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Conserved domains on  [gi|119580378|gb|EAW59974|]
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developmentally regulated GTP binding protein 1, isoform CRA_a [Homo sapiens]

Protein Classification

DRG domain-containing protein( domain architecture ID 10112295)

DRG domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 65-239 2.55e-114

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: 326.81  E-value: 2.55e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNL 144
Cdd:cd01896    1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378 145 ILIVLDVLKPLGHKKIIENELEGFGIRLNSKPPNIGFKKKDKGGINLTATCPQSELDAETVKSILAEYKIHNADVTLRSD 224
Cdd:cd01896   81 ILIVLDATKPEGQREILERELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLTKLDEKTVKAILREYKIHNADVLIRED 160

                        170
                 ....*....|....*
gi 119580378 225 ATADDLIDVVEGNSV 239
Cdd:cd01896  161 ITVDDLIDVIEGNRV 175
 
Name Accession Description Interval E-value
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 65-239 2.55e-114

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: 326.81  E-value: 2.55e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNL 144
Cdd:cd01896    1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378 145 ILIVLDVLKPLGHKKIIENELEGFGIRLNSKPPNIGFKKKDKGGINLTATCPQSELDAETVKSILAEYKIHNADVTLRSD 224
Cdd:cd01896   81 ILIVLDATKPEGQREILERELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLTKLDEKTVKAILREYKIHNADVLIRED 160

                        170
                 ....*....|....*
gi 119580378 225 ATADDLIDVVEGNSV 239
Cdd:cd01896  161 ITVDDLIDVIEGNRV 175
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
7-239 1.15e-106

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 312.12  E-value: 1.15e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378   7 KIAEIEAEMARTQKNKATAHHLGLLKARLAKLRRELITPKGGGGGGPGEgFDVAKTGDARIGFVGFPSVGKSTLLSNLAG 86
Cdd:COG1163    7 KIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEG-FAVKKSGDATVVLVGFPSVGKSTLLNKLTN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  87 VYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNLILIVLDVLKPlGHKKIIENELE 166
Cdd:COG1163   86 AKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFEL-EQYDVLKEELY 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119580378 167 GFGIRLNSKPPNIGFKKKDKGGINLTATCPQsELDAETVKSILAEYKIHNADVTLRSDATADDLIDVVEGNSV 239
Cdd:COG1163  165 DAGIRLNKPPPDVTIEKKGKGGIRVNSTGKL-DLDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRV 236
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 64-217 6.31e-37

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: 127.49  E-value: 6.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378   64 DARIGFVGFPSVGKSTLLSNLAGVY-SEVAAYEFTTLTTVPGVIRYKG--AKIQLLDLPGIIEGAKDGKGRGRQVIAVAR 140
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKgSITEYYPGTTRNYVTTVIEEDGktYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  141 TCNLILIVLDVLKPL-GHKKIIENELE-GFGIRLNSKPPNIG---FKKKDKGGINLTATCPQSELDAETVKSILAEYKIH 215
Cdd:TIGR00231  81 VFDIVILVLDVEEILeKQTKEIIHHADsGVPIILVGNKIDLKdadLKTHVASEFAKLNGEPIIPLSAETGKNIDSAFKIV 160


                  ..
gi 119580378  216 NA 217
Cdd:TIGR00231 161 EA 162
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 66-183 2.90e-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: 103.47  E-value: 2.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378   66 RIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARtCNLI 145
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFLAIIE-ADLI 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 119580378  146 LIVLDVLKPLghkKIIENELEGFGIRLNsKPPNIGFKK 183
Cdd:pfam01926  80 LFVVDSEEGI---TPLDEELLELLRENK-KPIILVLNK 113
obgE PRK12299
GTPase CgtA; Reviewed
 65-176 8.71e-21

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 88.97  E-value: 8.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAK-IQLLDLPGIIEGAKDGKGRGRQVIA-VARtC 142
Cdd:PRK12299 159 ADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKsFVIADIPGLIEGASEGAGLGHRFLKhIER-T 237

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 119580378 143 NLILIVLDV--LKPLGHKKIIENELEGFGIRLNSKP 176
Cdd:PRK12299 238 RLLLHLVDIeaVDPVEDYKTIRNELEKYSPELADKP 273
 
Name Accession Description Interval E-value
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
 65-239 2.55e-114

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: 326.81  E-value: 2.55e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNL 144
Cdd:cd01896    1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRGRQVIAVARTADL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378 145 ILIVLDVLKPLGHKKIIENELEGFGIRLNSKPPNIGFKKKDKGGINLTATCPQSELDAETVKSILAEYKIHNADVTLRSD 224
Cdd:cd01896   81 ILIVLDATKPEGQREILERELEGVGIRLNKKPPNVTIKKKKKGGINITSTVPLTKLDEKTVKAILREYKIHNADVLIRED 160

                        170
                 ....*....|....*
gi 119580378 225 ATADDLIDVVEGNSV 239
Cdd:cd01896  161 ITVDDLIDVIEGNRV 175
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
7-239 1.15e-106

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 312.12  E-value: 1.15e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378   7 KIAEIEAEMARTQKNKATAHHLGLLKARLAKLRRELITPKGGGGGGPGEgFDVAKTGDARIGFVGFPSVGKSTLLSNLAG 86
Cdd:COG1163    7 KIKALEEEISKTPYNKATEKHIGRLKAKLAELKEELEKRKKKSGGGGEG-FAVKKSGDATVVLVGFPSVGKSTLLNKLTN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  87 VYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNLILIVLDVLKPlGHKKIIENELE 166
Cdd:COG1163   86 AKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIEGAASGKGRGKEVLSVVRNADLILIVLDVFEL-EQYDVLKEELY 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119580378 167 GFGIRLNSKPPNIGFKKKDKGGINLTATCPQsELDAETVKSILAEYKIHNADVTLRSDATADDLIDVVEGNSV 239
Cdd:COG1163  165 DAGIRLNKPPPDVTIEKKGKGGIRVNSTGKL-DLDEEDIKKILREYGIVNADVLIREDVTLDDLIDALMGNRV 236
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 64-217 6.31e-37

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: 127.49  E-value: 6.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378   64 DARIGFVGFPSVGKSTLLSNLAGVY-SEVAAYEFTTLTTVPGVIRYKG--AKIQLLDLPGIIEGAKDGKGRGRQVIAVAR 140
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKgSITEYYPGTTRNYVTTVIEEDGktYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  141 TCNLILIVLDVLKPL-GHKKIIENELE-GFGIRLNSKPPNIG---FKKKDKGGINLTATCPQSELDAETVKSILAEYKIH 215
Cdd:TIGR00231  81 VFDIVILVLDVEEILeKQTKEIIHHADsGVPIILVGNKIDLKdadLKTHVASEFAKLNGEPIIPLSAETGKNIDSAFKIV 160


                  ..
gi 119580378  216 NA 217
Cdd:TIGR00231 161 EA 162
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 68-187 5.03e-29

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: 107.09  E-value: 5.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  68 GFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYK-GAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNLIL 146
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGdGVDIQIIDLPGLLDGASEGRGLGEQILAHLYRSDLIL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 119580378 147 IVLDVLK-----PLGHKKIIENELEGFGIRLNSKPPNIGFKKKDKG 187
Cdd:cd01881   81 HVIDASEdcvgdPLEDQKTLNEEVSGSFLFLKNKPEMIVANKIDMA 126
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 66-183 2.90e-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: 103.47  E-value: 2.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378   66 RIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARtCNLI 145
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFLAIIE-ADLI 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 119580378  146 LIVLDVLKPLghkKIIENELEGFGIRLNsKPPNIGFKK 183
Cdd:pfam01926  80 LFVVDSEEGI---TPLDEELLELLRENK-KPIILVLNK 113
MMR_HSR1_Xtn pfam16897
C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of ...
 187-239 4.08e-25

C-terminal region of MMR_HSR1 domain; MMR_HSR1_Xtn is the C-terminal region of some members of the MMR_HSR1 family.


Pssm-ID: 465301 [Multi-domain]  Cd Length: 105  Bit Score: 95.19  E-value: 4.08e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 119580378  187 GGINLTATCPQSELDAETVKSILAEYKIHNADVTLRSDATADDLIDVVEGNSV 239
Cdd:pfam16897   1 GGINITSTVPLTKLDEETIKAILREYKIHNADVLIREDVTVDDLIDVIEGNRV 53
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 65-176 4.56e-25

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: 96.72  E-value: 4.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYK-GAKIQLLDLPGIIEGAKDGKGRG----RQviaVA 139
Cdd:cd01898    1 ADVGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDdGRSFVIADIPGLIEGASEGKGLGhrflRH---IE 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 119580378 140 RtCNLILIVLDV---LKPLGHKKIIENELEGFGIRLNSKP 176
Cdd:cd01898   78 R-TRVLLHVIDLsgeDDPVEDYETIRNELEAYNPGLAEKP 116
Obg_CgtA TIGR02729
Obg family GTPase CgtA; This model describes a univeral, mostly one-gene-per-genome ...
 65-185 8.42e-23

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: 94.41  E-value: 8.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378   65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAK-IQLLDLPGIIEGAKDGKGRGRQVIA-VARtC 142
Cdd:TIGR02729 158 ADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLVPNLGVVRVDDGRsFVIADIPGLIEGASEGAGLGHRFLKhIER-T 236

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 119580378  143 NLILIVLDV-----LKPLGHKKIIENELEGFGIRLNSKPPNIGFKKKD 185
Cdd:TIGR02729 237 RVLLHLIDIspedgSDPVEDYEIIRNELKKYSPELAEKPRIVVLNKID 284
obgE PRK12299
GTPase CgtA; Reviewed
 65-176 8.71e-21

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 88.97  E-value: 8.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAK-IQLLDLPGIIEGAKDGKGRGRQVIA-VARtC 142
Cdd:PRK12299 159 ADVGLVGLPNAGKSTLISAVSAAKPKIADYPFTTLHPNLGVVRVDDYKsFVIADIPGLIEGASEGAGLGHRFLKhIER-T 237

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 119580378 143 NLILIVLDV--LKPLGHKKIIENELEGFGIRLNSKP 176
Cdd:PRK12299 238 RLLLHLVDIeaVDPVEDYKTIRNELEKYSPELADKP 273
obgE PRK12297
GTPase CgtA; Reviewed
 65-176 4.34e-20

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 87.85  E-value: 4.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAK-IQLLDLPGIIEGAKDGKGRGRQVIA-VARtC 142
Cdd:PRK12297 159 ADVGLVGFPNVGKSTLLSVVSNAKPKIANYHFTTLVPNLGVVETDDGRsFVMADIPGLIEGASEGVGLGHQFLRhIER-T 237

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 119580378 143 NLILIVLDVLK-----PLGHKKIIENELEGFGIRLNSKP 176
Cdd:PRK12297 238 RVIVHVIDMSGsegrdPIEDYEKINKELKLYNPRLLERP 276
Obg COG0536
GTPase involved in cell partioning and DNA repair [Cell cycle control, cell division, ...
 65-176 1.04e-19

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: 86.19  E-value: 1.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAK-IQLLDLPGIIEGAKDGKGRG----RQviaVA 139
Cdd:COG0536  158 ADVGLVGLPNAGKSTLLSAVSAAKPKIADYPFTTLVPNLGVVRVGDGRsFVIADIPGLIEGASEGAGLGhrflRH---IE 234

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 119580378 140 RtCNLILIVLDV-----LKPLGHKKIIENELEGFGIRLNSKP 176
Cdd:COG0536  235 R-TRVLLHVVDAapldgRDPVEDYEIIRNELEAYSPELAEKP 275
obgE PRK12298
GTPase CgtA; Reviewed
 65-185 5.84e-18

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 81.84  E-value: 5.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLttVP--GVIRYKGAK-IQLLDLPGIIEGAKDGKGRG-RQVIAVAR 140
Cdd:PRK12298 160 ADVGLLGLPNAGKSTFIRAVSAAKPKVADYPFTTL--VPnlGVVRVDDERsFVVADIPGLIEGASEGAGLGiRFLKHLER 237

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 119580378 141 tCNLILIVLDVLK-----PLGHKKIIENELEGFGIRLNSKPPNIGFKKKD 185
Cdd:PRK12298 238 -CRVLLHLIDIAPidgsdPVENARIIINELEKYSPKLAEKPRWLVFNKID 286
obgE PRK12296
GTPase CgtA; Reviewed
 65-172 4.06e-13

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 67.97  E-value: 4.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  65 ARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLttVP--GVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTC 142
Cdd:PRK12296 160 ADVGLVGFPSAGKSSLISALSAAKPKIADYPFTTL--VPnlGVVQAGDTRFTVADVPGLIPGASEGKGLGLDFLRHIERC 237

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 119580378 143 NLILIVLDVL------KPLGHKKIIENELEGFGIRL 172
Cdd:PRK12296 238 AVLVHVVDCAtlepgrDPLSDIDALEAELAAYAPAL 273
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 68-150 2.47e-12

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 62.65  E-value: 2.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  68 GFVGFPSVGKSTLLSNLAG-VYSEVAAYEFTTLTTVPGVIR-YKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNLI 145
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGqNVGIVSPIPGTTRDPVRKEWElLPLGPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80


                 ....*
gi 119580378 146 LIVLD 150
Cdd:cd00880   81 LLVVD 85
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 68-172 2.19e-10

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 57.47  E-value: 2.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  68 GFVGFPSVGKSTLLSNLAGV-YSEVAAYEFTTLTTVPGVIRYKGA--KIQLLDLPGIIEGakDGKGRGRQVIAVARTCNL 144
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGeVGEVSDVPGTTRDPDVYVKELDKGkvKLVLVDTPGLDEF--GGLGREELARLLLRGADL 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 119580378 145 ILIVLDVLKPLG---HKKIIENELEGFGIRL 172
Cdd:cd00882   79 ILLVVDSTDRESeedAKLLILRRLRKEGIPI 109
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 71-216 1.04e-09

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: 55.64  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  71 GFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGI----------IEgakdgkgrgRQVI-AVA 139
Cdd:cd01897    7 GYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLRWQVIDTPGIldrpleerntIE---------MQAItALA 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119580378 140 RTCNLILIVLDVLKPLGHKkiIENELEGF-GIR-LNSKPPNIGFKKKDKgginltatCPQSELDAETVKSILAEYKIHN 216
Cdd:cd01897   78 HLRAAVLFFIDPSETCGYS--IEEQLSLFkEIKpLFNKPVIVVLNKIDL--------LTEEDLSEIEKELEKEGEEVIK 146
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
71-123 1.02e-08

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 54.45  E-value: 1.02e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119580378  71 GFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIE 123
Cdd:COG1084  167 GYPNVGKSSLVSKVTSAKPEIASYPFTTKGIIVGHFERGHGRYQVIDTPGLLD 219
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 69-121 1.14e-07

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: 49.76  E-value: 1.14e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119580378  69 FVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGI 121
Cdd:cd01879    2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPGT 54
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
 67-134 1.96e-07

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: 50.69  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  67 IGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGV--------------------------IRYkgAKIQLLDLPG 120
Cdd:cd01899    1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVgyvrvecpckelgvscnprygkcidgKRY--VPVELIDVAG 78

                         90
                 ....*....|....
gi 119580378 121 IIEGAKDGKGRGRQ 134
Cdd:cd01899   79 LVPGAHEGKGLGNQ 92
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
66-121 4.53e-07

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 50.12  E-value: 4.53e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119580378  66 RIGFVGFPSVGKSTLLSNLAGVYSEVAAYefttlttvPGV--------IRYKGAKIQLLDLPGI 121
Cdd:COG0370    5 TIALVGNPNVGKTTLFNALTGSRQKVGNW--------PGVtvekkegkFKLKGKEIELVDLPGT 60
PRK09602 PRK09602
translation-associated GTPase; Reviewed
 66-151 3.22e-06

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 47.11  E-value: 3.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  66 RIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGV--------------------------IRYkgAKIQLLDLP 119
Cdd:PRK09602   3 TIGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVayvrvecpckelgvkcnprngkcidgTRF--IPVELIDVA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 119580378 120 GIIEGAKDGKGRGRQVIAVARTCNLILIVLDV 151
Cdd:PRK09602  81 GLVPGAHEGRGLGNQFLDDLRQADALIHVVDA 112
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 66-162 5.87e-05

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: 42.42  E-value: 5.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  66 RIGFVGFPSVGKSTLLSNLAG----VYSEVAAyefTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKdgKGRGRQVIAVART 141
Cdd:cd01895    4 KIAIIGRPNVGKSSLLNALLGeervIVSDIAG---TTRDSIDVPFEYDGQKYTLIDTAGIRKKGK--VTEGIEKYSVLRT 78

                         90       100
                 ....*....|....*....|....*....
gi 119580378 142 ------CNLILIVLDVLKPLGH--KKIIE 162
Cdd:cd01895   79 lkaierADVVLLVLDASEGITEqdLRIAG 107
PTZ00258 PTZ00258
GTP-binding protein; Provisional
 66-220 8.03e-05

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 43.01  E-value: 8.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  66 RIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTL------TTVPG------VIRYKGAKI-----QLLDLPGIIEGAKDG 128
Cdd:PTZ00258  23 KMGIVGLPNVGKSTTFNALCKQQVPAENFPFCTIdpntarVNVPDerfdwlCKHFKPKSIvpaqlDITDIAGLVKGASEG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378 129 KGRGRQVIAVARTCNLILIVL------------DVLKPLGHKKIIENEL-----EGFGIRLNSKPPNIGFKKKDKGGinl 191
Cdd:PTZ00258 103 EGLGNAFLSHIRAVDGIYHVVrafededithveGEIDPVRDLEIISSELilkdlEFVEKRLDELTKKRKKKKKKKEE--- 179

                        170       180       190
                 ....*....|....*....|....*....|.
gi 119580378 192 tatcpQSELDA-ETVKSILAEYK-IHNADVT 220
Cdd:PTZ00258 180 -----KVELDVlKKVLEWLEEGKpVRDGDWT 205
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 68-154 1.07e-04

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


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 41.17  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  68 GFVGFPSVGKSTLLSNLAGvySEVAAYEFTTLTTV---PGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNL 144
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFG--TEVAAVGDRRPTTRaaqAYVWQTGGDGLVLLDLPGVGERGRRDREYEELYRRLLPEADL 78

                         90
                 ....*....|
gi 119580378 145 ILIVLDVLKP 154
Cdd:cd11383   79 VLWLLDADDR 88
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 66-121 2.22e-04

Circularly permuted YlqF GTPase; Proteins of the YlqF 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. The YlqF subfamily is represented in all eukaryotes as well as a phylogenetically diverse array of bacteria (including gram-positive bacteria, proteobacteria, Synechocystis, Borrelia, and Thermotoga).


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 40.59  E-value: 2.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119580378  66 RIGFVGFPSVGKSTLLSNLAGV-YSEVAAyefttlttVPGV------IRYKGaKIQLLDLPGI 121
Cdd:cd01856  117 RAMVVGIPNVGKSTLINRLRGKkVAKVGN--------KPGVtrgqqwIRIGP-NIELLDTPGI 170
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 70-151 1.52e-03

EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first 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: 206681 [Multi-domain]  Cd Length: 157  Bit Score: 37.80  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  70 VGFPSVGKSTLLSNLAGVYSE-VAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAK--DGKGRgRQVIAVARTCNLIL 146
Cdd:cd01894    3 VGRPNVGKSTLFNRLTGRRDAiVSDTPGVTRDRKYGEAEWGGREFILIDTGGIEPDDEgiSKEIR-EQAEIAIEEADVIL 81


                 ....*
gi 119580378 147 IVLDV 151
Cdd:cd01894   82 FVVDG 86
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
 66-123 1.98e-03

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: 38.52  E-value: 1.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119580378   66 RIGFVGFPSVGKSTLLSNLAG----VYSEVAAyefTTLTTVPGVIRYKGAKIQLLDLPGIIE 123
Cdd:TIGR00436   2 FVAILGRPNVGKSTLLNQLHGqkisITSPKAQ---TTRNRISGIHTTGASQIIFIDTPGFHE 60
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 64-122 2.69e-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: 2.69e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119580378  64 DARIGFVGFPSVGKSTLLSNLAGvySEVaayefTTLTTVPGVIRY-----KGAKIQLLDLPGII 122
Cdd:cd01857   82 EATIGLVGYPNVGKSSLINALVG--SKK-----VSVSSTPGKTKHfqtifLEPGITLCDCPGLV 138
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 66-163 2.81e-03

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: 37.44  E-value: 2.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  66 RIGFV---GFPSVGKSTLLSNLAGvySEVAAYEF---TTLTTVPGVIRYKGAKIQLLDLPGIIEG-AKDGKGRGRQVIAV 138
Cdd:cd04163    2 KSGFVaiiGRPNVGKSTLLNALVG--QKISIVSPkpqTTRNRIRGIYTDDDAQIIFVDTPGIHKPkKKLGERMVKAAWSA 79

                         90       100
                 ....*....|....*....|....*..
gi 119580378 139 ARTCNLILIVLDVLKPLGH--KKIIEN 163
Cdd:cd04163   80 LKDVDLVLFVVDASEWIGEgdEFILEL 106
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 59-155 3.97e-03

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 38.24  E-value: 3.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  59 VAKTGDARIGFVGFPSVGKSTLLSNLAG----VYSEVAAyefTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKG---- 130
Cdd:PRK09518 445 LTPSGLRRVALVGRPNVGKSSLLNQLTHeeraVVNDLAG---TTRDPVDEIVEIDGEDWLFIDTAGIKRRQHKLTGaeyy 521

                         90       100
                 ....*....|....*....|....*...
gi 119580378 131 ---RGRQVIavaRTCNLILIVLDVLKPL 155
Cdd:PRK09518 522 sslRTQAAI---ERSELALFLFDASQPI 546
YeeP COG3596
Predicted GTPase [General function prediction only];
66-154 5.06e-03

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 37.44  E-value: 5.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  66 RIGFVGFPSVGKSTLLSNLAGV-YSEVAAYEFTtlTTVPGVIRYK---GAKIQLLDLPGIIEGAKDGKgRGRQVIAVART 141
Cdd:COG3596   41 VIALVGKTGAGKSSLINALFGAeVAEVGVGRPC--TREIQRYRLEsdgLPGLVLLDTPGLGEVNERDR-EYRELRELLPE 117

                         90
                 ....*....|...
gi 119580378 142 CNLILIVLDVLKP 154
Cdd:COG3596  118 ADLILWVVKADDR 130
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
61-129 7.28e-03

Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 36.62  E-value: 7.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  61 KTGDARIGFVGFPSVGKSTLLSNLAGvySEVAayefttlTT--VPGV----IRYKGAK-IQLLDLPGI----IEGAKDGK 129
Cdd:COG1161  110 KRRPIRVMIVGIPNVGKSTLINRLAG--KKVA-------KTgnKPGVtkgqQWIKLDDgLELLDTPGIlwpkFEDPEVGY 180
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 63-121 7.58e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 37.26  E-value: 7.58e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119580378  63 GDARIGFVGFPSVGKSTLLSNLAG----VYSEVAAyefTTLTTVPGVIRYKGAKIQLLDLPGI 121
Cdd:PRK03003 210 GPRRVALVGKPNVGKSSLLNKLAGeersVVDDVAG---TTVDPVDSLIELGGKTWRFVDTAGL 269
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
66-161 8.28e-03

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 36.93  E-value: 8.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119580378  66 RIGFVGFPSVGKSTLLSNLAG----VYSEVAAyefTTLTTVPGVIRYKGAKIQLLDLPGIiegakdgKGRGRQV-----I 136
Cdd:COG1160  177 KIAIVGRPNVGKSSLINALLGeervIVSDIAG---TTRDSIDTPFERDGKKYTLIDTAGI-------RRKGKVDegiekY 246

                         90       100       110
                 ....*....|....*....|....*....|...
gi 119580378 137 AVART------CNLILIVLDVLKPLGH--KKII 161
Cdd:COG1160  247 SVLRTlraierADVVLLVIDATEGITEqdLKIA 279
EHD cd09913
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ...
 112-154 8.87e-03

Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain (EHD) proteins regulate endocytic events; they have been linked to a number of Rab proteins through their association with mutual effectors, suggesting a coordinate role in endocytic regulation. Eukaryotic EHDs comprise four members (EHD1-4) in mammals and single members in Caenorhabditis elegans (Rme-1), Drosophila melanogaster (Past1) as well as several eukaryotic parasites. EHD1 regulates trafficking of multiple receptors from the endocytic recycling compartment (ERC) to the plasma membrane; EHD2 regulates trafficking from the plasma membrane by controlling Rac1 activity; EHD3 regulates endosome-to-Golgi transport, and preserves Golgi morphology; EHD4 is involved in the control of trafficking at the early endosome and regulates exit of cargo toward the recycling compartment as well as late endocytic pathway. Rme-1, an ortholog of human EHD1, controls the recycling of internalized receptors from the endocytic recycling compartment to the plasma membrane. In D. melanogaster, deletion of the Past1 gene leads to infertility as well as premature death of adult flies. Arabidopsis thaliana also has homologs of EHD proteins (AtEHD1 and AtEHD2), possibly involved in regulating endocytosis and signaling.


Pssm-ID: 206740  Cd Length: 241  Bit Score: 36.48  E-value: 8.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 119580378 112 KIQLLDLPGIIEGAKDGKGRGRQVIAVAR----TCNLILIVLDVLKP 154
Cdd:cd09913   89 SVTIVDTPGILSGEKQRQSRGYDFNAVCRwfaeRADLIFLLFDPHKL 135
 
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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