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Conserved domains on  [gi|56549685|ref|NP_054889|]
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GTP-binding protein 8 isoform 1 [Homo sapiens]

Protein Classification

GTP-binding protein( domain architecture ID 10785093)

GTP-binding protein such as YsxC, which is involved in the biogenesis of ribosomes, or EngB, an essential protein involved in cell division control

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, ...
 91-278 9.90e-66

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: 203.77  E-value: 9.90e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685  91 NRIDYVSSAVRIDHAPDLPRPEVCFIGRSNVGKSSLIKALF---SLApevevRVSKKPGHTKKMNFFKVGKHFTVVDMPG 167
Cdd:COG0218   4 KKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTnrkKLA-----RTSKTPGKTQLINFFLINDKFYLVDLPG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 168 YGF-RAP----EDFVDMVETYLKERRNLKRTFLLVDSVVGIQKTDNIAIEMCEEFALPYVIVLTKIDKSSKGHLLKQVLQ 242
Cdd:COG0218  79 YGYaKVSkaekEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKA 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 56549685 243 IQKFvnMKTQGCFPQLFPVSAVTFSGIHLLRCFIAS 278
Cdd:COG0218 159 IKKA--LGKDPAAPEVILFSSLKKEGIDELRAAIEE 192
 
Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 91-278 9.90e-66

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: 203.77  E-value: 9.90e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685  91 NRIDYVSSAVRIDHAPDLPRPEVCFIGRSNVGKSSLIKALF---SLApevevRVSKKPGHTKKMNFFKVGKHFTVVDMPG 167
Cdd:COG0218   4 KKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTnrkKLA-----RTSKTPGKTQLINFFLINDKFYLVDLPG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 168 YGF-RAP----EDFVDMVETYLKERRNLKRTFLLVDSVVGIQKTDNIAIEMCEEFALPYVIVLTKIDKSSKGHLLKQVLQ 242
Cdd:COG0218  79 YGYaKVSkaekEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKA 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 56549685 243 IQKFvnMKTQGCFPQLFPVSAVTFSGIHLLRCFIAS 278
Cdd:COG0218 159 IKKA--LGKDPAAPEVILFSSLKKEGIDELRAAIEE 192
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 112-280 1.13e-64

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: 200.04  E-value: 1.13e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 112 EVCFIGRSNVGKSSLIKALFSLApeVEVRVSKKPGHTKKMNFFKVGKHFTVVDMPGYGF-RAP----EDFVDMVETYLKE 186
Cdd:cd01876   1 EVAFAGRSNVGKSSLINALTNRK--KLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYaKVSkevrEKWGKLIEEYLEN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 187 RRNLKRTFLLVDSVVGIQKTDNIAIEMCEEFALPYVIVLTKIDKSSKGHLLKQVLQIQKFVNMKtqGCFPQLFPVSAVTF 266
Cdd:cd01876  79 RENLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLF--NILPPVILFSSKKG 156

                       170
                ....*....|....
gi 56549685 267 SGIHLLRCFIASVT 280
Cdd:cd01876 157 TGIDELRALIAEWL 170
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 95-270 5.46e-60

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: 188.45  E-value: 5.46e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685    95 YVSSAVRIDHAPDLPRPEVCFIGRSNVGKSSLIKALF---SLApevevRVSKKPGHTKKMNFFKVGKHFTVVDMPGYGF- 170
Cdd:TIGR03598   3 FVKSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTnrkKLA-----RTSKTPGRTQLINFFEVNDGFRLVDLPGYGYa 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685   171 RAPED----FVDMVETYLKERRNLKRTFLLVDSVVGIQKTDNIAIEMCEEFALPYVIVLTKIDKSSKGHLLKQVLQIQKF 246
Cdd:TIGR03598  78 KVSKEekekWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKA 157

                         170       180
                  ....*....|....*....|....
gi 56549685   247 VNMKTQGCFPQLFpvSAVTFSGIH 270
Cdd:TIGR03598 158 LKKDADDPSVQLF--SSLKKTGID 179
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 112-227 2.64e-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: 89.22  E-value: 2.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685   112 EVCFIGRSNVGKSSLIKALFslapEVEVRVSKKPGHTKKMNFFKV---GKHFTVVDMPGYgFRAPEDFVDMVETYLKERR 188
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALT----GAKAIVSDYPGTTRDPNEGRLelkGKQIILVDTPGL-IEGASEGEGLGRAFLAIIE 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 56549685   189 NlKRTFLLVDSVVGIQKTDNIAIEMCEEFALPYVIVLTK 227
Cdd:pfam01926  76 A-DLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
PRK04213 PRK04213
GTP-binding protein EngB;
110-230 1.68e-20

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 86.89  E-value: 1.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685  110 RPEVCFIGRSNVGKSSLIKALFSlapeVEVRVSKKPGHTKKMNFFKVGKhFTVVDMPGYGFRA--PEDFVDMVET----Y 183
Cdd:PRK04213   9 KPEIVFVGRSNVGKSTLVRELTG----KKVRVGKRPGVTRKPNHYDWGD-FILTDLPGFGFMSgvPKEVQEKIKDeivrY 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 56549685  184 LKER-RNLKRTFLLVD--SVVGI----QKTDNIAI--EM---CEEFALPYVIVLTKIDK 230
Cdd:PRK04213  84 IEDNaDRILAAVLVVDgkSFIEIierwEGRGEIPIdvEMfdfLRELGIPPIVAVNKMDK 142
 
Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 91-278 9.90e-66

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: 203.77  E-value: 9.90e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685  91 NRIDYVSSAVRIDHAPDLPRPEVCFIGRSNVGKSSLIKALF---SLApevevRVSKKPGHTKKMNFFKVGKHFTVVDMPG 167
Cdd:COG0218   4 KKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTnrkKLA-----RTSKTPGKTQLINFFLINDKFYLVDLPG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 168 YGF-RAP----EDFVDMVETYLKERRNLKRTFLLVDSVVGIQKTDNIAIEMCEEFALPYVIVLTKIDKSSKGHLLKQVLQ 242
Cdd:COG0218  79 YGYaKVSkaekEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKA 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 56549685 243 IQKFvnMKTQGCFPQLFPVSAVTFSGIHLLRCFIAS 278
Cdd:COG0218 159 IKKA--LGKDPAAPEVILFSSLKKEGIDELRAAIEE 192
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 112-280 1.13e-64

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: 200.04  E-value: 1.13e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 112 EVCFIGRSNVGKSSLIKALFSLApeVEVRVSKKPGHTKKMNFFKVGKHFTVVDMPGYGF-RAP----EDFVDMVETYLKE 186
Cdd:cd01876   1 EVAFAGRSNVGKSSLINALTNRK--KLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYaKVSkevrEKWGKLIEEYLEN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 187 RRNLKRTFLLVDSVVGIQKTDNIAIEMCEEFALPYVIVLTKIDKSSKGHLLKQVLQIQKFVNMKtqGCFPQLFPVSAVTF 266
Cdd:cd01876  79 RENLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLF--NILPPVILFSSKKG 156

                       170
                ....*....|....
gi 56549685 267 SGIHLLRCFIASVT 280
Cdd:cd01876 157 TGIDELRALIAEWL 170
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 95-270 5.46e-60

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: 188.45  E-value: 5.46e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685    95 YVSSAVRIDHAPDLPRPEVCFIGRSNVGKSSLIKALF---SLApevevRVSKKPGHTKKMNFFKVGKHFTVVDMPGYGF- 170
Cdd:TIGR03598   3 FVKSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTnrkKLA-----RTSKTPGRTQLINFFEVNDGFRLVDLPGYGYa 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685   171 RAPED----FVDMVETYLKERRNLKRTFLLVDSVVGIQKTDNIAIEMCEEFALPYVIVLTKIDKSSKGHLLKQVLQIQKF 246
Cdd:TIGR03598  78 KVSKEekekWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKA 157

                         170       180
                  ....*....|....*....|....
gi 56549685   247 VNMKTQGCFPQLFpvSAVTFSGIH 270
Cdd:TIGR03598 158 LKKDADDPSVQLF--SSLKKTGID 179
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 112-227 2.64e-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: 89.22  E-value: 2.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685   112 EVCFIGRSNVGKSSLIKALFslapEVEVRVSKKPGHTKKMNFFKV---GKHFTVVDMPGYgFRAPEDFVDMVETYLKERR 188
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALT----GAKAIVSDYPGTTRDPNEGRLelkGKQIILVDTPGL-IEGASEGEGLGRAFLAIIE 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 56549685   189 NlKRTFLLVDSVVGIQKTDNIAIEMCEEFALPYVIVLTK 227
Cdd:pfam01926  76 A-DLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
PRK04213 PRK04213
GTP-binding protein EngB;
110-230 1.68e-20

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 86.89  E-value: 1.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685  110 RPEVCFIGRSNVGKSSLIKALFSlapeVEVRVSKKPGHTKKMNFFKVGKhFTVVDMPGYGFRA--PEDFVDMVET----Y 183
Cdd:PRK04213   9 KPEIVFVGRSNVGKSTLVRELTG----KKVRVGKRPGVTRKPNHYDWGD-FILTDLPGFGFMSgvPKEVQEKIKDeivrY 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 56549685  184 LKER-RNLKRTFLLVD--SVVGI----QKTDNIAI--EM---CEEFALPYVIVLTKIDK 230
Cdd:PRK04213  84 IEDNaDRILAAVLVVDgkSFIEIierwEGRGEIPIdvEMfdfLRELGIPPIVAVNKMDK 142
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 114-269 6.66e-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: 65.17  E-value: 6.66e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 114 CFIGRSNVGKSSLIKALFSLAPEVevrVSKKPGHTKKMNFFKVGKH-----FTVVDMPGYGFRAPEDFVDMVETYLKERR 188
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGE---VSDVPGTTRDPDVYVKELDkgkvkLVLVDTPGLDEFGGLGREELARLLLRGAD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 189 NLkrtFLLVDSVVG--IQKTDNIAIEMCEEFALPYVIVLTKIDKSSKGHLLKQVLQIQKFvnmktQGCFPQLFPVSAVTF 266
Cdd:cd00882  78 LI---LLVVDSTDResEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELA-----KILGVPVFEVSAKTG 149


                ...
gi 56549685 267 SGI 269
Cdd:cd00882 150 EGV 152
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 113-273 3.28e-10

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: 57.86  E-value: 3.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 113 VCFIGRSNVGKSSLIKAL--FSLAPevevrVSKKPGHTKK-----MNFfkvGKH-FTVVDMPGY-------GFRapedfv 177
Cdd:cd04163   6 VAIIGRPNVGKSTLLNALvgQKISI-----VSPKPQTTRNrirgiYTD---DDAqIIFVDTPGIhkpkkklGER------ 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 178 dMVETYlkeRRNLKR---TFLLVDSVVGIQKTDNIAIEMCEEFALPYVIVLTKIDK-SSKGHLLKQVLQIQKFVNmktqg 253
Cdd:cd04163  72 -MVKAA---WSALKDvdlVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLvKDKEDLLPLLEKLKELHP----- 142

                       170       180
                ....*....|....*....|
gi 56549685 254 cFPQLFPVSAVTFSGIHLLR 273
Cdd:cd04163 143 -FAEIFPISALKGENVDELL 161
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 108-167 1.68e-09

A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC class I region and is highly homologous to a putative GTP-binding protein, MMR1 from mouse. These proteins represent a new subfamily of GTP-binding proteins that has only eukaryote members. This subfamily shows a circular permutation of the GTPase signature motifs so that the C-terminal strands 5, 6, and 7 (strand 6 contains the G4 box with sequence NKXD) are relocated to the N-terminus.


Pssm-ID: 206750 [Multi-domain]  Cd Length: 140  Bit Score: 54.93  E-value: 1.68e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 108 LPRPEVCFIGRSNVGKSSLIKALFSlapEVEVRVSKKPGHTKKMNFFKVGKHFTVVDMPG 167
Cdd:cd01857  80 LNEATIGLVGYPNVGKSSLINALVG---SKKVSVSSTPGKTKHFQTIFLEPGITLCDCPG 136
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 115-279 2.86e-08

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: 52.25  E-value: 2.86e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 115 FIGRSNVGKSSLIKALF---SLApevevrVSKKPGHTKKMNFFKVGKH----FTVVDMPGygfrapedfVDMVETYLKER 187
Cdd:cd00880   2 IFGRPNVGKSSLLNALLgqnVGI------VSPIPGTTRDPVRKEWELLplgpVVLIDTPG---------LDEEGGLGRER 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 188 rnLKRTF----------LLVDSVVGIQKTDNIAIEMcEEFALPYVIVLTKIDKSSKGhllKQVLQIQKFVNMKTQGCfpQ 257
Cdd:cd00880  67 --VEEARqvadradlvlLVVDSDLTPVEEEAKLGLL-RERGKPVLLVLNKIDLVPES---EEEELLRERKLELLPDL--P 138

                       170       180
                ....*....|....*....|..
gi 56549685 258 LFPVSAVTFSGIHLLRCFIASV 279
Cdd:cd00880 139 VIAVSALPGEGIDELRKKIAEL 160
YeeP COG3596
Predicted GTPase [General function prediction only];
108-235 3.95e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 53.62  E-value: 3.95e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 108 LPRPEVCFIGRSNVGKSSLIKALF--SLAPEVEVRvskkpGHTKKMNFFKV----GKHFTVVDMPGYGFRAPEDfvdmve 181
Cdd:COG3596  37 LPPPVIALVGKTGAGKSSLINALFgaEVAEVGVGR-----PCTREIQRYRLesdgLPGLVLLDTPGLGEVNERD------ 105

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56549685 182 tylKERRNLKRTFLLVDSVVGIQKTDNIAIEMCEEFA---------LPYVIVLTKIDKSSKGH 235
Cdd:COG3596 106 ---REYRELRELLPEADLILWVVKADDRALATDEEFLqalraqypdPPVLVVLTQVDRLEPER 165
era PRK00089
GTPase Era; Reviewed
 113-273 4.92e-08

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 53.13  E-value: 4.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685  113 VCFIGRSNVGKSSLIKAL--FSLAPevevrVSKKPGHT-KKMNFFKVGKHFTV--VDMPGYgFRApedfvdmvETYLKER 187
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALvgQKISI-----VSPKPQTTrHRIRGIVTEDDAQIifVDTPGI-HKP--------KRALNRA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685  188 --RNLKRTF-------LLVDSVVGIQKTDNIAIEMCEEFALPYVIVLTKIDK-SSKGHLLKQVLQIQKFVNmktqgcFPQ 257
Cdd:PRK00089  74 mnKAAWSSLkdvdlvlFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLvKDKEELLPLLEELSELMD------FAE 147

                        170
                 ....*....|....*.
gi 56549685  258 LFPVSAVTFSGIHLLR 273
Cdd:PRK00089 148 IVPISALKGDNVDELL 163
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
113-273 6.45e-08

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 52.68  E-value: 6.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 113 VCFIGRSNVGKSSLIKALfslapeVEVR---VSKKPGHT-KKMNFFKVGKHFTV--VDMPGYgFR--------------- 171
Cdd:COG1159   6 VAIVGRPNVGKSTLLNAL------VGQKvsiVSPKPQTTrHRIRGIVTREDAQIvfVDTPGI-HKpkrklgrrmnkaaws 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 172 APEDfVDMVetylkerrnlkrtFLLVDSVVGIQKTDNIAIEMCEEFALPYVIVLTKIDKSSKGHLLKQVLQIQKFVNmkt 251
Cdd:COG1159  79 ALED-VDVI-------------LFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLVKKEELLPLLAEYSELLD--- 141

                       170       180
                ....*....|....*....|..
gi 56549685 252 qgcFPQLFPVSAVTFSGIHLLR 273
Cdd:COG1159 142 ---FAEIVPISALKGDNVDELL 160
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 113-270 2.68e-07

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: 49.35  E-value: 2.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 113 VCFIGRSNVGKSSLIKAlfsLAPEVEVRVSKKPGHTK---KMNFFKVGKHFTVVDMPGYGFRAPEDfvDMVETY--LKER 187
Cdd:cd01895   5 IAIIGRPNVGKSSLLNA---LLGEERVIVSDIAGTTRdsiDVPFEYDGQKYTLIDTAGIRKKGKVT--EGIEKYsvLRTL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 188 RNLKR---TFLLVDSVVGIQKTD-NIAiEMCEEFALPYVIVLTKIDKSSKGHllKQVLQIQKFVNMKtqgcFPQLF---- 259
Cdd:cd01895  80 KAIERadvVLLVLDASEGITEQDlRIA-GLILEEGKALIIVVNKWDLVEKDE--KTMKEFEKELRRK----LPFLDyapi 152

                       170
                ....*....|..
gi 56549685 260 -PVSAVTFSGIH 270
Cdd:cd01895 153 vFISALTGQGVD 164
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 113-272 5.18e-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: 48.83  E-value: 5.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 113 VCFIGRSNVGKSSLIKAL------------------FSLAPEVEVRVSKKPGHtkkMNFFKVGKHFTVVDMPGYgfrapE 174
Cdd:cd00881   2 VGVIGHVDHGKTTLTGSLlyqtgaidrrgtrketflDTLKEERERGITIKTGV---VEFEWPKRRINFIDTPGH-----E 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 175 DFVDMVETYLkerRNLKRTFLLVDSVVGIQKTDNIAIEMCEEFALPYVIVLTKIDKSSKGHLLKQVLQIQKFVN----MK 250
Cdd:cd00881  74 DFSKETVRGL---AQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGEEDFDEVLREIKELLKligfTF 150

                       170       180
                ....*....|....*....|..
gi 56549685 251 TQGCFPQLFPVSAVTFSGIHLL 272
Cdd:cd00881 151 LKGKDVPIIPISALTGEGIEEL 172
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 113-272 6.12e-07

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 48.68  E-value: 6.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685   113 VCFIGRSNVGKSSLIKALFSLAPEVEVRVSKKPGHTKKMNFFKV------------------GKHFTVVDMPGYgfrapE 174
Cdd:pfam00009   6 IGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEAGLDNLPEerergitiksaavsfetkDYLINLIDTPGH-----V 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685   175 DFVDMVETYLkerrnlkRT----FLLVDSVVGIQKTDNIAIEMCEEFALPYVIVLTKIDKSSKGHLLKQVLQIQ-KFVNM 249
Cdd:pfam00009  81 DFVKEVIRGL-------AQadgaILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDGAELEEVVEEVSrELLEK 153

                         170       180
                  ....*....|....*....|....
gi 56549685   250 K-TQGCFPQLFPVSAVTFSGIHLL 272
Cdd:pfam00009 154 YgEDGEFVPVVPGSALKGEGVQTL 177
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 115-168 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: 48.03  E-value: 1.23e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56549685 115 FIGRSNVGKSSLIKALFSLAPEVEVR--------VSKKPGHTKKMNFFKVGKHFTVVDMPGY 168
Cdd:cd01855 130 VVGATNVGKSTLINALLKSNGGKVQAqalvqrltVSPIPGTTLGLIKIPLGEGKKLYDTPGI 191
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 108-167 2.69e-06

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: 46.37  E-value: 2.69e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56549685 108 LPRPEVCFI-GRSNVGKSSLIKalfSLAPEVEVRVSKKPGHTKKMNFFKVGKHFTVVDMPG 167
Cdd:cd01856 112 LPRPLRAMVvGIPNVGKSTLIN---RLRGKKVAKVGNKPGVTRGQQWIRIGPNIELLDTPG 169
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 113-270 7.05e-06

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 46.97  E-value: 7.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685  113 VCFIGRSNVGKSSLIKALFSlapevEVR--VSKKPGHTK---KMNFFKVGKHFTVVDMPgyGFRAPEDFVDMVETY--LK 185
Cdd:PRK00093 176 IAIIGRPNVGKSSLINALLG-----EERviVSDIAGTTRdsiDTPFERDGQKYTLIDTA--GIRRKGKVTEGVEKYsvIR 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685  186 ERRNLKR---TFLLVDSVVGIQKTD-NIAiEMCEEFALPYVIVLTK---IDKSSKGHLLKQVLQIQKFVNmktqgcFPQL 258
Cdd:PRK00093 249 TLKAIERadvVLLVIDATEGITEQDlRIA-GLALEAGRALVIVVNKwdlVDEKTMEEFKKELRRRLPFLD------YAPI 321

                        170
                 ....*....|..
gi 56549685  259 FPVSAVTFSGIH 270
Cdd:PRK00093 322 VFISALTGQGVD 333
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
120-167 9.13e-06

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 46.25  E-value: 9.13e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 56549685 120 NVGKSSLIKALfslAPEVEVRVSKKPGHTKKMNFFKVGKHFTVVDMPG 167
Cdd:COG1161 123 NVGKSTLINRL---AGKKVAKTGNKPGVTKGQQWIKLDDGLELLDTPG 167
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 113-167 1.07e-05

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


Pssm-ID: 206752 [Multi-domain]  Cd Length: 157  Bit Score: 44.62  E-value: 1.07e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 56549685 113 VCFIGRSNVGKSSLIKALFSLAPEVEVRVSKKPGHTKKMNFFKVGKHFTVVDMPG 167
Cdd:cd01859 102 VGVVGYPKVGKSSIINALKGRHSASTSPIPGSPGYTKGIQLVRIDSKIYLIDTPG 156
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
106-270 7.07e-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: 7.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 106 PDLPRPEVCFIGRSNVGKSSLIKALfsLAPEvevR--VSKKPGHTK-----KMNFFkvGKHFTVVDMPGygfrapedfV- 177
Cdd:COG1160 171 EEDDPIKIAIVGRPNVGKSSLINAL--LGEE---RviVSDIAGTTRdsidtPFERD--GKKYTLIDTAG---------Ir 234

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 178 ------DMVETY--LKERRNLKRT---FLLVDSVVGIQKTD-NIAiEMCEEFALPYVIVLTKID-----KSSKGHLLKQV 240
Cdd:COG1160 235 rkgkvdEGIEKYsvLRTLRAIERAdvvLLVIDATEGITEQDlKIA-GLALEAGKALVIVVNKWDlvekdRKTREELEKEI 313

                       170       180       190
                ....*....|....*....|....*....|
gi 56549685 241 LQIQKFVNmktqgcFPQLFPVSAVTFSGIH 270
Cdd:COG1160 314 RRRLPFLD------YAPIVFISALTGQGVD 337
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
 116-168 8.06e-05

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: 42.18  E-value: 8.06e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 56549685 116 IGRSNVGKSSLIKalfSLAPEVEVRVSKKPGHTKKMNFFKVGKHFTVVDMPGY 168
Cdd:cd04178 122 VGYPNVGKSSVIN---SLKRSRACNVGATPGVTKSMQEVHLDKHVKLLDSPGV 171
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 115-167 1.13e-04

Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, and archaea. They all exhibit a circular permutation of the GTPase signature motifs so that the order of the conserved G box motifs is G4-G5-G1-G2-G3, with G4 and G5 being permuted from the C-terminal region of proteins in the Ras superfamily to the N-terminus of YlqF-related GTPases.


Pssm-ID: 206746 [Multi-domain]  Cd Length: 146  Bit Score: 41.60  E-value: 1.13e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 56549685 115 FIGRSNVGKSSLIKAlfsLAPEVEVRVSKKPGHTKKMNFFKVGKHFTVVDMPG 167
Cdd:cd01849  96 VVGLPNVGKSSFINA---LLNKFKLKVGSIPGTTKLQQDVKLDKEIYLYDTPG 145
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
 115-269 1.13e-04

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: 41.61  E-value: 1.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 115 FIGRSNVGKSSLIKALFSlapeVEVRVSKKPGHTKKMNF----FKVGKHFTVVDMPGYGFRAPEDfVDMVETYLkerRNL 190
Cdd:cd01881   2 LVGLPNVGKSTLLSALTS----AKVEIASYPFTTLEPNVgvfeFGDGVDIQIIDLPGLLDGASEG-RGLGEQIL---AHL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 191 KRTFLLV--------DSVVGIQKTDNIAIEMCEEFA----LPYVIVLTKIDKSSKGHLLKQVLQIqkfvnmKTQGcfPQL 258
Cdd:cd01881  74 YRSDLILhvidasedCVGDPLEDQKTLNEEVSGSFLflknKPEMIVANKIDMASENNLKRLKLDK------LKRG--IPV 145

                       170
                ....*....|.
gi 56549685 259 FPVSAVTFSGI 269
Cdd:cd01881 146 VPTSALTRLGL 156
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
113-265 1.37e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 41.51  E-value: 1.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 113 VCFIGRSNVGKSSLIKAL----FSLAPE---VEVRVSKK----PGHTKKMNffkvgkhftVVDMPGYgfrapEDFVDMVE 181
Cdd:COG1100   6 IVVVGTGGVGKTSLVNRLvgdiFSLEKYlstNGVTIDKKelklDGLDVDLV---------IWDTPGQ-----DEFRETRQ 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 182 TYLKERRNLKRTFLLVDSVvgIQKTDNIAIEMCEEFA-----LPYVIVLTKIDKSSKGHLLKQvLQIQKFVNMKTqgcFP 256
Cdd:COG1100  72 FYARQLTGASLYLFVVDGT--REETLQSLYELLESLRrlgkkSPIILVLNKIDLYDEEEIEDE-ERLKEALSEDN---IV 145


                ....*....
gi 56549685 257 QLFPVSAVT 265
Cdd:COG1100 146 EVVATSAKT 154
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 115-230 2.73e-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: 40.40  E-value: 2.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 115 FIGRSNVGKSSLIKALF--SLAPEVEVRvskkPGHTKKMNF-FKVGKHF-TVVDMPGYGFRAPEDfvdmvETYLKERRNL 190
Cdd:cd11383   2 LMGKTGAGKSSLCNALFgtEVAAVGDRR----PTTRAAQAYvWQTGGDGlVLLDLPGVGERGRRD-----REYEELYRRL 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 56549685 191 KRTfllVDSVVGIQKTDNIAIEMCEEFALPYV--------IVLTKIDK 230
Cdd:cd11383  73 LPE---ADLVLWLLDADDRALAADHDFYLLPLaghdapllFVLNQVDP 117
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 113-174 2.91e-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: 40.60  E-value: 2.91e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56549685   113 VCFIGRSNVGKSSLIKAlfsLAPEVEVRVSKKPGHTKKmnffkvGKHFT-------------VVDMPgyGFRAPE 174
Cdd:pfam03193 109 TVLAGQSGVGKSTLLNA---LLPELDLRTGEISEKLGR------GRHTTthvelfplpggglLIDTP--GFRELG 172
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 122-273 3.05e-04

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.


Pssm-ID: 206676 [Multi-domain]  Cd Length: 192  Bit Score: 40.81  E-value: 3.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 122 GKSSLIKALFSLA--------PEvevrvSKKPGHTKKMNF--FKVGK---------------HFTVVDMPGYGfrapedf 176
Cdd:cd01889  12 GKTSLAKALSEIAstaafdknPQ-----SQERGITLDLGFssFEVDKpkhlednenpqienyQITLVDCPGHA------- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 177 vDMVETYLKERRNLKRTFLLVDSVVGIQKTDNIAIEMCEEFALPYVIVLTKID------KSSKGHLLKQVLQiqkfvnmK 250
Cdd:cd01889  80 -SLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDlipeeeRKRKIEKMKKRLQ-------K 151

                       170       180
                ....*....|....*....|....*..
gi 56549685 251 T--QGCFPQ--LFPVSAVTFSGIHLLR 273
Cdd:cd01889 152 TleKTRLKDspIIPVSAKPGEGEAELG 178
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 114-282 3.91e-04

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


Pssm-ID: 206667 [Multi-domain]  Cd Length: 159  Bit Score: 40.13  E-value: 3.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 114 CFIGRSNVGKSSLIKALFSLApeveVRVSKKPGHT--KKMNFFKV-GKHFTVVDMPG-YGFRA--PEDFVdmVETYLKER 187
Cdd:cd01879   1 ALVGNPNVGKTTLFNALTGAR----QKVGNWPGVTveKKEGEFKLgGKEIEIVDLPGtYSLTPysEDEKV--ARDFLLGE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 188 R-----------NLKRTFLLVDSVVgiqktdniaiemceEFALPYVIVLTKIDKS-SKGHllkqVLQIQKFvnMKTQGCf 255
Cdd:cd01879  75 EpdlivnvvdatNLERNLYLTLQLL--------------ELGLPVVVALNMIDEAeKRGI----KIDLDKL--SELLGV- 133

                       170       180
                ....*....|....*....|....*..
gi 56549685 256 pQLFPVSAVTFSGIHLLRCFIASVTGS 282
Cdd:cd01879 134 -PVVPTSARKGEGIDELLDAIAKLAES 159
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 116-272 9.83e-04

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: 38.94  E-value: 9.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 116 IGRSNVGKSSLIKAL-----------F-SLAPEVEVrVSKKPGHTkkmnffkvgkhFTVVDMPGY----------GFRap 173
Cdd:cd01898   6 VGLPNAGKSTLLSAIsnakpkiadypFtTLVPNLGV-VRVDDGRS-----------FVIADIPGLiegasegkglGHR-- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 174 edfvdmvetYLkerRNLKRTFLLVdSVVGIQKTDNI--AIEM-CEEFAL--------PYVIVLTKIDKSSKGHLLKQVLQ 242
Cdd:cd01898  72 ---------FL---RHIERTRVLL-HVIDLSGEDDPveDYETiRNELEAynpglaekPRIVVLNKIDLLDAEERFEKLKE 138

                       170       180       190
                ....*....|....*....|....*....|
gi 56549685 243 IQKFVNMKtqgcfpQLFPVSAVTFSGIHLL 272
Cdd:cd01898 139 LLKELKGK------KVFPISALTGEGLDEL 162
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 113-194 2.32e-03

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


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 38.53  E-value: 2.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 113 VCFIGRSNVGKSSLIKAlfsLAPEVEVR---VSKKpghTKKmnffkvGKHFT-------------VVDMPgyGFRAPeDF 176
Cdd:cd01854  88 SVLVGQSGVGKSTLLNA---LLPELVLAtgeISEK---LGR------GRHTTthrelfplpggglIIDTP--GFREL-GL 152

                        90
                ....*....|....*...
gi 56549685 177 VDMvetylkERRNLKRTF 194
Cdd:cd01854 153 LHI------DPEELAEYF 164
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 116-272 2.48e-03

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


Pssm-ID: 206681 [Multi-domain]  Cd Length: 157  Bit Score: 37.80  E-value: 2.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 116 IGRSNVGKSSLI-------KALfslapevevrVSKKPGHT---KKMNFFKVGKHFTVVDMPGygfrapedFVDMVETYLK 185
Cdd:cd01894   3 VGRPNVGKSTLFnrltgrrDAI----------VSDTPGVTrdrKYGEAEWGGREFILIDTGG--------IEPDDEGISK 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 186 E-RRNLKRT-------FLLVDSVVGIQKTDNIAIEMCEEFALPYVIVLTKIDKsskghlLKQVLQIQKFVNMktqGcFPQ 257
Cdd:cd01894  65 EiREQAEIAieeadviLFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDN------IKEEEEAAEFYSL---G-FGE 134

                       170
                ....*....|....*
gi 56549685 258 LFPVSAVTFSGIHLL 272
Cdd:cd01894 135 PIPISAEHGRGIGDL 149
PRK12288 PRK12288
small ribosomal subunit biogenesis GTPase RsgA;
115-141 5.73e-03

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237039 [Multi-domain]  Cd Length: 347  Bit Score: 37.91  E-value: 5.73e-03
                         10        20
                 ....*....|....*....|....*..
gi 56549685  115 FIGRSNVGKSSLIKALFslaPEVEVRV 141
Cdd:PRK12288 210 FVGQSGVGKSSLINALL---PEAEILV 233
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 122-279 6.01e-03

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 36.81  E-value: 6.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 122 GKSSLIKALF-----SLAPEvevrvsKKPGHTKKMNF----FKVGKHFTVVDMPGYgfrapEDFV----------DMVet 182
Cdd:cd04171  11 GKTTLIKALTgietdRLPEE------KKRGITIDLGFayldLPDGKRLGFIDVPGH-----EKFVknmlagaggiDAV-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 183 ylkerrnlkrtFLLVDSVVGI--QKTDNIAIemCEEFALPYVI-VLTKIDKSSKGHLLKQVLQIQKFV------NMKtqg 253
Cdd:cd04171  78 -----------LLVVAADEGImpQTREHLEI--LELLGIKKGLvVLTKADLVDEDRLELVEEEILELLagtflaDAP--- 141

                       170       180
                ....*....|....*....|....*.
gi 56549685 254 cfpqLFPVSAVTFSGIHLLRCFIASV 279
Cdd:cd04171 142 ----IFPVSSVTGEGIEELKNYLDEL 163
PRK12289 PRK12289
small ribosomal subunit biogenesis GTPase RsgA;
117-172 6.63e-03

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237040 [Multi-domain]  Cd Length: 352  Bit Score: 37.69  E-value: 6.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685  117 GRSNVGKSSLIKALFslaPEVEVRVSKKPGHTKKmnffkvGKHFT----VVDMPGYGFRA 172
Cdd:PRK12289 179 GPSGVGKSSLINRLI---PDVELRVGKVSGKLGR------GRHTTrhveLFELPNGGLLA 229
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 117-201 6.77e-03

Septin family protein [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 37.69  E-value: 6.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 117 GRSNVGKSSLIKALF--SLAPEVEVrVSKKPGHTKK---MNFFKV---GKHF----TVVDMPGYGfrapeDFVD------ 178
Cdd:COG5019  30 GESGLGKTTFINTLFgtSLVDETEI-DDIRAEGTSPtleIKITKAeleEDGFhlnlTVIDTPGFG-----DFIDnskcwe 103

                        90       100       110
                ....*....|....*....|....*....|.
gi 56549685 179 --------MVETYLKERRNLKRTFLLVDSVV 201
Cdd:COG5019 104 pivdyiddQFDQYLDEEQKIKRNPKFKDTRV 134
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 113-269 8.00e-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: 8.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685   113 VCFIGRSNVGKSSLikaLFSLAPEVEVRVSKKPGHTKKMNFFKV---GKH--FTVVDMPGYgfrapEDFVDMVETYLKER 187
Cdd:TIGR00231   4 IVIVGHPNVGKSTL---LNSLLGNKGSITEYYPGTTRNYVTTVIeedGKTykFNLLDTAGQ-----EDYDAIRRLYYPQV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685   188 RNLKRTFLLVDSVVGIQKT----DNIAIEMCEEfALPYVIVLTKIDKssKGHLLKQVLQiQKFVNMKtqgcFPQLFPVSA 263
Cdd:TIGR00231  76 ERSLRVFDIVILVLDVEEIlekqTKEIIHHADS-GVPIILVGNKIDL--KDADLKTHVA-SEFAKLN----GEPIIPLSA 147


                  ....*.
gi 56549685   264 VTFSGI 269
Cdd:TIGR00231 148 ETGKNI 153
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 116-201 8.48e-03

CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.


Pssm-ID: 206649  Cd Length: 275  Bit Score: 37.14  E-value: 8.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685 116 IGRSNVGKSSLIKALF--SLAPE-------------VEVRVSKkpgHTKKMNFFKVgkHFTVVDMPGYGfrapeDFVD-- 178
Cdd:cd01850  10 VGESGLGKSTFINTLFgtKLYPSkyppapgehitktVEIKISK---AELEENGVKL--KLTVIDTPGFG-----DNINns 79

                        90       100       110
                ....*....|....*....|....*....|....*
gi 56549685 179 -----MV-------ETYLKERRNLKRTFLLVDSVV 201
Cdd:cd01850  80 dcwkpIVdyiddqfESYLREESRINRNRRIPDTRV 114
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
 116-201 9.31e-03

Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this family bind GTP. As regards the septins, these are polypeptides of 30-65kDa with three characteriztic GTPase motifs (G-1, G-3 and G-4) that are similar to those of the Ras family. The G-4 motif is strictly conserved with a unique septin consensus of AKAD. Most septins are thought to have at least one coiled-coil region, which in some cases is necessary for intermolecular interactions that allow septins to polymerize to form rod-shaped complexes. In turn, these are arranged into tandem arrays to form filaments. They are multifunctional proteins, with roles in cytokinesis, sporulation, germ cell development, exocytosis and apoptosis.


Pssm-ID: 395596  Cd Length: 272  Bit Score: 36.89  E-value: 9.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549685   116 IGRSNVGKSSLIKALFS---------LAPEVEVRVSKKPGHTKKM---NFFKVgkHFTVVDMPGYG--------FRAPED 175
Cdd:pfam00735   9 VGESGLGKTTFINTLFLtdlyrargiPGPSEKIKKTVEIKAYTVEieeDGVKL--NLTVIDTPGFGdaidnsncWRPIVE 86

                          90       100
                  ....*....|....*....|....*..
gi 56549685   176 FVD-MVETYLKERRNLKRTFlLVDSVV 201
Cdd:pfam00735  87 YIDeQYEQYLRDESGLNRKS-IKDNRV 112
 
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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