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Conserved domains on  [gi|1701419495|ref|WP_141971880|]
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MULTISPECIES: ribosome biogenesis GTP-binding protein YihA/YsxC [Serratia]

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, ...
 7-199 1.58e-116

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: 329.73  E-value: 1.58e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495   7 NYHVTHFVTSAPDIRHLPGDAGIEVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVEDGIRLVDLPGYGY 86
Cdd:COG0218     2 KIKKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYGY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  87 AEVPEEMKRKWQRALGEYLQMRNSLKGLVVLMDIRHPLKDLDQQMIQWAVDVGTPVLLLLTKADKLASGARKAQLNMVRE 166
Cdd:COG0218    82 AKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIKK 161

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1701419495 167 AVLPFMGDIQVEAFSSLKKIGVDKLRQKLDTWF 199
Cdd:COG0218   162 ALGKDPAAPEVILFSSLKKEGIDELRAAIEEWL 194
 
Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 7-199 1.58e-116

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: 329.73  E-value: 1.58e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495   7 NYHVTHFVTSAPDIRHLPGDAGIEVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVEDGIRLVDLPGYGY 86
Cdd:COG0218     2 KIKKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYGY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  87 AEVPEEMKRKWQRALGEYLQMRNSLKGLVVLMDIRHPLKDLDQQMIQWAVDVGTPVLLLLTKADKLASGARKAQLNMVRE 166
Cdd:COG0218    82 AKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIKK 161

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1701419495 167 AVLPFMGDIQVEAFSSLKKIGVDKLRQKLDTWF 199
Cdd:COG0218   162 ALGKDPAAPEVILFSSLKKEGIDELRAAIEEWL 194
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 11-189 2.76e-109

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: 310.95  E-value: 2.76e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  11 THFVTSAPDIRHLPGDAGIEVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVEDGIRLVDLPGYGYAEVP 90
Cdd:TIGR03598   1 AEFVKSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFEVNDGFRLVDLPGYGYAKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  91 EEMKRKWQRALGEYLQMRNSLKGLVVLMDIRHPLKDLDQQMIQWAVDVGTPVLLLLTKADKLASGARKAQLNMVREAVLP 170
Cdd:TIGR03598  81 KEEKEKWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKALKK 160

                         170
                  ....*....|....*....
gi 1701419495 171 FMGDIQVEAFSSLKKIGVD 189
Cdd:TIGR03598 161 DADDPSVQLFSSLKKTGID 179
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 30-199 4.17e-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: 4.17e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  30 EVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVEDGIRLVDLPGYGYAEVPEEMKRKWQRALGEYLQMRN 109
Cdd:cd01876     1 EVAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAKVSKEVREKWGKLIEEYLENRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495 110 SLKGLVVLMDIRHPLKDLDQQMIQWAVDVGTPVLLLLTKADKLASGARKAQLNMVREAVLPFMGDIQVEAFSSLKKIGVD 189
Cdd:cd01876    81 NLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLFNILPPVILFSSKKGTGID 160

                         170
                  ....*....|
gi 1701419495 190 KLRQKLDTWF 199
Cdd:cd01876   161 ELRALIAEWL 170
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 30-148 8.94e-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: 8.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  30 EVAFAGRSNAGKSSALNTLTNQKslARTSKTPGRTQLINLFEVEDG---IRLVDLPGygyaeVPEEMKRKWQRALgEYLQ 106
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK--AIVSDYPGTTRDPNEGRLELKgkqIILVDTPG-----LIEGASEGEGLGR-AFLA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1701419495 107 MRNSlKGLVVLMDIRHPLKDLDQQMIQWAVDVGTPVLLLLTK 148
Cdd:pfam01926  73 IIEA-DLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
era PRK00089
GTPase Era; Reviewed
 31-195 1.09e-16

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 76.62  E-value: 1.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  31 VAFAGRSNAGKSSALNTLTNQKsLARTSKTP-------------GRTQLInlfevedgirLVDLPGYgyaevpeeMKRKw 97
Cdd:PRK00089    8 VAIVGRPNVGKSTLLNALVGQK-ISIVSPKPqttrhrirgivteDDAQII----------FVDTPGI--------HKPK- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  98 qRALGEYLqMRNSLKGL----VVLM--DIRHPLKDLDQQMIQWAVDVGTPVLLLLTKADKLASgarKAQLNMVREAVLPF 171
Cdd:PRK00089   68 -RALNRAM-NKAAWSSLkdvdLVLFvvDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVKD---KEELLPLLEELSEL 142

                         170       180
                  ....*....|....*....|....
gi 1701419495 172 MGDIQVEAFSSLKKIGVDKLRQKL 195
Cdd:PRK00089  143 MDFAEIVPISALKGDNVDELLDVI 166
 
Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 7-199 1.58e-116

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: 329.73  E-value: 1.58e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495   7 NYHVTHFVTSAPDIRHLPGDAGIEVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVEDGIRLVDLPGYGY 86
Cdd:COG0218     2 KIKKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYGY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  87 AEVPEEMKRKWQRALGEYLQMRNSLKGLVVLMDIRHPLKDLDQQMIQWAVDVGTPVLLLLTKADKLASGARKAQLNMVRE 166
Cdd:COG0218    82 AKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIKK 161

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1701419495 167 AVLPFMGDIQVEAFSSLKKIGVDKLRQKLDTWF 199
Cdd:COG0218   162 ALGKDPAAPEVILFSSLKKEGIDELRAAIEEWL 194
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 11-189 2.76e-109

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: 310.95  E-value: 2.76e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  11 THFVTSAPDIRHLPGDAGIEVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVEDGIRLVDLPGYGYAEVP 90
Cdd:TIGR03598   1 AEFVKSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFEVNDGFRLVDLPGYGYAKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  91 EEMKRKWQRALGEYLQMRNSLKGLVVLMDIRHPLKDLDQQMIQWAVDVGTPVLLLLTKADKLASGARKAQLNMVREAVLP 170
Cdd:TIGR03598  81 KEEKEKWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKALKK 160

                         170
                  ....*....|....*....
gi 1701419495 171 FMGDIQVEAFSSLKKIGVD 189
Cdd:TIGR03598 161 DADDPSVQLFSSLKKTGID 179
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 30-199 4.17e-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: 4.17e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  30 EVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVEDGIRLVDLPGYGYAEVPEEMKRKWQRALGEYLQMRN 109
Cdd:cd01876     1 EVAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAKVSKEVREKWGKLIEEYLENRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495 110 SLKGLVVLMDIRHPLKDLDQQMIQWAVDVGTPVLLLLTKADKLASGARKAQLNMVREAVLPFMGDIQVEAFSSLKKIGVD 189
Cdd:cd01876    81 NLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLFNILPPVILFSSKKGTGID 160

                         170
                  ....*....|
gi 1701419495 190 KLRQKLDTWF 199
Cdd:cd01876   161 ELRALIAEWL 170
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 32-199 2.46e-29

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: 106.95  E-value: 2.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  32 AFAGRSNAGKSSALNTLTNQKSLArTSKTPGRTQLINLFEVE----DGIRLVDLPGYGYAEVPEEMKRKwqralgEYLQM 107
Cdd:cd00880     1 AIFGRPNVGKSSLLNALLGQNVGI-VSPIPGTTRDPVRKEWEllplGPVVLIDTPGLDEEGGLGRERVE------EARQV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495 108 RNSLKGLVVLMDIRHPLKDLDQQmIQWAVDVGTPVLLLLTKADKLASGARKAQLnmvREAVLPFMGDIQVEAFSSLKKIG 187
Cdd:cd00880    74 ADRADLVLLVVDSDLTPVEEEAK-LGLLRERGKPVLLVLNKIDLVPESEEEELL---RERKLELLPDLPVIAVSALPGEG 149

                         170
                  ....*....|..
gi 1701419495 188 VDKLRQKLDTWF 199
Cdd:cd00880   150 IDELRKKIAELL 161
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 30-148 8.94e-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: 8.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  30 EVAFAGRSNAGKSSALNTLTNQKslARTSKTPGRTQLINLFEVEDG---IRLVDLPGygyaeVPEEMKRKWQRALgEYLQ 106
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK--AIVSDYPGTTRDPNEGRLELKgkqIILVDTPG-----LIEGASEGEGLGR-AFLA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1701419495 107 MRNSlKGLVVLMDIRHPLKDLDQQMIQWAVDVGTPVLLLLTK 148
Cdd:pfam01926  73 IIEA-DLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 32-195 3.01e-19

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: 80.58  E-value: 3.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  32 AFAGRSNAGKSSALNTLTNQKSLArTSKTPGRTQLINLFEVE-----DGIRLVDLPGYGYAEVPEEMKrkwqralgEYLQ 106
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGEVGE-VSDVPGTTRDPDVYVKEldkgkVKLVLVDTPGLDEFGGLGREE--------LARL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495 107 MRNSLKGLVVLMDIRHPLKDLDQQ--MIQWAVDVGTPVLLLLTKADKLASGARKAQLNMVREAvlpFMGDIQVEAFSSLK 184
Cdd:cd00882    72 LLRGADLILLVVDSTDRESEEDAKllILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELA---KILGVPVFEVSAKT 148

                         170
                  ....*....|.
gi 1701419495 185 KIGVDKLRQKL 195
Cdd:cd00882   149 GEGVDELFEKL 159
era PRK00089
GTPase Era; Reviewed
 31-195 1.09e-16

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 76.62  E-value: 1.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  31 VAFAGRSNAGKSSALNTLTNQKsLARTSKTP-------------GRTQLInlfevedgirLVDLPGYgyaevpeeMKRKw 97
Cdd:PRK00089    8 VAIVGRPNVGKSTLLNALVGQK-ISIVSPKPqttrhrirgivteDDAQII----------FVDTPGI--------HKPK- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  98 qRALGEYLqMRNSLKGL----VVLM--DIRHPLKDLDQQMIQWAVDVGTPVLLLLTKADKLASgarKAQLNMVREAVLPF 171
Cdd:PRK00089   68 -RALNRAM-NKAAWSSLkdvdLVLFvvDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVKD---KEELLPLLEELSEL 142

                         170       180
                  ....*....|....*....|....
gi 1701419495 172 MGDIQVEAFSSLKKIGVDKLRQKL 195
Cdd:PRK00089  143 MDFAEIVPISALKGDNVDELLDVI 166
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 31-195 1.15e-16

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: 74.03  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  31 VAFAGRSNAGKSSALNTLTNQKsLARTSKTP-------------GRTQLInlfevedgirLVDLPGYgyaevpeeMKRKw 97
Cdd:cd04163     6 VAIIGRPNVGKSTLLNALVGQK-ISIVSPKPqttrnrirgiytdDDAQII----------FVDTPGI--------HKPK- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  98 qRALGEYLqMRNSLKGL------VVLMDIRHPLKDLDQQMIQWAVDVGTPVLLLLTKADKLasgARKAQLNMVREAVLPF 171
Cdd:cd04163    66 -KKLGERM-VKAAWSALkdvdlvLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLV---KDKEDLLPLLEKLKEL 140

                         170       180
                  ....*....|....*....|....
gi 1701419495 172 MGDIQVEAFSSLKKIGVDKLRQKL 195
Cdd:cd04163   141 HPFAEIFPISALKGENVDELLEYI 164
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
31-195 1.50e-15

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 73.10  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  31 VAFAGRSNAGKSSALNTLTNQKsLARTSKTP-------------GRTQLInlfevedgirLVDLPGYgyaevpeeMKRKw 97
Cdd:COG1159     6 VAIVGRPNVGKSTLLNALVGQK-VSIVSPKPqttrhrirgivtrEDAQIV----------FVDTPGI--------HKPK- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  98 qRALGEYLqMRNSLKGL----VVLM--DIRHPLKDLDQQMIQWAVDVGTPVLLLLTKADKLASGARKAQLNMVREAvLPF 171
Cdd:COG1159    66 -RKLGRRM-NKAAWSALedvdVILFvvDATEKIGEGDEFILELLKKLKTPVILVINKIDLVKKEELLPLLAEYSEL-LDF 142

                         170       180
                  ....*....|....*....|....
gi 1701419495 172 MGDIQVeafSSLKKIGVDKLRQKL 195
Cdd:COG1159   143 AEIVPI---SALKGDNVDELLDEI 163
PRK04213 PRK04213
GTP-binding protein EngB;
24-201 7.37e-12

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 61.86  E-value: 7.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  24 PGDAGIEVAFAGRSNAGKSSALNTLTNQKslARTSKTPGRTQLINLFEVEDgIRLVDLPGYGYAE-VPEEMKRKWQRALG 102
Cdd:PRK04213    5 RPDRKPEIVFVGRSNVGKSTLVRELTGKK--VRVGKRPGVTRKPNHYDWGD-FILTDLPGFGFMSgVPKEVQEKIKDEIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495 103 EYLQ--MRNSLKGLVVL-----MDI--RHPLKD---LDQQMIQWAVDVGTPVLLLLTKADKLASgaRKAQLNMVREA--V 168
Cdd:PRK04213   82 RYIEdnADRILAAVLVVdgksfIEIieRWEGRGeipIDVEMFDFLRELGIPPIVAVNKMDKIKN--RDEVLDEIAERlgL 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1701419495 169 LPFMGDIQ-VEAFSSLKKIGVDKLRQKLDTWFNE 201
Cdd:PRK04213  160 YPPWRQWQdIIAPISAKKGGIEELKEAIRKRLHE 193
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 28-191 7.69e-12

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: 61.29  E-value: 7.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  28 GIEVAFAGRSNAGKSSALNTLTNQKslaR--TSKTPGRTQ--LINLFEVEDG-IRLVDLPGygyaevpeeMKRKWQRALG 102
Cdd:cd01895     2 PIKIAIIGRPNVGKSSLLNALLGEE---RviVSDIAGTTRdsIDVPFEYDGQkYTLIDTAG---------IRKKGKVTEG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495 103 -EYLQMRNSLKGL------VVLMDIRHPLKDLDQQMIQWAVDVGTPVLLLLTKADKLasGARKAQLNMVREAV---LPFM 172
Cdd:cd01895    70 iEKYSVLRTLKAIeradvvLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLV--EKDEKTMKEFEKELrrkLPFL 147

                         170
                  ....*....|....*....
gi 1701419495 173 GDIQVEAFSSLKKIGVDKL 191
Cdd:cd01895   148 DYAPIVFISALTGQGVDKL 166
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 28-195 1.86e-09

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: 54.42  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  28 GIEVAFAGRSNAGKSSALNTLTNQKSlARTSKTPGRT-----QLINLfeveDGI--RLVDLPGYGYAEVPEE---MKRKW 97
Cdd:cd04164     3 GIKVVIAGKPNVGKSSLLNALAGRDR-AIVSDIAGTTrdvieEEIDL----GGIpvRLIDTAGLRETEDEIEkigIERAR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  98 QRAlgeylqmRNSlkGLVVLM-DIRHPLKDLDQQMIQWAVDVgtPVLLLLTKADKLASGARKAQLNMvrEAVLpfmgdiq 176
Cdd:cd04164    78 EAI-------EEA--DLVLLVvDASEGLDEEDLEILELPAKK--PVIVVLNKSDLLSDAEGISELNG--KPII------- 137

                         170
                  ....*....|....*....
gi 1701419495 177 veAFSSLKKIGVDKLRQKL 195
Cdd:cd04164   138 --AISAKTGEGIDELKEAL 154
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 26-191 2.05e-09

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 56.21  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  26 DAGIEVAFAGRSNAGKSSALNTLTNQKslaR--TSKTPGRTQ-LIN-LFEVEDG-IRLVDLPGygyaevpeeMKRKwqra 100
Cdd:PRK00093  171 DEPIKIAIIGRPNVGKSSLINALLGEE---RviVSDIAGTTRdSIDtPFERDGQkYTLIDTAG---------IRRK---- 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495 101 lG------EYLQMRNSLKGL------VVLMDIRHPLKDLDQQMIQWAVDVGTPVLLLLTKADKLASGARKAQLNMVREAv 168
Cdd:PRK00093  235 -GkvtegvEKYSVIRTLKAIeradvvLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKWDLVDEKTMEEFKKELRRR- 312

                         170       180
                  ....*....|....*....|...
gi 1701419495 169 LPFMGDIQVEAFSSLKKIGVDKL 191
Cdd:PRK00093  313 LPFLDYAPIVFISALTGQGVDKL 335
YeeP COG3596
Predicted GTPase [General function prediction only];
30-152 2.93e-09

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 55.54  E-value: 2.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  30 EVAFAGRSNAGKSSALNTLTNQkSLARTSKTPGRTQLINLFEVE----DGIRLVDLPGYGYAEVPEEmkrkwqralgEYL 105
Cdd:COG3596    41 VIALVGKTGAGKSSLINALFGA-EVAEVGVGRPCTREIQRYRLEsdglPGLVLLDTPGLGEVNERDR----------EYR 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1701419495 106 QMRNSLKG--LVVL----MDIRH-PLKDLDQQMIQWAVDVgtPVLLLLTKADKL 152
Cdd:COG3596   110 ELRELLPEadLILWvvkaDDRALaTDEEFLQALRAQYPDP--PVLVVLTQVDRL 161
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 5-83 3.16e-09

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: 53.39  E-value: 3.16e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1701419495   5 NYNYHVTHFVTSAPDIrhlpgdagiEVAFAGRSNAGKSSALNTLTNQKsLARTSKTPGRTQLINLFEVEDGIRLVDLPG 83
Cdd:cd01857    68 KKEGIVVLFFSALNEA---------TIGLVGYPNVGKSSLINALVGSK-KVSVSSTPGKTKHFQTIFLEPGITLCDCPG 136
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 28-195 1.62e-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: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  28 GIEVAFAGRSNAGKSSALNTLTNQKSlARTSKTPGRT-----QLINLfeveDGI--RLVDLPGYGYAEVPEE---MKRKW 97
Cdd:COG0486   213 GIKVVIVGRPNVGKSSLLNALLGEER-AIVTDIAGTTrdvieERINI----GGIpvRLIDTAGLRETEDEVEkigIERAR 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  98 QRalgeylqMRNSlkGLVVLM-DIRHPLKDLDQQMIQWAVDVgtPVLLLLTKADklasgarkaqLNMVREAVLPFMGDIQ 176
Cdd:COG0486   288 EA-------IEEA--DLVLLLlDASEPLTEEDEEILEKLKDK--PVIVVLNKID----------LPSEADGELKSLPGEP 346

                         170
                  ....*....|....*....
gi 1701419495 177 VEAFSSLKKIGVDKLRQKL 195
Cdd:COG0486   347 VIAISAKTGEGIDELKEAI 365
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 31-167 2.34e-08

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: 51.78  E-value: 2.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  31 VAFAGRSNAGKSSALNTLTNQKSLArTSKTPgRTQLINL--FEVEDGIRLVDLPGYGyaeVPEEMKRKWQRalgEYLQmr 108
Cdd:cd09912     3 LAVVGEFSAGKSTLLNALLGEEVLP-TGVTP-TTAVITVlrYGLLKGVVLVDTPGLN---STIEHHTEITE---SFLP-- 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495 109 nSLKGLVVLMDIRHPLKDLDQQ-MIQWAVDVGTPVLLLLTKADKLASGARKAQLNMVREA 167
Cdd:cd09912    73 -RADAVIFVLSADQPLTESEREfLKEILKWSGKKIFFVLNKIDLLSEEELEEVLEYSREE 131
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
26-197 7.62e-08

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 51.56  E-value: 7.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  26 DAGIEVAFAGRSNAGKSSALNTLTNQKslaR--TSKTPGRTQ-LIN-LFEVEDG-IRLVDLPGygyaevpeeMKRKWQRA 100
Cdd:COG1160   173 DDPIKIAIVGRPNVGKSSLINALLGEE---RviVSDIAGTTRdSIDtPFERDGKkYTLIDTAG---------IRRKGKVD 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495 101 LG-EYL-QMRnSLKGL------VVLMDIRHPLKDLDQQMIQWAVDVGTPVLLLLTKADKLA--SGARKAQLNMVREAvLP 170
Cdd:COG1160   241 EGiEKYsVLR-TLRAIeradvvLLVIDATEGITEQDLKIAGLALEAGKALVIVVNKWDLVEkdRKTREELEKEIRRR-LP 318

                         170       180
                  ....*....|....*....|....*..
gi 1701419495 171 FMGDIQVEAFSSLKKIGVDKLRQKLDT 197
Cdd:COG1160   319 FLDYAPIVFISALTGQGVDKLLEAVDE 345
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 32-167 1.61e-07

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: 48.88  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  32 AFAGRSNAGKSSALNTLTnQKSLARTSKTPGRTQLINLFEV---EDGIRLVDLPGYGyaevpeEMKRKWQRALGEYLQMR 108
Cdd:cd11383     1 GLMGKTGAGKSSLCNALF-GTEVAAVGDRRPTTRAAQAYVWqtgGDGLVLLDLPGVG------ERGRRDREYEELYRRLL 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1701419495 109 NSLKGLVVLMDIRHPLKDLDQQMIQ-WAVDVGTPVLLLLTKADKL--ASGARKAQLNMVREA 167
Cdd:cd11383    74 PEADLVLWLLDADDRALAADHDFYLlPLAGHDAPLLFVLNQVDPVlaVSARTGWGLDELAEA 135
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 31-150 8.75e-07

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 48.64  E-value: 8.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  31 VAFAGRSNAGKSSALNTLTNQK-----SLARTSKTPgrtqLINLFEVED-GIRLVDLPGygyaevpeeMKRKWQRALG-E 103
Cdd:PRK09518  453 VALVGRPNVGKSSLLNQLTHEEravvnDLAGTTRDP----VDEIVEIDGeDWLFIDTAG---------IKRRQHKLTGaE 519

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1701419495 104 Y---LQMRNSLKG---LVVLMDIRHPLKDLDQQMIQWAVDVGTPVLLLLTKAD 150
Cdd:PRK09518  520 YyssLRTQAAIERselALFLFDASQPISEQDLKVMSMAVDAGRALVLVFNKWD 572
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
28-201 1.66e-06

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 47.80  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  28 GIEVAFAGRSNAGKSSALNTLTNQKSlARTSKTPGRT-----QLINLfeveDGI--RLVDLPGYGYAEVPEE---MKRKW 97
Cdd:PRK05291  215 GLKVVIAGRPNVGKSSLLNALLGEER-AIVTDIAGTTrdvieEHINL----DGIplRLIDTAGIRETDDEVEkigIERSR 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  98 QRAlgeylqmRNSlkGLVVLM-DIRHPLKDLDQQmiQWAVDVGTPVLLLLTKADkLASGARKAQLNmvreavlpFMGDIQ 176
Cdd:PRK05291  290 EAI-------EEA--DLVLLVlDASEPLTEEDDE--ILEELKDKPVIVVLNKAD-LTGEIDLEEEN--------GKPVIR 349

                         170       180
                  ....*....|....*....|....*
gi 1701419495 177 VeafSSLKKIGVDKLRQKLDTWFNE 201
Cdd:PRK05291  350 I---SAKTGEGIDELREAIKELAFG 371
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 28-195 5.18e-06

MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.


Pssm-ID: 463649 [Multi-domain]  Cd Length: 326  Bit Score: 45.93  E-value: 5.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  28 GIEVAFAGRSNAGKSSALNTLTNQKSlARTSKTPGRT-----QLINLfeveDGI--RLVDLPGYGYAEVPEE---MKRKW 97
Cdd:pfam12631  94 GIKVVIVGKPNVGKSSLLNALLGEER-AIVTDIPGTTrdvieETINI----GGIplRLIDTAGIRETDDEVEkigIERAR 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  98 QRAlgeylqmRNSlkGLVVLM-DIRHPLKDLDQQMIQWAVDvGTPVLLLLTKADKLAsgarkaqlnmvREAVLPFMGDIQ 176
Cdd:pfam12631 169 EAI-------EEA--DLVLLVlDASRPLDEEDLEILELLKD-KKPIIVVLNKSDLLG-----------EIDELEELKGKP 227

                         170
                  ....*....|....*....
gi 1701419495 177 VEAFSSLKKIGVDKLRQKL 195
Cdd:pfam12631 228 VLAISAKTGEGLDELEEAI 246
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 33-84 1.03e-05

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: 44.56  E-value: 1.03e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1701419495  33 FAGRSNAGKSSALNTL----------TNQKSLARTSKTPGRTQLINLFEVEDGIRLVDLPGY 84
Cdd:cd01855   130 VVGATNVGKSTLINALlksnggkvqaQALVQRLTVSPIPGTTLGLIKIPLGEGKKLYDTPGI 191
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 35-195 1.42e-05

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: 43.58  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  35 GRSNAGKSSALNTLTNQKsLARTSKTPGRT-----QLINLFEVEdgIRLVDLPGYGYAEVP--EEMKRKWQRALGEylqm 107
Cdd:cd01894     4 GRPNVGKSTLFNRLTGRR-DAIVSDTPGVTrdrkyGEAEWGGRE--FILIDTGGIEPDDEGisKEIREQAEIAIEE---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495 108 rnslKGLVVLM-DIRHPLKDLDQQMIQWAVDVGTPVLLLLTKADKLASGARKAQLNmvreavlpFMGDIQVEAFSSLKKI 186
Cdd:cd01894    77 ----ADVILFVvDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNIKEEEEAAEFY--------SLGFGEPIPISAEHGR 144


                  ....*....
gi 1701419495 187 GVDKLRQKL 195
Cdd:cd01894   145 GIGDLLDAI 153
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 38-83 1.45e-05

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: 43.67  E-value: 1.45e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1701419495  38 NAGKSSALNTLTNQKSlARTSKTPGRTQLINLFEVEDGIRLVDLPG 83
Cdd:cd01856   125 NVGKSTLINRLRGKKV-AKVGNKPGVTRGQQWIRIGPNIELLDTPG 169
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 18-83 1.63e-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: 43.14  E-value: 1.63e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1701419495  18 PDIRHLPGDAGIEVAFAGRSNAGKSSALNTLTNQKSLaRTSKTPGRTQLINLFEVEDGIRLVDLPG 83
Cdd:cd01849    81 KQKLKLKYKKGIRVGVVGLPNVGKSSFINALLNKFKL-KVGSIPGTTKLQQDVKLDKEIYLYDTPG 145
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 31-83 4.64e-05

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: 42.31  E-value: 4.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1701419495  31 VAFAGRSNAGKSSALNTLTNQKSlARTSKTPGR---TQLINLFEVEDGIRLVDLPG 83
Cdd:cd01859   102 VGVVGYPKVGKSSIINALKGRHS-ASTSPIPGSpgyTKGIQLVRIDSKIYLIDTPG 156
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 29-151 4.98e-04

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: 39.28  E-value: 4.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  29 IEVAFAGRSNAGKSSALNTLTnQKSLARTSKTPGRTQ-LINLFEVEDGIR----LVDLPGYgyaevpEEMKRKWqralge 103
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLL-GNKGSITEYYPGTTRnYVTTVIEEDGKTykfnLLDTAGQ------EDYDAIR------ 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1701419495 104 YLQMRNSLKGLVVLmDIRHPLKD-----LDQQMIQW-AVDVGTPVLLLLTKADK 151
Cdd:TIGR00231  69 RLYYPQVERSLRVF-DIVILVLDveeilEKQTKEIIhHADSGVPIILVGNKIDL 121
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
38-83 7.24e-04

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 39.71  E-value: 7.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1701419495  38 NAGKSSALNTLTNQKSlARTSKTPGRT---QLINLfevEDGIRLVDLPG 83
Cdd:COG1161   123 NVGKSTLINRLAGKKV-AKTGNKPGVTkgqQWIKL---DDGLELLDTPG 167
NGP_1 cd01858
A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; ...
 29-83 1.31e-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: 38.05  E-value: 1.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1701419495  29 IEVAFAGRSNAGKSSALNTLTNQKsLARTSKTPGRT---QLINLFEvedGIRLVDLPG 83
Cdd:cd01858   103 ISVGFIGYPNVGKSSVINTLRSKK-VCKVAPIPGETkvwQYITLMK---RIYLIDCPG 156
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 31-211 1.61e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 38.88  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  31 VAFAGRSNAGKSSALNTLTNQKsLARTSKTPGRT-----QLINLFEVEdgIRLVDLPGYGYAE--VPEEMKRKWQRALGE 103
Cdd:PRK00093    4 VAIVGRPNVGKSTLFNRLTGKR-DAIVADTPGVTrdriyGEAEWLGRE--FILIDTGGIEPDDdgFEKQIREQAELAIEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495 104 ylqmrnslKGLVVLM-DIRHPLKDLDQQMIQWAVDVGTPVLLLLTKADKLASgarkaqlnmvREAVLPF----MGDIQve 178
Cdd:PRK00093   81 --------ADVILFVvDGRAGLTPADEEIAKILRKSNKPVILVVNKVDGPDE----------EADAYEFyslgLGEPY-- 140

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1701419495 179 AFSSLKKIGVDKLRQKLdtwFNEIPPEVLPEDE 211
Cdd:PRK00093  141 PISAEHGRGIGDLLDAI---LEELPEEEEEDEE 170
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
25-83 2.64e-03

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 37.86  E-value: 2.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1701419495  25 GDAgiEVAFAGRSNAGKSSALNTLTNQKS----LARTSKT--PGrtqlinLFEVEDG-IRLVDLPG 83
Cdd:COG1163    62 GDA--TVVLVGFPSVGKSTLLNKLTNAKSevgaYEFTTLDvvPG------MLEYKGAkIQILDVPG 119
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
 31-154 3.31e-03

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


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 37.30  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  31 VAFAGRSNAGKSSALNTLTNQK-SLARTSKTPGRTQLINLFEVEDGIRLVDLPGYGYA--EVPEEMKrkwqralgeylqm 107
Cdd:cd04105     3 VLLLGPSDSGKTALFTKLTTGKvRSTVTSIEPNVASFYSNSSKGKKLTLVDVPGHEKLrdKLLEYLK------------- 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1701419495 108 rNSLKGLVVLMD---IRHPLKDLDQQMIQWAVDV-----GTPVLLLLTKADKLAS 154
Cdd:cd04105    70 -ASLKAIVFVVDsatFQKNIRDVAEFLYDILTDLekiknKIPILIACNKQDLFTA 123
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 31-150 3.49e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 37.64  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  31 VAFAGRSNAGKSSALNTLTNQK-----SLARTSKTPgRTQLINLfeveDGI--RLVDLPGygyaevpeeMKRKWQRALG- 102
Cdd:PRK03003  214 VALVGKPNVGKSSLLNKLAGEErsvvdDVAGTTVDP-VDSLIEL----GGKtwRFVDTAG---------LRRRVKQASGh 279

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1701419495 103 EY---LQMRNSLKG---LVVLMDIRHPLKDLDQQMIQWAVDVGTPVLLLLTKAD 150
Cdd:PRK03003  280 EYyasLRTHAAIEAaevAVVLIDASEPISEQDQRVLSMVIEAGRALVLAFNKWD 333
obgE PRK12297
GTPase CgtA; Reviewed
 11-83 5.39e-03

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 37.00  E-value: 5.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701419495  11 THFVTS---APDIRHlPGDAGIE------------VAFAGRSNAGKSSALNTLTNqkslAR--------TSKTPgrtqli 67
Cdd:PRK12297  127 AHFATStnqAPRIAE-NGEPGEErelrlelklladVGLVGFPNVGKSTLLSVVSN----AKpkianyhfTTLVP------ 195

                          90       100
                  ....*....|....*....|
gi 1701419495  68 NL--FEVEDGIRLV--DLPG 83
Cdd:PRK12297  196 NLgvVETDDGRSFVmaDIPG 215
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 31-83 8.32e-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: 36.22  E-value: 8.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1701419495  31 VAFAGRSNAGKSSALNTLTNQKSLartsktpgRTQLIN--------------LFEVEDGIRLVDLPG 83
Cdd:cd01854    88 SVLVGQSGVGKSTLLNALLPELVL--------ATGEISeklgrgrhttthreLFPLPGGGLIIDTPG 146
 
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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