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Conserved domains on  [gi|209447119|ref|NP_001129312|]
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putative GTP-binding protein 6 [Rattus norvegicus]

Protein Classification

HflX GTPase family protein( domain architecture ID 1002010)

HflX GTPase family protein similar to GTPase HflX, which is a GTP-binding protein with a GTP hydrolysis activity that is stimulated by binding to the 50S ribosome subunit, and it may play a role during protein synthesis or ribosome biogenesis

CATH:  3.40.50.300
Gene Ontology:  GO:0005525|GO:0043022|GO:0046872
PubMed:  26733579
SCOP:  4004038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HflX super family cl34447
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 83-503 1.84e-73

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


The actual alignment was detected with superfamily member COG2262:

Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 238.83  E-value: 1.84e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119  83 QRVCVLHPDVKRPAGKTPRStaewqVAEAAALVRALpGWSVARTLVVSSAAPGSRQVFGKGNFRDLTEKIRGCqDITSVF 162
Cdd:COG2262    9 ERAILVGVDLPGSDEDAEES-----LEELAELAETA-GAEVVGTVTQRRDKPDPATYIGKGKVEELAELVEEL-EADLVI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 163 LNVErMTPQTQKELETAWGLRVFDRFTLVLHIFRCNARTREARMQLALA----EIPLLRSSVSGDSEQQDqqGWGSRyim 238
Cdd:COG2262   82 FDDE-LSPSQQRNLEKALGVKVIDRTGLILDIFAQRARTREGKLQVELAqlqyLLPRLVGMWTHLSRQGG--GIGTR--- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 239 GSGES------------FSELRARALRDRELrlrrvlerlrdkRRLMRKERVRREFPVVSVVGYTNCGKTTLIRALTGEA 306
Cdd:COG2262  156 GPGETqletdrrlirdrIARLKRELEKVRKQ------------RELQRKRRKRSGIPTVALVGYTNAGKSTLFNRLTGAD 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 307 TLQpRDQPFATLDVTVHEGRLPSRLRVLYVDTIGFLSQLPHSLIHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLS 386
Cdd:COG2262  224 VLA-EDKLFATLDPTTRRLELPDGRPVLLTDTVGFIRKLPHQLVEAFRSTLEEVREADLLLHVVDASDPDFEEQIETVNE 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 387 TLRGLGL--RPALLesaveVHSKVDLVPG-------HTTPcsGALAVSAVSGRGLDELKAALEASVLRATGRQLLTIRVR 457
Cdd:COG2262  303 VLEELGAddKPIIL-----VFNKIDLLDDeelerlrAGYP--DAVFISAKTGEGIDELLEAIEERLPEDRVEVELLLPYS 375

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 209447119 458 LGGpQLGWLYNEAVVQQVQELPEGgaAHVTVVITQAAYGRFQKLFP 503
Cdd:COG2262  376 DGD-LVAWLHEHGEVLSEEYDEDG--TLLTVRLPPEDLARLEAYLV 418
 
Name Accession Description Interval E-value
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 83-503 1.84e-73

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 238.83  E-value: 1.84e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119  83 QRVCVLHPDVKRPAGKTPRStaewqVAEAAALVRALpGWSVARTLVVSSAAPGSRQVFGKGNFRDLTEKIRGCqDITSVF 162
Cdd:COG2262    9 ERAILVGVDLPGSDEDAEES-----LEELAELAETA-GAEVVGTVTQRRDKPDPATYIGKGKVEELAELVEEL-EADLVI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 163 LNVErMTPQTQKELETAWGLRVFDRFTLVLHIFRCNARTREARMQLALA----EIPLLRSSVSGDSEQQDqqGWGSRyim 238
Cdd:COG2262   82 FDDE-LSPSQQRNLEKALGVKVIDRTGLILDIFAQRARTREGKLQVELAqlqyLLPRLVGMWTHLSRQGG--GIGTR--- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 239 GSGES------------FSELRARALRDRELrlrrvlerlrdkRRLMRKERVRREFPVVSVVGYTNCGKTTLIRALTGEA 306
Cdd:COG2262  156 GPGETqletdrrlirdrIARLKRELEKVRKQ------------RELQRKRRKRSGIPTVALVGYTNAGKSTLFNRLTGAD 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 307 TLQpRDQPFATLDVTVHEGRLPSRLRVLYVDTIGFLSQLPHSLIHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLS 386
Cdd:COG2262  224 VLA-EDKLFATLDPTTRRLELPDGRPVLLTDTVGFIRKLPHQLVEAFRSTLEEVREADLLLHVVDASDPDFEEQIETVNE 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 387 TLRGLGL--RPALLesaveVHSKVDLVPG-------HTTPcsGALAVSAVSGRGLDELKAALEASVLRATGRQLLTIRVR 457
Cdd:COG2262  303 VLEELGAddKPIIL-----VFNKIDLLDDeelerlrAGYP--DAVFISAKTGEGIDELLEAIEERLPEDRVEVELLLPYS 375

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 209447119 458 LGGpQLGWLYNEAVVQQVQELPEGgaAHVTVVITQAAYGRFQKLFP 503
Cdd:COG2262  376 DGD-LVAWLHEHGEVLSEEYDEDG--TLLTVRLPPEDLARLEAYLV 418
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 270-441 2.64e-61

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: 199.61  E-value: 2.64e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 270 RRLMRKERVRREFPVVSVVGYTNCGKTTLIRALTGEATLqPRDQPFATLDVTVHEGRLPSRLRVLYVDTIGFLSQLPHSL 349
Cdd:cd01878   29 RELQRARRKRSGVPTVALVGYTNAGKSTLFNALTGADVL-AEDQLFATLDPTTRRIKLPGGREVLLTDTVGFIRDLPHQL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 350 IHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLRGLGlrpALLESAVEVHSKVDLVPG--------HTTPcsGA 421
Cdd:cd01878  108 VEAFRSTLEEVAEADLLLHVVDASDPDREEQIETVEEVLKELG---ADDIPIILVLNKIDLLDDeeleerlrAGRP--DA 182

                        170       180
                 ....*....|....*....|
gi 209447119 422 LAVSAVSGRGLDELKAALEA 441
Cdd:cd01878  183 VFISAKTGEGLDLLKEAIEE 202
GTP_HflX TIGR03156
GTP-binding protein HflX; This protein family is one of a number of homologous small, ...
 109-440 1.81e-59

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: 200.01  E-value: 1.81e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119  109 AEAAALVRALpGWSVARTLVVSSAAPGSRQVFGKGNFRDLTEKIRGCqDITSVFLNVErMTPQTQKELETAWGLRVFDRF 188
Cdd:TIGR03156  20 EELAELAETA-GAEVVGTVTQKRSRPDPATYIGKGKVEEIAELVEEL-EADLVIFDHE-LSPSQERNLEKALGCRVIDRT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119  189 TLVLHIFRCNARTREARMQLALAEIPLLRSSVSGDSEQQDQQ--GWGSRyimGSGESFSELRARALRDRELRLRRVLERL 266
Cdd:TIGR03156  97 GLILDIFAQRARTHEGKLQVELAQLKYLLPRLVGGWTHLSRQggGIGTR---GPGETQLETDRRLIRERIAQLKKELEKV 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119  267 RDKRRLMRKERVRREFPVVSVVGYTNCGKTTLIRALTGEATLQpRDQPFATLDVTVHEGRLPSRLRVLYVDTIGFLSQLP 346
Cdd:TIGR03156 174 EKQRERQRRRRKRADVPTVALVGYTNAGKSTLFNALTGADVYA-ADQLFATLDPTTRRLDLPDGGEVLLTDTVGFIRDLP 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119  347 HSLIHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLRGLGLR--PALLesaveVHSKVDLVPG-----HTTPCS 419
Cdd:TIGR03156 253 HELVAAFRATLEEVREADLLLHVVDASDPDREEQIEAVEKVLEELGAEdiPQLL-----VYNKIDLLDEprierLEEGYP 327

                         330       340
                  ....*....|....*....|.
gi 209447119  420 GALAVSAVSGRGLDELKAALE 440
Cdd:TIGR03156 328 EAVFVSAKTGEGLDLLLEAIA 348
PRK11058 PRK11058
GTPase HflX; Provisional
 130-373 1.05e-25

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 109.42  E-value: 1.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 130 SSAAPGSRQVFGKGNFRDLTEKIRGCQdiTSVFLNVERMTPQTQKELETAWGLRVFDRFTLVLHIFRCNARTREARMQLA 209
Cdd:PRK11058  48 SRKAPHPKYFVGEGKAVEIAEAVKATG--ASVVLFDHALSPAQERNLERLCECRVIDRTGLILDIFAQRARTHEGKLQVE 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 210 LAEIPLLRSS-VSGDSEQQDQQGW-GSRyimGSGESFSELRARALRDRELRLRRVLERLRDKRRLMRKERVRREFPVVSV 287
Cdd:PRK11058 126 LAQLRHLATRlVRGWTHLERQKGGiGLR---GPGETQLETDRRLLRNRIVQILSRLERVEKQREQGRRARIKADVPTVSL 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 288 VGYTNCGKTTLIRALTgEATLQPRDQPFATLDVTVHEGRLPSRLRVLYVDTIGFLSQLPHSLIHAFSATLEDVAYSDVLV 367
Cdd:PRK11058 203 VGYTNAGKSTLFNRIT-EARVYAADQLFATLDPTLRRIDVADVGETVLADTVGFIRHLPHDLVAAFKATLQETRQATLLL 281


                 ....*.
gi 209447119 368 HVTDVS 373
Cdd:PRK11058 282 HVVDAA 287
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 285-375 2.74e-15

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: 71.88  E-value: 2.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119  285 VSVVGYTNCGKTTLIRALTGEATlQPRDQPFATLDVTVHEGRLPSRlRVLYVDTIGFL--SQLPHSLIHAFSATLEdvay 362
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGAKA-IVSDYPGTTRDPNEGRLELKGK-QIILVDTPGLIegASEGEGLGRAFLAIIE---- 75

                          90
                  ....*....|...
gi 209447119  363 SDVLVHVTDVSHP 375
Cdd:pfam01926  76 ADLILFVVDSEEG 88
 
Name Accession Description Interval E-value
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 83-503 1.84e-73

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 238.83  E-value: 1.84e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119  83 QRVCVLHPDVKRPAGKTPRStaewqVAEAAALVRALpGWSVARTLVVSSAAPGSRQVFGKGNFRDLTEKIRGCqDITSVF 162
Cdd:COG2262    9 ERAILVGVDLPGSDEDAEES-----LEELAELAETA-GAEVVGTVTQRRDKPDPATYIGKGKVEELAELVEEL-EADLVI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 163 LNVErMTPQTQKELETAWGLRVFDRFTLVLHIFRCNARTREARMQLALA----EIPLLRSSVSGDSEQQDqqGWGSRyim 238
Cdd:COG2262   82 FDDE-LSPSQQRNLEKALGVKVIDRTGLILDIFAQRARTREGKLQVELAqlqyLLPRLVGMWTHLSRQGG--GIGTR--- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 239 GSGES------------FSELRARALRDRELrlrrvlerlrdkRRLMRKERVRREFPVVSVVGYTNCGKTTLIRALTGEA 306
Cdd:COG2262  156 GPGETqletdrrlirdrIARLKRELEKVRKQ------------RELQRKRRKRSGIPTVALVGYTNAGKSTLFNRLTGAD 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 307 TLQpRDQPFATLDVTVHEGRLPSRLRVLYVDTIGFLSQLPHSLIHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLS 386
Cdd:COG2262  224 VLA-EDKLFATLDPTTRRLELPDGRPVLLTDTVGFIRKLPHQLVEAFRSTLEEVREADLLLHVVDASDPDFEEQIETVNE 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 387 TLRGLGL--RPALLesaveVHSKVDLVPG-------HTTPcsGALAVSAVSGRGLDELKAALEASVLRATGRQLLTIRVR 457
Cdd:COG2262  303 VLEELGAddKPIIL-----VFNKIDLLDDeelerlrAGYP--DAVFISAKTGEGIDELLEAIEERLPEDRVEVELLLPYS 375

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 209447119 458 LGGpQLGWLYNEAVVQQVQELPEGgaAHVTVVITQAAYGRFQKLFP 503
Cdd:COG2262  376 DGD-LVAWLHEHGEVLSEEYDEDG--TLLTVRLPPEDLARLEAYLV 418
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 270-441 2.64e-61

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: 199.61  E-value: 2.64e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 270 RRLMRKERVRREFPVVSVVGYTNCGKTTLIRALTGEATLqPRDQPFATLDVTVHEGRLPSRLRVLYVDTIGFLSQLPHSL 349
Cdd:cd01878   29 RELQRARRKRSGVPTVALVGYTNAGKSTLFNALTGADVL-AEDQLFATLDPTTRRIKLPGGREVLLTDTVGFIRDLPHQL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 350 IHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLRGLGlrpALLESAVEVHSKVDLVPG--------HTTPcsGA 421
Cdd:cd01878  108 VEAFRSTLEEVAEADLLLHVVDASDPDREEQIETVEEVLKELG---ADDIPIILVLNKIDLLDDeeleerlrAGRP--DA 182

                        170       180
                 ....*....|....*....|
gi 209447119 422 LAVSAVSGRGLDELKAALEA 441
Cdd:cd01878  183 VFISAKTGEGLDLLKEAIEE 202
GTP_HflX TIGR03156
GTP-binding protein HflX; This protein family is one of a number of homologous small, ...
 109-440 1.81e-59

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: 200.01  E-value: 1.81e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119  109 AEAAALVRALpGWSVARTLVVSSAAPGSRQVFGKGNFRDLTEKIRGCqDITSVFLNVErMTPQTQKELETAWGLRVFDRF 188
Cdd:TIGR03156  20 EELAELAETA-GAEVVGTVTQKRSRPDPATYIGKGKVEEIAELVEEL-EADLVIFDHE-LSPSQERNLEKALGCRVIDRT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119  189 TLVLHIFRCNARTREARMQLALAEIPLLRSSVSGDSEQQDQQ--GWGSRyimGSGESFSELRARALRDRELRLRRVLERL 266
Cdd:TIGR03156  97 GLILDIFAQRARTHEGKLQVELAQLKYLLPRLVGGWTHLSRQggGIGTR---GPGETQLETDRRLIRERIAQLKKELEKV 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119  267 RDKRRLMRKERVRREFPVVSVVGYTNCGKTTLIRALTGEATLQpRDQPFATLDVTVHEGRLPSRLRVLYVDTIGFLSQLP 346
Cdd:TIGR03156 174 EKQRERQRRRRKRADVPTVALVGYTNAGKSTLFNALTGADVYA-ADQLFATLDPTTRRLDLPDGGEVLLTDTVGFIRDLP 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119  347 HSLIHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLRGLGLR--PALLesaveVHSKVDLVPG-----HTTPCS 419
Cdd:TIGR03156 253 HELVAAFRATLEEVREADLLLHVVDASDPDREEQIEAVEKVLEELGAEdiPQLL-----VYNKIDLLDEprierLEEGYP 327

                         330       340
                  ....*....|....*....|.
gi 209447119  420 GALAVSAVSGRGLDELKAALE 440
Cdd:TIGR03156 328 EAVFVSAKTGEGLDLLLEAIA 348
PRK11058 PRK11058
GTPase HflX; Provisional
 130-373 1.05e-25

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 109.42  E-value: 1.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 130 SSAAPGSRQVFGKGNFRDLTEKIRGCQdiTSVFLNVERMTPQTQKELETAWGLRVFDRFTLVLHIFRCNARTREARMQLA 209
Cdd:PRK11058  48 SRKAPHPKYFVGEGKAVEIAEAVKATG--ASVVLFDHALSPAQERNLERLCECRVIDRTGLILDIFAQRARTHEGKLQVE 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 210 LAEIPLLRSS-VSGDSEQQDQQGW-GSRyimGSGESFSELRARALRDRELRLRRVLERLRDKRRLMRKERVRREFPVVSV 287
Cdd:PRK11058 126 LAQLRHLATRlVRGWTHLERQKGGiGLR---GPGETQLETDRRLLRNRIVQILSRLERVEKQREQGRRARIKADVPTVSL 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 288 VGYTNCGKTTLIRALTgEATLQPRDQPFATLDVTVHEGRLPSRLRVLYVDTIGFLSQLPHSLIHAFSATLEDVAYSDVLV 367
Cdd:PRK11058 203 VGYTNAGKSTLFNRIT-EARVYAADQLFATLDPTLRRIDVADVGETVLADTVGFIRHLPHDLVAAFKATLQETRQATLLL 281


                 ....*.
gi 209447119 368 HVTDVS 373
Cdd:PRK11058 282 HVVDAA 287
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 285-375 2.74e-15

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: 71.88  E-value: 2.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119  285 VSVVGYTNCGKTTLIRALTGEATlQPRDQPFATLDVTVHEGRLPSRlRVLYVDTIGFL--SQLPHSLIHAFSATLEdvay 362
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGAKA-IVSDYPGTTRDPNEGRLELKGK-QIILVDTPGLIegASEGEGLGRAFLAIIE---- 75

                          90
                  ....*....|...
gi 209447119  363 SDVLVHVTDVSHP 375
Cdd:pfam01926  76 ADLILFVVDSEEG 88
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 287-441 3.07e-14

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: 70.35  E-value: 3.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 287 VVGYTNCGKTTLIRALTGEATLQPRDQPFATLDVTVHEGRLPSRLRVLYVDTIGFLSQlPHSLIHAFSATLEDVAYSDVL 366
Cdd:cd00880    2 IFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRKEWELLPLGPVVLIDTPGLDEE-GGLGRERVEEARQVADRADLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 367 VHVTDVSHPDAELQkaTVLSTLRGLGLrPALLesaveVHSKVDLVPGH------------TTPCSGALAVSAVSGRGLDE 434
Cdd:cd00880   81 LLVVDSDLTPVEEE--AKLGLLRERGK-PVLL-----VLNKIDLVPESeeeellrerkleLLPDLPVIAVSALPGEGIDE 152


                 ....*..
gi 209447119 435 LKAALEA 441
Cdd:cd00880  153 LRKKIAE 159
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 287-439 1.67e-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: 59.78  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 287 VVGYTNCGKTTLIRALTGEATLQPRDQPFATLDVTVHEGRLPSRLR-VLYVDTIGFLSQLPHSLIHAFSATLEDvaySDV 365
Cdd:cd00882    2 VVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKELDKGKVkLVLVDTPGLDEFGGLGREELARLLLRG---ADL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 366 LVHVTDVSHPDAEL-QKATVLSTLRGLGLrPALLesaveVHSKVDLVPGHT------------TPCSGALAVSAVSGRGL 432
Cdd:cd00882   79 ILLVVDSTDRESEEdAKLLILRRLRKEGI-PIIL-----VGNKIDLLEEREveellrleelakILGVPVFEVSAKTGEGV 152


                 ....*..
gi 209447119 433 DELKAAL 439
Cdd:cd00882  153 DELFEKL 159
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
285-452 3.86e-10

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 58.84  E-value: 3.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 285 VSVVGYTNCGKTTLIRALTGEATLQPRDQPfaTLDVTVHEGRLP---SRLRVLYVDTIGflsQLPHSLIHAFSAtlEDVA 361
Cdd:COG1100    6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLS--TNGVTIDKKELKldgLDVDLVIWDTPG---QDEFRETRQFYA--RQLT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 362 YSDVLVHVTDVSHPDAELQKATVLSTLRGLGL-RPALLesaveVHSKVDLVPGH-------------TTPCSGALAVSAV 427
Cdd:COG1100   79 GASLYLFVVDGTREETLQSLYELLESLRRLGKkSPIIL-----VLNKIDLYDEEeiedeerlkealsEDNIVEVVATSAK 153

                        170       180
                 ....*....|....*....|....*
gi 209447119 428 SGRGLDELKAALeASVLRATGRQLL 452
Cdd:COG1100  154 TGEGVEELFAAL-AEILRGEGDSLD 177
GTP-bdg_N pfam13167
GTP-binding GTPase N-terminal; This is the N-terminal region of GTP-binding HflX-like proteins. ...
 109-195 3.96e-10

GTP-binding GTPase N-terminal; This is the N-terminal region of GTP-binding HflX-like proteins. The full-length members bind and interact with the 50S ribosome and are GTPases, hydrolysing GTP/GDP/ATP/ADP. This N-terminal region is necessary for stability of the whole protein.


Pssm-ID: 463797 [Multi-domain]  Cd Length: 87  Bit Score: 56.20  E-value: 3.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119  109 AEAAALVRALpGWSVARTLVVSSAAPGSRQVFGKGNFRDLTEKIRGCqDITSVFLNVErMTPQTQKELETAWGLRVFDRF 188
Cdd:pfam13167   4 EELEELAETA-GAEVVGTVIQKRDKPDPATYIGKGKLEELKELVEAL-EADLVIFDDE-LSPSQQRNLEKALGVKVIDRT 80


                  ....*..
gi 209447119  189 TLVLHIF 195
Cdd:pfam13167  81 GLILDIF 87
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
285-441 2.40e-05

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 46.14  E-value: 2.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 285 VSVVGYTNCGKTTLIRALTGE--ATLQPRDQpfaTldvTVHegrlpsRLR---------VLYVDTIGFlsQLPHSLIHAF 353
Cdd:COG1159    6 VAIVGRPNVGKSTLLNALVGQkvSIVSPKPQ---T---TRH------RIRgivtredaqIVFVDTPGI--HKPKRKLGRR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 354 -----SATLEDVaysDVLVHVTDVSHPDAELQKAtVLSTLRGLGlRPALLesaveVHSKVDLVPGHTT-----------P 417
Cdd:COG1159   72 mnkaaWSALEDV---DVILFVVDATEKIGEGDEF-ILELLKKLK-TPVIL-----VINKIDLVKKEELlpllaeysellD 141

                        170       180
                 ....*....|....*....|....
gi 209447119 418 CSGALAVSAVSGRGLDELKAALEA 441
Cdd:COG1159  142 FAEIVPISALKGDNVDELLDEIAK 165
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 287-439 3.76e-05

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: 43.98  E-value: 3.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 287 VVGYTNCGKTTLIRALTGeaTLQ-----PRdqpfatldVTV--HEGRLPSRLRVLY-VDtigflsqLP--HSLiHAFSAT 356
Cdd:cd01879    2 LVGNPNVGKTTLFNALTG--ARQkvgnwPG--------VTVekKEGEFKLGGKEIEiVD-------LPgtYSL-TPYSED 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 357 lEDVAYS-------DVLVHVTDVSHPD---------AELQKATVL-------STLRGLGLRPALLESA--VEVhskvdlv 411
Cdd:cd01879   64 -EKVARDfllgeepDLIVNVVDATNLErnlyltlqlLELGLPVVValnmideAEKRGIKIDLDKLSELlgVPV------- 135

                        170       180
                 ....*....|....*....|....*...
gi 209447119 412 pghttpcsgaLAVSAVSGRGLDELKAAL 439
Cdd:cd01879  136 ----------VPTSARKGEGIDELLDAI 153
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 363-457 8.61e-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: 8.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 363 SDVLVHVTDVSHPDAELQKAtVLSTLRGlglRPALLesaveVHSKVDLVPGHTTPCS-----GALAVSAVSGRGLDELKA 437
Cdd:COG0486  293 ADLVLLLLDASEPLTEEDEE-ILEKLKD---KPVIV-----VLNKIDLPSEADGELKslpgePVIAISAKTGEGIDELKE 363

                         90       100
                 ....*....|....*....|..
gi 209447119 438 ALEASVLRATGRQ--LLTIRVR 457
Cdd:COG0486  364 AILELVGEGALEGegVLLTNAR 385
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 285-439 1.19e-04

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


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 42.83  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 285 VSVVGYTNCGKTTLIRALTGE--ATLQPRDQpfaTldvTVHegrlpsRLR---------VLYVDTIGFLSQ---LPHSLI 350
Cdd:cd04163    6 VAIIGRPNVGKSTLLNALVGQkiSIVSPKPQ---T---TRN------RIRgiytdddaqIIFVDTPGIHKPkkkLGERMV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 351 HAFSATLEDVaysDVLVHVTDVSHPDAELQKaTVLSTLRGLGlRPALLesaveVHSKVDLVPGHTT------------PC 418
Cdd:cd04163   74 KAAWSALKDV---DLVLFVVDASEWIGEGDE-FILELLKKSK-TPVIL-----VLNKIDLVKDKEDllplleklkelhPF 143

                        170       180
                 ....*....|....*....|.
gi 209447119 419 SGALAVSAVSGRGLDELKAAL 439
Cdd:cd04163  144 AEIFPISALKGENVDELLEYI 164
MobB COG1763
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ...
 283-302 7.24e-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: 40.16  E-value: 7.24e-04
                         10        20
                 ....*....|....*....|
gi 209447119 283 PVVSVVGYTNCGKTTLIRAL 302
Cdd:COG1763    2 PVLGIVGYSGSGKTTLLEKL 21
GTP-bdg_M pfam16360
GTP-binding GTPase Middle Region; This family locates between the N-terminal domain and ...
 199-255 1.25e-03

GTP-binding GTPase Middle Region; This family locates between the N-terminal domain and MMR_HSR1 50S ribosome-binding GTPase of GTP-binding HflX-like proteins. The full-length members bind and interact with the 50S ribosome and are GTPases, hydrolysing GTP/GDP/ATP/ADP. This region is unknown for its function.


Pssm-ID: 465103 [Multi-domain]  Cd Length: 79  Bit Score: 37.80  E-value: 1.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 209447119  199 ARTREARMQLALAEIPLLRSSVSGDSEQQDQQGWGSrYIMGSGESFSELRARALRDR 255
Cdd:pfam16360   2 ARTREAKLQVELAQLKYLLPRLRGMGTHLSRQGGGI-GTRGPGETKLETDRRLIRRR 57
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 270-304 2.05e-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: 2.05e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 209447119 270 RRLMRKERVRREFPVVSVVGYTNCGKTTLIRALTG 304
Cdd:cd01859   87 RRTIKELAIDGKPVIVGVVGYPKVGKSSIINALKG 121
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 285-443 3.16e-03

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: 38.24  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 285 VSVVGYTNCGKTTLIRALTGE--A--TLQP---RDqpfaTLDVTVHEGRLPSRLrvlyVDTIGflsqlphslIH------ 351
Cdd:cd04164    6 VVIAGKPNVGKSSLLNALAGRdrAivSDIAgttRD----VIEEEIDLGGIPVRL----IDTAG---------LRetedei 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 352 -------AFSATLEdvaySDVLVHVTDVSHP-DAELQKATVLSTLRGLglrpallesaVEVHSKVDLVPGHTTPCSGA-- 421
Cdd:cd04164   69 ekigierAREAIEE----ADLVLLVVDASEGlDEEDLEILELPAKKPV----------IVVLNKSDLLSDAEGISELNgk 134

                        170       180
                 ....*....|....*....|....
gi 209447119 422 --LAVSAVSGRGLDELKAALEASV 443
Cdd:cd04164  135 piIAISAKTGEGIDELKEALLELA 158
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 287-373 3.91e-03

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: 38.14  E-value: 3.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 287 VVGYTNCGKTTLIRALTgEATLQPRDQPFATLDVTVHEGRLPSRLRVLYVDTIGfLSQLPHS---LIHAFSATLEDvayS 363
Cdd:cd01881    2 LVGLPNVGKSTLLSALT-SAKVEIASYPFTTLEPNVGVFEFGDGVDIQIIDLPG-LLDGASEgrgLGEQILAHLYR---S 76

                         90
                 ....*....|
gi 209447119 364 DVLVHVTDVS 373
Cdd:cd01881   77 DLILHVIDAS 86
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 363-444 3.93e-03

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


Pssm-ID: 463649 [Multi-domain]  Cd Length: 326  Bit Score: 39.39  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119  363 SDVLVHVTDVSHPDAELQKATvlstLRGLGLRPALlesaVEVHSKVDLVPGHTTPCSGA----LAVSAVSGRGLDELKAA 438
Cdd:pfam12631 174 ADLVLLVLDASRPLDEEDLEI----LELLKDKKPI----IVVLNKSDLLGEIDELEELKgkpvLAISAKTGEGLDELEEA 245


                  ....*.
gi 209447119  439 LEASVL 444
Cdd:pfam12631 246 IKELFL 251
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
274-443 6.96e-03

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 38.94  E-value: 6.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 274 RKERVRREFPVVsVVGYTNCGKTTLIRALTGE--A--------TlqpRDqpfaTLDVTVHEGRLPSRLrvlyVDTIGfls 343
Cdd:PRK05291 208 QGEILREGLKVV-IAGRPNVGKSSLLNALLGEerAivtdiagtT---RD----VIEEHINLDGIPLRL----IDTAG--- 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209447119 344 qlphslIH-------------AFSAtLEDvaySDVLVHVTDVSHPDAELQKATVLSTLRglglRPALLesaveVHSKVDL 410
Cdd:PRK05291 273 ------IRetddevekigierSREA-IEE---ADLVLLVLDASEPLTEEDDEILEELKD----KPVIV-----VLNKADL 333

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 209447119 411 VPGHTTPC---SGALAVSAVSGRGLDELKAALEASV 443
Cdd:PRK05291 334 TGEIDLEEengKPVIRISAKTGEGIDELREAIKELA 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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