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Conserved domains on  [gi|162416050|sp|A4D1E9|]
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RecName: Full=GTP-binding protein 10; AltName: Full=Protein obg homolog 2; Short=ObgH2

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
6-353 3.31e-106

GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, chromosome partitioning, Replication, recombination, and repair];


:

Pssm-ID: 440302 [Multi-domain]  Cd Length: 343  Bit Score: 316.15  E-value: 3.31e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050   6 CVLFR--KY--------GNfidklrlftrGGSGGmgyprlggeggkggDVWVVAQNRM-TLkqLKDRYpRKRFVAGVGAN 74
Cdd:COG0536   18 CVSFRreKYvpkggpdgGD----------GGRGG--------------DVILVADENLnTL--LDFRY-KRHFKAENGEN 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  75 SKISALKGSKGKDCEIPVPVGISVTD-ENGKIIGELNKENDRILVAQGGLGG------KLLTN-----FLP-LKGQKRII 141
Cdd:COG0536   71 GMGKNRTGKNGEDLVIKVPVGTVVKDaETGEVLADLTEDGQRVVVAKGGRGGlgnahfKSSTNraprfAEPgEPGEERWL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 142 HLDLKLIADVGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDFKQISVADLPGLIEGAHMNKGMGHKFL 221
Cdd:COG0536  151 RLELKLLADVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGRSFVIADIPGLIEGASEGAGLGHRFL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 222 KHIERTRQLLFVVDISGFQLSShtqYRTAFETIIlltKELELYKEELQTKPALLAVNKMDLPDAQDKfhelmsqlqnpKD 301
Cdd:COG0536  231 RHIERTRVLLHVVDAAPLDGRD---PVEDYEIIR---NELEAYSPELAEKPRIVVLNKIDLLDAEEL-----------EE 293
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 162416050 302 FLHLFEKNMIPertvefqhIIPISAVTGEGIEELKNCIRKSLDEQANQENDA 353
Cdd:COG0536  294 LKAELEKLGGP--------VFPISAVTGEGLDELLYALAELLEELRAEEAEE 337
 
Name Accession Description Interval E-value
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
6-353 3.31e-106

GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, chromosome partitioning, Replication, recombination, and repair];


Pssm-ID: 440302 [Multi-domain]  Cd Length: 343  Bit Score: 316.15  E-value: 3.31e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050   6 CVLFR--KY--------GNfidklrlftrGGSGGmgyprlggeggkggDVWVVAQNRM-TLkqLKDRYpRKRFVAGVGAN 74
Cdd:COG0536   18 CVSFRreKYvpkggpdgGD----------GGRGG--------------DVILVADENLnTL--LDFRY-KRHFKAENGEN 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  75 SKISALKGSKGKDCEIPVPVGISVTD-ENGKIIGELNKENDRILVAQGGLGG------KLLTN-----FLP-LKGQKRII 141
Cdd:COG0536   71 GMGKNRTGKNGEDLVIKVPVGTVVKDaETGEVLADLTEDGQRVVVAKGGRGGlgnahfKSSTNraprfAEPgEPGEERWL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 142 HLDLKLIADVGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDFKQISVADLPGLIEGAHMNKGMGHKFL 221
Cdd:COG0536  151 RLELKLLADVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGRSFVIADIPGLIEGASEGAGLGHRFL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 222 KHIERTRQLLFVVDISGFQLSShtqYRTAFETIIlltKELELYKEELQTKPALLAVNKMDLPDAQDKfhelmsqlqnpKD 301
Cdd:COG0536  231 RHIERTRVLLHVVDAAPLDGRD---PVEDYEIIR---NELEAYSPELAEKPRIVVLNKIDLLDAEEL-----------EE 293
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 162416050 302 FLHLFEKNMIPertvefqhIIPISAVTGEGIEELKNCIRKSLDEQANQENDA 353
Cdd:COG0536  294 LKAELEKLGGP--------VFPISAVTGEGLDELLYALAELLEELRAEEAEE 337
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
25-337 1.60e-100

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: 300.88  E-value: 1.60e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050   25 GGSGGMGyprlggeggkgGDVWVVAQNRM-TLkqLKDRYpRKRFVAGVGANSKISALKGSKGKDCEIPVPVGISVTD-EN 102
Cdd:TIGR02729  34 GGDGGRG-----------GSVILEADENLnTL--LDFRY-QRHFKAENGENGMGKNRTGKSGEDLVIKVPVGTVVYDaDT 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  103 GKIIGELNKENDRILVAQGGLGG------KLLTNFLP------LKGQKRIIHLDLKLIADVGLVGFPNAGKSSLLSCVSH 170
Cdd:TIGR02729 100 GELLADLTEPGQRFLVAKGGRGGlgnahfKSSTNRAPrfatpgEPGEERWLRLELKLLADVGLVGLPNAGKSTLISAVSA 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  171 AKPAIADYAFTTLKPELGKIMYSDFKQISVADLPGLIEGAHMNKGMGHKFLKHIERTRQLLFVVDISGFQLSShtqYRTA 250
Cdd:TIGR02729 180 AKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGAGLGHRFLKHIERTRVLLHLIDISPEDGSD---PVED 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  251 FETIIlltKELELYKEELQTKPALLAVNKMDLPDAqDKFHELMsqlqnpKDFLHLFEKNmipertvefqhIIPISAVTGE 330
Cdd:TIGR02729 257 YEIIR---NELKKYSPELAEKPRIVVLNKIDLLDE-EELEELL------KELKKELGKP-----------VFPISALTGE 315

                  ....*..
gi 162416050  331 GIEELKN 337
Cdd:TIGR02729 316 GLDELLD 322
obgE PRK12299
GTPase CgtA; Reviewed
6-351 7.36e-100

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 299.68  E-value: 7.36e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050   6 CVLFR--KY--------GNfidklrlftrGGSGGmgyprlggeggkggDVWVVAQNRM-TLkqLKDRYpRKRFVAGVGAN 74
Cdd:PRK12299  19 CVSFRreKFipfggpdgGD----------GGRGG--------------SVILEADENLnTL--IDFRY-KRHFKAENGEN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  75 SKISALKGSKGKDCEIPVPVGISVTDEN-GKIIGELNKENDRILVAQGGLGGKLLTNFL------P------LKGQKRII 141
Cdd:PRK12299  72 GMGRNRTGKSGKDLVLKVPVGTQIYDADtGELIADLTEHGQRFLVAKGGKGGLGNAHFKsstnraPryatpgEPGEERWL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 142 HLDLKLIADVGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDFKQISVADLPGLIEGAHMNKGMGHKFL 221
Cdd:PRK12299 152 RLELKLLADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKSFVIADIPGLIEGASEGAGLGHRFL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 222 KHIERTRQLLFVVDISGFQLSShtqyrtAFETIIlltKELELYKEELQTKPALLAVNKMDLPDAQDKFHELMsqlqnpKD 301
Cdd:PRK12299 232 KHIERTRLLLHLVDIEAVDPVE------DYKTIR---NELEKYSPELADKPRILVLNKIDLLDEEEEREKRA------AL 296
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 162416050 302 FLHLFEKNmipertvefqhIIPISAVTGEGIEELKNCIRKSLDEQANQEN 351
Cdd:PRK12299 297 ELAALGGP-----------VFLISAVTGEGLDELLRALWELLEEARREEE 335
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
149-343 8.58e-84

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: 252.73  E-value: 8.58e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 149 ADVGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDFKQISVADLPGLIEGAHMNKGMGHKFLKHIERTR 228
Cdd:cd01898    1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGKGLGHRFLRHIERTR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 229 QLLFVVDISGFQlsshtqyrTAFETIILLTKELELYKEELQTKPALLAVNKMDLPDAQDKFHELMSQLQNPKDflhlfek 308
Cdd:cd01898   81 VLLHVIDLSGED--------DPVEDYETIRNELEAYNPGLAEKPRIVVLNKIDLLDAEERFEKLKELLKELKG------- 145
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 162416050 309 nmipertvefQHIIPISAVTGEGIEELKNCIRKSL 343
Cdd:cd01898  146 ----------KKVFPISALTGEGLDELLKKLAKLL 170
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
150-279 9.31e-28

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: 105.39  E-value: 9.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  150 DVGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDfKQISVADLPGLIEGAHMNKGMGHKFLKHIErTRQ 229
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKG-KQIILVDTPGLIEGASEGEGLGRAFLAIIE-ADL 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 162416050  230 LLFVVDisgfqlsshtqyrtAFETIILLTKELELYKEELQtKPALLAVNK 279
Cdd:pfam01926  79 ILFVVD--------------SEEGITPLDEELLELLRENK-KPIILVLNK 113
 
Name Accession Description Interval E-value
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
6-353 3.31e-106

GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, chromosome partitioning, Replication, recombination, and repair];


Pssm-ID: 440302 [Multi-domain]  Cd Length: 343  Bit Score: 316.15  E-value: 3.31e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050   6 CVLFR--KY--------GNfidklrlftrGGSGGmgyprlggeggkggDVWVVAQNRM-TLkqLKDRYpRKRFVAGVGAN 74
Cdd:COG0536   18 CVSFRreKYvpkggpdgGD----------GGRGG--------------DVILVADENLnTL--LDFRY-KRHFKAENGEN 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  75 SKISALKGSKGKDCEIPVPVGISVTD-ENGKIIGELNKENDRILVAQGGLGG------KLLTN-----FLP-LKGQKRII 141
Cdd:COG0536   71 GMGKNRTGKNGEDLVIKVPVGTVVKDaETGEVLADLTEDGQRVVVAKGGRGGlgnahfKSSTNraprfAEPgEPGEERWL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 142 HLDLKLIADVGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDFKQISVADLPGLIEGAHMNKGMGHKFL 221
Cdd:COG0536  151 RLELKLLADVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGRSFVIADIPGLIEGASEGAGLGHRFL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 222 KHIERTRQLLFVVDISGFQLSShtqYRTAFETIIlltKELELYKEELQTKPALLAVNKMDLPDAQDKfhelmsqlqnpKD 301
Cdd:COG0536  231 RHIERTRVLLHVVDAAPLDGRD---PVEDYEIIR---NELEAYSPELAEKPRIVVLNKIDLLDAEEL-----------EE 293
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 162416050 302 FLHLFEKNMIPertvefqhIIPISAVTGEGIEELKNCIRKSLDEQANQENDA 353
Cdd:COG0536  294 LKAELEKLGGP--------VFPISAVTGEGLDELLYALAELLEELRAEEAEE 337
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
25-337 1.60e-100

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: 300.88  E-value: 1.60e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050   25 GGSGGMGyprlggeggkgGDVWVVAQNRM-TLkqLKDRYpRKRFVAGVGANSKISALKGSKGKDCEIPVPVGISVTD-EN 102
Cdd:TIGR02729  34 GGDGGRG-----------GSVILEADENLnTL--LDFRY-QRHFKAENGENGMGKNRTGKSGEDLVIKVPVGTVVYDaDT 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  103 GKIIGELNKENDRILVAQGGLGG------KLLTNFLP------LKGQKRIIHLDLKLIADVGLVGFPNAGKSSLLSCVSH 170
Cdd:TIGR02729 100 GELLADLTEPGQRFLVAKGGRGGlgnahfKSSTNRAPrfatpgEPGEERWLRLELKLLADVGLVGLPNAGKSTLISAVSA 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  171 AKPAIADYAFTTLKPELGKIMYSDFKQISVADLPGLIEGAHMNKGMGHKFLKHIERTRQLLFVVDISGFQLSShtqYRTA 250
Cdd:TIGR02729 180 AKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGAGLGHRFLKHIERTRVLLHLIDISPEDGSD---PVED 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  251 FETIIlltKELELYKEELQTKPALLAVNKMDLPDAqDKFHELMsqlqnpKDFLHLFEKNmipertvefqhIIPISAVTGE 330
Cdd:TIGR02729 257 YEIIR---NELKKYSPELAEKPRIVVLNKIDLLDE-EELEELL------KELKKELGKP-----------VFPISALTGE 315

                  ....*..
gi 162416050  331 GIEELKN 337
Cdd:TIGR02729 316 GLDELLD 322
obgE PRK12299
GTPase CgtA; Reviewed
6-351 7.36e-100

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 299.68  E-value: 7.36e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050   6 CVLFR--KY--------GNfidklrlftrGGSGGmgyprlggeggkggDVWVVAQNRM-TLkqLKDRYpRKRFVAGVGAN 74
Cdd:PRK12299  19 CVSFRreKFipfggpdgGD----------GGRGG--------------SVILEADENLnTL--IDFRY-KRHFKAENGEN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  75 SKISALKGSKGKDCEIPVPVGISVTDEN-GKIIGELNKENDRILVAQGGLGGKLLTNFL------P------LKGQKRII 141
Cdd:PRK12299  72 GMGRNRTGKSGKDLVLKVPVGTQIYDADtGELIADLTEHGQRFLVAKGGKGGLGNAHFKsstnraPryatpgEPGEERWL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 142 HLDLKLIADVGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDFKQISVADLPGLIEGAHMNKGMGHKFL 221
Cdd:PRK12299 152 RLELKLLADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKSFVIADIPGLIEGASEGAGLGHRFL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 222 KHIERTRQLLFVVDISGFQLSShtqyrtAFETIIlltKELELYKEELQTKPALLAVNKMDLPDAQDKFHELMsqlqnpKD 301
Cdd:PRK12299 232 KHIERTRLLLHLVDIEAVDPVE------DYKTIR---NELEKYSPELADKPRILVLNKIDLLDEEEEREKRA------AL 296
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 162416050 302 FLHLFEKNmipertvefqhIIPISAVTGEGIEELKNCIRKSLDEQANQEN 351
Cdd:PRK12299 297 ELAALGGP-----------VFLISAVTGEGLDELLRALWELLEEARREEE 335
obgE PRK12297
GTPase CgtA; Reviewed
25-345 8.15e-99

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 300.09  E-value: 8.15e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  25 GGSGGMGyprlggeggkgGDVWVVA-QNRMTLkqLKDRYpRKRFVAGVGANSKISALKGSKGKDCEIPVPVGISVTD-EN 102
Cdd:PRK12297  35 GGDGGKG-----------GSVIFVAdEGLRTL--LDFRY-KRHFKAENGENGMGKNMHGRNGEDLIIKVPVGTVVKDaET 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 103 GKIIGELNKENDRILVAQGGLGGKLLTNF------------LPLKGQKRIIHLDLKLIADVGLVGFPNAGKSSLLSCVSH 170
Cdd:PRK12297 101 GEVIADLVEPGQEVVVAKGGRGGRGNAHFatstnqapriaeNGEPGEERELRLELKLLADVGLVGFPNVGKSTLLSVVSN 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 171 AKPAIADYAFTTLKPELGKIMYSDFKQISVADLPGLIEGAHMNKGMGHKFLKHIERTRQLLFVVDISGfqlsshTQYRTA 250
Cdd:PRK12297 181 AKPKIANYHFTTLVPNLGVVETDDGRSFVMADIPGLIEGASEGVGLGHQFLRHIERTRVIVHVIDMSG------SEGRDP 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 251 FETIILLTKELELYKEELQTKPALLAVNKMDLPDAQDKFhelmsqlqnpKDFLHLFEKNmipertvefqhIIPISAVTGE 330
Cdd:PRK12297 255 IEDYEKINKELKLYNPRLLERPQIVVANKMDLPEAEENL----------EEFKEKLGPK-----------VFPISALTGQ 313
                        330
                 ....*....|....*
gi 162416050 331 GIEELKNCIRKSLDE 345
Cdd:PRK12297 314 GLDELLYAVAELLEE 328
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
149-343 8.58e-84

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: 252.73  E-value: 8.58e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 149 ADVGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDFKQISVADLPGLIEGAHMNKGMGHKFLKHIERTR 228
Cdd:cd01898    1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGKGLGHRFLRHIERTR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 229 QLLFVVDISGFQlsshtqyrTAFETIILLTKELELYKEELQTKPALLAVNKMDLPDAQDKFHELMSQLQNPKDflhlfek 308
Cdd:cd01898   81 VLLHVIDLSGED--------DPVEDYETIRNELEAYNPGLAEKPRIVVLNKIDLLDAEERFEKLKELLKELKG------- 145
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 162416050 309 nmipertvefQHIIPISAVTGEGIEELKNCIRKSL 343
Cdd:cd01898  146 ----------KKVFPISALTGEGLDELLKKLAKLL 170
obgE PRK12298
GTPase CgtA; Reviewed
25-358 9.93e-83

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 257.49  E-value: 9.93e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  25 GGSGGMGyprlggeggkgGDVWVVA-QNRMTLKQLkdRYpRKRFVAGVGANSKISALKGSKGKDCEIPVPVGISVTD-EN 102
Cdd:PRK12298  36 GGDGGDG-----------GDVYLEAdENLNTLIDY--RF-ERHFRAERGQNGQGRDCTGKRGKDITIKVPVGTRVIDaDT 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 103 GKIIGELNKENDRILVAQGGLGG------KLLTNFLPLK------GQKRIIHLDLKLIADVGLVGFPNAGKSSLLSCVSH 170
Cdd:PRK12298 102 GEVIGDLTEHGQRLLVAKGGWHGlgntrfKSSVNRAPRQktpgtpGEERELKLELKLLADVGLLGLPNAGKSTFIRAVSA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 171 AKPAIADYAFTTLKPELGKIMYSDFKQISVADLPGLIEGAHMNKGMGHKFLKHIERTRQLLFVVDISGFQLSShtqYRTA 250
Cdd:PRK12298 182 AKPKVADYPFTTLVPNLGVVRVDDERSFVVADIPGLIEGASEGAGLGIRFLKHLERCRVLLHLIDIAPIDGSD---PVEN 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 251 FETIIlltKELELYKEELQTKPALLAVNKMDLPDAQdkfhELMSQLQnpkdflhlfeknMIPERTVEFQHIIPISAVTGE 330
Cdd:PRK12298 259 ARIII---NELEKYSPKLAEKPRWLVFNKIDLLDEE----EAEERAK------------AIVEALGWEGPVYLISAASGL 319
                        330       340
                 ....*....|....*....|....*...
gi 162416050 331 GIEELKNCIRKSLDEQANQENDALHKKQ 358
Cdd:PRK12298 320 GVKELCWDLMTFIEENPREEAEEAEAPE 347
obgE PRK12296
GTPase CgtA; Reviewed
15-336 6.50e-61

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 204.33  E-value: 6.50e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  15 FIDKLRLFTRGGSGG-------------MGYPrlggeggkggD----------VWVVAQNRMTLKQLKDRYPRKrfvAGV 71
Cdd:PRK12296   4 FVDRVVLHVKAGDGGngcasvhrekfkpLGGP----------DggnggrggsvVLVVDPQVTTLLDFHFRPHRK---ATN 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  72 GANSKISALKGSKGKDCEIPVPVGISVTDENGKIIGELNKENDRILVAQGGLGGklLTN------------F--LPLKGQ 137
Cdd:PRK12296  71 GKPGMGDNRDGAAGEDLVLPVPDGTVVLDEDGEVLADLVGAGTRFVAAAGGRGG--LGNaalaskarkapgFalLGEPGE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 138 KRIIHLDLKLIADVGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDfKQISVADLPGLIEGAHMNKGMG 217
Cdd:PRK12296 149 ERDLVLELKSVADVGLVGFPSAGKSSLISALSAAKPKIADYPFTTLVPNLGVVQAGD-TRFTVADVPGLIPGASEGKGLG 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 218 HKFLKHIERTRQLLFVVDI----SGfqlsshtqyRTAFETIILLTKELELYKEELQT---------KPALLAVNKMDLPD 284
Cdd:PRK12296 228 LDFLRHIERCAVLVHVVDCatlePG---------RDPLSDIDALEAELAAYAPALDGdlglgdlaeRPRLVVLNKIDVPD 298
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 162416050 285 AQDkfhelMSQLQNPKdflhlFEKNMIPertvefqhIIPISAVTGEGIEELK 336
Cdd:PRK12296 299 ARE-----LAEFVRPE-----LEARGWP--------VFEVSAASREGLRELS 332
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
152-343 1.60e-40

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: 140.99  E-value: 1.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 152 GLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDFKQISVADLPGLIEGAHMNKGMGHKFLKHIERTRQLL 231
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDGVDIQIIDLPGLLDGASEGRGLGEQILAHLYRSDLIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 232 FVVDISGfqlsshTQYRTAFETIILLTKELELYKEELQTKPALLAVNKMDLPDaqdkfhelmsqLQNPKDFLHLFEKNMI 311
Cdd:cd01881   81 HVIDASE------DCVGDPLEDQKTLNEEVSGSFLFLKNKPEMIVANKIDMAS-----------ENNLKRLKLDKLKRGI 143
                        170       180       190
                 ....*....|....*....|....*....|..
gi 162416050 312 PertvefqhIIPISAVTGEGIEELKNCIRKSL 343
Cdd:cd01881  144 P--------VVPTSALTRLGLDRVIRTIRKLL 167
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
150-279 9.31e-28

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: 105.39  E-value: 9.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  150 DVGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDfKQISVADLPGLIEGAHMNKGMGHKFLKHIErTRQ 229
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKG-KQIILVDTPGLIEGASEGEGLGRAFLAIIE-ADL 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 162416050  230 LLFVVDisgfqlsshtqyrtAFETIILLTKELELYKEELQtKPALLAVNK 279
Cdd:pfam01926  79 ILFVVD--------------SEEGITPLDEELLELLRENK-KPIILVLNK 113
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
149-344 1.26e-24

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 103.34  E-value: 1.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 149 ADVGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDfKQISVADLPGLIEGAHMNKGMGHKFL------- 221
Cdd:COG1163   64 ATVVLVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGMLEYKG-AKIQILDVPGLIEGAASGKGRGKEVLsvvrnad 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 222 -----------KHIERTRQLLFVVDIS----------------GFQLSSHTQYRTAFETIILLTKELELY------KEEL 268
Cdd:COG1163  143 lilivldvfelEQYDVLKEELYDAGIRlnkpppdvtiekkgkgGIRVNSTGKLDLDEEDIKKILREYGIVnadvliREDV 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 269 QT-------------KPALLAVNKMDLPDAqDKFHELMSQLQNPKDFlhlfeknmipertvefqhiIPISAVTGEGIEEL 335
Cdd:COG1163  223 TLddlidalmgnrvyKPAIVVVNKIDLADE-EYVEELKSKLPDGVPV-------------------IFISAEKGIGLEEL 282

                 ....*....
gi 162416050 336 KNCIRKSLD 344
Cdd:COG1163  283 KEEIFEELG 291
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
149-262 1.55e-22

Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding protein (DRG) subfamily is an uncharacterized member of the Obg family, an evolutionary branch of GTPase superfamily proteins. GTPases act as molecular switches regulating diverse cellular processes. DRG2 and DRG1 comprise the DRG subfamily in eukaryotes. In view of their widespread expression in various tissues and high conservation among distantly related species in eukaryotes and archaea, DRG proteins may regulate fundamental cellular processes. It is proposed that the DRG subfamily proteins play their physiological roles through RNA binding.


Pssm-ID: 206683 [Multi-domain]  Cd Length: 233  Bit Score: 94.92  E-value: 1.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 149 ADVGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDfKQISVADLPGLIEGAHMNKGMGHKFLKHIeRTR 228
Cdd:cd01896    1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKG-AKIQLLDLPGIIEGASDGKGRGRQVIAVA-RTA 78
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 162416050 229 QL-LFVVDISgfqlSSHTQYRtafetiiLLTKELE 262
Cdd:cd01896   79 DLiLIVLDAT----KPEGQRE-------ILERELE 102
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
152-343 1.84e-22

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: 92.69  E-value: 1.84e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 152 GLVGFPNAGKSSLLSCVSHAKPAI-ADYAFTTLKPELGKIMYSDFKQISVADLPGLIEGAHMNKGMGHKFLKHIERTRQL 230
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGIvSPIPGTTRDPVRKEWELLPLGPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 231 LFVVDisgfqlSSHTQYRTafetiilltkELELYKEELQTKPALLAVNKMDLPDAQDKFHELMSqlqnpkdflhlFEKNM 310
Cdd:cd00880   81 LLVVD------SDLTPVEE----------EAKLGLLRERGKPVLLVLNKIDLVPESEEEELLRE-----------RKLEL 133
                        170       180       190
                 ....*....|....*....|....*....|...
gi 162416050 311 IPErtvefQHIIPISAVTGEGIEELKNCIRKSL 343
Cdd:cd00880  134 LPD-----LPVIAVSALPGEGIDELRKKIAELL 161
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
153-337 5.90e-22

Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in eukaryotes ranging from trypanosomes to humans. NOG1 is functionally linked to ribosome biogenesis and found in association with the nuclear pore complexes and identified in many preribosomal complexes. Thus, defects in NOG1 can lead to defects in 60S biogenesis. The S. cerevisiae NOG1 gene is essential for cell viability, and mutations in the predicted G motifs abrogate function. It is a member of the ODN family of GTP-binding proteins that also includes the bacterial Obg and DRG proteins.


Pssm-ID: 206684 [Multi-domain]  Cd Length: 167  Bit Score: 91.47  E-value: 5.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 153 LVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYsDFKQISVADLPGL----------IEGAHMNKgmghkfLK 222
Cdd:cd01897    5 IAGYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDY-KYLRWQVIDTPGIldrpleerntIEMQAITA------LA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 223 HIERTrqLLFVVDISGFqlSSHTqyrtafetiilLTKELELYKE--ELQTKPALLAVNKMDLPDAQDkfhelmsqlqnpk 300
Cdd:cd01897   78 HLRAA--VLFFIDPSET--CGYS-----------IEEQLSLFKEikPLFNKPVIVVLNKIDLLTEED------------- 129
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 162416050 301 dflhlfEKNMIPERTVEFQHIIPISAVTGEGIEELKN 337
Cdd:cd01897  130 ------LSEIEKELEKEGEEVIKISTLTEEGVDELKN 160
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
155-346 2.98e-18

GTP-binding protein, GTP1/Obg family [General function prediction only];


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 84.88  E-value: 2.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 155 GFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDFKqISVADLPGL----------IEGAHMNKgmghkfLKHI 224
Cdd:COG1084  167 GYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGR-YQVIDTPGLldrplserneIERQAILA------LKHL 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 225 ERTrqLLFVVDISGfqlssHTQYrtafetiiLLTKELELYKE--ELQTKPALLAVNKMDLPDAQDkfhelmsqlqnpkdf 302
Cdd:COG1084  240 ADV--ILFLFDPSE-----TCGY--------SLEEQLNLLEEirSLFDVPVIVVINKIDLSDEEE--------------- 289
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 162416050 303 lhlfeknmiPERTVEFQhIIPISAVTGEGIEELKNCIRKSLDEQ 346
Cdd:COG1084  290 ---------LKEAEEEA-DIKISALTGEGVDELLDELIEALEEE 323
GTP1_OBG pfam01018
GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three ...
25-147 3.24e-18

GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three glycine-rich regions inserted into a small 8-stranded beta-sandwich these regions form six left-handed collagen-like helices packed and H-bonded together.


Pssm-ID: 460027 [Multi-domain]  Cd Length: 155  Bit Score: 80.85  E-value: 3.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050   25 GGSGGmgyprlggeggkggDVWVVAQNRM-TLKQLkdRYpRKRFVAGVGANSKISALKGSKGKDCEIPVPVGISVTD-EN 102
Cdd:pfam01018  36 GGRGG--------------DVILVADENLnTLLDF--RY-KRHFKAENGENGGGKNCHGKNGEDLIIKVPVGTVVKDaET 98
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 162416050  103 GKIIGELNKENDRILVAQGGLGGKLLTNFL------P------LKGQKRIIHLDLKL 147
Cdd:pfam01018  99 GEVLADLTEPGQRVLVAKGGRGGRGNAHFKtstnqaPrfaepgEPGEERWLELELKL 155
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
151-238 2.21e-15

Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They are characterized by a distinct glycine-rich motif immediately following the Walker B motif. The Ygr210 and YyaF/YchF subfamilies appear to form one major branch of the Obg-like family. Among eukaryotes, the Ygr210 subfamily is represented only in fungi. These fungal proteins form a tight cluster with their archaeal orthologs, which suggests the possibility of horizontal transfer from archaea to fungi.


Pssm-ID: 206686 [Multi-domain]  Cd Length: 318  Bit Score: 76.11  E-value: 2.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 151 VGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELG-----------------KIMYSDFKQ------ISVADLPGLI 207
Cdd:cd01899    1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGvgyvrvecpckelgvscNPRYGKCIDgkryvpVELIDVAGLV 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 162416050 208 EGAHMNKGMGHKFLKHIERTRQLLFVVDISG 238
Cdd:cd01899   81 PGAHEGKGLGNQFLDDLRDADVLIHVVDASG 111
PRK09602 PRK09602
translation-associated GTPase; Reviewed
151-238 1.06e-14

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 74.84  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 151 VGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKP--------------ELGKI------MYSD---FKQISVADLPGLI 207
Cdd:PRK09602   4 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPnvgvayvrvecpckELGVKcnprngKCIDgtrFIPVELIDVAGLV 83
                         90       100       110
                 ....*....|....*....|....*....|.
gi 162416050 208 EGAHMNKGMGHKFLKHIERTRQLLFVVDISG 238
Cdd:PRK09602  84 PGAHEGRGLGNQFLDDLRQADALIHVVDASG 114
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
151-345 1.08e-14

GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other bacteria. It plays a role in ribosome biogenesis. Few bacteria lack this protein. [Protein synthesis, Other]


Pssm-ID: 129528 [Multi-domain]  Cd Length: 270  Bit Score: 73.58  E-value: 1.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  151 VGLVGFPNAGKSSLLSCVSHAKPAI-ADYAFTTLKPELGkIMYSDFKQISVADLPGLIEGAH-----MNKGMgHKFLKHI 224
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHGQKISItSPKAQTTRNRISG-IHTTGASQIIFIDTPGFHEKKHslnrlMMKEA-RSAIGGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  225 ErtrQLLFVVDisgfqlSSHTQyrtafetiilltKELELYKEELQT--KPALLAVNKMDlpdaqdkfhelmsqLQNPKDF 302
Cdd:TIGR00436  81 D---LILFVVD------SDQWN------------GDGEFVLTKLQNlkRPVVLTRNKLD--------------NKFKDKL 125
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 162416050  303 LHLFEKNMIPErtvEFQHIIPISAVTGEGIEELKNCIRKSLDE 345
Cdd:TIGR00436 126 LPLIDKYAILE---DFKDIVPISALTGDNTSFLAAFIEVHLPE 165
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
151-341 5.28e-14

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: 69.32  E-value: 5.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  151 VGLVGFPNAGKSSLLSCVSHAKPAI-ADYAFTTLKPELGKIMY-SDFKQISVADLPGLIEGAHMNKGMghkflkhIERTR 228
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKGSItEYYPGTTRNYVTTVIEEdGKTYKFNLLDTAGQEDYDAIRRLY-------YPQVE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  229 QLLFVVDISGFQLSshtqyrtaFETIilLTKELELYKEELQTK-PALLAVNKMDLPDAQDKFHElmsqlqnpkdfLHLFE 307
Cdd:TIGR00231  77 RSLRVFDIVILVLD--------VEEI--LEKQTKEIIHHADSGvPIILVGNKIDLKDADLKTHV-----------ASEFA 135
                         170       180       190
                  ....*....|....*....|....*....|....
gi 162416050  308 KNmipertvEFQHIIPISAVTGEGIEELKNCIRK 341
Cdd:TIGR00231 136 KL-------NGEPIIPLSAETGKNIDSAFKIVEA 162
era PRK00089
GTPase Era; Reviewed
151-345 5.92e-14

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 71.62  E-value: 5.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 151 VGLVGFPNAGKSSLLSCVSHAKPAIadyafTTLKPE------LGkIMYSDFKQISVADLPGLIEGAH-MNKGMGHKFLKH 223
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQKISI-----VSPKPQttrhriRG-IVTEDDAQIIFVDTPGIHKPKRaLNRAMNKAAWSS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 224 IERTRQLLFVVDIsgfqlsshTQYRTAFETIILltkelELYKEelQTKPALLAVNKMDLPDAQDKFHELMSQLQnpkdfl 303
Cdd:PRK00089  82 LKDVDLVLFVVDA--------DEKIGPGDEFIL-----EKLKK--VKTPVILVLNKIDLVKDKEELLPLLEELS------ 140
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 162416050 304 hlfeknmipeRTVEFQHIIPISAVTGEGIEELKNCIRKSLDE 345
Cdd:PRK00089 141 ----------ELMDFAEIVPISALKGDNVDELLDVIAKYLPE 172
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
152-339 6.40e-14

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: 69.02  E-value: 6.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 152 GLVGFPNAGKSSLLSCVSHAKPAI-ADYAFTTLKPELGKI-MYSDFKQISVADLPGLIEGAHMnkGMGHKFLKHIERTRQ 229
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEvSDVPGTTRDPDVYVKeLDKGKVKLVLVDTPGLDEFGGL--GREELARLLLRGADL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 230 LLFVVDISGfqlsshtqyRTAFETIilltKELELYKEELQTKPALLAVNKMDLPDAQDKfhelmsqlQNPKDFLHLFEKN 309
Cdd:cd00882   79 ILLVVDSTD---------RESEEDA----KLLILRRLRKEGIPIILVGNKIDLLEEREV--------EELLRLEELAKIL 137
                        170       180       190
                 ....*....|....*....|....*....|
gi 162416050 310 MIPertvefqhIIPISAVTGEGIEELKNCI 339
Cdd:cd00882  138 GVP--------VFEVSAKTGEGVDELFEKL 159
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
151-343 1.09e-13

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: 68.26  E-value: 1.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 151 VGLVGFPNAGKSSLL--------SCVSHaKPAiadyafTTLKPELGkIMYSDFKQISVADLPGLIEGahmNKGMGHKFLK 222
Cdd:cd04163    6 VAIIGRPNVGKSTLLnalvgqkiSIVSP-KPQ------TTRNRIRG-IYTDDDAQIIFVDTPGIHKP---KKKLGERMVK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 223 HIERTRQ----LLFVVDIsgfqlsshTQYRTAFETIILltKELELYKeelqtKPALLAVNKMDLPDAQDKFHELMSQLQN 298
Cdd:cd04163   75 AAWSALKdvdlVLFVVDA--------SEWIGEGDEFIL--ELLKKSK-----TPVILVLNKIDLVKDKEDLLPLLEKLKE 139
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 162416050 299 pkdflhlfeknmiperTVEFQHIIPISAVTGEGIEELKNCIRKSL 343
Cdd:cd04163  140 ----------------LHPFAEIFPISALKGENVDELLEYIVEYL 168
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
151-346 1.39e-12

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 67.71  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 151 VGLVGFPNAGKSSLLSCVSHAKPAIadyafTTLKPE------LGKIMYSDFkQISVADLPGLIEGAH-MNKGMGHKFLKH 223
Cdd:COG1159    6 VAIVGRPNVGKSTLLNALVGQKVSI-----VSPKPQttrhriRGIVTREDA-QIVFVDTPGIHKPKRkLGRRMNKAAWSA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 224 IERTRQLLFVVDIsgfqlsshTQYRTAFETIILltkelELYKEelQTKPALLAVNKMDLPDAQdkfhELMSQLQnpkdfl 303
Cdd:COG1159   80 LEDVDVILFVVDA--------TEKIGEGDEFIL-----ELLKK--LKTPVILVINKIDLVKKE----ELLPLLA------ 134
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 162416050 304 HLFEKnmipertVEFQHIIPISAVTGEGIEELKNCIRKSLDEQ 346
Cdd:COG1159  135 EYSEL-------LDFAEIVPISALKGDNVDELLDEIAKLLPEG 170
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
153-354 6.84e-12

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: 66.62  E-value: 6.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 153 LVGFPNAGKSSLLSCVSHAKPAIadyafttlkpelgkimysdfkqisVADLPG----LIEgAHMNKGmGHKF-------L 221
Cdd:COG0486  218 IVGRPNVGKSSLLNALLGEERAI------------------------VTDIAGttrdVIE-ERINIG-GIPVrlidtagL 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 222 KH---------IERTRQ-------LLFVVDISGFqlsshtqyrtafetiilLTKELELYKEELQTKPALLAVNKMDLPDA 285
Cdd:COG0486  272 REtedevekigIERAREaieeadlVLLLLDASEP-----------------LTEEDEEILEKLKDKPVIVVLNKIDLPSE 334
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162416050 286 QDKfhelmsqlqnpkdflhlfeknmiPERTVEFQHIIPISAVTGEGIEELKNCIRKSLDEQANQENDAL 354
Cdd:COG0486  335 ADG-----------------------ELKSLPGEPVIAISAKTGEGIDELKEAILELVGEGALEGEGVL 380
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
151-343 2.33e-11

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: 62.48  E-value: 2.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 151 VGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKP--------ELGKIMYSD---FkqISvaDLP-GLIEGahmnkgmgh 218
Cdd:cd01878   44 VALVGYTNAGKSTLFNALTGADVLAEDQLFATLDPttrriklpGGREVLLTDtvgF--IR--DLPhQLVEA--------- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 219 kFLKHIERTRQ---LLFVVDISgfqlSSHT--QYRTAFETIilltKELelykeELQTKPALLAVNKMDLPDAQDKFHELM 293
Cdd:cd01878  111 -FRSTLEEVAEadlLLHVVDAS----DPDReeQIETVEEVL----KEL-----GADDIPIILVLNKIDLLDDEELEERLR 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 162416050 294 SQLQNPkdflhlfeknmipertvefqhiIPISAVTGEGIEELKNCIRKSL 343
Cdd:cd01878  177 AGRPDA----------------------VFISAKTGEGLDLLKEAIEELL 204
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
151-346 4.00e-11

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 63.95  E-value: 4.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 151 VGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDFKQISVAD-------LP-GLIEgAhmnkgmghkFLK 222
Cdd:COG2262  202 VALVGYTNAGKSTLFNRLTGADVLAEDKLFATLDPTTRRLELPDGRPVLLTDtvgfirkLPhQLVE-A---------FRS 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 223 HIERTRQ---LLFVVDISgfqlssHTQYRTAFETIILLTKELELykeelQTKPALLAVNKMDLPDAQDkfhelmsqlqnp 299
Cdd:COG2262  272 TLEEVREadlLLHVVDAS------DPDFEEQIETVNEVLEELGA-----DDKPIILVFNKIDLLDDEE------------ 328
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 162416050 300 kdflhlfeknmIPERTVEFQHIIPISAVTGEGIEELKNCIRKSLDEQ 346
Cdd:COG2262  329 -----------LERLRAGYPDAVFISAKTGEGIDELLEAIEERLPED 364
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
153-343 2.09e-10

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: 58.66  E-value: 2.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 153 LVGFPNAGKSSLLSCVSHAKPAIadyafttlkpelgkimysdfkqisVADLPG----LIEgAHMNKGmGHKFlkH----- 223
Cdd:cd04164    8 IAGKPNVGKSSLLNALAGRDRAI------------------------VSDIAGttrdVIE-EEIDLG-GIPV--Rlidta 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 224 -------------IERTRQ-------LLFVVDISGfqlsshtqyrtafetiiLLTKELELYKEELQTKPALLAVNKMDLP 283
Cdd:cd04164   60 glretedeiekigIERAREaieeadlVLLVVDASE-----------------GLDEEDLEILELPAKKPVIVVLNKSDLL 122
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 284 DAQDKFHELmsqlqnpkdflhlfeknmipertvEFQHIIPISAVTGEGIEELKNCIRKSL 343
Cdd:cd04164  123 SDAEGISEL------------------------NGKPIIAISAKTGEGIDELKEALLELA 158
PTZ00258 PTZ00258
GTP-binding protein; Provisional
151-234 3.50e-10

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 61.11  E-value: 3.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 151 VGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSD---------FK-------QISVADLPGLIEGAHMNK 214
Cdd:PTZ00258  24 MGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVPDerfdwlckhFKpksivpaQLDITDIAGLVKGASEGE 103
                         90       100
                 ....*....|....*....|
gi 162416050 215 GMGHKFLKHIERTRQLLFVV 234
Cdd:PTZ00258 104 GLGNAFLSHIRAVDGIYHVV 123
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
151-350 5.05e-10

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 58.07  E-value: 5.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 151 VGLVGFPNAGKSSLLSCVSHAKPAIADYAfTTLKPelgKIMYSDFK------QISVADLPGLIEgahmNKGMGHKFLKHI 224
Cdd:COG1100    6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYL-STNGV---TIDKKELKldgldvDLVIWDTPGQDE----FRETRQFYARQL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 225 ERTRQLLFVVDisgfqlSSHTQYRTAFETIILLTKELELykeelqTKPALLAVNKMDLPDAQDkfhelmsqLQNPKDFLH 304
Cdd:COG1100   78 TGASLYLFVVD------GTREETLQSLYELLESLRRLGK------KSPIILVLNKIDLYDEEE--------IEDEERLKE 137
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 162416050 305 LFEKNmipertvEFQHIIPISAVTGEGIEELKNCIRKSLDEQANQE 350
Cdd:COG1100  138 ALSED-------NIVEVVATSAKTGEGVEELFAALAEILRGEGDSL 176
PRK11058 PRK11058
GTPase HflX; Provisional
148-335 7.03e-10

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 60.12  E-value: 7.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 148 IADVGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDFKQISVADLPGLIEgaHMNKGMGHKFLKHIERT 227
Cdd:PRK11058 197 VPTVSLVGYTNAGKSTLFNRITEARVYAADQLFATLDPTLRRIDVADVGETVLADTVGFIR--HLPHDLVAAFKATLQET 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 228 RQ---LLFVVDISGFQLSSHTQyrtAFETIIlltkelelykEELQTK--PALLAVNKMDLPDaqdkfhelmsqlqnpkDF 302
Cdd:PRK11058 275 RQatlLLHVVDAADVRVQENIE---AVNTVL----------EEIDAHeiPTLLVMNKIDMLD----------------DF 325
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 162416050 303 LHLFEKNM--IPERtvefqhiIPISAVTGEGIEEL 335
Cdd:PRK11058 326 EPRIDRDEenKPIR-------VWLSAQTGAGIPLL 353
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
153-354 1.58e-09

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 59.35  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 153 LVGFPNAGKSSLLSCVSHAKPAIadyafttlkpelgkimysdfkqisVADLPG----LIEgAHMNKGmGHKF-------L 221
Cdd:PRK05291 220 IAGRPNVGKSSLLNALLGEERAI------------------------VTDIAGttrdVIE-EHINLD-GIPLrlidtagI 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 222 KH---------IERTRQL-------LFVVDISGfqlsshtqyrtafetiiLLTKELELYKEELQTKPALLAVNKMDLPDA 285
Cdd:PRK05291 274 REtddevekigIERSREAieeadlvLLVLDASE-----------------PLTEEDDEILEELKDKPVIVVLNKADLTGE 336
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162416050 286 QDKFHElmsqlqnpkdflhlfeknmipertvEFQHIIPISAVTGEGIEELKNCIRKSLDEQANQENDAL 354
Cdd:PRK05291 337 IDLEEE-------------------------NGKPVIRISAKTGEGIDELREAIKELAFGGFGGNQEGV 380
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
151-361 3.22e-09

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: 57.88  E-value: 3.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  151 VGLVGFPNAGKSSLLSCVSHAKPAIadyafttlkpelgkimysdfkqisVADLPG----LIEgAHMN-KGM--------- 216
Cdd:pfam12631  97 VVIVGKPNVGKSSLLNALLGEERAI------------------------VTDIPGttrdVIE-ETINiGGIplrlidtag 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  217 -----------GhkflkhIERTRQL-------LFVVDISgfqlsshtqyrtafetiILLTKELELYKEELQTKPALLAV- 277
Cdd:pfam12631 152 iretddevekiG------IERAREAieeadlvLLVLDAS-----------------RPLDEEDLEILELLKDKKPIIVVl 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  278 NKMDLPDAQDKfhelmsqlqnpkdflhlfeknmipERTVEFQHIIPISAVTGEGIEELKNCIRKSLDEQANQENDAL--- 354
Cdd:pfam12631 209 NKSDLLGEIDE------------------------LEELKGKPVLAISAKTGEGLDELEEAIKELFLAGEIASDGPIitn 264

                  ....*....
gi 162416050  355 --HKKQLLN 361
Cdd:pfam12631 265 arHKEALER 273
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
151-335 1.15e-08

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: 54.22  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 151 VGLVGFPNAGKSSLLSCVSHAKPAI------ADYAFTTLKPELG-----KIMYSDFKQ----ISVADLPGliegaHMNkg 215
Cdd:cd00881    2 VGVIGHVDHGKTTLTGSLLYQTGAIdrrgtrKETFLDTLKEERErgitiKTGVVEFEWpkrrINFIDTPG-----HED-- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 216 mghkFLKHIERT-RQL---LFVVDIS-GFQLsshtqyRTafETIILLTKELELykeelqtkPALLAVNKMDLPDaQDKFH 290
Cdd:cd00881   75 ----FSKETVRGlAQAdgaLLVVDANeGVEP------QT--REHLNIALAGGL--------PIIVAVNKIDRVG-EEDFD 133
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 162416050 291 ELMSQLqnpKDFLHLFEKNMIPERTVEfqhIIPISAVTGEGIEEL 335
Cdd:cd00881  134 EVLREI---KELLKLIGFTFLKGKDVP---IIPISALTGEGIEEL 172
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
153-341 6.44e-08

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: 51.69  E-value: 6.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 153 LVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDfKQISVADLPGL--IEGAHMNKGMGHKFLKHiERTRQL 230
Cdd:cd01879    2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGG-KEIEIVDLPGTysLTPYSEDEKVARDFLLG-EEPDLI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 231 LFVVDISgfQLSSHtqyrtafetIILLTKELELykeelqTKPALLAVNKMDLpdAQDKFHELmsqlqnpkDFLHLFEKNM 310
Cdd:cd01879   80 VNVVDAT--NLERN---------LYLTLQLLEL------GLPVVVALNMIDE--AEKRGIKI--------DLDKLSELLG 132
                        170       180       190
                 ....*....|....*....|....*....|.
gi 162416050 311 IPertvefqhIIPISAVTGEGIEELKNCIRK 341
Cdd:cd01879  133 VP--------VVPTSARKGEGIDELLDAIAK 155
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
153-334 9.21e-08

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: 51.04  E-value: 9.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 153 LVGFPNAGKSSLLScvshakpAIADYAFTTLKPELG----KIMYSDFKqISVADLPGLIEGAHMNKgmgHKFlkhiERTR 228
Cdd:cd00878    4 MLGLDGAGKTTILY-------KLKLGEVVTTIPTIGfnveTVEYKNVK-FTVWDVGGQDKIRPLWK---HYY----ENTD 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 229 QLLFVVDisgfqlSSHtqyRTAFETIIlltKELE--LYKEELQTKPALLAVNKMDLPDAqDKFHELMSQLQNPKDFLHLF 306
Cdd:cd00878   69 GLIFVVD------SSD---RERIEEAK---NELHklLNEEELKGAPLLILANKQDLPGA-LTESELIELLGLESIKGRRW 135
                        170       180
                 ....*....|....*....|....*...
gi 162416050 307 eknmipertvefqHIIPISAVTGEGIEE 334
Cdd:cd00878  136 -------------HIQPCSAVTGDGLDE 150
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
146-335 3.96e-07

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 49.83  E-value: 3.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  146 KLIADVGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELG-------------------KIMYSDFKqISVADLPGl 206
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEAGldnlpeerergitiksaavSFETKDYL-INLIDTPG- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  207 iegaHMNkgmghkFLKHIER-TRQL---LFVVDIS-GFQLSShtqyrtafETIILLTKELELykeelqtkPALLAVNKMD 281
Cdd:pfam00009  79 ----HVD------FVKEVIRgLAQAdgaILVVDAVeGVMPQT--------REHLRLARQLGV--------PIIVFINKMD 132
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 162416050  282 LPDAQDkFHELMSQLQNpkDFLHLFEKNMipertvEFQHIIPISAVTGEGIEEL 335
Cdd:pfam00009 133 RVDGAE-LEEVVEEVSR--ELLEKYGEDG------EFVPVVPGSALKGEGVQTL 177
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
151-374 1.02e-06

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 50.56  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 151 VGLVGFPNAGKSSLLSCVSHAKPAIA-DYAFTTLKPeLGKIMYSDFKQISVADLPGLIEGAHmnKGMGHKFLKH------ 223
Cdd:PRK09518 453 VALVGRPNVGKSSLLNQLTHEERAVVnDLAGTTRDP-VDEIVEIDGEDWLFIDTAGIKRRQH--KLTGAEYYSSlrtqaa 529
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 224 IERTRQLLFVVDISgfqlsshtqyrtafETIIllTKELELYKEELQTKPAL-LAVNKMDLPDAQDKfhELMSQLQNpkdf 302
Cdd:PRK09518 530 IERSELALFLFDAS--------------QPIS--EQDLKVMSMAVDAGRALvLVFNKWDLMDEFRR--QRLERLWK---- 587
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162416050 303 lhlfeknmipertVEFQHI-----IPISAVTGEGIEELKNCIRKSLDEQANQENDAlhkkqLLNLWISDTMSSTEPP 374
Cdd:PRK09518 588 -------------TEFDRVtwarrVNLSAKTGWHTNRLAPAMQEALESWDQRIPTG-----KLNAFLGKIQAEHPHP 646
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
151-343 5.08e-06

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: 46.35  E-value: 5.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 151 VGLVGFPNAGKSSLLSCVSHAKpaiaDYAFTTLKPelGK----IMYSDFKQISVADLPGLIeGAHMNKGMGHKFLKHIE- 225
Cdd:cd01876    2 VAFAGRSNVGKSSLINALTNRK----KLARTSKTP--GRtqliNFFNVGDKFRLVDLPGYG-YAKVSKEVREKWGKLIEe 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 226 --RTRQ----LLFVVDISGFqlsshtqyrtafetiilLTKE-LELYK--EELQtKPALLAVNKMDlpdaQDKFHELMSQL 296
Cdd:cd01876   75 ylENREnlkgVVLLIDARHG-----------------PTPIdLEMLEflEELG-IPFLIVLTKAD----KLKKSELAKVL 132
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 162416050 297 QNPKDFLHLFEknmipertvEFQHIIPISAVTGEGIEELKNCIRKSL 343
Cdd:cd01876  133 KKIKEELNLFN---------ILPPVILFSSKKGTGIDELRALIAEWL 170
Arl5_Arl8 cd04153
Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like ...
153-334 8.67e-06

Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like Arl4 and Arl7, are localized to the nucleus and nucleolus. Arl5 is developmentally regulated during embryogenesis in mice. Human Arl5 interacts with the heterochromatin protein 1-alpha (HP1alpha), a nonhistone chromosomal protein that is associated with heterochromatin and telomeres, and prevents telomere fusion. Arl5 may also play a role in embryonic nuclear dynamics and/or signaling cascades. Arl8 was identified from a fetal cartilage cDNA library. It is found in brain, heart, lung, cartilage, and kidney. No function has been assigned for Arl8 to date.


Pssm-ID: 133353 [Multi-domain]  Cd Length: 174  Bit Score: 45.80  E-value: 8.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 153 LVGFPNAGKSSLLscvshakpaiadYAFTT-----LKPELGkimySDFKQISVADLpgliegahmnkgmghKFLkhiert 227
Cdd:cd04153   20 IVGLDNAGKTTIL------------YQFLLgevvhTSPTIG----SNVEEIVYKNI---------------RFL------ 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 228 rqllfVVDISGFQL--SSHTQYRTAFETIIL-----------LTKElELYK----EELQTKPALLAVNKMDLPDAqdkfh 290
Cdd:cd04153   63 -----MWDIGGQESlrSSWNTYYTNTDAVILvidstdrerlpLTKE-ELYKmlahEDLRKAVLLVLANKQDLKGA----- 131
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 162416050 291 elMSqlqnPKDFLHLFEKNMIPERTvefQHIIPISAVTGEGIEE 334
Cdd:cd04153  132 --MT----PAEISESLGLTSIRDHT---WHIQGCCALTGEGLPE 166
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
276-335 1.61e-05

Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440298 [Multi-domain]  Cd Length: 502  Bit Score: 46.55  E-value: 1.61e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162416050 276 AVNKMDLPDAQ-DKfheLMSQLQnpkdflhlfEKNMIPER---TVEFqhiIPISAVTGEGIEEL 335
Cdd:COG0532  109 AINKIDKPGANpDR---VKQELA---------EHGLVPEEwggDTIF---VPVSAKTGEGIDEL 157
YeeP COG3596
Predicted GTPase [General function prediction only];
151-347 4.45e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 44.76  E-value: 4.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 151 VGLVGFPNAGKSSL--------LSCVSHAKP---AIADYAFTTlkpelgkimySDFKQISVADLPGL--IEGAHMNKGMG 217
Cdd:COG3596   42 IALVGKTGAGKSSLinalfgaeVAEVGVGRPctrEIQRYRLES----------DGLPGLVLLDTPGLgeVNERDREYREL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 218 HKFLKHIertRQLLFVVDISGFQLSShtqyrtafetiilltkELELYK---EELQTKPALLAVNKMDLPD-AQDKFHELm 293
Cdd:COG3596  112 RELLPEA---DLILWVVKADDRALAT----------------DEEFLQalrAQYPDPPVLVVLTQVDRLEpEREWDPPY- 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 162416050 294 sQLQNPKDFLHLFEK-NMIPERTVEF-QHIIPISA---VTGEGIEELKNCIRKSLDEQA 347
Cdd:COG3596  172 -NWPSPPKEQNIRRAlEAIAEQLGVPiDRVIPVSAaedRTGYGLEELVDALAEALPEAK 229
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
268-349 5.67e-05

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 43.36  E-value: 5.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 268 LQTKPALLAVNKMDLPDaQDKFHELMSQLQN--PKDFLHLFEknmipertvefqhIIPISAVTGEGIEELKNCIRKSLDE 345
Cdd:cd04171  101 LGIKKGLVVLTKADLVD-EDRLELVEEEILEllAGTFLADAP-------------IFPVSSVTGEGIEELKNYLDELAEP 166

                 ....
gi 162416050 346 QANQ 349
Cdd:cd04171  167 QSKD 170
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
151-339 8.03e-05

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


Pssm-ID: 460552 [Multi-domain]  Cd Length: 156  Bit Score: 42.44  E-value: 8.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  151 VGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDfKQISVADLPGL--IEGAHMNKGMGHKFLKHiERTR 228
Cdd:pfam02421   3 IALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFKYKG-YEIEIVDLPGIysLSPYSEEERVARDYLLN-EKPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  229 QLLFVVDisgfqlSSHTQyRTAFETIILLtkELElykeelqtKPALLAVNKMDLPDAQ----DkfHELMSQLQNpkdflh 304
Cdd:pfam02421  81 VIVNVVD------ATNLE-RNLYLTLQLL--ELG--------LPVVLALNMMDEAEKKgikiD--IKKLSELLG------ 135
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 162416050  305 lfeknmIPertvefqhIIPISAVTGEGIEELKNCI 339
Cdd:pfam02421 136 ------VP--------VVPTSARKGEGIDELLDAI 156
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
272-335 8.38e-05

Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 42.84  E-value: 8.38e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162416050 272 PALLAVNKMDLPDAQDKF-----HELMSQLQNPKDFLhlfeknmipeRTVEfqhIIPISAVTGEGIEEL 335
Cdd:cd01887  103 PIIVAINKIDKPYGTEADpervkNELSELGLVGEEWG----------GDVS---IVPISAKTGEGIDDL 158
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
153-334 9.84e-05

Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most Arf family members in the N-terminal extension. In is inactive, GDP-bound form, the N-terminal extension forms an elongated loop that is hydrophobically anchored into the membrane surface; however, it has been proposed that this region might form a helix in the GTP-bound form. The delta subunit of the rod-specific cyclic GMP phosphodiesterase type 6 (PDEdelta) is an Arl3 effector. Arl3 binds microtubules in a regulated manner to alter specific aspects of cytokinesis via interactions with retinitis pigmentosa 2 (RP2). It has been proposed that RP2 functions in concert with Arl3 to link the cell membrane and the cytoskeleton in photoreceptors as part of the cell signaling or vesicular transport machinery. In mice, the absence of Arl3 is associated with abnormal epithelial cell proliferation and cyst formation.


Pssm-ID: 206721 [Multi-domain]  Cd Length: 174  Bit Score: 42.77  E-value: 9.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 153 LVGFPNAGKSSLLScvshakpAIADYAFTTLKPELG---KIMYSDFKQISVADLPGliegahmNKGMGHKFLKHIERTRQ 229
Cdd:cd04155   20 LLGLDNAGKTTILK-------QLASEDISHITPTQGfniKNVQADGFKLNVWDIGG-------QRKIRPYWRNYFENTDV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 230 LLFVVDisgfqlsSHTQYRTAfETIILLTKELElyKEELQTKPALLAVNKMDLPDAQDKfHELMSQLQnpkdfLHLfekn 309
Cdd:cd04155   86 LIYVID-------SADRKRFE-EAGQELVELLE--EEKLAGVPVLVFANKQDLLTAAPA-EEVAEALN-----LHD---- 145
                        170       180
                 ....*....|....*....|....*
gi 162416050 310 mIPERTvefQHIIPISAVTGEGIEE 334
Cdd:cd04155  146 -IRDRS---WHIQACSAKTGEGLQE 166
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
151-341 2.20e-04

EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. 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. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 41.65  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 151 VGLVGFPNAGKSSLLSCVSHAKPAIA-DYAFTTLKPELGKIMYsDFKQISVADLPGLIEGAHMNKGM----GHKFLKHIE 225
Cdd:cd01895    5 IAIIGRPNVGKSSLLNALLGEERVIVsDIAGTTRDSIDVPFEY-DGQKYTLIDTAGIRKKGKVTEGIekysVLRTLKAIE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 226 RTRQLLFVVDIS-GFqlsshtqyrTAFETIILltkelELYKEELqtKPALLAVNKMDLPDAQDKF-----HELMSQLQnp 299
Cdd:cd01895   84 RADVVLLVLDASeGI---------TEQDLRIA-----GLILEEG--KALIIVVNKWDLVEKDEKTmkefeKELRRKLP-- 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 162416050 300 kdFLhlfeknmipertvEFQHIIPISAVTGEGIEELKNCIRK 341
Cdd:cd01895  146 --FL-------------DYAPIVFISALTGQGVDKLFDAIKE 172
Arl6 cd04157
Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small ...
234-334 2.54e-04

Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small GTPases. Arl6 expression is limited to the brain and kidney in adult mice, but it is expressed in the neural plate and somites during embryogenesis, suggesting a possible role for Arl6 in early development. Arl6 is also believed to have a role in cilia or flagella function. Several proteins have been identified that bind Arl6, including Arl6 interacting protein (Arl6ip), and SEC61beta, a subunit of the heterotrimeric conducting channel SEC61p. Based on Arl6 binding to these effectors, Arl6 is also proposed to play a role in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation. At least three specific homozygous Arl6 mutations in humans have been found to cause Bardet-Biedl syndrome, a disorder characterized by obesity, retinopathy, polydactyly, renal and cardiac malformations, learning disabilities, and hypogenitalism. Older literature suggests that Arl6 is a part of the Arl4/Arl7 subfamily, but analyses based on more recent sequence data place Arl6 in its own subfamily.


Pssm-ID: 206722 [Multi-domain]  Cd Length: 162  Bit Score: 41.26  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 234 VDISGFQLSSHTQYRTAFET-------IILLTK-----ELELYKEELQTK-----------PALLAVNKMDLPDAqdkfh 290
Cdd:cd04157   45 LSFTAFDMSGQGKYRGLWEHyykniqgIIFVIDssdrlRMVVAKDELELLlnhpdikhrriPILFYANKMDLPDA----- 119
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 162416050 291 elmsqlQNPKDFLHLFEKNMIPERTvefQHIIPISAVTGEGIEE 334
Cdd:cd04157  120 ------LTAVKITQLLCLENIKDKP---WHIFASSALTGEGLDE 154
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
271-377 2.61e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 42.73  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 271 KPALLAVNKMDLPDaQDKFHELMSQLqnpKDFLHLfeknmipertVEFQHIIPISAVTGEGIEELKNCIRKsLDEQANQE 350
Cdd:PRK00093 285 RALVIVVNKWDLVD-EKTMEEFKKEL---RRRLPF----------LDYAPIVFISALTGQGVDKLLEAIDE-AYENANRR 349
                         90       100
                 ....*....|....*....|....*..
gi 162416050 351 ndalHKKQLLNLWISDTMSSTEPPSKH 377
Cdd:PRK00093 350 ----ISTSVLNRVLEEAVERHPPPLVK 372
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
151-352 2.87e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 42.73  E-value: 2.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 151 VGLVGFPNAGKSSLLSCVSHAKPAIadyafttlkpelgkimysdfkqisVADLPGL----IEG-AHMNkgmGHKFLkhie 225
Cdd:PRK00093   4 VAIVGRPNVGKSTLFNRLTGKRDAI------------------------VADTPGVtrdrIYGeAEWL---GREFI---- 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 226 rtrqllfVVDISGFQLSSHT-------QYRTAFET--IIL--------LT---KEL--ELYKeelQTKPALLAVNKMDLP 283
Cdd:PRK00093  53 -------LIDTGGIEPDDDGfekqireQAELAIEEadVILfvvdgragLTpadEEIakILRK---SNKPVILVVNKVDGP 122
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162416050 284 DAQDKFHElmsqlqnpkdFLHLFeknmipertveFQHIIPISAVTGEGIEELKNCIRKSLDEQANQEND 352
Cdd:PRK00093 123 DEEADAYE----------FYSLG-----------LGEPYPISAEHGRGIGDLLDAILEELPEEEEEDEE 170
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
272-341 6.06e-04

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 40.84  E-value: 6.06e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 272 PALLAVNKMDLPDAQDkfhelmsqlqnPKDFLHLFEKNMIPertvefqhIIPISAVTGEGIEELKNCIRK 341
Cdd:cd01854   35 EPVIVLNKADLVDDEE-----------LEELLEIYEKLGYP--------VLAVSAKTGEGLDELRELLKG 85
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
275-332 9.43e-04

Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 442140 [Multi-domain]  Cd Length: 430  Bit Score: 41.23  E-value: 9.43e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162416050 275 LAVNKMDLPD-AQDKFHELMsqlqnpKDFLHLFEKnmipertVEFQHI--IPISAVTGEGI 332
Cdd:COG2895  153 VAVNKMDLVDySEEVFEEIV------ADYRAFAAK-------LGLEDItfIPISALKGDNV 200
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
153-334 1.09e-03

ADP-ribosylation factor family; Pfam combines a number of different Prosite families together


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 39.13  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  153 LVGFPNAGKSSLLScvshakpAIADYAFTTLKPELG----KIMYSDFKqISVADLpgliegahmnkGmGHKFLK-----H 223
Cdd:pfam00025   5 ILGLDNAGKTTILY-------KLKLGEIVTTIPTIGfnveTVTYKNVK-FTVWDV-----------G-GQESLRplwrnY 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050  224 IERTRQLLFVVDisgfqlSSHtqyRTAFETiillTKElELYK----EELQTKPALLAVNKMDLPDAqdkfhelMSQLQnP 299
Cdd:pfam00025  65 FPNTDAVIFVVD------SAD---RDRIEE----AKE-ELHAllneEELADAPLLILANKQDLPGA-------MSEAE-I 122
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 162416050  300 KDFLHLFEknmIPERTVEfqhIIPISAVTGEGIEE 334
Cdd:pfam00025 123 RELLGLHE---LKDRPWE---IQGCSAVTGEGLDE 151
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
271-377 1.11e-03

Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 40.78  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 271 KPALLAVNKMDL-PDAQDKFHELMSQLQNPKDFLhlfeknmipertvEFQHIIPISAVTGEGIEELKNCIRKSLDEqanq 349
Cdd:COG1160  287 KALVIVVNKWDLvEKDRKTREELEKEIRRRLPFL-------------DYAPIVFISALTGQGVDKLLEAVDEVYES---- 349
                         90       100       110
                 ....*....|....*....|....*....|..
gi 162416050 350 endalHKKQL----LNLWISDTMSSTEPPSKH 377
Cdd:COG1160  350 -----ANKRIstskLNRVLEEAVERHPPPAVK 376
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
151-334 1.99e-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: 38.55  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 151 VGLVGFPNAGKSSLLSCVSHAKPaiadyaFTTLkPELG----KIMYSDFKQISVADLPGlieGAHMNKGMGHkflkHIER 226
Cdd:cd04156    2 VLLLGLDSAGKSTLLYKLKHAEL------VTTI-PTVGfnveMLQLEKHLSLTVWDVGG---QEKMRTVWKC----YLEN 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 227 TRQLLFVVDISGFQLSSHTQyrtafetiilltKELE--LYKEELQTKPALLAVNKMDLPDA------QDKFHelMSQLQN 298
Cdd:cd04156   68 TDGLVYVVDSSDEARLDESQ------------KELKhiLKNEHIKGVPVVLLANKQDLPGAltaeeiTRRFK--LKKYCS 133
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 162416050 299 PKDFlhlfeknmipertvefqHIIPISAVTGEGIEE 334
Cdd:cd04156  134 DRDW-----------------YVQPCSAVTGEGLAE 152
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
321-349 3.73e-03

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 39.51  E-value: 3.73e-03
                         10        20
                 ....*....|....*....|....*....
gi 162416050 321 IIPISAVTGEGIEELKNcirkSLDEQANQ 349
Cdd:COG3276  143 IVPVSAVTGEGIDELRA----ALDALAAA 167
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
126-164 3.85e-03

A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein that functions as a regulator of cell growth and proliferation in stem cells and in several types of cancer cells, but is not expressed in the differentiated cells of most mammalian adult tissues. NS shuttles between the nucleolus and nucleoplasm bidirectionally at a rate that is fast and independent of cell type. Lowering GTP levels decreases the nucleolar retention of NS, and expression of NS is abruptly down-regulated during differentiation prior to terminal cell division. Found only in eukaryotes, NS consists of an N-terminal basic domain, a coiled-coil domain, a GTP-binding domain, an intermediate domain, and a C-terminal acidic domain. Experimental evidence indicates that NS uses its GTP-binding property as a molecular switch to control the transition between the nucleolus and nucleoplasm, and this process involves interaction between the basic, GTP-binding, and intermediate domains of the protein.


Pssm-ID: 206753 [Multi-domain]  Cd Length: 171  Bit Score: 37.94  E-value: 3.85e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 162416050 126 KLLTNFLPLKGQKRIIhldlkliaDVGLVGFPNAGKSSL 164
Cdd:cd04178  102 KLLKNYARNKGIKTSI--------TVGVVGYPNVGKSSV 132
PRK04213 PRK04213
GTP-binding protein EngB;
260-346 4.14e-03

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 37.97  E-value: 4.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 260 ELELYK--EELQTKPaLLAVNKMDLPDAQDKfhelmsQLQNPKDFLHLFEknmiPERtvEFQHII-PISAVTGeGIEELK 336
Cdd:PRK04213 119 DVEMFDflRELGIPP-IVAVNKMDKIKNRDE------VLDEIAERLGLYP----PWR--QWQDIIaPISAKKG-GIEELK 184
                         90
                 ....*....|
gi 162416050 337 NCIRKSLDEQ 346
Cdd:PRK04213 185 EAIRKRLHEA 194
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
151-167 4.15e-03

A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC class I region and is highly homologous to a putative GTP-binding protein, MMR1 from mouse. These proteins represent a new subfamily of GTP-binding proteins that has only eukaryote members. This subfamily shows a circular permutation of the GTPase signature motifs so that the C-terminal strands 5, 6, and 7 (strand 6 contains the G4 box with sequence NKXD) are relocated to the N-terminus.


Pssm-ID: 206750 [Multi-domain]  Cd Length: 140  Bit Score: 37.21  E-value: 4.15e-03
                         10
                 ....*....|....*..
gi 162416050 151 VGLVGFPNAGKSSLLSC 167
Cdd:cd01857   85 IGLVGYPNVGKSSLINA 101
Arfrp1 cd04160
Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a ...
230-334 4.20e-03

Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a membrane-associated Arf family member that lacks the N-terminal myristoylation motif. Arfrp1 is mainly associated with the trans-Golgi compartment and the trans-Golgi network, where it regulates the targeting of Arl1 and the GRIP domain-containing proteins, golgin-97 and golgin-245, onto Golgi membranes. It is also involved in the anterograde transport of the vesicular stomatitis virus G protein from the Golgi to the plasma membrane, and in the retrograde transport of TGN38 and Shiga toxin from endosomes to the trans-Golgi network. Arfrp1 also inhibits Arf/Sec7-dependent activation of phospholipase D. Deletion of Arfrp1 in mice causes embryonic lethality at the gastrulation stage and apoptosis of mesodermal cells, indicating its importance in development.


Pssm-ID: 206725 [Multi-domain]  Cd Length: 168  Bit Score: 37.71  E-value: 4.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 230 LLFVVDISGFQLSSHTqyRTAFETIILltkelelyKEELQTKPALLAVNKMDLPDAQ--DKFHELMSQLQNPkdflhlfe 307
Cdd:cd04160   78 VIYVIDSTDRERFNES--KSAFEKVIN--------NEALEGVPLLVLANKQDLPDALsvAEIKEVFDDCIAL-------- 139
                         90       100
                 ....*....|....*....|....*..
gi 162416050 308 knmIPERTVEFQhiiPISAVTGEGIEE 334
Cdd:cd04160  140 ---IGRRDCLVQ---PVSALEGEGVEE 160
PRK13768 PRK13768
GTPase; Provisional
271-335 7.07e-03

GTPase; Provisional


Pssm-ID: 237498 [Multi-domain]  Cd Length: 253  Bit Score: 37.93  E-value: 7.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162416050 271 KPALLAVNKMDLPDAQD-----KFHE----LMSQLQNPKDFLHLFEKNMIP--ERTVEFQHIIPISAVTGEGIEEL 335
Cdd:PRK13768 163 LPQIPVLNKADLLSEEElerilKWLEdpeyLLEELKLEKGLQGLLSLELLRalEETGLPVRVIPVSAKTGEGFDEL 238
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
153-288 7.48e-03

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 37.30  E-value: 7.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 153 LVGFPNAGKSSLLSCVSHAKPAiadYAFTTLKP-ELGKIMYSDF-KQISVADLPGliegahmNKGMGHKFLKHIE-RTRQ 229
Cdd:cd04105    5 LLGPSDSGKTALFTKLTTGKVR---STVTSIEPnVASFYSNSSKgKKLTLVDVPG-------HEKLRDKLLEYLKaSLKA 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 162416050 230 LLFVVDISGFQLSSHTqyrTA-FETIILLTkeLELYKEELqtkPALLAVNKMDLPDAQDK 288
Cdd:cd04105   75 IVFVVDSATFQKNIRD---VAeFLYDILTD--LEKIKNKI---PILIACNKQDLFTAKPA 126
 
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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