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Conserved domains on  [gi|1174098179|ref|WP_081436395|]
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ribosome biogenesis GTPase Der [Magnetococcus marinus]

Protein Classification

ribosome biogenesis GTPase Der( domain architecture ID 11439329)

ribosome biogenesis GTPase Der (EngA) is an essential bacterial GTPase that is required for 50S ribosomal subunit stability; it contains two consecutive GTPase domains and a KH-domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
1-463 0e+00

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


:

Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 678.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   1 MSklPLVALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTGGFEADPGETMVSLIRGQTIL 80
Cdd:COG1160     1 MS--PVVAIVGRPNVGKSTLFNRLTGRRDAIVDDTPGVTRDRIYGEAEWGGREFTLIDTGGIEPDDDDGLEAEIREQAEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  81 AIEEADIIVFVVDGSTGPLTDDYAIASHLRSSGKPVIIAANKSEKKAATASI-EFHELGMEPIIPISSAHGLGIGDLLET 159
Cdd:COG1160    79 AIEEADVILFVVDGRAGLTPLDEEIAKLLRRSGKPVILVVNKVDGPKREADAaEFYSLGLGEPIPISAEHGRGVGDLLDA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 160 LEEmtdamegfcrqpeeqLLPLEVEQENPEvareprfkGPLRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSID 239
Cdd:COG1160   159 VLE---------------LLPEEEEEEEED--------DPIKIAIVGRPNVGKSSLINALLGEERVIVSDIAGTTRDSID 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 240 VPITdANGETVILVDTAGIRRKSRVSLRVEKFAVIAALKSMERAEVAILVLDAQRGVTDQDKRIGSYALDAGCGLIFAVN 319
Cdd:COG1160   216 TPFE-RDGKKYTLIDTAGIRRKGKVDEGIEKYSVLRTLRAIERADVVLLVIDATEGITEQDLKIAGLALEAGKALVIVVN 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 320 KWDTMPPGQQTIRSFQEGLAIHFPRLTHCPVIFLSAKSGKRVEKLLPTARKVRQATQMRVSTSNLNRWLEQAIEKKAPPR 399
Cdd:COG1160   295 KWDLVEKDRKTREELEKEIRRRLPFLDYAPIVFISALTGQGVDKLLEAVDEVYESANKRISTSKLNRVLEEAVERHPPPA 374
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1174098179 400 AAGRPVKIRYCSQVSSSPPTFVFFCNRPEKMEESYKRYLENQLREAFALDGTPIRIMFKGGENP 463
Cdd:COG1160   375 VKGRRLKIYYATQVGTRPPTFVLFVNDPELLPFSYKRYLENQLREAFGFEGTPIRIEFRKRKNP 438
 
Name Accession Description Interval E-value
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
1-463 0e+00

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 678.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   1 MSklPLVALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTGGFEADPGETMVSLIRGQTIL 80
Cdd:COG1160     1 MS--PVVAIVGRPNVGKSTLFNRLTGRRDAIVDDTPGVTRDRIYGEAEWGGREFTLIDTGGIEPDDDDGLEAEIREQAEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  81 AIEEADIIVFVVDGSTGPLTDDYAIASHLRSSGKPVIIAANKSEKKAATASI-EFHELGMEPIIPISSAHGLGIGDLLET 159
Cdd:COG1160    79 AIEEADVILFVVDGRAGLTPLDEEIAKLLRRSGKPVILVVNKVDGPKREADAaEFYSLGLGEPIPISAEHGRGVGDLLDA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 160 LEEmtdamegfcrqpeeqLLPLEVEQENPEvareprfkGPLRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSID 239
Cdd:COG1160   159 VLE---------------LLPEEEEEEEED--------DPIKIAIVGRPNVGKSSLINALLGEERVIVSDIAGTTRDSID 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 240 VPITdANGETVILVDTAGIRRKSRVSLRVEKFAVIAALKSMERAEVAILVLDAQRGVTDQDKRIGSYALDAGCGLIFAVN 319
Cdd:COG1160   216 TPFE-RDGKKYTLIDTAGIRRKGKVDEGIEKYSVLRTLRAIERADVVLLVIDATEGITEQDLKIAGLALEAGKALVIVVN 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 320 KWDTMPPGQQTIRSFQEGLAIHFPRLTHCPVIFLSAKSGKRVEKLLPTARKVRQATQMRVSTSNLNRWLEQAIEKKAPPR 399
Cdd:COG1160   295 KWDLVEKDRKTREELEKEIRRRLPFLDYAPIVFISALTGQGVDKLLEAVDEVYESANKRISTSKLNRVLEEAVERHPPPA 374
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1174098179 400 AAGRPVKIRYCSQVSSSPPTFVFFCNRPEKMEESYKRYLENQLREAFALDGTPIRIMFKGGENP 463
Cdd:COG1160   375 VKGRRLKIYYATQVGTRPPTFVLFVNDPELLPFSYKRYLENQLREAFGFEGTPIRIEFRKRKNP 438
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
4-462 0e+00

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 639.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   4 LPLVALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTGGFEADPgETMVSLIRGQTILAIE 83
Cdd:PRK00093    1 KPVVAIVGRPNVGKSTLFNRLTGKRDAIVADTPGVTRDRIYGEAEWLGREFILIDTGGIEPDD-DGFEKQIREQAELAIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  84 EADIIVFVVDGSTGPLTDDYAIASHLRSSGKPVIIAANKSE-KKAATASIEFHELGMEPIIPISSAHGLGIGDLLETLEE 162
Cdd:PRK00093   80 EADVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDgPDEEADAYEFYSLGLGEPYPISAEHGRGIGDLLDAILE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 163 mtdamegfcrqpeeqLLPLEVEQENPEvareprfkGPLRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPI 242
Cdd:PRK00093  160 ---------------ELPEEEEEDEED--------EPIKIAIIGRPNVGKSSLINALLGEERVIVSDIAGTTRDSIDTPF 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 243 TDaNGETVILVDTAGIRRKSRVSLRVEKFAVIAALKSMERAEVAILVLDAQRGVTDQDKRIGSYALDAGCGLIFAVNKWD 322
Cdd:PRK00093  217 ER-DGQKYTLIDTAGIRRKGKVTEGVEKYSVIRTLKAIERADVVLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKWD 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 323 TMPpgQQTIRSFQEGLAIHFPRLTHCPVIFLSAKSGKRVEKLLPTARKVRQATQMRVSTSNLNRWLEQAIEKKAPPRAAG 402
Cdd:PRK00093  296 LVD--EKTMEEFKKELRRRLPFLDYAPIVFISALTGQGVDKLLEAIDEAYENANRRISTSVLNRVLEEAVERHPPPLVKG 373
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 403 RPVKIRYCSQVSSSPPTFVFFCNRPEKMEESYKRYLENQLREAFALDGTPIRIMFKGGEN 462
Cdd:PRK00093  374 RRLKIKYATQVGTNPPTFVLFVNDPELLPFSYKRYLENQLREAFDFEGTPIRLEFREKKN 433
GTPase_EngA TIGR03594
ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase ...
7-458 0e+00

ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase with a duplication of its GTP-binding domain. It is broadly to universally distributed among bacteria. It appears to function in ribosome biogenesis or stability. [Protein synthesis, Other]


Pssm-ID: 274667 [Multi-domain]  Cd Length: 428  Bit Score: 611.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTGGFEADpGETMVSLIRGQTILAIEEAD 86
Cdd:TIGR03594   1 VAIVGRPNVGKSTLFNRLTGKRDAIVDDTPGVTRDRIYGDAEWGGREFILIDTGGIEED-DDGIDAQIREQAEIAIEEAD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  87 IIVFVVDGSTGPLTDDYAIASHLRSSGKPVIIAANKSEKKAATASI-EFHELGMEPIIPISSAHGLGIGDLLETLEEmtd 165
Cdd:TIGR03594  80 VILFVVDGREGLTPEDEEIAKWLRKSGKPVILVANKIDGPKEDADAaEFYSLGFGEPIPISAEHGRGIGDLLDAILE--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 166 amegfcrqpeeqLLPLEVEQENPEvareprfKGPLRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPITdA 245
Cdd:TIGR03594 157 ------------LLPEEEEEEEEE-------EDPIKIAIIGRPNVGKSTLVNALLGEERVIVSDIAGTTRDSIDIPFE-R 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 246 NGETVILVDTAGIRRKSRVSLRVEKFAVIAALKSMERAEVAILVLDAQRGVTDQDKRIGSYALDAGCGLIFAVNKWDTMP 325
Cdd:TIGR03594 217 DGKKYTLIDTAGIRRKGKVTEGVEKYSVLRTLKAIERADVVLLVLDATEGITEQDLRIAGLALEAGKALVIVVNKWDLVE 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 326 PgQQTIRSFQEGLAIHFPRLTHCPVIFLSAKSGKRVEKLLPTARKVRQATQMRVSTSNLNRWLEQAIEKKAPPRAAGRPV 405
Cdd:TIGR03594 297 D-EKTRKEIKKELRRKLPFLDFAPIVFISALTGQGVDKLLDAIDKVYESANKRISTSKLNRVLEEAVAAHPPPLVGGRRV 375
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1174098179 406 KIRYCSQVSSSPPTFVFFCNRPEKMEESYKRYLENQLREAFALDGTPIRIMFK 458
Cdd:TIGR03594 376 KIKYATQVGTNPPTFVLFGNRPELLPFSYKRYLENQFREAFGFEGTPIRLEFK 428
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
198-372 2.75e-80

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: 246.96  E-value: 2.75e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 198 GPLRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPITDaNGETVILVDTAGIRRKSRVSLRVEKFAVIAAL 277
Cdd:cd01895     1 DPIKIAIIGRPNVGKSSLLNALLGEERVIVSDIAGTTRDSIDVPFEY-DGQKYTLIDTAGIRKKGKVTEGIEKYSVLRTL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 278 KSMERAEVAILVLDAQRGVTDQDKRIGSYALDAGCGLIFAVNKWDTMPPGQQTIRSFQEGLAIHFPRLTHCPVIFLSAKS 357
Cdd:cd01895    80 KAIERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVEKDEKTMKEFEKELRRKLPFLDYAPIVFISALT 159
                         170
                  ....*....|....*
gi 1174098179 358 GKRVEKLLPTARKVR 372
Cdd:cd01895   160 GQGVDKLFDAIKEVY 174
KH_dom-like pfam14714
KH-domain-like of EngA bacterial GTPase enzymes, C-terminal; The KH-like domain at the ...
378-458 2.54e-43

KH-domain-like of EngA bacterial GTPase enzymes, C-terminal; The KH-like domain at the C-terminus of the EngA subfamily of essential bacterial GTPases has a unique domain structure position. The two adjacent GTPase domains (GD1 and GD2), two domains of family MMR_HSR1, pfam01926, pack at either side of the C-terminal domain. This C-terminal domain resembles a KH domain but is missing the distinctive RNA recognition elements. Conserved motifs of the nucleotide binding site of GD1 are integral parts of the GD1-KH domain interface, suggesting the interactions between these two domains are directly influenced by the GTP/GDP cycling of the protein. In contrast, the GD2-KH domain interface is distal to the GDP binding site of GD2. This family has not been added to the KH clan since SCOP classifies it separately due to its missing the key KH motif/fold.


Pssm-ID: 464277 [Multi-domain]  Cd Length: 81  Bit Score: 147.55  E-value: 2.54e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 378 RVSTSNLNRWLEQAIEKKAPPRAAGRPVKIRYCSQVSSSPPTFVFFCNRPEKMEESYKRYLENQLREAFALDGTPIRIMF 457
Cdd:pfam14714   1 RISTSELNRVLEEAVARHPPPSVKGKRLKIYYATQVGTRPPTFVLFVNDPELVPFSYKRYLENQLREAFGFEGTPIRLIF 80

                  .
gi 1174098179 458 K 458
Cdd:pfam14714  81 R 81
 
Name Accession Description Interval E-value
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
1-463 0e+00

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 678.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   1 MSklPLVALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTGGFEADPGETMVSLIRGQTIL 80
Cdd:COG1160     1 MS--PVVAIVGRPNVGKSTLFNRLTGRRDAIVDDTPGVTRDRIYGEAEWGGREFTLIDTGGIEPDDDDGLEAEIREQAEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  81 AIEEADIIVFVVDGSTGPLTDDYAIASHLRSSGKPVIIAANKSEKKAATASI-EFHELGMEPIIPISSAHGLGIGDLLET 159
Cdd:COG1160    79 AIEEADVILFVVDGRAGLTPLDEEIAKLLRRSGKPVILVVNKVDGPKREADAaEFYSLGLGEPIPISAEHGRGVGDLLDA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 160 LEEmtdamegfcrqpeeqLLPLEVEQENPEvareprfkGPLRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSID 239
Cdd:COG1160   159 VLE---------------LLPEEEEEEEED--------DPIKIAIVGRPNVGKSSLINALLGEERVIVSDIAGTTRDSID 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 240 VPITdANGETVILVDTAGIRRKSRVSLRVEKFAVIAALKSMERAEVAILVLDAQRGVTDQDKRIGSYALDAGCGLIFAVN 319
Cdd:COG1160   216 TPFE-RDGKKYTLIDTAGIRRKGKVDEGIEKYSVLRTLRAIERADVVLLVIDATEGITEQDLKIAGLALEAGKALVIVVN 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 320 KWDTMPPGQQTIRSFQEGLAIHFPRLTHCPVIFLSAKSGKRVEKLLPTARKVRQATQMRVSTSNLNRWLEQAIEKKAPPR 399
Cdd:COG1160   295 KWDLVEKDRKTREELEKEIRRRLPFLDYAPIVFISALTGQGVDKLLEAVDEVYESANKRISTSKLNRVLEEAVERHPPPA 374
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1174098179 400 AAGRPVKIRYCSQVSSSPPTFVFFCNRPEKMEESYKRYLENQLREAFALDGTPIRIMFKGGENP 463
Cdd:COG1160   375 VKGRRLKIYYATQVGTRPPTFVLFVNDPELLPFSYKRYLENQLREAFGFEGTPIRIEFRKRKNP 438
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
4-462 0e+00

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 639.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   4 LPLVALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTGGFEADPgETMVSLIRGQTILAIE 83
Cdd:PRK00093    1 KPVVAIVGRPNVGKSTLFNRLTGKRDAIVADTPGVTRDRIYGEAEWLGREFILIDTGGIEPDD-DGFEKQIREQAELAIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  84 EADIIVFVVDGSTGPLTDDYAIASHLRSSGKPVIIAANKSE-KKAATASIEFHELGMEPIIPISSAHGLGIGDLLETLEE 162
Cdd:PRK00093   80 EADVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDgPDEEADAYEFYSLGLGEPYPISAEHGRGIGDLLDAILE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 163 mtdamegfcrqpeeqLLPLEVEQENPEvareprfkGPLRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPI 242
Cdd:PRK00093  160 ---------------ELPEEEEEDEED--------EPIKIAIIGRPNVGKSSLINALLGEERVIVSDIAGTTRDSIDTPF 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 243 TDaNGETVILVDTAGIRRKSRVSLRVEKFAVIAALKSMERAEVAILVLDAQRGVTDQDKRIGSYALDAGCGLIFAVNKWD 322
Cdd:PRK00093  217 ER-DGQKYTLIDTAGIRRKGKVTEGVEKYSVIRTLKAIERADVVLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKWD 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 323 TMPpgQQTIRSFQEGLAIHFPRLTHCPVIFLSAKSGKRVEKLLPTARKVRQATQMRVSTSNLNRWLEQAIEKKAPPRAAG 402
Cdd:PRK00093  296 LVD--EKTMEEFKKELRRRLPFLDYAPIVFISALTGQGVDKLLEAIDEAYENANRRISTSVLNRVLEEAVERHPPPLVKG 373
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 403 RPVKIRYCSQVSSSPPTFVFFCNRPEKMEESYKRYLENQLREAFALDGTPIRIMFKGGEN 462
Cdd:PRK00093  374 RRLKIKYATQVGTNPPTFVLFVNDPELLPFSYKRYLENQLREAFDFEGTPIRLEFREKKN 433
GTPase_EngA TIGR03594
ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase ...
7-458 0e+00

ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase with a duplication of its GTP-binding domain. It is broadly to universally distributed among bacteria. It appears to function in ribosome biogenesis or stability. [Protein synthesis, Other]


Pssm-ID: 274667 [Multi-domain]  Cd Length: 428  Bit Score: 611.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTGGFEADpGETMVSLIRGQTILAIEEAD 86
Cdd:TIGR03594   1 VAIVGRPNVGKSTLFNRLTGKRDAIVDDTPGVTRDRIYGDAEWGGREFILIDTGGIEED-DDGIDAQIREQAEIAIEEAD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  87 IIVFVVDGSTGPLTDDYAIASHLRSSGKPVIIAANKSEKKAATASI-EFHELGMEPIIPISSAHGLGIGDLLETLEEmtd 165
Cdd:TIGR03594  80 VILFVVDGREGLTPEDEEIAKWLRKSGKPVILVANKIDGPKEDADAaEFYSLGFGEPIPISAEHGRGIGDLLDAILE--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 166 amegfcrqpeeqLLPLEVEQENPEvareprfKGPLRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPITdA 245
Cdd:TIGR03594 157 ------------LLPEEEEEEEEE-------EDPIKIAIIGRPNVGKSTLVNALLGEERVIVSDIAGTTRDSIDIPFE-R 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 246 NGETVILVDTAGIRRKSRVSLRVEKFAVIAALKSMERAEVAILVLDAQRGVTDQDKRIGSYALDAGCGLIFAVNKWDTMP 325
Cdd:TIGR03594 217 DGKKYTLIDTAGIRRKGKVTEGVEKYSVLRTLKAIERADVVLLVLDATEGITEQDLRIAGLALEAGKALVIVVNKWDLVE 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 326 PgQQTIRSFQEGLAIHFPRLTHCPVIFLSAKSGKRVEKLLPTARKVRQATQMRVSTSNLNRWLEQAIEKKAPPRAAGRPV 405
Cdd:TIGR03594 297 D-EKTRKEIKKELRRKLPFLDFAPIVFISALTGQGVDKLLDAIDKVYESANKRISTSKLNRVLEEAVAAHPPPLVGGRRV 375
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1174098179 406 KIRYCSQVSSSPPTFVFFCNRPEKMEESYKRYLENQLREAFALDGTPIRIMFK 458
Cdd:TIGR03594 376 KIKYATQVGTNPPTFVLFGNRPELLPFSYKRYLENQFREAFGFEGTPIRLEFK 428
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
4-455 5.79e-113

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 341.56  E-value: 5.79e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   4 LPLVALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTGGFEADpGETMVSLIRGQTILAIE 83
Cdd:PRK03003   38 LPVVAVVGRPNVGKSTLVNRILGRREAVVEDVPGVTRDRVSYDAEWNGRRFTVVDTGGWEPD-AKGLQASVAEQAEVAMR 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  84 EADIIVFVVDGSTGPLTDDYAIASHLRSSGKPVIIAANK--SEKKAATASiEFHELGM-EPiIPISSAHGLGIGDLLETL 160
Cdd:PRK03003  117 TADAVLFVVDATVGATATDEAVARVLRRSGKPVILAANKvdDERGEADAA-ALWSLGLgEP-HPVSALHGRGVGDLLDAV 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 161 eemtdamegfcrqpeeqllpLEVEQENPEVAREPRfkGPLRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDV 240
Cdd:PRK03003  195 --------------------LAALPEVPRVGSASG--GPRRVALVGKPNVGKSSLLNKLAGEERSVVDDVAGTTVDPVDS 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 241 PITdANGETVILVDTAGIRRKSRVSLRVEKFAVIAALKSMERAEVAILVLDAQRGVTDQDKRIGSYALDAGCGLIFAVNK 320
Cdd:PRK03003  253 LIE-LGGKTWRFVDTAGLRRRVKQASGHEYYASLRTHAAIEAAEVAVVLIDASEPISEQDQRVLSMVIEAGRALVLAFNK 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 321 WDTMPPGQQTI--RSFQEGLAihfpRLTHCPVIFLSAKSGKRVEKLLPTARKVRQATQMRVSTSNLNRWLEQAIEKKAPP 398
Cdd:PRK03003  332 WDLVDEDRRYYleREIDRELA----QVPWAPRVNISAKTGRAVDKLVPALETALESWDTRIPTGRLNAWLGELVAATPPP 407
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1174098179 399 RAAGRPVKIRYCSQVSSSPPTFVFFCNRPekMEESYKRYLENQLREAFALDGTPIRI 455
Cdd:PRK03003  408 VRGGKQPRILFATQASTRPPTFVLFTTGF--LEAGYRRFLERRLRETFGFEGSPIRI 462
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
7-455 5.62e-107

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 333.68  E-value: 5.62e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTGGFEADpGETMVSLIRGQTILAIEEAD 86
Cdd:PRK09518  278 VAIVGRPNVGKSTLVNRILGRREAVVEDTPGVTRDRVSYDAEWAGTDFKLVDTGGWEAD-VEGIDSAIASQAQIAVSLAD 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  87 IIVFVVDGSTGPLTDDYAIASHLRSSGKPVIIAANKSEKKAATASI-EFHELGMEPIIPISSAHGLGIGDLLETLeemtd 165
Cdd:PRK09518  357 AVVFVVDGQVGLTSTDERIVRMLRRAGKPVVLAVNKIDDQASEYDAaEFWKLGLGEPYPISAMHGRGVGDLLDEA----- 431
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 166 amegfcrqpeeqllpLEVEQENPEVAREPRFKGPLRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDvPITDA 245
Cdd:PRK09518  432 ---------------LDSLKVAEKTSGFLTPSGLRRVALVGRPNVGKSSLLNQLTHEERAVVNDLAGTTRDPVD-EIVEI 495
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 246 NGETVILVDTAGIRRKSRVSLRVEKFAVIAALKSMERAEVAILVLDAQRGVTDQDKRIGSYALDAGCGLIFAVNKWDTMp 325
Cdd:PRK09518  496 DGEDWLFIDTAGIKRRQHKLTGAEYYSSLRTQAAIERSELALFLFDASQPISEQDLKVMSMAVDAGRALVLVFNKWDLM- 574
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 326 pgQQTIRSFQEGL-AIHFPRLTHCPVIFLSAKSGKRVEKLLPTARKVRQATQMRVSTSNLNRWLEQAIEKKAPPRAAGRP 404
Cdd:PRK09518  575 --DEFRRQRLERLwKTEFDRVTWARRVNLSAKTGWHTNRLAPAMQEALESWDQRIPTGKLNAFLGKIQAEHPHPLRGGKQ 652
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1174098179 405 VKIRYCSQVSSSPPTFVFFCNrpEKMEESYKRYLENQLREAFALDGTPIRI 455
Cdd:PRK09518  653 PRILFATQASTRPPRFVIFTT--GFLEHGYRRFLERSLREEFGFEGSPIQI 701
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
198-372 2.75e-80

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: 246.96  E-value: 2.75e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 198 GPLRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPITDaNGETVILVDTAGIRRKSRVSLRVEKFAVIAAL 277
Cdd:cd01895     1 DPIKIAIIGRPNVGKSSLLNALLGEERVIVSDIAGTTRDSIDVPFEY-DGQKYTLIDTAGIRKKGKVTEGIEKYSVLRTL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 278 KSMERAEVAILVLDAQRGVTDQDKRIGSYALDAGCGLIFAVNKWDTMPPGQQTIRSFQEGLAIHFPRLTHCPVIFLSAKS 357
Cdd:cd01895    80 KAIERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVEKDEKTMKEFEKELRRKLPFLDYAPIVFISALT 159
                         170
                  ....*....|....*
gi 1174098179 358 GKRVEKLLPTARKVR 372
Cdd:cd01895   160 GQGVDKLFDAIKEVY 174
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
8-162 8.29e-77

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: 237.33  E-value: 8.29e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   8 ALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTGGFEADPgETMVSLIRGQTILAIEEADI 87
Cdd:cd01894     1 AIVGRPNVGKSTLFNRLTGRRDAIVSDTPGVTRDRKYGEAEWGGREFILIDTGGIEPDD-EGISKEIREQAEIAIEEADV 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1174098179  88 IVFVVDGSTGPLTDDYAIASHLRSSGKPVIIAANKSEKKAATASI-EFHELGMEPIIPISSAHGLGIGDLLETLEE 162
Cdd:cd01894    80 ILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNIKEEEEAaEFYSLGFGEPIPISAEHGRGIGDLLDAILE 155
KH_dom-like pfam14714
KH-domain-like of EngA bacterial GTPase enzymes, C-terminal; The KH-like domain at the ...
378-458 2.54e-43

KH-domain-like of EngA bacterial GTPase enzymes, C-terminal; The KH-like domain at the C-terminus of the EngA subfamily of essential bacterial GTPases has a unique domain structure position. The two adjacent GTPase domains (GD1 and GD2), two domains of family MMR_HSR1, pfam01926, pack at either side of the C-terminal domain. This C-terminal domain resembles a KH domain but is missing the distinctive RNA recognition elements. Conserved motifs of the nucleotide binding site of GD1 are integral parts of the GD1-KH domain interface, suggesting the interactions between these two domains are directly influenced by the GTP/GDP cycling of the protein. In contrast, the GD2-KH domain interface is distal to the GDP binding site of GD2. This family has not been added to the KH clan since SCOP classifies it separately due to its missing the key KH motif/fold.


Pssm-ID: 464277 [Multi-domain]  Cd Length: 81  Bit Score: 147.55  E-value: 2.54e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 378 RVSTSNLNRWLEQAIEKKAPPRAAGRPVKIRYCSQVSSSPPTFVFFCNRPEKMEESYKRYLENQLREAFALDGTPIRIMF 457
Cdd:pfam14714   1 RISTSELNRVLEEAVARHPPPSVKGKRLKIYYATQVGTRPPTFVLFVNDPELVPFSYKRYLENQLREAFGFEGTPIRLIF 80

                  .
gi 1174098179 458 K 458
Cdd:pfam14714  81 R 81
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
7-122 3.46e-37

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: 132.36  E-value: 3.46e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRdALVDDTPGLTRDRQYGIMKRGDTPFPMVDTGGFeadPGETMVSLIRGQTILAIEEAD 86
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGAK-AIVSDYPGTTRDPNEGRLELKGKQIILVDTPGL---IEGASEGEGLGRAFLAIIEAD 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1174098179  87 IIVFVVDGSTGPLTDDYAIASHLRSSGKPVIIAANK 122
Cdd:pfam01926  78 LILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
8-163 6.68e-34

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: 125.05  E-value: 6.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   8 ALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQYGIM-KRGDTPFPMVDTGGF--EADPGETMVSLIRgqtiLAIEE 84
Cdd:cd00880     1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRKEWeLLPLGPVVLIDTPGLdeEGGLGRERVEEAR----QVADR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  85 ADIIVFVVDGSTGPLTDDYAIAShLRSSGKPVIIAANK------SEKKAATASIEFHELGMEPIIPISSAHGLGIGDLLE 158
Cdd:cd00880    77 ADLVLLVVDSDLTPVEEEAKLGL-LRERGKPVLLVLNKidlvpeSEEEELLRERKLELLPDLPVIAVSALPGEGIDELRK 155

                  ....*
gi 1174098179 159 TLEEM 163
Cdd:cd00880   156 KIAEL 160
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
200-365 9.14e-34

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: 124.53  E-value: 9.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 200 LRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPItDANGETVILVDTAGIRRKSRVslrVEKFAVIAALKS 279
Cdd:cd04164     4 IKVVIAGKPNVGKSSLLNALAGRDRAIVSDIAGTTRDVIEEEI-DLGGIPVRLIDTAGLRETEDE---IEKIGIERAREA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 280 MERAEVAILVLDAQRGVTDQDKRIgsYALDAGCGLIFAVNKWDTMPPgqqtirsfqeglAIHFPRLTHCPVIFLSAKSGK 359
Cdd:cd04164    80 IEEADLVLLVVDASEGLDEEDLEI--LELPAKKPVIVVLNKSDLLSD------------AEGISELNGKPIIAISAKTGE 145

                  ....*.
gi 1174098179 360 RVEKLL 365
Cdd:cd04164   146 GIDELK 151
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
200-365 3.15e-31

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: 125.17  E-value: 3.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 200 LRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPItDANGETVILVDTAGIRRKSRVslrVEKFAVIAALKS 279
Cdd:COG0486   214 IKVVIVGRPNVGKSSLLNALLGEERAIVTDIAGTTRDVIEERI-NIGGIPVRLIDTAGLRETEDE---VEKIGIERAREA 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 280 MERAEVAILVLDAQRGVTDQDKRIgsYALDAGCGLIFAVNKWDTMPPGQQTIRSFQEGlaihfprlthcPVIFLSAKSGK 359
Cdd:COG0486   290 IEEADLVLLLLDASEPLTEEDEEI--LEKLKDKPVIVVLNKIDLPSEADGELKSLPGE-----------PVIAISAKTGE 356

                  ....*.
gi 1174098179 360 RVEKLL 365
Cdd:COG0486   357 GIDELK 362
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
200-365 9.01e-31

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: 121.43  E-value: 9.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 200 LRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPItDANGETVILVDTAGIRRKSRVslrVEKFAVIAALKS 279
Cdd:pfam12631  95 IKVVIVGKPNVGKSSLLNALLGEERAIVTDIPGTTRDVIEETI-NIGGIPLRLIDTAGIRETDDE---VEKIGIERAREA 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 280 MERAEVAILVLDAQRGVTDQDKRIgSYALDAGCGLIFAVNKWDTMPPGQQTIrsfqeglaihfpRLTHCPVIFLSAKSGK 359
Cdd:pfam12631 171 IEEADLVLLVLDASRPLDEEDLEI-LELLKDKKPIIVVLNKSDLLGEIDELE------------ELKGKPVLAISAKTGE 237

                  ....*.
gi 1174098179 360 RVEKLL 365
Cdd:pfam12631 238 GLDELE 243
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
7-163 5.08e-30

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: 114.51  E-value: 5.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTGGF--EADPGETMVslIRgQTILAIEE 84
Cdd:cd04164     6 VVIAGKPNVGKSSLLNALAGRDRAIVSDIAGTTRDVIEEEIDLGGIPVRLIDTAGLreTEDEIEKIG--IE-RAREAIEE 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1174098179  85 ADIIVFVVDGSTGPLTDDYAIasHLRSSGKPVIIAANKSEKkaATASIEFHELGMEPIIPISSAHGLGIGDLLETLEEM 163
Cdd:cd04164    83 ADLVLLVVDASEGLDEEDLEI--LELPAKKPVIVVLNKSDL--LSDAEGISELNGKPIIAISAKTGEGIDELKEALLEL 157
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
7-163 1.66e-29

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: 113.33  E-value: 1.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTGGF---EADPGETMVSLIRGqtilAIE 83
Cdd:cd04163     6 VAIIGRPNVGKSTLLNALVGQKISIVSPKPQTTRNRIRGIYTDDDAQIIFVDTPGIhkpKKKLGERMVKAAWS----ALK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  84 EADIIVFVVDGSTGPLTDDYAIASHLRSSGKPVIIAANK----SEKKAATASIEFHELGM--EPIIPISSAHGLGIGDLL 157
Cdd:cd04163    82 DVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKidlvKDKEDLLPLLEKLKELHpfAEIFPISALKGENVDELL 161

                  ....*.
gi 1174098179 158 ETLEEM 163
Cdd:cd04163   162 EYIVEY 167
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
7-163 7.47e-29

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 115.09  E-value: 7.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTGGFEAdP----GETMVSLIRGqtilAI 82
Cdd:COG1159     6 VAIVGRPNVGKSTLLNALVGQKVSIVSPKPQTTRHRIRGIVTREDAQIVFVDTPGIHK-PkrklGRRMNKAAWS----AL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  83 EEADIIVFVVDGSTGPLTDDYAIASHLRSSGKPVIIAANKSE--KKAATASI--EFHELGM-EPIIPISSAHGLGIGDLL 157
Cdd:COG1159    81 EDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDlvKKEELLPLlaEYSELLDfAEIVPISALKGDNVDELL 160

                  ....*.
gi 1174098179 158 ETLEEM 163
Cdd:COG1159   161 DEIAKL 166
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
201-320 1.36e-28

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: 109.25  E-value: 1.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 201 RLAVVGCPNAGKSSLVNRLVGEeRLLASEIAGTTRDSIDVPITDaNGETVILVDTAGIrrksrVSLRVEKFAVIAALKSM 280
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGA-KAIVSDYPGTTRDPNEGRLEL-KGKQIILVDTPGL-----IEGASEGEGLGRAFLAI 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1174098179 281 ERAEVAILVLDAQRGVTDQDKRIGSYALDAGCGLIFAVNK 320
Cdd:pfam01926  74 IEADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
era PRK00089
GTPase Era; Reviewed
7-163 1.83e-28

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 113.99  E-value: 1.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTGGFEAdP----GETMVSLIRGqtilAI 82
Cdd:PRK00089    8 VAIVGRPNVGKSTLLNALVGQKISIVSPKPQTTRHRIRGIVTEDDAQIIFVDTPGIHK-PkralNRAMNKAAWS----SL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  83 EEADIIVFVVDGSTGPLTDDYAIASHLRSSGKPVIIAANK----SEKKAATASIEF--HELGMEPIIPISSAHGLGIGDL 156
Cdd:PRK00089   83 KDVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKidlvKDKEELLPLLEElsELMDFAEIVPISALKGDNVDEL 162

                  ....*..
gi 1174098179 157 LETLEEM 163
Cdd:PRK00089  163 LDVIAKY 169
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
7-163 5.57e-28

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: 115.93  E-value: 5.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRD--RQY----GImkrgdtPFPMVDTGGFE--ADPGETMvslirGQ- 77
Cdd:COG0486   216 VVIVGRPNVGKSSLLNALLGEERAIVTDIAGTTRDviEERinigGI------PVRLIDTAGLRetEDEVEKI-----GIe 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  78 -TILAIEEADIIVFVVDGSTGPLTDDYAIASHLRssGKPVIIAANKSEKKAAtASIEFHELGMEPIIPISSAHGLGIGDL 156
Cdd:COG0486   285 rAREAIEEADLVLLLLDASEPLTEEDEEILEKLK--DKPVIVVLNKIDLPSE-ADGELKSLPGEPVIAISAKTGEGIDEL 361

                  ....*..
gi 1174098179 157 LETLEEM 163
Cdd:COG0486   362 KEAILEL 368
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
200-365 3.32e-27

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 113.67  E-value: 3.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 200 LRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPItDANGETVILVDTAGIRRKSRVslrVEKFAVIAALKS 279
Cdd:PRK05291  216 LKVVIAGRPNVGKSSLLNALLGEERAIVTDIAGTTRDVIEEHI-NLDGIPLRLIDTAGIRETDDE---VEKIGIERSREA 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 280 MERAEVAILVLDAQRGVTDQDKRIgsYALDAGCGLIFAVNKWDTMPPGQQTIrsfqeglaihfprLTHCPVIFLSAKSGK 359
Cdd:PRK05291  292 IEEADLVLLVLDASEPLTEEDDEI--LEELKDKPVIVVLNKADLTGEIDLEE-------------ENGKPVIRISAKTGE 356

                  ....*.
gi 1174098179 360 RVEKLL 365
Cdd:PRK05291  357 GIDELR 362
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
203-365 1.41e-26

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 105.02  E-value: 1.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 203 AVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPITDANGETVILVDTAGIRRKSRV-SLRVEKfaviaALKSME 281
Cdd:cd00880     1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRKEWELLPLGPVVLIDTPGLDEEGGLgRERVEE-----ARQVAD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 282 RAEVAILVLDAQRGVTDQDKRIGSyALDAGCGLIFAVNKWDtMPPGQQTIRSFQEGLAIHFPrltHCPVIFLSAKSGKRV 361
Cdd:cd00880    76 RADLVLLVVDSDLTPVEEEAKLGL-LRERGKPVLLVLNKID-LVPESEEEELLRERKLELLP---DLPVIAVSALPGEGI 150

                  ....
gi 1174098179 362 EKLL 365
Cdd:cd00880   151 DELR 154
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
7-179 3.13e-25

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 107.89  E-value: 3.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTGGFE--ADP----GetmvslIRgQTIL 80
Cdd:PRK05291  218 VVIAGRPNVGKSSLLNALLGEERAIVTDIAGTTRDVIEEHINLDGIPLRLIDTAGIRetDDEvekiG------IE-RSRE 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  81 AIEEADIIVFVVDGSTGPLTDDYAIAshLRSSGKPVIIAANKSEKKAATASIefhELGMEPIIPISSAHGLGIGDLLETL 160
Cdd:PRK05291  291 AIEEADLVLLVLDASEPLTEEDDEIL--EELKDKPVIVVLNKADLTGEIDLE---EENGKPVIRISAKTGEGIDELREAI 365
                         170
                  ....*....|....*....
gi 1174098179 161 EEMtdAMEGFCRQPEEQLL 179
Cdd:PRK05291  366 KEL--AFGGFGGNQEGVFL 382
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
7-163 6.41e-25

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: 104.87  E-value: 6.41e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRD--RQY----GImkrgdtPFPMVDTGGF--EADPGETMvslirGQ- 77
Cdd:pfam12631  97 VVIVGKPNVGKSSLLNALLGEERAIVTDIPGTTRDviEETinigGI------PLRLIDTAGIreTDDEVEKI-----GIe 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  78 -TILAIEEADIIVFVVDGSTGPLTDDYAIASHLRsSGKPVIIAANKSEKkaATASIEFHELGMEPIIPISSAHGLGIGDL 156
Cdd:pfam12631 166 rAREAIEEADLVLLVLDASRPLDEEDLEILELLK-DKKPIIVVLNKSDL--LGEIDELEELKGKPVLAISAKTGEGLDEL 242

                  ....*..
gi 1174098179 157 LETLEEM 163
Cdd:pfam12631 243 EEAIKEL 249
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
8-160 9.96e-24

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: 97.14  E-value: 9.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   8 ALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQYG--IMKRGDTPFPMVDTGGFEadpgETMVSLIRGQTILAIEEA 85
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYvkELDKGKVKLVLVDTPGLD----EFGGLGREELARLLLRGA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  86 DIIVFVVDGSTGPLTDD--YAIASHLRSSGKPVIIAANK------SEKKAATASIEFHELGMEPIIPISSAHGLGIGDLL 157
Cdd:cd00882    77 DLILLVVDSTDRESEEDakLLILRRLRKEGIPIILVGNKidlleeREVEELLRLEELAKILGVPVFEVSAKTGEGVDELF 156

                  ...
gi 1174098179 158 ETL 160
Cdd:cd00882   157 EKL 159
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
7-161 2.23e-23

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: 96.29  E-value: 2.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRD-RQYGIMKRGDT-PFPMVDTGGFEAdpGETMVSLIRGQTILAIEE 84
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNyVTTVIEEDGKTyKFNLLDTAGQED--YDAIRRLYYPQVERSLRV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  85 ADIIVFVVDGSTGPLTDDYAIAsHLRSSGKPVIIAANKSEKKAATAS----IEFHELGMEPIIPISSAHGLGIGDLLETL 160
Cdd:TIGR00231  82 FDIVILVLDVEEILEKQTKEII-HHADSGVPIILVGNKIDLKDADLKthvaSEFAKLNGEPIIPLSAETGKNIDSAFKIV 160

                  .
gi 1174098179 161 E 161
Cdd:TIGR00231 161 E 161
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
203-365 9.17e-22

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: 91.75  E-value: 9.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 203 AVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPIT-DANGETVILVDTAGIRRKSRVSLRVEkfaviaALKSME 281
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKElDKGKVKLVLVDTPGLDEFGGLGREEL------ARLLLR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 282 RAEVAILVLDAQRGVTDQDKRIGSYALDAGCG--LIFAVNKWDTMPPGQQTirsfQEGLAIHFPRLTHCPVIFLSAKSGK 359
Cdd:cd00882    75 GADLILLVVDSTDRESEEDAKLLILRRLRKEGipIILVGNKIDLLEEREVE----ELLRLEELAKILGVPVFEVSAKTGE 150

                  ....*.
gi 1174098179 360 RVEKLL 365
Cdd:cd00882   151 GVDELF 156
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
201-364 1.89e-20

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: 88.20  E-value: 1.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 201 RLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPITdANGET--VILVDTAGIRRKSrvslRVEKFAVIAALK 278
Cdd:TIGR00231   3 KIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIE-EDGKTykFNLLDTAGQEDYD----AIRRLYYPQVER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 279 SMERAEVAILVLDAQRGVTDQDKRIGSYAlDAGCGLIFAVNKWDtmppgqQTIRSFQEGLAIHFPRLTHCPVIFLSAKSG 358
Cdd:TIGR00231  78 SLRVFDIVILVLDVEEILEKQTKEIIHHA-DSGVPIILVGNKID------LKDADLKTHVASEFAKLNGEPIIPLSAETG 150

                  ....*.
gi 1174098179 359 KRVEKL 364
Cdd:TIGR00231 151 KNIDSA 156
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
203-324 2.17e-20

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: 87.49  E-value: 2.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 203 AVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPItDANGETVILVDTAGIrrkSRVSLRVEKFAVIAALKSMER 282
Cdd:cd01894     1 AIVGRPNVGKSTLFNRLTGRRDAIVSDTPGVTRDRKYGEA-EWGGREFILIDTGGI---EPDDEGISKEIREQAEIAIEE 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1174098179 283 AEVAILVLDAQRGVTDQDKRIGSYALDAGCGLIFAVNKWDTM 324
Cdd:cd01894    77 ADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNI 118
era PRK00089
GTPase Era; Reviewed
203-365 8.48e-20

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 89.34  E-value: 8.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 203 AVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPITDANGEtVILVDTAGIRRKSRvslRVEKFAVIAALKSMER 282
Cdd:PRK00089    9 AIVGRPNVGKSTLLNALVGQKISIVSPKPQTTRHRIRGIVTEDDAQ-IIFVDTPGIHKPKR---ALNRAMNKAAWSSLKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 283 AEVAILVLDAQRGVTDQDKRIGSYALDAGCGLIFAVNKWDTMPPgQQTIRSFQEGLAIHFPrltHCPVIFLSAKSGKRVE 362
Cdd:PRK00089   85 VDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVKD-KEELLPLLEELSELMD---FAEIVPISALKGDNVD 160

                  ...
gi 1174098179 363 KLL 365
Cdd:PRK00089  161 ELL 163
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
8-166 6.00e-19

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: 83.66  E-value: 6.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   8 ALVGRPNVGKSTLFNRLTRTRdALVDDTPGLTRDRQYGIMKRGDTPFPMVDTggfeadPGetMVSLiRGQTI-------- 79
Cdd:cd01879     1 ALVGNPNVGKTTLFNALTGAR-QKVGNWPGVTVEKKEGEFKLGGKEIEIVDL------PG--TYSL-TPYSEdekvardf 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  80 LAIEEADIIVFVVDgstgpltddyaiASHLRSS----------GKPVIIAANKS-EKKAATASIEF----HELGMePIIP 144
Cdd:cd01879    71 LLGEEPDLIVNVVD------------ATNLERNlyltlqllelGLPVVVALNMIdEAEKRGIKIDLdklsELLGV-PVVP 137
                         170       180
                  ....*....|....*....|..
gi 1174098179 145 ISSAHGLGIGDLLETLEEMTDA 166
Cdd:cd01879   138 TSARKGEGIDELLDAIAKLAES 159
mnmE_trmE_thdF TIGR00450
tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF ...
195-373 6.46e-19

tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF (thiophene and furan oxidation protein), is a GTPase involved in tRNA modification to create 5-methylaminomethyl-2-thiouridine in the wobble position of some tRNAs. This protein and GidA form an alpha2/beta2 heterotetramer. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273083 [Multi-domain]  Cd Length: 442  Bit Score: 89.08  E-value: 6.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 195 RFKGPLRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPItDANGETVILVDTAGIRRKSRvslRVEKFAVI 274
Cdd:TIGR00450 199 KLDDGFKLAIVGSPNVGKSSLLNALLKQDRAIVSDIKGTTRDVVEGDF-ELNGILIKLLDTAGIREHAD---FVERLGIE 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 275 AALKSMERAEVAILVLDAQRGVTDQDKRIgSYALDAGCGLIFAVNKWDTMPPGQQTirsfqeglaihFPRLTHCPVIFLS 354
Cdd:TIGR00450 275 KSFKAIKQADLVIYVLDASQPLTKDDFLI-IDLNKSKKPFILVLNKIDLKINSLEF-----------FVSSKVLNSSNLS 342
                         170
                  ....*....|....*....
gi 1174098179 355 AKSGKRVEKLLPTARKVRQ 373
Cdd:TIGR00450 343 AKQLKIKALVDLLTQKINA 361
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
203-365 6.51e-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: 83.66  E-value: 6.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 203 AVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPITDANGEtVILVDTAGIRRKSRvslRVEKFAVIAALKSMER 282
Cdd:cd04163     7 AIIGRPNVGKSTLLNALVGQKISIVSPKPQTTRNRIRGIYTDDDAQ-IIFVDTPGIHKPKK---KLGERMVKAAWSALKD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 283 AEVAILVLDAQRGVTDQDKRIgsyaLD----AGCGLIFAVNKWDTMPPGQQTIRSFQEGLAIHFPrlthCPVIFLSAKSG 358
Cdd:cd04163    83 VDLVLFVVDASEWIGEGDEFI----LEllkkSKTPVILVLNKIDLVKDKEDLLPLLEKLKELHPF----AEIFPISALKG 154

                  ....*..
gi 1174098179 359 KRVEKLL 365
Cdd:cd04163   155 ENVDELL 161
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
203-365 2.18e-18

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 85.43  E-value: 2.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 203 AVVGCPNAGKSSLVNRLVGEErlLA--SEIAGTTRDSIDVPITDANGEtVILVDTAGIRRKSRvslRVEKFAVIAALKSM 280
Cdd:COG1159     7 AIVGRPNVGKSTLLNALVGQK--VSivSPKPQTTRHRIRGIVTREDAQ-IVFVDTPGIHKPKR---KLGRRMNKAAWSAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 281 ERAEVAILVLDAQRGVTDQDKRIGSYALDAGCGLIFAVNKWDTMPPGQ--QTIRSFQEGLAIHfprlthcPVIFLSAKSG 358
Cdd:COG1159    81 EDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLVKKEEllPLLAEYSELLDFA-------EIVPISALKG 153

                  ....*..
gi 1174098179 359 KRVEKLL 365
Cdd:COG1159   154 DNVDELL 160
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
7-160 2.20e-17

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: 79.03  E-value: 2.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRDAlVDDTPGLTRDRQYGIMKRGDTPFPMVDTggfeadPGetMVSL-------IRGQTI 79
Cdd:pfam02421   3 IALVGNPNVGKTTLFNALTGANQH-VGNWPGVTVEKKEGKFKYKGYEIEIVDL------PG--IYSLspyseeeRVARDY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  80 LAIEEADIIVFVVDgstgpltddyaiASHLRSS----------GKPVIIAANKS-EKKAATASIEFHELGME---PIIPI 145
Cdd:pfam02421  74 LLNEKPDVIVNVVD------------ATNLERNlyltlqllelGLPVVLALNMMdEAEKKGIKIDIKKLSELlgvPVVPT 141
                         170
                  ....*....|....*
gi 1174098179 146 SSAHGLGIGDLLETL 160
Cdd:pfam02421 142 SARKGEGIDELLDAI 156
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
7-178 4.38e-17

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: 81.28  E-value: 4.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTGGFEADP---GETMVSLIRGqtilAIE 83
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHGQKISITSPKAQTTRNRISGIHTTGASQIIFIDTPGFHEKKhslNRLMMKEARS----AIG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  84 EADIIVFVVDGSTGPlTDDYAIASHLRSSGKPVIIAANKSEKKAATASIEFHE-----LGMEPIIPISSAHGLGIGDLLE 158
Cdd:TIGR00436  79 GVDLILFVVDSDQWN-GDGEFVLTKLQNLKRPVVLTRNKLDNKFKDKLLPLIDkyailEDFKDIVPISALTGDNTSFLAA 157
                         170       180
                  ....*....|....*....|
gi 1174098179 159 TLEEMTDamEGFCRQPEEQL 178
Cdd:TIGR00436 158 FIEVHLP--EGPFRYPEDYV 175
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
2-245 6.79e-17

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 83.63  E-value: 6.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   2 SKLPLVALVGRPNVGKSTLFNRLTRTRdALVDDTPGLTRDRQYGIMKRGDTPFPMVDTggfeadPG---------ETMVS 72
Cdd:COG0370     1 MKMITIALVGNPNVGKTTLFNALTGSR-QKVGNWPGVTVEKKEGKFKLKGKEIELVDL------PGtyslsayspDEKVA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  73 lirgQTILAIEEADIIVFVVDgstgpltddyaiASHLRSS----------GKPVIIAANKS---EKKAATASIEF--HEL 137
Cdd:COG0370    74 ----RDFLLEEKPDVVVNVVD------------ATNLERNlyltlqllelGIPVVLALNMMdeaEKKGIKIDVEKlsKLL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 138 GMePIIPISSAHGLGIGDLLETLEEmtdAMEGFCRQPEEQLLPLEVEQENPEVAR--EPRFKGPLRLAVV----GCPNAG 211
Cdd:COG0370   138 GV-PVVPTSARKGKGIDELKEAIIE---AAEGKKPRPLRIDYPEEIEEAIEELEEllEEDGPYPSRWLAIklleGDEEVL 213
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1174098179 212 KssLVNRLVGEERLLASEIAGTTRDSIDVPITDA 245
Cdd:COG0370   214 E--LLSELLELLEEIREELEEELGEDLESIIADA 245
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
7-164 3.34e-16

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: 76.01  E-value: 3.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLT-RTRDALVDDTPGLTRDRQYGIMkrgDTPFPMVDT-G-GFEADP-------GETMVSLIRG 76
Cdd:cd01876     2 VAFAGRSNVGKSSLINALTnRKKLARTSKTPGRTQLINFFNV---GDKFRLVDLpGyGYAKVSkevrekwGKLIEEYLEN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  77 QTILAieeadIIVFVVDGSTGPLTDDYAIASHLRSSGKPVIIAANKSEK-------KAATASIEFHEL--GMEPIIPISS 147
Cdd:cd01876    79 RENLK-----GVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKlkkselaKVLKKIKEELNLfnILPPVILFSS 153
                         170
                  ....*....|....*..
gi 1174098179 148 AHGLGIGDLLETLEEMT 164
Cdd:cd01876   154 KKGTGIDELRALIAEWL 170
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
8-159 8.17e-16

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: 75.12  E-value: 8.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   8 ALVGRPNVGKSTLFNRLTRTrDALVDDTPGLTRDRQYGIMKRGD-TPFPMVDTGGFEADPGETMVsliRGQTILA-IEEA 85
Cdd:cd01881     1 GLVGLPNVGKSTLLSALTSA-KVEIASYPFTTLEPNVGVFEFGDgVDIQIIDLPGLLDGASEGRG---LGEQILAhLYRS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  86 DIIVFVVDGS---TGPLTDDYAI------ASHLRSSGKPVIIAANKSEK-KAATASIEFHELGMEPI--IPISSAHGLGI 153
Cdd:cd01881    77 DLILHVIDASedcVGDPLEDQKTlneevsGSFLFLKNKPEMIVANKIDMaSENNLKRLKLDKLKRGIpvVPTSALTRLGL 156

                  ....*.
gi 1174098179 154 GDLLET 159
Cdd:cd01881   157 DRVIRT 162
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
200-364 1.66e-15

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 74.25  E-value: 1.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 200 LRLAVVGCPNAGKSSLVNRLVGEERLLASEIA--GTTRDSIDVPITDANgETVILVDTAGIRRKSRVSlrvEKFAviaal 277
Cdd:COG1100     4 KKIVVVGTGGVGKTSLVNRLVGDIFSLEKYLStnGVTIDKKELKLDGLD-VDLVIWDTPGQDEFRETR---QFYA----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 278 KSMERAEVAILVLDAQRGVTDQD-KRIGSYALDAGCG--LIFAVNKWDTMPPGQqtIRSfQEGLAIHFPRLTHCPVIFLS 354
Cdd:COG1100    75 RQLTGASLYLFVVDGTREETLQSlYELLESLRRLGKKspIILVLNKIDLYDEEE--IED-EERLKEALSEDNIVEVVATS 151
                         170
                  ....*....|
gi 1174098179 355 AKSGKRVEKL 364
Cdd:COG1100   152 AKTGEGVEEL 161
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
86-291 2.63e-15

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 75.91  E-value: 2.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  86 DIIVFVVD-----GSTGPLTDDYAiashlrsSGKPVIIAANKSE--KKAATAS-IE-FHELGMePIIPISSAHGLGIGDL 156
Cdd:COG1161    25 DLVIEVVDariplSSRNPMLDELV-------GNKPRLLVLNKADlaDPSVTKQwLKyFEKQGV-DALAISAKKGKGIKEL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 157 LETLEEMTdamegfcrqpeeqllpleveqenPEVAREPRfkgPLRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRD 236
Cdd:COG1161    97 IEAIRELA-----------------------PEKGIKRR---PIRVMIVGIPNVGKSTLINRLAGKKVAKTGNKPGVTKG 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 237 SIDVPItdanGETVILVDTAGI---RRKSRVSLRveKFAVIAALKS--MERAEVAILVLD 291
Cdd:COG1161   151 QQWIKL----DDGLELLDTPGIlwpKFEDPEVGY--KLAATGAIKDevLDLEEVALFLLG 204
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
2-162 3.10e-14

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: 71.34  E-value: 3.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   2 SKLPLVALVGRPNVGKSTLFNRLTRtRDALVDD--------TpglTRdrqygimkRGDTP----FPMVDTGGFeadpget 69
Cdd:cd01878    39 SGVPTVALVGYTNAGKSTLFNALTG-ADVLAEDqlfatldpT---TR--------RIKLPggreVLLTDTVGF------- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  70 mvslIRG----------QTILAIEEADIIVFVVDGSTgPLTDDYAIASH--LRS---SGKPVIIAANKSEKKAATASIEF 134
Cdd:cd01878   100 ----IRDlphqlveafrSTLEEVAEADLLLHVVDASD-PDREEQIETVEevLKElgaDDIPIILVLNKIDLLDDEELEER 174
                         170       180
                  ....*....|....*....|....*...
gi 1174098179 135 HELGMEPIIPISSAHGLGIGDLLETLEE 162
Cdd:cd01878   175 LRAGRPDAVFISAKTGEGLDLLKEAIEE 202
mnmE_trmE_thdF TIGR00450
tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF ...
7-133 3.20e-14

tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF (thiophene and furan oxidation protein), is a GTPase involved in tRNA modification to create 5-methylaminomethyl-2-thiouridine in the wobble position of some tRNAs. This protein and GidA form an alpha2/beta2 heterotetramer. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273083 [Multi-domain]  Cd Length: 442  Bit Score: 74.44  E-value: 3.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTGGF-EADPGETMVSLIRgqTILAIEEA 85
Cdd:TIGR00450 206 LAIVGSPNVGKSSLLNALLKQDRAIVSDIKGTTRDVVEGDFELNGILIKLLDTAGIrEHADFVERLGIEK--SFKAIKQA 283
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1174098179  86 DIIVFVVDGSTgPLTDDYAIASHLRSSGKPVIIAANKSEKKAATASIE 133
Cdd:TIGR00450 284 DLVIYVLDASQ-PLTKDDFLIIDLNKSKKPFILVLNKIDLKINSLEFF 330
YeeP COG3596
Predicted GTPase [General function prediction only];
177-404 1.66e-13

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 71.34  E-value: 1.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 177 QLLPLEVEQE-NPEVAREPRFKGPLRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPITDANGETVILVDT 255
Cdd:COG3596    16 KRLPQVLRELlAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLESDGLPGLVLLDT 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 256 AG---IRRKSRVSLRVEKFAviaalksmERAEVAILVLDAQRGVTDQDKRIGSYALDAGCG--LIFAVNKWDTMPPGQ-- 328
Cdd:COG3596    96 PGlgeVNERDREYRELRELL--------PEADLILWVVKADDRALATDEEFLQALRAQYPDppVLVVLTQVDRLEPERew 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 329 ------------QTIRSFQEGLAIHFPRLTHcPVIFLSAKSGKR---VEKLLPT-ARKVRQATQMRvstsnLNRWLEQAI 392
Cdd:COG3596   168 dppynwpsppkeQNIRRALEAIAEQLGVPID-RVIPVSAAEDRTgygLEELVDAlAEALPEAKRSR-----LARLLRAKA 241
                         250
                  ....*....|..
gi 1174098179 393 EKKAPPRAAGRP 404
Cdd:COG3596   242 IDRYTLLAAAAA 253
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
11-188 1.74e-13

ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane protein required for iron(II) update, is encoded in an operon with FeoA (75 amino acids), which is also required, and is regulated by Fur. There appear to be two copies in Archaeoglobus fulgidus and Clostridium acetobutylicum. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273077 [Multi-domain]  Cd Length: 591  Bit Score: 72.85  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  11 GRPNVGKSTLFNRLTRTrDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTGG---FEADPGETMVSlirgQTILAIEEADI 87
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGA-NQTVGNWPGVTVEKKEGKLGFQGEDIEIVDLPGiysLTTFSLEEEVA----RDYLLNEKPDL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  88 IVFVVDGSTgpLTDDYAIASHLRSSGKPVIIAANK---SEKKAATASIEFHE--LGMePIIPISSAHGLGIGDLLETLEE 162
Cdd:TIGR00437  76 VVNVVDASN--LERNLYLTLQLLELGIPMILALNLvdeAEKKGIRIDEEKLEerLGV-PVVPTSATEGRGIERLKDAIRK 152
                         170       180
                  ....*....|....*....|....*.
gi 1174098179 163 MTDAMEGFCRQPEEQLLPLEVEQENP 188
Cdd:TIGR00437 153 AIGLKELKKRAIEIVPEAYQVVEVVE 178
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
86-258 3.09e-13

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: 67.02  E-value: 3.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  86 DIIVFVVDgSTGPLTDDYAIASHLRSS-GKPVIIAANKSEK--KAATAS--IEFHELGMEPIIPISSAHGLGIgdlletl 160
Cdd:cd01849     1 DVVVEVVD-ARDPLSSRNPDIEVLINEkNKKLIMVLNKADLvpKEVLRKwvAELSELYGTKTFFISATNGQGI------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 161 eemtdamegfcrqpeEQLLPLEVEQENPEVAreprfKGPLRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDV 240
Cdd:cd01849    73 ---------------LKLKAEITKQKLKLKY-----KKGIRVGVVGLPNVGKSSFINALLNKFKLKVGSIPGTTKLQQDV 132
                         170
                  ....*....|....*...
gi 1174098179 241 PITdangETVILVDTAGI 258
Cdd:cd01849   133 KLD----KEIYLYDTPGI 146
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
4-166 1.12e-12

GTP-binding protein, GTP1/Obg family [General function prediction only];


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 68.71  E-value: 1.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   4 LPLVALVGRPNVGKSTLFNRLTRTRDAlVDDTPGLTRDRQYGIMKRGDTPFPMVDTGGFEADPGETMVSlIRGQTILAIE 83
Cdd:COG1084   160 LPTIVVAGYPNVGKSSLVSKVTSAKPE-IASYPFTTKGIIVGHFERGHGRYQVIDTPGLLDRPLSERNE-IERQAILALK 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  84 E-ADIIVFVVDGSTG---PLTDDYAIASHLRSS-GKPVIIAANKSEkkaATASIEFHELGMEPIIPISSAHGLGIGDLLE 158
Cdd:COG1084   238 HlADVILFLFDPSETcgySLEEQLNLLEEIRSLfDVPVIVVINKID---LSDEEELKEAEEEADIKISALTGEGVDELLD 314

                  ....*...
gi 1174098179 159 TLEEMTDA 166
Cdd:COG1084   315 ELIEALEE 322
obgE PRK12297
GTPase CgtA; Reviewed
7-197 1.78e-12

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 68.97  E-value: 1.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRdalvddtPgltrdrqygimKRGDTPF----P---MVDTGGFE----AD-PGetmvsLI 74
Cdd:PRK12297  161 VGLVGFPNVGKSTLLSVVSNAK-------P-----------KIANYHFttlvPnlgVVETDDGRsfvmADiPG-----LI 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  75 RGqtilA-------------IEEADIIVFVVD--GSTG--PLTDDYAIASHLRS-----SGKPVIIAANKSEKKAATASI 132
Cdd:PRK12297  218 EG----AsegvglghqflrhIERTRVIVHVIDmsGSEGrdPIEDYEKINKELKLynprlLERPQIVVANKMDLPEAEENL 293
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1174098179 133 E--FHELGmEPIIPISSAHGLGIGDLLETLEEMTDAMegfcrqPEEQLLPLEVEQE--NPEVAREPRFK 197
Cdd:PRK12297  294 EefKEKLG-PKVFPISALTGQGLDELLYAVAELLEET------PEFPLEEEEVEEEvyYKFEEEEKDFT 355
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
5-163 2.19e-12

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: 65.27  E-value: 2.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   5 PLVALVGRPNVGKSTLFNRLTRTrDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTGGFEADPGETMvSLIRGQTILAIEE 84
Cdd:cd01897     1 RTLVIAGYPNVGKSSLVNKLTRA-KPEVAPYPFTTKSLFVGHFDYKYLRWQVIDTPGILDRPLEER-NTIEMQAITALAH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  85 -ADIIVFVVDGSTgplTDDYAIAS--HLRSS-----GKPVIIAANKSEKK---AATASIEFHELGMEPIIPISSAHGLGI 153
Cdd:cd01897    79 lRAAVLFFIDPSE---TCGYSIEEqlSLFKEikplfNKPVIVVLNKIDLLteeDLSEIEKELEKEGEEVIKISTLTEEGV 155
                         170
                  ....*....|
gi 1174098179 154 GDLLETLEEM 163
Cdd:cd01897   156 DELKNKACEL 165
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
7-162 2.51e-12

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: 65.14  E-value: 2.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRdalvddtPgltrdrqygimKRGDTPF----P---MVDTGGFE----AD-PGetmvsLI 74
Cdd:cd01898     3 VGLVGLPNAGKSTLLSAISNAK-------P-----------KIADYPFttlvPnlgVVRVDDGRsfviADiPG-----LI 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  75 RGqtilA-------------IEEADIIVFVVDGSTG--PLTDDYAIASHLRS-----SGKPVIIAANK-----SEKKAAT 129
Cdd:cd01898    60 EG----AsegkglghrflrhIERTRVLLHVIDLSGEddPVEDYETIRNELEAynpglAEKPRIVVLNKidlldAEERFEK 135
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1174098179 130 ASIEFHELGMEPIIPISSAHGLGIGDLLETLEE 162
Cdd:cd01898   136 LKELLKELKGKKVFPISALTGEGLDELLKKLAK 168
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
200-295 2.80e-12

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: 67.03  E-value: 2.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 200 LRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPITDANGETvILVDTAGIRRKSRVSLRVEKFAVIAALKS 279
Cdd:TIGR00436   1 GFVAILGRPNVGKSTLLNQLHGQKISITSPKAQTTRNRISGIHTTGASQI-IFIDTPGFHEKKHSLNRLMMKEARSAIGG 79
                          90
                  ....*....|....*.
gi 1174098179 280 MeraEVAILVLDAQRG 295
Cdd:TIGR00436  80 V---DLILFVVDSDQW 92
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
2-163 5.06e-12

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 67.42  E-value: 5.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   2 SKLPLVALVGRPNVGKSTLFNRLTRTrDALVDD--------TpglTRdrqyGIMKRGDTPFPMVDTGGFeadpgetmVS- 72
Cdd:COG2262   197 SGIPTVALVGYTNAGKSTLFNRLTGA-DVLAEDklfatldpT---TR----RLELPDGRPVLLTDTVGF--------IRk 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  73 ----LI---RGqTILAIEEADIIVFVVDGStgpltdDYAIASHLRSS----------GKPVIIAANKSEkKAATASIEFH 135
Cdd:COG2262   261 lphqLVeafRS-TLEEVREADLLLHVVDAS------DPDFEEQIETVnevleelgadDKPIILVFNKID-LLDDEELERL 332
                         170       180
                  ....*....|....*....|....*...
gi 1174098179 136 ELGMEPIIPISSAHGLGIGDLLETLEEM 163
Cdd:COG2262   333 RAGYPDAVFISAKTGEGIDELLEAIEER 360
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
7-168 1.89e-11

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 62.69  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTR-TRDALVDDTP-GLTRDRQYGIMKRGDTPFPMVDTggfeadPGETMVSLIRGQTILAIEE 84
Cdd:COG1100     6 IVVVGTGGVGKTSLVNRLVGdIFSLEKYLSTnGVTIDKKELKLDGLDVDLVIWDT------PGQDEFRETRQFYARQLTG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  85 ADIIVFVVDGSTGPLTDD-YAIASHLRSSGK--PVIIAANKS-----EKKAATASIE--FHELGMEPIIPISSAHGLGIG 154
Cdd:COG1100    80 ASLYLFVVDGTREETLQSlYELLESLRRLGKksPIILVLNKIdlydeEEIEDEERLKeaLSEDNIVEVVATSAKTGEGVE 159
                         170
                  ....*....|....
gi 1174098179 155 DLLETLEEMTDAME 168
Cdd:COG1100   160 ELFAALAEILRGEG 173
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
78-258 4.71e-10

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: 4.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  78 TILAIEE----ADIIVFVVDG-----STGPLTDDYaiashlrSSGKPVIIAANKSEK--KAATASI--EFHELGmEPIIP 144
Cdd:cd01856     9 ALRQIKEklklVDVVIEVRDAriplsSRNPDLDKI-------LGNKPRLIVLNKADLadPAKTKKWlkYFKSQG-EPVLF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 145 ISSAHGLGIGDLLETLEEMTDAMEgfcrqpeeqllpleveqENPEVAREPRfkgPLRLAVVGCPNAGKSSLVNRLVGEER 224
Cdd:cd01856    81 VNAKNGKGVKKLLKKAKKLLKENE-----------------KLKAKGLLPR---PLRAMVVGIPNVGKSTLINRLRGKKV 140
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1174098179 225 LLASEIAGTTRDSIDVPITDangeTVILVDTAGI 258
Cdd:cd01856   141 AKVGNKPGVTRGQQWIRIGP----NIELLDTPGI 170
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
88-258 5.02e-10

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: 58.82  E-value: 5.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  88 IVFVVDGSTGPLTDDYAIASHLrsSGKPVIIAANKSE---KKAATASIE------FHELGMEP--IIPISSAHGLGIGDL 156
Cdd:cd01855    37 VVHVVDIFDFPGSLIPGLAELI--GAKPVILVGNKIDllpKDVKPNRLKqwvkkrLKIGGLKIkdVILVSAKKGWGVEEL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 157 LETLEEMTdamegfcrqpeeqllpleveqenpevareprfKGPLRLAVVGCPNAGKSSLVNRLVGE-----------ERL 225
Cdd:cd01855   115 IEEIKKLA--------------------------------KYRGDVYVVGATNVGKSTLINALLKSnggkvqaqalvQRL 162
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1174098179 226 LASEIAGTTRDSIDVPItdanGETVILVDTAGI 258
Cdd:cd01855   163 TVSPIPGTTLGLIKIPL----GEGKKLYDTPGI 191
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
75-167 5.24e-10

Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 58.25  E-value: 5.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  75 RGQTIlaieeADIIVFVVDGSTG--PLTDDyAIAsHLRSSGKPVIIAANKSEKKAATASI---------EFHELGME--- 140
Cdd:cd01887    68 RGASV-----TDIAILVVAADDGvmPQTIE-AIN-HAKAANVPIIVAINKIDKPYGTEADpervknelsELGLVGEEwgg 140
                          90       100
                  ....*....|....*....|....*....
gi 1174098179 141 --PIIPISSAHGLGIGDLLETLEEMTDAM 167
Cdd:cd01887   141 dvSIVPISAKTGEGIDDLLEAILLLAEVL 169
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
8-160 1.95e-09

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: 55.81  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   8 ALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQ---YGIMKRGDTpfpMVDTGGFeaDPGETMVSLIRGQTILAIEE 84
Cdd:cd11383     1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQayvWQTGGDGLV---LLDLPGV--GERGRRDREYEELYRRLLPE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  85 ADIIVFVVDgstgplTDDYAIAS-------HLRSSGKPVIIAANKSekkaatasiefhelgmEPIIPISSAHGLGIGDLL 157
Cdd:cd11383    76 ADLVLWLLD------ADDRALAAdhdfyllPLAGHDAPLLFVLNQV----------------DPVLAVSARTGWGLDELA 133

                  ...
gi 1174098179 158 ETL 160
Cdd:cd11383   134 EAL 136
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
4-163 2.22e-09

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: 57.00  E-value: 2.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   4 LPLVALVGRPNVGKSTLFNRLTRTRD-ALVDDTPGLTR--------DRQYgimkrgdtpfpMVDT-G-GFEADP------ 66
Cdd:COG0218    23 LPEIAFAGRSNVGKSSLINALTNRKKlARTSKTPGKTQlinfflinDKFY-----------LVDLpGyGYAKVSkaekek 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  67 -GETMVSLIRGQTILAieeadIIVFVVDGSTGPLTDDYAIASHLRSSGKPVIIAANK------SEKKAATASIEfHELGM 139
Cdd:COG0218    92 wQKLIEDYLEGRENLK-----GVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKadklkkSELAKQLKAIK-KALGK 165
                         170       180
                  ....*....|....*....|....*...
gi 1174098179 140 EP----IIPISSAHGLGIGDLLETLEEM 163
Cdd:COG0218   166 DPaapeVILFSSLKKEGIDELRAAIEEW 193
obgE PRK12299
GTPase CgtA; Reviewed
7-168 4.60e-09

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 57.77  E-value: 4.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRdalvddtPgltrdrqygimKRGDTPF----P---MVDTGGFE----AD-PGetmvsLI 74
Cdd:PRK12299  161 VGLVGLPNAGKSTLISAVSAAK-------P-----------KIADYPFttlhPnlgVVRVDDYKsfviADiPG-----LI 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  75 RGqtilA-------------IEEADIIVFVVDGST-GPLTDDYAIASHLRS-----SGKPVIIAANKS-----EKKAATA 130
Cdd:PRK12299  218 EG----AsegaglghrflkhIERTRLLLHLVDIEAvDPVEDYKTIRNELEKyspelADKPRILVLNKIdlldeEEEREKR 293
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1174098179 131 SIEFHELGMEPIIPISSAHGLGIGDLLETLEEMTDAME 168
Cdd:PRK12299  294 AALELAALGGPVFLISAVTGEGLDELLRALWELLEEAR 331
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
1-162 6.34e-09

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 58.57  E-value: 6.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   1 MSKLPLvALVGRPNVGKSTLFNRLTRTRDAlVDDTPGLTRDRQYGIMKRGDTPFPMVDTggfeadPGETMVSLIRGQT-- 78
Cdd:PRK09554    1 MKKLTI-GLIGNPNSGKTTLFNQLTGARQR-VGNWAGVTVERKEGQFSTTDHQVTLVDL------PGTYSLTTISSQTsl 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  79 --------ILAiEEADIIVFVVDGSTgpLTDDYAIASHLRSSGKPVIIAANK---SEKKAATASIEFHE--LGMePIIPI 145
Cdd:PRK09554   73 deqiachyILS-GDADLLINVVDASN--LERNLYLTLQLLELGIPCIVALNMldiAEKQNIRIDIDALSarLGC-PVIPL 148
                         170
                  ....*....|....*..
gi 1174098179 146 SSAHGLGIGDLLETLEE 162
Cdd:PRK09554  149 VSTRGRGIEALKLAIDR 165
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
7-96 2.20e-08

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 55.96  E-value: 2.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTrDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTggfeadPGetmvsLI--------RGQT 78
Cdd:COG1163    66 VVLVGFPSVGKSTLLNKLTNA-KSEVGAYEFTTLDVVPGMLEYKGAKIQILDV------PG-----LIegaasgkgRGKE 133
                          90
                  ....*....|....*....
gi 1174098179  79 ILA-IEEADIIVFVVDGST 96
Cdd:COG1163   134 VLSvVRNADLILIVLDVFE 152
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
7-162 3.65e-08

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: 53.07  E-value: 3.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRtrDALVDDTPGLTRDRQYGIMK----RGDTpfpmVDTGGFEADPGETMVSLI-------- 74
Cdd:cd00881     2 VGVIGHVDHGKTTLTGSLLY--QTGAIDRRGTRKETFLDTLKeereRGIT----IKTGVVEFEWPKRRINFIdtpghedf 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  75 RGQTILAIEEADIIVFVVDGSTGPLTDDYAIASHLRSSGKPVIIAANKS--------EKKAATASIEFHELG-------M 139
Cdd:cd00881    76 SKETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIdrvgeedfDEVLREIKELLKLIGftflkgkD 155
                         170       180
                  ....*....|....*....|...
gi 1174098179 140 EPIIPISSAHGLGIGDLLETLEE 162
Cdd:cd00881   156 VPIIPISALTGEGIEELLDAIVE 178
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
200-356 4.88e-08

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: 52.93  E-value: 4.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 200 LRLAVVGCPNAGKSSLVNRLVGEErLLASEIAGTTrdSIDVPITDANGETVILVDTAGIrrKSRVSLRVEkfaviAALKS 279
Cdd:cd09912     1 FLLAVVGEFSAGKSTLLNALLGEE-VLPTGVTPTT--AVITVLRYGLLKGVVLVDTPGL--NSTIEHHTE-----ITESF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 280 MERAEVAILVLDAQRGVTDQDKR-IGSYALDAGCGLIFAVNKWD--TMPPGQQTIRSFQEGLAIHFPRLTHCPVIFLSAK 356
Cdd:cd09912    71 LPRADAVIFVLSADQPLTESEREfLKEILKWSGKKIFFVLNKIDllSEEELEEVLEYSREELGVLELGGGEPRIFPVSAK 150
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
82-258 5.26e-08

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: 52.32  E-value: 5.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  82 IEEADIIVFVVDGSTGPLTDDYAIASHLRSSGKPVIIAANKSE---KKAATASIEFHELGMEPIIPISSAHGLGIGDLLE 158
Cdd:cd01859     9 IKEADVVLEVVDARDPELTRSRKLERMALELGKKLIIVLNKADlvpREVLEKWKEVFESEGLPVVYVSARERLGTRILRR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 159 TLEEMtdAMEGFcrqpeeqllpleveqenpevareprfkgPLRLAVVGCPNAGKSSLVNRLVGEERLLASEI---AGTTR 235
Cdd:cd01859    89 TIKEL--AIDGK----------------------------PVIVGVVGYPKVGKSSIINALKGRHSASTSPIpgsPGYTK 138
                         170       180
                  ....*....|....*....|...
gi 1174098179 236 DSIDVPItdanGETVILVDTAGI 258
Cdd:cd01859   139 GIQLVRI----DSKIYLIDTPGV 157
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
203-371 5.71e-08

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: 52.07  E-value: 5.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 203 AVVGCPNAGKSSLVNRLVGeERLLASEIAGTTRDSIdVPITDANGETVILVDTAGIrrksrVSLRV----EKFAVIAALK 278
Cdd:cd01879     1 ALVGNPNVGKTTLFNALTG-ARQKVGNWPGVTVEKK-EGEFKLGGKEIEIVDLPGT-----YSLTPysedEKVARDFLLG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 279 smERAEVAILVLDA---QRG--VTDQdkrigsyALDAGCGLIFAVNKWDtmppgqqtiRSFQEGLAIHFPRLTH---CPV 350
Cdd:cd01879    74 --EEPDLIVNVVDAtnlERNlyLTLQ-------LLELGLPVVVALNMID---------EAEKRGIKIDLDKLSEllgVPV 135
                         170       180
                  ....*....|....*....|.
gi 1174098179 351 IFLSAKSGKRVEKLLPTARKV 371
Cdd:cd01879   136 VPTSARKGEGIDELLDAIAKL 156
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
7-53 9.55e-08

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


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 51.76  E-value: 9.55e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQYGIMKRG----DTP 53
Cdd:cd01856   118 AMVVGIPNVGKSTLINRLRGKKVAKVGNKPGVTRGQQWIRIGPNiellDTP 168
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
201-365 1.20e-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: 51.53  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 201 RLAVVGCPNAGKSSLVNRLVGE--ERLLASEIAGTTRD----------SIDV-PIT-DANGETVILVDTAGirrksrvsl 266
Cdd:cd00881     1 NVGVIGHVDHGKTTLTGSLLYQtgAIDRRGTRKETFLDtlkeerergiTIKTgVVEfEWPKRRINFIDTPG--------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 267 rVEKF--AVIAAlksMERAEVAILVLDAQRGVTDQDKRIGSYALDAGCGLIFAVNKWDTMPPGQ-----QTIRSFQEGLA 339
Cdd:cd00881    72 -HEDFskETVRG---LAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGEEDfdevlREIKELLKLIG 147
                         170       180
                  ....*....|....*....|....*.
gi 1174098179 340 IHFPRLTHCPVIFLSAKSGKRVEKLL 365
Cdd:cd00881   148 FTFLKGKDVPIIPISALTGEGIEELL 173
YeeP COG3596
Predicted GTPase [General function prediction only];
5-163 5.31e-07

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 51.31  E-value: 5.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   5 PLVALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRD-RQYGIMKRGDTPFPMVDTGGFEADPGETmvsLIRGQTILAIE 83
Cdd:COG3596    40 PVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREiQRYRLESDGLPGLVLLDTPGLGEVNERD---REYRELRELLP 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  84 EADIIVFVVDGSTGPLTDDYAIASHLRS--SGKPVIIAANKSEK----------------------KAATASIEFH-ELG 138
Cdd:COG3596   117 EADLILWVVKADDRALATDEEFLQALRAqyPDPPVLVVLTQVDRleperewdppynwpsppkeqniRRALEAIAEQlGVP 196
                         170       180
                  ....*....|....*....|....*...
gi 1174098179 139 MEPIIPISSA---HGLGIGDLLETLEEM 163
Cdd:COG3596   197 IDRVIPVSAAedrTGYGLEELVDALAEA 224
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
202-365 1.65e-06

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: 48.29  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 202 LAVVGCPNAGKSSLVNRLV--------GEERLLASEIAGTTRD-------SIDVPITDANGET--VILVDTAGirrksrv 264
Cdd:pfam00009   6 IGIIGHVDHGKTTLTDRLLyytgaiskRGEVKGEGEAGLDNLPeerergiTIKSAAVSFETKDylINLIDTPG------- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 265 slrVEKFA--VIAALKSMEraeVAILVLDAQRGVTDQDKRIGSYALDAGCGLIFAVNKWDtMPPGQQTIRSFQE-----G 337
Cdd:pfam00009  79 ---HVDFVkeVIRGLAQAD---GAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMD-RVDGAELEEVVEEvsrelL 151
                         170       180
                  ....*....|....*....|....*...
gi 1174098179 338 LAIHFPRLTHcPVIFLSAKSGKRVEKLL 365
Cdd:pfam00009 152 EKYGEDGEFV-PVVPGSALKGEGVQTLL 178
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
189-365 2.27e-06

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: 48.22  E-value: 2.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 189 EVAREPRFKGPL-RLAVVGCPNAGKSSLVNRLVGEERLLASEIAGT---TRDSIDVPitdaNGETVILVDTAGIRRKSRV 264
Cdd:cd01878    30 ELQRARRKRSGVpTVALVGYTNAGKSTLFNALTGADVLAEDQLFATldpTTRRIKLP----GGREVLLTDTVGFIRDLPH 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 265 SLrvekfavIAALKS-----MErAEVAILVLDA-------QRGVTDQ-DKRIGsyALDAGCglIFAVNKWDTMPPGQQTI 331
Cdd:cd01878   106 QL-------VEAFRStleevAE-ADLLLHVVDAsdpdreeQIETVEEvLKELG--ADDIPI--ILVLNKIDLLDDEELEE 173
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1174098179 332 RsfqegLAIHFPrlthcPVIFLSAKSGKRVEKLL 365
Cdd:cd01878   174 R-----LRAGRP-----DAVFISAKTGEGLDLLK 197
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
7-98 4.31e-06

Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding protein (DRG) subfamily is an uncharacterized member of the Obg family, an evolutionary branch of GTPase superfamily proteins. GTPases act as molecular switches regulating diverse cellular processes. DRG2 and DRG1 comprise the DRG subfamily in eukaryotes. In view of their widespread expression in various tissues and high conservation among distantly related species in eukaryotes and archaea, DRG proteins may regulate fundamental cellular processes. It is proposed that the DRG subfamily proteins play their physiological roles through RNA binding.


Pssm-ID: 206683 [Multi-domain]  Cd Length: 233  Bit Score: 47.93  E-value: 4.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTrDALVDDTPGLTRDRQYGIMKRGDTPFPMVDTggfeadPGetmvsLIRG---------Q 77
Cdd:cd01896     3 VALVGFPSVGKSTLLSKLTNT-KSEVAAYEFTTLTCVPGVMEYKGAKIQLLDL------PG-----IIEGasdgkgrgrQ 70
                          90       100
                  ....*....|....*....|.
gi 1174098179  78 TILAIEEADIIVFVVDGSTGP 98
Cdd:cd01896    71 VIAVARTADLILIVLDATKPE 91
infB CHL00189
translation initiation factor 2; Provisional
5-165 5.94e-06

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 49.06  E-value: 5.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   5 PLVALVGRPNVGKSTLFNRLTRTRDAlVDDTPGLTR-------DRQYGIMKRGDTpfpMVDTGGFEADPGetMVSliRGQ 77
Cdd:CHL00189  245 PIVTILGHVDHGKTTLLDKIRKTQIA-QKEAGGITQkigayevEFEYKDENQKIV---FLDTPGHEAFSS--MRS--RGA 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  78 TILAIEeadIIVFVVDGSTGPLTDDyAIaSHLRSSGKPVIIAANKSEKKAATASIEFHEL-----------GMEPIIPIS 146
Cdd:CHL00189  317 NVTDIA---ILIIAADDGVKPQTIE-AI-NYIQAANVPIIVAINKIDKANANTERIKQQLakynlipekwgGDTPMIPIS 391
                         170
                  ....*....|....*....
gi 1174098179 147 SAHGLGIGDLLETLEEMTD 165
Cdd:CHL00189  392 ASQGTNIDKLLETILLLAE 410
SRPRB pfam09439
Signal recognition particle receptor beta subunit; The beta subunit of the signal recognition ...
2-124 9.42e-06

Signal recognition particle receptor beta subunit; The beta subunit of the signal recognition particle receptor (SRP) is a transmembrane GTPase which anchors the alpha subunit to the endoplasmic reticulum membrane.


Pssm-ID: 462797 [Multi-domain]  Cd Length: 181  Bit Score: 46.28  E-value: 9.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   2 SKLPLVALVGRPNVGKSTLFNRLT--RTRDALVDDTPGLTrdrqYGIMKRGDTPFPMVDTggfeadPGETMVSLIRGQTI 79
Cdd:pfam09439   1 SSQPAVIIAGLCDSGKTSLFTLLTtdSVRPTVTSQEPSAA----YRYMLNKGNSFTLIDF------PGHVKLRYKLLETL 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1174098179  80 LAIEEADIIVFVVDGSTGP--LTD------DYAIASHLRSSGKPVIIAANKSE 124
Cdd:pfam09439  71 KDSSSLKGIVFVVDSTIFPkeVTDtaeflyDILSITELLKNGIDILIACNKQE 123
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
10-43 1.11e-05

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 47.02  E-value: 1.11e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1174098179  10 VGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQ 43
Cdd:COG1161   119 VGIPNVGKSTLINRLAGKKVAKTGNKPGVTKGQQ 152
PRK04213 PRK04213
GTP-binding protein EngB;
5-162 1.48e-05

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 45.68  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   5 PLVALVGRPNVGKSTLFNRLTrTRDALVDDTPGLTR---DRQYGIMKRGDTP-FpmvdtgGFEADPGETMVSLIRGQTIL 80
Cdd:PRK04213   10 PEIVFVGRSNVGKSTLVRELT-GKKVRVGKRPGVTRkpnHYDWGDFILTDLPgF------GFMSGVPKEVQEKIKDEIVR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  81 AIEE-ADII---VFVVDG-----------STGPLTDDYAIASHLRSSGKPVIIAANKSEK-KAATASIEF--HELGMEP- 141
Cdd:PRK04213   83 YIEDnADRIlaaVLVVDGksfieiierweGRGEIPIDVEMFDFLRELGIPPIVAVNKMDKiKNRDEVLDEiaERLGLYPp 162
                         170       180
                  ....*....|....*....|....*...
gi 1174098179 142 -------IIPISSAHGlGIGDLLETLEE 162
Cdd:PRK04213  163 wrqwqdiIAPISAKKG-GIEELKEAIRK 189
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
7-43 1.94e-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: 44.87  E-value: 1.94e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQ 43
Cdd:cd04178   119 VGVVGYPNVGKSSVINSLKRSRACNVGATPGVTKSMQ 155
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
1-43 2.56e-05

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: 45.96  E-value: 2.56e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1174098179   1 MSKLPLVALV-GRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQ 43
Cdd:TIGR03596 114 LKNRPIRAMIvGIPNVGKSTLINRLAGKKVAKVGNRPGVTKGQQ 157
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
3-162 6.98e-05

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: 43.67  E-value: 6.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   3 KLPLVALVGRPNVGKSTLFNRLT-----RTRDALVDDTPGLTRD-----RQYGI-MKRGDTPFP-------MVDTGGfEA 64
Cdd:pfam00009   2 RHRNIGIIGHVDHGKTTLTDRLLyytgaISKRGEVKGEGEAGLDnlpeeRERGItIKSAAVSFEtkdylinLIDTPG-HV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  65 DPGETMvslIRGqtiLAIeeADIIVFVVDGSTGPLTDDYAIASHLRSSGKPVIIAANK-----------SEKKAATASIE 133
Cdd:pfam00009  81 DFVKEV---IRG---LAQ--ADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKmdrvdgaeleeVVEEVSRELLE 152
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1174098179 134 FHELGME--PIIPISSAHGLGIGDLLETLEE 162
Cdd:pfam00009 153 KYGEDGEfvPVVPGSALKGEGVQTLLDALDE 183
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
203-326 8.02e-05

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


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 42.71  E-value: 8.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 203 AVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPITDaNGETVILVDTAGIRRKSRVSLRVEKfaviAALKSMER 282
Cdd:cd11383     1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQAYVWQT-GGDGLVLLDLPGVGERGRRDREYEE----LYRRLLPE 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1174098179 283 AEVAILVLDAQ-RGVTDQDKRIGSYALDAGCGLIFAVNKWDTMPP 326
Cdd:cd11383    76 ADLVLWLLDADdRALAADHDFYLLPLAGHDAPLLFVLNQVDPVLA 120
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
132-259 1.19e-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: 42.91  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 132 IEFHELGMEPIIPISSAhglgigDLLETLEEMTDAMEGFcRQPEEQLLPLEVEQENPEVAREPRFKGPLrLAVVGCPNAG 211
Cdd:pfam03193  47 VLAEASGIEPVIVLNKI------DLLDEEEELEELLKIY-RAIGYPVLFVSAKTGEGIEALKELLKGKT-TVLAGQSGVG 118
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1174098179 212 KSSLVNRLVGEERLLASEIAG-------TTRDSIDVPItDANGetvILVDTAGIR 259
Cdd:pfam03193 119 KSTLLNALLPELDLRTGEISEklgrgrhTTTHVELFPL-PGGG---LLIDTPGFR 169
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
6-61 1.53e-04

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


Pssm-ID: 206752 [Multi-domain]  Cd Length: 157  Bit Score: 42.31  E-value: 1.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1174098179   6 LVALVGRPNVGKSTLFNRLTRTRDAL---VDDTPGLTRDRQygiMKRGDTPFPMVDTGG 61
Cdd:cd01859   101 IVGVVGYPKVGKSSIINALKGRHSAStspIPGSPGYTKGIQ---LVRIDSKIYLIDTPG 156
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
7-44 1.60e-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: 41.99  E-value: 1.60e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQY 44
Cdd:cd01849    94 VGVVGLPNVGKSSFINALLNKFKLKVGSIPGTTKLQQD 131
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
5-128 3.02e-04

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


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 41.92  E-value: 3.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   5 PLVALVGRPNVGKSTLFNRLTrtrdalvDDTPGLTRDRQ-----YGIMKRG-DTPFPMVDTggfeadPGETMVsliRGQT 78
Cdd:cd04105     1 PTVLLLGPSDSGKTALFTKLT-------TGKVRSTVTSIepnvaSFYSNSSkGKKLTLVDV------PGHEKL---RDKL 64
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1174098179  79 ILAIEEADI-IVFVVDGSTGP--LTD------DYAIASHLRSSGKPVIIAANKSEKKAA 128
Cdd:cd04105    65 LEYLKASLKaIVFVVDSATFQknIRDvaeflyDILTDLEKIKNKIPILIACNKQDLFTA 123
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
10-27 3.16e-04

YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of GTPases: Obg, DRG, Ygr210, and NOG1. Obg is an essential gene that is involved in DNA replication in C. crescentus and Streptomyces griseus and is associated with the ribosome. Several members of the family, including YchF, possess the TGS domain related to the RNA-binding proteins. Experimental data and genomic analysis suggest that YchF may be part of a nucleoprotein complex and may function as a GTP-dependent translational factor.


Pssm-ID: 206687 [Multi-domain]  Cd Length: 274  Bit Score: 42.45  E-value: 3.16e-04
                          10
                  ....*....|....*...
gi 1174098179  10 VGRPNVGKSTLFNRLTRT 27
Cdd:cd01900     4 VGLPNVGKSTLFNALTKS 21
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
9-53 3.27e-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: 41.87  E-value: 3.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   9 LVGRPNVGKSTLFNRLTRT-----------RDALVDDTPGLTRD-RQYGIMKRG---DTP 53
Cdd:cd01855   130 VVGATNVGKSTLINALLKSnggkvqaqalvQRLTVSPIPGTTLGlIKIPLGEGKklyDTP 189
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
191-258 3.58e-04

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: 41.41  E-value: 3.58e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1174098179 191 AREPRFKGPLRLAVVGCPNAGKSSLVNRLVGEERLLASEIAGTTRDSIDVPITDangeTVILVDTAGI 258
Cdd:cd04178   108 ARNKGIKTSITVGVVGYPNVGKSSVINSLKRSRACNVGATPGVTKSMQEVHLDK----HVKLLDSPGV 171
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
9-27 4.66e-04

Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 42.32  E-value: 4.66e-04
                          10
                  ....*....|....*....
gi 1174098179   9 LVGRPNVGKSTLFNRLTRT 27
Cdd:COG0012     5 IVGLPNVGKSTLFNALTKA 23
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
189-365 9.26e-04

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 41.61  E-value: 9.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 189 EVAREPRFKGPL-RLAVVGCPNAGKSSLVNRLVGEE-----RLLA---SeiagTTRdSIDVPitdaNGETVILVDTAG-I 258
Cdd:COG2262   188 ELQRKRRKRSGIpTVALVGYTNAGKSTLFNRLTGADvlaedKLFAtldP----TTR-RLELP----DGRPVLLTDTVGfI 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 259 RRksrvsLRVEkfaVIAALKS-MEraEVA-----ILVLDA-------QRGVTDQ--------DKRIgsyaldagcglIFA 317
Cdd:COG2262   259 RK-----LPHQ---LVEAFRStLE--EVReadllLHVVDAsdpdfeeQIETVNEvleelgadDKPI-----------ILV 317
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1174098179 318 VNKWDTMPPGqqtirsfqeglAIHFPRLTHCPVIFLSAKSGKRVEKLL 365
Cdd:COG2262   318 FNKIDLLDDE-----------ELERLRAGYPDAVFISAKTGEGIDELL 354
PRK09602 PRK09602
translation-associated GTPase; Reviewed
101-148 1.12e-03

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 41.33  E-value: 1.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1174098179 101 DDYAIASHLRSSGKPVIIAANKSEKKAATASIE-FHELGMEPIIPISSA 148
Cdd:PRK09602  205 DLLELARELRKISKPMVIAANKADLPPAEENIErLKEEKYYIVVPTSAE 253
PRK11058 PRK11058
GTPase HflX; Provisional
4-162 1.65e-03

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 40.86  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   4 LPLVALVGRPNVGKSTLFNRLTrTRDALVDDTPGLTRD---RQYGIMKRGDTpfPMVDTGGFEADPGETMVSLIRGqTIL 80
Cdd:PRK11058  197 VPTVSLVGYTNAGKSTLFNRIT-EARVYAADQLFATLDptlRRIDVADVGET--VLADTVGFIRHLPHDLVAAFKA-TLQ 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  81 AIEEADIIVFVVDGSTGPLTDDYA----IASHLRSSGKPVIIAANKSEK-KAATASIEFHELGMEPIIPISSAHGLGIGD 155
Cdd:PRK11058  273 ETRQATLLLHVVDAADVRVQENIEavntVLEEIDAHEIPTLLVMNKIDMlDDFEPRIDRDEENKPIRVWLSAQTGAGIPL 352

                  ....*..
gi 1174098179 156 LLETLEE 162
Cdd:PRK11058  353 LFQALTE 359
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
210-259 1.92e-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: 39.69  E-value: 1.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1174098179 210 AGKSSLVNRLVGEERLLASEI-----AG--TTRDSIDVPItDANGetvILVDTAGIR 259
Cdd:cd01854    96 VGKSTLLNALLPELVLATGEIseklgRGrhTTTHRELFPL-PGGG---LIIDTPGFR 148
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
202-258 3.02e-03

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: 38.31  E-value: 3.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179 202 LAVVGCPNAGKSSLVNRLVGEErllaSEIAG---TTRdSIDVPITDANGETVILVDTAGI 258
Cdd:cd01897     3 LVIAGYPNVGKSSLVNKLTRAK----PEVAPypfTTK-SLFVGHFDYKYLRWQVIDTPGI 57
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
7-36 4.37e-03

Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They are characterized by a distinct glycine-rich motif immediately following the Walker B motif. The Ygr210 and YyaF/YchF subfamilies appear to form one major branch of the Obg-like family. Among eukaryotes, the Ygr210 subfamily is represented only in fungi. These fungal proteins form a tight cluster with their archaeal orthologs, which suggests the possibility of horizontal transfer from archaea to fungi.


Pssm-ID: 206686 [Multi-domain]  Cd Length: 318  Bit Score: 39.13  E-value: 4.37e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTrDALVDDTP 36
Cdd:cd01899     1 IGLVGKPNVGKSTFFNAATLA-DVEIANYP 29
Arl2l1_Arl13_like cd04161
Arl2-like protein 1 (Arl2l1) and Arl13; Arl2l1 (Arl2-like protein 1) and Arl13 form a ...
7-147 4.68e-03

Arl2-like protein 1 (Arl2l1) and Arl13; Arl2l1 (Arl2-like protein 1) and Arl13 form a subfamily of the Arf family of small GTPases. Arl2l1 was identified in human cells during a search for the gene(s) responsible for Bardet-Biedl syndrome (BBS). Like Arl6, the identified BBS gene, Arl2l1 is proposed to have cilia-specific functions. Arl13 is found on the X chromosome, but its expression has not been confirmed; it may be a pseudogene.


Pssm-ID: 133361 [Multi-domain]  Cd Length: 167  Bit Score: 37.76  E-value: 4.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRqygiMKRGDTPFPMVDTGGfeadpgetmVSLIRGQTILAIEEAD 86
Cdd:cd04161     2 LLTVGLDNAGKTTLVSALQGEIPKKVAPTVGFTPTK----LRLDKYEVCIFDLGG---------GANFRGIWVNYYAEAH 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1174098179  87 IIVFVVDGSTGP--------LTDdyaIASHLRSSGKPVIIAANKSEKKAAtasiefheLGMEPIIPISS 147
Cdd:cd04161    69 GLVFVVDSSDDDrvqevkeiLRE---LLQHPRVSGKPILVLANKQDKKNA--------LLGADVIEYLS 126
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
7-43 4.69e-03

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: 37.60  E-value: 4.69e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRDALVDDTPGLTRDRQ 43
Cdd:cd01857    85 IGLVGYPNVGKSSLINALVGSKKVSVSSTPGKTKHFQ 121
PTZ00258 PTZ00258
GTP-binding protein; Provisional
9-27 4.87e-03

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 39.16  E-value: 4.87e-03
                          10
                  ....*....|....*....
gi 1174098179   9 LVGRPNVGKSTLFNRLTRT 27
Cdd:PTZ00258   26 IVGLPNVGKSTTFNALCKQ 44
PRK09602 PRK09602
translation-associated GTPase; Reviewed
6-25 5.17e-03

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 39.02  E-value: 5.17e-03
                          10        20
                  ....*....|....*....|
gi 1174098179   6 LVALVGRPNVGKSTLFNRLT 25
Cdd:PRK09602    3 TIGLVGKPNVGKSTFFNAAT 22
NOG1 pfam06858
Nucleolar GTP-binding protein 1 (NOG1); This family represents a conserved region of ...
77-123 5.49e-03

Nucleolar GTP-binding protein 1 (NOG1); This family represents a conserved region of approximately 60 residues in length within nucleolar GTP-binding protein 1 (NOG1). In S. cerevisiae, the NOG1 gene has been shown to be essential for cell viability, suggesting that NOG1 may play an important role in nucleolar functions. Family members include eukaryotic, bacterial and archaeal proteins.


Pssm-ID: 462021 [Multi-domain]  Cd Length: 58  Bit Score: 35.11  E-value: 5.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1174098179  77 QTILAIEE-ADIIVFVVDGSTgplTDDYAIAS--HLRSS------GKPVIIAANKS 123
Cdd:pfam06858   5 QAIAALAHlADAVLFVIDPSE---TCGYSLEEqlSLFEEikplfaNKPVIVVLNKI 57
Dynamin_N pfam00350
Dynamin family;
202-235 5.98e-03

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 37.60  E-value: 5.98e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1174098179 202 LAVVGCPNAGKSSLVNRLVGEErLLASEIAGTTR 235
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRD-ILPRGPGPTTR 33
obgE PRK12296
GTPase CgtA; Reviewed
7-201 7.54e-03

GTPase CgtA; Reviewed


Pssm-ID: 237045 [Multi-domain]  Cd Length: 500  Bit Score: 38.70  E-value: 7.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179   7 VALVGRPNVGKSTLFNRLTRTRDAlVDDTPGLTRDRQYGIMKRGDTPFPMVDTggfeadPGetmvsLIRG---------Q 77
Cdd:PRK12296  162 VGLVGFPSAGKSSLISALSAAKPK-IADYPFTTLVPNLGVVQAGDTRFTVADV------PG-----LIPGasegkglglD 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174098179  78 TILAIEEADIIVFVVDGST-----GPLTDDYAIASHLRSSG--------------KPVIIAANK-----SEKKAATASIE 133
Cdd:PRK12296  230 FLRHIERCAVLVHVVDCATlepgrDPLSDIDALEAELAAYApaldgdlglgdlaeRPRLVVLNKidvpdARELAEFVRPE 309
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1174098179 134 FHELGMePIIPISSAHGLGigdlletLEEMTDAM-----EGFCRQPEEQ-----LLPLEVEQENPEVAREPRFKGPLR 201
Cdd:PRK12296  310 LEARGW-PVFEVSAASREG-------LRELSFALaelveEARAAEPEAEptrivIRPKAVDDAGFTVERDGDGEGGFR 379
 
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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