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Conserved domains on  [gi|1907159694|ref|XP_036020610|]
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putative GTP-binding protein 6 isoform X4 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 65-236 3.30e-62

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: 195.76  E-value: 3.30e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  65 RRLMRKERVRREFPVVSVVGYTNCGKTTLIQALTGEAALqPRDQPFATLDVTVHAGLLPSRLRILYVDTIGFLSQLPHSL 144
Cdd:cd01878    29 RELQRARRKRSGVPTVALVGYTNAGKSTLFNALTGADVL-AEDQLFATLDPTTRRIKLPGGREVLLTDTVGFIRDLPHQL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 145 IHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLR--GLHLPPallesALEVHSKVDLVPGYTPPCS------GA 216
Cdd:cd01878   108 VEAFRSTLEEVAEADLLLHVVDASDPDREEQIETVEEVLKelGADDIP-----IILVLNKIDLLDDEELEERlragrpDA 182

                         170       180
                  ....*....|....*....|
gi 1907159694 217 LAVSAISGRGLDELKAALEA 236
Cdd:cd01878   183 VFISAKTGEGLDLLKEAIEE 202
 
Name Accession Description Interval E-value
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 65-236 3.30e-62

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: 195.76  E-value: 3.30e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  65 RRLMRKERVRREFPVVSVVGYTNCGKTTLIQALTGEAALqPRDQPFATLDVTVHAGLLPSRLRILYVDTIGFLSQLPHSL 144
Cdd:cd01878    29 RELQRARRKRSGVPTVALVGYTNAGKSTLFNALTGADVL-AEDQLFATLDPTTRRIKLPGGREVLLTDTVGFIRDLPHQL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 145 IHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLR--GLHLPPallesALEVHSKVDLVPGYTPPCS------GA 216
Cdd:cd01878   108 VEAFRSTLEEVAEADLLLHVVDASDPDREEQIETVEEVLKelGADDIP-----IILVLNKIDLLDDEELEERlragrpDA 182

                         170       180
                  ....*....|....*....|
gi 1907159694 217 LAVSAISGRGLDELKAALEA 236
Cdd:cd01878   183 VFISAKTGEGLDLLKEAIEE 202
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 65-298 1.74e-59

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 195.69  E-value: 1.74e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  65 RRLMRKERVRREFPVVSVVGYTNCGKTTLIQALTGEAALQpRDQPFATLDVTVHAGLLPSRLRILYVDTIGFLSQLPHSL 144
Cdd:COG2262   187 RELQRKRRKRSGIPTVALVGYTNAGKSTLFNRLTGADVLA-EDKLFATLDPTTRRLELPDGRPVLLTDTVGFIRKLPHQL 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 145 IHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLRGL---HLPpallesALEVHSKVDLVPG-------YTPPcs 214
Cdd:COG2262   266 VEAFRSTLEEVREADLLLHVVDASDPDFEEQIETVNEVLEELgadDKP------IILVFNKIDLLDDeelerlrAGYP-- 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 215 GALAVSAISGRGLDELKAALEASVLRATGRQVLTLCVRLGGpQLGWLYKEAVVQQVQELPEGdaAHVTVVITQAAYGRFR 294
Cdd:COG2262   338 DAVFISAKTGEGIDELLEAIEERLPEDRVEVELLLPYSDGD-LVAWLHEHGEVLSEEYDEDG--TLLTVRLPPEDLARLE 414


                  ....
gi 1907159694 295 KLFP 298
Cdd:COG2262   415 AYLV 418
GTP_HflX TIGR03156
GTP-binding protein HflX; This protein family is one of a number of homologous small, ...
 65-235 7.15e-46

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


Pssm-ID: 274455 [Multi-domain]  Cd Length: 351  Bit Score: 158.40  E-value: 7.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  65 RRLMRKERVRREFPVVSVVGYTNCGKTTLIQALTGEAALQpRDQPFATLDVTVHAGLLPSRLRILYVDTIGFLSQLPHSL 144
Cdd:TIGR03156 177 RERQRRRRKRADVPTVALVGYTNAGKSTLFNALTGADVYA-ADQLFATLDPTTRRLDLPDGGEVLLTDTVGFIRDLPHEL 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 145 IHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLRGL---HLPpallesALEVHSKVDLVPGY-----TPPCSGA 216
Cdd:TIGR03156 256 VAAFRATLEEVREADLLLHVVDASDPDREEQIEAVEKVLEELgaeDIP------QLLVYNKIDLLDEPrierlEEGYPEA 329

                         170
                  ....*....|....*....
gi 1907159694 217 LAVSAISGRGLDELKAALE 235
Cdd:TIGR03156 330 VFVSAKTGEGLDLLLEAIA 348
PRK11058 PRK11058
GTPase HflX; Provisional
 69-234 1.33e-20

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 91.32  E-value: 1.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  69 RKERVRREFPVVSVVGYTNCGKTTLIQALTgEAALQPRDQPFATLDVTVHAGLLPSRLRILYVDTIGFLSQLPHSLIHAF 148
Cdd:PRK11058  189 RRARIKADVPTVSLVGYTNAGKSTLFNRIT-EARVYAADQLFATLDPTLRRIDVADVGETVLADTVGFIRHLPHDLVAAF 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 149 SATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLRGL--HLPPALLesaleVHSKVDLVPGYTPPCSG-------ALAV 219
Cdd:PRK11058  268 KATLQETRQATLLLHVVDAADVRVQENIEAVNTVLEEIdaHEIPTLL-----VMNKIDMLDDFEPRIDRdeenkpiRVWL 342

                         170
                  ....*....|....*
gi 1907159694 220 SAISGRGLDELKAAL 234
Cdd:PRK11058  343 SAQTGAGIPLLFQAL 357
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 80-193 3.79e-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: 73.04  E-value: 3.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  80 VSVVGYTNCGKTTLIQALTGEAAlQPRDQPFATLDVTVHAgLLPSRLRILYVDTIGFL--SQLPHSLIHAFSATLEdvay 157
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGAKA-IVSDYPGTTRDPNEGR-LELKGKQIILVDTPGLIegASEGEGLGRAFLAIIE---- 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907159694 158 SDVLVHVTDVSHPdAELQKATVLSTLRGLHLPPALL 193
Cdd:pfam01926  76 ADLILFVVDSEEG-ITPLDEELLELLRENKKPIILV 110
 
Name Accession Description Interval E-value
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 65-236 3.30e-62

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: 195.76  E-value: 3.30e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  65 RRLMRKERVRREFPVVSVVGYTNCGKTTLIQALTGEAALqPRDQPFATLDVTVHAGLLPSRLRILYVDTIGFLSQLPHSL 144
Cdd:cd01878    29 RELQRARRKRSGVPTVALVGYTNAGKSTLFNALTGADVL-AEDQLFATLDPTTRRIKLPGGREVLLTDTVGFIRDLPHQL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 145 IHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLR--GLHLPPallesALEVHSKVDLVPGYTPPCS------GA 216
Cdd:cd01878   108 VEAFRSTLEEVAEADLLLHVVDASDPDREEQIETVEEVLKelGADDIP-----IILVLNKIDLLDDEELEERlragrpDA 182

                         170       180
                  ....*....|....*....|
gi 1907159694 217 LAVSAISGRGLDELKAALEA 236
Cdd:cd01878   183 VFISAKTGEGLDLLKEAIEE 202
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 65-298 1.74e-59

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 195.69  E-value: 1.74e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  65 RRLMRKERVRREFPVVSVVGYTNCGKTTLIQALTGEAALQpRDQPFATLDVTVHAGLLPSRLRILYVDTIGFLSQLPHSL 144
Cdd:COG2262   187 RELQRKRRKRSGIPTVALVGYTNAGKSTLFNRLTGADVLA-EDKLFATLDPTTRRLELPDGRPVLLTDTVGFIRKLPHQL 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 145 IHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLRGL---HLPpallesALEVHSKVDLVPG-------YTPPcs 214
Cdd:COG2262   266 VEAFRSTLEEVREADLLLHVVDASDPDFEEQIETVNEVLEELgadDKP------IILVFNKIDLLDDeelerlrAGYP-- 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 215 GALAVSAISGRGLDELKAALEASVLRATGRQVLTLCVRLGGpQLGWLYKEAVVQQVQELPEGdaAHVTVVITQAAYGRFR 294
Cdd:COG2262   338 DAVFISAKTGEGIDELLEAIEERLPEDRVEVELLLPYSDGD-LVAWLHEHGEVLSEEYDEDG--TLLTVRLPPEDLARLE 414


                  ....
gi 1907159694 295 KLFP 298
Cdd:COG2262   415 AYLV 418
GTP_HflX TIGR03156
GTP-binding protein HflX; This protein family is one of a number of homologous small, ...
 65-235 7.15e-46

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


Pssm-ID: 274455 [Multi-domain]  Cd Length: 351  Bit Score: 158.40  E-value: 7.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  65 RRLMRKERVRREFPVVSVVGYTNCGKTTLIQALTGEAALQpRDQPFATLDVTVHAGLLPSRLRILYVDTIGFLSQLPHSL 144
Cdd:TIGR03156 177 RERQRRRRKRADVPTVALVGYTNAGKSTLFNALTGADVYA-ADQLFATLDPTTRRLDLPDGGEVLLTDTVGFIRDLPHEL 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 145 IHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLRGL---HLPpallesALEVHSKVDLVPGY-----TPPCSGA 216
Cdd:TIGR03156 256 VAAFRATLEEVREADLLLHVVDASDPDREEQIEAVEKVLEELgaeDIP------QLLVYNKIDLLDEPrierlEEGYPEA 329

                         170
                  ....*....|....*....
gi 1907159694 217 LAVSAISGRGLDELKAALE 235
Cdd:TIGR03156 330 VFVSAKTGEGLDLLLEAIA 348
PRK11058 PRK11058
GTPase HflX; Provisional
 69-234 1.33e-20

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 91.32  E-value: 1.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  69 RKERVRREFPVVSVVGYTNCGKTTLIQALTgEAALQPRDQPFATLDVTVHAGLLPSRLRILYVDTIGFLSQLPHSLIHAF 148
Cdd:PRK11058  189 RRARIKADVPTVSLVGYTNAGKSTLFNRIT-EARVYAADQLFATLDPTLRRIDVADVGETVLADTVGFIRHLPHDLVAAF 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 149 SATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLRGL--HLPPALLesaleVHSKVDLVPGYTPPCSG-------ALAV 219
Cdd:PRK11058  268 KATLQETRQATLLLHVVDAADVRVQENIEAVNTVLEEIdaHEIPTLL-----VMNKIDMLDDFEPRIDRdeenkpiRVWL 342

                         170
                  ....*....|....*
gi 1907159694 220 SAISGRGLDELKAAL 234
Cdd:PRK11058  343 SAQTGAGIPLLFQAL 357
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 80-193 3.79e-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: 73.04  E-value: 3.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  80 VSVVGYTNCGKTTLIQALTGEAAlQPRDQPFATLDVTVHAgLLPSRLRILYVDTIGFL--SQLPHSLIHAFSATLEdvay 157
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGAKA-IVSDYPGTTRDPNEGR-LELKGKQIILVDTPGLIegASEGEGLGRAFLAIIE---- 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907159694 158 SDVLVHVTDVSHPdAELQKATVLSTLRGLHLPPALL 193
Cdd:pfam01926  76 ADLILFVVDSEEG-ITPLDEELLELLRENKKPIILV 110
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 82-236 6.63e-12

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: 62.65  E-value: 6.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  82 VVGYTNCGKTTLIQALTGEAALQPRDQPFATLDVTVHAGLLPSRLRILYVDTIGFLSQlPHSLIHAFSATLEDVAYSDVL 161
Cdd:cd00880     2 IFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRKEWELLPLGPVVLIDTPGLDEE-GGLGRERVEEARQVADRADLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 162 VHVTDVSHPDAELQkaTVLSTLRGLHLpPALLesaleVHSKVDLVPG------YTPPCSGAL------AVSAISGRGLDE 229
Cdd:cd00880    81 LLVVDSDLTPVEEE--AKLGLLRERGK-PVLL-----VLNKIDLVPEseeeelLRERKLELLpdlpviAVSALPGEGIDE 152


                  ....*..
gi 1907159694 230 LKAALEA 236
Cdd:cd00880   153 LRKKIAE 159
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 82-234 1.82e-10

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: 58.62  E-value: 1.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  82 VVGYTNCGKTTLIQALTGEAALQPRDQPFATLD-VTVHAGLLPSRLRILYVDTIGFLSQLPHSLIHAFSATLEDvaySDV 160
Cdd:cd00882     2 VVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDpDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELARLLLRG---ADL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 161 LVHVTDVSHPDAELQKATVLSTLRGLHLPPALLesaleVHSKVDLVPGYT------------PPCSGALAVSAISGRGLD 228
Cdd:cd00882    79 ILLVVDSTDRESEEDAKLLILRRLRKEGIPIIL-----VGNKIDLLEEREveellrleelakILGVPVFEVSAKTGEGVD 153


                  ....*.
gi 1907159694 229 ELKAAL 234
Cdd:cd00882   154 ELFEKL 159
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 80-234 4.77e-07

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: 49.00  E-value: 4.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  80 VSVVGYTNCGKTTLIQALTGE--AALQPRDQpfaTldvTVHagllpsRLR---------ILYVDTIGFLSQ---LPHSLI 145
Cdd:cd04163     6 VAIIGRPNVGKSTLLNALVGQkiSIVSPKPQ---T---TRN------RIRgiytdddaqIIFVDTPGIHKPkkkLGERMV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 146 HAFSATLEDVaysDVLVHVTDVSHPDAELQKaTVLSTLRGLHLPPALlesaleVHSKVDLVP------------GYTPPC 213
Cdd:cd04163    74 KAAWSALKDV---DLVLFVVDASEWIGEGDE-FILELLKKSKTPVIL------VLNKIDLVKdkedllplleklKELHPF 143

                         170       180
                  ....*....|....*....|.
gi 1907159694 214 SGALAVSAISGRGLDELKAAL 234
Cdd:cd04163   144 AEIFPISALKGENVDELLEYI 164
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
80-236 1.27e-06

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 48.83  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  80 VSVVGYTNCGKTTLIQALTGE--AALQPRDQpfaTldvTVHagllpsRLR---------ILYVDTIGFlsQLPHSLIHAF 148
Cdd:COG1159     6 VAIVGRPNVGKSTLLNALVGQkvSIVSPKPQ---T---TRH------RIRgivtredaqIVFVDTPGI--HKPKRKLGRR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 149 -----SATLEDVaysDVLVHVTDVSHPDAELQKAtVLSTLRGLHLP-------------PALLESALEVHSKVD---LVP 207
Cdd:COG1159    72 mnkaaWSALEDV---DVILFVVDATEKIGEGDEF-ILELLKKLKTPvilvinkidlvkkEELLPLLAEYSELLDfaeIVP 147

                         170       180
                  ....*....|....*....|....*....
gi 1907159694 208 gytppcsgalaVSAISGRGLDELKAALEA 236
Cdd:COG1159   148 -----------ISALKGDNVDELLDEIAK 165
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
80-244 3.48e-06

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 46.51  E-value: 3.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  80 VSVVGYTNCGKTTLIQALTGEAALQPRDQPfaTLDVTVHAGLLP---SRLRILYVDTIGflsQLPHSLIHAFSAtlEDVA 156
Cdd:COG1100     6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLS--TNGVTIDKKELKldgLDVDLVIWDTPG---QDEFRETRQFYA--RQLT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 157 YSDVLVHVTDVSHPDAELQKATVLSTLRGLHLP-PALLesaleVHSKVDLVPGY-------------TPPCSGALAVSAI 222
Cdd:COG1100    79 GASLYLFVVDGTREETLQSLYELLESLRRLGKKsPIIL-----VLNKIDLYDEEeiedeerlkealsEDNIVEVVATSAK 153

                         170       180
                  ....*....|....*....|..
gi 1907159694 223 SGRGLDELKAALeASVLRATGR 244
Cdd:COG1100   154 TGEGVEELFAAL-AEILRGEGD 174
era PRK00089
GTPase Era; Reviewed
 80-236 2.51e-05

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 45.04  E-value: 2.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  80 VSVVGYTNCGKTTLIQALTGE--AALQPRDQpfaTldvTVHagllpsRLR---------ILYVDTIGFlsQLPHSLIH-- 146
Cdd:PRK00089    8 VAIVGRPNVGKSTLLNALVGQkiSIVSPKPQ---T---TRH------RIRgivteddaqIIFVDTPGI--HKPKRALNra 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 147 ---AFSATLEDVaysDVLVHVTDVSH---PDAELqkatVLSTLRGLHLP-----------------PALLESALEVHSKV 203
Cdd:PRK00089   74 mnkAAWSSLKDV---DLVLFVVDADEkigPGDEF----ILEKLKKVKTPvilvlnkidlvkdkeelLPLLEELSELMDFA 146

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1907159694 204 DLVPgytppcsgalaVSAISGRGLDELKAALEA 236
Cdd:PRK00089  147 EIVP-----------ISALKGDNVDELLDVIAK 168
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 71-238 2.90e-05

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: 45.05  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  71 ERVRREFPVVsVVGYTNCGKTTLIQALTG-EAAL---QP---RDqpfaTLDVTVHAGLLPsrLRIlyVDTIGflsqlphs 143
Cdd:COG0486   208 ELLREGIKVV-IVGRPNVGKSSLLNALLGeERAIvtdIAgttRD----VIEERINIGGIP--VRL--IDTAG-------- 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 144 lIH-------------AFSAtLEDvaySDVLVHVTDVSHPDAELQKAtVLSTLRGLHLppallesaLEVHSKVDLVPGYT 210
Cdd:COG0486   271 -LRetedevekigierAREA-IEE---ADLVLLLLDASEPLTEEDEE-ILEKLKDKPV--------IVVLNKIDLPSEAD 336

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1907159694 211 PPCS-----GALAVSAISGRGLDELKAALEASV 238
Cdd:COG0486   337 GELKslpgePVIAISAKTGEGIDELKEAILELV 369
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 79-234 5.62e-05

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: 42.44  E-value: 5.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  79 VVSVVGYTNCGKTTLIQALTGeAALQ----PRdqpfatldVTV---HAGLLPSRLRILYVDTIGflsqlphslIHAFSAT 151
Cdd:pfam02421   2 TIALVGNPNVGKTTLFNALTG-ANQHvgnwPG--------VTVekkEGKFKYKGYEIEIVDLPG---------IYSLSPY 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 152 LED--VAYS-------DVLVHVTDVSHPD---------AELQKATVL-------STLRGLHLPPALLESALEVhskvdlv 206
Cdd:pfam02421  64 SEEerVARDyllnekpDVIVNVVDATNLErnlyltlqlLELGLPVVLalnmmdeAEKKGIKIDIKKLSELLGV------- 136

                         170       180
                  ....*....|....*....|....*...
gi 1907159694 207 pgytpPCsgaLAVSAISGRGLDELKAAL 234
Cdd:pfam02421 137 -----PV---VPTSARKGEGIDELLDAI 156
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 80-238 1.25e-04

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


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 41.71  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  80 VSVVGYTNCGKTTLIQALTG-EAAL---QP---RDqpfaTLDVTVHAGLLPSRLrilyVDTIGflsqlphslIH------ 146
Cdd:cd04164     6 VVIAGKPNVGKSSLLNALAGrDRAIvsdIAgttRD----VIEEEIDLGGIPVRL----IDTAG---------LRetedei 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 147 -------AFSATLEdvaySDVLVHVTDVSHP-DAELQKATVLSTLRGLHLppallesaleVHSKVDLVPGYTPPCSGA-- 216
Cdd:cd04164    69 ekigierAREAIEE----ADLVLLVVDASEGlDEEDLEILELPAKKPVIV----------VLNKSDLLSDAEGISELNgk 134

                         170       180
                  ....*....|....*....|....
gi 1907159694 217 --LAVSAISGRGLDELKAALEASV 238
Cdd:cd04164   135 piIAISAKTGEGIDELKEALLELA 158
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 72-239 2.49e-04

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: 42.08  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  72 RVRREFPVVSVVGYTNCGKTTLIQALTG-EAAL---QP---RDqpfaTLDVTVHAGLLPsrLRIlyVDTIGflsqlphsl 144
Cdd:pfam12631  89 RILREGIKVVIVGKPNVGKSSLLNALLGeERAIvtdIPgttRD----VIEETINIGGIP--LRL--IDTAG--------- 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 145 IHAfsaTLEDV------------AYSDVLVHVTDVSHPDAELQKATVLSTLRGLHLppallesaLEVHSKVDLVPGYTPP 212
Cdd:pfam12631 152 IRE---TDDEVekigierareaiEEADLVLLVLDASRPLDEEDLEILELLKDKKPI--------IVVLNKSDLLGEIDEL 220

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1907159694 213 CSGA----LAVSAISGRGLDELKAALEASVL 239
Cdd:pfam12631 221 EELKgkpvLAISAKTGEGLDELEEAIKELFL 251
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 65-99 5.24e-04

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


Pssm-ID: 206752 [Multi-domain]  Cd Length: 157  Bit Score: 39.99  E-value: 5.24e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1907159694  65 RRLMRKERVRREFPVVSVVGYTNCGKTTLIQALTG 99
Cdd:cd01859    87 RRTIKELAIDGKPVIVGVVGYPKVGKSSIINALKG 121
MobB COG1763
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ...
 78-97 5.31e-04

Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 441369 [Multi-domain]  Cd Length: 162  Bit Score: 39.78  E-value: 5.31e-04
                          10        20
                  ....*....|....*....|
gi 1907159694  78 PVVSVVGYTNCGKTTLIQAL 97
Cdd:COG1763     2 PVLGIVGYSGSGKTTLLEKL 21
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 82-168 7.58e-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: 39.68  E-value: 7.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  82 VVGYTNCGKTTLIQALTgEAALQPRDQPFATLdvTVHAGLLPSR--LRILYVDTIGfLSQLPHS---LIHAFSATLEDva 156
Cdd:cd01881     2 LVGLPNVGKSTLLSALT-SAKVEIASYPFTTL--EPNVGVFEFGdgVDIQIIDLPG-LLDGASEgrgLGEQILAHLYR-- 75

                          90
                  ....*....|..
gi 1907159694 157 ySDVLVHVTDVS 168
Cdd:cd01881    76 -SDLILHVIDAS 86
EutP COG4917
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ...
 82-235 2.22e-03

Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];


Pssm-ID: 443945 [Multi-domain]  Cd Length: 145  Bit Score: 37.86  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  82 VVGYTNCGKTTLIQALTGEAALQPRDQpfatlDVTVHAGLL--PS------RLR---ILY---VDTIGFL-------SQL 140
Cdd:COG4917     6 LIGRSGAGKTTLTQALNGEELEYRKTQ-----AVEYYDNIIdtPGeyienpRFYkalIATaqdADVIVLVqdateprSVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 141 PHSLIHAFSatledvaySDVLVHVTDVSHPDAELQKATvlstlrglhlppALLESAlevhskvdlvpGYTPPcsgaLAVS 220
Cdd:COG4917    81 PPGFAKAFN--------KPVIGVITKIDLPEADVERAR------------KWLKSA-----------GVEPI----FIVS 125

                         170
                  ....*....|....*
gi 1907159694 221 AISGRGLDELKAALE 235
Cdd:COG4917   126 SVTGEGIEELKEYLE 140
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
69-238 2.28e-03

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 39.32  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694  69 RKERVRREFPVVsVVGYTNCGKTTLIQALTG-EAAL---QP---RDqpfaTLDVTVHAGLLPSRLrilyVDTIGflsqlp 141
Cdd:PRK05291  208 QGEILREGLKVV-IAGRPNVGKSSLLNALLGeERAIvtdIAgttRD----VIEEHINLDGIPLRL----IDTAG------ 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159694 142 hslIH-------------AFSAtLEDvaySDVLVHVTDVSHPDAELQKAtvlstlrglHLPPALLESALEVHSKVDLVP- 207
Cdd:PRK05291  273 ---IRetddevekigierSREA-IEE---ADLVLLVLDASEPLTEEDDE---------ILEELKDKPVIVVLNKADLTGe 336

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1907159694 208 --GYTPPCSGALAVSAISGRGLDELKAALEASV 238
Cdd:PRK05291  337 idLEEENGKPVIRISAKTGEGIDELREAIKELA 369
 
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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