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Conserved domains on  [gi|1907159678|ref|XP_036020606|]
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putative GTP-binding protein 6 isoform X2 [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 ...
 113-284 7.26e-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: 196.53  E-value: 7.26e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 113 RRLMRKERVRREFPVVSVVGYTNCGKTTLIQALTGEAALqPRDQPFATLDVTVHAGLLPSRLRILYVDTIGFLSQLPHSL 192
Cdd:cd01878    29 RELQRARRKRSGVPTVALVGYTNAGKSTLFNALTGADVL-AEDQLFATLDPTTRRIKLPGGREVLLTDTVGFIRDLPHQL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 193 IHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLR--GLHLPPallesALEVHSKVDLVPGYTPPCS------GA 264
Cdd:cd01878   108 VEAFRSTLEEVAEADLLLHVVDASDPDREEQIETVEEVLKelGADDIP-----IILVLNKIDLLDDEELEERlragrpDA 182

                         170       180
                  ....*....|....*....|
gi 1907159678 265 LAVSAISGRGLDELKAALEA 284
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 ...
 113-284 7.26e-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: 196.53  E-value: 7.26e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 113 RRLMRKERVRREFPVVSVVGYTNCGKTTLIQALTGEAALqPRDQPFATLDVTVHAGLLPSRLRILYVDTIGFLSQLPHSL 192
Cdd:cd01878    29 RELQRARRKRSGVPTVALVGYTNAGKSTLFNALTGADVL-AEDQLFATLDPTTRRIKLPGGREVLLTDTVGFIRDLPHQL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 193 IHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLR--GLHLPPallesALEVHSKVDLVPGYTPPCS------GA 264
Cdd:cd01878   108 VEAFRSTLEEVAEADLLLHVVDASDPDREEQIETVEEVLKelGADDIP-----IILVLNKIDLLDDEELEERlragrpDA 182

                         170       180
                  ....*....|....*....|
gi 1907159678 265 LAVSAISGRGLDELKAALEA 284
Cdd:cd01878   183 VFISAKTGEGLDLLKEAIEE 202
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 29-346 1.19e-61

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 203.01  E-value: 1.19e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678  29 DRFTLVLHIFRCNARTREARMQLALA----EIPLLRSSVntdsGQQDQQ--GWGSRyimGSGESPTELRaralrdrelrl 102
Cdd:COG2262   104 DRTGLILDIFAQRARTREGKLQVELAqlqyLLPRLVGMW----THLSRQggGIGTR---GPGETQLETD----------- 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 103 rrvlerlrdkRRL---------------------MRKERVRREFPVVSVVGYTNCGKTTLIQALTGEAALQpRDQPFATL 161
Cdd:COG2262   166 ----------RRLirdriarlkrelekvrkqrelQRKRRKRSGIPTVALVGYTNAGKSTLFNRLTGADVLA-EDKLFATL 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 162 DVTVHAGLLPSRLRILYVDTIGFLSQLPHSLIHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLRGL---HLPp 238
Cdd:COG2262   235 DPTTRRLELPDGRPVLLTDTVGFIRKLPHQLVEAFRSTLEEVREADLLLHVVDASDPDFEEQIETVNEVLEELgadDKP- 313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 239 allesALEVHSKVDLVPG-------YTPPcsGALAVSAISGRGLDELKAALEASVLRATGRQVLTLCVRLGGpQLGWLYK 311
Cdd:COG2262   314 -----IILVFNKIDLLDDeelerlrAGYP--DAVFISAKTGEGIDELLEAIEERLPEDRVEVELLLPYSDGD-LVAWLHE 385

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1907159678 312 EAVVQQVQELPEGdaAHVTVVITQAAYGRFRKLFP 346
Cdd:COG2262   386 HGEVLSEEYDEDG--TLLTVRLPPEDLARLEAYLV 418
GTP_HflX TIGR03156
GTP-binding protein HflX; This protein family is one of a number of homologous small, ...
 29-283 9.67e-48

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: 164.57  E-value: 9.67e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678  29 DRFTLVLHIFRCNARTREARMQLALAEIpLLRSSVNTDSGQQ-DQQ--GWGSRyimGSGESPTELRARALRDRELRLRRV 105
Cdd:TIGR03156  94 DRTGLILDIFAQRARTHEGKLQVELAQL-KYLLPRLVGGWTHlSRQggGIGTR---GPGETQLETDRRLIRERIAQLKKE 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 106 LERLRDKRRLMRKERVRREFPVVSVVGYTNCGKTTLIQALTGEAALQpRDQPFATLDVTVHAGLLPSRLRILYVDTIGFL 185
Cdd:TIGR03156 170 LEKVEKQRERQRRRRKRADVPTVALVGYTNAGKSTLFNALTGADVYA-ADQLFATLDPTTRRLDLPDGGEVLLTDTVGFI 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 186 SQLPHSLIHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLRGL---HLPpallesALEVHSKVDLVPGY----- 257
Cdd:TIGR03156 249 RDLPHELVAAFRATLEEVREADLLLHVVDASDPDREEQIEAVEKVLEELgaeDIP------QLLVYNKIDLLDEPrierl 322

                         250       260
                  ....*....|....*....|....*.
gi 1907159678 258 TPPCSGALAVSAISGRGLDELKAALE 283
Cdd:TIGR03156 323 EEGYPEAVFVSAKTGEGLDLLLEAIA 348
PRK11058 PRK11058
GTPase HflX; Provisional
 29-282 1.74e-23

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 100.56  E-value: 1.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678  29 DRFTLVLHIFRCNARTREARMQLALAEIPLLRSSVNTDSGQQDQQ--GWGSRyimGSGESPTELRARALRDRELRLRRVL 106
Cdd:PRK11058  102 DRTGLILDIFAQRARTHEGKLQVELAQLRHLATRLVRGWTHLERQkgGIGLR---GPGETQLETDRRLLRNRIVQILSRL 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 107 ERLRDKRRLMRKERVRREFPVVSVVGYTNCGKTTLIQALTgEAALQPRDQPFATLDVTVHAGLLPSRLRILYVDTIGFLS 186
Cdd:PRK11058  179 ERVEKQREQGRRARIKADVPTVSLVGYTNAGKSTLFNRIT-EARVYAADQLFATLDPTLRRIDVADVGETVLADTVGFIR 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 187 QLPHSLIHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLRGL--HLPPALLesaleVHSKVDLVPGYTPPCSG- 263
Cdd:PRK11058  258 HLPHDLVAAFKATLQETRQATLLLHVVDAADVRVQENIEAVNTVLEEIdaHEIPTLL-----VMNKIDMLDDFEPRIDRd 332

                         250       260
                  ....*....|....*....|....*
gi 1907159678 264 ------ALAVSAISGRGLDELKAAL 282
Cdd:PRK11058  333 eenkpiRVWLSAQTGAGIPLLFQAL 357
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 128-241 5.99e-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: 5.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 128 VSVVGYTNCGKTTLIQALTGEAAlQPRDQPFATLDVTVHAgLLPSRLRILYVDTIGFL--SQLPHSLIHAFSATLEdvay 205
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGAKA-IVSDYPGTTRDPNEGR-LELKGKQIILVDTPGLIegASEGEGLGRAFLAIIE---- 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907159678 206 SDVLVHVTDVSHPdAELQKATVLSTLRGLHLPPALL 241
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 ...
 113-284 7.26e-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: 196.53  E-value: 7.26e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 113 RRLMRKERVRREFPVVSVVGYTNCGKTTLIQALTGEAALqPRDQPFATLDVTVHAGLLPSRLRILYVDTIGFLSQLPHSL 192
Cdd:cd01878    29 RELQRARRKRSGVPTVALVGYTNAGKSTLFNALTGADVL-AEDQLFATLDPTTRRIKLPGGREVLLTDTVGFIRDLPHQL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 193 IHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLR--GLHLPPallesALEVHSKVDLVPGYTPPCS------GA 264
Cdd:cd01878   108 VEAFRSTLEEVAEADLLLHVVDASDPDREEQIETVEEVLKelGADDIP-----IILVLNKIDLLDDEELEERlragrpDA 182

                         170       180
                  ....*....|....*....|
gi 1907159678 265 LAVSAISGRGLDELKAALEA 284
Cdd:cd01878   183 VFISAKTGEGLDLLKEAIEE 202
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 29-346 1.19e-61

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 203.01  E-value: 1.19e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678  29 DRFTLVLHIFRCNARTREARMQLALA----EIPLLRSSVntdsGQQDQQ--GWGSRyimGSGESPTELRaralrdrelrl 102
Cdd:COG2262   104 DRTGLILDIFAQRARTREGKLQVELAqlqyLLPRLVGMW----THLSRQggGIGTR---GPGETQLETD----------- 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 103 rrvlerlrdkRRL---------------------MRKERVRREFPVVSVVGYTNCGKTTLIQALTGEAALQpRDQPFATL 161
Cdd:COG2262   166 ----------RRLirdriarlkrelekvrkqrelQRKRRKRSGIPTVALVGYTNAGKSTLFNRLTGADVLA-EDKLFATL 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 162 DVTVHAGLLPSRLRILYVDTIGFLSQLPHSLIHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLRGL---HLPp 238
Cdd:COG2262   235 DPTTRRLELPDGRPVLLTDTVGFIRKLPHQLVEAFRSTLEEVREADLLLHVVDASDPDFEEQIETVNEVLEELgadDKP- 313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 239 allesALEVHSKVDLVPG-------YTPPcsGALAVSAISGRGLDELKAALEASVLRATGRQVLTLCVRLGGpQLGWLYK 311
Cdd:COG2262   314 -----IILVFNKIDLLDDeelerlrAGYP--DAVFISAKTGEGIDELLEAIEERLPEDRVEVELLLPYSDGD-LVAWLHE 385

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1907159678 312 EAVVQQVQELPEGdaAHVTVVITQAAYGRFRKLFP 346
Cdd:COG2262   386 HGEVLSEEYDEDG--TLLTVRLPPEDLARLEAYLV 418
GTP_HflX TIGR03156
GTP-binding protein HflX; This protein family is one of a number of homologous small, ...
 29-283 9.67e-48

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: 164.57  E-value: 9.67e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678  29 DRFTLVLHIFRCNARTREARMQLALAEIpLLRSSVNTDSGQQ-DQQ--GWGSRyimGSGESPTELRARALRDRELRLRRV 105
Cdd:TIGR03156  94 DRTGLILDIFAQRARTHEGKLQVELAQL-KYLLPRLVGGWTHlSRQggGIGTR---GPGETQLETDRRLIRERIAQLKKE 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 106 LERLRDKRRLMRKERVRREFPVVSVVGYTNCGKTTLIQALTGEAALQpRDQPFATLDVTVHAGLLPSRLRILYVDTIGFL 185
Cdd:TIGR03156 170 LEKVEKQRERQRRRRKRADVPTVALVGYTNAGKSTLFNALTGADVYA-ADQLFATLDPTTRRLDLPDGGEVLLTDTVGFI 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 186 SQLPHSLIHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLRGL---HLPpallesALEVHSKVDLVPGY----- 257
Cdd:TIGR03156 249 RDLPHELVAAFRATLEEVREADLLLHVVDASDPDREEQIEAVEKVLEELgaeDIP------QLLVYNKIDLLDEPrierl 322

                         250       260
                  ....*....|....*....|....*.
gi 1907159678 258 TPPCSGALAVSAISGRGLDELKAALE 283
Cdd:TIGR03156 323 EEGYPEAVFVSAKTGEGLDLLLEAIA 348
PRK11058 PRK11058
GTPase HflX; Provisional
 29-282 1.74e-23

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 100.56  E-value: 1.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678  29 DRFTLVLHIFRCNARTREARMQLALAEIPLLRSSVNTDSGQQDQQ--GWGSRyimGSGESPTELRARALRDRELRLRRVL 106
Cdd:PRK11058  102 DRTGLILDIFAQRARTHEGKLQVELAQLRHLATRLVRGWTHLERQkgGIGLR---GPGETQLETDRRLLRNRIVQILSRL 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 107 ERLRDKRRLMRKERVRREFPVVSVVGYTNCGKTTLIQALTgEAALQPRDQPFATLDVTVHAGLLPSRLRILYVDTIGFLS 186
Cdd:PRK11058  179 ERVEKQREQGRRARIKADVPTVSLVGYTNAGKSTLFNRIT-EARVYAADQLFATLDPTLRRIDVADVGETVLADTVGFIR 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 187 QLPHSLIHAFSATLEDVAYSDVLVHVTDVSHPDAELQKATVLSTLRGL--HLPPALLesaleVHSKVDLVPGYTPPCSG- 263
Cdd:PRK11058  258 HLPHDLVAAFKATLQETRQATLLLHVVDAADVRVQENIEAVNTVLEEIdaHEIPTLL-----VMNKIDMLDDFEPRIDRd 332

                         250       260
                  ....*....|....*....|....*
gi 1907159678 264 ------ALAVSAISGRGLDELKAAL 282
Cdd:PRK11058  333 eenkpiRVWLSAQTGAGIPLLFQAL 357
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 128-241 5.99e-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: 5.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 128 VSVVGYTNCGKTTLIQALTGEAAlQPRDQPFATLDVTVHAgLLPSRLRILYVDTIGFL--SQLPHSLIHAFSATLEdvay 205
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGAKA-IVSDYPGTTRDPNEGR-LELKGKQIILVDTPGLIegASEGEGLGRAFLAIIE---- 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907159678 206 SDVLVHVTDVSHPdAELQKATVLSTLRGLHLPPALL 241
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 ...
 130-284 4.24e-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: 63.42  E-value: 4.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 130 VVGYTNCGKTTLIQALTGEAALQPRDQPFATLDVTVHAGLLPSRLRILYVDTIGFLSQlPHSLIHAFSATLEDVAYSDVL 209
Cdd:cd00880     2 IFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRKEWELLPLGPVVLIDTPGLDEE-GGLGRERVEEARQVADRADLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 210 VHVTDVSHPDAELQkaTVLSTLRGLHLpPALLesaleVHSKVDLVPG------YTPPCSGAL------AVSAISGRGLDE 277
Cdd:cd00880    81 LLVVDSDLTPVEEE--AKLGLLRERGK-PVLL-----VLNKIDLVPEseeeelLRERKLELLpdlpviAVSALPGEGIDE 152


                  ....*..
gi 1907159678 278 LKAALEA 284
Cdd:cd00880   153 LRKKIAE 159
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 130-282 2.40e-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: 2.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 130 VVGYTNCGKTTLIQALTGEAALQPRDQPFATLD-VTVHAGLLPSRLRILYVDTIGFLSQLPHSLIHAFSATLEDvaySDV 208
Cdd:cd00882     2 VVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDpDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELARLLLRG---ADL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 209 LVHVTDVSHPDAELQKATVLSTLRGLHLPPALLesaleVHSKVDLVPGYT------------PPCSGALAVSAISGRGLD 276
Cdd:cd00882    79 ILLVVDSTDRESEEDAKLLILRRLRKEGIPIIL-----VGNKIDLLEEREveellrleelakILGVPVFEVSAKTGEGVD 153


                  ....*.
gi 1907159678 277 ELKAAL 282
Cdd:cd00882   154 ELFEKL 159
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 128-282 5.94e-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: 5.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 128 VSVVGYTNCGKTTLIQALTGE--AALQPRDQpfaTldvTVHagllpsRLR---------ILYVDTIGFLSQ---LPHSLI 193
Cdd:cd04163     6 VAIIGRPNVGKSTLLNALVGQkiSIVSPKPQ---T---TRN------RIRgiytdddaqIIFVDTPGIHKPkkkLGERMV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 194 HAFSATLEDVaysDVLVHVTDVSHPDAELQKaTVLSTLRGLHLPPALlesaleVHSKVDLVP------------GYTPPC 261
Cdd:cd04163    74 KAAWSALKDV---DLVLFVVDASEWIGEGDE-FILELLKKSKTPVIL------VLNKIDLVKdkedllplleklKELHPF 143

                         170       180
                  ....*....|....*....|.
gi 1907159678 262 SGALAVSAISGRGLDELKAAL 282
Cdd:cd04163   144 AEIFPISALKGENVDELLEYI 164
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
128-284 1.36e-06

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 49.22  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 128 VSVVGYTNCGKTTLIQALTGE--AALQPRDQpfaTldvTVHagllpsRLR---------ILYVDTIGFlsQLPHSLIHAF 196
Cdd:COG1159     6 VAIVGRPNVGKSTLLNALVGQkvSIVSPKPQ---T---TRH------RIRgivtredaqIVFVDTPGI--HKPKRKLGRR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 197 -----SATLEDVaysDVLVHVTDVSHPDAELQKAtVLSTLRGLHLP-------------PALLESALEVHSKVD---LVP 255
Cdd:COG1159    72 mnkaaWSALEDV---DVILFVVDATEKIGEGDEF-ILELLKKLKTPvilvinkidlvkkEELLPLLAEYSELLDfaeIVP 147

                         170       180
                  ....*....|....*....|....*....
gi 1907159678 256 gytppcsgalaVSAISGRGLDELKAALEA 284
Cdd:COG1159   148 -----------ISALKGDNVDELLDEIAK 165
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
128-292 2.49e-06

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 47.28  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 128 VSVVGYTNCGKTTLIQALTGEAALQPRDQPfaTLDVTVHAGLLP---SRLRILYVDTIGflsQLPHSLIHAFSAtlEDVA 204
Cdd:COG1100     6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLS--TNGVTIDKKELKldgLDVDLVIWDTPG---QDEFRETRQFYA--RQLT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 205 YSDVLVHVTDVSHPDAELQKATVLSTLRGLHLP-PALLesaleVHSKVDLVPGY-------------TPPCSGALAVSAI 270
Cdd:COG1100    79 GASLYLFVVDGTREETLQSLYELLESLRRLGKKsPIIL-----VLNKIDLYDEEeiedeerlkealsEDNIVEVVATSAK 153

                         170       180
                  ....*....|....*....|..
gi 1907159678 271 SGRGLDELKAALeASVLRATGR 292
Cdd:COG1100   154 TGEGVEELFAAL-AEILRGEGD 174
era PRK00089
GTPase Era; Reviewed
 128-284 3.27e-05

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 45.04  E-value: 3.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 128 VSVVGYTNCGKTTLIQALTGE--AALQPRDQpfaTldvTVHagllpsRLR---------ILYVDTIGFlsQLPHSLIH-- 194
Cdd:PRK00089    8 VAIVGRPNVGKSTLLNALVGQkiSIVSPKPQ---T---TRH------RIRgivteddaqIIFVDTPGI--HKPKRALNra 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 195 ---AFSATLEDVaysDVLVHVTDVSH---PDAELqkatVLSTLRGLHLP-----------------PALLESALEVHSKV 251
Cdd:PRK00089   74 mnkAAWSSLKDV---DLVLFVVDADEkigPGDEF----ILEKLKKVKTPvilvlnkidlvkdkeelLPLLEELSELMDFA 146

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1907159678 252 DLVPgytppcsgalaVSAISGRGLDELKAALEA 284
Cdd:PRK00089  147 EIVP-----------ISALKGDNVDELLDVIAK 168
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 127-282 3.29e-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: 43.59  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 127 VVSVVGYTNCGKTTLIQALTGeAALQ----PRdqpfatldVTV---HAGLLPSRLRILYVDTIGflsqlphslIHAFSAT 199
Cdd:pfam02421   2 TIALVGNPNVGKTTLFNALTG-ANQHvgnwPG--------VTVekkEGKFKYKGYEIEIVDLPG---------IYSLSPY 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 200 LED--VAYS-------DVLVHVTDVSHPD---------AELQKATVL-------STLRGLHLPPALLESALEVhskvdlv 254
Cdd:pfam02421  64 SEEerVARDyllnekpDVIVNVVDATNLErnlyltlqlLELGLPVVLalnmmdeAEKKGIKIDIKKLSELLGV------- 136

                         170       180
                  ....*....|....*....|....*...
gi 1907159678 255 pgytpPCsgaLAVSAISGRGLDELKAAL 282
Cdd:pfam02421 137 -----PV---VPTSARKGEGIDELLDAI 156
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 119-286 3.40e-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: 45.44  E-value: 3.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 119 ERVRREFPVVsVVGYTNCGKTTLIQALTG-EAAL---QP---RDqpfaTLDVTVHAGLLPsrLRIlyVDTIGflsqlphs 191
Cdd:COG0486   208 ELLREGIKVV-IVGRPNVGKSSLLNALLGeERAIvtdIAgttRD----VIEERINIGGIP--VRL--IDTAG-------- 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 192 lIH-------------AFSAtLEDvaySDVLVHVTDVSHPDAELQKAtVLSTLRGLHLppallesaLEVHSKVDLVPGYT 258
Cdd:COG0486   271 -LRetedevekigierAREA-IEE---ADLVLLLLDASEPLTEEDEE-ILEKLKDKPV--------IVVLNKIDLPSEAD 336

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1907159678 259 PPCS-----GALAVSAISGRGLDELKAALEASV 286
Cdd:COG0486   337 GELKslpgePVIAISAKTGEGIDELKEAILELV 369
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 128-286 1.52e-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: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 128 VSVVGYTNCGKTTLIQALTG-EAAL---QP---RDqpfaTLDVTVHAGLLPSRLrilyVDTIGflsqlphslIH------ 194
Cdd:cd04164     6 VVIAGKPNVGKSSLLNALAGrDRAIvsdIAgttRD----VIEEEIDLGGIPVRL----IDTAG---------LRetedei 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 195 -------AFSATLEdvaySDVLVHVTDVSHP-DAELQKATVLSTLRGLHLppallesaleVHSKVDLVPGYTPPCSGA-- 264
Cdd:cd04164    69 ekigierAREAIEE----ADLVLLVVDASEGlDEEDLEILELPAKKPVIV----------VLNKSDLLSDAEGISELNgk 134

                         170       180
                  ....*....|....*....|....
gi 1907159678 265 --LAVSAISGRGLDELKAALEASV 286
Cdd:cd04164   135 piIAISAKTGEGIDELKEALLELA 158
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 120-287 1.85e-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: 42.85  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 120 RVRREFPVVSVVGYTNCGKTTLIQALTG-EAAL---QP---RDqpfaTLDVTVHAGLLPsrLRIlyVDTIGflsqlphsl 192
Cdd:pfam12631  89 RILREGIKVVIVGKPNVGKSSLLNALLGeERAIvtdIPgttRD----VIEETINIGGIP--LRL--IDTAG--------- 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 193 IHAfsaTLEDV------------AYSDVLVHVTDVSHPDAELQKATVLSTLRGLHLppallesaLEVHSKVDLVPGYTPP 260
Cdd:pfam12631 152 IRE---TDDEVekigierareaiEEADLVLLVLDASRPLDEEDLEILELLKDKKPI--------IVVLNKSDLLGEIDEL 220

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1907159678 261 CSGA----LAVSAISGRGLDELKAALEASVL 287
Cdd:pfam12631 221 EELKgkpvLAISAKTGEGLDELEEAIKELFL 251
MobB COG1763
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ...
 126-145 4.87e-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: 4.87e-04
                          10        20
                  ....*....|....*....|
gi 1907159678 126 PVVSVVGYTNCGKTTLIQAL 145
Cdd:COG1763     2 PVLGIVGYSGSGKTTLLEKL 21
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 113-147 6.25e-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: 6.25e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1907159678 113 RRLMRKERVRREFPVVSVVGYTNCGKTTLIQALTG 147
Cdd:cd01859    87 RRTIKELAIDGKPVIVGVVGYPKVGKSSIINALKG 121
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 130-216 9.25e-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: 9.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 130 VVGYTNCGKTTLIQALTgEAALQPRDQPFATLdvTVHAGLLPSR--LRILYVDTIGfLSQLPHS---LIHAFSATLEDva 204
Cdd:cd01881     2 LVGLPNVGKSTLLSALT-SAKVEIASYPFTTL--EPNVGVFEFGdgVDIQIIDLPG-LLDGASEgrgLGEQILAHLYR-- 75

                          90
                  ....*....|..
gi 1907159678 205 ySDVLVHVTDVS 216
Cdd:cd01881    76 -SDLILHVIDAS 86
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
117-286 2.24e-03

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 39.71  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 117 RKERVRREFPVVsVVGYTNCGKTTLIQALTG-EAAL---QP---RDqpfaTLDVTVHAGLLPSRLrilyVDTIGflsqlp 189
Cdd:PRK05291  208 QGEILREGLKVV-IAGRPNVGKSSLLNALLGeERAIvtdIAgttRD----VIEEHINLDGIPLRL----IDTAG------ 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 190 hslIH-------------AFSAtLEDvaySDVLVHVTDVSHPDAELQKAtvlstlrglHLPPALLESALEVHSKVDLVP- 255
Cdd:PRK05291  273 ---IRetddevekigierSREA-IEE---ADLVLLVLDASEPLTEEDDE---------ILEELKDKPVIVVLNKADLTGe 336

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1907159678 256 --GYTPPCSGALAVSAISGRGLDELKAALEASV 286
Cdd:PRK05291  337 idLEEENGKPVIRISAKTGEGIDELREAIKELA 369
EutP COG4917
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ...
 130-283 2.68e-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: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 130 VVGYTNCGKTTLIQALTGEAALQPRDQpfatlDVTVHAGLL--PS------RLR---ILY---VDTIGFL-------SQL 188
Cdd:COG4917     6 LIGRSGAGKTTLTQALNGEELEYRKTQ-----AVEYYDNIIdtPGeyienpRFYkalIATaqdADVIVLVqdateprSVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907159678 189 PHSLIHAFSatledvaySDVLVHVTDVSHPDAELQKATvlstlrglhlppALLESAlevhskvdlvpGYTPPcsgaLAVS 268
Cdd:COG4917    81 PPGFAKAFN--------KPVIGVITKIDLPEADVERAR------------KWLKSA-----------GVEPI----FIVS 125

                         170
                  ....*....|....*
gi 1907159678 269 AISGRGLDELKAALE 283
Cdd:COG4917   126 SVTGEGIEELKEYLE 140
 
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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