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Conserved domains on  [gi|493579264|ref|WP_006532354|]
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GTPase HflX [Streptococcus infantarius]

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

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List of domain hits

 Name Accession Description Interval E-value
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 1-410 0e+00

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


:

Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 555.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264   1 MIETSEHQERVILLGVELPDT-ENFDMSMEELASLAKTAGAQVVSSYRQKREKYDSKSLIGSGKLAEIKAIVDADEIDTV 79
Cdd:COG2262    1 MFEREERGERAILVGVDLPGSdEDAEESLEELAELAETAGAEVVGTVTQRRDKPDPATYIGKGKVEELAELVEELEADLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264  80 IVNDRLTPRQNVNLESELGVKVIDRMQLILDIFAMRARSHEGKLQVHLAQLKYMLPRLVGQGVMLSRQAGGIGSRGPGES 159
Cdd:COG2262   81 IFDDELSPSQQRNLEKALGVKVIDRTGLILDIFAQRARTREGKLQVELAQLQYLLPRLVGMWTHLSRQGGGIGTRGPGET 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 160 QLELNRRSIRNQISDIERQLKVVEKNRETGREKRTESQVFKIGLIGYTNAGKSTIMNVLTNDKQYEADELFATLDATTKQ 239
Cdd:COG2262  161 QLETDRRLIRDRIARLKRELEKVRKQRELQRKRRKRSGIPTVALVGYTNAGKSTLFNRLTGADVLAEDKLFATLDPTTRR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 240 IYLQNQFQVTLTDTVGFIQNLPTELVAAFKSTLEENRHVDLLLHVIDASDPNHAEHEKVVLNLLKDLDMLDIPRLAVYNK 319
Cdd:COG2262  241 LELPDGRPVLLTDTVGFIRKLPHQLVEAFRSTLEEVREADLLLHVVDASDPDFEEQIETVNEVLEELGADDKPIILVFNK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 320 MDVAEH----FAATAFPN-VRISARDKDARSLLRRLIINEMREIFEPFSIRVHQNQAYKLYDLNKIALLDRYDFVEEYEN 394
Cdd:COG2262  321 IDLLDDeeleRLRAGYPDaVFISAKTGEGIDELLEAIEERLPEDRVEVELLLPYSDGDLVAWLHEHGEVLSEEYDEDGTL 400

                        410
                 ....*....|....*.
gi 493579264 395 ITGYINPKNKWRLEEF 410
Cdd:COG2262  401 LTVRLPPEDLARLEAY 416
 
Name Accession Description Interval E-value
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 1-410 0e+00

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 555.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264   1 MIETSEHQERVILLGVELPDT-ENFDMSMEELASLAKTAGAQVVSSYRQKREKYDSKSLIGSGKLAEIKAIVDADEIDTV 79
Cdd:COG2262    1 MFEREERGERAILVGVDLPGSdEDAEESLEELAELAETAGAEVVGTVTQRRDKPDPATYIGKGKVEELAELVEELEADLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264  80 IVNDRLTPRQNVNLESELGVKVIDRMQLILDIFAMRARSHEGKLQVHLAQLKYMLPRLVGQGVMLSRQAGGIGSRGPGES 159
Cdd:COG2262   81 IFDDELSPSQQRNLEKALGVKVIDRTGLILDIFAQRARTREGKLQVELAQLQYLLPRLVGMWTHLSRQGGGIGTRGPGET 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 160 QLELNRRSIRNQISDIERQLKVVEKNRETGREKRTESQVFKIGLIGYTNAGKSTIMNVLTNDKQYEADELFATLDATTKQ 239
Cdd:COG2262  161 QLETDRRLIRDRIARLKRELEKVRKQRELQRKRRKRSGIPTVALVGYTNAGKSTLFNRLTGADVLAEDKLFATLDPTTRR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 240 IYLQNQFQVTLTDTVGFIQNLPTELVAAFKSTLEENRHVDLLLHVIDASDPNHAEHEKVVLNLLKDLDMLDIPRLAVYNK 319
Cdd:COG2262  241 LELPDGRPVLLTDTVGFIRKLPHQLVEAFRSTLEEVREADLLLHVVDASDPDFEEQIETVNEVLEELGADDKPIILVFNK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 320 MDVAEH----FAATAFPN-VRISARDKDARSLLRRLIINEMREIFEPFSIRVHQNQAYKLYDLNKIALLDRYDFVEEYEN 394
Cdd:COG2262  321 IDLLDDeeleRLRAGYPDaVFISAKTGEGIDELLEAIEERLPEDRVEVELLLPYSDGDLVAWLHEHGEVLSEEYDEDGTL 400

                        410
                 ....*....|....*.
gi 493579264 395 ITGYINPKNKWRLEEF 410
Cdd:COG2262  401 LTVRLPPEDLARLEAY 416
GTP_HflX TIGR03156
GTP-binding protein HflX; This protein family is one of a number of homologous small, ...
 10-355 0e+00

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: 515.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264   10 RVILLGVELPDTENFDMSMEELASLAKTAGAQVVSSYRQKREKYDSKSLIGSGKLAEIKAIVDADEIDTVIVNDRLTPRQ 89
Cdd:TIGR03156   1 RAILVGVDLGNEDDEEESLEELAELAETAGAEVVGTVTQKRSRPDPATYIGKGKVEEIAELVEELEADLVIFDHELSPSQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264   90 NVNLESELGVKVIDRMQLILDIFAMRARSHEGKLQVHLAQLKYMLPRLVGQGVMLSRQAGGIGSRGPGESQLELNRRSIR 169
Cdd:TIGR03156  81 ERNLEKALGCRVIDRTGLILDIFAQRARTHEGKLQVELAQLKYLLPRLVGGWTHLSRQGGGIGTRGPGETQLETDRRLIR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264  170 NQISDIERQLKVVEKNRETGREKRTESQVFKIGLIGYTNAGKSTIMNVLTNDKQYEADELFATLDATTKQIYLQNQFQVT 249
Cdd:TIGR03156 161 ERIAQLKKELEKVEKQRERQRRRRKRADVPTVALVGYTNAGKSTLFNALTGADVYAADQLFATLDPTTRRLDLPDGGEVL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264  250 LTDTVGFIQNLPTELVAAFKSTLEENRHVDLLLHVIDASDPNHAEHEKVVLNLLKDLDMLDIPRLAVYNKMDVA--EHFA 327
Cdd:TIGR03156 241 LTDTVGFIRDLPHELVAAFRATLEEVREADLLLHVVDASDPDREEQIEAVEKVLEELGAEDIPQLLVYNKIDLLdePRIE 320

                         330       340       350
                  ....*....|....*....|....*....|.
gi 493579264  328 ATAFPN---VRISARDKDARSLLRRLIINEM 355
Cdd:TIGR03156 321 RLEEGYpeaVFVSAKTGEGLDLLLEAIAERL 351
PRK11058 PRK11058
GTPase HflX; Provisional
 1-326 8.48e-96

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 293.55  E-value: 8.48e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264   1 MIETSEHQERVILLGVELP---DTENfdmsMEELASLAKTAGAQVVSSYRQKREKYDSKSLIGSGKLAEIKAIVDADEID 77
Cdd:PRK11058   1 MFDRYEAGEQAVLVHIYFSqdkDMED----LQEFESLVSSAGVEALQVITGSRKAPHPKYFVGEGKAVEIAEAVKATGAS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264  78 TVIVNDRLTPRQNVNLESELGVKVIDRMQLILDIFAMRARSHEGKLQVHLAQLKYMLPRLVGQGVMLSRQAGGIGSRGPG 157
Cdd:PRK11058  77 VVLFDHALSPAQERNLERLCECRVIDRTGLILDIFAQRARTHEGKLQVELAQLRHLATRLVRGWTHLERQKGGIGLRGPG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 158 ESQLELNRRSIRNQISDIERQLKVVEKNRETGREKRTESQVFKIGLIGYTNAGKSTIMNVLTNDKQYEADELFATLDATT 237
Cdd:PRK11058 157 ETQLETDRRLLRNRIVQILSRLERVEKQREQGRRARIKADVPTVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 238 KQIYLQNQFQVTLTDTVGFIQNLPTELVAAFKSTLEENRHVDLLLHVIDASDPNHAEHEKVVLNLLKDLDMLDIPRLAVY 317
Cdd:PRK11058 237 RRIDVADVGETVLADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVVDAADVRVQENIEAVNTVLEEIDAHEIPTLLVM 316


                 ....*....
gi 493579264 318 NKMDVAEHF 326
Cdd:PRK11058 317 NKIDMLDDF 325
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 158-355 1.13e-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: 282.43  E-value: 1.13e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 158 ESQLELNRRSIRNQISDIERQLKVVEKNRETGREKRTESQVFKIGLIGYTNAGKSTIMNVLTNDKQYEADELFATLDATT 237
Cdd:cd01878    1 ETQLETDRRLIRERIAKLRKELEKVKKQRELQRARRKRSGVPTVALVGYTNAGKSTLFNALTGADVLAEDQLFATLDPTT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 238 KQIYLQNQFQVTLTDTVGFIQNLPTELVAAFKSTLEENRHVDLLLHVIDASDPNHAEHEKVVLNLLKDLDMLDIPRLAVY 317
Cdd:cd01878   81 RRIKLPGGREVLLTDTVGFIRDLPHQLVEAFRSTLEEVAEADLLLHVVDASDPDREEQIETVEEVLKELGADDIPIILVL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 493579264 318 NKMD------VAEHFAATAFPNVRISARDKDARSLLRRLIINEM 355
Cdd:cd01878  161 NKIDllddeeLEERLRAGRPDAVFISAKTGEGLDLLKEAIEELL 204
GTP-bdg_N pfam13167
GTP-binding GTPase N-terminal; This is the N-terminal region of GTP-binding HflX-like proteins. ...
 27-112 1.98e-39

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: 135.94  E-value: 1.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264   27 SMEELASLAKTAGAQVVSSYRQKREKYDSKSLIGSGKLAEIKAIVDADEIDTVIVNDRLTPRQNVNLESELGVKVIDRMQ 106
Cdd:pfam13167   2 SLEELEELAETAGAEVVGTVIQKRDKPDPATYIGKGKLEELKELVEALEADLVIFDDELSPSQQRNLEKALGVKVIDRTG 81


                  ....*.
gi 493579264  107 LILDIF 112
Cdd:pfam13167  82 LILDIF 87
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
 200-322 5.36e-04

Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene required for transport of secretory proteins from the endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 197556 [Multi-domain]  Cd Length: 184  Bit Score: 40.69  E-value: 5.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264   200 KIGLIGYTNAGKSTIMNVLTNDKqyeADELFATLDATTKQIYLQNqFQVTLTDTVGFIQnlptelvaAFKSTLEENRHVD 279
Cdd:smart00178  19 KILFLGLDNAGKTTLLHMLKNDR---LAQHQPTQHPTSEELAIGN-IKFTTFDLGGHQQ--------ARRLWKDYFPEVN 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 493579264   280 LLLHVIDASDPNHAEHEKVVLN-LLKDLDMLDIPRLAVYNKMDV 322
Cdd:smart00178  87 GIVYLVDAYDKERFAESKRELDaLLSDEELATVPFLILGNKIDA 130
 
Name Accession Description Interval E-value
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 1-410 0e+00

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 555.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264   1 MIETSEHQERVILLGVELPDT-ENFDMSMEELASLAKTAGAQVVSSYRQKREKYDSKSLIGSGKLAEIKAIVDADEIDTV 79
Cdd:COG2262    1 MFEREERGERAILVGVDLPGSdEDAEESLEELAELAETAGAEVVGTVTQRRDKPDPATYIGKGKVEELAELVEELEADLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264  80 IVNDRLTPRQNVNLESELGVKVIDRMQLILDIFAMRARSHEGKLQVHLAQLKYMLPRLVGQGVMLSRQAGGIGSRGPGES 159
Cdd:COG2262   81 IFDDELSPSQQRNLEKALGVKVIDRTGLILDIFAQRARTREGKLQVELAQLQYLLPRLVGMWTHLSRQGGGIGTRGPGET 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 160 QLELNRRSIRNQISDIERQLKVVEKNRETGREKRTESQVFKIGLIGYTNAGKSTIMNVLTNDKQYEADELFATLDATTKQ 239
Cdd:COG2262  161 QLETDRRLIRDRIARLKRELEKVRKQRELQRKRRKRSGIPTVALVGYTNAGKSTLFNRLTGADVLAEDKLFATLDPTTRR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 240 IYLQNQFQVTLTDTVGFIQNLPTELVAAFKSTLEENRHVDLLLHVIDASDPNHAEHEKVVLNLLKDLDMLDIPRLAVYNK 319
Cdd:COG2262  241 LELPDGRPVLLTDTVGFIRKLPHQLVEAFRSTLEEVREADLLLHVVDASDPDFEEQIETVNEVLEELGADDKPIILVFNK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 320 MDVAEH----FAATAFPN-VRISARDKDARSLLRRLIINEMREIFEPFSIRVHQNQAYKLYDLNKIALLDRYDFVEEYEN 394
Cdd:COG2262  321 IDLLDDeeleRLRAGYPDaVFISAKTGEGIDELLEAIEERLPEDRVEVELLLPYSDGDLVAWLHEHGEVLSEEYDEDGTL 400

                        410
                 ....*....|....*.
gi 493579264 395 ITGYINPKNKWRLEEF 410
Cdd:COG2262  401 LTVRLPPEDLARLEAY 416
GTP_HflX TIGR03156
GTP-binding protein HflX; This protein family is one of a number of homologous small, ...
 10-355 0e+00

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: 515.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264   10 RVILLGVELPDTENFDMSMEELASLAKTAGAQVVSSYRQKREKYDSKSLIGSGKLAEIKAIVDADEIDTVIVNDRLTPRQ 89
Cdd:TIGR03156   1 RAILVGVDLGNEDDEEESLEELAELAETAGAEVVGTVTQKRSRPDPATYIGKGKVEEIAELVEELEADLVIFDHELSPSQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264   90 NVNLESELGVKVIDRMQLILDIFAMRARSHEGKLQVHLAQLKYMLPRLVGQGVMLSRQAGGIGSRGPGESQLELNRRSIR 169
Cdd:TIGR03156  81 ERNLEKALGCRVIDRTGLILDIFAQRARTHEGKLQVELAQLKYLLPRLVGGWTHLSRQGGGIGTRGPGETQLETDRRLIR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264  170 NQISDIERQLKVVEKNRETGREKRTESQVFKIGLIGYTNAGKSTIMNVLTNDKQYEADELFATLDATTKQIYLQNQFQVT 249
Cdd:TIGR03156 161 ERIAQLKKELEKVEKQRERQRRRRKRADVPTVALVGYTNAGKSTLFNALTGADVYAADQLFATLDPTTRRLDLPDGGEVL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264  250 LTDTVGFIQNLPTELVAAFKSTLEENRHVDLLLHVIDASDPNHAEHEKVVLNLLKDLDMLDIPRLAVYNKMDVA--EHFA 327
Cdd:TIGR03156 241 LTDTVGFIRDLPHELVAAFRATLEEVREADLLLHVVDASDPDREEQIEAVEKVLEELGAEDIPQLLVYNKIDLLdePRIE 320

                         330       340       350
                  ....*....|....*....|....*....|.
gi 493579264  328 ATAFPN---VRISARDKDARSLLRRLIINEM 355
Cdd:TIGR03156 321 RLEEGYpeaVFVSAKTGEGLDLLLEAIAERL 351
PRK11058 PRK11058
GTPase HflX; Provisional
 1-326 8.48e-96

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 293.55  E-value: 8.48e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264   1 MIETSEHQERVILLGVELP---DTENfdmsMEELASLAKTAGAQVVSSYRQKREKYDSKSLIGSGKLAEIKAIVDADEID 77
Cdd:PRK11058   1 MFDRYEAGEQAVLVHIYFSqdkDMED----LQEFESLVSSAGVEALQVITGSRKAPHPKYFVGEGKAVEIAEAVKATGAS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264  78 TVIVNDRLTPRQNVNLESELGVKVIDRMQLILDIFAMRARSHEGKLQVHLAQLKYMLPRLVGQGVMLSRQAGGIGSRGPG 157
Cdd:PRK11058  77 VVLFDHALSPAQERNLERLCECRVIDRTGLILDIFAQRARTHEGKLQVELAQLRHLATRLVRGWTHLERQKGGIGLRGPG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 158 ESQLELNRRSIRNQISDIERQLKVVEKNRETGREKRTESQVFKIGLIGYTNAGKSTIMNVLTNDKQYEADELFATLDATT 237
Cdd:PRK11058 157 ETQLETDRRLLRNRIVQILSRLERVEKQREQGRRARIKADVPTVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 238 KQIYLQNQFQVTLTDTVGFIQNLPTELVAAFKSTLEENRHVDLLLHVIDASDPNHAEHEKVVLNLLKDLDMLDIPRLAVY 317
Cdd:PRK11058 237 RRIDVADVGETVLADTVGFIRHLPHDLVAAFKATLQETRQATLLLHVVDAADVRVQENIEAVNTVLEEIDAHEIPTLLVM 316


                 ....*....
gi 493579264 318 NKMDVAEHF 326
Cdd:PRK11058 317 NKIDMLDDF 325
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 158-355 1.13e-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: 282.43  E-value: 1.13e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 158 ESQLELNRRSIRNQISDIERQLKVVEKNRETGREKRTESQVFKIGLIGYTNAGKSTIMNVLTNDKQYEADELFATLDATT 237
Cdd:cd01878    1 ETQLETDRRLIRERIAKLRKELEKVKKQRELQRARRKRSGVPTVALVGYTNAGKSTLFNALTGADVLAEDQLFATLDPTT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 238 KQIYLQNQFQVTLTDTVGFIQNLPTELVAAFKSTLEENRHVDLLLHVIDASDPNHAEHEKVVLNLLKDLDMLDIPRLAVY 317
Cdd:cd01878   81 RRIKLPGGREVLLTDTVGFIRDLPHQLVEAFRSTLEEVAEADLLLHVVDASDPDREEQIETVEEVLKELGADDIPIILVL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 493579264 318 NKMD------VAEHFAATAFPNVRISARDKDARSLLRRLIINEM 355
Cdd:cd01878  161 NKIDllddeeLEERLRAGRPDAVFISAKTGEGLDLLKEAIEELL 204
GTP-bdg_N pfam13167
GTP-binding GTPase N-terminal; This is the N-terminal region of GTP-binding HflX-like proteins. ...
 27-112 1.98e-39

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: 135.94  E-value: 1.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264   27 SMEELASLAKTAGAQVVSSYRQKREKYDSKSLIGSGKLAEIKAIVDADEIDTVIVNDRLTPRQNVNLESELGVKVIDRMQ 106
Cdd:pfam13167   2 SLEELEELAETAGAEVVGTVIQKRDKPDPATYIGKGKLEELKELVEALEADLVIFDDELSPSQQRNLEKALGVKVIDRTG 81


                  ....*.
gi 493579264  107 LILDIF 112
Cdd:pfam13167  82 LILDIF 87
GTP-bdg_M pfam16360
GTP-binding GTPase Middle Region; This family locates between the N-terminal domain and ...
 115-193 2.61e-39

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: 135.26  E-value: 2.61e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493579264  115 RARSHEGKLQVHLAQLKYMLPRLVGQGVMLSRQAGGIGSRGPGESQLELNRRSIRNQISDIERQLKVVEKNRETGREKR 193
Cdd:pfam16360   1 RARTREAKLQVELAQLKYLLPRLRGMGTHLSRQGGGIGTRGPGETKLETDRRLIRRRIAKLKKELEKVRKQRELQRKRR 79
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 200-319 9.57e-25

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: 97.69  E-value: 9.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264  200 KIGLIGYTNAGKSTIMNVLTNDKQYEADELFATLDATTKQIYLQNQfQVTLTDTVGFIQNLPTE--LVAAFKSTLEenrh 277
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGK-QIILVDTPGLIEGASEGegLGRAFLAIIE---- 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 493579264  278 VDLLLHVIDASDPnhaeHEKVVLNLLKDLDMLDIPRLAVYNK 319
Cdd:pfam01926  76 ADLILFVVDSEEG----ITPLDEELLELLRENKKPIILVLNK 113
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 202-353 1.24e-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: 71.12  E-value: 1.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 202 GLIGYTNAGKSTIMNVLTNDKQYEADEL-FATLDATTKQIYLQNQFQVTLTDTVGFIQNlPTELVAAFKSTLEENRHVDL 280
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGIVSPIpGTTRDPVRKEWELLPLGPVVLIDTPGLDEE-GGLGRERVEEARQVADRADL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 281 LLHVIDASDPNHaEHEKVVLNLLKdldmLDIPRLAVYNKMDV---AEHFAATAF---------PNVRISARDKDARSLLR 348
Cdd:cd00880   80 VLLVVDSDLTPV-EEEAKLGLLRE----RGKPVLLVLNKIDLvpeSEEEELLRErklellpdlPVIAVSALPGEGIDELR 154


                 ....*
gi 493579264 349 RLIIN 353
Cdd:cd00880  155 KKIAE 159
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 202-357 9.90e-13

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: 65.56  E-value: 9.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 202 GLIGYTNAGKSTIMNVLTNDKQYE-ADELFATLDATTKQIYLQ-NQFQVTLTDTVGFIQNLPTELVAAFKSTLEEnrhVD 279
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEvSDVPGTTRDPDVYVKELDkGKVKLVLVDTPGLDEFGGLGREELARLLLRG---AD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 280 LLLHVIDASDPNHAEHEKvvLNLLKDLDMLDIPRLAVYNKMDVAEHFAATAFPNVRISARDKDAR----SLLRRLIINEM 355
Cdd:cd00882   78 LILLVVDSTDRESEEDAK--LLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAKILGVPvfevSAKTGEGVDEL 155


                 ..
gi 493579264 356 RE 357
Cdd:cd00882  156 FE 157
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 200-355 1.33e-12

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: 65.56  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 200 KIGLIGYTNAGKSTIMNVLTNDKqyeadeLFATLDA--TTKQ----IYLQNQFQVTLTDTVGFIQ---NLPTELVAAFKS 270
Cdd:cd04163    5 FVAIIGRPNVGKSTLLNALVGQK------ISIVSPKpqTTRNrirgIYTDDDAQIIFVDTPGIHKpkkKLGERMVKAAWS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 271 TLEEnrhVDLLLHVIDASDPNHAEHEKvVLNLLKDldmLDIPRLAVYNKMDVAEH----------------FAATaFPnv 334
Cdd:cd04163   79 ALKD---VDLVLFVVDASEWIGEGDEF-ILELLKK---SKTPVILVLNKIDLVKDkedllplleklkelhpFAEI-FP-- 148

                        170       180
                 ....*....|....*....|.
gi 493579264 335 rISARDKDARSLLRRLIINEM 355
Cdd:cd04163  149 -ISALKGENVDELLEYIVEYL 168
YeeP COG3596
Predicted GTPase [General function prediction only];
186-367 2.99e-11

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 64.02  E-value: 2.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 186 RETGREKRTESQVFKIGLIGYTNAGKSTIMNVLTNDKQYEADElfatLDATTKQIY---LQNQ--FQVTLTDTVGFIQ-N 259
Cdd:COG3596   27 AEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGV----GRPCTREIQryrLESDglPGLVLLDTPGLGEvN 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 260 LPTELVAAFKSTLEEnrhVDLLLHVIDASDPNHAEHEKVVLNLLKDLDmlDIPRLAVYNKMDVAEHFAATAFPNVRISAR 339
Cdd:COG3596  103 ERDREYRELRELLPE---ADLILWVVKADDRALATDEEFLQALRAQYP--DPPVLVVLTQVDRLEPEREWDPPYNWPSPP 177

                        170       180
                 ....*....|....*....|....*...
gi 493579264 340 DKDArslLRRLiINEMREIFEPFSIRVH 367
Cdd:COG3596  178 KEQN---IRRA-LEAIAEQLGVPIDRVI 201
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 202-324 2.23e-10

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: 58.94  E-value: 2.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 202 GLIGYTNAGKSTIMNVLTNDKQYEADELFATLDATTKQIYLQNQFQVTLTDTVGFIQNLPTE--LVAAFKSTLEENrhvD 279
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDGVDIQIIDLPGLLDGASEGrgLGEQILAHLYRS---D 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 493579264 280 LLLHVIDASDPNHAEHEKVVLNL-----LKDLDMLDIPRLAVYNKMDVAE 324
Cdd:cd01881   78 LILHVIDASEDCVGDPLEDQKTLneevsGSFLFLKNKPEMIVANKIDMAS 127
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 201-322 9.08e-10

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: 57.43  E-value: 9.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 201 IGLIGYTNAGKSTIMNVLTNDKQYEADELFatldaTTKQ-----IYLQNQFQVTLTDTVGFIQNlptelvAAfkstleEN 275
Cdd:cd01898    3 VGLVGLPNAGKSTLLSAISNAKPKIADYPF-----TTLVpnlgvVRVDDGRSFVIADIPGLIEG------AS------EG 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493579264 276 --------RHV---DLLLHVIDASDPNHAEHE-KVVLNLLK--DLDMLDIPRLAVYNKMDV 322
Cdd:cd01898   66 kglghrflRHIertRVLLHVIDLSGEDDPVEDyETIRNELEayNPGLAEKPRIVVLNKIDL 126
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
201-357 2.33e-09

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 58.08  E-value: 2.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 201 IGLIGYTNAGKSTIMNVL-------TNDK-QyeadelfatldaTTKQ----IYLQNQFQVTLTDTVGFIQN---LPTELV 265
Cdd:COG1159    6 VAIVGRPNVGKSTLLNALvgqkvsiVSPKpQ------------TTRHrirgIVTREDAQIVFVDTPGIHKPkrkLGRRMN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 266 AAFKSTLEEnrhVDLLLHVIDASDPNHAEHEKvVLNLLKDldmLDIPRLAVYNKMDVAE---------------HFAATa 330
Cdd:COG1159   74 KAAWSALED---VDVILFVVDATEKIGEGDEF-ILELLKK---LKTPVILVINKIDLVKkeellpllaeysellDFAEI- 145

                        170       180
                 ....*....|....*....|....*..
gi 493579264 331 FPnvrISARDKDARSLLRRLIINEMRE 357
Cdd:COG1159  146 VP---ISALKGDNVDELLDEIAKLLPE 169
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
 201-322 3.08e-09

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


Pssm-ID: 274271 [Multi-domain]  Cd Length: 328  Bit Score: 57.82  E-value: 3.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264  201 IGLIGYTNAGKSTIMNVLTNDKQYEADELFATLdatTKQI---YLQNQFQVTLTDTVGFIQNlptelvAAfkstleEN-- 275
Cdd:TIGR02729 160 VGLVGLPNAGKSTLISAVSAAKPKIADYPFTTL---VPNLgvvRVDDGRSFVIADIPGLIEG------AS------EGag 224

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493579264  276 ------RHVD---LLLHVIDASDPNH---AEHEKVVLNLLK--DLDMLDIPRLAVYNKMDV 322
Cdd:TIGR02729 225 lghrflKHIErtrVLLHLIDISPEDGsdpVEDYEIIRNELKkySPELAEKPRIVVLNKIDL 285
era PRK00089
GTPase Era; Reviewed
 201-357 3.55e-09

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 57.36  E-value: 3.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 201 IGLIGYTNAGKSTIMNVLTNDK--------QyeadelfatldaTTKQ----IYLQNQFQVTLTDTVGFIQ---NLPTELV 265
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQKisivspkpQ------------TTRHrirgIVTEDDAQIIFVDTPGIHKpkrALNRAMN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 266 AAFKSTLEEnrhVDLLLHVIDASDPNHAEHEKvVLNLLKDldmLDIPRLAVYNKMD--------------VAEHFAATAF 331
Cdd:PRK00089  76 KAAWSSLKD---VDLVLFVVDADEKIGPGDEF-ILEKLKK---VKTPVILVLNKIDlvkdkeellplleeLSELMDFAEI 148

                        170       180
                 ....*....|....*....|....*.
gi 493579264 332 pnVRISARDKDARSLLRRLIINEMRE 357
Cdd:PRK00089 149 --VPISALKGDNVDELLDVIAKYLPE 172
obgE PRK12299
GTPase CgtA; Reviewed
 201-324 4.43e-08

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 54.31  E-value: 4.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 201 IGLIGYTNAGKSTIMNVLTNDKQYEADELFatldaTTKQIYL-----QNQFQVTLTDTVGFIQNlptelvAAfkstleEN 275
Cdd:PRK12299 161 VGLVGLPNAGKSTLISAVSAAKPKIADYPF-----TTLHPNLgvvrvDDYKSFVIADIPGLIEG------AS------EG 223

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493579264 276 --------RHVD---LLLHVIDASDPNHAEHEKVVLNLLK--DLDMLDIPRLAVYNKMDVAE 324
Cdd:PRK12299 224 aglghrflKHIErtrLLLHLVDIEAVDPVEDYKTIRNELEkySPELADKPRILVLNKIDLLD 285
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 162-357 1.19e-07

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: 53.53  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 162 ELNRRSIRNQISDIERQLKVVEKNRETGREKRtesQVFKIGLIGYTNAGKSTIMNVLTNdkqYEAdelfA--------TL 233
Cdd:COG0486  180 FLDREELLERLEELREELEALLASARQGELLR---EGIKVVIVGRPNVGKSSLLNALLG---EER----AivtdiagtTR 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 234 DATTKQIYLQNqFQVTLTDTVG------FIQNLPTELvaafksTLEENRHVDLLLHVIDASDPNHAEHEKVvLNLLKDld 307
Cdd:COG0486  250 DVIEERINIGG-IPVRLIDTAGlretedEVEKIGIER------AREAIEEADLVLLLLDASEPLTEEDEEI-LEKLKD-- 319

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 493579264 308 mldIPRLAVYNKMDVAEHFAAT-----AFPNVRISARDKDARSLLRRLIINEMRE 357
Cdd:COG0486  320 ---KPVIVVLNKIDLPSEADGElkslpGEPVIAISAKTGEGIDELKEAILELVGE 371
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
162-363 4.27e-07

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 51.65  E-value: 4.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 162 ELNRRSIRNQISDIERQLKVVEKNRETGREKRtesQVFKIGLIGYTNAGKSTIMNVLTNdkqYEAdelfA--------TL 233
Cdd:PRK05291 182 FLSDEKILEKLEELIAELEALLASARQGEILR---EGLKVVIAGRPNVGKSSLLNALLG---EER----AivtdiagtTR 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 234 DATTKQIYLQNqFQVTLTDTVG------FIQNLPTELvaafksTLEENRHVDLLLHVIDASDPNHAEHEKVVLNLlkdld 307
Cdd:PRK05291 252 DVIEEHINLDG-IPLRLIDTAGiretddEVEKIGIER------SREAIEEADLVLLVLDASEPLTEEDDEILEEL----- 319

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493579264 308 mLDIPRLAVYNKMDVAEHFAATAFPN---VRISARDKDARSLLRRLIINEMREIFEPFS 363
Cdd:PRK05291 320 -KDKPVIVVLNKADLTGEIDLEEENGkpvIRISAKTGEGIDELREAIKELAFGGFGGNQ 377
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 201-351 4.63e-07

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: 49.43  E-value: 4.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 201 IGLIGYTNAGKSTIMNVLTNDKQyeadelFATLDAT---TKQIylqNQFQVT----LTDTVGFI-QNLPTELVAAFKST- 271
Cdd:cd01876    2 VAFAGRSNVGKSSLINALTNRKK------LARTSKTpgrTQLI---NFFNVGdkfrLVDLPGYGyAKVSKEVREKWGKLi 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 272 ---LEENRHVDLLLHVIDASDPnHAEHEKVVLNLLKDldmLDIPRLAVYNKMD-------------VAEHFAA-TAFPNV 334
Cdd:cd01876   73 eeyLENRENLKGVVLLIDARHG-PTPIDLEMLEFLEE---LGIPFLIVLTKADklkkselakvlkkIKEELNLfNILPPV 148

                        170
                 ....*....|....*...
gi 493579264 335 R-ISARDKDARSLLRRLI 351
Cdd:cd01876  149 IlFSSKKGTGIDELRALI 166
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 199-340 1.09e-06

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 48.14  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264  199 FKIGLIGYTNAGKSTIMNVLTNDKQY--EADElFATLDATTKQIYLQN-QFQVTLTDTVG-----FIQNLPTELVAAFKS 270
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNKGSitEYYP-GTTRNYVTTVIEEDGkTYKFNLLDTAGqedydAIRRLYYPQVERSLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264  271 TleenrhVDLLLHVIDASDPNhAEHEKVVLNLLKDldmlDIPRLAVYNKMD---------VAEHFAATAF-PNVRISARD 340
Cdd:TIGR00231  81 V------FDIVILVLDVEEIL-EKQTKEIIHHADS----GVPIILVGNKIDlkdadlkthVASEFAKLNGePIIPLSAET 149
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 203-325 1.68e-06

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


Pssm-ID: 206667 [Multi-domain]  Cd Length: 159  Bit Score: 47.45  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 203 LIGYTNAGKSTIMNVLTNDKQYEADelFA--TLDATTKQIYLQNQfQVTLTDTVGfIQNL----PTELVAafKSTLEENR 276
Cdd:cd01879    2 LVGNPNVGKTTLFNALTGARQKVGN--WPgvTVEKKEGEFKLGGK-EIEIVDLPG-TYSLtpysEDEKVA--RDFLLGEE 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 493579264 277 hVDLLLHVIDASDPNHAehekvvLNLLKDLDMLDIPRLAVYNKMDVAEH 325
Cdd:cd01879   76 -PDLIVNVVDATNLERN------LYLTLQLLELGLPVVVALNMIDEAEK 117
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
201-350 2.71e-06

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 49.72  E-value: 2.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 201 IGLIGYTNAGKSTIMNVLTNDKQYEADELFATLDATTKQiYLQNQFQVTLTDTVGfIQNLPTelvAAFKSTLEE------ 274
Cdd:PRK09554   6 IGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQ-FSTTDHQVTLVDLPG-TYSLTT---ISSQTSLDEqiachy 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493579264 275 --NRHVDLLLHVIDASdpNHAEHEKVVLNLLKdldmLDIPRLAVYNKMDVAEHfaatafPNVRIsardkDARSLLRRL 350
Cdd:PRK09554  81 ilSGDADLLINVVDAS--NLERNLYLTLQLLE----LGIPCIVALNMLDIAEK------QNIRI-----DIDALSARL 141
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 199-355 4.17e-06

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: 46.33  E-value: 4.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 199 FKIGLIGYTNAGKSTIMNVLTNDkqyeadelfatlDA--------TTK-----QIYLQNqFQVTLTDTVG------FIQN 259
Cdd:cd04164    4 IKVVIAGKPNVGKSSLLNALAGR------------DRaivsdiagTTRdvieeEIDLGG-IPVRLIDTAGlretedEIEK 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 260 LPTELvaafksTLEENRHVDLLLHVIDASDPNHAEhEKVVLNLLKdldmlDIPRLAVYNKMDVAEHFAATAFPN----VR 335
Cdd:cd04164   71 IGIER------AREAIEEADLVLLVVDASEGLDEE-DLEILELPA-----KKPVIVVLNKSDLLSDAEGISELNgkpiIA 138

                        170       180
                 ....*....|....*....|
gi 493579264 336 ISARDKDARSLLRRLIINEM 355
Cdd:cd04164  139 ISAKTGEGIDELKEALLELA 158
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 156-371 9.21e-06

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: 47.09  E-value: 9.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264  156 PGESQLELNRRSIRNQISDIERQLKVVEKNRETGREKRtesQVFKIGLIGYTNAGKSTIMNVLTNDkqyeadelfatlDA 235
Cdd:pfam12631  55 PEDDIEELTEEELLERLEELLAELEKLLATADRGRILR---EGIKVVIVGKPNVGKSSLLNALLGE------------ER 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264  236 --------TTK-----QIYLQNqFQVTLTDTVGfIQNlPTELVAAF--KSTLEENRHVDLLLHVIDASDPNHAEhEKVVL 300
Cdd:pfam12631 120 aivtdipgTTRdvieeTINIGG-IPLRLIDTAG-IRE-TDDEVEKIgiERAREAIEEADLVLLVLDASRPLDEE-DLEIL 195

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493579264  301 NLLKDldmlDIPRLAVYNKMD----VAEHFAATAFPNVRISARDKDARSLLRRLIINEMREIF----EPFSIRVHQNQA 371
Cdd:pfam12631 196 ELLKD----KKPIIVVLNKSDllgeIDELEELKGKPVLAISAKTGEGLDELEEAIKELFLAGEiasdGPIITNARHKEA 270
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
 200-324 2.70e-05

ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.


Pssm-ID: 206644 [Multi-domain]  Cd Length: 158  Bit Score: 44.10  E-value: 2.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 200 KIGLIGYTNAGKSTIMNvltndkqyeadelfatldattkqiYLQNQFQVTLTDTVGFiqNLPTELVAAFKSTL------E 273
Cdd:cd00878    1 RILMLGLDGAGKTTILY------------------------KLKLGEVVTTIPTIGF--NVETVEYKNVKFTVwdvggqD 54

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 274 ENRH--------VDLLLHVIDASDPNH-AEHEKVVLNLLKDLDMLDIPRLAVYNKMDVAE 324
Cdd:cd00878   55 KIRPlwkhyyenTDGLIFVVDSSDRERiEEAKNELHKLLNEEELKGAPLLILANKQDLPG 114
Arl10_like cd04159
Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from ...
 201-326 4.19e-05

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: 43.46  E-value: 4.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 201 IGLIGYTNAGKSTIMNVLTNDKQyeADELFATLDATTKQIYLQNqfqVTLT--DTVGfiQnlptelvAAFKSTLEEN-RH 277
Cdd:cd04159    2 ITLVGLQNSGKTTLVNVIASGQF--SEDTIPTVGFNMRKVTKGN---VTIKvwDLGG--Q-------PRFRSMWERYcRG 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 493579264 278 VDLLLHVIDASDPNHAEHEKVVLN-LLKDLDMLDIPRLAVYNKMDVAEHF 326
Cdd:cd04159   68 VNAIVYVVDAADREKLEVAKNELHdLLEKPSLEGIPLLVLGNKNDLPGAL 117
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 202-354 6.25e-05

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


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 42.71  E-value: 6.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 202 GLIGYTNAGKSTIMNVLTndkQYEADELFATLDATTKQIYLQNQFQ---VTLTDTVGF--IQNLPTELVAAFKSTLEEnr 276
Cdd:cd11383    1 GLMGKTGAGKSSLCNALF---GTEVAAVGDRRPTTRAAQAYVWQTGgdgLVLLDLPGVgeRGRRDREYEELYRRLLPE-- 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493579264 277 hVDLLLHVIDASDPNHAE-HEKVVLNLLKDldmlDIPRLAVYNKMDvaehfaatafPNVRISARDKDARSLLRRLIINE 354
Cdd:cd11383   76 -ADLVLWLLDADDRALAAdHDFYLLPLAGH----DAPLLFVLNQVD----------PVLAVSARTGWGLDELAEALITA 139
obgE PRK12297
GTPase CgtA; Reviewed
 201-324 7.56e-05

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 44.71  E-value: 7.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 201 IGLIGYTNAGKSTIMNVLTNDKQYEADELFATLdatTKQ---IYLQNQFQVTLTDTVGFIQN------LPTELVaafkst 271
Cdd:PRK12297 161 VGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTL---VPNlgvVETDDGRSFVMADIPGLIEGasegvgLGHQFL------ 231

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493579264 272 leenRHVD---LLLHVIDAS-----DPnhAEHEKVVLNLLK--DLDMLDIPRLAVYNKMDVAE 324
Cdd:PRK12297 232 ----RHIErtrVIVHVIDMSgsegrDP--IEDYEKINKELKlyNPRLLERPQIVVANKMDLPE 288
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 200-324 3.91e-04

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 42.24  E-value: 3.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 200 KIGLIGYTNAGKSTIMNVLTNdKQYEADEL-FATLDATTKQI--------YLQNQF--------QVTLTDTVGFIQNLPT 262
Cdd:PTZ00258  23 KMGIVGLPNVGKSTTFNALCK-QQVPAENFpFCTIDPNTARVnvpderfdWLCKHFkpksivpaQLDITDIAGLVKGASE 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493579264 263 --ELVAAFKSTLeenRHVDLLLHVIDA---SDPNHAEHE-------KVVLN--LLKDLDMLD--IPRLAVYNKMDVAE 324
Cdd:PTZ00258 102 geGLGNAFLSHI---RAVDGIYHVVRAfedEDITHVEGEidpvrdlEIISSelILKDLEFVEkrLDELTKKRKKKKKK 176
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
166-305 3.92e-04

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 42.09  E-value: 3.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 166 RSIRNQISDIERQLKVVEKNRET----GR------------EKRTES--------QVFKIG-----LIGYTNAGKSTIMN 216
Cdd:COG1163    2 MTIEEKIKALEEEISKTPYNKATekhiGRlkaklaelkeelEKRKKKsggggegfAVKKSGdatvvLVGFPSVGKSTLLN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 217 VLTNDKQYEADELFATLDATT-----KQIYLQnqfqvtLTDTVGFIQNlptelvAAF-----KSTLEENRHVDLLLHVID 286
Cdd:COG1163   82 KLTNAKSEVGAYEFTTLDVVPgmleyKGAKIQ------ILDVPGLIEG------AASgkgrgKEVLSVVRNADLILIVLD 149

                        170
                 ....*....|....*....
gi 493579264 287 ASDPnhaEHEKVVLNLLKD 305
Cdd:COG1163  150 VFEL---EQYDVLKEELYD 165
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
 200-322 5.36e-04

Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene required for transport of secretory proteins from the endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 197556 [Multi-domain]  Cd Length: 184  Bit Score: 40.69  E-value: 5.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264   200 KIGLIGYTNAGKSTIMNVLTNDKqyeADELFATLDATTKQIYLQNqFQVTLTDTVGFIQnlptelvaAFKSTLEENRHVD 279
Cdd:smart00178  19 KILFLGLDNAGKTTLLHMLKNDR---LAQHQPTQHPTSEELAIGN-IKFTTFDLGGHQQ--------ARRLWKDYFPEVN 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 493579264   280 LLLHVIDASDPNHAEHEKVVLN-LLKDLDMLDIPRLAVYNKMDV 322
Cdd:smart00178  87 GIVYLVDAYDKERFAESKRELDaLLSDEELATVPFLILGNKIDA 130
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 201-321 1.56e-03

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 39.20  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 201 IGLIGYTNAGKSTIMNVLT----------NDKQYEADELFA------TLDATTKQIYlQNQFQVTLTDTVG---FIQNLP 261
Cdd:cd00881    2 VGVIGHVDHGKTTLTGSLLyqtgaidrrgTRKETFLDTLKEerergiTIKTGVVEFE-WPKRRINFIDTPGhedFSKETV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 262 TELVAAfkstleenrhvDLLLHVIDASDPNHAEHEKVVLNLLkdldMLDIPRLAVYNKMD 321
Cdd:cd00881   81 RGLAQA-----------DGALLVVDANEGVEPQTREHLNIAL----AGGLPIIVAVNKID 125
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 275-351 5.45e-03

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


Pssm-ID: 206752 [Multi-domain]  Cd Length: 157  Bit Score: 37.30  E-value: 5.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 275 NRHVDLLLHVIDASDPNHA---EHEKVVLNLLKdldmldiPRLAVYNKMD---------VAEHFAATAFPNVRISARDKD 342
Cdd:cd01859    9 IKEADVVLEVVDARDPELTrsrKLERMALELGK-------KLIIVLNKADlvprevlekWKEVFESEGLPVVYVSARERL 81


                 ....*....
gi 493579264 343 ARSLLRRLI 351
Cdd:cd01859   82 GTRILRRTI 90
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
 203-322 5.64e-03

Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), also known as Arl11, is a member of the Arf family of small GTPases that is believed to play a major role in apoptotic signaling. ARLTS1 is widely expressed and functions as a tumor suppressor gene in several human cancers. ARLTS1 is a low-penetrance suppressor that accounts for a small percentage of familial melanoma or familial chronic lymphocytic leukemia (CLL). ARLTS1 inactivation seems to occur most frequently through biallelic down-regulation by hypermethylation of the promoter. In breast cancer, ARLTS1 alterations were typically a combination of a hypomorphic polymorphism plus loss of heterozygosity. In a case of thyroid adenoma, ARLTS1 alterations were polymorphism plus promoter hypermethylation. The nonsense polymorphism Trp149Stop occurs with significantly greater frequency in familial cancer cases than in sporadic cancer cases, and the Cys148Arg polymorphism is associated with an increase in high-risk familial breast cancer.


Pssm-ID: 133356 [Multi-domain]  Cd Length: 160  Bit Score: 37.39  E-value: 5.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493579264 203 LIGYTNAGKSTIMNVLtndKQYEADELFATLDATTKQIYLQNQFQVTLTDTVGfiqnlPTELVAAFKSTLEEnrhVDLLL 282
Cdd:cd04156    4 LLGLDSAGKSTLLYKL---KHAELVTTIPTVGFNVEMLQLEKHLSLTVWDVGG-----QEKMRTVWKCYLEN---TDGLV 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 493579264 283 HVIDASDPNH-AEHEKVVLNLLKDLDMLDIPRLAVYNKMDV 322
Cdd:cd04156   73 YVVDSSDEARlDESQKELKHILKNEHIKGVPVVLLANKQDL 113
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 186-219 5.87e-03

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


Pssm-ID: 206752 [Multi-domain]  Cd Length: 157  Bit Score: 37.30  E-value: 5.87e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 493579264 186 RETGREKRTESQVFKIGLIGYTNAGKSTIMNVLT 219
Cdd:cd01859   87 RRTIKELAIDGKPVIVGVVGYPKVGKSSIINALK 120
 
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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