVFPSSTPKSLQVLL--- 401
Cdd:TIGR03596 119 --------IRAMIVGIPNVGKSTLINRLAGKKVAKVGNRPGVTKGQQWIKLSDNLELLDTPGILWPKFEDQEVGLKLaat 190
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20129659   402 GSfpISQLAVPYRSL-KFLGEHL--NLPQLLRLHLPEDYDEWSAVAISDAWAYKRGFLTaKAARPDRYRAANHILR 474
Cdd:TIGR03596 191 GA--IKDEALDLEDVaLFLLEYLleHYPELLKERYKLDELPEDPVELLEAIAKKRGCLL-KGGELDLDRAAEILLN 263
NGP_1 cd01858
A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; ...
166-386 9.43e-17

A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; Autoantigen NGP-1 (Nucleolar G-protein gene 1) has been shown to localize in the nucleolus and nucleolar organizers in all cell types analyzed, which is indicative of a function in ribosomal assembly. NGP-1 and its homologs show 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 NKXD motif) are relocated to the N terminus.


Pssm-ID: 206751 [Multi-domain]  Cd Length: 157  Bit Score: 77.72  E-value: 9.43e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 166 QLWRVLEFSDILLIIVDVRYATLMFPPSLYDYIINTLK-KHAIVVFNKVDLVEPHAVVAWRQYFRDRYPQLpvvlfasfl 244
Cdd:cd01858   1 ELYKVIDSSDVIIQVLDARDPMGTRCKHVEKYLRKEKPhKHLIFVLNKCDLVPTWVTKRWVKVLSKEYPTL--------- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 245 prsrkgsqrgpqAHRRSMEGVYniykecqryvqGEVDLttweqkiredmrsdqLDILDEISTAVEGELKISssidttphe 324
Cdd:cd01858  72 ------------AFHASITNPF-----------GKGAL---------------INLLRQFAKLHSDKKQIS--------- 104
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20129659 325 hvkyhsgvltIGCIGFPNVGKSSLINALKGRKVVSVSRTPGHTKHFQTIFLTPLVRLCDCPG 386
Cdd:cd01858 105 ----------VGFIGYPNVGKSSVINTLRSKKVCKVAPIPGETKVWQYITLMKRIYLIDCPG 156
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
171-386 2.96e-16

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


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 76.80  E-value: 2.96e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 171 LEFSDILLIIVDVR--YATLmfPPSLYDYIINtlKKHaIVVFNKVDLVEPHAVVAWRQYFRDrypqlpvvlfasflprsr 248
Cdd:cd01856  17 LKLVDVVIEVRDARipLSSR--NPDLDKILGN--KPR-LIVLNKADLADPAKTKKWLKYFKS------------------ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 249 kgsqrgpqahrrsmEGVYNIYKECQRyvqgevdlttweqkiredmRSDQLDILDEIstavegeLKISSSIDTTPHEHVKY 328
Cdd:cd01856  74 --------------QGEPVLFVNAKN-------------------GKGVKKLLKKA-------KKLLKENEKLKAKGLLP 113
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20129659 329 HSgvLTIGCIGFPNVGKSSLINALKGRKVVSVSRTPGHTKHFQTIFLTPLVRLCDCPG 386
Cdd:cd01856 114 RP--LRAMVVGIPNVGKSTLINRLRGKKVAKVGNKPGVTRGQQWIRIGPNIELLDTPG 169
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
334-397 6.79e-16

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: 73.81  E-value: 6.79e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20129659   334 TIGCIGFPNVGKSSLINALKGRKVVsVSRTPGHTKHFQTIFLTPL---VRLCDCPGLVFPSSTPKSL 397
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAI-VSDYPGTTRDPNEGRLELKgkqIILVDTPGLIEGASEGEGL 66
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
328-390 2.34e-09

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: 56.70  E-value: 2.34e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20129659 328 YHSGVLTIgcIGFPNVGKSSLINALKGRKVVSVSRTPGHTKH----------FQTIFLtplvrlcDCPGLVFP 390
Cdd:cd04163   1 FKSGFVAI--IGRPNVGKSTLLNALVGQKISIVSPKPQTTRNrirgiytdddAQIIFV-------DTPGIHKP 64
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
338-386 2.37e-09

YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 56.75  E-value: 2.37e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 20129659 338 IGFPNVGKSSLINAL-KGRKVVSVSRTPGHTKHFQTIFLTPLVRLCDCPG 386
Cdd:cd01876   5 AGRSNVGKSSLINALtNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPG 54
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
338-388 2.31e-08

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: 53.61  E-value: 2.31e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20129659 338 IGFPNVGKSSLINALKGRKVVSVSRTPGHTKHFQTIFLTPL-----VRLCDCPGLV 388
Cdd:cd00882   3 VGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKELDkgkvkLVLVDTPGLD 58
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
338-387 2.96e-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: 53.40  E-value: 2.96e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20129659 338 IGFPNVGKSSLINALKGRKVVSVSRTPGHTKH-----FQTIFLTPLVrLCDCPGL 387
Cdd:cd00880   3 FGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDpvrkeWELLPLGPVV-LIDTPGL 56
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
342-386 1.13e-07

ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other]


Pssm-ID: 274670 [Multi-domain]  Cd Length: 179  Bit Score: 52.09  E-value: 1.13e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 20129659   342 NVGKSSLINALKGRK-VVSVSRTPGHTkhfQTI---FLTPLVRLCDCPG 386
Cdd:TIGR03598  28 NVGKSSLINALTNRKkLARTSKTPGRT---QLInffEVNDGFRLVDLPG 73
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
342-386 1.34e-07

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 439988 [Multi-domain]  Cd Length: 194  Bit Score: 52.00  E-value: 1.34e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 20129659 342 NVGKSSLINALKGRK-VVSVSRTPGHTkhfQTI--F-LTPLVRLCDCPG 386
Cdd:COG0218  33 NVGKSSLINALTNRKkLARTSKTPGKT---QLInfFlINDKFYLVDLPG 78
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
328-377 1.78e-07

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 53.07  E-value: 1.78e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129659 328 YHSGVLTIgcIGFPNVGKSSLINALKGRKVVSVSRTPG----------HTKHFQTIFL-TP 377
Cdd:COG1159   1 FRSGFVAI--VGRPNVGKSTLLNALVGQKVSIVSPKPQttrhrirgivTREDAQIVFVdTP 59
era PRK00089
GTPase Era; Reviewed
327-377 4.27e-07

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 51.97  E-value: 4.27e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20129659  327 KYHSGVLTIgcIGFPNVGKSSLINALKGRKVVSVSRTPG----------HTKHFQTIFL-TP 377
Cdd:PRK00089   2 GFKSGFVAI--VGRPNVGKSTLLNALVGQKISIVSPKPQttrhrirgivTEDDAQIIFVdTP 61
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
331-367 2.88e-06

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


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 47.81  E-value: 2.88e-06
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 20129659 331 GVLTIGCIGFPNVGKSSLINALKGRKVVSVSRTPGHT 367
Cdd:cd01895   1 DPIKIAIIGRPNVGKSSLLNALLGEERVIVSDIAGTT 37
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
322-367 1.79e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 47.35  E-value: 1.79e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 20129659  322 PHEHVKYHSGVLTIGCIGFPNVGKSSLINALKGRKVVSVSRTPGHT 367
Cdd:PRK00093 163 EEEEEDEEDEPIKIAIIGRPNVGKSSLINALLGEERVIVSDIAGTT 208
YeeP COG3596
Predicted GTPase [General function prediction only];
324-387 2.15e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 46.68  E-value: 2.15e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20129659 324 EHVKYHSGVLTIGCIGFPNVGKSSLINALKGRKVVSVSRTPGHTKHFQTIFLT----PLVRLCDCPGL 387
Cdd:COG3596  31 ERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLEsdglPGLVLLDTPGL 98
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
335-387 3.03e-05

GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other bacteria. It plays a role in ribosome biogenesis. Few bacteria lack this protein. [Protein synthesis, Other]


Pssm-ID: 129528 [Multi-domain]  Cd Length: 270  Bit Score: 45.84  E-value: 3.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 20129659   335 IGCIGFPNVGKSSLINALKGRKVVSVSRTPGHTKH-FQTIFLTPL--VRLCDCPGL 387
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHGQKISITSPKAQTTRNrISGIHTTGAsqIIFIDTPGF 58
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
338-387 4.77e-05

Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 44.56  E-value: 4.77e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129659 338 IGFPNVGKSSLINAL----KGRKVVS-------VSRTPGHTKHFQTIFLTPLVRLCDCPGL 387
Cdd:cd01855 131 VGATNVGKSTLINALlksnGGKVQAQalvqrltVSPIPGTTLGLIKIPLGEGKKLYDTPGI 191
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
335-372 5.56e-05

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: 43.90  E-value: 5.56e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 20129659   335 IGCIGFPNVGKSSLINALKGRKVVSVSRTPGHTKHFQT 372
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVT 41
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
168-242 7.58e-05

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: 43.39  E-value: 7.58e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20129659 168 WRVLEFSDILLIIVDVRyatlmFPPSLYDYIINTL---KKHAIVVFNKVDLVEPHAVVAWRQYFRDRY-PQLPVVLFAS 242
Cdd:cd00880  71 RQVADRADLVLLVVDSD-----LTPVEEEAKLGLLrerGKPVLLVLNKIDLVPESEEEELLRERKLELlPDLPVIAVSA 144
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
338-367 1.34e-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: 42.48  E-value: 1.34e-04
                        10        20        30
                ....*....|....*....|....*....|
gi 20129659 338 IGFPNVGKSSLINALKGRKVVSVSRTPGHT 367
Cdd:cd04164   9 AGKPNVGKSSLLNALAGRDRAIVSDIAGTT 38
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
161-242 2.44e-04

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: 42.06  E-value: 2.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659 161 LETWRQLWRVLEFSDILLIIVDV-RYATLMFPPSLYDYIINTLKKHAIVVFNKVDLVEPHAVVAW-RQYFRDRYPQLPVV 238
Cdd:cd00882  63 LGREELARLLLRGADLILLVVDStDRESEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELlRLEELAKILGVPVF 142

                ....
gi 20129659 239 LFAS 242
Cdd:cd00882 143 EVSA 146
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
335-352 3.09e-04

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: 41.64  E-value: 3.09e-04
                        10
                ....*....|....*...
gi 20129659 335 IGCIGFPNVGKSSLINAL 352
Cdd:cd01898   3 VGLVGLPNAGKSTLLSAI 20
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
336-388 4.48e-04

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: 41.23  E-value: 4.48e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20129659 336 GCIGFPNVGKSSLINALKGRKvVSVSRTPGHTK-----HFQTIFLTPlVRLCDCPGLV 388
Cdd:cd01881   1 GLVGLPNVGKSTLLSALTSAK-VEIASYPFTTLepnvgVFEFGDGVD-IQIIDLPGLL 56
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
333-386 5.17e-04

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 43.17  E-value: 5.17e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20129659  333 LTIGCIGFPNVGKSSLINALKG--RKV-----VSVSRTPGHtkhfqtiFLTP--LVRLCDCPG 386
Cdd:PRK09554   4 LTIGLIGNPNSGKTTLFNQLTGarQRVgnwagVTVERKEGQ-------FSTTdhQVTLVDLPG 59
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
168-238 6.05e-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: 40.91  E-value: 6.05e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20129659 168 WRVLEFSDILLIIVDVRYatlmfPPSLYD-YIINTLKKH---AIVVFNKVDLVEPHAVVAWR-QYFRDRYPQLPVV 238
Cdd:cd04163  77 WSALKDVDLVLFVVDASE-----WIGEGDeFILELLKKSktpVILVLNKIDLVKDKEDLLPLlEKLKELHPFAEIF 147
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
330-367 6.25e-04

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 42.32  E-value: 6.25e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 20129659 330 SGVLTIGCIGFPNVGKSSLINALKGRKVVSVSRTPGHT 367
Cdd:COG1160 173 DDPIKIAIVGRPNVGKSSLINALLGEERVIVSDIAGTT 210
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
332-368 6.65e-04

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 42.47  E-value: 6.65e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 20129659  332 VLTIGCIGFPNVGKSSLINALKGRKVVSVSRTPGHTK 368
Cdd:PRK09518 275 VGVVAIVGRPNVGKSTLVNRILGRREAVVEDTPGVTR 311
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
333-386 8.77e-04

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: 40.13  E-value: 8.77e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129659   333 LTIGCIGFPNVGKSSLINALKGRKV-------VSVSRTPGHTKHFQTifltpLVRLCDCPG 386
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTGANQhvgnwpgVTVEKKEGKFKYKGY-----EIEIVDLPG 56
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
330-357 1.29e-03

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 41.32  E-value: 1.29e-03
                        10        20
                ....*....|....*....|....*...
gi 20129659 330 SGVLTIGCIGFPNVGKSSLINALKGRKV 357
Cdd:COG1163  61 SGDATVVLVGFPSVGKSTLLNKLTNAKS 88
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
338-367 1.92e-03

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


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 40.81  E-value: 1.92e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 20129659 338 IGFPNVGKSSLINALKGRKVVSVSRTPGHT 367
Cdd:COG0486 219 VGRPNVGKSSLLNALLGEERAIVTDIAGTT 248
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
338-369 2.52e-03

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: 38.98  E-value: 2.52e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 20129659 338 IGFPNVGKSSLINALKGRKV-------VSVSRTPGHTKH 369
Cdd:cd01879   3 VGNPNVGKTTLFNALTGARQkvgnwpgVTVEKKEGEFKL 41
GTPase_YqeH TIGR03597
ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of ...
338-408 2.78e-03

ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of GTPases involved in ribosome biogenesis. Like YqlF, it shows a cyclical permutation relative to GTPases EngA (in which the GTPase domain is duplicated), Era, and others. Members of this protein family are found in a relatively small number of bacterial species, including Bacillus subtilis but not Escherichia coli. [Protein synthesis, Other]


Pssm-ID: 213834 [Multi-domain]  Cd Length: 360  Bit Score: 40.30  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659   338 IGFPNVGKSSLINAL-----KGRKVVSVSRTPGHTKHFQTIfltPLVR---LCDCPGLVFPSS-----TPKSLQVLLGSF 404
Cdd:TIGR03597 160 VGVTNVGKSSLINKLlkqnnGDKDVITTSPFPGTTLDLIEI---PLDDghsLYDTPGIINSHQmahylDKKDLKYITPKK 236

                  ....
gi 20129659   405 PISQ 408
Cdd:TIGR03597 237 EIKP 240
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
168-238 3.50e-03

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 39.59  E-value: 3.50e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129659 168 WRVLEFSDILLIIVDVRYatlmfPPSLYD-YIINTLKKH---AIVVFNKVDLVEPHAVVAWRQYFRDRYPQLPVV 238
Cdd:COG1159  77 WSALEDVDVILFVVDATE-----KIGEGDeFILELLKKLktpVILVINKIDLVKKEELLPLLAEYSELLDFAEIV 146
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
287-367 3.76e-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: 39.77  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129659   287 QKIREdMRSDQLDIL-----------DEISTAVEGEL-----KISSSIDT---TPHEHVKYHSGVLT-IgcIGFPNVGKS 346
Cdd:pfam12631  32 RKIEE-LREKLLELLalieaaidfpeDDIEELTEEELlerleELLAELEKllaTADRGRILREGIKVvI--VGKPNVGKS 108
                          90       100
                  ....*....|....*....|.
gi 20129659   347 SLINALKGRKVVSVSRTPGHT 367
Cdd:pfam12631 109 SLLNALLGEERAIVTDIPGTT 129
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
338-367 3.95e-03

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 39.71  E-value: 3.95e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 20129659  338 IGFPNVGKSSLINALKGRKVVSVSRTPGHT 367
Cdd:PRK05291 221 AGRPNVGKSSLLNALLGEERAIVTDIAGTT 250
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
333-352 4.47e-03

Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 39.62  E-value: 4.47e-03
                        10        20
                ....*....|....*....|
gi 20129659 333 LTIGCIGFPNVGKSSLINAL 352
Cdd:COG0012   1 LKCGIVGLPNVGKSTLFNAL 20
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
338-367 5.67e-03

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: 37.80  E-value: 5.67e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 20129659 338 IGFPNVGKSSLINALKGRKVVSVSRTPGHT 367
Cdd:cd01894   3 VGRPNVGKSTLFNRLTGRRDAIVSDTPGVT 32
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
333-386 6.45e-03

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 39.33  E-value: 6.45e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129659 333 LTIGCIGFPNVGKSSLINALKGRKV-------VSVSRTPGHTKHFQTIfltplVRLCDCPG 386
Cdd:COG0370   4 ITIALVGNPNVGKTTLFNALTGSRQkvgnwpgVTVEKKEGKFKLKGKE-----IELVDLPG 59
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
334-354 7.58e-03

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: 38.30  E-value: 7.58e-03
                        10        20
                ....*....|....*....|.
gi 20129659 334 TIGCIGFPNVGKSSLINALKG 354
Cdd:cd01896   2 RVALVGFPSVGKSTLLSKLTN 22
 
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