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Conserved domains on  [gi|119369257|sp|Q32A36|]
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RecName: Full=Probable GTP-binding protein EngB

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, ...
 5-197 3.01e-119

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: 336.27  E-value: 3.01e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257   5 NYQQTHFVMSAPDIRHLPSDTGIEVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVADGKRLVDLPGYGY 84
Cdd:COG0218    2 KIKKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  85 AEVPEEMKRKWQRALGEYLEKRQSLQGLVVLMDIRHPLKDLDQQMIEWAVDSNIAVLVLLTKADKLASGARKAQLNMVRE 164
Cdd:COG0218   82 AKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIKK 161

                        170       180       190
                 ....*....|....*....|....*....|...
gi 119369257 165 AVLAFNGDVQVETFSSLKKQGVDKLRQKLDTWF 197
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, ...
 5-197 3.01e-119

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: 336.27  E-value: 3.01e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257   5 NYQQTHFVMSAPDIRHLPSDTGIEVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVADGKRLVDLPGYGY 84
Cdd:COG0218    2 KIKKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  85 AEVPEEMKRKWQRALGEYLEKRQSLQGLVVLMDIRHPLKDLDQQMIEWAVDSNIAVLVLLTKADKLASGARKAQLNMVRE 164
Cdd:COG0218   82 AKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIKK 161

                        170       180       190
                 ....*....|....*....|....*....|...
gi 119369257 165 AVLAFNGDVQVETFSSLKKQGVDKLRQKLDTWF 197
Cdd:COG0218  162 ALGKDPAAPEVILFSSLKKEGIDELRAAIEEWL 194
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 9-187 2.75e-112

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: 318.26  E-value: 2.75e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257    9 THFVMSAPDIRHLPSDTGIEVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVADGKRLVDLPGYGYAEVP 88
Cdd:TIGR03598   1 AEFVKSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFEVNDGFRLVDLPGYGYAKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257   89 EEMKRKWQRALGEYLEKRQSLQGLVVLMDIRHPLKDLDQQMIEWAVDSNIAVLVLLTKADKLASGARKAQLNMVREAVLA 168
Cdd:TIGR03598  81 KEEKEKWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKALKK 160

                         170
                  ....*....|....*....
gi 119369257  169 FNGDVQVETFSSLKKQGVD 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 ...
 28-197 5.39e-93

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: 268.99  E-value: 5.39e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  28 EVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVADGKRLVDLPGYGYAEVPEEMKRKWQRALGEYLEKRQ 107
Cdd:cd01876    1 EVAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAKVSKEVREKWGKLIEEYLENRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257 108 SLQGLVVLMDIRHPLKDLDQQMIEWAVDSNIAVLVLLTKADKLASGARKAQLNMVREAVLAFNGDVQVETFSSLKKQGVD 187
Cdd:cd01876   81 NLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLFNILPPVILFSSKKGTGID 160

                        170
                 ....*....|
gi 119369257 188 KLRQKLDTWF 197
Cdd:cd01876  161 ELRALIAEWL 170
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 28-146 2.49e-24

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: 92.30  E-value: 2.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257   28 EVAFAGRSNAGKSSALNTLTNQKslARTSKTPGRTQLINLFEVADGKR---LVDLPGygyaeVPEEMKRKWQRALgEYLE 104
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK--AIVSDYPGTTRDPNEGRLELKGKqiiLVDTPG-----LIEGASEGEGLGR-AFLA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 119369257  105 KRQSlQGLVVLMDIRHPLKDLDQQMIEWAVDSNIAVLVLLTK 146
Cdd:pfam01926  73 IIEA-DLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
era PRK00089
GTPase Era; Reviewed
 29-193 3.88e-15

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 72.00  E-value: 3.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  29 VAFAGRSNAGKSSALNTLTNQKsLARTSKTP-------------GRTQLInlfevadgkrLVDLPGYgyaevpeeMKRKw 95
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQK-ISIVSPKPqttrhrirgivteDDAQII----------FVDTPGI--------HKPK- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  96 qRALGEYLEK--RQSLQG--LVVLM-DIRHPLKDLDQQMIEWAVDSNIAVLVLLTKADKLASgarKAQLNMVREAVLAFN 170
Cdd:PRK00089  68 -RALNRAMNKaaWSSLKDvdLVLFVvDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVKD---KEELLPLLEELSELM 143

                        170       180
                 ....*....|....*....|...
gi 119369257 171 GDVQVETFSSLKKQGVDKLRQKL 193
Cdd:PRK00089 144 DFAEIVPISALKGDNVDELLDVI 166
 
Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 5-197 3.01e-119

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: 336.27  E-value: 3.01e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257   5 NYQQTHFVMSAPDIRHLPSDTGIEVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVADGKRLVDLPGYGY 84
Cdd:COG0218    2 KIKKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  85 AEVPEEMKRKWQRALGEYLEKRQSLQGLVVLMDIRHPLKDLDQQMIEWAVDSNIAVLVLLTKADKLASGARKAQLNMVRE 164
Cdd:COG0218   82 AKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIKK 161

                        170       180       190
                 ....*....|....*....|....*....|...
gi 119369257 165 AVLAFNGDVQVETFSSLKKQGVDKLRQKLDTWF 197
Cdd:COG0218  162 ALGKDPAAPEVILFSSLKKEGIDELRAAIEEWL 194
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 9-187 2.75e-112

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: 318.26  E-value: 2.75e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257    9 THFVMSAPDIRHLPSDTGIEVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVADGKRLVDLPGYGYAEVP 88
Cdd:TIGR03598   1 AEFVKSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFEVNDGFRLVDLPGYGYAKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257   89 EEMKRKWQRALGEYLEKRQSLQGLVVLMDIRHPLKDLDQQMIEWAVDSNIAVLVLLTKADKLASGARKAQLNMVREAVLA 168
Cdd:TIGR03598  81 KEEKEKWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKALKK 160

                         170
                  ....*....|....*....
gi 119369257  169 FNGDVQVETFSSLKKQGVD 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 ...
 28-197 5.39e-93

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: 268.99  E-value: 5.39e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  28 EVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVADGKRLVDLPGYGYAEVPEEMKRKWQRALGEYLEKRQ 107
Cdd:cd01876    1 EVAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAKVSKEVREKWGKLIEEYLENRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257 108 SLQGLVVLMDIRHPLKDLDQQMIEWAVDSNIAVLVLLTKADKLASGARKAQLNMVREAVLAFNGDVQVETFSSLKKQGVD 187
Cdd:cd01876   81 NLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLFNILPPVILFSSKKGTGID 160

                        170
                 ....*....|
gi 119369257 188 KLRQKLDTWF 197
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 ...
 30-197 1.06e-27

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: 102.71  E-value: 1.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  30 AFAGRSNAGKSSALNTLTNQKSLArTSKTPGRTQLINLFEV----ADGKRLVDLPGYGYAEVPEEMKRKwqralgEYLEK 105
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGI-VSPIPGTTRDPVRKEWellpLGPVVLIDTPGLDEEGGLGRERVE------EARQV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257 106 RQSLQGLVVLMDIRHPLKDLDQQmIEWAVDSNIAVLVLLTKADKLASGARKAQLnmvREAVLAFNGDVQVETFSSLKKQG 185
Cdd:cd00880   74 ADRADLVLLVVDSDLTPVEEEAK-LGLLRERGKPVLLVLNKIDLVPESEEEELL---RERKLELLPDLPVIAVSALPGEG 149

                        170
                 ....*....|..
gi 119369257 186 VDKLRQKLDTWF 197
Cdd:cd00880  150 IDELRKKIAELL 161
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 28-146 2.49e-24

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: 92.30  E-value: 2.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257   28 EVAFAGRSNAGKSSALNTLTNQKslARTSKTPGRTQLINLFEVADGKR---LVDLPGygyaeVPEEMKRKWQRALgEYLE 104
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK--AIVSDYPGTTRDPNEGRLELKGKqiiLVDTPG-----LIEGASEGEGLGR-AFLA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 119369257  105 KRQSlQGLVVLMDIRHPLKDLDQQMIEWAVDSNIAVLVLLTK 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 1.08e-18

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


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 79.04  E-value: 1.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  30 AFAGRSNAGKSSALNTLTNQKSLArTSKTPGRTQLINLFEVADGK-----RLVDLPGYGYAEVPEEMKRKWQRALGeyle 104
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGE-VSDVPGTTRDPDVYVKELDKgkvklVLVDTPGLDEFGGLGREELARLLLRG---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257 105 krqsLQGLVVLMDIRHPLKDLDQQ--MIEWAVDSNIAVLVLLTKADKLASGARKAQLnmvREAVLAFNGDVQVETFSSLK 182
Cdd:cd00882   76 ----ADLILLVVDSTDRESEEDAKllILRRLRKEGIPIILVGNKIDLLEEREVEELL---RLEELAKILGVPVFEVSAKT 148

                        170
                 ....*....|.
gi 119369257 183 KQGVDKLRQKL 193
Cdd:cd00882  149 GEGVDELFEKL 159
era PRK00089
GTPase Era; Reviewed
 29-193 3.88e-15

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 72.00  E-value: 3.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  29 VAFAGRSNAGKSSALNTLTNQKsLARTSKTP-------------GRTQLInlfevadgkrLVDLPGYgyaevpeeMKRKw 95
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQK-ISIVSPKPqttrhrirgivteDDAQII----------FVDTPGI--------HKPK- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  96 qRALGEYLEK--RQSLQG--LVVLM-DIRHPLKDLDQQMIEWAVDSNIAVLVLLTKADKLASgarKAQLNMVREAVLAFN 170
Cdd:PRK00089  68 -RALNRAMNKaaWSSLKDvdLVLFVvDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVKD---KEELLPLLEELSELM 143

                        170       180
                 ....*....|....*....|...
gi 119369257 171 GDVQVETFSSLKKQGVDKLRQKL 193
Cdd:PRK00089 144 DFAEIVPISALKGDNVDELLDVI 166
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 29-193 1.05e-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: 68.64  E-value: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  29 VAFAGRSNAGKSSALNTLTNQKsLARTSKTP-------------GRTQLInlfevadgkrLVDLPGYgyaevpeeMKRKw 95
Cdd:cd04163    6 VAIIGRPNVGKSTLLNALVGQK-ISIVSPKPqttrnrirgiytdDDAQII----------FVDTPGI--------HKPK- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  96 qRALGEYLEK--RQSLQG--LVVLM-DIRHPLKDLDQQMIEWAVDSNIAVLVLLTKADKLasgARKAQLNMVREAVLAFN 170
Cdd:cd04163   66 -KKLGERMVKaaWSALKDvdLVLFVvDASEWIGEGDEFILELLKKSKTPVILVLNKIDLV---KDKEDLLPLLEKLKELH 141

                        170       180
                 ....*....|....*....|...
gi 119369257 171 GDVQVETFSSLKKQGVDKLRQKL 193
Cdd:cd04163  142 PFAEIFPISALKGENVDELLEYI 164
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
29-193 7.78e-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: 7.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  29 VAFAGRSNAGKSSALNTLTNQKsLARTSKTP-------------GRTQLInlfevadgkrLVDLPGYgyaevpeeMKRKw 95
Cdd:COG1159    6 VAIVGRPNVGKSTLLNALVGQK-VSIVSPKPqttrhrirgivtrEDAQIV----------FVDTPGI--------HKPK- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  96 qRALGEYLEK--RQSLQG--LVVLM-DIRHPLKDLDQQMIEWAVDSNIAVLVLLTKADKLasgaRKAQLNMVREAVLAFN 170
Cdd:COG1159   66 -RKLGRRMNKaaWSALEDvdVILFVvDATEKIGEGDEFILELLKKLKTPVILVINKIDLV----KKEELLPLLAEYSELL 140

                        170       180
                 ....*....|....*....|...
gi 119369257 171 GDVQVETFSSLKKQGVDKLRQKL 193
Cdd:COG1159  141 DFAEIVPISALKGDNVDELLDEI 163
PRK04213 PRK04213
GTP-binding protein EngB;
22-201 1.38e-13

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 66.48  E-value: 1.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  22 PSDTGIEVAFAGRSNAGKSSALNTLTNQKslARTSKTPGRTQLINLFEVADgKRLVDLPGYGYAE-VPEEMKRKWQRALG 100
Cdd:PRK04213   5 RPDRKPEIVFVGRSNVGKSTLVRELTGKK--VRVGKRPGVTRKPNHYDWGD-FILTDLPGFGFMSgVPKEVQEKIKDEIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257 101 EYLE---KRQSLQGLVV----LMDI--RHPLKD---LDQQMIEWAVDSNIAVLVLLTKADKLASgaRKAQLNMVREAvLA 168
Cdd:PRK04213  82 RYIEdnaDRILAAVLVVdgksFIEIieRWEGRGeipIDVEMFDFLRELGIPPIVAVNKMDKIKN--RDEVLDEIAER-LG 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 119369257 169 FNGDVQ--VETFS--SLKKQGVDKLRQKLDTWFSEMQ 201
Cdd:PRK04213 159 LYPPWRqwQDIIApiSAKKGGIEELKEAIRKRLHEAK 195
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 26-189 4.41e-13

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: 64.38  E-value: 4.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  26 GIEVAFAGRSNAGKSSALNTLTNQKslaR--TSKTPGRTQ--LINLFEVaDGKR--LVDLPGygyaevpeeMKRKwqRAL 99
Cdd:cd01895    2 PIKIAIIGRPNVGKSSLLNALLGEE---RviVSDIAGTTRdsIDVPFEY-DGQKytLIDTAG---------IRKK--GKV 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257 100 GEYLEKRQSLQGL---------VVLMDIRHPLKDLDQQMIEWAVDSNIAVLVLLTKADKLasGARKAQLNMVREAV---L 167
Cdd:cd01895   67 TEGIEKYSVLRTLkaieradvvLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLV--EKDEKTMKEFEKELrrkL 144

                        170       180
                 ....*....|....*....|..
gi 119369257 168 AFNGDVQVETFSSLKKQGVDKL 189
Cdd:cd01895  145 PFLDYAPIVFISALTGQGVDKL 166
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 22-189 3.83e-11

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 61.22  E-value: 3.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  22 PSDTGIEVAFAGRSNAGKSSALNTLTNQKslaR--TSKTPGRTQ-LIN-LFEVaDGK--RLVDLPGygyaevpeeMKRKw 95
Cdd:PRK00093 169 EEDEPIKIAIIGRPNVGKSSLINALLGEE---RviVSDIAGTTRdSIDtPFER-DGQkyTLIDTAG---------IRRK- 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  96 qRALGEYLEK----RqSLQGL------VVLMDIRHPLKDLDQQMIEWAVDSNIAVLVLLTKADKLASGARKAQLNMVREA 165
Cdd:PRK00093 235 -GKVTEGVEKysviR-TLKAIeradvvLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKWDLVDEKTMEEFKKELRRR 312

                        170       180
                 ....*....|....*....|....
gi 119369257 166 vLAFNGDVQVETFSSLKKQGVDKL 189
Cdd:PRK00093 313 -LPFLDYAPIVFISALTGQGVDKL 335
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
22-195 1.64e-09

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 56.57  E-value: 1.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  22 PSDTGIEVAFAGRSNAGKSSALNTLTNQKslaR--TSKTPGRTQ-LIN-LFEVaDGK--RLVDLPGygyaevpeeMKRKw 95
Cdd:COG1160  171 EEDDPIKIAIVGRPNVGKSSLINALLGEE---RviVSDIAGTTRdSIDtPFER-DGKkyTLIDTAG---------IRRK- 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  96 qRALGEYLEKRQSLQGL---------VVLMDIRHPLKDLDQQMIEWAVDSNIAVLVLLTKADKLA--SGARKAQLNMVRE 164
Cdd:COG1160  237 -GKVDEGIEKYSVLRTLraieradvvLLVIDATEGITEQDLKIAGLALEAGKALVIVVNKWDLVEkdRKTREELEKEIRR 315

                        170       180       190
                 ....*....|....*....|....*....|.
gi 119369257 165 AvLAFNGDVQVETFSSLKKQGVDKLRQKLDT 195
Cdd:COG1160  316 R-LPFLDYAPIVFISALTGQGVDKLLEAVDE 345
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 25-193 4.26e-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: 53.27  E-value: 4.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  25 TGIEVAFAGRSNAGKSSALNTLTNQKSlARTSKTPGRT-----QLINLfevaDGK--RLVDLPGYGYAEVPEE---MKRK 94
Cdd:cd04164    2 EGIKVVIAGKPNVGKSSLLNALAGRDR-AIVSDIAGTTrdvieEEIDL----GGIpvRLIDTAGLRETEDEIEkigIERA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  95 WQRAlgeylekRQSlqGLVVLM-DIRHPLKDLDQQMIEWavDSNIAVLVLLTKADKLASGARKAQLNMvrEAVLAfngdv 173
Cdd:cd04164   77 REAI-------EEA--DLVLLVvDASEGLDEEDLEILEL--PAKKPVIVVLNKSDLLSDAEGISELNG--KPIIA----- 138

                        170       180
                 ....*....|....*....|
gi 119369257 174 qvetFSSLKKQGVDKLRQKL 193
Cdd:cd04164  139 ----ISAKTGEGIDELKEAL 154
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 26-205 5.29e-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: 51.99  E-value: 5.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  26 GIEVAFAGRSNAGKSSALNTLTNQKSlARTSKTPGRT-----QLINLfevaDGK--RLVDLPGYGYAEVPEE---MKRKW 95
Cdd:COG0486  213 GIKVVIVGRPNVGKSSLLNALLGEER-AIVTDIAGTTrdvieERINI----GGIpvRLIDTAGLRETEDEVEkigIERAR 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  96 QRAlgeylekRQSlqGLVVLM-DIRHPLKDLDQQMIEWAVDSNiaVLVLLTKADKLASGArkaqlnmvrEAVLAFNGDVQ 174
Cdd:COG0486  288 EAI-------EEA--DLVLLLlDASEPLTEEDEEILEKLKDKP--VIVVLNKIDLPSEAD---------GELKSLPGEPV 347

                        170       180       190
                 ....*....|....*....|....*....|.
gi 119369257 175 VETfSSLKKQGVDKLRQKLDTWFSEMQPVEE 205
Cdd:COG0486  348 IAI-SAKTGEGIDELKEAILELVGEGALEGE 377
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 29-165 2.40e-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: 48.70  E-value: 2.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  29 VAFAGRSNAGKSSALNTLTNQKSLArTSKTPgRTQLINL--FEVADGKRLVDLPGYGyaeVPEEMKRKWQRalgEYLEKr 106
Cdd:cd09912    3 LAVVGEFSAGKSTLLNALLGEEVLP-TGVTP-TTAVITVlrYGLLKGVVLVDTPGLN---STIEHHTEITE---SFLPR- 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257 107 qsLQGLVVLMDIRHPLKDLDQQ-MIEWAVDSNIAVLVLLTKADKLASGARKAQLNMVREA 165
Cdd:cd09912   74 --ADAVIFVLSADQPLTESEREfLKEILKWSGKKIFFVLNKIDLLSEEELEEVLEYSREE 131
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 29-148 2.54e-07

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 50.18  E-value: 2.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  29 VAFAGRSNAGKSSALNTLTNQK-----SLARTSKTPgrtqlINLFEVADGK--RLVDLPGygyaevpeeMKRKWQRALG- 100
Cdd:PRK09518 453 VALVGRPNVGKSSLLNQLTHEEravvnDLAGTTRDP-----VDEIVEIDGEdwLFIDTAG---------IKRRQHKLTGa 518

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119369257 101 EY---LEKRQSLQG---LVVLMDIRHPLKDLDQQMIEWAVDSNIAVLVLLTKAD 148
Cdd:PRK09518 519 EYyssLRTQAAIERselALFLFDASQPISEQDLKVMSMAVDAGRALVLVFNKWD 572
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 29-81 1.53e-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: 46.07  E-value: 1.53e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119369257  29 VAFAGRSNAGKSSALNTLTNQKsLARTSKTPGRT---QLINLfevADGKRLVDLPG 81
Cdd:cd01857   85 IGLVGYPNVGKSSLINALVGSK-KVSVSSTPGKTkhfQTIFL---EPGITLCDCPG 136
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
26-193 1.73e-06

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 47.80  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  26 GIEVAFAGRSNAGKSSALNTLTNQKSlARTSKTPGRT-----QLINLfevaDGK--RLVDLPGygyaevpeemkrkwQRA 98
Cdd:PRK05291 215 GLKVVIAGRPNVGKSSLLNALLGEER-AIVTDIAGTTrdvieEHINL----DGIplRLIDTAG--------------IRE 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  99 LGEYLEK------RQSLQG--LVVLM-DIRHPLKDLDQQmiEWAVDSNIAVLVLLTKADkLASGARKAQLnmvreavlaf 169
Cdd:PRK05291 276 TDDEVEKigiersREAIEEadLVLLVlDASEPLTEEDDE--ILEELKDKPVIVVLNKAD-LTGEIDLEEE---------- 342

                        170       180
                 ....*....|....*....|....
gi 119369257 170 NGDVQVETfSSLKKQGVDKLRQKL 193
Cdd:PRK05291 343 NGKPVIRI-SAKTGEGIDELREAI 365
YeeP COG3596
Predicted GTPase [General function prediction only];
28-150 2.05e-06

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 47.07  E-value: 2.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  28 EVAFAGRSNAGKSSALNTLTNQkSLARTSKTPGRTQLINLFEV----ADGKRLVDLPGYGyaEVPEemKRKWQRALGEYL 103
Cdd:COG3596   41 VIALVGKTGAGKSSLINALFGA-EVAEVGVGRPCTREIQRYRLesdgLPGLVLLDTPGLG--EVNE--RDREYRELRELL 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119369257 104 EKrqsLQGLVVLMDIRHPLKDLD----QQMIEWAVDsnIAVLVLLTKADKL 150
Cdd:COG3596  116 PE---ADLILWVVKADDRALATDeeflQALRAQYPD--PPVLVVLTQVDRL 161
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 31-82 1.23e-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: 44.18  E-value: 1.23e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119369257  31 FAGRSNAGKSSALNTL----------TNQKSLARTSKTPGRTQLINLFEVADGKRLVDLPGY 82
Cdd:cd01855  130 VVGATNVGKSTLINALlksnggkvqaQALVQRLTVSPIPGTTLGLIKIPLGEGKKLYDTPGI 191
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 26-193 1.84e-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: 44.39  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257   26 GIEVAFAGRSNAGKSSALNTLTNQKSlARTSKTPGRT-----QLINLfevaDGK--RLVDLPGYGYAEVPEE---MKRKW 95
Cdd:pfam12631  94 GIKVVIVGKPNVGKSSLLNALLGEER-AIVTDIPGTTrdvieETINI----GGIplRLIDTAGIRETDDEVEkigIERAR 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257   96 QRAlgeylekRQSlqGLVVLM-DIRHPLKDLDQQMIEwAVDSNIAVLVLLTKADklasgarkaqLNMVREAVLAFNGDVQ 174
Cdd:pfam12631 169 EAI-------EEA--DLVLLVlDASRPLDEEDLEILE-LLKDKKPIIVVLNKSD----------LLGEIDELEELKGKPV 228

                         170
                  ....*....|....*....
gi 119369257  175 VETfSSLKKQGVDKLRQKL 193
Cdd:pfam12631 229 LAI-SAKTGEGLDELEEAI 246
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 30-165 5.61e-05

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


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 41.56  E-value: 5.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  30 AFAGRSNAGKSSALNTLTnQKSLARTSKTPGRTQLINLFEVADGKR---LVDLPGYGyaevpeEMKRKWQRALGEYLEKR 106
Cdd:cd11383    1 GLMGKTGAGKSSLCNALF-GTEVAAVGDRRPTTRAAQAYVWQTGGDglvLLDLPGVG------ERGRRDREYEELYRRLL 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119369257 107 QSLQGLVVLMDIRHPLKDLDQQMIE-WAVDSNIAVLVLLTKADKL--ASGARKAQLNMVREA 165
Cdd:cd11383   74 PEADLVLWLLDADDRALAADHDFYLlPLAGHDAPLLFVLNQVDPVlaVSARTGWGLDELAEA 135
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 13-81 7.32e-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: 41.22  E-value: 7.32e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119369257  13 MSAPDIRHLPSDTGIEVAFAGRSNAGKSSALNTLTNQKSLaRTSKTPGRTQLINLFEVADGKRLVDLPG 81
Cdd:cd01849   78 EITKQKLKLKYKKGIRVGVVGLPNVGKSSFINALLNKFKL-KVGSIPGTTKLQQDVKLDKEIYLYDTPG 145
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
 101-177 1.18e-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: 41.35  E-value: 1.18e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119369257 101 EYLEKRQSLQGLVVLMDIRHPLKDLDQQMIEWAVDSNIAV--LVLLTKADKLASgarkAQLNMVREAVLAFNGDVQVET 177
Cdd:cd03112  109 EELESRLRLDGVVTVVDAKNFLKQLDEEDVSDLAVDQIAFadVIVLNKTDLVDE----EELEALRARIRALNPGAKIVE 183
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 36-81 2.50e-04

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


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 40.20  E-value: 2.50e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 119369257  36 NAGKSSALNTLTNQKSlARTSKTPGRTQLINLFEVADGKRLVDLPG 81
Cdd:cd01856  125 NVGKSTLINRLRGKKV-AKVGNKPGVTRGQQWIRIGPNIELLDTPG 169
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 29-81 6.75e-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: 38.84  E-value: 6.75e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119369257  29 VAFAGRSNAGKSSALNTLTNQKSlARTSKTPGR---TQLINLFEVADGKRLVDLPG 81
Cdd:cd01859  102 VGVVGYPKVGKSSIINALKGRHS-ASTSPIPGSpgyTKGIQLVRIDSKIYLIDTPG 156
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 33-159 1.02e-03

EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206681 [Multi-domain]  Cd Length: 157  Bit Score: 38.19  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  33 GRSNAGKSSALNTLTNQKsLARTSKTPG--RTQLINLFEVADGK-RLVDLPGYGYAEVP--EEMKRKWQRALGEylekrq 107
Cdd:cd01894    4 GRPNVGKSTLFNRLTGRR-DAIVSDTPGvtRDRKYGEAEWGGREfILIDTGGIEPDDEGisKEIREQAEIAIEE------ 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119369257 108 slQGLVV-LMDIRHPLKDLDQQMIEWAVDSNIAVLVLLTKADKLASGARKAQL 159
Cdd:cd01894   77 --ADVILfVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNIKEEEEAAEF 127
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 29-148 1.04e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 39.18  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  29 VAFAGRSNAGKSSALNTLTNQK-----SLARTSKTPgRTQLINLfevaDGK--RLVDLPGygyaevpeeMKRKWQRALG- 100
Cdd:PRK03003 214 VALVGKPNVGKSSLLNKLAGEErsvvdDVAGTTVDP-VDSLIEL----GGKtwRFVDTAG---------LRRRVKQASGh 279

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119369257 101 EY---LEKRQSLQG---LVVLMDIRHPLKDLDQQMIEWAVDSNIAVLVLLTKAD 148
Cdd:PRK03003 280 EYyasLRTHAAIEAaevAVVLIDASEPISEQDQRVLSMVIEAGRALVLAFNKWD 333
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
 29-152 1.06e-03

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


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 38.46  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  29 VAFAGRSNAGKSSALNTLTNQK-SLARTSKTPGRTQLINLFEVADGKRLVDLPGYGyaevpeemkrkwqRALGEYLEK-R 106
Cdd:cd04105    3 VLLLGPSDSGKTALFTKLTTGKvRSTVTSIEPNVASFYSNSSKGKKLTLVDVPGHE-------------KLRDKLLEYlK 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119369257 107 QSLQGLVVLMD---IRHPLKDLDQQMIEWAVDSN-----IAVLVLLTKADKLAS 152
Cdd:cd04105   70 ASLKAIVFVVDsatFQKNIRDVAEFLYDILTDLEkiknkIPILIACNKQDLFTA 123
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 133-193 1.31e-03

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


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 38.53  E-value: 1.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119369257 133 AVDSNIAVLVLLTKADKLASGARKAQLNMVREAvlafngDVQVETFSSLKKQGVDKLRQKL 193
Cdd:cd01854   29 AEASGIEPVIVLNKADLVDDEELEELLEIYEKL------GYPVLAVSAKTGEGLDELRELL 83
PRK12289 PRK12289
small ribosomal subunit biogenesis GTPase RsgA;
31-109 2.54e-03

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237040 [Multi-domain]  Cd Length: 352  Bit Score: 38.07  E-value: 2.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257  31 FAGRSNAGKSSALNTLTNQKSLaRTSKTPGR-------TQLINLFEVADGKRLVDLPGYGYAEV---PEEmkrkwqraLG 100
Cdd:PRK12289 177 VAGPSGVGKSSLINRLIPDVEL-RVGKVSGKlgrgrhtTRHVELFELPNGGLLADTPGFNQPDLdcsPRE--------LA 247

                         90
                 ....*....|
gi 119369257 101 EYL-EKRQSL 109
Cdd:PRK12289 248 HYFpEARQRL 257
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
36-81 2.87e-03

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 37.78  E-value: 2.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 119369257  36 NAGKSSALNTLTNQKSlARTSKTPGRT---QLINLfevADGKRLVDLPG 81
Cdd:COG1161  123 NVGKSTLINRLAGKKV-AKTGNKPGVTkgqQWIKL---DDGLELLDTPG 167
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 27-149 7.03e-03

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: 35.81  E-value: 7.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119369257   27 IEVAFAGRSNAGKSSALNTLTnQKSLARTSKTPGRTQ-LINLFEVADGKR----LVDLPGygyaevpEEMKRKWQRALGe 101
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLL-GNKGSITEYYPGTTRnYVTTVIEEDGKTykfnLLDTAG-------QEDYDAIRRLYY- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 119369257  102 ylekRQSLQGLVVLmDIRHPLKDL------DQQMIEWAVDSNIAVLVLLTKADK 149
Cdd:TIGR00231  73 ----PQVERSLRVF-DIVILVLDVeeilekQTKEIIHHADSGVPIILVGNKIDL 121
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 119369257  27 IEVAFAGRSNAGKSSALNTLTNQKsLARTSKTPGRT---QLINLFevadgKR--LVDLPG 81
Cdd:cd01858  103 ISVGFIGYPNVGKSSVINTLRSKK-VCKVAPIPGETkvwQYITLM-----KRiyLIDCPG 156
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 29-81 9.70e-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: 35.60  E-value: 9.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119369257   29 VAFAGRSNAGKSSALNTLTNQKSLA--RTSKTPGR----TQLINLFEVADGKRLVDLPG 81
Cdd:pfam03193 109 TVLAGQSGVGKSTLLNALLPELDLRtgEISEKLGRgrhtTTHVELFPLPGGGLLIDTPG 167
 
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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