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Conserved domains on  [gi|226842026|gb|ACO84692|]
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ribosome biogenesis GTP-binding protein YsxC [Clostridium botulinum A2 str. Kyoto]

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, ...
 3-192 1.87e-111

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: 315.86  E-value: 1.87e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026   3 MEIKKAEFVISAVKKTQYPEDGRPEVAFVGRSNVGKSTLINTLTNRRKLVKVSSTPGKTRLINFFVINDNMYFVDLPGYG 82
Cdd:COG0218    1 MKIKKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  83 YAKVSKKEKENWGYIMEQYLVERDQLKKIVLLVDSRHKPTSDDINMYNWIKHYNYEVLVVGTKLDKLKRNDINKNKKIIR 162
Cdd:COG0218   81 YAKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIK 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 226842026 163 DTLKMDKD-DKILLISSLSKEGKEEVLEQIL 192
Cdd:COG0218  161 KALGKDPAaPEVILFSSLKKEGIDELRAAIE 191
 
Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 3-192 1.87e-111

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: 315.86  E-value: 1.87e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026   3 MEIKKAEFVISAVKKTQYPEDGRPEVAFVGRSNVGKSTLINTLTNRRKLVKVSSTPGKTRLINFFVINDNMYFVDLPGYG 82
Cdd:COG0218    1 MKIKKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  83 YAKVSKKEKENWGYIMEQYLVERDQLKKIVLLVDSRHKPTSDDINMYNWIKHYNYEVLVVGTKLDKLKRNDINKNKKIIR 162
Cdd:COG0218   81 YAKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIK 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 226842026 163 DTLKMDKD-DKILLISSLSKEGKEEVLEQIL 192
Cdd:COG0218  161 KALGKDPAaPEVILFSSLKKEGIDELRAAIE 191
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 8-185 3.87e-106

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: 302.09  E-value: 3.87e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026    8 AEFVISAVKKTQYPEDGRPEVAFVGRSNVGKSTLINTLTNRRKLVKVSSTPGKTRLINFFVINDNMYFVDLPGYGYAKVS 87
Cdd:TIGR03598   1 AEFVKSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFEVNDGFRLVDLPGYGYAKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026   88 KKEKENWGYIMEQYLVERDQLKKIVLLVDSRHKPTSDDINMYNWIKHYNYEVLVVGTKLDKLKRNDINKNKKIIRDTLKM 167
Cdd:TIGR03598  81 KEEKEKWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKALKK 160

                         170
                  ....*....|....*....
gi 226842026  168 DKDD-KILLISSLSKEGKE 185
Cdd:TIGR03598 161 DADDpSVQLFSSLKKTGID 179
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 27-192 9.68e-84

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: 245.11  E-value: 9.68e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  27 EVAFVGRSNVGKSTLINTLTNRRKLVKVSSTPGKTRLINFFVINDNMYFVDLPGYGYAKVSKKEKENWGYIMEQYLVERD 106
Cdd:cd01876    1 EVAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAKVSKEVREKWGKLIEEYLENRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026 107 QLKKIVLLVDSRHKPTSDDINMYNWIKHYNYEVLVVGTKLDKLKRNDINKNKKIIRDTLKMDK-DDKILLISSLSKEGKE 185
Cdd:cd01876   81 NLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLFNiLPPVILFSSKKGTGID 160


                 ....*..
gi 226842026 186 EVLEQIL 192
Cdd:cd01876  161 ELRALIA 167
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 27-145 4.10e-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: 91.53  E-value: 4.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026   27 EVAFVGRSNVGKSTLINTLTNRRklVKVSSTPGKTRLINFFVINDN---MYFVDLPGygyakVSKKEKENWGyIMEQYLV 103
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK--AIVSDYPGTTRDPNEGRLELKgkqIILVDTPG-----LIEGASEGEG-LGRAFLA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 226842026  104 ERDQlKKIVLLVDSRHKPTSDDINMYNWIKHYNYEVLVVGTK 145
Cdd:pfam01926  73 IIEA-DLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
PRK04213 PRK04213
GTP-binding protein EngB;
17-167 4.23e-17

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 75.34  E-value: 4.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  17 KTQYPEDGRPEVAFVGRSNVGKSTLINTLTNRRklVKVSSTPGKTRLINFFVINDNMyFVDLPGYGY-AKVSKKEKENWG 95
Cdd:PRK04213   1 MFETRPDRKPEIVFVGRSNVGKSTLVRELTGKK--VRVGKRPGVTRKPNHYDWGDFI-LTDLPGFGFmSGVPKEVQEKIK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  96 YIMEQYLVER-DQLKKIVLLVDS--------RHKPTSD---DINMYNWIKHYNYEVLVVGTKLDKLKRNDINKNKkiIRD 163
Cdd:PRK04213  78 DEIVRYIEDNaDRILAAVLVVDGksfieiieRWEGRGEipiDVEMFDFLRELGIPPIVAVNKMDKIKNRDEVLDE--IAE 155


                 ....
gi 226842026 164 TLKM 167
Cdd:PRK04213 156 RLGL 159
 
Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 3-192 1.87e-111

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: 315.86  E-value: 1.87e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026   3 MEIKKAEFVISAVKKTQYPEDGRPEVAFVGRSNVGKSTLINTLTNRRKLVKVSSTPGKTRLINFFVINDNMYFVDLPGYG 82
Cdd:COG0218    1 MKIKKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  83 YAKVSKKEKENWGYIMEQYLVERDQLKKIVLLVDSRHKPTSDDINMYNWIKHYNYEVLVVGTKLDKLKRNDINKNKKIIR 162
Cdd:COG0218   81 YAKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIK 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 226842026 163 DTLKMDKD-DKILLISSLSKEGKEEVLEQIL 192
Cdd:COG0218  161 KALGKDPAaPEVILFSSLKKEGIDELRAAIE 191
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 8-185 3.87e-106

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: 302.09  E-value: 3.87e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026    8 AEFVISAVKKTQYPEDGRPEVAFVGRSNVGKSTLINTLTNRRKLVKVSSTPGKTRLINFFVINDNMYFVDLPGYGYAKVS 87
Cdd:TIGR03598   1 AEFVKSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFEVNDGFRLVDLPGYGYAKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026   88 KKEKENWGYIMEQYLVERDQLKKIVLLVDSRHKPTSDDINMYNWIKHYNYEVLVVGTKLDKLKRNDINKNKKIIRDTLKM 167
Cdd:TIGR03598  81 KEEKEKWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKALKK 160

                         170
                  ....*....|....*....
gi 226842026  168 DKDD-KILLISSLSKEGKE 185
Cdd:TIGR03598 161 DADDpSVQLFSSLKKTGID 179
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 27-192 9.68e-84

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: 245.11  E-value: 9.68e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  27 EVAFVGRSNVGKSTLINTLTNRRKLVKVSSTPGKTRLINFFVINDNMYFVDLPGYGYAKVSKKEKENWGYIMEQYLVERD 106
Cdd:cd01876    1 EVAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAKVSKEVREKWGKLIEEYLENRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026 107 QLKKIVLLVDSRHKPTSDDINMYNWIKHYNYEVLVVGTKLDKLKRNDINKNKKIIRDTLKMDK-DDKILLISSLSKEGKE 185
Cdd:cd01876   81 NLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLFNiLPPVILFSSKKGTGID 160


                 ....*..
gi 226842026 186 EVLEQIL 192
Cdd:cd01876  161 ELRALIA 167
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 27-145 4.10e-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: 91.53  E-value: 4.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026   27 EVAFVGRSNVGKSTLINTLTNRRklVKVSSTPGKTRLINFFVINDN---MYFVDLPGygyakVSKKEKENWGyIMEQYLV 103
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK--AIVSDYPGTTRDPNEGRLELKgkqIILVDTPG-----LIEGASEGEG-LGRAFLA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 226842026  104 ERDQlKKIVLLVDSRHKPTSDDINMYNWIKHYNYEVLVVGTK 145
Cdd:pfam01926  73 IIEA-DLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 28-192 8.53e-19

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: 79.04  E-value: 8.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  28 VAFVGRSNVGKSTLINTLTNrRKLVKVSSTPGKTRLINFFVINDNMY---FVDLPGYgyakVSKKEKenwgyiMEQYLVE 104
Cdd:cd04163    6 VAIIGRPNVGKSTLLNALVG-QKISIVSPKPQTTRNRIRGIYTDDDAqiiFVDTPGI----HKPKKK------LGERMVK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026 105 --RDQLKK---IVLLVDSRHKPTSDDINMYNWIKHYNYEVLVVGTKLDKLKRNDinKNKKIIRDTLKMDKDDKILLISSL 179
Cdd:cd04163   75 aaWSALKDvdlVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLVKDKE--DLLPLLEKLKELHPFAEIFPISAL 152

                        170
                 ....*....|...
gi 226842026 180 SKEGKEEVLEQIL 192
Cdd:cd04163  153 KGENVDELLEYIV 165
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 29-192 1.99e-17

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: 75.57  E-value: 1.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  29 AFVGRSNVGKSTLINTLTNrRKLVKVSSTPGKTRLINFFVI-----NDNMYFVDLPGYGYAKVSKKEKENWGYImeqylv 103
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLG-GEVGEVSDVPGTTRDPDVYVKeldkgKVKLVLVDTPGLDEFGGLGREELARLLL------ 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026 104 erDQLKKIVLLVDSRHKPTSDDINMY--NWIKHYNYEVLVVGTKLDKLKRNDINKNKKIIRdtLKMDKDDKILLISSLSK 181
Cdd:cd00882   74 --RGADLILLVVDSTDRESEEDAKLLilRRLRKEGIPIILVGNKIDLLEEREVEELLRLEE--LAKILGVPVFEVSAKTG 149

                        170
                 ....*....|.
gi 226842026 182 EGKEEVLEQIL 192
Cdd:cd00882  150 EGVDELFEKLI 160
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 29-192 4.11e-17

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: 74.59  E-value: 4.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  29 AFVGRSNVGKSTLINTLTNrRKLVKVSSTPGKTRLINFFVI----NDNMYFVDLPGYGYAKVSKKEKEnwgyimEQYLVE 104
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLG-QNVGIVSPIPGTTRDPVRKEWellpLGPVVLIDTPGLDEEGGLGRERV------EEARQV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026 105 RDQLKKIVLLVDSRHKPTSDDiNMYNWIKHYNYEVLVVGTKLDKLKRNDinKNKKIIRDTLKMDKDDKILLISSLSKEGK 184
Cdd:cd00880   74 ADRADLVLLVVDSDLTPVEEE-AKLGLLRERGKPVLLVLNKIDLVPESE--EEELLRERKLELLPDLPVIAVSALPGEGI 150


                 ....*...
gi 226842026 185 EEVLEQIL 192
Cdd:cd00880  151 DELRKKIA 158
PRK04213 PRK04213
GTP-binding protein EngB;
17-167 4.23e-17

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 75.34  E-value: 4.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  17 KTQYPEDGRPEVAFVGRSNVGKSTLINTLTNRRklVKVSSTPGKTRLINFFVINDNMyFVDLPGYGY-AKVSKKEKENWG 95
Cdd:PRK04213   1 MFETRPDRKPEIVFVGRSNVGKSTLVRELTGKK--VRVGKRPGVTRKPNHYDWGDFI-LTDLPGFGFmSGVPKEVQEKIK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  96 YIMEQYLVER-DQLKKIVLLVDS--------RHKPTSD---DINMYNWIKHYNYEVLVVGTKLDKLKRNDINKNKkiIRD 163
Cdd:PRK04213  78 DEIVRYIEDNaDRILAAVLVVDGksfieiieRWEGRGEipiDVEMFDFLRELGIPPIVAVNKMDKIKNRDEVLDE--IAE 155


                 ....
gi 226842026 164 TLKM 167
Cdd:PRK04213 156 RLGL 159
era PRK00089
GTPase Era; Reviewed
 28-194 2.99e-16

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 74.70  E-value: 2.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  28 VAFVGRSNVGKSTLINTLTNrRKLVKVSSTPGKTR-LINFFVINDN--MYFVDLPGygyakVSKKEKEnwgyiMEQYLVE 104
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVG-QKISIVSPKPQTTRhRIRGIVTEDDaqIIFVDTPG-----IHKPKRA-----LNRAMNK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026 105 --RDQLKK---IVLLVDSRHKPTSDDINMYNWIKHYNYEVLVVGTKLDKLKRNDinKNKKIIRDTLKMDKDDKILLISSL 179
Cdd:PRK00089  77 aaWSSLKDvdlVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVKDKE--ELLPLLEELSELMDFAEIVPISAL 154

                        170
                 ....*....|....*
gi 226842026 180 SKEGKEEVLEQILVY 194
Cdd:PRK00089 155 KGDNVDELLDVIAKY 169
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
28-192 4.01e-15

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 71.56  E-value: 4.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  28 VAFVGRSNVGKSTLINTLTNrRKLVKVSSTPGKTR-LINFFVINDN--MYFVDLPGYgyakvsKKEKenwgYIMEQYLVE 104
Cdd:COG1159    6 VAIVGRPNVGKSTLLNALVG-QKVSIVSPKPQTTRhRIRGIVTREDaqIVFVDTPGI------HKPK----RKLGRRMNK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026 105 --RDQLKK---IVLLVDSRHKPTSDDINMYNWIKHYNYEVLVVGTKLDKLKRNDINKNKKIIRDtlKMDKDDkILLISSL 179
Cdd:COG1159   75 aaWSALEDvdvILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLVKKEELLPLLAEYSE--LLDFAE-IVPISAL 151

                        170
                 ....*....|...
gi 226842026 180 SKEGKEEVLEQIL 192
Cdd:COG1159  152 KGDNVDELLDEIA 164
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 28-192 1.97e-14

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: 67.84  E-value: 1.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  28 VAFVGRSNVGKSTLINTLTNRRKLVkVSSTPGKTR--LINFFVIND-NMYFVDLPGygyakVSKKEKENWGyiMEQYLVE 104
Cdd:cd01895    5 IAIIGRPNVGKSSLLNALLGEERVI-VSDIAGTTRdsIDVPFEYDGqKYTLIDTAG-----IRKKGKVTEG--IEKYSVL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026 105 RDQ--LKK---IVLLVDSRHKPTSDDINMYNWIKHYNYEVLVVGTKLDKL--KRNDINKNKKIIRDTLKMDKDDKILLIS 177
Cdd:cd01895   77 RTLkaIERadvVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVekDEKTMKEFEKELRRKLPFLDYAPIVFIS 156

                        170
                 ....*....|....*
gi 226842026 178 SLSKEGKEEVLEQIL 192
Cdd:cd01895  157 ALTGQGVDKLFDAIK 171
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 29-151 5.42e-13

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: 63.61  E-value: 5.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  29 AFVGRSNVGKSTLINTLTNRRKLVkVSSTPGKTRLINFFVIN-DNMYF--VDLPGYgyakvSKKEKENWGYIMEQYLVER 105
Cdd:cd01894    1 AIVGRPNVGKSTLFNRLTGRRDAI-VSDTPGVTRDRKYGEAEwGGREFilIDTGGI-----EPDDEGISKEIREQAEIAI 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 226842026 106 DQLKKIVLLVDSRHKPTSDDINMYNWIKHYNYEVLVVGTKLDKLKR 151
Cdd:cd01894   75 EEADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNIKE 120
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 21-192 1.40e-11

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 61.99  E-value: 1.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  21 PEDGRPEVAFVGRSNVGKSTLINTLTNRRKLVkVSSTPGKTR-LIN-FFVINDNMY-FVDLPGygyakVSKKEK--ENwg 95
Cdd:PRK00093 169 EEDEPIKIAIIGRPNVGKSSLINALLGEERVI-VSDIAGTTRdSIDtPFERDGQKYtLIDTAG-----IRRKGKvtEG-- 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  96 yiMEQYLVERdQLKKI------VLLVDSRHKPTSDDINmynwIKHYNYE----VLVVGTKLDKLKRNDINKNKKIIRDTL 165
Cdd:PRK00093 241 --VEKYSVIR-TLKAIeradvvLLVIDATEGITEQDLR----IAGLALEagraLVIVVNKWDLVDEKTMEEFKKELRRRL 313

                        170       180
                 ....*....|....*....|....*..
gi 226842026 166 KMDKDDKILLISSLSKEGKEEVLEQIL 192
Cdd:PRK00093 314 PFLDYAPIVFISALTGQGVDKLLEAID 340
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 28-80 2.60e-11

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: 58.78  E-value: 2.60e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 226842026  28 VAFVGRSNVGKSTLINTLTNRrKLVKVSSTPGKTRLINFFVINDNMYFVDLPG 80
Cdd:cd01857   85 IGLVGYPNVGKSSLINALVGS-KKVSVSSTPGKTKHFQTIFLEPGITLCDCPG 136
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 28-80 5.90e-11

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: 58.31  E-value: 5.90e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 226842026  28 VAFVGRSNVGKSTLINTLTNrRKLVKVSSTPGKTRLINFFVINDNMYFVDLPG 80
Cdd:cd01856  118 AMVVGIPNVGKSTLINRLRG-KKVAKVGNKPGVTRGQQWIRIGPNIELLDTPG 169
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 27-192 1.47e-10

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: 59.30  E-value: 1.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  27 EVAFVGRSNVGKSTLINTLTNR-RKLvkVSSTPGKTR-----LINFfvinDNMYFV-----------DlpgygyaKVskk 89
Cdd:COG0486  215 KVVIVGRPNVGKSSLLNALLGEeRAI--VTDIAGTTRdvieeRINI----GGIPVRlidtaglreteD-------EV--- 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  90 EKEnwGyimeqylVER--DQLKK---IVLLVDSRHKPTSDDINMYNWIKHYNyeVLVVGTKLDKLKRNDINknkkiirdt 164
Cdd:COG0486  279 EKI--G-------IERarEAIEEadlVLLLLDASEPLTEEDEEILEKLKDKP--VIVVLNKIDLPSEADGE--------- 338

                        170       180
                 ....*....|....*....|....*...
gi 226842026 165 LKMDKDDKILLISSLSKEGKEEVLEQIL 192
Cdd:COG0486  339 LKSLPGEPVIAISAKTGEGIDELKEAIL 366
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 26-153 3.48e-10

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 58.14  E-value: 3.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  26 PEVAFVGRSNVGKSTLINTLTNRRKLVkVSSTPGKTRlinffvinDNMyfvdlpgYGYAKVSKKE------------KEN 93
Cdd:PRK00093   2 PVVAIVGRPNVGKSTLFNRLTGKRDAI-VADTPGVTR--------DRI-------YGEAEWLGREfilidtggiepdDDG 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226842026  94 W-GYIMEQYLVERDQLKKIVLLVDSRHKPTSDDINMYNWIKHYNYEVLVVGTKLDKLKRND 153
Cdd:PRK00093  66 FeKQIREQAELAIEEADVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDGPDEEA 126
YeeP COG3596
Predicted GTPase [General function prediction only];
22-149 4.71e-10

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 57.47  E-value: 4.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  22 EDGRPEVAFVGRSNVGKSTLINTLTnRRKLVKVSSTPGKTRLINFFVIN----DNMYFVDLPGYGyaKVSKKEKENWGYi 97
Cdd:COG3596   36 ELPPPVIALVGKTGAGKSSLINALF-GAEVAEVGVGRPCTREIQRYRLEsdglPGLVLLDTPGLG--EVNERDREYREL- 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 226842026  98 mEQYLVERDqlkkIVLLVDSRHKPTSD-DINMYNWIKHYNYE--VLVVGTKLDKL 149
Cdd:COG3596  112 -RELLPEAD----LILWVVKADDRALAtDEEFLQALRAQYPDppVLVVLTQVDRL 161
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 28-192 9.25e-10

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 54.81  E-value: 9.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  28 VAFVGRSNVGKSTLINTLTNRRKLVkVSSTPGKTR-LINFFVINDNMYF--VDLPGYgyakvskKEKENwgyIMEQYLVE 104
Cdd:cd04164    6 VVIAGKPNVGKSSLLNALAGRDRAI-VSDIAGTTRdVIEEEIDLGGIPVrlIDTAGL-------RETED---EIEKIGIE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026 105 R--DQLKK---IVLLVDSRHKPTSDDINMYNWIKhyNYEVLVVGTKLDKLKRNDINKNKkiirdtlkmdKDDKILLISSL 179
Cdd:cd04164   75 RarEAIEEadlVLLVVDASEGLDEEDLEILELPA--KKPVIVVLNKSDLLSDAEGISEL----------NGKPIIAISAK 142

                        170
                 ....*....|...
gi 226842026 180 SKEGKEEVLEQIL 192
Cdd:cd04164  143 TGEGIDELKEALL 155
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
26-153 1.42e-09

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 56.19  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  26 PEVAFVGRSNVGKSTLINTLTNRRKLVkVSSTPGKTRLINFFVIN-DNMYF--VDLPGYGYAKVSKKEKEnwgyIMEQYL 102
Cdd:COG1160    3 PVVAIVGRPNVGKSTLFNRLTGRRDAI-VDDTPGVTRDRIYGEAEwGGREFtlIDTGGIEPDDDDGLEAE----IREQAE 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 226842026 103 V---ERDqlkKIVLLVDSRHKPTSDDINMYNWIKHYNYEVLVVGTKLDKLKRND 153
Cdd:COG1160   78 LaieEAD---VILFVVDGRAGLTPLDEEIAKLLRRSGKPVILVVNKVDGPKREA 128
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 29-191 4.38e-09

Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; The Obg-like subfamily consists of five well-delimited, ancient subfamilies, namely Obg, DRG, YyaF/YchF, Ygr210, and NOG1. Four of these groups (Obg, DRG, YyaF/YchF, and Ygr210) are characterized by a distinct glycine-rich motif immediately following the Walker B motif (G3 box). Obg/CgtA is an essential gene that is involved in the initiation of sporulation and DNA replication in the bacteria Caulobacter and Bacillus, but its exact molecular role is unknown. Furthermore, several OBG family members possess a C-terminal RNA-binding domain, the TGS domain, which is also present in threonyl-tRNA synthetase and in bacterial guanosine polyphosphatase SpoT. Nog1 is a nucleolar protein that might function in ribosome assembly. The DRG and Nog1 subfamilies are ubiquitous in archaea and eukaryotes, the Ygr210 subfamily is present in archaea and fungi, and the Obg and YyaF/YchF subfamilies are ubiquitous in bacteria and eukaryotes. The Obg/Nog1 and DRG subfamilies appear to form one major branch of the Obg family and the Ygr210 and YchF subfamilies form another branch. No GEFs, GAPs, or GDIs for Obg have been identified.


Pssm-ID: 206668 [Multi-domain]  Cd Length: 167  Bit Score: 53.17  E-value: 4.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  29 AFVGRSNVGKSTLINTLTnrRKLVKVSSTPGKTRLINFFVIND----NMYFVDLPGygyakVSKKEKENWGYImEQYLVE 104
Cdd:cd01881    1 GLVGLPNVGKSTLLSALT--SAKVEIASYPFTTLEPNVGVFEFgdgvDIQIIDLPG-----LLDGASEGRGLG-EQILAH 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026 105 RDQLKKIVLLVDSRHKptsDDINMYNWIKHYNYEVLVVGTKLD-KLKRNDINKNKKIIRDTLKMDKDDK------ILLIS 177
Cdd:cd01881   73 LYRSDLILHVIDASED---CVGDPLEDQKTLNEEVSGSFLFLKnKPEMIVANKIDMASENNLKRLKLDKlkrgipVVPTS 149

                        170
                 ....*....|....
gi 226842026 178 SLSKEGKEEVLEQI 191
Cdd:cd01881  150 ALTRLGLDRVIRTI 163
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
21-62 7.35e-09

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 54.26  E-value: 7.35e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 226842026  21 PEDGRPEVAFVGRSNVGKSTLINTLTNRRKLVkVSSTPGKTR 62
Cdd:COG1160  171 EEDDPIKIAIVGRPNVGKSSLINALLGEERVI-VSDIAGTTR 211
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
 31-80 2.67e-08

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: 52.13  E-value: 2.67e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 226842026   31 VGRSNVGKSTLINTLTNRRKlVKVSSTPGKTRLINFFVINDNMYFVDLPG 80
Cdd:TIGR03596 124 VGIPNVGKSTLINRLAGKKV-AKVGNRPGVTKGQQWIKLSDNLELLDTPG 172
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
6-80 2.85e-08

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 52.03  E-value: 2.85e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226842026   6 KKAEFVISAVKKTQYPEDGRPE---VAFVGRSNVGKSTLINTLTNRRKlVKVSSTPGKTRLINFFVINDNMYFVDLPG 80
Cdd:COG1161   91 KGIKELIEAIRELAPEKGIKRRpirVMIVGIPNVGKSTLINRLAGKKV-AKTGNKPGVTKGQQWIKLDDGLELLDTPG 167
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
28-192 3.34e-08

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 52.42  E-value: 3.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  28 VAFVGRSNVGKSTLINTLTNRRKLVkVSSTPGKTR--LINFFVINdnmyfvdlpgyGYA--------------KVskkEK 91
Cdd:PRK05291 218 VVIAGRPNVGKSSLLNALLGEERAI-VTDIAGTTRdvIEEHINLD-----------GIPlrlidtagiretddEV---EK 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  92 EnwGyimeqylVER--DQLKK---IVLLVDSRHKPTSDDINMYNWIKHYNyeVLVVGTKLDKLKRNDINknkkiirdtlk 166
Cdd:PRK05291 283 I--G-------IERsrEAIEEadlVLLVLDASEPLTEEDDEILEELKDKP--VIVVLNKADLTGEIDLE----------- 340

                        170       180
                 ....*....|....*....|....*.
gi 226842026 167 MDKDDKILLISSLSKEGKEEVLEQIL 192
Cdd:PRK05291 341 EENGKPVIRISAKTGEGIDELREAIK 366
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 27-192 5.69e-08

Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain.


Pssm-ID: 206685 [Multi-domain]  Cd Length: 170  Bit Score: 50.12  E-value: 5.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  27 EVAFVGRSNVGKSTLINTLTNRRklVKVSSTPGKTRLINFFVINDNMY----FVDLPGygyakvskkekenwgyIME--- 99
Cdd:cd01898    2 DVGLVGLPNAGKSTLLSAISNAK--PKIADYPFTTLVPNLGVVRVDDGrsfvIADIPG----------------LIEgas 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026 100 -------QYL--VERDQLkkIVLLVDSrhKPTSDDINMYNWIKH----YNYE-----VLVVGTKLDKLkrnDINKNKKII 161
Cdd:cd01898   64 egkglghRFLrhIERTRV--LLHVIDL--SGEDDPVEDYETIRNeleaYNPGlaekpRIVVLNKIDLL---DAEERFEKL 136

                        170       180       190
                 ....*....|....*....|....*....|.
gi 226842026 162 RDTLKMDKDDKILLISSLSKEGKEEVLEQIL 192
Cdd:cd01898  137 KELLKELKGKKVFPISALTGEGLDELLKKLA 167
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 26-62 5.76e-08

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 51.51  E-value: 5.76e-08
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 226842026  26 PEVAFVGRSNVGKSTLINTLTNRRKLVkVSSTPGKTR 62
Cdd:PRK03003  39 PVVAVVGRPNVGKSTLVNRILGRREAV-VEDVPGVTR 74
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 24-126 1.13e-07

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 50.95  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  24 GRPEVAFVGRSNVGKSTLINTLTNRRKLVkVSSTPGKTR--LINFFVINDNMY-FVDLPGYGYAKVSKKEKENWGYIMEQ 100
Cdd:PRK09518 449 GLRRVALVGRPNVGKSSLLNQLTHEERAV-VNDLAGTTRdpVDEIVEIDGEDWlFIDTAGIKRRQHKLTGAEYYSSLRTQ 527

                         90       100
                 ....*....|....*....|....*.
gi 226842026 101 YLVERDQLkkIVLLVDSRHKPTSDDI 126
Cdd:PRK09518 528 AAIERSEL--ALFLFDASQPISEQDL 551
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
28-192 1.31e-07

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 49.21  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  28 VAFVGRSNVGKSTLINTLTNRR-KLVKVSSTPG---KTRLINFFVINDNMYFVDLPG-YGYAKVSkkekenwgyimEQYL 102
Cdd:COG1100    6 IVVVGTGGVGKTSLVNRLVGDIfSLEKYLSTNGvtiDKKELKLDGLDVDLVIWDTPGqDEFRETR-----------QFYA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026 103 VERDQLKKIVLLVDSRHKPTsdDINMYNWIKH-----YNYEVLVVGTKLDKLKRNDInKNKKIIRDTLKMDKDDKILLIS 177
Cdd:COG1100   75 RQLTGASLYLFVVDGTREET--LQSLYELLESlrrlgKKSPIILVLNKIDLYDEEEI-EDEERLKEALSEDNIVEVVATS 151

                        170
                 ....*....|....*
gi 226842026 178 SLSKEGKEEVLEQIL 192
Cdd:COG1100  152 AKTGEGVEELFAALA 166
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
28-80 1.44e-07

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 50.50  E-value: 1.44e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226842026  28 VAFVGRSNVGKSTLINTLTNRRklVKVSSTPGKT--RLINFFVINDNMY-FVDLPG 80
Cdd:COG0370    6 IALVGNPNVGKTTLFNALTGSR--QKVGNWPGVTveKKEGKFKLKGKEIeLVDLPG 59
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 28-191 1.68e-07

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: 48.60  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026   28 VAFVGRSNVGKSTLINTLTNRRklVKVSSTPGKT---RLINFFVINDNMYFVDLPG-YGYAKVSKKEKenwgyIMEQYLV 103
Cdd:pfam02421   3 IALVGNPNVGKTTLFNALTGAN--QHVGNWPGVTvekKEGKFKYKGYEIEIVDLPGiYSLSPYSEEER-----VARDYLL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  104 ErDQLKKIVLLVDSrhkpTSDDINMY--NWIKHYNYEVLVVGTKLDKLKRNDINKNKKIIRDTLKMdkddKILLISSLSK 181
Cdd:pfam02421  76 N-EKPDVIVNVVDA----TNLERNLYltLQLLELGLPVVLALNMMDEAEKKGIKIDIKKLSELLGV----PVVPTSARKG 146

                         170
                  ....*....|
gi 226842026  182 EGKEEVLEQI 191
Cdd:pfam02421 147 EGIDELLDAI 156
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 29-192 1.94e-07

Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) subfamily. E. coli has an iron(II) transport system, known as feo, which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.


Pssm-ID: 206667 [Multi-domain]  Cd Length: 159  Bit Score: 48.61  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  29 AFVGRSNVGKSTLINTLTNRRklVKVSSTPGKT--RLINFFVINDNMY-FVDLPG-YGYAKVSKKEKenwgyimeqylVE 104
Cdd:cd01879    1 ALVGNPNVGKTTLFNALTGAR--QKVGNWPGVTveKKEGEFKLGGKEIeIVDLPGtYSLTPYSEDEK-----------VA 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026 105 RDQLKK-----IVLLVDSrhkpTSDDINMY--NWIKHYNYEVLVVGTKLDKLKRNDINKNKKIIRDTLKMdkddKILLIS 177
Cdd:cd01879   68 RDFLLGeepdlIVNVVDA----TNLERNLYltLQLLELGLPVVVALNMIDEAEKRGIKIDLDKLSELLGV----PVVPTS 139

                        170
                 ....*....|....*
gi 226842026 178 SLSKEGKEEVLEQIL 192
Cdd:cd01879  140 ARKGEGIDELLDAIA 154
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 28-192 3.14e-07

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 48.45  E-value: 3.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  28 VAFVGRSNVGKSTLINTLT------NRRKLVKVSSTPG-----------KTRLINFFVINDNMYFVDLPGYgyakvskke 90
Cdd:cd00881    2 VGVIGHVDHGKTTLTGSLLyqtgaiDRRGTRKETFLDTlkeerergitiKTGVVEFEWPKRRINFIDTPGH--------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  91 kENWGYIMEQYLVERDqlkKIVLLVDSRHKPTSDDINMYNWIKHYNYEVLVVGTKLDKLKRNDINKNKKIIRDTLK---- 166
Cdd:cd00881   73 -EDFSKETVRGLAQAD---GALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGEEDFDEVLREIKELLKligf 148

                        170       180
                 ....*....|....*....|....*....
gi 226842026 167 ---MDKDDKILLISSLSKEGKEEVLEQIL 192
Cdd:cd00881  149 tflKGKDVPIIPISALTGEGIEELLDAIV 177
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 19-80 3.82e-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: 47.70  E-value: 3.82e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226842026  19 QYPEDGRP-EVAFVGRSNVGKSTLINTLTnRRKLVKVSSTPGK---TRLINFFVINDNMYFVDLPG 80
Cdd:cd01859   92 ELAIDGKPvIVGVVGYPKVGKSSIINALK-GRHSASTSPIPGSpgyTKGIQLVRIDSKIYLIDTPG 156
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 28-192 4.81e-07

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: 48.63  E-value: 4.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026   28 VAFVGRSNVGKSTLINTLTNRRKLVkVSSTPGKTR-------LINFFVINdnmyFVDLPG--YGYAKVskkEKEnwGyim 98
Cdd:pfam12631  97 VVIVGKPNVGKSSLLNALLGEERAI-VTDIPGTTRdvieetiNIGGIPLR----LIDTAGirETDDEV---EKI--G--- 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026   99 eqylVER--DQLKK---IVLLVDSRHKPTSDDINMYNWIKHYNYeVLVVGTKLDKLKRNDINKNKkiirdtlkmdKDDKI 173
Cdd:pfam12631 164 ----IERarEAIEEadlVLLVLDASRPLDEEDLEILELLKDKKP-IIVVLNKSDLLGEIDELEEL----------KGKPV 228

                         170
                  ....*....|....*....
gi 226842026  174 LLISSLSKEGKEEVLEQIL 192
Cdd:pfam12631 229 LAISAKTGEGLDELEEAIK 247
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 28-147 6.71e-07

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 48.64  E-value: 6.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  28 VAFVGRSNVGKSTLINTLTNRRKLVkVSSTPGKTRL----------INFFVINDNMYFVDLPGYGYAKVSKKEKEnwgyi 97
Cdd:PRK09518 278 VAIVGRPNVGKSTLVNRILGRREAV-VEDTPGVTRDrvsydaewagTDFKLVDTGGWEADVEGIDSAIASQAQIA----- 351

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 226842026  98 MEQYLVerdqlkkIVLLVDSRHKPTSDDINMYNWIKHYNYEVLVVGTKLD 147
Cdd:PRK09518 352 VSLADA-------VVFVVDGQVGLTSTDERIVRMLRRAGKPVVLAVNKID 394
NGP_1 cd01858
A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; ...
 28-80 7.87e-07

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: 46.91  E-value: 7.87e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 226842026  28 VAFVGRSNVGKSTLINTLTNrRKLVKVSSTPGKTRLINFFVINDNMYFVDLPG 80
Cdd:cd01858  105 VGFIGYPNVGKSSVINTLRS-KKVCKVAPIPGETKVWQYITLMKRIYLIDCPG 156
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 2-80 3.66e-06

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: 44.68  E-value: 3.66e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226842026   2 EMEIKKAEFVISAVKKTQYPEDGRpeVAFVGRSNVGKSTLINTLTNRRKLvKVSSTPGKTRLINFFVINDNMYFVDLPG 80
Cdd:cd01849   70 QGILKLKAEITKQKLKLKYKKGIR--VGVVGLPNVGKSSFINALLNKFKL-KVGSIPGTTKLQQDVKLDKEIYLYDTPG 145
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
 28-194 3.98e-06

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: 45.84  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026   28 VAFVGRSNVGKSTLINTLTNRRKLVkVSSTPGKTRL-INFFVIND--NMYFVDLPGYgyakvSKKEKENWGYIMEQYLVE 104
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHGQKISI-TSPKAQTTRNrISGIHTTGasQIIFIDTPGF-----HEKKHSLNRLMMKEARSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  105 RDQLKKIVLLVDSRHKPTSDDInMYNWIKHYNYEVLVVGTKLDKlkrndINKNKKI--IRDTLKMDKDDKILLISSLSKE 182
Cdd:TIGR00436  77 IGGVDLILFVVDSDQWNGDGEF-VLTKLQNLKRPVVLTRNKLDN-----KFKDKLLplIDKYAILEDFKDIVPISALTGD 150

                         170
                  ....*....|..
gi 226842026  183 GKEEVLEQILVY 194
Cdd:TIGR00436 151 NTSFLAAFIEVH 162
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
 28-81 5.88e-06

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


Pssm-ID: 206753 [Multi-domain]  Cd Length: 171  Bit Score: 44.49  E-value: 5.88e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 226842026  28 VAFVGRSNVGKSTLINTLTnRRKLVKVSSTPGKTRLINFFVINDNMYFVDLPGY 81
Cdd:cd04178  119 VGVVGYPNVGKSSVINSLK-RSRACNVGATPGVTKSMQEVHLDKHVKLLDSPGV 171
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 35-192 9.10e-06

Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in eukaryotes ranging from trypanosomes to humans. NOG1 is functionally linked to ribosome biogenesis and found in association with the nuclear pore complexes and identified in many preribosomal complexes. Thus, defects in NOG1 can lead to defects in 60S biogenesis. The S. cerevisiae NOG1 gene is essential for cell viability, and mutations in the predicted G motifs abrogate function. It is a member of the ODN family of GTP-binding proteins that also includes the bacterial Obg and DRG proteins.


Pssm-ID: 206684 [Multi-domain]  Cd Length: 167  Bit Score: 44.09  E-value: 9.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  35 NVGKSTLINTLTNRRklVKVSSTPGKTRLIN--FFVINDNMY-FVDLPGygyakvskkekenwgyIMEQYLVERDQLKK- 110
Cdd:cd01897   10 NVGKSSLVNKLTRAK--PEVAPYPFTTKSLFvgHFDYKYLRWqVIDTPG----------------ILDRPLEERNTIEMq 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026 111 -----------IVLLVD-SRH--KPTSDDINMYNWIK-HYNYEVLVVGTKLDKLKRNDINKNKKIIRdtlkmDKDDKILL 175
Cdd:cd01897   72 aitalahlraaVLFFIDpSETcgYSIEEQLSLFKEIKpLFNKPVIVVLNKIDLLTEEDLSEIEKELE-----KEGEEVIK 146

                        170
                 ....*....|....*..
gi 226842026 176 ISSLSKEGKEEVLEQIL 192
Cdd:cd01897  147 ISTLTEEGVDELKNKAC 163
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 30-81 1.19e-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: 43.79  E-value: 1.19e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226842026  30 FVGRSNVGKSTLINTL----------TNRRKLVKVSSTPGKTRLINFFVINDNMYFVDLPGY 81
Cdd:cd01855  130 VVGATNVGKSTLINALlksnggkvqaQALVQRLTVSPIPGTTLGLIKIPLGEGKKLYDTPGI 191
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
 21-62 3.49e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 43.42  E-value: 3.49e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 226842026  21 PEDGRPEVAFVGRSNVGKSTLINTLTNRRKLVkVSSTPGKTR 62
Cdd:PRK03003 207 ASGGPRRVALVGKPNVGKSSLLNKLAGEERSV-VDDVAGTTV 247
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 99-191 1.44e-04

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: 40.71  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  99 EQYLVERDQLKK----IVLLVDSRHKPTSDDINMYNWIKhyNYEVLVVGTKLDKL-KRNDINKNKKIIRDTLKMD--KDD 171
Cdd:cd01855   21 EDFLEILSTLLNdnalVVHVVDIFDFPGSLIPGLAELIG--AKPVILVGNKIDLLpKDVKPNRLKQWVKKRLKIGglKIK 98

                         90       100
                 ....*....|....*....|
gi 226842026 172 KILLISSLSKEGKEEVLEQI 191
Cdd:cd01855   99 DVILVSAKKGWGVEELIEEI 118
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 28-80 2.08e-04

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


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 40.46  E-value: 2.08e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 226842026  28 VAFVGRSNVGKSTLINTLTNRRKLV--KVSSTPGK----TRLINFFVINDNMYFVDLPG 80
Cdd:cd01854   88 SVLVGQSGVGKSTLLNALLPELVLAtgEISEKLGRgrhtTTHRELFPLPGGGLIIDTPG 146
GTPase_YqeH TIGR03597
ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of ...
 10-81 2.51e-04

ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of GTPases involved in ribosome biogenesis. Like YqlF, it shows a cyclical permutation relative to GTPases EngA (in which the GTPase domain is duplicated), Era, and others. Members of this protein family are found in a relatively small number of bacterial species, including Bacillus subtilis but not Escherichia coli. [Protein synthesis, Other]


Pssm-ID: 213834 [Multi-domain]  Cd Length: 360  Bit Score: 40.68  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026   10 FVISAVKKT------QYPEDGRP--EVAFVGRSNVGKSTLINTL----TNRRKLVKVSSTPGKTRLINFFVINDNMYFVD 77
Cdd:TIGR03597 131 ILVSAKKGNgidellDKIKKARNkkDVYVVGVTNVGKSSLINKLlkqnNGDKDVITTSPFPGTTLDLIEIPLDDGHSLYD 210


                  ....
gi 226842026   78 LPGY 81
Cdd:TIGR03597 211 TPGI 214
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 29-148 3.01e-04

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: 39.25  E-value: 3.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  29 AFVGRSNVGKSTLINTLTnRRKLVKVSSTPGKTRLINFFVIN---DNMYFVDLPGYGYAKVSKKEKEnwgyimEQYLVER 105
Cdd:cd11383    1 GLMGKTGAGKSSLCNALF-GTEVAAVGDRRPTTRAAQAYVWQtggDGLVLLDLPGVGERGRRDREYE------ELYRRLL 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 226842026 106 DQLKKIVLLVDSRHKPTSDDINMY-NWIKHYNYEVLVVGTKLDK 148
Cdd:cd11383   74 PEADLVLWLLDADDRALAADHDFYlLPLAGHDAPLLFVLNQVDP 117
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 28-80 3.47e-04

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: 39.45  E-value: 3.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 226842026   28 VAFVGRSNVGKSTLINTLTNRRKL----VKVSSTPGK--TRLINFFVINDNMYFVDLPG 80
Cdd:pfam03193 109 TVLAGQSGVGKSTLLNALLPELDLrtgeISEKLGRGRhtTTHVELFPLPGGGLLIDTPG 167
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 26-53 7.67e-04

HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.


Pssm-ID: 206666 [Multi-domain]  Cd Length: 204  Bit Score: 38.98  E-value: 7.67e-04
                         10        20
                 ....*....|....*....|....*...
gi 226842026  26 PEVAFVGRSNVGKSTLINTLTNRRKLVK 53
Cdd:cd01878   42 PTVALVGYTNAGKSTLFNALTGADVLAE 69
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
14-47 1.05e-03

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 39.01  E-value: 1.05e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 226842026  14 AVKKTqypedGRPEVAFVGRSNVGKSTLINTLTN 47
Cdd:COG1163   57 AVKKS-----GDATVVLVGFPSVGKSTLLNKLTN 85
RsgA COG1162
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
28-80 1.54e-03

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


Pssm-ID: 440776 [Multi-domain]  Cd Length: 300  Bit Score: 38.17  E-value: 1.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 226842026  28 VAFVGRSNVGKSTLINTLTNRRKLV--KVSSTPGK----TRLINFFVINDNMYFVDLPG 80
Cdd:COG1162  169 SVLVGQSGVGKSTLINALLPDADLAtgEISEKLGRgrhtTTHAELYPLPGGGWLIDTPG 227
PRK01889 PRK01889
GTPase RsgA; Reviewed
 28-45 2.18e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 37.99  E-value: 2.18e-03
                         10
                 ....*....|....*...
gi 226842026  28 VAFVGRSNVGKSTLINTL 45
Cdd:PRK01889 198 VALLGSSGVGKSTLVNAL 215
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 28-190 2.21e-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: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026  28 VAFVGRSNVGKSTLINTLTNrRKLVKVSSTPgKTRLINF--FVINDNMYFVDLPGYGyAKVSKKEKENWGYIMEQYLVer 105
Cdd:cd09912    3 LAVVGEFSAGKSTLLNALLG-EEVLPTGVTP-TTAVITVlrYGLLKGVVLVDTPGLN-STIEHHTEITESFLPRADAV-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226842026 106 dqlkkiVLLVDSRHKPTSDDIN-MYNWIKHYNYEVLVVGTKLDKLKRNDINKNKKIIRDTLKMDK----DDKILLISSLS 180
Cdd:cd09912   78 ------IFVLSADQPLTESEREfLKEILKWSGKKIFFVLNKIDLLSEEELEEVLEYSREELGVLElgggEPRIFPVSAKE 151

                        170
                 ....*....|....*
gi 226842026 181 -----KEGKEEVLEQ 190
Cdd:cd09912  152 alearLQGDEELLEQ 166
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 26-53 2.66e-03

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 37.76  E-value: 2.66e-03
                         10        20
                 ....*....|....*....|....*...
gi 226842026  26 PEVAFVGRSNVGKSTLINTLTNRRKLVK 53
Cdd:COG2262  200 PTVALVGYTNAGKSTLFNRLTGADVLAE 227
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 28-62 5.22e-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: 36.20  E-value: 5.22e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 226842026   28 VAFVGRSNVGKSTLINTLTnRRKLVKVSSTPGKTR 62
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLL-GNKGSITEYYPGTTR 37
 
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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