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Conserved domains on  [gi|568920345|ref|XP_006500738|]
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mitochondrial ribosome-associated GTPase 2 isoform X4 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Obg_CgtA super family cl37158
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
112-387 1.85e-105

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]


The actual alignment was detected with superfamily member TIGR02729:

Pssm-ID: 274271 [Multi-domain]  Cd Length: 328  Bit Score: 314.36  E-value: 1.85e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345  112 HIILRVDQQVKSLSSVlsQYQGF----SGEDGGSKNCSGRGGATLYIQVPVGTLVK--EGDKIVADLSNLGDEYVAALGG 185
Cdd:TIGR02729  42 SVILEADENLNTLLDF--RYQRHfkaeNGENGMGKNRTGKSGEDLVIKVPVGTVVYdaDTGELLADLTEPGQRFLVAKGG 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345  186 AGGKGNRFFLANDNRAPVTCTPGQPGQERVLYLELKTMAHAGMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIV 265
Cdd:TIGR02729 120 RGGLGNAHFKSSTNRAPRFATPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVV 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345  266 HYEGHQQVAVADIPGIIRGAHQNKGLGLSFLRHIERCRFFLFVVDLTLPEPWTQVDDLKY---ELEKFEEGLSERSHVII 342
Cdd:TIGR02729 200 RVDDGRSFVIADIPGLIEGASEGAGLGHRFLKHIERTRVLLHLIDISPEDGSDPVEDYEIirnELKKYSPELAEKPRIVV 279
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 568920345  343 ANKIDLP---QARARLPQLQARLGQEAIGLSALTGENLEQLLLHLKEL 387
Cdd:TIGR02729 280 LNKIDLLdeeELEELLKELKKELGKPVFPISALTGEGLDELLDALAEL 327
 
Name Accession Description Interval E-value
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
112-387 1.85e-105

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: 314.36  E-value: 1.85e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345  112 HIILRVDQQVKSLSSVlsQYQGF----SGEDGGSKNCSGRGGATLYIQVPVGTLVK--EGDKIVADLSNLGDEYVAALGG 185
Cdd:TIGR02729  42 SVILEADENLNTLLDF--RYQRHfkaeNGENGMGKNRTGKSGEDLVIKVPVGTVVYdaDTGELLADLTEPGQRFLVAKGG 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345  186 AGGKGNRFFLANDNRAPVTCTPGQPGQERVLYLELKTMAHAGMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIV 265
Cdd:TIGR02729 120 RGGLGNAHFKSSTNRAPRFATPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVV 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345  266 HYEGHQQVAVADIPGIIRGAHQNKGLGLSFLRHIERCRFFLFVVDLTLPEPWTQVDDLKY---ELEKFEEGLSERSHVII 342
Cdd:TIGR02729 200 RVDDGRSFVIADIPGLIEGASEGAGLGHRFLKHIERTRVLLHLIDISPEDGSDPVEDYEIirnELKKYSPELAEKPRIVV 279
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 568920345  343 ANKIDLP---QARARLPQLQARLGQEAIGLSALTGENLEQLLLHLKEL 387
Cdd:TIGR02729 280 LNKIDLLdeeELEELLKELKKELGKPVFPISALTGEGLDELLDALAEL 327
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
112-398 9.86e-105

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: 313.07  E-value: 9.86e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 112 HIILRVDQQVKSLSSVLSQ--YQGFSGEDGGSKNCSGRGGATLYIQVPVGTLVK--EGDKIVADLSNLGDEYVaalggag 187
Cdd:COG0536   42 DVILVADENLNTLLDFRYKrhFKAENGENGMGKNRTGKNGEDLVIKVPVGTVVKdaETGEVLADLTEDGQRVVvakggrg 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 188 gkgNRFFLANDNRAPVTCTPGQPGQERVLYLELKTMAHAGMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIVHY 267
Cdd:COG0536  122 glgNAHFKSSTNRAPRFAEPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRV 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 268 EGHQQVAVADIPGIIRGAHQNKGLGLSFLRHIERCRFFLFVVDLTLPE---PWTQVDDLKYELEKFEEGLSERSHVIIAN 344
Cdd:COG0536  202 GDGRSFVIADIPGLIEGASEGAGLGHRFLRHIERTRVLLHVVDAAPLDgrdPVEDYEIIRNELEAYSPELAEKPRIVVLN 281
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568920345 345 KIDLPQARArLPQLQA---RLGQEAIGLSALTGENLEQLLLHLKELHDAHIEAELEQ 398
Cdd:COG0536  282 KIDLLDAEE-LEELKAeleKLGGPVFPISAVTGEGLDELLYALAELLEELRAEEAEE 337
obgE PRK12299
GTPase CgtA; Reviewed
112-395 1.70e-101

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 304.30  E-value: 1.70e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 112 HIILRVDQQVKSLSSVLSQ--YQGFSGEDGGSKNCSGRGGATLYIQVPVGTLVK--EGDKIVADLSNLGDEYVAALGGAG 187
Cdd:PRK12299  43 SVILEADENLNTLIDFRYKrhFKAENGENGMGRNRTGKSGKDLVLKVPVGTQIYdaDTGELIADLTEHGQRFLVAKGGKG 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 188 GKGNRFFLANDNRAPVTCTPGQPGQERVLYLELKTMAHAGMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIVHY 267
Cdd:PRK12299 123 GLGNAHFKSSTNRAPRYATPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRV 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 268 EGHQQVAVADIPGIIRGAHQNKGLGLSFLRHIERCRFFLFVVDLTLPEPWTQVDDLKYELEKFEEGLSERSHVIIANKID 347
Cdd:PRK12299 203 DDYKSFVIADIPGLIEGASEGAGLGHRFLKHIERTRLLLHLVDIEAVDPVEDYKTIRNELEKYSPELADKPRILVLNKID 282
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568920345 348 LPQAR----ARLPQLQARLGQEAIGLSALTGENLEQLLLHLKELHDAHIEAE 395
Cdd:PRK12299 283 LLDEEeereKRAALELAALGGPVFLISAVTGEGLDELLRALWELLEEARREE 334
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
224-387 8.58e-83

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: 250.80  E-value: 8.58e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 224 AHAGMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIVHYEGHQQVAVADIPGIIRGAHQNKGLGLSFLRHIERCR 303
Cdd:cd01898    1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGKGLGHRFLRHIERTR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 304 FFLFVVDLTLPE-PWTQVDDLKYELEKFEEGLSERSHVIIANKIDLPQARARLPQLQARL----GQEAIGLSALTGENLE 378
Cdd:cd01898   81 VLLHVIDLSGEDdPVEDYETIRNELEAYNPGLAEKPRIVVLNKIDLLDAEERFEKLKELLkelkGKKVFPISALTGEGLD 160

                 ....*....
gi 568920345 379 QLLLHLKEL 387
Cdd:cd01898  161 ELLKKLAKL 169
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
225-345 6.02e-30

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: 111.56  E-value: 6.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345  225 HAGMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIVHYEGHqQVAVADIPGIIRGAHQNKGLGLSFLRHIErCRF 304
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGK-QIILVDTPGLIEGASEGEGLGRAFLAIIE-ADL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 568920345  305 FLFVVDLTlpEPWTQVDDlkyELEKFEEGlSERSHVIIANK 345
Cdd:pfam01926  79 ILFVVDSE--EGITPLDE---ELLELLRE-NKKPIILVLNK 113
 
Name Accession Description Interval E-value
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
112-387 1.85e-105

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: 314.36  E-value: 1.85e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345  112 HIILRVDQQVKSLSSVlsQYQGF----SGEDGGSKNCSGRGGATLYIQVPVGTLVK--EGDKIVADLSNLGDEYVAALGG 185
Cdd:TIGR02729  42 SVILEADENLNTLLDF--RYQRHfkaeNGENGMGKNRTGKSGEDLVIKVPVGTVVYdaDTGELLADLTEPGQRFLVAKGG 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345  186 AGGKGNRFFLANDNRAPVTCTPGQPGQERVLYLELKTMAHAGMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIV 265
Cdd:TIGR02729 120 RGGLGNAHFKSSTNRAPRFATPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVV 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345  266 HYEGHQQVAVADIPGIIRGAHQNKGLGLSFLRHIERCRFFLFVVDLTLPEPWTQVDDLKY---ELEKFEEGLSERSHVII 342
Cdd:TIGR02729 200 RVDDGRSFVIADIPGLIEGASEGAGLGHRFLKHIERTRVLLHLIDISPEDGSDPVEDYEIirnELKKYSPELAEKPRIVV 279
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 568920345  343 ANKIDLP---QARARLPQLQARLGQEAIGLSALTGENLEQLLLHLKEL 387
Cdd:TIGR02729 280 LNKIDLLdeeELEELLKELKKELGKPVFPISALTGEGLDELLDALAEL 327
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
112-398 9.86e-105

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: 313.07  E-value: 9.86e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 112 HIILRVDQQVKSLSSVLSQ--YQGFSGEDGGSKNCSGRGGATLYIQVPVGTLVK--EGDKIVADLSNLGDEYVaalggag 187
Cdd:COG0536   42 DVILVADENLNTLLDFRYKrhFKAENGENGMGKNRTGKNGEDLVIKVPVGTVVKdaETGEVLADLTEDGQRVVvakggrg 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 188 gkgNRFFLANDNRAPVTCTPGQPGQERVLYLELKTMAHAGMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIVHY 267
Cdd:COG0536  122 glgNAHFKSSTNRAPRFAEPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRV 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 268 EGHQQVAVADIPGIIRGAHQNKGLGLSFLRHIERCRFFLFVVDLTLPE---PWTQVDDLKYELEKFEEGLSERSHVIIAN 344
Cdd:COG0536  202 GDGRSFVIADIPGLIEGASEGAGLGHRFLRHIERTRVLLHVVDAAPLDgrdPVEDYEIIRNELEAYSPELAEKPRIVVLN 281
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568920345 345 KIDLPQARArLPQLQA---RLGQEAIGLSALTGENLEQLLLHLKELHDAHIEAELEQ 398
Cdd:COG0536  282 KIDLLDAEE-LEELKAeleKLGGPVFPISAVTGEGLDELLYALAELLEELRAEEAEE 337
obgE PRK12299
GTPase CgtA; Reviewed
112-395 1.70e-101

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 304.30  E-value: 1.70e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 112 HIILRVDQQVKSLSSVLSQ--YQGFSGEDGGSKNCSGRGGATLYIQVPVGTLVK--EGDKIVADLSNLGDEYVAALGGAG 187
Cdd:PRK12299  43 SVILEADENLNTLIDFRYKrhFKAENGENGMGRNRTGKSGKDLVLKVPVGTQIYdaDTGELIADLTEHGQRFLVAKGGKG 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 188 GKGNRFFLANDNRAPVTCTPGQPGQERVLYLELKTMAHAGMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIVHY 267
Cdd:PRK12299 123 GLGNAHFKSSTNRAPRYATPGEPGEERWLRLELKLLADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRV 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 268 EGHQQVAVADIPGIIRGAHQNKGLGLSFLRHIERCRFFLFVVDLTLPEPWTQVDDLKYELEKFEEGLSERSHVIIANKID 347
Cdd:PRK12299 203 DDYKSFVIADIPGLIEGASEGAGLGHRFLKHIERTRLLLHLVDIEAVDPVEDYKTIRNELEKYSPELADKPRILVLNKID 282
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568920345 348 LPQAR----ARLPQLQARLGQEAIGLSALTGENLEQLLLHLKELHDAHIEAE 395
Cdd:PRK12299 283 LLDEEeereKRAALELAALGGPVFLISAVTGEGLDELLRALWELLEEARREE 334
obgE PRK12297
GTPase CgtA; Reviewed
112-398 8.47e-101

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 305.87  E-value: 8.47e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 112 HIILRVDQQVKSLSSVLSQ--YQGFSGEDGGSKNCSGRGGATLYIQVPVGTLVK--EGDKIVADLSNLGDEYVAALGGAG 187
Cdd:PRK12297  43 SVIFVADEGLRTLLDFRYKrhFKAENGENGMGKNMHGRNGEDLIIKVPVGTVVKdaETGEVIADLVEPGQEVVVAKGGRG 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 188 GKGNRFFLANDNRAPVTCTPGQPGQERVLYLELKTMAHAGMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIVHY 267
Cdd:PRK12297 123 GRGNAHFATSTNQAPRIAENGEPGEERELRLELKLLADVGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVET 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 268 EGHQQVAVADIPGIIRGAHQNKGLGLSFLRHIERCRFFLFVVDLTLPE---PWTQVDDLKYELEKFEEGLSERSHVIIAN 344
Cdd:PRK12297 203 DDGRSFVMADIPGLIEGASEGVGLGHQFLRHIERTRVIVHVIDMSGSEgrdPIEDYEKINKELKLYNPRLLERPQIVVAN 282
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568920345 345 KIDLPQARARLPQLQARLGQEAIGLSALTGENLEQLLLHLKELHDAHIEAELEQ 398
Cdd:PRK12297 283 KMDLPEAEENLEEFKEKLGPKVFPISALTGQGLDELLYAVAELLEETPEFPLEE 336
obgE PRK12298
GTPase CgtA; Reviewed
112-402 2.81e-86

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 267.50  E-value: 2.81e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 112 HIILRVDQQVKSLssVLSQYQGF----SGEDGGSKNCSGRGGATLYIQVPVGTLVKEGD--KIVADLSNLGDEYVAALGG 185
Cdd:PRK12298  44 DVYLEADENLNTL--IDYRFERHfraeRGQNGQGRDCTGKRGKDITIKVPVGTRVIDADtgEVIGDLTEHGQRLLVAKGG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 186 AGGKGNRFFLANDNRAPVTCTPGQPGQERVLYLELKTMAHAGMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIV 265
Cdd:PRK12298 122 WHGLGNTRFKSSVNRAPRQKTPGTPGEERELKLELKLLADVGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPNLGVV 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 266 HYEGHQQVAVADIPGIIRGAHQNKGLGLSFLRHIERCRFFLFVVDLTlpePWTQVDDLK------YELEKFEEGLSERSH 339
Cdd:PRK12298 202 RVDDERSFVVADIPGLIEGASEGAGLGIRFLKHLERCRVLLHLIDIA---PIDGSDPVEnariiiNELEKYSPKLAEKPR 278
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568920345 340 VIIANKIDL---PQARARLPQLQARLGQEA--IGLSALTGENLEQLLLHLKELHDAHIEAELEQGRQP 402
Cdd:PRK12298 279 WLVFNKIDLldeEEAEERAKAIVEALGWEGpvYLISAASGLGVKELCWDLMTFIEENPREEAEEAEAP 346
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
224-387 8.58e-83

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: 250.80  E-value: 8.58e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 224 AHAGMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIVHYEGHQQVAVADIPGIIRGAHQNKGLGLSFLRHIERCR 303
Cdd:cd01898    1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGRSFVIADIPGLIEGASEGKGLGHRFLRHIERTR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 304 FFLFVVDLTLPE-PWTQVDDLKYELEKFEEGLSERSHVIIANKIDLPQARARLPQLQARL----GQEAIGLSALTGENLE 378
Cdd:cd01898   81 VLLHVIDLSGEDdPVEDYETIRNELEAYNPGLAEKPRIVVLNKIDLLDAEERFEKLKELLkelkGKKVFPISALTGEGLD 160

                 ....*....
gi 568920345 379 QLLLHLKEL 387
Cdd:cd01898  161 ELLKKLAKL 169
obgE PRK12296
GTPase CgtA; Reviewed
113-404 1.05e-67

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 222.82  E-value: 1.05e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 113 IILRVDQQVKSLssvL-----SQYQGFSGEDGGSKNCSGRGGATLYIQVPVGTLVKEGD-KIVADLSNLGDEYVAALGGA 186
Cdd:PRK12296  46 VVLVVDPQVTTL---LdfhfrPHRKATNGKPGMGDNRDGAAGEDLVLPVPDGTVVLDEDgEVLADLVGAGTRFVAAAGGR 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 187 GGKGNRFfLANDNR-APVTCTPGQPGQERVLYLELKTMAHAGMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIV 265
Cdd:PRK12296 123 GGLGNAA-LASKARkAPGFALLGEPGEERDLVLELKSVADVGLVGFPSAGKSSLISALSAAKPKIADYPFTTLVPNLGVV 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 266 HYeGHQQVAVADIPGIIRGAHQNKGLGLSFLRHIERCRFFLFVVDL-TLPE---PWTQVDDLKYELEKFEE--------- 332
Cdd:PRK12296 202 QA-GDTRFTVADVPGLIPGASEGKGLGLDFLRHIERCAVLVHVVDCaTLEPgrdPLSDIDALEAELAAYAPaldgdlglg 280
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568920345 333 GLSERSHVIIANKIDLPQARARL----PQLQARlGQEAIGLSALTGENLEQLLLHLKELHDAHIEAE--LEQGRQPLR 404
Cdd:PRK12296 281 DLAERPRLVVLNKIDVPDARELAefvrPELEAR-GWPVFEVSAASREGLRELSFALAELVEEARAAEpeAEPTRIVIR 357
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
227-381 7.72e-36

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: 129.05  E-value: 7.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 227 GMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIVHYEGHQQVAVADIPGIIRGAHQNKGLGLSFLRHIERCRFFL 306
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDGVDIQIIDLPGLLDGASEGRGLGEQILAHLYRSDLIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 307 FVVDLTLPEPWTQVDDLK---YELEKFEEGLSERSHVIIANKIDLPQAR--ARLPQLQARLGQEAIGLSALTGENLEQLL 381
Cdd:cd01881   81 HVIDASEDCVGDPLEDQKtlnEEVSGSFLFLKNKPEMIVANKIDMASENnlKRLKLDKLKRGIPVVPTSALTRLGLDRVI 160
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
225-345 6.02e-30

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: 111.56  E-value: 6.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345  225 HAGMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIVHYEGHqQVAVADIPGIIRGAHQNKGLGLSFLRHIErCRF 304
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGK-QIILVDTPGLIEGASEGEGLGRAFLAIIE-ADL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 568920345  305 FLFVVDLTlpEPWTQVDDlkyELEKFEEGlSERSHVIIANK 345
Cdd:pfam01926  79 ILFVVDSE--EGITPLDE---ELLELLRE-NKKPIILVLNK 113
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
224-330 5.23e-27

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: 107.63  E-value: 5.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 224 AHAGMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIVHYEGhQQVAVADIPGIIRGAHQNKGLGLSFLRHIERCR 303
Cdd:cd01896    1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKG-AKIQLLDLPGIIEGASDGKGRGRQVIAVARTAD 79
                         90       100
                 ....*....|....*....|....*..
gi 568920345 304 FFLFVVDLTLPEpwTQVDDLKYELEKF 330
Cdd:cd01896   80 LILIVLDATKPE--GQREILERELEGV 104
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
228-380 6.82e-26

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 107.58  E-value: 6.82e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 228 MVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIVHYEGhQQVAVADIPGIIRGAHQNKGLGLSFLRHIERCRFFLF 307
Cdd:COG1163   68 LVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGMLEYKG-AKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILI 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 308 VVDLTLPEpwtQVDDLKYELEK---------------------------------------------------------- 329
Cdd:COG1163  147 VLDVFELE---QYDVLKEELYDagirlnkpppdvtiekkgkggirvnstgkldldeedikkilreygivnadvliredvt 223
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 330 ---FEEGLSE-RSHV---IIANKIDLPQaRARLPQLQARLGQ--EAIGLSALTGENLEQL 380
Cdd:COG1163  224 lddLIDALMGnRVYKpaiVVVNKIDLAD-EEYVEELKSKLPDgvPVIFISAEKGIGLEEL 282
GTP1_OBG pfam01018
GTP1/OBG; The N-terminal domain of Swiss:P20964 has the OBG fold, which is formed by three ...
107-222 1.12e-24

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: 98.96  E-value: 1.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345  107 GGNGGHIILRVDQQVKSLSSVLSQ--YQGFSGEDGGSKNCSGRGGATLYIQVPVGTLVKEGD--KIVADLSNLGDEYVAA 182
Cdd:pfam01018  36 GGRGGDVILVADENLNTLLDFRYKrhFKAENGENGGGKNCHGKNGEDLIIKVPVGTVVKDAEtgEVLADLTEPGQRVLVA 115
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568920345  183 LGGAGGKGNRFFLANDNRAPVTCTPGQPGQERVLYLELKT 222
Cdd:pfam01018 116 KGGRGGRGNAHFKTSTNQAPRFAEPGEPGEERWLELELKL 155
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
227-381 1.38e-21

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: 90.38  E-value: 1.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 227 GMVGFPNAGKSSLLRAISNAKPA-VASYPFTTLNPHVGIVHYEGHQQVAVADIPGIIRGAHQNKGLGLSFLRHIERCRFF 305
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGiVSPIPGTTRDPVRKEWELLPLGPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 306 LFVVDLTLPEpwtqvDDLKYELEKFEEglSERSHVIIANKIDLPQARARL-----PQLQARLGQEAIGLSALTGENLEQL 380
Cdd:cd00880   81 LLVVDSDLTP-----VEEEAKLGLLRE--RGKPVLLVLNKIDLVPESEEEellreRKLELLPDLPVIAVSALPGEGIDEL 153

                 .
gi 568920345 381 L 381
Cdd:cd00880  154 R 154
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
230-397 1.92e-20

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 91.43  E-value: 1.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 230 GFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGivHYE-GHQQVAVADIPGII-----------RGAhqnkglgLSFLR 297
Cdd:COG1084  167 GYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVG--HFErGHGRYQVIDTPGLLdrplserneieRQA-------ILALK 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 298 HIERCrfFLFVVDLTlpepwtqvDDLKYELEKFEEGLSE-RSH-----VIIANKIDLpqarARLPQLQARLGQEAIGLSA 371
Cdd:COG1084  238 HLADV--ILFLFDPS--------ETCGYSLEEQLNLLEEiRSLfdvpvIVVINKIDL----SDEEELKEAEEEADIKISA 303
                        170       180
                 ....*....|....*....|....*.
gi 568920345 372 LTGENLEQLLLHLKELHDAHIEAELE 397
Cdd:COG1084  304 LTGEGVDELLDELIEALEEEPELPPE 329
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
230-387 2.71e-20

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: 87.23  E-value: 2.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 230 GFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGivHYE-GHQQVAVADIPGIIRGAHQNKG----LGLSFLRHIERCrf 304
Cdd:cd01897    7 GYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVG--HFDyKYLRWQVIDTPGILDRPLEERNtiemQAITALAHLRAA-- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 305 FLFVVDLTlpepwtqvDDLKYELEK----FEE--GLSERSHVIIANKIDL--PQARARLPQLQARLGQEAIGLSALTGEN 376
Cdd:cd01897   83 VLFFIDPS--------ETCGYSIEEqlslFKEikPLFNKPVIVVLNKIDLltEEDLSEIEKELEKEGEEVIKISTLTEEG 154
                        170
                 ....*....|.
gi 568920345 377 LEQLLLHLKEL 387
Cdd:cd01897  155 VDELKNKACEL 165
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
229-381 1.46e-17

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: 79.42  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 229 VGFPNAGKSSLLRAISNAK-PAVASYPFTTLNPHVGIVHYEGHQ-QVAVADIPGIIRGahQNKGLGLSFLRHIERCRFFL 306
Cdd:cd00882    3 VGRGGVGKSSLLNALLGGEvGEVSDVPGTTRDPDVYVKELDKGKvKLVLVDTPGLDEF--GGLGREELARLLLRGADLIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 307 FVVDLTLPEpwtQVDDLKYELEKFEEGlSERSHVIIANKIDLPQAR-----ARLPQLQARLGQEAIGLSALTGENLEQLL 381
Cdd:cd00882   81 LVVDSTDRE---SEEDAKLLILRRLRK-EGIPIILVGNKIDLLEEReveelLRLEELAKILGVPVFEVSAKTGEGVDELF 156
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
226-299 1.13e-15

Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 77.75  E-value: 1.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 226 AGMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIV------------HYEG----HQQVAVADIPGIIRGAHQNK 289
Cdd:COG0012    3 CGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGVVpvpderldklaeIVKPkkivPATIEFVDIAGLVKGASKGE 82
                         90
                 ....*....|
gi 568920345 290 GLGLSFLRHI 299
Cdd:COG0012   83 GLGNQFLANI 92
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
227-310 1.56e-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: 76.88  E-value: 1.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 227 GMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIVHYE--------GHQQ---------------VAVADIPGIIR 283
Cdd:cd01899    2 GLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVGYVRvecpckelGVSCnprygkcidgkryvpVELIDVAGLVP 81
                         90       100
                 ....*....|....*....|....*..
gi 568920345 284 GAHQNKGLGLSFLRHIERCRFFLFVVD 310
Cdd:cd01899   82 GAHEGKGLGNQFLDDLRDADVLIHVVD 108
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
226-299 1.63e-15

YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of GTPases: Obg, DRG, Ygr210, and NOG1. Obg is an essential gene that is involved in DNA replication in C. crescentus and Streptomyces griseus and is associated with the ribosome. Several members of the family, including YchF, possess the TGS domain related to the RNA-binding proteins. Experimental data and genomic analysis suggest that YchF may be part of a nucleoprotein complex and may function as a GTP-dependent translational factor.


Pssm-ID: 206687 [Multi-domain]  Cd Length: 274  Bit Score: 75.96  E-value: 1.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 226 AGMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIV------------HYEG----HQQVAVADIPGIIRGAHQNK 289
Cdd:cd01900    1 IGIVGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIVpvpderldklaeIVKPkkivPATIEFVDIAGLVKGASKGE 80
                         90
                 ....*....|
gi 568920345 290 GLGLSFLRHI 299
Cdd:cd01900   81 GLGNKFLSHI 90
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
229-387 1.85e-14

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: 70.57  E-value: 1.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 229 VGFPNAGKSSLLRAISNAKPA-VASYPFTTLNPHVGIVHYEGHQQVAVaDIPGIIrgaHQNKGLGLSFLRH----IERCR 303
Cdd:cd04163    9 IGRPNVGKSTLLNALVGQKISiVSPKPQTTRNRIRGIYTDDDAQIIFV-DTPGIH---KPKKKLGERMVKAawsaLKDVD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 304 FFLFVVDLTlpEPWTqvDDLKYELEKFEEglSERSHVIIANKIDLPQARARLPQLQARL-----GQEAIGLSALTGENLE 378
Cdd:cd04163   85 LVLFVVDAS--EWIG--EGDEFILELLKK--SKTPVILVLNKIDLVKDKEDLLPLLEKLkelhpFAEIFPISALKGENVD 158

                 ....*....
gi 568920345 379 QLLLHLKEL 387
Cdd:cd04163  159 ELLEYIVEY 167
era PRK00089
GTPase Era; Reviewed
229-387 2.47e-14

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 72.77  E-value: 2.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 229 VGFPNAGKSSLLRAISNAKPA-VASYPFTTLNPHVGIVHYEGHQQVAVaDIPGIIRGAHQ-NKGLGLSFLRHIERCRFFL 306
Cdd:PRK00089  11 VGRPNVGKSTLLNALVGQKISiVSPKPQTTRHRIRGIVTEDDAQIIFV-DTPGIHKPKRAlNRAMNKAAWSSLKDVDLVL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 307 FVVDLTlpEPWTQVDdlKYELEKFEEglSERSHVIIANKIDLPQARARLPQLQARLGQ-----EAIGLSALTGENLEQLL 381
Cdd:PRK00089  90 FVVDAD--EKIGPGD--EFILEKLKK--VKTPVILVLNKIDLVKDKEELLPLLEELSElmdfaEIVPISALKGDNVDELL 163

                 ....*.
gi 568920345 382 LHLKEL 387
Cdd:PRK00089 164 DVIAKY 169
PRK09602 PRK09602
translation-associated GTPase; Reviewed
223-310 3.09e-14

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 73.69  E-value: 3.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 223 MAHAGMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGI-------VHYE--------------GHQQVAVA--DIP 279
Cdd:PRK09602   1 MITIGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVayvrvecPCKElgvkcnprngkcidGTRFIPVEliDVA 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 568920345 280 GIIRGAHQNKGLGLSFLRHIERCRFFLFVVD 310
Cdd:PRK09602  81 GLVPGAHEGRGLGNQFLDDLRQADALIHVVD 111
PTZ00258 PTZ00258
GTP-binding protein; Provisional
227-309 6.77e-14

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 72.67  E-value: 6.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 227 GMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIV------------HYEGHQQVA----VADIPGIIRGAHQNKG 290
Cdd:PTZ00258  25 GIVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVnvpderfdwlckHFKPKSIVPaqldITDIAGLVKGASEGEG 104
                         90
                 ....*....|....*....
gi 568920345 291 LGLSFLRHIERCRFFLFVV 309
Cdd:PTZ00258 105 LGNAFLSHIRAVDGIYHVV 123
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
228-386 6.80e-13

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 66.54  E-value: 6.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 228 MVGFPNAGKSSLLRAISNAKPAVASYpfttLNPHvGIVHY-------EGHQQVAVADIPGI--IRGAHQnkglglSFLRH 298
Cdd:COG1100    8 VVGTGGVGKTSLVNRLVGDIFSLEKY----LSTN-GVTIDkkelkldGLDVDLVIWDTPGQdeFRETRQ------FYARQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 299 IERCRFFLFVVDLTLPEPWTqvdDLKYELEKFEE-GLSERShVIIANKIDLPQARARLPQ--LQARLGQEAIG----LSA 371
Cdd:COG1100   77 LTGASLYLFVVDGTREETLQ---SLYELLESLRRlGKKSPI-ILVLNKIDLYDEEEIEDEerLKEALSEDNIVevvaTSA 152
                        170
                 ....*....|....*
gi 568920345 372 LTGENLEQLLLHLKE 386
Cdd:COG1100  153 KTGEGVEELFAALAE 167
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
229-387 1.69e-12

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 67.32  E-value: 1.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 229 VGFPNAGKSSLLRAISNAKPA-VASYPFTTLNPHVGIVHYEGHQQVAVaDIPGIIRGAHQnkgLGLSFLR----HIERCR 303
Cdd:COG1159    9 VGRPNVGKSTLLNALVGQKVSiVSPKPQTTRHRIRGIVTREDAQIVFV-DTPGIHKPKRK---LGRRMNKaawsALEDVD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 304 FFLFVVDLTlpEPWTQVDdlKYELEKFEEglSERSHVIIANKIDLPQARARLPQLQA--RLGQEA--IGLSALTGENLEQ 379
Cdd:COG1159   85 VILFVVDAT--EKIGEGD--EFILELLKK--LKTPVILVINKIDLVKKEELLPLLAEysELLDFAeiVPISALKGDNVDE 158

                 ....*...
gi 568920345 380 LLLHLKEL 387
Cdd:COG1159  159 LLDEIAKL 166
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
229-387 2.31e-12

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: 64.44  E-value: 2.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 229 VGFPNAGKSSLLRAISNakpavasypfttlnphvgivhyeghQQVA-VADIPG----IIRGAHQNKGLGLSF-----LRH 298
Cdd:cd04164    9 AGKPNVGKSSLLNALAG-------------------------RDRAiVSDIAGttrdVIEEEIDLGGIPVRLidtagLRE 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 299 ---------IERCR-------FFLFVVDLTlpEPWTQVDDLKYELekfeegLSERSHVIIANKIDLPQARARLPQLqarL 362
Cdd:cd04164   64 tedeiekigIERAReaieeadLVLLVVDAS--EGLDEEDLEILEL------PAKKPVIVVLNKSDLLSDAEGISEL---N 132
                        170       180
                 ....*....|....*....|....*
gi 568920345 363 GQEAIGLSALTGENLEQLLLHLKEL 387
Cdd:cd04164  133 GKPIIAISAKTGEGIDELKEALLEL 157
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
229-387 4.32e-12

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: 64.79  E-value: 4.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 229 VGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIVHYEGHQQVAVADIPGIIRG-AHQnkgLGLSF---LRHIERCRF 304
Cdd:cd01878   47 VGYTNAGKSTLFNALTGADVLAEDQLFATLDPTTRRIKLPGGREVLLTDTVGFIRDlPHQ---LVEAFrstLEEVAEADL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 305 FLFVVDLTLPEPWTQVDDLKYELEkfEEGLSERSHVIIANKIDLPQARARLPQLQARLGqEAIGLSALTGENLEQLLLHL 384
Cdd:cd01878  124 LLHVVDASDPDREEQIETVEEVLK--ELGADDIPIILVLNKIDLLDDEELEERLRAGRP-DAVFISAKTGEGLDLLKEAI 200

                 ...
gi 568920345 385 KEL 387
Cdd:cd01878  201 EEL 203
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
227-380 1.31e-11

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: 62.39  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345  227 GMVGFPNAGKSSLLRAISNAKPA-VASYPFTTLNPHVGIVHYEGHQ-QVAVADIPGIIRGAHQNKGlglsFLRHIERcrf 304
Cdd:TIGR00231   5 VIVGHPNVGKSTLLNSLLGNKGSiTEYYPGTTRNYVTTVIEEDGKTyKFNLLDTAGQEDYDAIRRL----YYPQVER--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345  305 FLFVVDLTL--------PEPWTqvddlkYELEKFEEGLSERshVIIANKIDLPQARArLPQLQ---ARLGQEA-IGLSAL 372
Cdd:TIGR00231  78 SLRVFDIVIlvldveeiLEKQT------KEIIHHADSGVPI--ILVGNKIDLKDADL-KTHVAsefAKLNGEPiIPLSAE 148

                  ....*...
gi 568920345  373 TGENLEQL 380
Cdd:TIGR00231 149 TGKNIDSA 156
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
229-387 2.40e-11

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: 65.08  E-value: 2.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 229 VGFPNAGKSSLLRAISNakpavasypfttlnphvgivhyeghQQVA-VADIPG----IIRGAHQNKGLGLSF-----LRH 298
Cdd:COG0486  219 VGRPNVGKSSLLNALLG-------------------------EERAiVTDIAGttrdVIEERINIGGIPVRLidtagLRE 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 299 ---------IERCR-------FFLFVVDLTlpEPWTQVDdlkyelEKFEEGLSERSHVIIANKIDLPQARARlpQLQARL 362
Cdd:COG0486  274 tedevekigIERAReaieeadLVLLLLDAS--EPLTEED------EEILEKLKDKPVIVVLNKIDLPSEADG--ELKSLP 343
                        170       180
                 ....*....|....*....|....*
gi 568920345 363 GQEAIGLSALTGENLEQLLLHLKEL 387
Cdd:COG0486  344 GEPVIAISAKTGEGIDELKEAILEL 368
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
228-390 4.42e-11

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: 60.93  E-value: 4.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 228 MVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIVHYEGHqQVAVADIPGI--IRGAHQNKGLGLSFLRHiERCRFF 305
Cdd:cd01879    2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGK-EIEIVDLPGTysLTPYSEDEKVARDFLLG-EEPDLI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 306 LFVVD---------LTLpepwtQVddlkyelekFEEGLsersHVIIA-NKIDLpqARAR-----LPQLQARLGQEAIGLS 370
Cdd:cd01879   80 VNVVDatnlernlyLTL-----QL---------LELGL----PVVVAlNMIDE--AEKRgikidLDKLSELLGVPVVPTS 139
                        170       180
                 ....*....|....*....|
gi 568920345 371 ALTGENLEQLLLHLKELHDA 390
Cdd:cd01879  140 ARKGEGIDELLDAIAKLAES 159
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
229-387 5.64e-11

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 63.98  E-value: 5.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 229 VGFPNAGKSSLLRAISNAKPA-VASYPFTT---LnphvgivhyegHQQVAVADIP-------GI-----------IRGAH 286
Cdd:PRK05291 221 AGRPNVGKSSLLNALLGEERAiVTDIAGTTrdvI-----------EEHINLDGIPlrlidtaGIretddevekigIERSR 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 287 QnkglglsflrHIERCRFFLFVVDLTlpEPWTQVDDLKYELEKfeeglsERSHVIIANKIDLPQArarlPQLQARLGQEA 366
Cdd:PRK05291 290 E----------AIEEADLVLLVLDAS--EPLTEEDDEILEELK------DKPVIVVLNKADLTGE----IDLEEENGKPV 347
                        170       180
                 ....*....|....*....|.
gi 568920345 367 IGLSALTGENLEQLLLHLKEL 387
Cdd:PRK05291 348 IRISAKTGEGIDELREAIKEL 368
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
229-387 2.63e-10

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: 61.34  E-value: 2.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345  229 VGFPNAGKSSLLRAISNakpavasypfttlnphvgivhyeghQQVA-VADIPG----IIRGAHQNKGLGLSF-----LRH 298
Cdd:pfam12631 100 VGKPNVGKSSLLNALLG-------------------------EERAiVTDIPGttrdVIEETINIGGIPLRLidtagIRE 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345  299 ----------------IERCRFFLFVVDLTlpEPWTQVDdlkyelEKFEEGLSERSHVI-IANKIDLPQArarLPQLQAR 361
Cdd:pfam12631 155 tddevekigierareaIEEADLVLLVLDAS--RPLDEED------LEILELLKDKKPIIvVLNKSDLLGE---IDELEEL 223
                         170       180
                  ....*....|....*....|....*.
gi 568920345  362 LGQEAIGLSALTGENLEQLLLHLKEL 387
Cdd:pfam12631 224 KGKPVLAISAKTGEGLDELEEAIKEL 249
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
229-396 7.33e-10

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 60.10  E-value: 7.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 229 VGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIVHYEGHQQVAVADIPGIIRG-AHQnkglgL--SF---LRHIERC 302
Cdd:COG2262  205 VGYTNAGKSTLFNRLTGADVLAEDKLFATLDPTTRRLELPDGRPVLLTDTVGFIRKlPHQ-----LveAFrstLEEVREA 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 303 RFFLFVVDLTLPEPWTQ---VDDLKYELekfeeGLSERSHVIIANKIDL--PQARARLPQLQArlgqEAIGLSALTGENL 377
Cdd:COG2262  280 DLLLHVVDASDPDFEEQietVNEVLEEL-----GADDKPIILVFNKIDLldDEELERLRAGYP----DAVFISAKTGEGI 350
                        170       180
                 ....*....|....*....|
gi 568920345 378 EQLLLHLKE-LHDAHIEAEL 396
Cdd:COG2262  351 DELLEAIEErLPEDRVEVEL 370
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
226-399 1.36e-09

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: 58.55  E-value: 1.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345  226 AGMVGFPNAGKSSLLRAISNAKPAVAS-YPFTTLNPHVGIvHYEGHQQVAVADIPGIIRGAHQNKGLGLSFLRH-IERCR 303
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHGQKISITSpKAQTTRNRISGI-HTTGASQIIFIDTPGFHEKKHSLNRLMMKEARSaIGGVD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345  304 FFLFVVDLTlpePWTQVDDLKyeLEKFEEglSERSHVIIANKIDLPQARARLPQLQARLGQE----AIGLSALTGENLEQ 379
Cdd:TIGR00436  82 LILFVVDSD---QWNGDGEFV--LTKLQN--LKRPVVLTRNKLDNKFKDKLLPLIDKYAILEdfkdIVPISALTGDNTSF 154
                         170       180
                  ....*....|....*....|
gi 568920345  380 LLlhlkelhdAHIEAELEQG 399
Cdd:TIGR00436 155 LA--------AFIEVHLPEG 166
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
228-381 1.78e-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: 53.35  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 228 MVGFPNAGKSSLLRAIsnakpavASYPFTTLNPHVG----IVHYEGHQqVAVADIPGiirgahQNKglglsfLRHI---- 299
Cdd:cd00878    4 MLGLDGAGKTTILYKL-------KLGEVVTTIPTIGfnveTVEYKNVK-FTVWDVGG------QDK------IRPLwkhy 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 300 -ERCRFFLFVVDLTLPEpwtQVDDLKYELEKF--EEGLSERSHVIIANKIDLPQARaRLPQLQARLGQEAI--------G 368
Cdd:cd00878   64 yENTDGLIFVVDSSDRE---RIEEAKNELHKLlnEEELKGAPLLILANKQDLPGAL-TESELIELLGLESIkgrrwhiqP 139
                        170
                 ....*....|...
gi 568920345 369 LSALTGENLEQLL 381
Cdd:cd00878  140 CSAVTGDGLDEGL 152
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
228-387 1.63e-07

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: 50.49  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 228 MVGFPNAGKSSLLRAISNAKPaVASYPftTLNPHVGIVHYEGHQQVAVADIPGiirgahQNKgLGLSFLRHIERCRFFLF 307
Cdd:cd04156    4 LLGLDSAGKSTLLYKLKHAEL-VTTIP--TVGFNVEMLQLEKHLSLTVWDVGG------QEK-MRTVWKCYLENTDGLVY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 308 VVDLTLPEpwtQVDDLKYELEKF--EEGLSERSHVIIANKIDLPQA--------RARLPQLQARLGQEAIGLSALTGENL 377
Cdd:cd04156   74 VVDSSDEA---RLDESQKELKHIlkNEHIKGVPVVLLANKQDLPGAltaeeitrRFKLKKYCSDRDWYVQPCSAVTGEGL 150
                        170
                 ....*....|
gi 568920345 378 EQLLLHLKEL 387
Cdd:cd04156  151 AEAFRKLASF 160
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
228-388 2.38e-07

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: 50.51  E-value: 2.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 228 MVGFPNAGKSSLLRAISNAKPAVAS-YPFTTLNPHVGIVHYEGHQQVAVaDIPGIIRGAHQNKGL----GLSFLRHIERC 302
Cdd:cd01895    7 IIGRPNVGKSSLLNALLGEERVIVSdIAGTTRDSIDVPFEYDGQKYTLI-DTAGIRKKGKVTEGIekysVLRTLKAIERA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 303 RFFLFVVDLTlpEPWTQVDdlkyelEK-----FEEGlseRSHVIIANKIDLPQA------------RARLPQLQ-ARLgq 364
Cdd:cd01895   86 DVVLLVLDAS--EGITEQD------LRiagliLEEG---KALIIVVNKWDLVEKdektmkefekelRRKLPFLDyAPI-- 152
                        170       180
                 ....*....|....*....|....
gi 568920345 365 eaIGLSALTGENLEQLLLHLKELH 388
Cdd:cd01895  153 --VFISALTGQGVDKLFDAIKEVY 174
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
229-391 3.77e-06

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 48.87  E-value: 3.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 229 VGFPNAGKSSLLRAISNAKPAVAS-YPFTTLNPhvgI---VHYEGHQQVAVaDIPGIIRGAHQNKGL-GLSFLR---HIE 300
Cdd:COG1160  181 VGRPNVGKSSLINALLGEERVIVSdIAGTTRDS---IdtpFERDGKKYTLI-DTAGIRRKGKVDEGIeKYSVLRtlrAIE 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 301 RCRFFLFVVDLTlpEPWTQVDdlkyelEK-----FEEGlseRSHVIIANKIDL------------PQARARLPQLQ-ARL 362
Cdd:COG1160  257 RADVVLLVIDAT--EGITEQD------LKiaglaLEAG---KALVIVVNKWDLvekdrktreeleKEIRRRLPFLDyAPI 325
                        170       180
                 ....*....|....*....|....*....
gi 568920345 363 gqeaIGLSALTGENLEQLLLHLKELHDAH 391
Cdd:COG1160  326 ----VFISALTGQGVDKLLEAVDEVYESA 350
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
228-394 4.92e-06

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 48.64  E-value: 4.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 228 MVGFPNAGKSSLLRAISNAKPAVAS-YPFTTLNPHVGIVHYEGHQQVAVaDIPGIIRGAHQNKGLGL-SFLRH---IERC 302
Cdd:PRK09518 455 LVGRPNVGKSSLLNQLTHEERAVVNdLAGTTRDPVDEIVEIDGEDWLFI-DTAGIKRRQHKLTGAEYySSLRTqaaIERS 533
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 303 RFFLFVVDLTlpEPWTQvDDLKYELEKFEEGlseRSHVIIANKIDLPQARARlpQLQARLGQ---------EAIGLSALT 373
Cdd:PRK09518 534 ELALFLFDAS--QPISE-QDLKVMSMAVDAG---RALVLVFNKWDLMDEFRR--QRLERLWKtefdrvtwaRRVNLSAKT 605
                        170       180
                 ....*....|....*....|.
gi 568920345 374 GEnleqlllHLKELHDAHIEA 394
Cdd:PRK09518 606 GW-------HTNRLAPAMQEA 619
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
221-405 8.94e-06

Fe2+ transporter FeoB [Inorganic ion transport and metabolism];


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 47.81  E-value: 8.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 221 KTMAHAGMVGFPNAGKSSLLRAISNAKPAVASYPFTTLNPHVGIVHYEGHqQVAVADIPGIIrgahqnkglGLS------ 294
Cdd:COG0370    1 MKMITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKGK-EIELVDLPGTY---------SLSayspde 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 295 -----FLRHiERCRFFLFVVD---------LTLpepwtqvdDLKyELEKfeeglsersHVIIA-NKIDLpqARAR----- 354
Cdd:COG0370   71 kvardFLLE-EKPDVVVNVVDatnlernlyLTL--------QLL-ELGI---------PVVLAlNMMDE--AEKKgikid 129
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568920345 355 LPQLQARLGQEAIGLSALTGENLEQLLLHLKELH------------DAHIEAELEQ--------GRQPLRW 405
Cdd:COG0370  130 VEKLSKLLGVPVVPTSARKGKGIDELKEAIIEAAegkkprplridyPEEIEEAIEEleelleedGPYPSRW 200
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
216-281 1.10e-04

Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH 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.


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 42.64  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 216 LYLELKTMAHAG----MVGFPNAGKSSLLRAI------------SNAKPAVASYPFTTLNphvgIVHYEGHQQVAVADIP 279
Cdd:cd01855  114 LIEEIKKLAKYRgdvyVVGATNVGKSTLINALlksnggkvqaqaLVQRLTVSPIPGTTLG----LIKIPLGEGKKLYDTP 189

                 ..
gi 568920345 280 GI 281
Cdd:cd01855  190 GI 191
Arl2 cd04154
Arf-like 2 (Arl2) GTPase; Arl2 (Arf-like 2) GTPases are members of the Arf family that bind ...
228-379 2.43e-04

Arf-like 2 (Arl2) GTPase; Arl2 (Arf-like 2) GTPases are members of the Arf family that bind GDP and GTP with very low affinity. Unlike most Arf family proteins, Arl2 is not myristoylated at its N-terminal helix. The protein PDE-delta, first identified in photoreceptor rod cells, binds specifically to Arl2 and is structurally very similar to RhoGDI. Despite the high structural similarity between Arl2 and Rho proteins and between PDE-delta and RhoGDI, the interactions between the GTPases and their effectors are very different. In its GTP bound form, Arl2 interacts with the protein Binder of Arl2 (BART), and the complex is believed to play a role in mitochondrial adenine nucleotide transport. In its GDP bound form, Arl2 interacts with tubulin- folding Cofactor D; this interaction is believed to play a role in regulation of microtubule dynamics that impact the cytoskeleton, cell division, and cytokinesis.


Pssm-ID: 206720 [Multi-domain]  Cd Length: 173  Bit Score: 41.54  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 228 MVGFPNAGKSSLLRAISNAkpavasyPFTTLNPHVGI----VHYEGHQqVAVADIPGiirgahqNKGLGLSFLRHIERCR 303
Cdd:cd04154   19 MLGLDNAGKTTILKKFNGE-------DISTISPTLGFniktLEYNGYK-LNIWDVGG-------QKSLRSYWRNYFESTD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 304 FFLFVVDLTLPEpwtQVDDLKYELEKF--EEGLSERSHVIIANKIDLPQARArLPQLQARLGQEAI--------GLSALT 373
Cdd:cd04154   84 ALIWVVDSSDRA---RLEDCKRELQKLlvEERLAGATLLIFANKQDLPGALS-PEEIREVLELDSIkshhwrifGCSAVT 159

                 ....*.
gi 568920345 374 GENLEQ 379
Cdd:cd04154  160 GENLLD 165
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
228-381 4.93e-04

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


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 40.29  E-value: 4.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345  228 MVGFPNAGKSSLLRAISNaKPAVASYPftTLNPHVGIVHYEGHQqVAVADIpgiirGAHQNkglglsfLRHIERCRF--- 304
Cdd:pfam00025   5 ILGLDNAGKTTILYKLKL-GEIVTTIP--TIGFNVETVTYKNVK-FTVWDV-----GGQES-------LRPLWRNYFpnt 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345  305 --FLFVVDLTLPEpwtQVDDLKYELEKF--EEGLSERSHVIIANKIDLPQArARLPQLQARLGQEAI--------GLSAL 372
Cdd:pfam00025  69 daVIFVVDSADRD---RIEEAKEELHALlnEEELADAPLLILANKQDLPGA-MSEAEIRELLGLHELkdrpweiqGCSAV 144

                  ....*....
gi 568920345  373 TGENLEQLL 381
Cdd:pfam00025 145 TGEGLDEGL 153
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
213-259 9.52e-04

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: 39.14  E-value: 9.52e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568920345 213 ERVLYLELKTMAHAGMVGFPNAGKSSLLRAISNAKP-AVASYP-----FTTLN 259
Cdd:cd01857   72 IVVLFFSALNEATIGLVGYPNVGKSSLINALVGSKKvSVSSTPgktkhFQTIF 124
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
229-387 1.61e-03

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: 39.03  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 229 VGFPNAGKSSLLRAISNAK--PAVASYPFTT--LNphvgivHYEGHQQVAVADIPG-----IIRGAHQN-KGLGLSFLRH 298
Cdd:cd01876    5 AGRSNVGKSSLINALTNRKklARTSKTPGRTqlIN------FFNVGDKFRLVDLPGygyakVSKEVREKwGKLIEEYLEN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 299 IERCRFFLFVVDLTLPepwTQVDDLKYeLEKFEEglSERSHVIIANKID-LPQ--ARARLPQLQARLGQEA-----IGLS 370
Cdd:cd01876   79 RENLKGVVLLIDARHG---PTPIDLEM-LEFLEE--LGIPFLIVLTKADkLKKseLAKVLKKIKEELNLFNilppvILFS 152
                        170
                 ....*....|....*..
gi 568920345 371 ALTGENLEQLLLHLKEL 387
Cdd:cd01876  153 SKKGTGIDELRALIAEW 169
PRK00098 PRK00098
GTPase RsgA; Reviewed
340-386 1.61e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 40.19  E-value: 1.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568920345 340 VIIANKIDL----PQARARLpQLQARLGQEAIGLSALTGENLEQLLLHLKE 386
Cdd:PRK00098 115 IIVLNKIDLlddlEEARELL-ALYRAIGYDVLELSAKEGEGLDELKPLLAG 164
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
227-262 1.72e-03

Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, and archaea. They all exhibit a circular permutation of the GTPase signature motifs so that the order of the conserved G box motifs is G4-G5-G1-G2-G3, with G4 and G5 being permuted from the C-terminal region of proteins in the Ras superfamily to the N-terminus of YlqF-related GTPases.


Pssm-ID: 206746 [Multi-domain]  Cd Length: 146  Bit Score: 38.52  E-value: 1.72e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 568920345 227 GMVGFPNAGKSSLLRAISNAKPAVASY--PFTTLNPHV 262
Cdd:cd01849   95 GVVGLPNVGKSSFINALLNKFKLKVGSipGTTKLQQDV 132
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
340-403 2.42e-03

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: 40.00  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 340 VIIA-NKIDLPQARarlP-----QLQAR------LGQEAI--GLSALTGENLEQLL---------LHLKELHDAH----- 391
Cdd:COG0532  106 IIVAiNKIDKPGAN---PdrvkqELAEHglvpeeWGGDTIfvPVSAKTGEGIDELLemillqaevLELKANPDRPargtv 182
                         90
                 ....*....|..
gi 568920345 392 IEAELEQGRQPL 403
Cdd:COG0532  183 IEAKLDKGRGPV 194
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
228-384 4.40e-03

Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible.


Pssm-ID: 206640 [Multi-domain]  Cd Length: 159  Bit Score: 37.44  E-value: 4.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 228 MVGFPNAGKSSLLRAISNAKpavasypFT-TLNPHVGI------VHYEGHQ-QVAVADIPGIIRgahqNKGLGLSFLRHi 299
Cdd:cd00154    5 LIGDSGVGKTSLLLRFVDNK-------FSeNYKSTIGVdfksktIEVDGKKvKLQIWDTAGQER----FRSITSSYYRG- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 300 erCRFFLFVVDLTLPEPWTQVDDLKYELEkfEEGLSERSHVIIANKIDLPQARA----RLPQLQARLGQEAIGLSALTGE 375
Cdd:cd00154   73 --AHGAILVYDVTNRESFENLDKWLNELK--EYAPPNIPIILVGNKSDLEDERQvsteEAQQFAKENGLLFFETSAKTGE 148

                 ....*....
gi 568920345 376 NLEQLLLHL 384
Cdd:cd00154  149 NVDEAFESL 157
Rab28 cd04109
Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown ...
306-375 4.79e-03

Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown to be a late embryogenesis-abundant (Lea) protein that is regulated by the plant hormone abcisic acid (ABA). In Arabidopsis, Rab28 is expressed during embryo development and is generally restricted to provascular tissues in mature embryos. Unlike maize Rab28, it is not ABA-inducible. Characterization of the human Rab28 homolog revealed two isoforms, which differ by a 95-base pair insertion, producing an alternative sequence for the 30 amino acids at the C-terminus. The two human isoforms are presumably the result of alternative splicing. Since they differ at the C-terminus but not in the GTP-binding region, they are predicted to be targeted to different cellular locations. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 206694 [Multi-domain]  Cd Length: 213  Bit Score: 38.24  E-value: 4.79e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568920345 306 LFVVDLTLPEPWTQVDDLKYELEK-FEEGLSERSHVIIANKIDLPQARARLPQLQARLGQE----AIGLSALTGE 375
Cdd:cd04109   78 CLVYDITNSQSFENLEDWLSVVKKvNEESETKPKMVLVGNKTDLEHNRQVTAEKHARFAQEndmeSIFVSAKTGD 152
Arl5_Arl8 cd04153
Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like ...
228-381 5.48e-03

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: 37.71  E-value: 5.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 228 MVGFPNAGKSSLLRAISnAKPAVASYPftTLNPHVGIVHYEGhQQVAVADIPGiirgahqNKGLGLSFLRHIERCRFFLF 307
Cdd:cd04153   20 IVGLDNAGKTTILYQFL-LGEVVHTSP--TIGSNVEEIVYKN-IRFLMWDIGG-------QESLRSSWNTYYTNTDAVIL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920345 308 VVDLTLPEpwtQVDDLKYELEKF--EEGLSERSHVIIANKIDLPQA---------------RARLPQLQarlgqeaiGLS 370
Cdd:cd04153   89 VIDSTDRE---RLPLTKEELYKMlaHEDLRKAVLLVLANKQDLKGAmtpaeiseslgltsiRDHTWHIQ--------GCC 157
                        170
                 ....*....|.
gi 568920345 371 ALTGENLEQLL 381
Cdd:cd04153  158 ALTGEGLPEGL 168
 
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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