NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|445990749|ref|WP_000068604|]
View 

GTPase HflX [Staphylococcus aureus]

Protein Classification

HflX GTPase family protein( domain architecture ID 11455136)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 8-412 2.41e-180

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


:

Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 508.47  E-value: 2.41e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749   8 DIKIKLEKAVLVGVHAQDDKQfNFESTMEELSSLSETCQLEVLGQITQNRDRVDRKYYVGKGKIEEIQAFIEFKDIDVVI 87
Cdd:COG2262    3 EREERGERAILVGVDLPGSDE-DAEESLEELAELAETAGAEVVGTVTQRRDKPDPATYIGKGKVEELAELVEELEADLVI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749  88 TNDELTTAQSKSLNEALGVKIIDRTQLILEIFALRARSKEGKLQVELAQLDYLLPRLQGHGKSLSRLgggigtrgpgETK 167
Cdd:COG2262   82 FDDELSPSQQRNLEKALGVKVIDRTGLILDIFAQRARTREGKLQVELAQLQYLLPRLVGMWTHLSRQgggigtrgpgETQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 168 LEMDRRHIRTRMNEIKHQLRTVEEHRERYRNKRNQNQVFQVALVGYTNAGKSSWFNVLANEETYEKDQLFATLDPKTRQI 247
Cdd:COG2262  162 LETDRRLIRDRIARLKRELEKVRKQRELQRKRRKRSGIPTVALVGYTNAGKSTLFNRLTGADVLAEDKLFATLDPTTRRL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 248 QINDGFNLIISDTVGFIQKLPTTLIAAFKSTLEEAKGADLLVHVVDSSHPEYRTQYDTVNDLIKQLDMSHISQIVIFNKK 327
Cdd:COG2262  242 ELPDGRPVLLTDTVGFIRKLPHQLVEAFRSTLEEVREADLLLHVVDASDPDFEEQIETVNEVLEELGADDKPIILVFNKI 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 328 DLCDHAS-NRPASDLPN-VFVSSKNDGDKLLVKTLFIDEIKRQLTYYDEAIATNNADRLYFLKQHTLVTELKYDEIENVY 405
Cdd:COG2262  322 DLLDDEElERLRAGYPDaVFISAKTGEGIDELLEAIEERLPEDRVEVELLLPYSDGDLVAWLHEHGEVLSEEYDEDGTLL 401


                 ....*..
gi 445990749 406 RIKGFKK 412
Cdd:COG2262  402 TVRLPPE 408
 
Name Accession Description Interval E-value
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 8-412 2.41e-180

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 508.47  E-value: 2.41e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749   8 DIKIKLEKAVLVGVHAQDDKQfNFESTMEELSSLSETCQLEVLGQITQNRDRVDRKYYVGKGKIEEIQAFIEFKDIDVVI 87
Cdd:COG2262    3 EREERGERAILVGVDLPGSDE-DAEESLEELAELAETAGAEVVGTVTQRRDKPDPATYIGKGKVEELAELVEELEADLVI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749  88 TNDELTTAQSKSLNEALGVKIIDRTQLILEIFALRARSKEGKLQVELAQLDYLLPRLQGHGKSLSRLgggigtrgpgETK 167
Cdd:COG2262   82 FDDELSPSQQRNLEKALGVKVIDRTGLILDIFAQRARTREGKLQVELAQLQYLLPRLVGMWTHLSRQgggigtrgpgETQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 168 LEMDRRHIRTRMNEIKHQLRTVEEHRERYRNKRNQNQVFQVALVGYTNAGKSSWFNVLANEETYEKDQLFATLDPKTRQI 247
Cdd:COG2262  162 LETDRRLIRDRIARLKRELEKVRKQRELQRKRRKRSGIPTVALVGYTNAGKSTLFNRLTGADVLAEDKLFATLDPTTRRL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 248 QINDGFNLIISDTVGFIQKLPTTLIAAFKSTLEEAKGADLLVHVVDSSHPEYRTQYDTVNDLIKQLDMSHISQIVIFNKK 327
Cdd:COG2262  242 ELPDGRPVLLTDTVGFIRKLPHQLVEAFRSTLEEVREADLLLHVVDASDPDFEEQIETVNEVLEELGADDKPIILVFNKI 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 328 DLCDHAS-NRPASDLPN-VFVSSKNDGDKLLVKTLFIDEIKRQLTYYDEAIATNNADRLYFLKQHTLVTELKYDEIENVY 405
Cdd:COG2262  322 DLLDDEElERLRAGYPDaVFISAKTGEGIDELLEAIEERLPEDRVEVELLLPYSDGDLVAWLHEHGEVLSEEYDEDGTLL 401


                 ....*..
gi 445990749 406 RIKGFKK 412
Cdd:COG2262  402 TVRLPPE 408
GTP_HflX TIGR03156
GTP-binding protein HflX; This protein family is one of a number of homologous small, ...
 15-360 5.09e-171

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: 481.97  E-value: 5.09e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749   15 KAVLVGVHAQDDKQFnfESTMEELSSLSETCQLEVLGQITQNRDRVDRKYYVGKGKIEEIQAFIEFKDIDVVITNDELTT 94
Cdd:TIGR03156   1 RAILVGVDLGNEDDE--EESLEELAELAETAGAEVVGTVTQKRSRPDPATYIGKGKVEEIAELVEELEADLVIFDHELSP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749   95 AQSKSLNEALGVKIIDRTQLILEIFALRARSKEGKLQVELAQLDYLLPRLQGHGKSLSRLGGGIGTRGPGETKLEMDRRH 174
Cdd:TIGR03156  79 SQERNLEKALGCRVIDRTGLILDIFAQRARTHEGKLQVELAQLKYLLPRLVGGWTHLSRQGGGIGTRGPGETQLETDRRL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749  175 IRTRMNEIKHQLRTVEEHRERYRNKRNQNQVFQVALVGYTNAGKSSWFNVLANEETYEKDQLFATLDPKTRQIQINDGFN 254
Cdd:TIGR03156 159 IRERIAQLKKELEKVEKQRERQRRRRKRADVPTVALVGYTNAGKSTLFNALTGADVYAADQLFATLDPTTRRLDLPDGGE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749  255 LIISDTVGFIQKLPTTLIAAFKSTLEEAKGADLLVHVVDSSHPEYRTQYDTVNDLIKQLDMSHISQIVIFNKKDLCDHAS 334
Cdd:TIGR03156 239 VLLTDTVGFIRDLPHELVAAFRATLEEVREADLLLHVVDASDPDREEQIEAVEKVLEELGAEDIPQLLVYNKIDLLDEPR 318

                         330       340
                  ....*....|....*....|....*....
gi 445990749  335 NRPASDLPN--VFVSSKN-DGDKLLVKTL 360
Cdd:TIGR03156 319 IERLEEGYPeaVFVSAKTgEGLDLLLEAI 347
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 165-350 3.14e-94

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: 281.27  E-value: 3.14e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 165 ETKLEMDRRHIRTRMNEIKHQLRTVEEHRERYRNKRNQNQVFQVALVGYTNAGKSSWFNVLANEETYEKDQLFATLDPKT 244
Cdd:cd01878    1 ETQLETDRRLIRERIAKLRKELEKVKKQRELQRARRKRSGVPTVALVGYTNAGKSTLFNALTGADVLAEDQLFATLDPTT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 245 RQIQINDGFNLIISDTVGFIQKLPTTLIAAFKSTLEEAKGADLLVHVVDSSHPEYRTQYDTVNDLIKQLDMSHISQIVIF 324
Cdd:cd01878   81 RRIKLPGGREVLLTDTVGFIRDLPHQLVEAFRSTLEEVAEADLLLHVVDASDPDREEQIETVEEVLKELGADDIPIILVL 160

                        170       180
                 ....*....|....*....|....*....
gi 445990749 325 NKKDLCD---HASNRPASDLPNVFVSSKN 350
Cdd:cd01878  161 NKIDLLDdeeLEERLRAGRPDAVFISAKT 189
PRK11058 PRK11058
GTPase HflX; Provisional
 14-360 7.44e-81

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 255.03  E-value: 7.44e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749  14 EKAVLVGVHAQDDKQFNfesTMEELSSLSETCQLEVLGQITQNRDRVDRKYYVGKGKIEEIQAFIEFKDIDVVITNDELT 93
Cdd:PRK11058   9 EQAVLVHIYFSQDKDME---DLQEFESLVSSAGVEALQVITGSRKAPHPKYFVGEGKAVEIAEAVKATGASVVLFDHALS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749  94 TAQSKSLNEALGVKIIDRTQLILEIFALRARSKEGKLQVELAQLDYLLPRLQGHGKSLSRLGGGIGTRGPGETKLEMDRR 173
Cdd:PRK11058  86 PAQERNLERLCECRVIDRTGLILDIFAQRARTHEGKLQVELAQLRHLATRLVRGWTHLERQKGGIGLRGPGETQLETDRR 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 174 HIRTRMNEIKHQLRTVEEHRERYRNKRNQNQVFQVALVGYTNAGKSSWFNVLANEETYEKDQLFATLDPKTRQIQINDGF 253
Cdd:PRK11058 166 LLRNRIVQILSRLERVEKQREQGRRARIKADVPTVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVADVG 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 254 NLIISDTVGFIQKLPTTLIAAFKSTLEEAKGADLLVHVVDSSHPEYRTQYDTVNDLIKQLDMSHISQIVIFNKKDLCDHA 333
Cdd:PRK11058 246 ETVLADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVVDAADVRVQENIEAVNTVLEEIDAHEIPTLLVMNKIDMLDDF 325

                        330       340       350
                 ....*....|....*....|....*....|..
gi 445990749 334 SNRPASDLPN----VFVSSKN-DGDKLLVKTL 360
Cdd:PRK11058 326 EPRIDRDEENkpirVWLSAQTgAGIPLLFQAL 357
GTP-bdg_N pfam13167
GTP-binding GTPase N-terminal; This is the N-terminal region of GTP-binding HflX-like proteins. ...
 35-119 3.49e-38

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: 132.86  E-value: 3.49e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749   35 MEELSSLSETCQLEVLGQITQNRDRVDRKYYVGKGKIEEIQAFIEFKDIDVVITNDELTTAQSKSLNEALGVKIIDRTQL 114
Cdd:pfam13167   3 LEELEELAETAGAEVVGTVIQKRDKPDPATYIGKGKLEELKELVEALEADLVIFDDELSPSQQRNLEKALGVKVIDRTGL 82


                  ....*
gi 445990749  115 ILEIF 119
Cdd:pfam13167  83 ILDIF 87
 
Name Accession Description Interval E-value
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 8-412 2.41e-180

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 508.47  E-value: 2.41e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749   8 DIKIKLEKAVLVGVHAQDDKQfNFESTMEELSSLSETCQLEVLGQITQNRDRVDRKYYVGKGKIEEIQAFIEFKDIDVVI 87
Cdd:COG2262    3 EREERGERAILVGVDLPGSDE-DAEESLEELAELAETAGAEVVGTVTQRRDKPDPATYIGKGKVEELAELVEELEADLVI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749  88 TNDELTTAQSKSLNEALGVKIIDRTQLILEIFALRARSKEGKLQVELAQLDYLLPRLQGHGKSLSRLgggigtrgpgETK 167
Cdd:COG2262   82 FDDELSPSQQRNLEKALGVKVIDRTGLILDIFAQRARTREGKLQVELAQLQYLLPRLVGMWTHLSRQgggigtrgpgETQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 168 LEMDRRHIRTRMNEIKHQLRTVEEHRERYRNKRNQNQVFQVALVGYTNAGKSSWFNVLANEETYEKDQLFATLDPKTRQI 247
Cdd:COG2262  162 LETDRRLIRDRIARLKRELEKVRKQRELQRKRRKRSGIPTVALVGYTNAGKSTLFNRLTGADVLAEDKLFATLDPTTRRL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 248 QINDGFNLIISDTVGFIQKLPTTLIAAFKSTLEEAKGADLLVHVVDSSHPEYRTQYDTVNDLIKQLDMSHISQIVIFNKK 327
Cdd:COG2262  242 ELPDGRPVLLTDTVGFIRKLPHQLVEAFRSTLEEVREADLLLHVVDASDPDFEEQIETVNEVLEELGADDKPIILVFNKI 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 328 DLCDHAS-NRPASDLPN-VFVSSKNDGDKLLVKTLFIDEIKRQLTYYDEAIATNNADRLYFLKQHTLVTELKYDEIENVY 405
Cdd:COG2262  322 DLLDDEElERLRAGYPDaVFISAKTGEGIDELLEAIEERLPEDRVEVELLLPYSDGDLVAWLHEHGEVLSEEYDEDGTLL 401


                 ....*..
gi 445990749 406 RIKGFKK 412
Cdd:COG2262  402 TVRLPPE 408
GTP_HflX TIGR03156
GTP-binding protein HflX; This protein family is one of a number of homologous small, ...
 15-360 5.09e-171

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: 481.97  E-value: 5.09e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749   15 KAVLVGVHAQDDKQFnfESTMEELSSLSETCQLEVLGQITQNRDRVDRKYYVGKGKIEEIQAFIEFKDIDVVITNDELTT 94
Cdd:TIGR03156   1 RAILVGVDLGNEDDE--EESLEELAELAETAGAEVVGTVTQKRSRPDPATYIGKGKVEEIAELVEELEADLVIFDHELSP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749   95 AQSKSLNEALGVKIIDRTQLILEIFALRARSKEGKLQVELAQLDYLLPRLQGHGKSLSRLGGGIGTRGPGETKLEMDRRH 174
Cdd:TIGR03156  79 SQERNLEKALGCRVIDRTGLILDIFAQRARTHEGKLQVELAQLKYLLPRLVGGWTHLSRQGGGIGTRGPGETQLETDRRL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749  175 IRTRMNEIKHQLRTVEEHRERYRNKRNQNQVFQVALVGYTNAGKSSWFNVLANEETYEKDQLFATLDPKTRQIQINDGFN 254
Cdd:TIGR03156 159 IRERIAQLKKELEKVEKQRERQRRRRKRADVPTVALVGYTNAGKSTLFNALTGADVYAADQLFATLDPTTRRLDLPDGGE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749  255 LIISDTVGFIQKLPTTLIAAFKSTLEEAKGADLLVHVVDSSHPEYRTQYDTVNDLIKQLDMSHISQIVIFNKKDLCDHAS 334
Cdd:TIGR03156 239 VLLTDTVGFIRDLPHELVAAFRATLEEVREADLLLHVVDASDPDREEQIEAVEKVLEELGAEDIPQLLVYNKIDLLDEPR 318

                         330       340
                  ....*....|....*....|....*....
gi 445990749  335 NRPASDLPN--VFVSSKN-DGDKLLVKTL 360
Cdd:TIGR03156 319 IERLEEGYPeaVFVSAKTgEGLDLLLEAI 347
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 165-350 3.14e-94

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: 281.27  E-value: 3.14e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 165 ETKLEMDRRHIRTRMNEIKHQLRTVEEHRERYRNKRNQNQVFQVALVGYTNAGKSSWFNVLANEETYEKDQLFATLDPKT 244
Cdd:cd01878    1 ETQLETDRRLIRERIAKLRKELEKVKKQRELQRARRKRSGVPTVALVGYTNAGKSTLFNALTGADVLAEDQLFATLDPTT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 245 RQIQINDGFNLIISDTVGFIQKLPTTLIAAFKSTLEEAKGADLLVHVVDSSHPEYRTQYDTVNDLIKQLDMSHISQIVIF 324
Cdd:cd01878   81 RRIKLPGGREVLLTDTVGFIRDLPHQLVEAFRSTLEEVAEADLLLHVVDASDPDREEQIETVEEVLKELGADDIPIILVL 160

                        170       180
                 ....*....|....*....|....*....
gi 445990749 325 NKKDLCD---HASNRPASDLPNVFVSSKN 350
Cdd:cd01878  161 NKIDLLDdeeLEERLRAGRPDAVFISAKT 189
PRK11058 PRK11058
GTPase HflX; Provisional
 14-360 7.44e-81

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 255.03  E-value: 7.44e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749  14 EKAVLVGVHAQDDKQFNfesTMEELSSLSETCQLEVLGQITQNRDRVDRKYYVGKGKIEEIQAFIEFKDIDVVITNDELT 93
Cdd:PRK11058   9 EQAVLVHIYFSQDKDME---DLQEFESLVSSAGVEALQVITGSRKAPHPKYFVGEGKAVEIAEAVKATGASVVLFDHALS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749  94 TAQSKSLNEALGVKIIDRTQLILEIFALRARSKEGKLQVELAQLDYLLPRLQGHGKSLSRLGGGIGTRGPGETKLEMDRR 173
Cdd:PRK11058  86 PAQERNLERLCECRVIDRTGLILDIFAQRARTHEGKLQVELAQLRHLATRLVRGWTHLERQKGGIGLRGPGETQLETDRR 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 174 HIRTRMNEIKHQLRTVEEHRERYRNKRNQNQVFQVALVGYTNAGKSSWFNVLANEETYEKDQLFATLDPKTRQIQINDGF 253
Cdd:PRK11058 166 LLRNRIVQILSRLERVEKQREQGRRARIKADVPTVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVADVG 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 254 NLIISDTVGFIQKLPTTLIAAFKSTLEEAKGADLLVHVVDSSHPEYRTQYDTVNDLIKQLDMSHISQIVIFNKKDLCDHA 333
Cdd:PRK11058 246 ETVLADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVVDAADVRVQENIEAVNTVLEEIDAHEIPTLLVMNKIDMLDDF 325

                        330       340       350
                 ....*....|....*....|....*....|..
gi 445990749 334 SNRPASDLPN----VFVSSKN-DGDKLLVKTL 360
Cdd:PRK11058 326 EPRIDRDEENkpirVWLSAQTgAGIPLLFQAL 357
GTP-bdg_N pfam13167
GTP-binding GTPase N-terminal; This is the N-terminal region of GTP-binding HflX-like proteins. ...
 35-119 3.49e-38

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: 132.86  E-value: 3.49e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749   35 MEELSSLSETCQLEVLGQITQNRDRVDRKYYVGKGKIEEIQAFIEFKDIDVVITNDELTTAQSKSLNEALGVKIIDRTQL 114
Cdd:pfam13167   3 LEELEELAETAGAEVVGTVIQKRDKPDPATYIGKGKLEELKELVEALEADLVIFDDELSPSQQRNLEKALGVKVIDRTGL 82


                  ....*
gi 445990749  115 ILEIF 119
Cdd:pfam13167  83 ILDIF 87
GTP-bdg_M pfam16360
GTP-binding GTPase Middle Region; This family locates between the N-terminal domain and ...
 122-200 2.32e-29

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: 109.07  E-value: 2.32e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445990749  122 RARSKEGKLQVELAQLDYLLPRLQGHGKSLSRLGGGIGTRGPGETKLEMDRRHIRTRMNEIKHQLRTVEEHRERYRNKR 200
Cdd:pfam16360   1 RARTREAKLQVELAQLKYLLPRLRGMGTHLSRQGGGIGTRGPGETKLETDRRLIRRRIAKLKKELEKVRKQRELQRKRR 79
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 207-326 2.15e-22

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: 91.14  E-value: 2.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749  207 QVALVGYTNAGKSSWFNVLANEETYEKDQLFATLDPKTRQIQInDGFNLIISDTVGFIQKLPT--TLIAAFKSTLEeakg 284
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLEL-KGKQIILVDTPGLIEGASEgeGLGRAFLAIIE---- 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 445990749  285 ADLLVHVVDSSHPeyRTQYDtvNDLIKQLDMSHISQIVIFNK 326
Cdd:pfam01926  76 ADLILFVVDSEEG--ITPLD--EELLELLRENKKPIILVLNK 113
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
169-360 7.39e-16

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 79.00  E-value: 7.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 169 EMDRRHIRTRMNEIKHQLrtvEEHRERYRNKRNQNQVFQVALVGYTNAGKSSWFNVLANEE---------Tyekdqlfat 239
Cdd:PRK05291 182 FLSDEKILEKLEELIAEL---EALLASARQGEILREGLKVVIAGRPNVGKSSLLNALLGEEraivtdiagT--------- 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 240 ldpkTR-----QIQInDGFNLIISDTVGF-----------IQKlpttliaafksTLEEAKGADLLVHVVDSSHPeyrtqy 303
Cdd:PRK05291 250 ----TRdvieeHINL-DGIPLRLIDTAGIretddevekigIER-----------SREAIEEADLVLLVLDASEP------ 307

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 445990749 304 DTVNDLIKQLDMSHISQIVIFNKKDLCDHASNRPASDLPNVFVSSKN-DGDKLLVKTL 360
Cdd:PRK05291 308 LTEEDDEILEELKDKPVIVVLNKADLTGEIDLEEENGKPVIRISAKTgEGIDELREAI 365
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 206-360 1.02e-14

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: 71.37  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 206 FQVALVGYTNAGKSSWFNVLANEE---------TyekdqlfatldpkTR-----QIQInDGFNLIISDTVGF-------- 263
Cdd:cd04164    4 IKVVIAGKPNVGKSSLLNALAGRDraivsdiagT-------------TRdvieeEIDL-GGIPVRLIDTAGLretedeie 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 264 ---IQKlpttliaafksTLEEAKGADLLVHVVDSSHPEyrtqydTVNDLIKQLDMSHISQIVIFNKKDLCDHASNRPASD 340
Cdd:cd04164   70 kigIER-----------AREAIEEADLVLLVVDASEGL------DEEDLEILELPAKKPVIVVLNKSDLLSDAEGISELN 132

                        170       180
                 ....*....|....*....|..
gi 445990749 341 LPN-VFVSSKN-DGDKLLVKTL 360
Cdd:cd04164  133 GKPiIAISAKTgEGIDELKEAL 154
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 209-372 2.86e-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: 69.97  E-value: 2.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 209 ALVGYTNAGKSSWFNVLANEETYE-KDQLFATLDPKTRQIQINDGFNLIISDTVGFIQKlPTTLIAAFKSTLEEAKGADL 287
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGIvSPIPGTTRDPVRKEWELLPLGPVVLIDTPGLDEE-GGLGRERVEEARQVADRADL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 288 LVHVVDSSHPEYRtQYDTVNDLIKqldmSHISQIVIFNKKDLCDHASNRPA---------SDLPNVFVSSKNDGDkllvk 358
Cdd:cd00880   80 VLLVVDSDLTPVE-EEAKLGLLRE----RGKPVLLVLNKIDLVPESEEEELlrerklellPDLPVIAVSALPGEG----- 149

                        170
                 ....*....|....
gi 445990749 359 tlfIDEIKRQLTYY 372
Cdd:cd00880  150 ---IDELRKKIAEL 160
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 169-379 3.58e-14

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: 73.94  E-value: 3.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 169 EMDRRHIRTRMNEIKHQLrtvEEHRERYRNKRNQNQVFQVALVGYTNAGKSSWFNVLANEE---------Tyekdqlfat 239
Cdd:COG0486  180 FLDREELLERLEELREEL---EALLASARQGELLREGIKVVIVGRPNVGKSSLLNALLGEEraivtdiagT--------- 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 240 ldpkTR-----QIQInDGFNLIISDTVGF-----------IQKlpttliaafksTLEEAKGADLLVHVVDSSHPEyrtqY 303
Cdd:COG0486  248 ----TRdvieeRINI-GGIPVRLIDTAGLretedevekigIER-----------AREAIEEADLVLLLLDASEPL----T 307

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445990749 304 DTVNDLIKQLDMSHIsqIVIFNKKDLCDHASN--RPASDLPNVFVSSK-NDGDKLLVKTLfIDEIKRQLTYYDEAIATN 379
Cdd:COG0486  308 EEDEEILEKLKDKPV--IVVLNKIDLPSEADGelKSLPGEPVIAISAKtGEGIDELKEAI-LELVGEGALEGEGVLLTN 383
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 169-379 5.66e-14

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: 72.13  E-value: 5.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749  169 EMDRRHIRTRMNEIKHQLrtvEEHRERYRNKRNQNQVFQVALVGYTNAGKSSWFNVLANEE---------Tyekdqlfat 239
Cdd:pfam12631  61 ELTEEELLERLEELLAEL---EKLLATADRGRILREGIKVVIVGKPNVGKSSLLNALLGEEraivtdipgT--------- 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749  240 ldpkTR-----QIQInDGFNLIISDTVGF-----------IQKlpttliaafksTLEEAKGADLLVHVVDSSHPEyrTQY 303
Cdd:pfam12631 129 ----TRdvieeTINI-GGIPLRLIDTAGIretddevekigIER-----------AREAIEEADLVLLVLDASRPL--DEE 190

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445990749  304 DTvNDLIKQLDMSHIsqIVIFNKKDLCDHASNRP-ASDLPNVFVSSKN-DGDKLLVKTLFiDEIKRQLTYYDEAIATN 379
Cdd:pfam12631 191 DL-EILELLKDKKPI--IVVLNKSDLLGEIDELEeLKGKPVLAISAKTgEGLDELEEAIK-ELFLAGEIASDGPIITN 264
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 209-350 1.34e-11

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: 62.47  E-value: 1.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 209 ALVGYTNAGKSSWFNVLANEETYEKDQLFA-TLDPKTRQIQIN-DGFNLIISDTVGFIQKLPTTLiaaFKSTLEEAKGAD 286
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGtTRDPDVYVKELDkGKVKLVLVDTPGLDEFGGLGR---EELARLLLRGAD 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445990749 287 LLVHVVDSShpEYRTQYDTVNDLIKQLDMSHISQIVIFNKKDLCDHASNRPA---------SDLPNVFVSSKN 350
Cdd:cd00882   78 LILLVVDST--DRESEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELlrleelakiLGVPVFEVSAKT 148
YeeP COG3596
Predicted GTPase [General function prediction only];
177-329 3.17e-10

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 60.94  E-value: 3.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 177 TRMNEIKHQLRTVEEH-RERYRNKRNQNQVFQVALVGYTNAGKSSWFNVLANEETYEKDQlfatLDPKTRQIQI-----N 250
Cdd:COG3596   10 ERLEALKRLPQVLRELlAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGV----GRPCTREIQRyrlesD 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445990749 251 DGFNLIISDTVGFIQKLPTTliAAFKSTLEEAKGADLLVHVVDSSHPEYRTQYDTVNDLIKQLDMSHIsqIVIFNKKDL 329
Cdd:COG3596   86 GLPGLVLLDTPGLGEVNERD--REYRELRELLPEADLILWVVKADDRALATDEEFLQALRAQYPDPPV--LVVLTQVDR 160
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 209-335 1.84e-08

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: 53.55  E-value: 1.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 209 ALVGYTNAGKSSWFNVLANEETYEKDQLFATLDPKTRQIQINDGFNLIISDTVGFIQKLPT--TLIAAFKSTLEEakgAD 286
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDGVDIQIIDLPGLLDGASEgrGLGEQILAHLYR---SD 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 445990749 287 LLVHVVDSSHPEYR---TQYDTVNDLIK--QLDMSHISQIVIFNKKDLCDHASN 335
Cdd:cd01881   78 LILHVIDASEDCVGdplEDQKTLNEEVSgsFLFLKNKPEMIVANKIDMASENNL 131
Arl10_like cd04159
Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from ...
 208-334 4.32e-06

Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from a human cancer-derived EST dataset. No functional information about the subfamily is available at the current time, but crystal structures of human Arl10b and Arl10c have been solved.


Pssm-ID: 206724 [Multi-domain]  Cd Length: 159  Bit Score: 46.54  E-value: 4.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 208 VALVGYTNAGKSSWFNVLANEETYEkdQLFATLDPKTRQIQINdGFNLIISDTVGfiQklpttliAAFKSTLEE-AKGAD 286
Cdd:cd04159    2 ITLVGLQNSGKTTLVNVIASGQFSE--DTIPTVGFNMRKVTKG-NVTIKVWDLGG--Q-------PRFRSMWERyCRGVN 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 445990749 287 LLVHVVDSSHPE-YRTQYDTVNDLIKQLDMSHISQIVIFNKKDLCDHAS 334
Cdd:cd04159   70 AIVYVVDAADREkLEVAKNELHDLLEKPSLEGIPLLVLGNKNDLPGALS 118
obgE PRK12299
GTPase CgtA; Reviewed
 208-368 6.58e-06

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 47.76  E-value: 6.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 208 VALVGYTNAGKSSWFNVLANEET----YEkdqlFATLDPKTRQIQINDGFNLIISDTVGFIqklpttliaafkstlEEA- 282
Cdd:PRK12299 161 VGLVGLPNAGKSTLISAVSAAKPkiadYP----FTTLHPNLGVVRVDDYKSFVIADIPGLI---------------EGAs 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 283 KGADL-------------LVHVVDSSHPEYRTQYDTVNDLIKQLD--MSHISQIVIFNKKDLCDH--------ASNRPAS 339
Cdd:PRK12299 222 EGAGLghrflkhiertrlLLHLVDIEAVDPVEDYKTIRNELEKYSpeLADKPRILVLNKIDLLDEeeerekraALELAAL 301

                        170       180       190
                 ....*....|....*....|....*....|..
gi 445990749 340 DLPNVFVSS-KNDGDKLLVKTL--FIDEIKRQ 368
Cdd:PRK12299 302 GGPVFLISAvTGEGLDELLRALweLLEEARRE 333
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 208-331 6.94e-06

Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain.


Pssm-ID: 206685 [Multi-domain]  Cd Length: 170  Bit Score: 45.88  E-value: 6.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 208 VALVGYTNAGKSSWFNVLANEET----YEkdqlFATLDPKTRQIQINDGFNLIISDTVGFIqklpttliaafkstleeaK 283
Cdd:cd01898    3 VGLVGLPNAGKSTLLSAISNAKPkiadYP----FTTLVPNLGVVRVDDGRSFVIADIPGLI------------------E 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445990749 284 GAD-----------------LLVHVVDSSHPE-YRTQYDTVNDLIKQ--LDMSHISQIVIFNKKDLCD 331
Cdd:cd01898   61 GASegkglghrflrhiertrVLLHVIDLSGEDdPVEDYETIRNELEAynPGLAEKPRIVVLNKIDLLD 128
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 207-331 1.90e-05

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 46.71  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 207 QVALVGYTNAGKSSWFNVLANEETYEKDQLFA-TLDPKTRQIQInDGFNLIISDTVGFIQKLPTTLIAAFKSTLEEA--- 282
Cdd:PRK09518 452 RVALVGRPNVGKSSLLNQLTHEERAVVNDLAGtTRDPVDEIVEI-DGEDWLFIDTAGIKRRQHKLTGAEYYSSLRTQaai 530

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 445990749 283 KGADLLVHVVDSSHPeyrtqydtvndlIKQLDMSHISQIV--------IFNKKDLCD 331
Cdd:PRK09518 531 ERSELALFLFDASQP------------ISEQDLKVMSMAVdagralvlVFNKWDLMD 575
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 208-334 2.34e-05

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: 44.37  E-value: 2.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 208 VALVGYTNAGKSSWFNVLANEE---TYEKDQlfaTldpkTRQ----IQINDGFNLIISDTVGFIQ---KLPTTLIAAFKS 277
Cdd:cd04163    6 VAIIGRPNVGKSTLLNALVGQKisiVSPKPQ---T----TRNrirgIYTDDDAQIIFVDTPGIHKpkkKLGERMVKAAWS 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 445990749 278 TLEEakgADLLVHVVDSSHPeyRTQYD-TVNDLIKQLDMSHisqIVIFNKKDLCDHAS 334
Cdd:cd04163   79 ALKD---VDLVLFVVDASEW--IGEGDeFILELLKKSKTPV---ILVLNKIDLVKDKE 128
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 207-328 3.15e-05

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


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 44.04  E-value: 3.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 207 QVALVGYTNAGKSSWFNVLaneeTYEKDQLFATLDP-KTRQI---QINDGFNLIisDTVGFI-QKLPTTLIAAFKST--- 278
Cdd:cd01876    1 EVAFAGRSNVGKSSLINAL----TNRKKLARTSKTPgRTQLInffNVGDKFRLV--DLPGYGyAKVSKEVREKWGKLiee 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 445990749 279 -LEEAKGADLLVHVVDSSHPEyrTQYDtvNDLIKQLDMSHISQIVIFNKKD 328
Cdd:cd01876   75 yLENRENLKGVVLLIDARHGP--TPID--LEMLEFLEELGIPFLIVLTKAD 121
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
207-306 9.64e-05

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 44.02  E-value: 9.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 207 QVALVGYTNAGKSSWFNVLANEET----YEkdqlFATLDP-------KTRQIQINDGFNLII--SDTVGFIQKlpttLIA 273
Cdd:COG1163   65 TVVLVGFPSVGKSTLLNKLTNAKSevgaYE----FTTLDVvpgmleyKGAKIQILDVPGLIEgaASGKGRGKE----VLS 136

                         90       100       110
                 ....*....|....*....|....*....|...
gi 445990749 274 AfkstleeAKGADLLVHVVDSSHPEyrtQYDTV 306
Cdd:COG1163  137 V-------VRNADLILIVLDVFELE---QYDVL 159
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
207-329 1.37e-03

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 39.58  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 207 QVALVGYTNAGKSSwfnvLAN---EETYEKDQLFATLDPKTRQIQI---NDGFNLIISDTVG--FIQKLPTTLIAAFKst 278
Cdd:COG1100    5 KIVVVGTGGVGKTS----LVNrlvGDIFSLEKYLSTNGVTIDKKELkldGLDVDLVIWDTPGqdEFRETRQFYARQLT-- 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 445990749 279 leeakGADLLVHVVDSSHPEYRTQYDTVNDLIKQLDMsHISQIVIFNKKDL 329
Cdd:COG1100   79 -----GASLYLFVVDGTREETLQSLYELLESLRRLGK-KSPIILVLNKIDL 123
era PRK00089
GTPase Era; Reviewed
 208-329 1.45e-03

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 40.42  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445990749 208 VALVGYTNAGKSSWFNVLANEE---TYEKDQlfaTldpkTRQ----IQINDGFNLIISDTVGFIQ---KLPTTLIAAFKS 277
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQKisiVSPKPQ---T----TRHrirgIVTEDDAQIIFVDTPGIHKpkrALNRAMNKAAWS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 445990749 278 TLEEakgADLLVHVVDSSHPeYRTQYDTVNDLIKQLDMSHisqIVIFNKKDL 329
Cdd:PRK00089  81 SLKD---VDLVLFVVDADEK-IGPGDEFILEKLKKVKTPV---ILVLNKIDL 125
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
 268-333 2.86e-03

cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino acid sequence of YjiA protein in E. coli contains several conserved motifs that characterizes it as a P-loop GTPase. YijA gene is among the genes significantly induced in response to DNA-damage caused by mitomycin. YijA gene is a homologue of the CobW gene which encodes the cobalamin synthesis protein/P47K.


Pssm-ID: 349766  Cd Length: 198  Bit Score: 38.66  E-value: 2.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445990749 268 PTTLIAAFKSTLEEAKGADL--LVHVVDSSH-PEYRTQYDTVNDLIKQLDMSHIsqiVIFNKKDLCDHA 333
Cdd:cd03112   98 PGPIAQTLWSDEELESRLRLdgVVTVVDAKNfLKQLDEEDVSDLAVDQIAFADV---IVLNKTDLVDEE 163
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH