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Conserved domains on  [gi|268325198|emb|CBH38786|]
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conserved hypothetical protein, GTPase family [uncultured archaeon]

Protein Classification

OBG GTPase family GTP-binding protein( domain architecture ID 11439361)

OBG GTPase family GTP-binding protein may function as a GTPase, such as Saccharomyces cerevisiae RBG1, which is involved in ribosomal function, and developmentally regulated GTP-binding proteins, which may regulate fundamental cellular processes, perhaps by binding to RNA

CATH:  3.40.50.300|3.10.20.30
EC:  3.6.5.-
Gene Ontology:  GO:0005525|GO:0003924
PubMed:  15827604|11916378
SCOP:  4004038|4001813|4007676

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
1-365 0e+00

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


:

Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 599.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198   1 MTIEEEIKNVEDEIWKTPYNKATSHHVGRLKAKLARLKDDLQKRAtAKSSGKGKGYFVKKSGHATIVLVGFPSVGKSTLL 80
Cdd:COG1163    2 MTIEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRK-KKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  81 NRLTGTSAEVAAYEFTTLEVIPGTLIYKGAQLQFLDVPGLIQGAAAGRGHGKEVISVMRNADLILILVDVFQQQQYDILL 160
Cdd:COG1163   81 NKLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELEQYDVLK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 161 KELYDAGIRINANPPLVAIRKASRGGIIINRTVDLDYDNKVIRAVLAEYRIHNGEVLIRERITIDELIDAVLGNRKYVRA 240
Cdd:COG1163  161 EELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLDLDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRVYKPA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 241 LTVINKTDLADSETLLTCMARFP---DAVPISAAVGINMDVLKDKIYNELGFMRIYMKPPGASPDMDNPLVIRRDSTITD 317
Cdd:COG1163  241 IVVVNKIDLADEEYVEELKSKLPdgvPVIFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKGSTVGD 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 268325198 318 VCSTIHRDFVDRFRYARIWGKSVKYGGQRVGLSHVLEEGDVLSFVIRK 365
Cdd:COG1163  321 VCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIKK 368
 
Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
1-365 0e+00

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 599.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198   1 MTIEEEIKNVEDEIWKTPYNKATSHHVGRLKAKLARLKDDLQKRAtAKSSGKGKGYFVKKSGHATIVLVGFPSVGKSTLL 80
Cdd:COG1163    2 MTIEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRK-KKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  81 NRLTGTSAEVAAYEFTTLEVIPGTLIYKGAQLQFLDVPGLIQGAAAGRGHGKEVISVMRNADLILILVDVFQQQQYDILL 160
Cdd:COG1163   81 NKLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELEQYDVLK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 161 KELYDAGIRINANPPLVAIRKASRGGIIINRTVDLDYDNKVIRAVLAEYRIHNGEVLIRERITIDELIDAVLGNRKYVRA 240
Cdd:COG1163  161 EELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLDLDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRVYKPA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 241 LTVINKTDLADSETLLTCMARFP---DAVPISAAVGINMDVLKDKIYNELGFMRIYMKPPGASPDMDNPLVIRRDSTITD 317
Cdd:COG1163  241 IVVVNKIDLADEEYVEELKSKLPdgvPVIFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKGSTVGD 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 268325198 318 VCSTIHRDFVDRFRYARIWGKSVKYGGQRVGLSHVLEEGDVLSFVIRK 365
Cdd:COG1163  321 VCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIKK 368
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 64-295 3.98e-114

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: 331.43  E-value: 3.98e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  64 ATIVLVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLEVIPGTLIYKGAQLQFLDVPGLIQGAAAGRGHGKEVISVMRNADL 143
Cdd:cd01896    1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 144 ILILVDVFQ-QQQYDILLKELYDAGIRINANPPLVAIRKASRGGIIINRTVDL-DYDNKVIRAVLAEYRIHNGEVLIRER 221
Cdd:cd01896   81 ILIVLDATKpEGQREILERELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLtKLDEKTVKAILREYKIHNADVLIRED 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 268325198 222 ITIDELIDAVLGNRKYVRALTVINKTDLADSEtLLTCMARFPDAVPISAAVGINMDVLKDKIYNELGFMRIYMK 295
Cdd:cd01896  161 ITVDDLIDVIEGNRVYIPCLYVYNKIDLISIE-ELDRLARIPNSVVISAEKDLNLDELLERIWDYLGLIRIYTK 233
MMR_HSR1_Xtn pfam16897
C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of ...
 185-289 1.70e-44

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: 148.73  E-value: 1.70e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  185 GGIIINRTVDLDY-DNKVIRAVLAEYRIHNGEVLIRERITIDELIDAVLGNRKYVRALTVINKTDLADSETLLTcMARFP 263
Cdd:pfam16897   1 GGINITSTVPLTKlDEETIKAILREYKIHNADVLIREDVTVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDR-LAREP 79

                          90       100
                  ....*....|....*....|....*.
gi 268325198  264 DAVPISAAVGINMDVLKDKIYNELGF 289
Cdd:pfam16897  80 DSVPISAEKGLNLDELKERIWEYLGL 105
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
 68-287 1.10e-17

Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome GTP-binding protein that associates with ribosomal subunits and appears to play a role in ribosomal RNA maturation. This GTPase, related to the nucleolar protein Obg, is designated CgtA in bacteria. Mutations in this gene are pleiotropic, but it appears that effects on cellular functions such as chromosome partition may be secondary to the effect on ribosome structure. Recent work done in Vibrio cholerae shows an essential role in the stringent response, in which RelA-dependent ability to synthesize the alarmone ppGpp is required for deletion of this GTPase to be lethal. [Protein synthesis, Other]


Pssm-ID: 274271 [Multi-domain]  Cd Length: 328  Bit Score: 82.85  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198   68 LVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLEVIPGTLIYKGAQ-LQFLDVPGLIQGAAAGRGHGKEVISVMRNADLILI 146
Cdd:TIGR02729 162 LVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRsFVIADIPGLIEGASEGAGLGHRFLKHIERTRVLLH 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  147 LVDVFQQQQYDILlkelydagirinanpplvairkasrggiiinrtvdLDYdnKVIRAVLAEYrihNGEVLIRERItide 226
Cdd:TIGR02729 242 LIDISPEDGSDPV-----------------------------------EDY--EIIRNELKKY---SPELAEKPRI---- 277

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 268325198  227 lidavlgnrkyvralTVINKTDLADSETLLTCMARFPDA-----VPISAAVGINMDVLKDKIYNEL 287
Cdd:TIGR02729 278 ---------------VVLNKIDLLDEEELEELLKELKKElgkpvFPISALTGEGLDELLDALAELL 328
obgE PRK12299
GTPase CgtA; Reviewed
 68-291 1.39e-16

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 79.73  E-value: 1.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  68 LVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLEVIPGTLIYKGAQ-LQFLDVPGLIQGAAAGRG-------HgkevisVMR 139
Cdd:PRK12299 163 LVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKsFVIADIPGLIEGASEGAGlghrflkH------IER 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 140 NAdLILILVDVFQQ---QQYDILLKELydagirinanpplvairkasrggiiinrtvdldydnkviravlaeyRIHNGEV 216
Cdd:PRK12299 237 TR-LLLHLVDIEAVdpvEDYKTIRNEL----------------------------------------------EKYSPEL 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 217 LIRERItidelidavlgnrkyvralTVINKTDLADSETLLTCMARFPDA------VPISAAVGINMDVLKDKIYNELGFM 290
Cdd:PRK12299 270 ADKPRI-------------------LVLNKIDLLDEEEEREKRAALELAalggpvFLISAVTGEGLDELLRALWELLEEA 330


                 .
gi 268325198 291 R 291
Cdd:PRK12299 331 R 331
 
Name Accession Description Interval E-value
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
1-365 0e+00

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 599.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198   1 MTIEEEIKNVEDEIWKTPYNKATSHHVGRLKAKLARLKDDLQKRAtAKSSGKGKGYFVKKSGHATIVLVGFPSVGKSTLL 80
Cdd:COG1163    2 MTIEEKIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRK-KKSGGGGEGFAVKKSGDATVVLVGFPSVGKSTLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  81 NRLTGTSAEVAAYEFTTLEVIPGTLIYKGAQLQFLDVPGLIQGAAAGRGHGKEVISVMRNADLILILVDVFQQQQYDILL 160
Cdd:COG1163   81 NKLTNAKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFELEQYDVLK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 161 KELYDAGIRINANPPLVAIRKASRGGIIINRTVDLDYDNKVIRAVLAEYRIHNGEVLIRERITIDELIDAVLGNRKYVRA 240
Cdd:COG1163  161 EELYDAGIRLNKPPPDVTIEKKGKGGIRVNSTGKLDLDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRVYKPA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 241 LTVINKTDLADSETLLTCMARFP---DAVPISAAVGINMDVLKDKIYNELGFMRIYMKPPGASPDMDNPLVIRRDSTITD 317
Cdd:COG1163  241 IVVVNKIDLADEEYVEELKSKLPdgvPVIFISAEKGIGLEELKEEIFEELGLIRVYLKPPGGKADMEEPLILRKGSTVGD 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 268325198 318 VCSTIHRDFVDRFRYARIWGKSVKYGGQRVGLSHVLEEGDVLSFVIRK 365
Cdd:COG1163  321 VCEKIHRDFVERFRYARVWGKSAKHPGQRVGLDHVLEDGDIVEIIIKK 368
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 64-295 3.98e-114

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: 331.43  E-value: 3.98e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  64 ATIVLVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLEVIPGTLIYKGAQLQFLDVPGLIQGAAAGRGHGKEVISVMRNADL 143
Cdd:cd01896    1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 144 ILILVDVFQ-QQQYDILLKELYDAGIRINANPPLVAIRKASRGGIIINRTVDL-DYDNKVIRAVLAEYRIHNGEVLIRER 221
Cdd:cd01896   81 ILIVLDATKpEGQREILERELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLtKLDEKTVKAILREYKIHNADVLIRED 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 268325198 222 ITIDELIDAVLGNRKYVRALTVINKTDLADSEtLLTCMARFPDAVPISAAVGINMDVLKDKIYNELGFMRIYMK 295
Cdd:cd01896  161 ITVDDLIDVIEGNRVYIPCLYVYNKIDLISIE-ELDRLARIPNSVVISAEKDLNLDELLERIWDYLGLIRIYTK 233
MMR_HSR1_Xtn pfam16897
C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of ...
 185-289 1.70e-44

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: 148.73  E-value: 1.70e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  185 GGIIINRTVDLDY-DNKVIRAVLAEYRIHNGEVLIRERITIDELIDAVLGNRKYVRALTVINKTDLADSETLLTcMARFP 263
Cdd:pfam16897   1 GGINITSTVPLTKlDEETIKAILREYKIHNADVLIREDVTVDDLIDVIEGNRVYIPCLYVYNKIDLISIEELDR-LAREP 79

                          90       100
                  ....*....|....*....|....*.
gi 268325198  264 DAVPISAAVGINMDVLKDKIYNELGF 289
Cdd:pfam16897  80 DSVPISAEKGLNLDELKERIWEYLGL 105
TGS_DRG cd01666
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein ...
 287-363 3.80e-37

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: 128.51  E-value: 3.80e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 268325198 287 LGFMRIYMKPPGASPDMDNPLVIRRDSTITDVCSTIHRDFVDRFRYARIWGKSVKYGGQRVGLSHVLEEGDVLSFVI 363
Cdd:cd01666    1 LGIIRVYTKPPGKKPDFDEPFILRRGSTVEDVAEKIHKDLAENFKYARVWGKSVKFDGQRVGLDHVLEDGDIVEIHK 77
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 65-181 4.22e-29

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: 108.86  E-value: 4.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198   65 TIVLVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLEVIPGTLIYKGAQLQFLDVPGLIQGAAAGRGHGKEVISVmRNADLI 144
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFLAI-IEADLI 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 268325198  145 LILVDVfqQQQYDILLKELYDAGIRINAnPPLVAIRK 181
Cdd:pfam01926  80 LFVVDS--EEGITPLDEELLELLRENKK-PIILVLNK 113
TGS_DRG2 cd17231
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 2 ...
 286-362 8.37e-28

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: 104.00  E-value: 8.37e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 268325198 286 ELGFMRIYMKPPGASPDMDNPLVIRRDSTITDVCSTIHRDFVDRFRYARIWGKSVKYGGQRVGLSHVLEEGDVLSFV 362
Cdd:cd17231    1 YLALIRVYTKKRGERPDFGDAIILRRGATVEHVCHRIHRTLASQFKYALVWGTSTKYSPQRVGLTHVMEDEDVIQIV 77
TGS_DRG1 cd17230
TGS (ThrRS, GTPase and SpoT) domain found in developmentally regulated GTP binding protein 1 ...
 287-362 2.93e-25

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: 97.34  E-value: 2.93e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 268325198 287 LGFMRIYMKPPGASPDMDNPLVIRRD-STITDVCSTIHRDFVDRFRYARIWGKSVKYGGQRVGLSHVLEEGDVLSFV 362
Cdd:cd17230    2 LNLVRIYTKPKGQLPDYEEPVVLRSGkSTVEDFCNKIHKSLIKEFKYALVWGSSVKHNPQRVGKDHVLEDEDVVQIV 78
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 67-287 2.66e-24

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: 97.46  E-value: 2.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  67 VLVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLEVIPGTLIYK-GAQLQFLDVPGLIQGAAAGRGHGKEVISVMRNADLIL 145
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGdGVDIQIIDLPGLLDGASEGRGLGEQILAHLYRSDLIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 146 ILVDVFQQQQYDILlkelydagirinanpplvairkasrggiiinrtvdldydnkviravlaeyrihngevliRERITID 225
Cdd:cd01881   81 HVIDASEDCVGDPL-----------------------------------------------------------EDQKTLN 101

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 268325198 226 ELIDAVLGNRKYVRALTVINKTDLADSETLLTC----MARFPDAVPISAAVGINMDVLKDKIYNEL 287
Cdd:cd01881  102 EEVSGSFLFLKNKPEMIVANKIDMASENNLKRLkldkLKRGIPVVPTSALTRLGLDRVIRTIRKLL 167
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 68-287 1.60e-20

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: 87.48  E-value: 1.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  68 LVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLevIP--GTLIYK-GAQLQFLDVPGLIQGAAAGRGHGkevISVMR---NA 141
Cdd:cd01898    5 LVGLPNAGKSTLLSAISNAKPKIADYPFTTL--VPnlGVVRVDdGRSFVIADIPGLIEGASEGKGLG---HRFLRhieRT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 142 DLILILVDVFQQ----QQYDILLKELydagirinanpplvairkasrggiiinrtvdldydnkviravlaeyrihngevl 217
Cdd:cd01898   80 RVLLHVIDLSGEddpvEDYETIRNEL------------------------------------------------------ 105

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 268325198 218 ireritidELIDAVLGNRKYVralTVINKTDLADSETLLTCMARFPDA------VPISAAVGINMDVLKDKIYNEL 287
Cdd:cd01898  106 --------EAYNPGLAEKPRI---VVLNKIDLLDAEERFEKLKELLKElkgkkvFPISALTGEGLDELLKKLAKLL 170
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
 68-287 6.52e-18

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


Pssm-ID: 440302 [Multi-domain]  Cd Length: 343  Bit Score: 83.49  E-value: 6.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  68 LVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLEVIPGTLIYKGAQlQFL--DVPGLIQGAAAGRG-------HgkevisVM 138
Cdd:COG0536  162 LVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGR-SFViaDIPGLIEGASEGAGlghrflrH------IE 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 139 RNAdLILILVDVFQQ------QQYDILLKELydagirinanpplvairKAsrggiiinrtvdldYDNKviravLAEyrih 212
Cdd:COG0536  235 RTR-VLLHVVDAAPLdgrdpvEDYEIIRNEL-----------------EA--------------YSPE-----LAE---- 273

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 268325198 213 ngevliRERItidelidavlgnrkyvralTVINKTDLADSETLLTCMARFPDA----VPISAAVGINMDVLKDKIYNEL 287
Cdd:COG0536  274 ------KPRI-------------------VVLNKIDLLDAEELEELKAELEKLggpvFPISAVTGEGLDELLYALAELL 327
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
 68-287 1.10e-17

Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome GTP-binding protein that associates with ribosomal subunits and appears to play a role in ribosomal RNA maturation. This GTPase, related to the nucleolar protein Obg, is designated CgtA in bacteria. Mutations in this gene are pleiotropic, but it appears that effects on cellular functions such as chromosome partition may be secondary to the effect on ribosome structure. Recent work done in Vibrio cholerae shows an essential role in the stringent response, in which RelA-dependent ability to synthesize the alarmone ppGpp is required for deletion of this GTPase to be lethal. [Protein synthesis, Other]


Pssm-ID: 274271 [Multi-domain]  Cd Length: 328  Bit Score: 82.85  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198   68 LVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLEVIPGTLIYKGAQ-LQFLDVPGLIQGAAAGRGHGKEVISVMRNADLILI 146
Cdd:TIGR02729 162 LVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRsFVIADIPGLIEGASEGAGLGHRFLKHIERTRVLLH 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  147 LVDVFQQQQYDILlkelydagirinanpplvairkasrggiiinrtvdLDYdnKVIRAVLAEYrihNGEVLIRERItide 226
Cdd:TIGR02729 242 LIDISPEDGSDPV-----------------------------------EDY--EIIRNELKKY---SPELAEKPRI---- 277

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 268325198  227 lidavlgnrkyvralTVINKTDLADSETLLTCMARFPDA-----VPISAAVGINMDVLKDKIYNEL 287
Cdd:TIGR02729 278 ---------------VVLNKIDLLDEEELEELLKELKKElgkpvFPISALTGEGLDELLDALAELL 328
obgE PRK12299
GTPase CgtA; Reviewed
 68-291 1.39e-16

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 79.73  E-value: 1.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  68 LVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLEVIPGTLIYKGAQ-LQFLDVPGLIQGAAAGRG-------HgkevisVMR 139
Cdd:PRK12299 163 LVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKsFVIADIPGLIEGASEGAGlghrflkH------IER 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 140 NAdLILILVDVFQQ---QQYDILLKELydagirinanpplvairkasrggiiinrtvdldydnkviravlaeyRIHNGEV 216
Cdd:PRK12299 237 TR-LLLHLVDIEAVdpvEDYKTIRNEL----------------------------------------------EKYSPEL 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 217 LIRERItidelidavlgnrkyvralTVINKTDLADSETLLTCMARFPDA------VPISAAVGINMDVLKDKIYNELGFM 290
Cdd:PRK12299 270 ADKPRI-------------------LVLNKIDLLDEEEEREKRAALELAalggpvFLISAVTGEGLDELLRALWELLEEA 330


                 .
gi 268325198 291 R 291
Cdd:PRK12299 331 R 331
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 67-170 1.10e-15

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: 73.82  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  67 VLVGFPSVGKSTLLNRLTG-TSAEVAAYEFTTLEVIPGTL-IYKGAQLQFLDVPGLIQGAAAGRGHGKEVISVMRNADLI 144
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGqNVGIVSPIPGTTRDPVRKEWeLLPLGPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80

                         90       100
                 ....*....|....*....|....*..
gi 268325198 145 LILVDV-FQQQQYDILLKELYDAGIRI 170
Cdd:cd00880   81 LLVVDSdLTPVEEEAKLGLLRERGKPV 107
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 66-175 3.20e-15

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: 72.40  E-value: 3.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198   66 IVLVGFPSVGKSTLLNRLTGTS-AEVAAYEFTTLEVIPGTLIYKG--AQLQFLDVPGLIQGAAAGRGHGKEVISVMRNAD 142
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKgSITEYYPGTTRNYVTTVIEEDGktYKFNLLDTAGQEDYDAIRRLYYPQVERSLRVFD 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 268325198  143 LILILVDVFQ--QQQYDILLKEL-YDAGIRINANPP 175
Cdd:TIGR00231  84 IVILVLDVEEilEKQTKEIIHHAdSGVPIILVGNKI 119
obgE PRK12297
GTPase CgtA; Reviewed
 68-287 3.59e-15

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 76.29  E-value: 3.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  68 LVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLEVIPGTLIYKGAQlQFL--DVPGLIQGAAAGRGHGKEV---ISVMRnad 142
Cdd:PRK12297 163 LVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGR-SFVmaDIPGLIEGASEGVGLGHQFlrhIERTR--- 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 143 LILILVDVfqqqqydillkelydAGIRiNANPplvairkasrggiiINrtvdlDYdnKVIRAVLAEYrihngevlireri 222
Cdd:PRK12297 239 VIVHVIDM---------------SGSE-GRDP--------------IE-----DY--EKINKELKLY------------- 268

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 223 tideliDAVLGNRKyvrALTVINKTDLADSETLLtcmARF-----PDAVPISAAVGINMDVLKDKIYNEL 287
Cdd:PRK12297 269 ------NPRLLERP---QIVVANKMDLPEAEENL---EEFkeklgPKVFPISALTGQGLDELLYAVAELL 326
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
65-237 1.17e-14

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 74.10  E-value: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  65 TIVLVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLEVIPGTLIYKGAQLQFLDVPGL----------IQgaaagrghgKEV 134
Cdd:COG1084  162 TIVVAGYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGRYQVIDTPGLldrplserneIE---------RQA 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 135 ISVMRN-ADLILILVDVFQQQQYDI-----LLKELYDagiRINAnPPLVAIRKasrggiiinrtVDLDYDNKVIRAVLAE 208
Cdd:COG1084  233 ILALKHlADVILFLFDPSETCGYSLeeqlnLLEEIRS---LFDV-PVIVVINK-----------IDLSDEEELKEAEEEA 297

                        170       180
                 ....*....|....*....|....*....
gi 268325198 209 YRihngEVLIRERITIDELIDAVLGNRKY 237
Cdd:COG1084  298 DI----KISALTGEGVDELLDELIEALEE 322
TGS pfam02824
TGS domain; The TGS domain is named after ThrRS, GTPase, and SpoT. Interestingly, TGS domain ...
 290-362 2.45e-14

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


Pssm-ID: 427005 [Multi-domain]  Cd Length: 60  Bit Score: 66.80  E-value: 2.45e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 268325198  290 MRIYMkPPGASPDmdnplvIRRDSTITDVCSTIHRDFVDRFRYARIWgksvkygGQRVGLSHVLEEGDVLSFV 362
Cdd:pfam02824   1 IRVYT-PDGKVPD------LPRGATPEDFAYAIHTSLAKKFIYAKVN-------GQLVGLDHPLEDGDVVEIV 59
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 65-120 2.81e-14

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


Pssm-ID: 206684 [Multi-domain]  Cd Length: 167  Bit Score: 69.90  E-value: 2.81e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 268325198  65 TIVLVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLEVIPGTLIYKGAQLQFLDVPGL 120
Cdd:cd01897    2 TLVIAGYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLRWQVIDTPGI 57
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 29-287 4.54e-13

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 69.73  E-value: 4.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  29 RLKAKLARLKDDLQK----RATAKSSGKgkgyfvkKSGHATIVLVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLE----- 99
Cdd:COG2262  168 LIRDRIARLKRELEKvrkqRELQRKRRK-------RSGIPTVALVGYTNAGKSTLFNRLTGADVLAEDKLFATLDpttrr 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 100 -VIPGtliykgaQLQFL---------DVP-GLIqgaAAGRGHGKEVisvmRNADLILILVDVfqqqqydillkelydagi 168
Cdd:COG2262  241 lELPD-------GRPVLltdtvgfirKLPhQLV---EAFRSTLEEV----READLLLHVVDA------------------ 288

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 169 rinANPplvairkasrggiiinrtvdlDYDNKvIRAVLaeyrihngEVLirERITIDElidavlgnrkyVRALTVINKTD 248
Cdd:COG2262  289 ---SDP---------------------DFEEQ-IETVN--------EVL--EELGADD-----------KPIILVFNKID 322

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 268325198 249 LADSETLLTCMARFPDAVPISAAVGINMDVLKDKIYNEL 287
Cdd:COG2262  323 LLDDEELERLRAGYPDAVFISAKTGEGIDELLEAIEERL 361
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
 66-150 1.85e-12

Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They are characterized by a distinct glycine-rich motif immediately following the Walker B motif. The Ygr210 and YyaF/YchF subfamilies appear to form one major branch of the Obg-like family. Among eukaryotes, the Ygr210 subfamily is represented only in fungi. These fungal proteins form a tight cluster with their archaeal orthologs, which suggests the possibility of horizontal transfer from archaea to fungi.


Pssm-ID: 206686 [Multi-domain]  Cd Length: 318  Bit Score: 67.25  E-value: 1.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  66 IVLVGFPSVGKSTLLNRLTGTSAEVAAYEFTT------------------LEVIPGTLIYKGAQ------LQFLDVPGLI 121
Cdd:cd01899    1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTidpnvgvgyvrvecpckeLGVSCNPRYGKCIDgkryvpVELIDVAGLV 80

                         90       100
                 ....*....|....*....|....*....
gi 268325198 122 QGAAAGRGHGKEVISVMRNADLILILVDV 150
Cdd:cd01899   81 PGAHEGKGLGNQFLDDLRDADVLIHVVDA 109
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 67-232 1.97e-12

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: 64.40  E-value: 1.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  67 VLVGFPSVGKSTLLNRLTG-TSAEVAAYEFTTLE--VIPGTLIYKGAQLQFLDVPGLIQGAAAGRGHgkEVISVMRNADL 143
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGgEVGEVSDVPGTTRDpdVYVKELDKGKVKLVLVDTPGLDEFGGLGREE--LARLLLRGADL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 144 ILILVDVfQQQQYDILLKELYDAGIRINANPPLVAIRKasrggiiinrtVDLDYDNKVIRAVLAEYRIHNGEVLI----- 218
Cdd:cd00882   79 ILLVVDS-TDRESEEDAKLLILRRLRKEGIPIILVGNK-----------IDLLEEREVEELLRLEELAKILGVPVfevsa 146

                        170
                 ....*....|....
gi 268325198 219 RERITIDELIDAVL 232
Cdd:cd00882  147 KTGEGVDELFEKLI 160
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 29-287 1.30e-11

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: 63.25  E-value: 1.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  29 RLKAKLARLKDDLQK----RATAKSSGKgkgyfvkKSGHATIVLVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLE----- 99
Cdd:cd01878   10 LIRERIAKLRKELEKvkkqRELQRARRK-------RSGVPTVALVGYTNAGKSTLFNALTGADVLAEDQLFATLDpttrr 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 100 -VIPGtliykGAQLQFLDVPGLIQG-----AAAGRGHGKEVisvmRNADLILILVDVfqqqqydillkelydagirinAN 173
Cdd:cd01878   83 iKLPG-----GREVLLTDTVGFIRDlphqlVEAFRSTLEEV----AEADLLLHVVDA---------------------SD 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 174 PPLVAIRKASrggiiinrtvdldydnkviRAVLAEyrihngevlirerITIDElidavlgnrkyVRALTVINKTDLADSE 253
Cdd:cd01878  133 PDREEQIETV-------------------EEVLKE-------------LGADD-----------IPIILVLNKIDLLDDE 169

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 268325198 254 TLLTCM-ARFPDAVPISAAVGINMDVLKDKIYNEL 287
Cdd:cd01878  170 ELEERLrAGRPDAVFISAKTGEGLDLLKEAIEELL 204
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 59-287 1.64e-11

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: 62.09  E-value: 1.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  59 KKSGHATIVlvGFPSVGKSTLLNRLTG-----TSAEVAayefTTLEVIPGTLIYKGAQLQFLDVPGLIQG-AAAGRGHGK 132
Cdd:cd04163    1 FKSGFVAII--GRPNVGKSTLLNALVGqkisiVSPKPQ----TTRNRIRGIYTDDDAQIIFVDTPGIHKPkKKLGERMVK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 133 EVISVMRNADLILILVDVFqqqqydillkelydagirinanpplvairkasrggiiinrtvdldydnkviravlaeyrih 212
Cdd:cd04163   75 AAWSALKDVDLVLFVVDAS------------------------------------------------------------- 93

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 213 ngevliRERITIDELIDAVLGNRKyVRALTVINKTDLA-DSETLL------TCMARFPDAVPISAAVGINMDVLKDKIYN 285
Cdd:cd04163   94 ------EWIGEGDEFILELLKKSK-TPVILVLNKIDLVkDKEDLLplleklKELHPFAEIFPISALKGENVDELLEYIVE 166


                 ..
gi 268325198 286 EL 287
Cdd:cd04163  167 YL 168
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
60-287 4.36e-11

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 63.08  E-value: 4.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  60 KSGHATIVlvGFPSVGKSTLLNRLTG-----TSAEVAayefTTLEVIPGTLIYKGAQLQFLDVPGLIQGAAA-GRGHGKE 133
Cdd:COG1159    2 RSGFVAIV--GRPNVGKSTLLNALVGqkvsiVSPKPQ----TTRHRIRGIVTREDAQIVFVDTPGIHKPKRKlGRRMNKA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 134 VISVMRNADLILILVDvfqqqqydillkelydagirinanpplvAIRKASRGgiiinrtvdldydnkviravlaeyrihn 213
Cdd:COG1159   76 AWSALEDVDVILFVVD----------------------------ATEKIGEG---------------------------- 99

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 214 gevlireritiDELIDAVLGNRKyVRALTVINKTDLADSETLLTCMAR------FPDAVPISAAVGINMDVLKDKIYNEL 287
Cdd:COG1159  100 -----------DEFILELLKKLK-TPVILVINKIDLVKKEELLPLLAEyselldFAEIVPISALKGDNVDELLDEIAKLL 167
obgE PRK12296
GTPase CgtA; Reviewed
 64-133 1.74e-10

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 62.19  E-value: 1.74e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 268325198  64 ATIVLVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLevIP--GTLIYKGAQLQFLDVPGLIQGAAAGRGHGKE 133
Cdd:PRK12296 160 ADVGLVGFPSAGKSSLISALSAAKPKIADYPFTTL--VPnlGVVQAGDTRFTVADVPGLIPGASEGKGLGLD 229
era PRK00089
GTPase Era; Reviewed
 60-287 2.17e-10

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 60.83  E-value: 2.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  60 KSGHATIVlvGFPSVGKSTLLNRLTG-----TSAEVAayefTTLEVIPGTLIYKGAQLQFLDVPGLIQGAAA-GRGHGKE 133
Cdd:PRK00089   4 KSGFVAIV--GRPNVGKSTLLNALVGqkisiVSPKPQ----TTRHRIRGIVTEDDAQIIFVDTPGIHKPKRAlNRAMNKA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 134 VISVMRNADLILILVDVFQQqqydillkelydagirinanpplvairkasrggiiinrtvdldydnkviravlaeyrIHN 213
Cdd:PRK00089  78 AWSSLKDVDLVLFVVDADEK---------------------------------------------------------IGP 100

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 214 GEVLIRERItidelidavlgNRKYVRALTVINKTDLA-DSETLLTCMAR------FPDAVPISAAVGINMDVLKDKIYNE 286
Cdd:PRK00089 101 GDEFILEKL-----------KKVKTPVILVLNKIDLVkDKEELLPLLEElselmdFAEIVPISALKGDNVDELLDVIAKY 169


                 .
gi 268325198 287 L 287
Cdd:PRK00089 170 L 170
PRK09602 PRK09602
translation-associated GTPase; Reviewed
 65-150 2.87e-10

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 60.98  E-value: 2.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  65 TIVLVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLE---------------------------------VIPGTLIykgaq 111
Cdd:PRK09602   3 TIGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDpnvgvayvrvecpckelgvkcnprngkcidgtrFIPVELI----- 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 268325198 112 lqflDVPGLIQGAAAGRGHGKEVISVMRNADLILILVDV 150
Cdd:PRK09602  78 ----DVAGLVPGAHEGRGLGNQFLDDLRQADALIHVVDA 112
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 65-119 3.82e-10

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


Pssm-ID: 460552 [Multi-domain]  Cd Length: 156  Bit Score: 57.85  E-value: 3.82e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 268325198   65 TIVLVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLEVIPGTLIYKGAQLQFLDVPG 119
Cdd:pfam02421   2 TIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFKYKGYEIEIVDLPG 56
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 68-119 3.88e-10

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: 57.85  E-value: 3.88e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 268325198  68 LVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLEVIPGTLIYKGAQLQFLDVPG 119
Cdd:cd01879    2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPG 53
obgE PRK12298
GTPase CgtA; Reviewed
 68-164 1.69e-09

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 58.73  E-value: 1.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  68 LVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLEVIPGTLIYkGAQLQFL--DVPGLIQGAAAGRGHGKEVIS-VMRNAdLI 144
Cdd:PRK12298 164 LLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPNLGVVRV-DDERSFVvaDIPGLIEGASEGAGLGIRFLKhLERCR-VL 241

                         90       100
                 ....*....|....*....|....*.
gi 268325198 145 LILVDVFQQ------QQYDILLKELY 164
Cdd:PRK12298 242 LHLIDIAPIdgsdpvENARIIINELE 267
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 68-151 2.49e-09

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 58.42  E-value: 2.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  68 LVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLEviPGTL--------------IYK-----GAQLQFLDVPGLIQGAAAGR 128
Cdd:PTZ00258  26 IVGLPNVGKSTTFNALCKQQVPAENFPFCTID--PNTArvnvpderfdwlckHFKpksivPAQLDITDIAGLVKGASEGE 103

                         90       100
                 ....*....|....*....|...
gi 268325198 129 GHGKEVISVMRNADLILILVDVF 151
Cdd:PTZ00258 104 GLGNAFLSHIRAVDGIYHVVRAF 126
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
 66-163 3.96e-09

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: 57.01  E-value: 3.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198   66 IVLVGFPSVGKSTLLNRLTG-TSAEVAAYEFTTLEVIPGTLIYKGAQLQFLDVPGL-IQGAAAGRGHGKEVISVMRNADL 143
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHGqKISITSPKAQTTRNRISGIHTTGASQIIFIDTPGFhEKKHSLNRLMMKEARSAIGGVDL 82

                          90       100
                  ....*....|....*....|
gi 268325198  144 ILILVDVFQQQQYDILLKEL 163
Cdd:TIGR00436  83 ILFVVDSDQWNGDGEFVLTK 102
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 28-289 1.80e-08

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: 55.84  E-value: 1.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  28 GRLKAKLARLKDDLQKraTAKSSGKGKGYfvkKSGhATIVLVGFPSVGKSTLLNRLTGTSA----EVAAyefTTLEVIPG 103
Cdd:COG0486  184 EELLERLEELREELEA--LLASARQGELL---REG-IKVVIVGRPNVGKSSLLNALLGEERaivtDIAG---TTRDVIEE 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 104 TLIYKGAQLQFLDVPGL------IqgaaagrghgkEVISVMR------NADLILILVDvfqqqqydillkelydagirin 171
Cdd:COG0486  255 RINIGGIPVRLIDTAGLretedeV-----------EKIGIERareaieEADLVLLLLD---------------------- 301

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 172 anpplvairkASRGgiiinrtvdldydnkviravlaeyrihngevlireritIDELIDAVLGNRKYVRALTVINKTDLAD 251
Cdd:COG0486  302 ----------ASEP--------------------------------------LTEEDEEILEKLKDKPVIVVLNKIDLPS 333

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 268325198 252 SETLLTCMARFPDAVPISAAVGINMDVLKDKIYNELGF 289
Cdd:COG0486  334 EADGELKSLPGEPVIAISAKTGEGIDELKEAILELVGE 371
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
65-119 4.63e-08

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 54.74  E-value: 4.63e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 268325198  65 TIVLVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLEVIPGTLIYKGAQLQFLDVPG 119
Cdd:COG0370    5 TIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKGKEIELVDLPG 59
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
 70-190 5.76e-08

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


Pssm-ID: 273077 [Multi-domain]  Cd Length: 591  Bit Score: 54.36  E-value: 5.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198   70 GFPSVGKSTLLNRLTGTSAEVAAYEFTTLEVIPGTLIYKGAQLQFLDVPGlIQGAAAGRGHGKEVISVMRN--ADLILIL 147
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGFQGEDIEIVDLPG-IYSLTTFSLEEEVARDYLLNekPDLVVNV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 268325198  148 VDVFQQQQYDILLKELYDAGIrinanPPLVAI---RKASRGGIIIN 190
Cdd:TIGR00437  80 VDASNLERNLYLTLQLLELGI-----PMILALnlvDEAEKKGIRID 120
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 28-285 1.31e-07

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: 52.48  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198   28 GRLKAKLARLKDDLQKraTAKSSGKGKGYfvkKSGhATIVLVGFPSVGKSTLLNRLTGT-SAEVAAYEFTTLEVIPGTLI 106
Cdd:pfam12631  65 EELLERLEELLAELEK--LLATADRGRIL---REG-IKVVIVGKPNVGKSSLLNALLGEeRAIVTDIPGTTRDVIEETIN 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  107 YKGAQLQFLDVPGLiqgaaagRGHGKEV--------ISVMRNADLILILVDvfqqqqydillkelydagirinanpplva 178
Cdd:pfam12631 139 IGGIPLRLIDTAGI-------RETDDEVekigieraREAIEEADLVLLVLD----------------------------- 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  179 irkASRGgiiinrtvdLDYDnkviravlaeyrihngevlireritiDELIDAVLGNRKYVraLTVINKTDLADSETLLTC 258
Cdd:pfam12631 183 ---ASRP---------LDEE--------------------------DLEILELLKDKKPI--IVVLNKSDLLGEIDELEE 222

                         250       260
                  ....*....|....*....|....*..
gi 268325198  259 mARFPDAVPISAAVGINMDVLKDKIYN 285
Cdd:pfam12631 223 -LKGKPVLAISAKTGEGLDELEEAIKE 248
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
30-285 2.34e-07

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 52.42  E-value: 2.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  30 LKAKLARLKDDLQKraTAKSSGKGKGYfvkKSGhATIVLVGFPSVGKSTLLNRLTGT-SAEVAAYEFTTLEVIPGTLIYK 108
Cdd:PRK05291 188 ILEKLEELIAELEA--LLASARQGEIL---REG-LKVVIAGRPNVGKSSLLNALLGEeRAIVTDIAGTTRDVIEEHINLD 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 109 GAQLQFLDVPGLiqgaaagRGHGKEV--------ISVMRNADLILILVDvfqqqqydillkelydagirinanpplvair 180
Cdd:PRK05291 262 GIPLRLIDTAGI-------RETDDEVekigiersREAIEEADLVLLVLD------------------------------- 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 181 kASRGgiiinrtvdldydnkviravlaeyrihngevlireritIDELIDAVLGNRKYVRALTVINKTDLADSETLLtcMA 260
Cdd:PRK05291 304 -ASEP--------------------------------------LTEEDDEILEELKDKPVIVVLNKADLTGEIDLE--EE 342

                        250       260
                 ....*....|....*....|....*
gi 268325198 261 RFPDAVPISAAVGINMDVLKDKIYN 285
Cdd:PRK05291 343 NGKPVIRISAKTGEGIDELREAIKE 367
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
64-287 3.60e-07

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 49.59  E-value: 3.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  64 ATIVLVGFPSVGKSTLLNRLTGTSAEVAAYEfTTLevipGTLIYK--------GAQLQFLDVPG-LIQgaaagRGHGKEV 134
Cdd:COG1100    4 KKIVVVGTGGVGKTSLVNRLVGDIFSLEKYL-STN----GVTIDKkelkldglDVDLVIWDTPGqDEF-----RETRQFY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 135 ISVMRNADLILILVDVfqqqqydillkelydagirinanpplvairkasrggiiinrtvdldydnkviravlaeyrihng 214
Cdd:COG1100   74 ARQLTGASLYLFVVDG---------------------------------------------------------------- 89

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 215 eVLIRERITIDELIDAVLGNRKYVRALTVINKTDLADSETL---LTCMARFPDA-----VPISAAVGINMDVLKDKIYNE 286
Cdd:COG1100   90 -TREETLQSLYELLESLRRLGKKSPIILVLNKIDLYDEEEIedeERLKEALSEDnivevVATSAKTGEGVEELFAALAEI 168


                 .
gi 268325198 287 L 287
Cdd:COG1100  169 L 169
YeeP COG3596
Predicted GTPase [General function prediction only];
60-179 7.76e-07

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 50.15  E-value: 7.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  60 KSGHATIVLVGFPSVGKSTLLNRLTGTS-AEVAAYEFTTLEVIPGTLIYKGAQ-LQFLDVPGLIQGAAAGRGHgKEVISV 137
Cdd:COG3596   36 ELPPPVIALVGKTGAGKSSLINALFGAEvAEVGVGRPCTREIQRYRLESDGLPgLVLLDTPGLGEVNERDREY-RELREL 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 268325198 138 MRNADLILILVDVfqQQQYDILLKELYDAGIRINANPPLVAI 179
Cdd:COG3596  115 LPEADLILWVVKA--DDRALATDEEFLQALRAQYPDPPVLVV 154
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 67-150 8.20e-07

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


Pssm-ID: 206681 [Multi-domain]  Cd Length: 157  Bit Score: 48.20  E-value: 8.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  67 VLVGFPSVGKSTLLNRLTGT-SAEVAAYEFTTLEVIPGTLIYKGAQLQFLDVPGL------IQGAAAgrghgKEVISVMR 139
Cdd:cd01894    1 AIVGRPNVGKSTLFNRLTGRrDAIVSDTPGVTRDRKYGEAEWGGREFILIDTGGIepddegISKEIR-----EQAEIAIE 75

                         90
                 ....*....|.
gi 268325198 140 NADLILILVDV 150
Cdd:cd01894   76 EADVILFVVDG 86
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 67-149 2.48e-06

YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 46.56  E-value: 2.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  67 VLVGFPSVGKSTLLNRLTGTS-AEVAAYEFTTLEVIPGTLIYKGAQLQFLDVPGLIQGAAAGRGHGKEVISVMRNADLIL 145
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTEvAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPGVGERGRRDREYEELYRRLLPEADLVL 80


                 ....
gi 268325198 146 ILVD 149
Cdd:cd11383   81 WLLD 84
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 65-182 1.11e-05

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: 45.18  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  65 TIVLVGFPSVGKSTLLNRLTGT-SAEVAAYEFTTLEVIPGTLIYKGAQLQFLDVPGLiqgaaagRGHGKEV--ISVMR-- 139
Cdd:cd04164    5 KVVIAGKPNVGKSSLLNALAGRdRAIVSDIAGTTRDVIEEEIDLGGIPVRLIDTAGL-------RETEDEIekIGIERar 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 268325198 140 ----NADLILILVDVFQQQQydillKELYDAGIRINANPPLVAIRKA 182
Cdd:cd04164   78 eaieEADLVLLVVDASEGLD-----EEDLEILELPAKKPVIVVLNKS 119
TGS_Obg cd04938
TGS (ThrRS, GTPase and SpoT) domain found in the Obg protein family; The Obg family of GTPases ...
 288-362 2.35e-05

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: 42.05  E-value: 2.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198 288 GFMRIYMKPPGAS-------PDMDNPLVIRRDSTITDVCSTIHRDFVDRFRYAriwgksVKYGGQR-VGLSHVLEEGDVL 359
Cdd:cd04938    1 GLIPVYPVKNIQTftngsgnSVFRDCVLVKKGTTVKDFANKIHTDLEKGFINA------EGIGGRRlEGEDYILQDNDVV 74


                 ...
gi 268325198 360 SFV 362
Cdd:cd04938   75 KFT 77
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 31-119 3.54e-05

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: 43.67  E-value: 3.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  31 KAKLARLKDDLQKRATAKSSGKGKGYFVKKsghATIVLVGFPSVGKSTLLNRLTGT-SAEVAAYefttleviPGT----- 104
Cdd:cd01856   86 GKGVKKLLKKAKKLLKENEKLKAKGLLPRP---LRAMVVGIPNVGKSTLINRLRGKkVAKVGNK--------PGVtrgqq 154

                         90
                 ....*....|....*
gi 268325198 105 LIYKGAQLQFLDVPG 119
Cdd:cd01856  155 WIRIGPNIELLDTPG 169
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 65-150 2.10e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 43.11  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  65 TIVLVGFPSVGKSTLLNRLTGT-SAEVAAYEFTTLEVIPGTLIYKGAQLQFLDVPGL------IQGAAAgrghgKEVISV 137
Cdd:PRK00093   3 VVAIVGRPNVGKSTLFNRLTGKrDAIVADTPGVTRDRIYGEAEWLGREFILIDTGGIepdddgFEKQIR-----EQAELA 77

                         90
                 ....*....|...
gi 268325198 138 MRNADLILILVDV 150
Cdd:PRK00093  78 IEEADVILFVVDG 90
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 13-152 2.30e-04

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 43.24  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  13 EIWK----TPYNKATSHhvGRLKAKLARLKDDLQKRATAKSSgkgkgyFVKKSGHATIVLVGFPSVGKSTLLNRLTGTS- 87
Cdd:PRK09518 404 EFWKlglgEPYPISAMH--GRGVGDLLDEALDSLKVAEKTSG------FLTPSGLRRVALVGRPNVGKSSLLNQLTHEEr 475

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 268325198  88 AEVAAYEFTTLEVIPGTLIYKGAQLQFLDVPGLIQGAAAGRGH----GKEVISVMRNADLILILVDVFQ 152
Cdd:PRK09518 476 AVVNDLAGTTRDPVDEIVEIDGEDWLFIDTAGIKRRQHKLTGAeyysSLRTQAAIERSELALFLFDASQ 544
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 66-150 2.40e-04

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: 41.26  E-value: 2.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  66 IVLVGFPSVGKSTLLNRLTG-----TSaEVAAyefTTLEVIPGTLIYKGAQLQFLDVPGLIQgaaagRGH---GKEVISV 137
Cdd:cd01895    5 IAIIGRPNVGKSSLLNALLGeerviVS-DIAG---TTRDSIDVPFEYDGQKYTLIDTAGIRK-----KGKvteGIEKYSV 75

                         90
                 ....*....|....*....
gi 268325198 138 MR------NADLILILVDV 150
Cdd:cd01895   76 LRtlkaieRADVVLLVLDA 94
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
65-86 3.48e-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: 3.48e-04
                         10        20
                 ....*....|....*....|..
gi 268325198  65 TIVLVGFPSVGKSTLLNRLTGT 86
Cdd:COG1160    4 VVAIVGRPNVGKSTLFNRLTGR 25
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
65-119 6.02e-04

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 42.01  E-value: 6.02e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 268325198  65 TIVLVGFPSVGKSTLLNRLTGTSAEVAAYEFTTLEVIPGTLIYKGAQLQFLDVPG 119
Cdd:PRK09554   5 TIGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQFSTTDHQVTLVDLPG 59
TGS_MJ1332_like cd01669
TGS (ThrRS, GTPase and SpoT) domain found in Methanocaldococcus jannaschii uncharacterized ...
 307-362 7.53e-04

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


Pssm-ID: 340460 [Multi-domain]  Cd Length: 78  Bit Score: 37.68  E-value: 7.53e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 268325198 307 LVIRRDSTITDVCSTIHRDFVDRFRYAriwgKSVKYGgQRVGLSHVLEEGDVLSFV 362
Cdd:cd01669   27 ILLKRGSTPRDLAYKIHTDLGKGFLYA----IDARTK-MRLGEDYELKHGDVVKIV 77
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 64-119 1.35e-03

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: 38.84  E-value: 1.35e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 268325198  64 ATIVLVGFPSVGKSTLLNRLTG-----TSAEVAAYEFTTLEvipgTLIYKGAQLQFLDVPG 119
Cdd:cd01859  100 VIVGVVGYPKVGKSSIINALKGrhsasTSPIPGSPGYTKGI----QLVRIDSKIYLIDTPG 156
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 66-149 2.40e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 39.65  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  66 IVLVGFPSVGKSTLLNRLTG-----TSaEVAAyefTTLEVIPGTLIYKGAQLQFLDVPGLiqgaaagRGHGK-----EVI 135
Cdd:PRK00093 176 IAIIGRPNVGKSSLINALLGeerviVS-DIAG---TTRDSIDTPFERDGQKYTLIDTAGI-------RRKGKvtegvEKY 244

                         90       100
                 ....*....|....*....|
gi 268325198 136 SVMR------NADLILILVD 149
Cdd:PRK00093 245 SVIRtlkaieRADVVLLVID 264
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 64-121 3.98e-03

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


Pssm-ID: 206750 [Multi-domain]  Cd Length: 140  Bit Score: 37.21  E-value: 3.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 268325198  64 ATIVLVGFPSVGKSTLLNRLTGtSAEVAAYE-------FTTLEVIPGtliykgaqLQFLDVPGLI 121
Cdd:cd01857   83 ATIGLVGYPNVGKSSLINALVG-SKKVSVSStpgktkhFQTIFLEPG--------ITLCDCPGLV 138
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
66-149 7.67e-03

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 38.08  E-value: 7.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268325198  66 IVLVGFPSVGKSTLLNRLTG-----TSAevaayefttlevIPGT--------LIYKGAQLQFLDVPGLiqgaaagRGHGK 132
Cdd:COG1160  178 IAIVGRPNVGKSSLINALLGeerviVSD------------IAGTtrdsidtpFERDGKKYTLIDTAGI-------RRKGK 238

                         90       100
                 ....*....|....*....|....*...
gi 268325198 133 -----EVISVMR------NADLILILVD 149
Cdd:COG1160  239 vdegiEKYSVLRtlraieRADVVLLVID 266
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 65-85 7.74e-03

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ 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. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 37.38  E-value: 7.74e-03
                         10        20
                 ....*....|....*....|..
gi 268325198  65 TIVLVGfPS-VGKSTLLNRLTG 85
Cdd:cd01854   87 TSVLVG-QSgVGKSTLLNALLP 107
 
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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