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Conserved domains on  [gi|490994092|ref|WP_004855823|]
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MULTISPECIES: ribosome biogenesis GTP-binding protein YihA/YsxC [Klebsiella]

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, ...
 5-196 1.52e-118

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: 334.73  E-value: 1.52e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092   5 NYQLTHFVTSAPDIRHLPADTGIEVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVAEGKRLVDLPGYGY 84
Cdd:COG0218    2 KIKKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  85 AQVPEEMKIKWQRALGEYLEKRLCLKGLVVLMDIRHPLKDLDQQMIQWAVESDIPVLVLLTKADKLASGARKAQIAMVRE 164
Cdd:COG0218   82 AKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIKK 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 490994092 165 AVTAFNGDVQVEAFSSLKKQGVDKLRQKLDSW 196
Cdd:COG0218  162 ALGKDPAAPEVILFSSLKKEGIDELRAAIEEW 193
 
Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 5-196 1.52e-118

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: 334.73  E-value: 1.52e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092   5 NYQLTHFVTSAPDIRHLPADTGIEVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVAEGKRLVDLPGYGY 84
Cdd:COG0218    2 KIKKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  85 AQVPEEMKIKWQRALGEYLEKRLCLKGLVVLMDIRHPLKDLDQQMIQWAVESDIPVLVLLTKADKLASGARKAQIAMVRE 164
Cdd:COG0218   82 AKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIKK 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 490994092 165 AVTAFNGDVQVEAFSSLKKQGVDKLRQKLDSW 196
Cdd:COG0218  162 ALGKDPAAPEVILFSSLKKEGIDELRAAIEEW 193
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 9-187 2.34e-114

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: 323.27  E-value: 2.34e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092    9 THFVTSAPDIRHLPADTGIEVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVAEGKRLVDLPGYGYAQVP 88
Cdd:TIGR03598   1 AEFVKSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFEVNDGFRLVDLPGYGYAKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092   89 EEMKIKWQRALGEYLEKRLCLKGLVVLMDIRHPLKDLDQQMIQWAVESDIPVLVLLTKADKLASGARKAQIAMVREAVTA 168
Cdd:TIGR03598  81 KEEKEKWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKALKK 160

                         170
                  ....*....|....*....
gi 490994092  169 FNGDVQVEAFSSLKKQGVD 187
Cdd:TIGR03598 161 DADDPSVQLFSSLKKTGID 179
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 28-196 4.20e-94

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: 271.69  E-value: 4.20e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  28 EVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVAEGKRLVDLPGYGYAQVPEEMKIKWQRALGEYLEKRL 107
Cdd:cd01876    1 EVAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAKVSKEVREKWGKLIEEYLENRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092 108 CLKGLVVLMDIRHPLKDLDQQMIQWAVESDIPVLVLLTKADKLASGARKAQIAMVREAVTAFNGDVQVEAFSSLKKQGVD 187
Cdd:cd01876   81 NLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLFNILPPVILFSSKKGTGID 160


                 ....*....
gi 490994092 188 KLRQKLDSW 196
Cdd:cd01876  161 ELRALIAEW 169
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 28-146 2.97e-25

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: 94.99  E-value: 2.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092   28 EVAFAGRSNAGKSSALNTLTNQKslARTSKTPGRTQLINLFEVAEGKR---LVDLPGygyaqVPEEMKIKWQRALgEYLE 104
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK--AIVSDYPGTTRDPNEGRLELKGKqiiLVDTPG-----LIEGASEGEGLGR-AFLA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 490994092  105 KRLClKGLVVLMDIRHPLKDLDQQMIQWAVESDIPVLVLLTK 146
Cdd:pfam01926  73 IIEA-DLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
PRK04213 PRK04213
GTP-binding protein EngB;
24-149 9.84e-14

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 66.86  E-value: 9.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  24 DTGIEVAFAGRSNAGKSSALNTLTNQKslARTSKTPGRTQLINLFEVAEgKRLVDLPGYGY-AQVPEEMKIKWQRALGEY 102
Cdd:PRK04213   7 DRKPEIVFVGRSNVGKSTLVRELTGKK--VRVGKRPGVTRKPNHYDWGD-FILTDLPGFGFmSGVPKEVQEKIKDEIVRY 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490994092 103 LE---KRLCLKGLVV----LMDI--RHPLKD---LDQQMIQWAVESDIPVLVLLTKADK 149
Cdd:PRK04213  84 IEdnaDRILAAVLVVdgksFIEIieRWEGRGeipIDVEMFDFLRELGIPPIVAVNKMDK 142
 
Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 5-196 1.52e-118

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: 334.73  E-value: 1.52e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092   5 NYQLTHFVTSAPDIRHLPADTGIEVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVAEGKRLVDLPGYGY 84
Cdd:COG0218    2 KIKKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  85 AQVPEEMKIKWQRALGEYLEKRLCLKGLVVLMDIRHPLKDLDQQMIQWAVESDIPVLVLLTKADKLASGARKAQIAMVRE 164
Cdd:COG0218   82 AKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIKK 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 490994092 165 AVTAFNGDVQVEAFSSLKKQGVDKLRQKLDSW 196
Cdd:COG0218  162 ALGKDPAAPEVILFSSLKKEGIDELRAAIEEW 193
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 9-187 2.34e-114

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: 323.27  E-value: 2.34e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092    9 THFVTSAPDIRHLPADTGIEVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVAEGKRLVDLPGYGYAQVP 88
Cdd:TIGR03598   1 AEFVKSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFEVNDGFRLVDLPGYGYAKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092   89 EEMKIKWQRALGEYLEKRLCLKGLVVLMDIRHPLKDLDQQMIQWAVESDIPVLVLLTKADKLASGARKAQIAMVREAVTA 168
Cdd:TIGR03598  81 KEEKEKWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKALKK 160

                         170
                  ....*....|....*....
gi 490994092  169 FNGDVQVEAFSSLKKQGVD 187
Cdd:TIGR03598 161 DADDPSVQLFSSLKKTGID 179
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 28-196 4.20e-94

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: 271.69  E-value: 4.20e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  28 EVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVAEGKRLVDLPGYGYAQVPEEMKIKWQRALGEYLEKRL 107
Cdd:cd01876    1 EVAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAKVSKEVREKWGKLIEEYLENRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092 108 CLKGLVVLMDIRHPLKDLDQQMIQWAVESDIPVLVLLTKADKLASGARKAQIAMVREAVTAFNGDVQVEAFSSLKKQGVD 187
Cdd:cd01876   81 NLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLFNILPPVILFSSKKGTGID 160


                 ....*....
gi 490994092 188 KLRQKLDSW 196
Cdd:cd01876  161 ELRALIAEW 169
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 30-196 1.42e-26

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: 99.63  E-value: 1.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  30 AFAGRSNAGKSSALNTLTNQKSLArTSKTPGRTQLINLFEVAEGK----RLVDLPGYGYAQVPEEMKIkwQRALGEYLEK 105
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGI-VSPIPGTTRDPVRKEWELLPlgpvVLIDTPGLDEEGGLGRERV--EEARQVADRA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092 106 RLCLkgLVVlmDIRHPLKDLDQQmIQWAVESDIPVLVLLTKADKLASGARKAQIamvREAVTAFNGDVQVEAFSSLKKQG 185
Cdd:cd00880   78 DLVL--LVV--DSDLTPVEEEAK-LGLLRERGKPVLLVLNKIDLVPESEEEELL---RERKLELLPDLPVIAVSALPGEG 149

                        170
                 ....*....|.
gi 490994092 186 VDKLRQKLDSW 196
Cdd:cd00880  150 IDELRKKIAEL 160
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 28-146 2.97e-25

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: 94.99  E-value: 2.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092   28 EVAFAGRSNAGKSSALNTLTNQKslARTSKTPGRTQLINLFEVAEGKR---LVDLPGygyaqVPEEMKIKWQRALgEYLE 104
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK--AIVSDYPGTTRDPNEGRLELKGKqiiLVDTPG-----LIEGASEGEGLGR-AFLA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 490994092  105 KRLClKGLVVLMDIRHPLKDLDQQMIQWAVESDIPVLVLLTK 146
Cdd:pfam01926  73 IIEA-DLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 30-193 3.52e-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: 3.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  30 AFAGRSNAGKSSALNTLTNQKSLArTSKTPGRTQLINLFEVAEGK-----RLVDLPGYGYAQVPEEMKIKWQRALGeyle 104
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGE-VSDVPGTTRDPDVYVKELDKgkvklVLVDTPGLDEFGGLGREELARLLLRG---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092 105 krlcLKGLVVLMDIRHPLKDLDQQ--MIQWAVESDIPVLVLLTKADKLasgARKAQIAMVREAVTAFNGDVQVEAFSSLK 182
Cdd:cd00882   76 ----ADLILLVVDSTDRESEEDAKllILRRLRKEGIPIILVGNKIDLL---EEREVEELLRLEELAKILGVPVFEVSAKT 148

                        170
                 ....*....|.
gi 490994092 183 KQGVDKLRQKL 193
Cdd:cd00882  149 GEGVDELFEKL 159
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 29-193 3.58e-14

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 67.49  E-value: 3.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  29 VAFAGRSNAGKSSALNTLTNQKsLARTSKTP-------------GRTQLInlfevaegkrLVDLPGYgyaqvpeemkIKW 95
Cdd:cd04163    6 VAIIGRPNVGKSTLLNALVGQK-ISIVSPKPqttrnrirgiytdDDAQII----------FVDTPGI----------HKP 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  96 QRALGEYLeKRLCLKGL------VVLMDIRHPLKDLDQQMIQWAVESDIPVLVLLTKADKLasgARKAQIAMVREAVTAF 169
Cdd:cd04163   65 KKKLGERM-VKAAWSALkdvdlvLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLV---KDKEDLLPLLEKLKEL 140

                        170       180
                 ....*....|....*....|....
gi 490994092 170 NGDVQVEAFSSLKKQGVDKLRQKL 193
Cdd:cd04163  141 HPFAEIFPISALKGENVDELLEYI 164
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
29-193 8.10e-14

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 68.48  E-value: 8.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  29 VAFAGRSNAGKSSALNTLTNQKsLARTSKTP-------------GRTQLInlfevaegkrLVDLPGYgyaqvpeemkIKW 95
Cdd:COG1159    6 VAIVGRPNVGKSTLLNALVGQK-VSIVSPKPqttrhrirgivtrEDAQIV----------FVDTPGI----------HKP 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  96 QRALGEYLeKRLCLKGL----VVLM--DIRHPLKDLDQQMIQWAVESDIPVLVLLTKADKLasgaRKAQIAMVREAVTAF 169
Cdd:COG1159   65 KRKLGRRM-NKAAWSALedvdVILFvvDATEKIGEGDEFILELLKKLKTPVILVINKIDLV----KKEELLPLLAEYSEL 139

                        170       180
                 ....*....|....*....|....
gi 490994092 170 NGDVQVEAFSSLKKQGVDKLRQKL 193
Cdd:COG1159  140 LDFAEIVPISALKGDNVDELLDEI 163
PRK04213 PRK04213
GTP-binding protein EngB;
24-149 9.84e-14

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 66.86  E-value: 9.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  24 DTGIEVAFAGRSNAGKSSALNTLTNQKslARTSKTPGRTQLINLFEVAEgKRLVDLPGYGY-AQVPEEMKIKWQRALGEY 102
Cdd:PRK04213   7 DRKPEIVFVGRSNVGKSTLVRELTGKK--VRVGKRPGVTRKPNHYDWGD-FILTDLPGFGFmSGVPKEVQEKIKDEIVRY 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490994092 103 LE---KRLCLKGLVV----LMDI--RHPLKD---LDQQMIQWAVESDIPVLVLLTKADK 149
Cdd:PRK04213  84 IEdnaDRILAAVLVVdgksFIEIieRWEGRGeipIDVEMFDFLRELGIPPIVAVNKMDK 142
era PRK00089
GTPase Era; Reviewed
 29-193 1.28e-13

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 67.77  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  29 VAFAGRSNAGKSSALNTLTNQKsLARTSKTP-------------GRTQLInlfevaegkrLVDLPGYgyaqvpeemkIKW 95
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQK-ISIVSPKPqttrhrirgivteDDAQII----------FVDTPGI----------HKP 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  96 QRALGEYLEK--RLCLKG--LVVLM-DIRHPLKDLDQQMIQWAVESDIPVLVLLTKADKLASgarKAQIAMVREAVTAFN 170
Cdd:PRK00089  67 KRALNRAMNKaaWSSLKDvdLVLFVvDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVKD---KEELLPLLEELSELM 143

                        170       180
                 ....*....|....*....|...
gi 490994092 171 GDVQVEAFSSLKKQGVDKLRQKL 193
Cdd:PRK00089 144 DFAEIVPISALKGDNVDELLDVI 166
YeeP COG3596
Predicted GTPase [General function prediction only];
28-193 9.29e-09

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 54.00  E-value: 9.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  28 EVAFAGRSNAGKSSALNTLTNQkSLARTSKTPGRTQLINLFEVAEGK----RLVDLPGYGYAQVPEEmkikWQRALGEYL 103
Cdd:COG3596   41 VIALVGKTGAGKSSLINALFGA-EVAEVGVGRPCTREIQRYRLESDGlpglVLLDTPGLGEVNERDR----EYRELRELL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092 104 EkrlCLKGLVVLMDIRHPLKDLDQQMIQWAVE--SDIPVLVLLTKADKL---------ASGARKAQIAMVREAVTAFNGD 172
Cdd:COG3596  116 P---EADLILWVVKADDRALATDEEFLQALRAqyPDPPVLVVLTQVDRLeperewdppYNWPSPPKEQNIRRALEAIAEQ 192

                        170       180
                 ....*....|....*....|....*....
gi 490994092 173 VQVE-----AFSSLKKQ---GVDKLRQKL 193
Cdd:COG3596  193 LGVPidrviPVSAAEDRtgyGLEELVDAL 221
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 25-193 4.55e-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: 50.57  E-value: 4.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  25 TGIEVAFAGRSNAGKSSALNTLTNQKSlARTSKTPGRT-----QLINL--FEVaegkRLVDLPGYGYAQVPEEmKIKWQR 97
Cdd:cd04164    2 EGIKVVIAGKPNVGKSSLLNALAGRDR-AIVSDIAGTTrdvieEEIDLggIPV----RLIDTAGLRETEDEIE-KIGIER 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  98 ALGEYLEKRLCLkglvVLMDIRHPLKDLDQQMIQWAveSDIPVLVLLTKADKLASGARKAQIamvreavtafNGDVQVeA 177
Cdd:cd04164   76 AREAIEEADLVL----LVVDASEGLDEEDLEILELP--AKKPVIVVLNKSDLLSDAEGISEL----------NGKPII-A 138

                        170
                 ....*....|....*.
gi 490994092 178 FSSLKKQGVDKLRQKL 193
Cdd:cd04164  139 ISAKTGEGIDELKEAL 154
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 26-189 7.64e-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: 7.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  26 GIEVAFAGRSNAGKSSALNTLTNQKslaR--TSKTPGRTQ--LINLFEVaEGKR--LVDLPGygyaqvpeemkIKWQRAL 99
Cdd:cd01895    2 PIKIAIIGRPNVGKSSLLNALLGEE---RviVSDIAGTTRdsIDVPFEY-DGQKytLIDTAG-----------IRKKGKV 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092 100 GEYLEKRLCLKGL---------VVLMDIRHPLKDLDQQMIQWAVESDIPVLVLLTKADKLasGARKAQIAMVREAVT--- 167
Cdd:cd01895   67 TEGIEKYSVLRTLkaieradvvLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLV--EKDEKTMKEFEKELRrkl 144

                        170       180
                 ....*....|....*....|..
gi 490994092 168 AFNGDVQVEAFSSLKKQGVDKL 189
Cdd:cd01895  145 PFLDYAPIVFISALTGQGVDKL 166
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 22-189 8.65e-08

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 51.59  E-value: 8.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  22 PADTGIEVAFAGRSNAGKSSALNTLTNQKslaR--TSKTPGRTQ-LIN-LFEVaEGK--RLVDLPGygyaqvpeeM---- 91
Cdd:PRK00093 169 EEDEPIKIAIIGRPNVGKSSLINALLGEE---RviVSDIAGTTRdSIDtPFER-DGQkyTLIDTAG---------Irrkg 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  92 KIKwqralgEYLEKRLCLKGL---------VVLMDIRHPLKDLDQQMIQWAVESDIPVLVLLTKADKLASGARKAQIAMV 162
Cdd:PRK00093 236 KVT------EGVEKYSVIRTLkaieradvvLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKWDLVDEKTMEEFKKEL 309

                        170       180
                 ....*....|....*....|....*..
gi 490994092 163 REAVtAFNGDVQVEAFSSLKKQGVDKL 189
Cdd:PRK00093 310 RRRL-PFLDYAPIVFISALTGQGVDKL 335
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 29-165 4.63e-07

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: 47.93  E-value: 4.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  29 VAFAGRSNAGKSSALNTLTNQKSLArTSKTPgRTQLINL--FEVAEGKRLVDLPGYGYAQVPEEMKIKwqralgEYLEKr 106
Cdd:cd09912    3 LAVVGEFSAGKSTLLNALLGEEVLP-TGVTP-TTAVITVlrYGLLKGVVLVDTPGLNSTIEHHTEITE------SFLPR- 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092 107 lcLKGLVVLMDIRHPLKDLDQQ-MIQWAVESDIPVLVLLTKADKLASGARKAQIAMVREA 165
Cdd:cd09912   74 --ADAVIFVLSADQPLTESEREfLKEILKWSGKKIFFVLNKIDLLSEEELEEVLEYSREE 131
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 26-193 1.01e-06

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: 48.13  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  26 GIEVAFAGRSNAGKSSALNTLTNQKSlARTSKTPGRT-----QLINLfevaEGK--RLVDLpgygyA-------QVpEEM 91
Cdd:COG0486  213 GIKVVIVGRPNVGKSSLLNALLGEER-AIVTDIAGTTrdvieERINI----GGIpvRLIDT-----AglretedEV-EKI 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  92 KIKwqRALGEylekrlcLKG--LVVLM-DIRHPLKDLDQQMIQWAveSDIPVLVLLTKADKLASGArkaqiamvrEAVTA 168
Cdd:COG0486  282 GIE--RAREA-------IEEadLVLLLlDASEPLTEEDEEILEKL--KDKPVIVVLNKIDLPSEAD---------GELKS 341

                        170       180
                 ....*....|....*....|....*
gi 490994092 169 FNGDVQVeAFSSLKKQGVDKLRQKL 193
Cdd:COG0486  342 LPGEPVI-AISAKTGEGIDELKEAI 365
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 29-81 3.03e-06

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: 45.30  E-value: 3.03e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490994092  29 VAFAGRSNAGKSSALNTLTNQKsLARTSKTPGRTQLINLFEVAEGKRLVDLPG 81
Cdd:cd01857   85 IGLVGYPNVGKSSLINALVGSK-KVSVSSTPGKTKHFQTIFLEPGITLCDCPG 136
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 31-82 6.08e-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: 44.95  E-value: 6.08e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490994092  31 FAGRSNAGKSSALNTL----------TNQKSLARTSKTPGRTQLINLFEVAEGKRLVDLPGY 82
Cdd:cd01855  130 VVGATNVGKSTLINALlksnggkvqaQALVQRLTVSPIPGTTLGLIKIPLGEGKKLYDTPGI 191
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 30-149 9.85e-06

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: 43.87  E-value: 9.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  30 AFAGRSNAGKSSALNTLTnQKSLARTSKTPGRTQLINLFEVA---EGKRLVDLPGYGYAQVPEEmkikWQRALGEYLEKR 106
Cdd:cd11383    1 GLMGKTGAGKSSLCNALF-GTEVAAVGDRRPTTRAAQAYVWQtggDGLVLLDLPGVGERGRRDR----EYEELYRRLLPE 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 490994092 107 LCLkgLVVLMDIRHPLKDLDQQMIQ-WAVESDIPVLVLLTKADK 149
Cdd:cd11383   76 ADL--VLWLLDADDRALAADHDFYLlPLAGHDAPLLFVLNQVDP 117
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
26-193 1.07e-05

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 45.10  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  26 GIEVAFAGRSNAGKSSALNTLTNQKSlARTSKTPGRT-----QLINLfevaEGK--RLVDLPGYGYAQVPEEmKIKWQRA 98
Cdd:PRK05291 215 GLKVVIAGRPNVGKSSLLNALLGEER-AIVTDIAGTTrdvieEHINL----DGIplRLIDTAGIRETDDEVE-KIGIERS 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  99 LGEylekrlcLKG--LVVLM-DIRHPLKDLDQQmiQWAVESDIPVLVLLTKADkLASGARKAQIamvreavtafNGDVQV 175
Cdd:PRK05291 289 REA-------IEEadLVLLVlDASEPLTEEDDE--ILEELKDKPVIVVLNKAD-LTGEIDLEEE----------NGKPVI 348

                        170
                 ....*....|....*...
gi 490994092 176 eAFSSLKKQGVDKLRQKL 193
Cdd:PRK05291 349 -RISAKTGEGIDELREAI 365
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
22-189 1.24e-05

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 45.01  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  22 PADTGIEVAFAGRSNAGKSSALNTLTNQKslaR--TSKTPGRTQ-LIN-LFEVaEGK--RLVDLPGygyaqvpeeM---- 91
Cdd:COG1160  171 EEDDPIKIAIVGRPNVGKSSLINALLGEE---RviVSDIAGTTRdSIDtPFER-DGKkyTLIDTAG---------Irrkg 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  92 KIKwqralgEYLEKRLCLKGL---------VVLMDIRHPLKDLDQQMIQWAVESDIPVLVLLTKADKLA--SGARKAQIA 160
Cdd:COG1160  238 KVD------EGIEKYSVLRTLraieradvvLLVIDATEGITEQDLKIAGLALEAGKALVIVVNKWDLVEkdRKTREELEK 311

                        170       180
                 ....*....|....*....|....*....
gi 490994092 161 MVREAVtAFNGDVQVEAFSSLKKQGVDKL 189
Cdd:COG1160  312 EIRRRL-PFLDYAPIVFISALTGQGVDKL 339
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 26-193 8.49e-05

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: 42.47  E-value: 8.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092   26 GIEVAFAGRSNAGKSSALNTLTNQKSlARTSKTPGRT-----QLINLfevaEGK--RLVDLPG--YGYAQVpEEMKIKwq 96
Cdd:pfam12631  94 GIKVVIVGKPNVGKSSLLNALLGEER-AIVTDIPGTTrdvieETINI----GGIplRLIDTAGirETDDEV-EKIGIE-- 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092   97 RALgEYLEKrlclKGLVVLM-DIRHPLKDLDQQMIQwAVESDIPVLVLLTKADKLASGARKAQiamvreavtafNGDVQV 175
Cdd:pfam12631 166 RAR-EAIEE----ADLVLLVlDASRPLDEEDLEILE-LLKDKKPIIVVLNKSDLLGEIDELEE-----------LKGKPV 228

                         170
                  ....*....|....*...
gi 490994092  176 EAFSSLKKQGVDKLRQKL 193
Cdd:pfam12631 229 LAISAKTGEGLDELEEAI 246
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 24-81 1.33e-04

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: 40.45  E-value: 1.33e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490994092  24 DTGIEVAFAGRSNAGKSSALNTLTNQKSLaRTSKTPGRTQLINLFEVAEGKRLVDLPG 81
Cdd:cd01849   89 KKGIRVGVVGLPNVGKSSFINALLNKFKL-KVGSIPGTTKLQQDVKLDKEIYLYDTPG 145
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 133-193 2.18e-04

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


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 40.84  E-value: 2.18e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490994092 133 AVESDIPVLVLLTKADKLASGARKAQIAMVREAvtafngDVQVEAFSSLKKQGVDKLRQKL 193
Cdd:cd01854   29 AEASGIEPVIVLNKADLVDDEELEELLEIYEKL------GYPVLAVSAKTGEGLDELRELL 83
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 30-199 2.73e-04

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: 39.75  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  30 AFAGRSNAGKSSALNTLTNqkSLARTSKTPGRTqlinlFEVAEGK--------RLVDLPG-Y---GYAqvPEEmKIKwqr 97
Cdd:cd01879    1 ALVGNPNVGKTTLFNALTG--ARQKVGNWPGVT-----VEKKEGEfklggkeiEIVDLPGtYsltPYS--EDE-KVA--- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  98 algeyleKRLCLKG----LVVLMDIRHplkdLDQQM---IQwAVESDIPVLVLLTKADKlasgARKAQIAMVREAVTAFN 170
Cdd:cd01879   68 -------RDFLLGEepdlIVNVVDATN----LERNLyltLQ-LLELGLPVVVALNMIDE----AEKRGIKIDLDKLSELL 131

                        170       180
                 ....*....|....*....|....*....
gi 490994092 171 GdVQVEAFSSLKKQGVDKLRQKLDSWYND 199
Cdd:cd01879  132 G-VPVVPTSARKGEGIDELLDAIAKLAES 159
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 29-81 2.78e-04

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: 39.99  E-value: 2.78e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490994092  29 VAFAGRSNAGKSSALNTLTNQKSlARTSKTPGR---TQLINLFEVAEGKRLVDLPG 81
Cdd:cd01859  102 VGVVGYPKVGKSSIINALKGRHS-ASTSPIPGSpgyTKGIQLVRIDSKIYLIDTPG 156
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 29-195 3.59e-04

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 40.46  E-value: 3.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  29 VAFAGRSNAGKSSALNTLTNQKSLA------------RTSKTPGR----------------TQLINLF-----EVAEgkr 75
Cdd:COG2262  202 VALVGYTNAGKSTLFNRLTGADVLAedklfatldpttRRLELPDGrpvlltdtvgfirklpHQLVEAFrstleEVRE--- 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  76 lVDLpgygyaqvpeemkikwqralgeylekrlclkgLVVLMDIRHPlkDLDQQMiqWAVES--------DIPVLVLLTKA 147
Cdd:COG2262  279 -ADL--------------------------------LLHVVDASDP--DFEEQI--ETVNEvleelgadDKPIILVFNKI 321

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 490994092 148 DKLASGARKAQIAMVREAVtafngdvqveAFSSLKKQGVDKLRQKLDS 195
Cdd:COG2262  322 DLLDDEELERLRAGYPDAV----------FISAKTGEGIDELLEAIEE 359
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 33-158 4.48e-04

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: 39.34  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  33 GRSNAGKSSALNTLTNQKsLARTSKTPGRTQLInLFEVAE--GKR--LVDLPGYGYAQVP--EEMKIKWQRALGEylekr 106
Cdd:cd01894    4 GRPNVGKSTLFNRLTGRR-DAIVSDTPGVTRDR-KYGEAEwgGREfiLIDTGGIEPDDEGisKEIREQAEIAIEE----- 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490994092 107 lclKGLVV-LMDIRHPLKDLDQQMIQWAVESDIPVLVLLTKADKLASGARKAQ 158
Cdd:cd01894   77 ---ADVILfVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNIKEEEEAAE 126
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
 101-175 5.01e-04

cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino acid sequence of YjiA protein in E. coli contains several conserved motifs that characterizes it as a P-loop GTPase. YijA gene is among the genes significantly induced in response to DNA-damage caused by mitomycin. YijA gene is a homologue of the CobW gene which encodes the cobalamin synthesis protein/P47K.


Pssm-ID: 349766  Cd Length: 198  Bit Score: 39.43  E-value: 5.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092 101 EYLEKRLCLKGLVVLMDIRHPLKDLDQQMI------QWAVeSDipvLVLLTKADKLASgarkAQIAMVREAVTAFNGDVQ 174
Cdd:cd03112  109 EELESRLRLDGVVTVVDAKNFLKQLDEEDVsdlavdQIAF-AD---VIVLNKTDLVDE----EELEALRARIRALNPGAK 180


                 .
gi 490994092 175 V 175
Cdd:cd03112  181 I 181
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 36-81 5.42e-04

Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. The YlqF subfamily is represented in all eukaryotes as well as a phylogenetically diverse array of bacteria (including gram-positive bacteria, proteobacteria, Synechocystis, Borrelia, and Thermotoga).


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 39.05  E-value: 5.42e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 490994092  36 NAGKSSALNTLTNQKSlARTSKTPGRTQLINLFEVAEGKRLVDLPG 81
Cdd:cd01856  125 NVGKSTLINRLRGKKV-AKVGNKPGVTRGQQWIRIGPNIELLDTPG 169
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 141-206 1.48e-03

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


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 39.13  E-value: 1.48e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490994092 141 LVLLTKADkLASGARkaqIAMVREAVTAF-NG----DVQVEAFSSLKKQGVDKLRQKLDSWYNDIPPQEAS 206
Cdd:COG3276  108 IVVLTKAD-LVDEEW---LELVEEEIRELlAGtfleDAPIVPVSAVTGEGIDELRAALDALAAAVPARDAD 174
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
 29-152 2.21e-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: 37.69  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  29 VAFAGRSNAGKSSALNTLTNQK-SLARTSKTPGRTQLINLFEVAEGKRLVDLPGYGyaQVPEEMKikwqralgEYLEKRl 107
Cdd:cd04105    3 VLLLGPSDSGKTALFTKLTTGKvRSTVTSIEPNVASFYSNSSKGKKLTLVDVPGHE--KLRDKLL--------EYLKAS- 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490994092 108 cLKGLVVLMDIRHPLKDLDQQ--------MIQWAVESDIPVLVLLTKADKLAS 152
Cdd:cd04105   72 -LKAIVFVVDSATFQKNIRDVaeflydilTDLEKIKNKIPILIACNKQDLFTA 123
PRK12289 PRK12289
small ribosomal subunit biogenesis GTPase RsgA;
31-91 4.28e-03

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237040 [Multi-domain]  Cd Length: 352  Bit Score: 37.30  E-value: 4.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490994092  31 FAGRSNAGKSSALNTLTNQKSLaRTSKTPGR-------TQLINLFEVAEGKRLVDLPGYGYAQV---PEEM 91
Cdd:PRK12289 177 VAGPSGVGKSSLINRLIPDVEL-RVGKVSGKlgrgrhtTRHVELFELPNGGLLADTPGFNQPDLdcsPREL 246
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
36-81 7.34e-03

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 36.62  E-value: 7.34e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 490994092  36 NAGKSSALNTLTNQKSlARTSKTPGRT---QLINLfevAEGKRLVDLPG 81
Cdd:COG1161  123 NVGKSTLINRLAGKKV-AKTGNKPGVTkgqQWIKL---DDGLELLDTPG 167
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 2-81 7.52e-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: 35.98  E-value: 7.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092    2 TNWNYQLthFVTSA------PDIR-HLPADTgieVAFAGRSNAGKSSALNTLTNQKSLA--RTSKTPGR----TQLINLF 68
Cdd:pfam03193  80 RAIGYPV--LFVSAktgegiEALKeLLKGKT---TVLAGQSGVGKSTLLNALLPELDLRtgEISEKLGRgrhtTTHVELF 154

                          90
                  ....*....|...
gi 490994092   69 EVAEGKRLVDLPG 81
Cdd:pfam03193 155 PLPGGGLLIDTPG 167
NGP_1 cd01858
A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; ...
 27-81 8.72e-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: 35.35  E-value: 8.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994092  27 IEVAFAGRSNAGKSSALNTLTNQKsLARTSKTPGRT---QLINLFevaegKR--LVDLPG 81
Cdd:cd01858  103 ISVGFIGYPNVGKSSVINTLRSKK-VCKVAPIPGETkvwQYITLM-----KRiyLIDCPG 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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