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Conserved domains on  [gi|578642210|gb|EUO76904|]
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ribosome biogenesis GTP-binding protein YsxC [Staphylococcus aureus M1404]

Protein Classification

GTP-binding protein( domain architecture ID 10785093)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 1-195 3.23e-97

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: 280.03  E-value: 3.23e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210   1 MKVNpnNIELIISAVKEEQYPETELSEVALSGRSNVGKSTFINSMIGRKNMARTSQQPGKTQTLNFYNIDEQLIFVDVPG 80
Cdd:COG0218    1 MKIK--KAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210  81 YGYAKVSKTQREKFGKMIEEYITKRENLQLVIQLVDLRHDPTQDDILMYNYLKHFDIPTLVICTKEDKIPKGKVQKHIKN 160
Cdd:COG0218   79 YGYAKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKA 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 578642210 161 IKTQLDMDPD-DTIVSYSSIQNNKQQQIWNLIEPYI 195
Cdd:COG0218  159 IKKALGKDPAaPEVILFSSLKKEGIDELRAAIEEWL 194
 
Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 1-195 3.23e-97

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: 280.03  E-value: 3.23e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210   1 MKVNpnNIELIISAVKEEQYPETELSEVALSGRSNVGKSTFINSMIGRKNMARTSQQPGKTQTLNFYNIDEQLIFVDVPG 80
Cdd:COG0218    1 MKIK--KAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210  81 YGYAKVSKTQREKFGKMIEEYITKRENLQLVIQLVDLRHDPTQDDILMYNYLKHFDIPTLVICTKEDKIPKGKVQKHIKN 160
Cdd:COG0218   79 YGYAKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKA 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 578642210 161 IKTQLDMDPD-DTIVSYSSIQNNKQQQIWNLIEPYI 195
Cdd:COG0218  159 IKKALGKDPAaPEVILFSSLKKEGIDELRAAIEEWL 194
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 9-178 1.07e-92

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: 268.19  E-value: 1.07e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210    9 ELIISAVKEEQYPETELSEVALSGRSNVGKSTFINSMIGRKNMARTSQQPGKTQTLNFYNIDEQLIFVDVPGYGYAKVSK 88
Cdd:TIGR03598   2 EFVKSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFEVNDGFRLVDLPGYGYAKVSK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210   89 TQREKFGKMIEEYITKRENLQLVIQLVDLRHDPTQDDILMYNYLKHFDIPTLVICTKEDKIPKGKVQKHIKNIKTQLDMD 168
Cdd:TIGR03598  82 EEKEKWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKALKKD 161

                         170
                  ....*....|.
gi 578642210  169 PDD-TIVSYSS 178
Cdd:TIGR03598 162 ADDpSVQLFSS 172
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 27-195 3.05e-77

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: 228.55  E-value: 3.05e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210  27 EVALSGRSNVGKSTFINSMIGRKNMARTSQQPGKTQTLNFYNIDEQLIFVDVPGYGYAKVSKTQREKFGKMIEEYITKRE 106
Cdd:cd01876    1 EVAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAKVSKEVREKWGKLIEEYLENRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210 107 NLQLVIQLVDLRHDPTQDDILMYNYLKHFDIPTLVICTKEDKIPKGKVQKHIKNIKTQLDM-DPDDTIVSYSSIQNNKQQ 185
Cdd:cd01876   81 NLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLfNILPPVILFSSKKGTGID 160

                        170
                 ....*....|
gi 578642210 186 QIWNLIEPYI 195
Cdd:cd01876  161 ELRALIAEWL 170
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 27-145 1.66e-22

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: 87.29  E-value: 1.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210   27 EVALSGRSNVGKSTFINSMIGRKnmARTSQQPGKTQTLNFYNI---DEQLIFVDVPG-YGYAKVSKTQREKFGKMIEEyi 102
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK--AIVSDYPGTTRDPNEGRLelkGKQIILVDTPGlIEGASEGEGLGRAFLAIIEA-- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 578642210  103 tkrenlQLVIQLVDLRHDPTQDDILMYNYLKHFDIPTLVICTK 145
Cdd:pfam01926  77 ------DLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
PRK04213 PRK04213
GTP-binding protein EngB;
27-174 1.10e-18

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 79.58  E-value: 1.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210  27 EVALSGRSNVGKSTFINSMIGRKnmARTSQQPGKTQTLNFYNIDEqLIFVDVPGYGY-AKVSKTQREKFGKMIEEYI-TK 104
Cdd:PRK04213  11 EIVFVGRSNVGKSTLVRELTGKK--VRVGKRPGVTRKPNHYDWGD-FILTDLPGFGFmSGVPKEVQEKIKDEIVRYIeDN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210 105 RENLQLVIQLVDL--------RHDPTQD---DILMYNYLKHFDIPTLVICTKEDKIPkgKVQKHIKNIKTQLDMDP---- 169
Cdd:PRK04213  88 ADRILAAVLVVDGksfieiieRWEGRGEipiDVEMFDFLRELGIPPIVAVNKMDKIK--NRDEVLDEIAERLGLYPpwrq 165


                 ....*.
gi 578642210 170 -DDTIV 174
Cdd:PRK04213 166 wQDIIA 171
 
Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 1-195 3.23e-97

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: 280.03  E-value: 3.23e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210   1 MKVNpnNIELIISAVKEEQYPETELSEVALSGRSNVGKSTFINSMIGRKNMARTSQQPGKTQTLNFYNIDEQLIFVDVPG 80
Cdd:COG0218    1 MKIK--KAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210  81 YGYAKVSKTQREKFGKMIEEYITKRENLQLVIQLVDLRHDPTQDDILMYNYLKHFDIPTLVICTKEDKIPKGKVQKHIKN 160
Cdd:COG0218   79 YGYAKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKA 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 578642210 161 IKTQLDMDPD-DTIVSYSSIQNNKQQQIWNLIEPYI 195
Cdd:COG0218  159 IKKALGKDPAaPEVILFSSLKKEGIDELRAAIEEWL 194
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 9-178 1.07e-92

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: 268.19  E-value: 1.07e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210    9 ELIISAVKEEQYPETELSEVALSGRSNVGKSTFINSMIGRKNMARTSQQPGKTQTLNFYNIDEQLIFVDVPGYGYAKVSK 88
Cdd:TIGR03598   2 EFVKSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFEVNDGFRLVDLPGYGYAKVSK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210   89 TQREKFGKMIEEYITKRENLQLVIQLVDLRHDPTQDDILMYNYLKHFDIPTLVICTKEDKIPKGKVQKHIKNIKTQLDMD 168
Cdd:TIGR03598  82 EEKEKWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKALKKD 161

                         170
                  ....*....|.
gi 578642210  169 PDD-TIVSYSS 178
Cdd:TIGR03598 162 ADDpSVQLFSS 172
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 27-195 3.05e-77

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: 228.55  E-value: 3.05e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210  27 EVALSGRSNVGKSTFINSMIGRKNMARTSQQPGKTQTLNFYNIDEQLIFVDVPGYGYAKVSKTQREKFGKMIEEYITKRE 106
Cdd:cd01876    1 EVAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAKVSKEVREKWGKLIEEYLENRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210 107 NLQLVIQLVDLRHDPTQDDILMYNYLKHFDIPTLVICTKEDKIPKGKVQKHIKNIKTQLDM-DPDDTIVSYSSIQNNKQQ 185
Cdd:cd01876   81 NLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLfNILPPVILFSSKKGTGID 160

                        170
                 ....*....|
gi 578642210 186 QIWNLIEPYI 195
Cdd:cd01876  161 ELRALIAEWL 170
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 27-145 1.66e-22

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: 87.29  E-value: 1.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210   27 EVALSGRSNVGKSTFINSMIGRKnmARTSQQPGKTQTLNFYNI---DEQLIFVDVPG-YGYAKVSKTQREKFGKMIEEyi 102
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK--AIVSDYPGTTRDPNEGRLelkGKQIILVDTPGlIEGASEGEGLGRAFLAIIEA-- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 578642210  103 tkrenlQLVIQLVDLRHDPTQDDILMYNYLKHFDIPTLVICTK 145
Cdd:pfam01926  77 ------DLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
PRK04213 PRK04213
GTP-binding protein EngB;
27-174 1.10e-18

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 79.58  E-value: 1.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210  27 EVALSGRSNVGKSTFINSMIGRKnmARTSQQPGKTQTLNFYNIDEqLIFVDVPGYGY-AKVSKTQREKFGKMIEEYI-TK 104
Cdd:PRK04213  11 EIVFVGRSNVGKSTLVRELTGKK--VRVGKRPGVTRKPNHYDWGD-FILTDLPGFGFmSGVPKEVQEKIKDEIVRYIeDN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210 105 RENLQLVIQLVDL--------RHDPTQD---DILMYNYLKHFDIPTLVICTKEDKIPkgKVQKHIKNIKTQLDMDP---- 169
Cdd:PRK04213  88 ADRILAAVLVVDGksfieiieRWEGRGEipiDVEMFDFLRELGIPPIVAVNKMDKIK--NRDEVLDEIAERLGLYPpwrq 165


                 ....*.
gi 578642210 170 -DDTIV 174
Cdd:PRK04213 166 wQDIIA 171
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
28-166 1.07e-15

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 73.10  E-value: 1.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210  28 VALSGRSNVGKSTFINSMIGRKnMARTSQQPgktQT-----LNFYNIDE-QLIFVDVPGYgyakvsktQREKfgKMIEEY 101
Cdd:COG1159    6 VAIVGRPNVGKSTLLNALVGQK-VSIVSPKP---QTtrhriRGIVTREDaQIVFVDTPGI--------HKPK--RKLGRR 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210 102 ITK--RENLQ---LVIQLVDLRHDPTQDDILMYNYLKHFDIPTLVICTKEDKIPKGKVQKHIKNIKTQLD 166
Cdd:COG1159   72 MNKaaWSALEdvdVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLVKKEELLPLLAEYSELLD 141
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 28-182 3.21e-15

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: 69.80  E-value: 3.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210  28 VALSGRSNVGKSTFINSMIGRKnMARTSQQPGKT--QTLNFYNIDE-QLIFVDVPGYgyakvsKTQREKFGKMIEEYITK 104
Cdd:cd04163    6 VAIIGRPNVGKSTLLNALVGQK-ISIVSPKPQTTrnRIRGIYTDDDaQIIFVDTPGI------HKPKKKLGERMVKAAWS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210 105 R-ENLQLVIQLVDLRHDPTQDDILMYNYLKHFDIPTLVICTKEDKI-PKGKVQKHIKNIKtqlDMDPDDTIVSYSSIQNN 182
Cdd:cd04163   79 AlKDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLVkDKEDLLPLLEKLK---ELHPFAEIFPISALKGE 155
era PRK00089
GTPase Era; Reviewed
 28-194 2.62e-14

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 69.31  E-value: 2.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210  28 VALSGRSNVGKSTFINSMIGRKnMARTSQQPgktQT-----LNFYNIDE-QLIFVDVPGYgyakvsktQREKfgKMIEEY 101
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQK-ISIVSPKP---QTtrhriRGIVTEDDaQIIFVDTPGI--------HKPK--RALNRA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210 102 ITK--RENLQ---LVIQLVDLRHDPTQDDILMYNYLKHFDIPTLVICTKEDKI-PKGKVQKHIKNIKTQLDMDPddtIVS 175
Cdd:PRK00089  74 MNKaaWSSLKdvdLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVkDKEELLPLLEELSELMDFAE---IVP 150

                        170
                 ....*....|....*....
gi 578642210 176 YSSIQNNKQQQIWNLIEPY 194
Cdd:PRK00089 151 ISALKGDNVDELLDVIAKY 169
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 32-156 8.95e-13

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: 63.24  E-value: 8.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210  32 GRSNVGKSTFINSMIGrKNMARTSQQPGKTQTLNFYNI-----DEQLIFVDVPGYgyakvsktqrEKFGKMIEEYITKR- 105
Cdd:cd00882    4 GRGGVGKSSLLNALLG-GEVGEVSDVPGTTRDPDVYVKeldkgKVKLVLVDTPGL----------DEFGGLGREELARLl 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578642210 106 -ENLQLVIQLVDLRHDPTQDDILMY--NYLKHFDIPTLVICTKEDKIPKGKVQK 156
Cdd:cd00882   73 lRGADLILLVVDSTDRESEEDAKLLilRRLRKEGIPIILVGNKIDLLEEREVEE 126
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
 28-196 1.07e-10

GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other bacteria. It plays a role in ribosome biogenesis. Few bacteria lack this protein. [Protein synthesis, Other]


Pssm-ID: 129528 [Multi-domain]  Cd Length: 270  Bit Score: 58.94  E-value: 1.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210   28 VALSGRSNVGKSTFINSMIGRKNmARTSQQPGKTQ---TLNFYNIDEQLIFVDVPGYgyakvSKTQREKFGKMIEEYITK 104
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHGQKI-SITSPKAQTTRnriSGIHTTGASQIIFIDTPGF-----HEKKHSLNRLMMKEARSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210  105 RENLQLVIQLVDLRHDPtQDDILMYNYLKHFDIPTLVICTKEDKIPKGKVQKHIKNIKTQLDMDPddtIVSYSSIQNNKQ 184
Cdd:TIGR00436  77 IGGVDLILFVVDSDQWN-GDGEFVLTKLQNLKRPVVLTRNKLDNKFKDKLLPLIDKYAILEDFKD---IVPISALTGDNT 152

                         170
                  ....*....|..
gi 578642210  185 QQIWNLIEPYIS 196
Cdd:TIGR00436 153 SFLAAFIEVHLP 164
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 29-192 1.35e-10

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: 57.26  E-value: 1.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210  29 ALSGRSNVGKSTFINSMIGrKNMARTSQQPGKTQTLNFYNI----DEQLIFVDVPGYGYAKVSKTQREkfgkmiEEYITK 104
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLG-QNVGIVSPIPGTTRDPVRKEWellpLGPVVLIDTPGLDEEGGLGRERV------EEARQV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210 105 RENLQLVIQLVDLRHDPTqDDILMYNYLKHFDIPTLVICTKEDKIPKGKVQKHIKNIKTQLdmDPDDTIVSYSSiqnNKQ 184
Cdd:cd00880   74 ADRADLVLLVVDSDLTPV-EEEAKLGLLRERGKPVLLVLNKIDLVPESEEEELLRERKLEL--LPDLPVIAVSA---LPG 147


                 ....*...
gi 578642210 185 QQIWNLIE 192
Cdd:cd00880  148 EGIDELRK 155
YeeP COG3596
Predicted GTPase [General function prediction only];
1-164 1.23e-09

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 56.31  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210   1 MKVNPNNIELIISAVK----------EEQYPETELS----EVALSGRSNVGKSTFINSMIGRkNMARTSQQPGKTQTLNF 66
Cdd:COG3596    1 MSTEVSSLTERLEALKrlpqvlrellAEALERLLVElpppVIALVGKTGAGKSSLINALFGA-EVAEVGVGRPCTREIQR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210  67 Y----NIDEQLIFVDVPGYGyakvSKTQREKFGKMIEEYItkrENLQLVIQLVDlRHDPTQD-DILMYNYLK--HFDIPT 139
Cdd:COG3596   80 YrlesDGLPGLVLLDTPGLG----EVNERDREYRELRELL---PEADLILWVVK-ADDRALAtDEEFLQALRaqYPDPPV 151

                        170       180
                 ....*....|....*....|....*
gi 578642210 140 LVICTKEDKIPKGKVQKHIKNIKTQ 164
Cdd:COG3596  152 LVVLTQVDRLEPEREWDPPYNWPSP 176
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
35-80 6.67e-09

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 53.96  E-value: 6.67e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 578642210  35 NVGKSTFINSMIGRKnMARTSQQPGKTQTLNFYNIDEQLIFVDVPG 80
Cdd:COG1161  123 NVGKSTLINRLAGKK-VAKTGNKPGVTKGQQWIKLDDGLELLDTPG 167
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 28-80 1.08e-08

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: 51.46  E-value: 1.08e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578642210  28 VALSGRSNVGKSTFINSMIGRKnMARTSQQPGKTQTLNFYNIDEQLIFVDVPG 80
Cdd:cd01857   85 IGLVGYPNVGKSSLINALVGSK-KVSVSSTPGKTKHFQTIFLEPGITLCDCPG 136
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 2-80 1.46e-08

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: 51.76  E-value: 1.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210   2 KVNPNNIELIISAVKEEQYPETELSEVALSGRS---------NVGKSTFINSMIGRKNmARTSQQPGKTQTLNFYNIDEQ 72
Cdd:cd01856   83 AKNGKGVKKLLKKAKKLLKENEKLKAKGLLPRPlramvvgipNVGKSTLINRLRGKKV-AKVGNKPGVTRGQQWIRIGPN 161


                 ....*...
gi 578642210  73 LIFVDVPG 80
Cdd:cd01856  162 IELLDTPG 169
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 29-151 2.22e-08

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: 51.28  E-value: 2.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210  29 ALSGRSNVGKSTFINSMIGRKNmARTSQQPGKTQTLNFYNI---DEQLIFVDVPGYgyakvsktqrEKFGKMIEEYITKR 105
Cdd:cd01894    1 AIVGRPNVGKSTLFNRLTGRRD-AIVSDTPGVTRDRKYGEAewgGREFILIDTGGI----------EPDDEGISKEIREQ 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578642210 106 -----ENLQLVIQLVDLRHDPTQDDILMYNYLKHFDIPTLVICTKEDKIPK 151
Cdd:cd01894   70 aeiaiEEADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNIKE 120
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
 35-80 6.50e-07

ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding proteins involved in ribosome biogenesis, including the essential YlqF protein of Bacillus subtilis, which is an essential protein. They are related to Era, EngA, and other GTPases of ribosome biogenesis, but are circularly permuted. This family is not universal, and is not present in Escherichia coli, and so is not as well studied as some other GTPases. This model is built for bacterial members. [Protein synthesis, Other]


Pssm-ID: 274669 [Multi-domain]  Cd Length: 276  Bit Score: 48.27  E-value: 6.50e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578642210   35 NVGKSTFINSMIGRKNmARTSQQPGKTQTLNFYNIDEQLIFVDVPG 80
Cdd:TIGR03596 128 NVGKSTLINRLAGKKV-AKVGNRPGVTKGQQWIKLSDNLELLDTPG 172
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 21-80 9.45e-07

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


Pssm-ID: 206752 [Multi-domain]  Cd Length: 157  Bit Score: 46.54  E-value: 9.45e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578642210  21 PETELSEVALSGRSNVGKSTFINSMIGRKNmARTSQQPGK---TQTLNFYNIDEQLIFVDVPG 80
Cdd:cd01859   95 IDGKPVIVGVVGYPKVGKSSIINALKGRHS-ASTSPIPGSpgyTKGIQLVRIDSKIYLIDTPG 156
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 6-81 1.23e-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: 46.87  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210   6 NNIELIISAVKEEQYPETElseVALSGRSNVGKSTFINSMIGR----------KNMARTSQQPGKTQTLNFYNIDEQLIF 75
Cdd:cd01855  109 WGVEELIEEIKKLAKYRGD---VYVVGATNVGKSTLINALLKSnggkvqaqalVQRLTVSPIPGTTLGLIKIPLGEGKKL 185


                 ....*.
gi 578642210  76 VDVPGY 81
Cdd:cd01855  186 YDTPGI 191
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 28-165 2.14e-06

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: 45.89  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210  28 VALSGRSNVGKSTFINSMIGRKNMArTSQQPGKTQ----TLNFYNiDEQLIFVDVPGygyakVSKtqREKFGKMIEEYIT 103
Cdd:cd01895    5 IAIIGRPNVGKSSLLNALLGEERVI-VSDIAGTTRdsidVPFEYD-GQKYTLIDTAG-----IRK--KGKVTEGIEKYSV 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578642210 104 KR-----ENLQLVIQLVDLRHDPTQDDILMYNYLKHFDIPTLVICTKEDKIPKGKVQ--KHIKNIKTQL 165
Cdd:cd01895   76 LRtlkaiERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVEKDEKTmkEFEKELRRKL 144
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
8-47 2.68e-05

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 43.86  E-value: 2.68e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 578642210   8 IELIISAVKEEQYPETELSE--VALSGRSNVGKSTFINSMIG 47
Cdd:COG1160  156 LDAVLELLPEEEEEEEEDDPikIAIVGRPNVGKSSLINALLG 197
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
28-149 3.11e-05

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 43.47  E-value: 3.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210  28 VALSGRSNVGKSTFINSMIGRKnMARTSQQPGKTQTLNFYNI---DEQLIFVDVPGYGYAK---VSKTQREKFGKMIEEy 101
Cdd:COG1160    5 VAIVGRPNVGKSTLFNRLTGRR-DAIVDDTPGVTRDRIYGEAewgGREFTLIDTGGIEPDDddgLEAEIREQAELAIEE- 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 578642210 102 itkrenLQLVIQLVDLRHDPTQDDILMYNYLKHFDIPTLVICTKEDKI 149
Cdd:COG1160   83 ------ADVILFVVDGRAGLTPLDEEIAKLLRRSGKPVILVVNKVDGP 124
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 8-61 4.51e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 43.11  E-value: 4.51e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 578642210   8 IELIISAVKEEQYPETELSE--VALSGRSNVGKSTFINSMIGRKnmaR--TSQQPGKT 61
Cdd:PRK00093 154 LDAILEELPEEEEEDEEDEPikIAIIGRPNVGKSSLINALLGEE---RviVSDIAGTT 208
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 28-149 5.28e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 42.73  E-value: 5.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210  28 VALSGRSNVGKSTFINSMIGRKNmARTSQQPGKTQTLNFYNI---DEQLIFVDVPGYGYAK--VSKTQREKFGKMIEEyi 102
Cdd:PRK00093   4 VAIVGRPNVGKSTLFNRLTGKRD-AIVADTPGVTRDRIYGEAewlGREFILIDTGGIEPDDdgFEKQIREQAELAIEE-- 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 578642210 103 tkrenLQLVIQLVDLRHDPTQDDILMYNYLKHFDIPTLVICTKEDKI 149
Cdd:PRK00093  81 -----ADVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDGP 122
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 28-149 9.21e-05

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: 41.20  E-value: 9.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210   28 VALSGRSNVGKSTFINSMIGRKnMARTSQQPGKTQTLNFYNIDE-----QLIFVDVPGygyakvsktqREKFGKMIEEYI 102
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNK-GSITEYYPGTTRNYVTTVIEEdgktyKFNLLDTAG----------QEDYDAIRRLYY 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578642210  103 TKREN----LQLVIQLVDLRHDPTQDDILMYNYLKHfDIPTLVICTKEDKI 149
Cdd:TIGR00231  73 PQVERslrvFDIVILVLDVEEILEKQTKEIIHHADS-GVPIILVGNKIDLK 122
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 17-147 6.51e-04

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 39.78  E-value: 6.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210  17 EEQYPETELSEVALSGRSNVGKSTFINSMIGRKNmARTSQQPGKTQT----------LNFYNIDEQLIFVDVPGYGYAKV 86
Cdd:PRK09518 267 DEKAGPKAVGVVAIVGRPNVGKSTLVNRILGRRE-AVVEDTPGVTRDrvsydaewagTDFKLVDTGGWEADVEGIDSAIA 345

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578642210  87 SKTQrekfgkmieeyiTKRENLQLVIQLVDLRHDPTQDDILMYNYLKHFDIPTLVICTKED 147
Cdd:PRK09518 346 SQAQ------------IAVSLADAVVFVVDGQVGLTSTDERIVRMLRRAGKPVVLAVNKID 394
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 28-119 6.69e-04

Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (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: 460552 [Multi-domain]  Cd Length: 156  Bit Score: 38.59  E-value: 6.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210   28 VALSGRSNVGKSTFINSMIGRKnmARTSQQPGKT---QTLNFYNIDEQLIFVDVPGYgYAKVSKTQREKFGKmieEYITK 104
Cdd:pfam02421   3 IALVGNPNVGKTTLFNALTGAN--QHVGNWPGVTvekKEGKFKYKGYEIEIVDLPGI-YSLSPYSEEERVAR---DYLLN 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 578642210  105 RE---------------NLQLVIQLVDLRH 119
Cdd:pfam02421  77 EKpdvivnvvdatnlerNLYLTLQLLELGL 106
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
 6-82 1.38e-03

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


Pssm-ID: 461536 [Multi-domain]  Cd Length: 375  Bit Score: 38.62  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210    6 NNIELIISAVKEE-QYPETELSEVALSGRSNVGKSTFINSM--IGRKNMA-------RTSQQPGKTQTLNFYNIdeqlIF 75
Cdd:pfam05049  15 GNLQKVVSIIKKAiQEISSAPLKIAVTGDSGNGKSSFINALrgIGHEEDGsaptgvvETTMKRTPYSHPHFPNV----VL 90


                  ....*..
gi 578642210   76 VDVPGYG 82
Cdd:pfam05049  91 WDLPGLG 97
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
 28-81 1.92e-03

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


Pssm-ID: 206753 [Multi-domain]  Cd Length: 171  Bit Score: 37.55  E-value: 1.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578642210  28 VALSGRSNVGKSTFINSMIgRKNMARTSQQPGKTQTLNFYNIDEQLIFVDVPGY 81
Cdd:cd04178  119 VGVVGYPNVGKSSVINSLK-RSRACNVGATPGVTKSMQEVHLDKHVKLLDSPGV 171
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 28-49 2.03e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 38.03  E-value: 2.03e-03
                         10        20
                 ....*....|....*....|..
gi 578642210  28 VALSGRSNVGKSTFINSMIGRK 49
Cdd:PRK03003  41 VAVVGRPNVGKSTLVNRILGRR 62
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 28-80 2.51e-03

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: 37.14  E-value: 2.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578642210  28 VALSGRSNVGKSTFINSMIGRKNMArTSQQP--GKTqTLNFYNIDEQLIFVDVPG 80
Cdd:cd09912    3 LAVVGEFSAGKSTLLNALLGEEVLP-TGVTPttAVI-TVLRYGLLKGVVLVDTPG 55
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 28-151 3.06e-03

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: 36.70  E-value: 3.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578642210  28 VALSGRSNVGKSTFINSMIGRkNMARTSQQPGKT-----QTLNFYNIDeqLIFVDVPGYgyaKVSKTQREKFGkmIEEYI 102
Cdd:cd04164    6 VVIAGKPNVGKSSLLNALAGR-DRAIVSDIAGTTrdvieEEIDLGGIP--VRLIDTAGL---RETEDEIEKIG--IERAR 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 578642210 103 TKRENLQLVIQLVDLRHDPTQDDILMYNYLKhfDIPTLVICTKEDKIPK 151
Cdd:cd04164   78 EAIEEADLVLLVVDASEGLDEEDLEILELPA--KKPVIVVLNKSDLLSD 124
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 28-80 9.88e-03

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: 35.05  E-value: 9.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578642210  28 VALSGRSNVGKSTFINSmIGRKNMARTSQQPGKTQTLNFYNIDEQLIFVDVPG 80
Cdd:cd01849   94 VGVVGLPNVGKSSFINA-LLNKFKLKVGSIPGTTKLQQDVKLDKEIYLYDTPG 145
 
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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