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Conserved domains on  [gi|637068864|ref|WP_024417937|]
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ribosome biogenesis GTP-binding protein YihA/YsxC [Streptococcus suis]

Protein Classification

GTP-binding protein( domain architecture ID 10785093)

GTP-binding protein similar to YsxC/EngB, a GTPase associated with ribosome biogenesis; belongs to the large superfamily of translation factor-related (TRAFAC) GTPases

CATH:  3.40.50.300
Gene Ontology:  GO:0046872|GO:0005525
PubMed:  16333325|11916378|11489118
SCOP:  4004043

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 1-193 3.26e-113

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];


:

Pssm-ID: 439988 [Multi-domain]  Cd Length: 194  Bit Score: 320.48  E-value: 3.26e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864   1 MQIntHNAEILLSAVSKAQYPGDDIPEIALAGRSNVGKSSFINTLLGRKNLARTSGKPGKTQQLNFYNIDDKIRFVDVPG 80
Cdd:COG0218    1 MKI--KKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  81 YGYAKVSKTERAKWGKMIEEYLTTRENLRVVVSLVDMRHEPSADDVQMYDFLKYYEIPVIIVATKADKIPRGKWNKHESI 160
Cdd:COG0218   79 YGYAKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKA 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 637068864 161 IKKKLDFDKN-DQFVIFSSETRHGYDQAWDAILS 193
Cdd:COG0218  159 IKKALGKDPAaPEVILFSSLKKEGIDELRAAIEE 192
 
Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 1-193 3.26e-113

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 439988 [Multi-domain]  Cd Length: 194  Bit Score: 320.48  E-value: 3.26e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864   1 MQIntHNAEILLSAVSKAQYPGDDIPEIALAGRSNVGKSSFINTLLGRKNLARTSGKPGKTQQLNFYNIDDKIRFVDVPG 80
Cdd:COG0218    1 MKI--KKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  81 YGYAKVSKTERAKWGKMIEEYLTTRENLRVVVSLVDMRHEPSADDVQMYDFLKYYEIPVIIVATKADKIPRGKWNKHESI 160
Cdd:COG0218   79 YGYAKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKA 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 637068864 161 IKKKLDFDKN-DQFVIFSSETRHGYDQAWDAILS 193
Cdd:COG0218  159 IKKALGKDPAaPEVILFSSLKKEGIDELRAAIEE 192
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 8-183 3.68e-104

ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other]


Pssm-ID: 274670 [Multi-domain]  Cd Length: 179  Bit Score: 297.08  E-value: 3.68e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864    8 AEILLSAVSKAQYPGDDIPEIALAGRSNVGKSSFINTLLGRKNLARTSGKPGKTQQLNFYNIDDKIRFVDVPGYGYAKVS 87
Cdd:TIGR03598   1 AEFVKSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFEVNDGFRLVDLPGYGYAKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864   88 KTERAKWGKMIEEYLTTRENLRVVVSLVDMRHEPSADDVQMYDFLKYYEIPVIIVATKADKIPRGKWNKHESIIKKKLDF 167
Cdd:TIGR03598  81 KEEKEKWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKALKK 160

                         170
                  ....*....|....*..
gi 637068864  168 DKNDQFVI-FSSETRHG 183
Cdd:TIGR03598 161 DADDPSVQlFSSLKKTG 177
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 27-195 2.41e-91

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: 264.37  E-value: 2.41e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  27 EIALAGRSNVGKSSFINTLLGRKNLARTSGKPGKTQQLNFYNIDDKIRFVDVPGYGYAKVSKTERAKWGKMIEEYLTTRE 106
Cdd:cd01876    1 EVAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAKVSKEVREKWGKLIEEYLENRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864 107 NLRVVVSLVDMRHEPSADDVQMYDFLKYYEIPVIIVATKADKIPRGKWNKHESIIKKKLD-FDKNDQFVIFSSETRHGYD 185
Cdd:cd01876   81 NLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNlFNILPPVILFSSKKGTGID 160

                        170
                 ....*....|
gi 637068864 186 QAWDAILSNI 195
Cdd:cd01876  161 ELRALIAEWL 170
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 27-145 6.39e-26

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: 96.15  E-value: 6.39e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864   27 EIALAGRSNVGKSSFINTLLGRKnlARTSGKPGKTQQLNFYNI---DDKIRFVDVPGygyakVSKTERAKWGkMIEEYLT 103
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK--AIVSDYPGTTRDPNEGRLelkGKQIILVDTPG-----LIEGASEGEG-LGRAFLA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 637068864  104 TRENlRVVVSLVDMRHEPSADDVQMYDFLKYYEIPVIIVATK 145
Cdd:pfam01926  73 IIEA-DLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
PRK04213 PRK04213
GTP-binding protein EngB;
21-149 3.71e-21

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 86.12  E-value: 3.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  21 PGDDIPEIALAGRSNVGKSSFINTLLGRKnlARTSGKPGKTQQLNFYNIDDKIrFVDVPGYGY-AKVSKTERAKWGKMIE 99
Cdd:PRK04213   5 RPDRKPEIVFVGRSNVGKSTLVRELTGKK--VRVGKRPGVTRKPNHYDWGDFI-LTDLPGFGFmSGVPKEVQEKIKDEIV 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637068864 100 EYL-TTRENLRVVVSLVDM--------RHEPSAD---DVQMYDFLKYYEIPVIIVATKADKI 149
Cdd:PRK04213  82 RYIeDNADRILAAVLVVDGksfieiieRWEGRGEipiDVEMFDFLRELGIPPIVAVNKMDKI 143
 
Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 1-193 3.26e-113

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 439988 [Multi-domain]  Cd Length: 194  Bit Score: 320.48  E-value: 3.26e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864   1 MQIntHNAEILLSAVSKAQYPGDDIPEIALAGRSNVGKSSFINTLLGRKNLARTSGKPGKTQQLNFYNIDDKIRFVDVPG 80
Cdd:COG0218    1 MKI--KKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  81 YGYAKVSKTERAKWGKMIEEYLTTRENLRVVVSLVDMRHEPSADDVQMYDFLKYYEIPVIIVATKADKIPRGKWNKHESI 160
Cdd:COG0218   79 YGYAKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKA 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 637068864 161 IKKKLDFDKN-DQFVIFSSETRHGYDQAWDAILS 193
Cdd:COG0218  159 IKKALGKDPAaPEVILFSSLKKEGIDELRAAIEE 192
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 8-183 3.68e-104

ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other]


Pssm-ID: 274670 [Multi-domain]  Cd Length: 179  Bit Score: 297.08  E-value: 3.68e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864    8 AEILLSAVSKAQYPGDDIPEIALAGRSNVGKSSFINTLLGRKNLARTSGKPGKTQQLNFYNIDDKIRFVDVPGYGYAKVS 87
Cdd:TIGR03598   1 AEFVKSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFEVNDGFRLVDLPGYGYAKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864   88 KTERAKWGKMIEEYLTTRENLRVVVSLVDMRHEPSADDVQMYDFLKYYEIPVIIVATKADKIPRGKWNKHESIIKKKLDF 167
Cdd:TIGR03598  81 KEEKEKWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKALKK 160

                         170
                  ....*....|....*..
gi 637068864  168 DKNDQFVI-FSSETRHG 183
Cdd:TIGR03598 161 DADDPSVQlFSSLKKTG 177
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 27-195 2.41e-91

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: 264.37  E-value: 2.41e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  27 EIALAGRSNVGKSSFINTLLGRKNLARTSGKPGKTQQLNFYNIDDKIRFVDVPGYGYAKVSKTERAKWGKMIEEYLTTRE 106
Cdd:cd01876    1 EVAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAKVSKEVREKWGKLIEEYLENRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864 107 NLRVVVSLVDMRHEPSADDVQMYDFLKYYEIPVIIVATKADKIPRGKWNKHESIIKKKLD-FDKNDQFVIFSSETRHGYD 185
Cdd:cd01876   81 NLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNlFNILPPVILFSSKKGTGID 160

                        170
                 ....*....|
gi 637068864 186 QAWDAILSNI 195
Cdd:cd01876  161 ELRALIAEWL 170
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 27-145 6.39e-26

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: 96.15  E-value: 6.39e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864   27 EIALAGRSNVGKSSFINTLLGRKnlARTSGKPGKTQQLNFYNI---DDKIRFVDVPGygyakVSKTERAKWGkMIEEYLT 103
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK--AIVSDYPGTTRDPNEGRLelkGKQIILVDTPG-----LIEGASEGEG-LGRAFLA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 637068864  104 TRENlRVVVSLVDMRHEPSADDVQMYDFLKYYEIPVIIVATK 145
Cdd:pfam01926  73 IIEA-DLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
PRK04213 PRK04213
GTP-binding protein EngB;
21-149 3.71e-21

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 86.12  E-value: 3.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  21 PGDDIPEIALAGRSNVGKSSFINTLLGRKnlARTSGKPGKTQQLNFYNIDDKIrFVDVPGYGY-AKVSKTERAKWGKMIE 99
Cdd:PRK04213   5 RPDRKPEIVFVGRSNVGKSTLVRELTGKK--VRVGKRPGVTRKPNHYDWGDFI-LTDLPGFGFmSGVPKEVQEKIKDEIV 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 637068864 100 EYL-TTRENLRVVVSLVDM--------RHEPSAD---DVQMYDFLKYYEIPVIIVATKADKI 149
Cdd:PRK04213  82 RYIeDNADRILAAVLVVDGksfieiieRWEGRGEipiDVEMFDFLRELGIPPIVAVNKMDKI 143
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 28-183 5.12e-20

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: 82.51  E-value: 5.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  28 IALAGRSNVGKSSFINTLLGRKnLARTSGKPGKTQQ--LNFYNIDD-KIRFVDVPGygyakVSKTERAKWGKMIEEYLTT 104
Cdd:cd04163    6 VAIIGRPNVGKSTLLNALVGQK-ISIVSPKPQTTRNriRGIYTDDDaQIIFVDTPG-----IHKPKKKLGERMVKAAWSA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864 105 RENLRVVVSLVDMRHEPSADDVQMYDFLKYYEIPVIIVATKADKI-PRGKWNKHESIIKKKLDFDKndqFVIFSSETRHG 183
Cdd:cd04163   80 LKDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLVkDKEDLLPLLEKLKELHPFAE---IFPISALKGEN 156
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 29-193 6.12e-20

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: 82.12  E-value: 6.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  29 ALAGRSNVGKSSFINTLLGrKNLARTSGKPGKTQQLNFYNI-----DDKIRFVDVPGYGYAKVSKTErakwgkmiEEYLT 103
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLG-GEVGEVSDVPGTTRDPDVYVKeldkgKVKLVLVDTPGLDEFGGLGRE--------ELARL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864 104 TRENLRVVVSLVDMRHEPSADDVQMY--DFLKYYEIPVIIVATKADKIPRgkWNKHESIIKKKLDFDKNDQFVIFSSETR 181
Cdd:cd00882   72 LLRGADLILLVVDSTDRESEEDAKLLilRRLRKEGIPIILVGNKIDLLEE--REVEELLRLEELAKILGVPVFEVSAKTG 149

                        170
                 ....*....|..
gi 637068864 182 HGYDQAWDAILS 193
Cdd:cd00882  150 EGVDELFEKLIE 161
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 29-186 5.56e-18

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: 76.90  E-value: 5.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  29 ALAGRSNVGKSSFINTLLGRKNLArTSGKPGKTQQLNFYNI----DDKIRFVDVPGYGYAKVSKTERakwgkmIEEYLTT 104
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGI-VSPIPGTTRDPVRKEWellpLGPVVLIDTPGLDEEGGLGRER------VEEARQV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864 105 RENLRVVVSLVDMRHEPSaDDVQMYDFLKYYEIPVIIVATKADKIPRGKWNKHESIIKKKLDFDknDQFVIFSSETRHGY 184
Cdd:cd00880   74 ADRADLVLLVVDSDLTPV-EEEAKLGLLRERGKPVLLVLNKIDLVPESEEEELLRERKLELLPD--LPVIAVSALPGEGI 150


                 ..
gi 637068864 185 DQ 186
Cdd:cd00880  151 DE 152
YeeP COG3596
Predicted GTPase [General function prediction only];
26-195 2.13e-16

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 75.57  E-value: 2.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  26 PEIALAGRSNVGKSSFINTLLGRkNLARTS-GKPGkTQQLNFY----NIDDKIRFVDVPGYGyakvSKTERAKWGKMIEE 100
Cdd:COG3596   40 PVIALVGKTGAGKSSLINALFGA-EVAEVGvGRPC-TREIQRYrlesDGLPGLVLLDTPGLG----EVNERDREYRELRE 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864 101 YLTTRENLRVVVSLVDMRHEPsadDVQMYDFLK--YYEIPVIIVATKADKI-PRGKWNKH-------------ESIIKKK 164
Cdd:COG3596  114 LLPEADLILWVVKADDRALAT---DEEFLQALRaqYPDPPVLVVLTQVDRLePEREWDPPynwpsppkeqnirRALEAIA 190

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 637068864 165 LDFDKNDQFVI-FSS-ETRHGY--DQAWDAILSNI 195
Cdd:COG3596  191 EQLGVPIDRVIpVSAaEDRTGYglEELVDALAEAL 225
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
28-194 6.08e-16

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 73.87  E-value: 6.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  28 IALAGRSNVGKSSFINTLLGRKnLARTSGKPGKT--QQLNFYNIDD-KIRFVDVPGYgyakvsktERAKwgKMIEEYL-- 102
Cdd:COG1159    6 VAIVGRPNVGKSTLLNALVGQK-VSIVSPKPQTTrhRIRGIVTREDaQIVFVDTPGI--------HKPK--RKLGRRMnk 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864 103 TTRENLR---VVVSLVDMRHEPSADDVQMYDFLKYYEIPVIIVATKADKIPRGKWNKHESIIKKKLDFdknDQFVIFSSE 179
Cdd:COG1159   75 AAWSALEdvdVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLVKKEELLPLLAEYSELLDF---AEIVPISAL 151

                        170
                 ....*....|....*
gi 637068864 180 TRHGYDQAWDAILSN 194
Cdd:COG1159  152 KGDNVDELLDEIAKL 166
era PRK00089
GTPase Era; Reviewed
 28-194 2.34e-14

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 69.31  E-value: 2.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  28 IALAGRSNVGKSSFINTLLGRKnLARTSGKPGKTQ-QLN-FYNIDD-KIRFVDVPGygyakVSKTERAkwgkmIEEYL-- 102
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQK-ISIVSPKPQTTRhRIRgIVTEDDaQIIFVDTPG-----IHKPKRA-----LNRAMnk 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864 103 TTRENLR---VVVSLVDMRHEPSADDVQMYDFLKYYEIPVIIVATKADKI-PRGKWNKHESIIKKKLDFDKndqFVIFSS 178
Cdd:PRK00089  77 AAWSSLKdvdLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVkDKEELLPLLEELSELMDFAE---IVPISA 153

                        170
                 ....*....|....*.
gi 637068864 179 ETRHGYDQAWDAILSN 194
Cdd:PRK00089 154 LKGDNVDELLDVIAKY 169
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 28-80 1.81e-10

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: 56.47  E-value: 1.81e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 637068864  28 IALAGRSNVGKSSFINTLLGRKnLARTSGKPGKTQQLNFYNIDDKIRFVDVPG 80
Cdd:cd01857   85 IGLVGYPNVGKSSLINALVGSK-KVSVSSTPGKTKHFQTIFLEPGITLCDCPG 136
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 35-80 6.20e-10

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: 55.61  E-value: 6.20e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 637068864  35 NVGKSSFINTLLGRKnLARTSGKPGKTQQLNFYNIDDKIRFVDVPG 80
Cdd:cd01856  125 NVGKSTLINRLRGKK-VAKVGNKPGVTRGQQWIRIGPNIELLDTPG 169
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 29-195 1.08e-09

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: 54.75  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  29 ALAGRSNVGKSSFINTLLGRKnLARTSGKPGKTQQLNFYNI---DDKIRFVDVPGYGYAKVS-------KTERAkwgkmI 98
Cdd:cd01894    1 AIVGRPNVGKSTLFNRLTGRR-DAIVSDTPGVTRDRKYGEAewgGREFILIDTGGIEPDDEGiskeireQAEIA-----I 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  99 EEylttrenLRVVVSLVDMRHEPSADDVQMYDFLKYYEIPVIIVATKADKIprgkwnKHESIIKK--KLDFDKndqFVIF 176
Cdd:cd01894   75 EE-------ADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNI------KEEEEAAEfySLGFGE---PIPI 138

                        170
                 ....*....|....*....
gi 637068864 177 SSETRHGYDQAWDAILSNI 195
Cdd:cd01894  139 SAEHGRGIGDLLDAILELL 157
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
35-80 5.89e-09

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 53.96  E-value: 5.89e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 637068864  35 NVGKSSFINTLLGRKnLARTSGKPGKTQQLNFYNIDDKIRFVDVPG 80
Cdd:COG1161  123 NVGKSTLINRLAGKK-VAKTGNKPGVTKGQQWIKLDDGLELLDTPG 167
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 28-192 9.35e-09

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 52.55  E-value: 9.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  28 IALAGRSNVGKSSFINTLLGRKNLA----RTSGKPgktqQLNFYNIDDKIRFVDVPGYGyakVSKTERAKWgkmIEEYLt 103
Cdd:cd09912    3 LAVVGEFSAGKSTLLNALLGEEVLPtgvtPTTAVI----TVLRYGLLKGVVLVDTPGLN---STIEHHTEI---TESFL- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864 104 trENLRVVVSLVDMRHEPSADDVQ-MYDFLKYYEIPVIIVATKADKI---PRGKWNKHESIIKKKLDFDKNDQFVIFSS- 178
Cdd:cd09912   72 --PRADAVIFVLSADQPLTESEREfLKEILKWSGKKIFFVLNKIDLLseeELEEVLEYSREELGVLELGGGEPRIFPVSa 149

                        170
                 ....*....|....*
gi 637068864 179 -ETRHGYDQAWDAIL 192
Cdd:cd09912  150 kEALEARLQGDEELL 164
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 27-186 1.23e-08

tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 53.53  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  27 EIALAGRSNVGKSSFINTLLGRkNLARTSGKPGKT-----QQLNFYNIddKIRFVDvpgygyakvskT------------ 89
Cdd:COG0486  215 KVVIVGRPNVGKSSLLNALLGE-ERAIVTDIAGTTrdvieERINIGGI--PVRLID-----------Taglretedevek 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  90 ---ERAKwgKMIEEylttrenLRVVVSLVDMRHEPSADDVQMYDFLKyyEIPVIIVATKADKIPRgkwnkhesiIKKKLD 166
Cdd:COG0486  281 igiERAR--EAIEE-------ADLVLLLLDASEPLTEEDEEILEKLK--DKPVIVVLNKIDLPSE---------ADGELK 340

                        170       180
                 ....*....|....*....|
gi 637068864 167 FDKNDQFVIFSSETRHGYDQ 186
Cdd:COG0486  341 SLPGEPVIAISAKTGEGIDE 360
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 28-150 1.23e-08

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: 51.73  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  28 IALAGRSNVGKSSFINTLLGRkNLARTSGKPGKT-----QQLNFYNIddKIRFVDVPGygyakVSKT---------ERAK 93
Cdd:cd04164    6 VVIAGKPNVGKSSLLNALAGR-DRAIVSDIAGTTrdvieEEIDLGGI--PVRLIDTAG-----LRETedeiekigiERAR 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 637068864  94 wgKMIEEylttrENLRVVVslVDMRHEPSADDVQMYDFLKyyEIPVIIVATKADKIP 150
Cdd:cd04164   78 --EAIEE-----ADLVLLV--VDASEGLDEEDLEILELPA--KKPVIVVLNKSDLLS 123
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
28-192 2.58e-08

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 51.14  E-value: 2.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  28 IALAGRSNVGKSSFINTLLGRKNLAR----TSGKPGKTQQLNFYNIDDKIRFVDVPGygyakvskterakwgkmIEEYLT 103
Cdd:COG1100    6 IVVVGTGGVGKTSLVNRLVGDIFSLEkylsTNGVTIDKKELKLDGLDVDLVIWDTPG-----------------QDEFRE 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864 104 TRENLR-------VVVSLVDMRHEPSadDVQMYDFLK-----YYEIPVIIVATKADKIPRGKWNKHESiIKKKLDFDKND 171
Cdd:COG1100   69 TRQFYArqltgasLYLFVVDGTREET--LQSLYELLEslrrlGKKSPIILVLNKIDLYDEEEIEDEER-LKEALSEDNIV 145

                        170       180
                 ....*....|....*....|.
gi 637068864 172 QFVIFSSETRHGYDQAWDAIL 192
Cdd:COG1100  146 EVVATSAKTGEGVEELFAALA 166
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 24-192 6.91e-08

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: 50.12  E-value: 6.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  24 DIPEIALAGRSNVGKSSFINTLLGrKNLARTSGKPGKTQQ--LNFYNIDD-KIRFVDVPGygyakVSKteRAKWGKMIEE 100
Cdd:cd01895    1 DPIKIAIIGRPNVGKSSLLNALLG-EERVIVSDIAGTTRDsiDVPFEYDGqKYTLIDTAG-----IRK--KGKVTEGIEK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864 101 YLTTR-----ENLRVVVSLVDMRHEPSADDVQMYDFLKYYEIPVIIVATKADKIPRGKW--NKHESIIKKKLDFDKNDQF 173
Cdd:cd01895   73 YSVLRtlkaiERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVEKDEKtmKEFEKELRRKLPFLDYAPI 152

                        170
                 ....*....|....*....
gi 637068864 174 VIFSSETRHGYDQAWDAIL 192
Cdd:cd01895  153 VFISALTGQGVDKLFDAIK 171
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 29-149 7.45e-08

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: 49.26  E-value: 7.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  29 ALAGRSNVGKSSFINTLLGrKNLARTSGKPGKT---QQLNFYNIDDKIRFVDVPGYGYAKVSKTERAkwgkmiEEYLTTR 105
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFG-TEVAAVGDRRPTTraaQAYVWQTGGDGLVLLDLPGVGERGRRDREYE------ELYRRLL 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 637068864 106 ENLRVVVSLVDMRHEPSADDVQMYD-FLKYYEIPVIIVATKADKI 149
Cdd:cd11383   74 PEADLVLWLLDADDRALAADHDFYLlPLAGHDAPLLFVLNQVDPV 118
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 23-192 8.60e-08

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 51.20  E-value: 8.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  23 DDIPEIALAGRSNVGKSSFINTLLGRKnlaR--TSGKPG------KTqqlnFYNIDDK-IRFVDVPG--------YG--- 82
Cdd:PRK00093 171 DEPIKIAIIGRPNVGKSSLINALLGEE---RviVSDIAGttrdsiDT----PFERDGQkYTLIDTAGirrkgkvtEGvek 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  83 YAkVSKTERAkwgkmIEeylttRENlrVVVSLVDMRHEPSADDVQMYDFLKYYEIPVIIVATKADKIPRGKWNKHESIIK 162
Cdd:PRK00093 244 YS-VIRTLKA-----IE-----RAD--VVLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKWDLVDEKTMEEFKKELR 310

                        170       180       190
                 ....*....|....*....|....*....|
gi 637068864 163 KKLDFDKNDQFVIFSSETRHGYDQAWDAIL 192
Cdd:PRK00093 311 RRLPFLDYAPIVFISALTGQGVDKLLEAID 340
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 29-191 1.76e-07

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: 48.93  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  29 ALAGRSNVGKSSFINTLLGRKnlARTSGKPGKTQQLN---FYNID-DKIRFVDVPGYgyakvskTERAKWGK-MIEEYLT 103
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAK--VEIASYPFTTLEPNvgvFEFGDgVDIQIIDLPGL-------LDGASEGRgLGEQILA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864 104 TRENLRVVVSLVDMRHEPSADDVQMYDFLKY---------YEIPVIIVATKADKIPRgkwnkhESIIKKKLDFDKNDQFV 174
Cdd:cd01881   72 HLYRSDLILHVIDASEDCVGDPLEDQKTLNEevsgsflflKNKPEMIVANKIDMASE------NNLKRLKLDKLKRGIPV 145

                        170
                 ....*....|....*...
gi 637068864 175 I-FSSETRHGYDQAWDAI 191
Cdd:cd01881  146 VpTSALTRLGLDRVIRTI 163
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 28-80 1.98e-07

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


Pssm-ID: 206752 [Multi-domain]  Cd Length: 157  Bit Score: 48.47  E-value: 1.98e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 637068864  28 IALAGRSNVGKSSFINTLLGRKNlARTS---GKPGKTQQLNFYNIDDKIRFVDVPG 80
Cdd:cd01859  102 VGVVGYPKVGKSSIINALKGRHS-ASTSpipGSPGYTKGIQLVRIDSKIYLIDTPG 156
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 25-149 2.42e-07

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 49.66  E-value: 2.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  25 IPEIALAGRSNVGKSSFINTLLGRKnLARTSGKPGKTQQLNFYNI---DDKIRFVDVPGYGYAKVS-------KTERAkw 94
Cdd:PRK00093   1 KPVVAIVGRPNVGKSTLFNRLTGKR-DAIVADTPGVTRDRIYGEAewlGREFILIDTGGIEPDDDGfekqireQAELA-- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 637068864  95 gkmIEEylttrenLRVVVSLVDMRHEPSADDVQMYDFLKYYEIPVIIVATKADKI 149
Cdd:PRK00093  78 ---IEE-------ADVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDGP 122
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
25-149 8.14e-07

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 48.10  E-value: 8.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  25 IPEIALAGRSNVGKSSFINTLLGRKnLARTSGKPGKTQQLNFY--NIDDKiRF--VDVPGYGYAKVS--------KTERA 92
Cdd:COG1160    2 SPVVAIVGRPNVGKSTLFNRLTGRR-DAIVDDTPGVTRDRIYGeaEWGGR-EFtlIDTGGIEPDDDDgleaeireQAELA 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 637068864  93 kwgkmIEEylttrenLRVVVSLVDMRHEPSADDVQMYDFLKYYEIPVIIVATKADKI 149
Cdd:COG1160   80 -----IEE-------ADVILFVVDGRAGLTPLDEEIAKLLRRSGKPVILVVNKVDGP 124
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
23-192 9.55e-07

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 48.10  E-value: 9.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  23 DDIPEIALAGRSNVGKSSFINTLLGrKNLARTSGKPGKTQ-----QLNFYniDDKIRFVDVPGygyakVSKteRAKWGKM 97
Cdd:COG1160  173 DDPIKIAIVGRPNVGKSSLINALLG-EERVIVSDIAGTTRdsidtPFERD--GKKYTLIDTAG-----IRR--KGKVDEG 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  98 IEEY--LTTRENLR---VVVSLVDMRHEPSADDVQMYDF-LKYYeIPVIIVATKADKIP--RGKWNKHESIIKKKLDFDK 169
Cdd:COG1160  243 IEKYsvLRTLRAIEradVVLLVIDATEGITEQDLKIAGLaLEAG-KALVIVVNKWDLVEkdRKTREELEKEIRRRLPFLD 321

                        170       180
                 ....*....|....*....|...
gi 637068864 170 NDQFVIFSSETRHGYDQAWDAIL 192
Cdd:COG1160  322 YAPIVFISALTGQGVDKLLEAVD 344
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
28-193 1.24e-06

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 47.80  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  28 IALAGRSNVGKSSFINTLLGRkNLARTSGKPGKT-----QQLNFYNIddKIRFVDVPGygyakVSKT---------ERAK 93
Cdd:PRK05291 218 VVIAGRPNVGKSSLLNALLGE-ERAIVTDIAGTTrdvieEHINLDGI--PLRLIDTAG-----IRETddevekigiERSR 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  94 wgKMIEEylttrenLRVVVSLVDMRHEPSADDVQMYDFLKyyEIPVIIVATKADKIPrgkwnkhesiiKKKLDFDKNDQF 173
Cdd:PRK05291 290 --EAIEE-------ADLVLLVLDASEPLTEEDDEILEELK--DKPVIVVLNKADLTG-----------EIDLEEENGKPV 347

                        170       180
                 ....*....|....*....|
gi 637068864 174 VIFSSETRHGYDQAWDAILS 193
Cdd:PRK05291 348 IRISAKTGEGIDELREAIKE 367
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 32-81 2.62e-06

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: 45.72  E-value: 2.62e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  32 GRSNVGKSSFINTLLGR----------KNLARTSGKPGKTQQLNFYNIDDKIRFVDVPGY 81
Cdd:cd01855  132 GATNVGKSTLINALLKSnggkvqaqalVQRLTVSPIPGTTLGLIKIPLGEGKKLYDTPGI 191
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
 35-81 3.37e-06

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


Pssm-ID: 206753 [Multi-domain]  Cd Length: 171  Bit Score: 45.26  E-value: 3.37e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 637068864  35 NVGKSSFINTLLGRKNLArTSGKPGKTQQLNFYNIDDKIRFVDVPGY 81
Cdd:cd04178  126 NVGKSSVINSLKRSRACN-VGATPGVTKSMQEVHLDKHVKLLDSPGV 171
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 28-149 4.12e-06

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 45.06  E-value: 4.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864   28 IALAGRSNVGKSSFINTLLGRKnLARTSGKPGKTQQLNFY-----NIDDKIRFVDVPGygyakvskteRAKWGKMIEEYL 102
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNK-GSITEYYPGTTRNYVTTvieedGKTYKFNLLDTAG----------QEDYDAIRRLYY 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 637068864  103 TTRENLRVVVSLV----DMRHEPSADDVQMYDFLKyYEIPVIIVATKADKI 149
Cdd:TIGR00231  73 PQVERSLRVFDIVilvlDVEEILEKQTKEIIHHAD-SGVPIILVGNKIDLK 122
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 28-147 1.68e-05

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 44.40  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  28 IALAGRSNVGKSSFINTLLGRKNlARTSGKPGKTQQ----------LNFYNIDDKIRFVDVPGYGYAKVSKTERAkwgkm 97
Cdd:PRK09518 278 VAIVGRPNVGKSTLVNRILGRRE-AVVEDTPGVTRDrvsydaewagTDFKLVDTGGWEADVEGIDSAIASQAQIA----- 351

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 637068864  98 ieeyLTTREnlrVVVSLVDMRHEPSADDVQMYDFLKYYEIPVIIVATKAD 147
Cdd:PRK09518 352 ----VSLAD---AVVFVVDGQVGLTSTDERIVRMLRRAGKPVVLAVNKID 394
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 28-80 1.77e-05

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: 42.76  E-value: 1.77e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 637068864  28 IALAGRSNVGKSSFINTLLgRKNLARTSGKPGKTQQLNFYNIDDKIRFVDVPG 80
Cdd:cd01849   94 VGVVGLPNVGKSSFINALL-NKFKLKVGSIPGTTKLQQDVKLDKEIYLYDTPG 145
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 29-80 8.26e-05

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: 41.29  E-value: 8.26e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 637068864  29 ALAGRSNVGKSSFINTLLGRKnlARTSGKPGKT--QQLNFYNIDDK-IRFVDVPG 80
Cdd:cd01879    1 ALVGNPNVGKTTLFNALTGAR--QKVGNWPGVTveKKEGEFKLGGKeIEIVDLPG 53
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 28-82 4.46e-04

CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.


Pssm-ID: 206649  Cd Length: 275  Bit Score: 39.84  E-value: 4.46e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 637068864  28 IALAGRSNVGKSSFINTLLGRKnLARTSGKPGKTQ--------QLNFYNIDD-----KIRFVDVPGYG 82
Cdd:cd01850    7 IMVVGESGLGKSTFINTLFGTK-LYPSKYPPAPGEhitktveiKISKAELEEngvklKLTVIDTPGFG 73
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 26-147 5.69e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 39.95  E-value: 5.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  26 PEIALAGRSNVGKSSFINTLLGRKNlARTSGKPGKTQqlnfynidDKI---------RFVDVPGYGYAKVSKTERAKWGK 96
Cdd:PRK03003  39 PVVAVVGRPNVGKSTLVNRILGRRE-AVVEDVPGVTR--------DRVsydaewngrRFTVVDTGGWEPDAKGLQASVAE 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 637068864  97 MIEEYLTTREnlrVVVSLVDMRHEPSADDVQMYDFLKYYEIPVIIVATKAD 147
Cdd:PRK03003 110 QAEVAMRTAD---AVLFVVDATVGATATDEAVARVLRRSGKPVILAANKVD 157
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 28-48 7.26e-04

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: 39.39  E-value: 7.26e-04
                          10        20
                  ....*....|....*....|.
gi 637068864   28 IALAGRSNVGKSSFINTLLGR 48
Cdd:pfam12631  97 VVIVGKPNVGKSSLLNALLGE 117
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
 26-147 1.13e-03

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


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 38.46  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  26 PEIALAGRSNVGKSSFINTLL-GRKNLARTSGKPGKTQQLNFYNIDDKIRFVDVPGYGYAKvskterakwgKMIEEYLTT 104
Cdd:cd04105    1 PTVLLLGPSDSGKTALFTKLTtGKVRSTVTSIEPNVASFYSNSSKGKKLTLVDVPGHEKLR----------DKLLEYLKA 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 637068864 105 RenLRVVVSLVDmrhepSADDVQ--------MYDFL-----KYYEIPVIIVATKAD 147
Cdd:cd04105   71 S--LKAIVFVVD-----SATFQKnirdvaefLYDILtdlekIKNKIPILIACNKQD 119
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 28-52 1.21e-03

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


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 38.15  E-value: 1.21e-03
                         10        20
                 ....*....|....*....|....*
gi 637068864  28 IALAGRSNVGKSSFINTLLGRKNLA 52
Cdd:cd01854   88 SVLVGQSGVGKSTLLNALLPELVLA 112
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 26-127 1.34e-03

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 39.01  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864  26 PEIALAGRSNVGKSSFINTLLGRK-----NLARTSGKPGKTqqlnFYNIDDKI-RFVDVPGygyakVSKTERAKWGKMIE 99
Cdd:PRK09518 451 RRVALVGRPNVGKSSLLNQLTHEEravvnDLAGTTRDPVDE----IVEIDGEDwLFIDTAG-----IKRRQHKLTGAEYY 521

                         90       100       110
                 ....*....|....*....|....*....|.
gi 637068864 100 EYLTTRENLR---VVVSLVDMRHEPSADDVQ 127
Cdd:PRK09518 522 SSLRTQAAIErseLALFLFDASQPISEQDLK 552
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
28-80 1.50e-03

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 38.56  E-value: 1.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 637068864  28 IALAGRSNVGKSSFINTLLGRKnlARTSGKPGKTQQL---NFYNIDDKIRFVDVPG 80
Cdd:COG0370    6 IALVGNPNVGKTTLFNALTGSR--QKVGNWPGVTVEKkegKFKLKGKEIELVDLPG 59
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 22-80 2.32e-03

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 37.14  E-value: 2.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 637068864   22 GDDIPEI---------ALAGRSNVGKSSFINTLLGRKNLA--RTSGKPGK----TQQLNFYNIDDKIRFVDVPG 80
Cdd:pfam03193  94 GEGIEALkellkgkttVLAGQSGVGKSTLLNALLPELDLRtgEISEKLGRgrhtTTHVELFPLPGGGLLIDTPG 167
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
 7-82 5.20e-03

Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a role in in intracellular defence. IIGP is predominantly associated with the Golgi apparatus and also localizes to the endoplasmic reticulum and exerts a distinct role in IFN-induced intracellular membrane trafficking or processing.


Pssm-ID: 461536 [Multi-domain]  Cd Length: 375  Bit Score: 36.69  E-value: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637068864    7 NAEILLSAVSKAQYPGDDIP-EIALAGRSNVGKSSFINTLLGRKN---------LARTSGKPGKTQQLNFYNIDdkirFV 76
Cdd:pfam05049  16 NLQKVVSIIKKAIQEISSAPlKIAVTGDSGNGKSSFINALRGIGHeedgsaptgVVETTMKRTPYSHPHFPNVV----LW 91


                  ....*.
gi 637068864   77 DVPGYG 82
Cdd:pfam05049  92 DLPGLG 97
NGP_1 cd01858
A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; ...
 28-80 6.68e-03

A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; Autoantigen NGP-1 (Nucleolar G-protein gene 1) has been shown to localize in the nucleolus and nucleolar organizers in all cell types analyzed, which is indicative of a function in ribosomal assembly. NGP-1 and its homologs show 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 NKXD motif) are relocated to the N terminus.


Pssm-ID: 206751 [Multi-domain]  Cd Length: 157  Bit Score: 35.74  E-value: 6.68e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 637068864  28 IALAGRSNVGKSSFINTlLGRKNLARTSGKPGKTQQLNFYNIDDKIRFVDVPG 80
Cdd:cd01858  105 VGFIGYPNVGKSSVINT-LRSKKVCKVAPIPGETKVWQYITLMKRIYLIDCPG 156
 
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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