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Conserved domains on  [gi|490246132|ref|WP_004144309|]
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MULTISPECIES: ribosome biogenesis GTPase Der [Klebsiella]

Protein Classification

ribosome biogenesis GTPase Der( domain architecture ID 11478009)

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

CATH:  3.40.50.300
PubMed:  25389271|12467572
SCOP:  4004038

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
2-464 0e+00

GTP-binding protein Der; Reviewed


:

Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 754.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   2 IPVVALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGREFICIDTGGIDGTEEGVETRMAEQSLLAIEE 81
Cdd:PRK00093   1 KPVVAIVGRPNVGKSTLFNRLTGKRDAIVADTPGVTRDRIYGEAEWLGREFILIDTGGIEPDDDGFEKQIREQAELAIEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  82 ADVVLFMVDARAGLMPADIAIAKHLRSREKPTFLVANKTDGIDVDQAMADFWSLGLGDIYPIAASHGRGVTSLLEQALlp 161
Cdd:PRK00093  81 ADVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDGPDEEADAYEFYSLGLGEPYPISAEHGRGIGDLLDAIL-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 162 wvdevnpqeevdedaeywakfeaeqngeAEEEPEDDFNPQDLPIKLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRD 241
Cdd:PRK00093 159 ----------------------------EELPEEEEEDEEDEPIKIAIIGRPNVGKSSLINALLGEERVIVSDIAGTTRD 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 242 SIYIPMQRDEREYVLIDTAGVRKRGKITDVVEKFSVIKTLQAIEDANVVLLVIDAREGISDQDLSLLGFILNSGRSLVIV 321
Cdd:PRK00093 211 SIDTPFERDGQKYTLIDTAGIRRKGKVTEGVEKYSVIRTLKAIERADVVLLVIDATEGITEQDLRIAGLALEAGRALVIV 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 322 VNKWDGLSQEVKEQVKETLDYRLGFIDFARVHFISALHGSGVGNLFESVREAYDSATRRVSTAMLTRIMNMAAEDHQPPL 401
Cdd:PRK00093 291 VNKWDLVDEKTMEEFKKELRRRLPFLDYAPIVFISALTGQGVDKLLEAIDEAYENANRRISTSVLNRVLEEAVERHPPPL 370
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490246132 402 VRGRRVKLKYAHAGGYNPPIVVIHGNQVKDLPDSYKRYLMNYFRKSLDVMGTPIRIQFKEGEN 464
Cdd:PRK00093 371 VKGRRLKIKYATQVGTNPPTFVLFVNDPELLPFSYKRYLENQLREAFDFEGTPIRLEFREKKN 433
 
Name Accession Description Interval E-value
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
2-464 0e+00

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 754.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   2 IPVVALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGREFICIDTGGIDGTEEGVETRMAEQSLLAIEE 81
Cdd:PRK00093   1 KPVVAIVGRPNVGKSTLFNRLTGKRDAIVADTPGVTRDRIYGEAEWLGREFILIDTGGIEPDDDGFEKQIREQAELAIEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  82 ADVVLFMVDARAGLMPADIAIAKHLRSREKPTFLVANKTDGIDVDQAMADFWSLGLGDIYPIAASHGRGVTSLLEQALlp 161
Cdd:PRK00093  81 ADVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDGPDEEADAYEFYSLGLGEPYPISAEHGRGIGDLLDAIL-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 162 wvdevnpqeevdedaeywakfeaeqngeAEEEPEDDFNPQDLPIKLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRD 241
Cdd:PRK00093 159 ----------------------------EELPEEEEEDEEDEPIKIAIIGRPNVGKSSLINALLGEERVIVSDIAGTTRD 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 242 SIYIPMQRDEREYVLIDTAGVRKRGKITDVVEKFSVIKTLQAIEDANVVLLVIDAREGISDQDLSLLGFILNSGRSLVIV 321
Cdd:PRK00093 211 SIDTPFERDGQKYTLIDTAGIRRKGKVTEGVEKYSVIRTLKAIERADVVLLVIDATEGITEQDLRIAGLALEAGRALVIV 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 322 VNKWDGLSQEVKEQVKETLDYRLGFIDFARVHFISALHGSGVGNLFESVREAYDSATRRVSTAMLTRIMNMAAEDHQPPL 401
Cdd:PRK00093 291 VNKWDLVDEKTMEEFKKELRRRLPFLDYAPIVFISALTGQGVDKLLEAIDEAYENANRRISTSVLNRVLEEAVERHPPPL 370
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490246132 402 VRGRRVKLKYAHAGGYNPPIVVIHGNQVKDLPDSYKRYLMNYFRKSLDVMGTPIRIQFKEGEN 464
Cdd:PRK00093 371 VKGRRLKIKYATQVGTNPPTFVLFVNDPELLPFSYKRYLENQLREAFDFEGTPIRLEFREKKN 433
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
1-465 0e+00

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 750.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   1 MIPVVALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGREFICIDTGGID-GTEEGVETRMAEQSLLAI 79
Cdd:COG1160    1 MSPVVAIVGRPNVGKSTLFNRLTGRRDAIVDDTPGVTRDRIYGEAEWGGREFTLIDTGGIEpDDDDGLEAEIREQAELAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  80 EEADVVLFMVDARAGLMPADIAIAKHLRSREKPTFLVANKTDGIDVDQAMADFWSLGLGDIYPIAASHGRGVTSLLEQAL 159
Cdd:COG1160   81 EEADVILFVVDGRAGLTPLDEEIAKLLRRSGKPVILVVNKVDGPKREADAAEFYSLGLGEPIPISAEHGRGVGDLLDAVL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 160 lpwvdevnpqeevdedaeywAKFEAEQngeaEEEPEDDfnpqdlPIKLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTT 239
Cdd:COG1160  161 --------------------ELLPEEE----EEEEEDD------PIKIAIVGRPNVGKSSLINALLGEERVIVSDIAGTT 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 240 RDSIYIPMQRDEREYVLIDTAGVRKRGKITDVVEKFSVIKTLQAIEDANVVLLVIDAREGISDQDLSLLGFILNSGRSLV 319
Cdd:COG1160  211 RDSIDTPFERDGKKYTLIDTAGIRRKGKVDEGIEKYSVLRTLRAIERADVVLLVIDATEGITEQDLKIAGLALEAGKALV 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 320 IVVNKWDGLS--QEVKEQVKETLDYRLGFIDFARVHFISALHGSGVGNLFESVREAYDSATRRVSTAMLTRIMNMAAEDH 397
Cdd:COG1160  291 IVVNKWDLVEkdRKTREELEKEIRRRLPFLDYAPIVFISALTGQGVDKLLEAVDEVYESANKRISTSKLNRVLEEAVERH 370
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490246132 398 QPPLVRGRRVKLKYAHAGGYNPPIVVIHGNQVKDLPDSYKRYLMNYFRKSLDVMGTPIRIQFKEGENP 465
Cdd:COG1160  371 PPPAVKGRRLKIYYATQVGTRPPTFVLFVNDPELLPFSYKRYLENQLREAFGFEGTPIRIEFRKRKNP 438
GTPase_EngA TIGR03594
ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase ...
5-460 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: 699.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132    5 VALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGREFICIDTGGIDGTEEGVETRMAEQSLLAIEEADV 84
Cdd:TIGR03594   1 VAIVGRPNVGKSTLFNRLTGKRDAIVDDTPGVTRDRIYGDAEWGGREFILIDTGGIEEDDDGIDAQIREQAEIAIEEADV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   85 VLFMVDARAGLMPADIAIAKHLRSREKPTFLVANKTDGIDVDQAMADFWSLGLGDIYPIAASHGRGVTSLLEQALLPWvd 164
Cdd:TIGR03594  81 ILFVVDGREGLTPEDEEIAKWLRKSGKPVILVANKIDGPKEDADAAEFYSLGFGEPIPISAEHGRGIGDLLDAILELL-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  165 evnPQEEVDEDAEywakfeaeqngeaeeepeddfnpqDLPIKLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSIY 244
Cdd:TIGR03594 159 ---PEEEEEEEEE------------------------EDPIKIAIIGRPNVGKSTLVNALLGEERVIVSDIAGTTRDSID 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  245 IPMQRDEREYVLIDTAGVRKRGKITDVVEKFSVIKTLQAIEDANVVLLVIDAREGISDQDLSLLGFILNSGRSLVIVVNK 324
Cdd:TIGR03594 212 IPFERDGKKYTLIDTAGIRRKGKVTEGVEKYSVLRTLKAIERADVVLLVLDATEGITEQDLRIAGLALEAGKALVIVVNK 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  325 WDGL-SQEVKEQVKETLDYRLGFIDFARVHFISALHGSGVGNLFESVREAYDSATRRVSTAMLTRIMNMAAEDHQPPLVR 403
Cdd:TIGR03594 292 WDLVeDEKTRKEIKKELRRKLPFLDFAPIVFISALTGQGVDKLLDAIDKVYESANKRISTSKLNRVLEEAVAAHPPPLVG 371
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 490246132  404 GRRVKLKYAHAGGYNPPIVVIHGNQVKDLPDSYKRYLMNYFRKSLDVMGTPIRIQFK 460
Cdd:TIGR03594 372 GRRVKIKYATQVGTNPPTFVLFGNRPELLPFSYKRYLENQFREAFGFEGTPIRLEFK 428
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
204-374 2.04e-95

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: 285.87  E-value: 2.04e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 204 PIKLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSIYIPMQRDEREYVLIDTAGVRKRGKITDVVEKFSVIKTLQA 283
Cdd:cd01895    2 PIKIAIIGRPNVGKSSLLNALLGEERVIVSDIAGTTRDSIDVPFEYDGQKYTLIDTAGIRKKGKVTEGIEKYSVLRTLKA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 284 IEDANVVLLVIDAREGISDQDLSLLGFILNSGRSLVIVVNKWDGLS--QEVKEQVKETLDYRLGFIDFARVHFISALHGS 361
Cdd:cd01895   82 IERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVEkdEKTMKEFEKELRRKLPFLDYAPIVFISALTGQ 161
                        170
                 ....*....|...
gi 490246132 362 GVGNLFESVREAY 374
Cdd:cd01895  162 GVDKLFDAIKEVY 174
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
5-119 1.23e-38

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: 136.21  E-value: 1.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132    5 VALVGRPNVGKSTLFNRLTRTRdALVADFPGLTRDRKYGRAEVEGREFICIDTGGIdgTEEGVETRMAEQSLLAIEEADV 84
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGAK-AIVSDYPGTTRDPNEGRLELKGKQIILVDTPGL--IEGASEGEGLGRAFLAIIEADL 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 490246132   85 VLFMVDARAGLMPADIAIAKHLRSREKPTFLVANK 119
Cdd:pfam01926  79 ILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
 
Name Accession Description Interval E-value
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
2-464 0e+00

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 754.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   2 IPVVALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGREFICIDTGGIDGTEEGVETRMAEQSLLAIEE 81
Cdd:PRK00093   1 KPVVAIVGRPNVGKSTLFNRLTGKRDAIVADTPGVTRDRIYGEAEWLGREFILIDTGGIEPDDDGFEKQIREQAELAIEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  82 ADVVLFMVDARAGLMPADIAIAKHLRSREKPTFLVANKTDGIDVDQAMADFWSLGLGDIYPIAASHGRGVTSLLEQALlp 161
Cdd:PRK00093  81 ADVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDGPDEEADAYEFYSLGLGEPYPISAEHGRGIGDLLDAIL-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 162 wvdevnpqeevdedaeywakfeaeqngeAEEEPEDDFNPQDLPIKLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRD 241
Cdd:PRK00093 159 ----------------------------EELPEEEEEDEEDEPIKIAIIGRPNVGKSSLINALLGEERVIVSDIAGTTRD 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 242 SIYIPMQRDEREYVLIDTAGVRKRGKITDVVEKFSVIKTLQAIEDANVVLLVIDAREGISDQDLSLLGFILNSGRSLVIV 321
Cdd:PRK00093 211 SIDTPFERDGQKYTLIDTAGIRRKGKVTEGVEKYSVIRTLKAIERADVVLLVIDATEGITEQDLRIAGLALEAGRALVIV 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 322 VNKWDGLSQEVKEQVKETLDYRLGFIDFARVHFISALHGSGVGNLFESVREAYDSATRRVSTAMLTRIMNMAAEDHQPPL 401
Cdd:PRK00093 291 VNKWDLVDEKTMEEFKKELRRRLPFLDYAPIVFISALTGQGVDKLLEAIDEAYENANRRISTSVLNRVLEEAVERHPPPL 370
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490246132 402 VRGRRVKLKYAHAGGYNPPIVVIHGNQVKDLPDSYKRYLMNYFRKSLDVMGTPIRIQFKEGEN 464
Cdd:PRK00093 371 VKGRRLKIKYATQVGTNPPTFVLFVNDPELLPFSYKRYLENQLREAFDFEGTPIRLEFREKKN 433
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
1-465 0e+00

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 750.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   1 MIPVVALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGREFICIDTGGID-GTEEGVETRMAEQSLLAI 79
Cdd:COG1160    1 MSPVVAIVGRPNVGKSTLFNRLTGRRDAIVDDTPGVTRDRIYGEAEWGGREFTLIDTGGIEpDDDDGLEAEIREQAELAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  80 EEADVVLFMVDARAGLMPADIAIAKHLRSREKPTFLVANKTDGIDVDQAMADFWSLGLGDIYPIAASHGRGVTSLLEQAL 159
Cdd:COG1160   81 EEADVILFVVDGRAGLTPLDEEIAKLLRRSGKPVILVVNKVDGPKREADAAEFYSLGLGEPIPISAEHGRGVGDLLDAVL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 160 lpwvdevnpqeevdedaeywAKFEAEQngeaEEEPEDDfnpqdlPIKLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTT 239
Cdd:COG1160  161 --------------------ELLPEEE----EEEEEDD------PIKIAIVGRPNVGKSSLINALLGEERVIVSDIAGTT 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 240 RDSIYIPMQRDEREYVLIDTAGVRKRGKITDVVEKFSVIKTLQAIEDANVVLLVIDAREGISDQDLSLLGFILNSGRSLV 319
Cdd:COG1160  211 RDSIDTPFERDGKKYTLIDTAGIRRKGKVDEGIEKYSVLRTLRAIERADVVLLVIDATEGITEQDLKIAGLALEAGKALV 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 320 IVVNKWDGLS--QEVKEQVKETLDYRLGFIDFARVHFISALHGSGVGNLFESVREAYDSATRRVSTAMLTRIMNMAAEDH 397
Cdd:COG1160  291 IVVNKWDLVEkdRKTREELEKEIRRRLPFLDYAPIVFISALTGQGVDKLLEAVDEVYESANKRISTSKLNRVLEEAVERH 370
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490246132 398 QPPLVRGRRVKLKYAHAGGYNPPIVVIHGNQVKDLPDSYKRYLMNYFRKSLDVMGTPIRIQFKEGENP 465
Cdd:COG1160  371 PPPAVKGRRLKIYYATQVGTRPPTFVLFVNDPELLPFSYKRYLENQLREAFGFEGTPIRIEFRKRKNP 438
GTPase_EngA TIGR03594
ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase ...
5-460 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: 699.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132    5 VALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGREFICIDTGGIDGTEEGVETRMAEQSLLAIEEADV 84
Cdd:TIGR03594   1 VAIVGRPNVGKSTLFNRLTGKRDAIVDDTPGVTRDRIYGDAEWGGREFILIDTGGIEEDDDGIDAQIREQAEIAIEEADV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   85 VLFMVDARAGLMPADIAIAKHLRSREKPTFLVANKTDGIDVDQAMADFWSLGLGDIYPIAASHGRGVTSLLEQALLPWvd 164
Cdd:TIGR03594  81 ILFVVDGREGLTPEDEEIAKWLRKSGKPVILVANKIDGPKEDADAAEFYSLGFGEPIPISAEHGRGIGDLLDAILELL-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  165 evnPQEEVDEDAEywakfeaeqngeaeeepeddfnpqDLPIKLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSIY 244
Cdd:TIGR03594 159 ---PEEEEEEEEE------------------------EDPIKIAIIGRPNVGKSTLVNALLGEERVIVSDIAGTTRDSID 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  245 IPMQRDEREYVLIDTAGVRKRGKITDVVEKFSVIKTLQAIEDANVVLLVIDAREGISDQDLSLLGFILNSGRSLVIVVNK 324
Cdd:TIGR03594 212 IPFERDGKKYTLIDTAGIRRKGKVTEGVEKYSVLRTLKAIERADVVLLVLDATEGITEQDLRIAGLALEAGKALVIVVNK 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  325 WDGL-SQEVKEQVKETLDYRLGFIDFARVHFISALHGSGVGNLFESVREAYDSATRRVSTAMLTRIMNMAAEDHQPPLVR 403
Cdd:TIGR03594 292 WDLVeDEKTRKEIKKELRRKLPFLDFAPIVFISALTGQGVDKLLDAIDKVYESANKRISTSKLNRVLEEAVAAHPPPLVG 371
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 490246132  404 GRRVKLKYAHAGGYNPPIVVIHGNQVKDLPDSYKRYLMNYFRKSLDVMGTPIRIQFK 460
Cdd:TIGR03594 372 GRRVKIKYATQVGTNPPTFVLFGNRPELLPFSYKRYLENQFREAFGFEGTPIRLEFK 428
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
3-458 2.13e-111

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 337.71  E-value: 2.13e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   3 PVVALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGREFICIDTGGIDGTEEGVETRMAEQSLLAIEEA 82
Cdd:PRK03003  39 PVVAVVGRPNVGKSTLVNRILGRREAVVEDVPGVTRDRVSYDAEWNGRRFTVVDTGGWEPDAKGLQASVAEQAEVAMRTA 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  83 DVVLFMVDARAGLMPADIAIAKHLRSREKPTFLVANKTDGIDVDQAMADFWSLGLGDIYPIAASHGRGVTSLLEQAL--L 160
Cdd:PRK03003 119 DAVLFVVDATVGATATDEAVARVLRRSGKPVILAANKVDDERGEADAAALWSLGLGEPHPVSALHGRGVGDLLDAVLaaL 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 161 PwvdevnpqeevdedaeywakfeaeqngeaeEEPEDDfNPQDLPIKLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTR 240
Cdd:PRK03003 199 P------------------------------EVPRVG-SASGGPRRVALVGKPNVGKSSLLNKLAGEERSVVDDVAGTTV 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 241 DSIYIPMQRDEREYVLIDTAGVRKRGKITDVVEKFSVIKTLQAIEDANVVLLVIDAREGISDQDLSLLGFILNSGRSLVI 320
Cdd:PRK03003 248 DPVDSLIELGGKTWRFVDTAGLRRRVKQASGHEYYASLRTHAAIEAAEVAVVLIDASEPISEQDQRVLSMVIEAGRALVL 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 321 VVNKWDGLSQEVKEQVKETLDYRLGFIDFA-RVHfISALHGSGVGNLFESVREAYDSATRRVSTAMLTRIMNMAAEDHQP 399
Cdd:PRK03003 328 AFNKWDLVDEDRRYYLEREIDRELAQVPWApRVN-ISAKTGRAVDKLVPALETALESWDTRIPTGRLNAWLGELVAATPP 406
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490246132 400 PLVRGRRVKLKYAHAGGYNPPIVVIHGNQVkdLPDSYKRYLMNYFRKSLDVMGTPIRIQ 458
Cdd:PRK03003 407 PVRGGKQPRILFATQASTRPPTFVLFTTGF--LEAGYRRFLERRLRETFGFEGSPIRIS 463
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
4-460 2.11e-103

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 324.83  E-value: 2.11e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   4 VVALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGREFICIDTGGIDGTEEGVETRMAEQSLLAIEEAD 83
Cdd:PRK09518 277 VVAIVGRPNVGKSTLVNRILGRREAVVEDTPGVTRDRVSYDAEWAGTDFKLVDTGGWEADVEGIDSAIASQAQIAVSLAD 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  84 VVLFMVDARAGLMPADIAIAKHLRSREKPTFLVANKTDGIDVDQAMADFWSLGLGDIYPIAASHGRGVTSLLEQALlpwv 163
Cdd:PRK09518 357 AVVFVVDGQVGLTSTDERIVRMLRRAGKPVVLAVNKIDDQASEYDAAEFWKLGLGEPYPISAMHGRGVGDLLDEAL---- 432
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 164 dEVNPqeevdedaeywakfeaeqngeaEEEPEDDFNPQDLPIKLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSI 243
Cdd:PRK09518 433 -DSLK----------------------VAEKTSGFLTPSGLRRVALVGRPNVGKSSLLNQLTHEERAVVNDLAGTTRDPV 489
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 244 YIPMQRDEREYVLIDTAGVRKRGKITDVVEKFSVIKTLQAIEDANVVLLVIDAREGISDQDLSLLGFILNSGRSLVIVVN 323
Cdd:PRK09518 490 DEIVEIDGEDWLFIDTAGIKRRQHKLTGAEYYSSLRTQAAIERSELALFLFDASQPISEQDLKVMSMAVDAGRALVLVFN 569
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 324 KWDGLSQEVKEQVKETLDYRLGFIDFARVHFISALHGSGVGNLFESVREAYDSATRRVSTAMLTRIMNMAAEDHQPPLVR 403
Cdd:PRK09518 570 KWDLMDEFRRQRLERLWKTEFDRVTWARRVNLSAKTGWHTNRLAPAMQEALESWDQRIPTGKLNAFLGKIQAEHPHPLRG 649
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490246132 404 GRRVKLKYAHAGGYNPPIVVIHGNQVkdLPDSYKRYLMNYFRKSLDVMGTPIRIQFK 460
Cdd:PRK09518 650 GKQPRILFATQASTRPPRFVIFTTGF--LEHGYRRFLERSLREEFGFEGSPIQISVN 704
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
204-374 2.04e-95

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: 285.87  E-value: 2.04e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 204 PIKLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSIYIPMQRDEREYVLIDTAGVRKRGKITDVVEKFSVIKTLQA 283
Cdd:cd01895    2 PIKIAIIGRPNVGKSSLLNALLGEERVIVSDIAGTTRDSIDVPFEYDGQKYTLIDTAGIRKKGKVTEGIEKYSVLRTLKA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 284 IEDANVVLLVIDAREGISDQDLSLLGFILNSGRSLVIVVNKWDGLS--QEVKEQVKETLDYRLGFIDFARVHFISALHGS 361
Cdd:cd01895   82 IERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVEkdEKTMKEFEKELRRKLPFLDYAPIVFISALTGQ 161
                        170
                 ....*....|...
gi 490246132 362 GVGNLFESVREAY 374
Cdd:cd01895  162 GVDKLFDAIKEVY 174
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
6-159 7.08e-89

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: 268.53  E-value: 7.08e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   6 ALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGREFICIDTGGIDGTEEGVETRMAEQSLLAIEEADVV 85
Cdd:cd01894    1 AIVGRPNVGKSTLFNRLTGRRDAIVSDTPGVTRDRKYGEAEWGGREFILIDTGGIEPDDEGISKEIREQAEIAIEEADVI 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490246132  86 LFMVDARAGLMPADIAIAKHLRSREKPTFLVANKTDGIDVDQAMADFWSLGLGDIYPIAASHGRGVTSLLEQAL 159
Cdd:cd01894   81 LFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNIKEEEEAAEFYSLGFGEPIPISAEHGRGIGDLLDAIL 154
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
208-374 9.17e-45

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: 154.13  E-value: 9.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 208 AIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSIYIPMQRDEREYVLIDTAGvrkrgkITDVVEKFS---VIKTLQAI 284
Cdd:cd01894    1 AIVGRPNVGKSTLFNRLTGRRDAIVSDTPGVTRDRKYGEAEWGGREFILIDTGG------IEPDDEGISkeiREQAEIAI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 285 EDANVVLLVIDAREGISDQDLSLLGFILNSGRSLVIVVNKWDGLSQEvkEQVKETldYRLGFIDfarVHFISALHGSGVG 364
Cdd:cd01894   75 EEADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNIKEE--EEAAEF--YSLGFGE---PIPISAEHGRGIG 147
                        170
                 ....*....|
gi 490246132 365 NLFESVREAY 374
Cdd:cd01894  148 DLLDAILELL 157
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
5-119 1.23e-38

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: 136.21  E-value: 1.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132    5 VALVGRPNVGKSTLFNRLTRTRdALVADFPGLTRDRKYGRAEVEGREFICIDTGGIdgTEEGVETRMAEQSLLAIEEADV 84
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGAK-AIVSDYPGTTRDPNEGRLELKGKQIILVDTPGL--IEGASEGEGLGRAFLAIIEADL 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 490246132   85 VLFMVDARAGLMPADIAIAKHLRSREKPTFLVANK 119
Cdd:pfam01926  79 ILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
205-366 9.20e-37

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: 133.00  E-value: 9.20e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 205 IKLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSIYIPMQRDEREYVLIDTAGVRKRgkiTDVVEKFSVIKTLQAI 284
Cdd:cd04164    4 IKVVIAGKPNVGKSSLLNALAGRDRAIVSDIAGTTRDVIEEEIDLGGIPVRLIDTAGLRET---EDEIEKIGIERAREAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 285 EDANVVLLVIDAREGISDQDLSLLgfILNSGRSLVIVVNKWDgLSQEVKEQVKETLDyrlgfidfaRVHFISALHGSGVG 364
Cdd:cd04164   81 EEADLVLLVVDASEGLDEEDLEIL--ELPAKKPVIVVLNKSD-LLSDAEGISELNGK---------PIIAISAKTGEGID 148

                 ..
gi 490246132 365 NL 366
Cdd:cd04164  149 EL 150
KH_dom-like pfam14714
KH-domain-like of EngA bacterial GTPase enzymes, C-terminal; The KH-like domain at the ...
380-460 2.44e-36

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: 129.06  E-value: 2.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  380 RVSTAMLTRIMNMAAEDHQPPLVRGRRVKLKYAHAGGYNPPIVVIHGNQVKDLPDSYKRYLMNYFRKSLDVMGTPIRIQF 459
Cdd:pfam14714   1 RISTSELNRVLEEAVARHPPPSVKGKRLKIYYATQVGTRPPTFVLFVNDPELVPFSYKRYLENQLREAFGFEGTPIRLIF 80

                  .
gi 490246132  460 K 460
Cdd:pfam14714  81 R 81
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
206-324 9.01e-36

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: 128.51  E-value: 9.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  206 KLAIVGRPNVGKSTLTNRILGEdRVVVYDMPGTTRDSIYIPMQRDEREYVLIDTAGVrkrgkITDVVEKFSVIKTLQAIE 285
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGA-KAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGL-----IEGASEGEGLGRAFLAII 74
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 490246132  286 DANVVLLVIDAREGISDQDLSLLGFILNSGRSLVIVVNK 324
Cdd:pfam01926  75 EADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
205-388 2.34e-35

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: 136.73  E-value: 2.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 205 IKLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSIyipmqrdeREYV--------LIDTAGVRKRgkiTDVVEKFS 276
Cdd:COG0486  214 IKVVIVGRPNVGKSSLLNALLGEERAIVTDIAGTTRDVI--------EERIniggipvrLIDTAGLRET---EDEVEKIG 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 277 VIKTLQAIEDANVVLLVIDAREGISDQDLSLLGFIlnSGRSLVIVVNKWDgLSQEVKEQVKEtldyrlgfIDFARVHFIS 356
Cdd:COG0486  283 IERAREAIEEADLVLLLLDASEPLTEEDEEILEKL--KDKPVIVVLNKID-LPSEADGELKS--------LPGEPVIAIS 351
                        170       180       190
                 ....*....|....*....|....*....|..
gi 490246132 357 ALHGSGVGNLFESVREAYDSATRRVSTAMLTR 388
Cdd:COG0486  352 AKTGEGIDELKEAILELVGEGALEGEGVLLTN 383
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
205-388 6.35e-35

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: 132.99  E-value: 6.35e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  205 IKLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSIyipmqrdeREYV--------LIDTAGVRKRgkiTDVVEKFS 276
Cdd:pfam12631  95 IKVVIVGKPNVGKSSLLNALLGEERAIVTDIPGTTRDVI--------EETIniggiplrLIDTAGIRET---DDEVEKIG 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  277 VIKTLQAIEDANVVLLVIDAREGISDQDLSLLGFILNsGRSLVIVVNKWDgLSQEVKEQVKETLDYRLgfidfarvhFIS 356
Cdd:pfam12631 164 IERAREAIEEADLVLLVLDASRPLDEEDLEILELLKD-KKPIIVVLNKSD-LLGEIDELEELKGKPVL---------AIS 232
                         170       180       190
                  ....*....|....*....|....*....|..
gi 490246132  357 ALHGSGVGNLFESVREAYDSATRRVSTAMLTR 388
Cdd:pfam12631 233 AKTGEGLDELEEAIKELFLAGEIASDGPIITN 264
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
208-372 2.02e-32

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: 121.41  E-value: 2.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 208 AIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRD---SIYIpmqRDEREYVLIDTAGVRKRGKITDvveKFSVIKTLQAI 284
Cdd:cd04163    7 AIIGRPNVGKSTLLNALVGQKISIVSPKPQTTRNrirGIYT---DDDAQIIFVDTPGIHKPKKKLG---ERMVKAAWSAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 285 EDANVVLLVIDAREGISDQDLSLLGFILNSGRSLVIVVNKWDGLSQevKEQVKETLDYRLGFIDFARVHFISALHGSGVG 364
Cdd:cd04163   81 KDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLVKD--KEDLLPLLEKLKELHPFAEIFPISALKGENVD 158

                 ....*...
gi 490246132 365 NLFESVRE 372
Cdd:cd04163  159 ELLEYIVE 166
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
208-372 1.56e-31

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: 118.89  E-value: 1.56e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 208 AIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSIYIPMQ-RDEREYVLIDTAGVRKrgkiTDVVEKFSVIKTLQAIED 286
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRKEWElLPLGPVVLIDTPGLDE----EGGLGRERVEEARQVADR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 287 ANVVLLVIDAREGISDQDLsLLGFILNSGRSLVIVVNKWDgLSQEvKEQVKETLDYRLGFIDFARVHFISALHGSGVGNL 366
Cdd:cd00880   77 ADLVLLVVDSDLTPVEEEA-KLGLLRERGKPVLLVLNKID-LVPE-SEEEELLRERKLELLPDLPVIAVSALPGEGIDEL 153

                 ....*.
gi 490246132 367 FESVRE 372
Cdd:cd00880  154 RKKIAE 159
era PRK00089
GTPase Era; Reviewed
208-372 5.05e-31

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 121.31  E-value: 5.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 208 AIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSIYIPMQRDEREYVLIDTAGV-RKRGKItdvvEKFSVIKTLQAIED 286
Cdd:PRK00089   9 AIVGRPNVGKSTLLNALVGQKISIVSPKPQTTRHRIRGIVTEDDAQIIFVDTPGIhKPKRAL----NRAMNKAAWSSLKD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 287 ANVVLLVIDAREGISDQDLSLLGFILNSGRSLVIVVNKWDGLSQevKEQVKETLDYRLGFIDFARVHFISALHGSGVGNL 366
Cdd:PRK00089  85 VDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVKD--KEELLPLLEELSELMDFAEIVPISALKGDNVDEL 162

                 ....*.
gi 490246132 367 FESVRE 372
Cdd:PRK00089 163 LDVIAK 168
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
208-372 4.03e-30

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 118.94  E-value: 4.03e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 208 AIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSIYIPMQRDEREYVLIDTAGV-RKRGKITDVVEKFSviktLQAIED 286
Cdd:COG1159    7 AIVGRPNVGKSTLLNALVGQKVSIVSPKPQTTRHRIRGIVTREDAQIVFVDTPGIhKPKRKLGRRMNKAA----WSALED 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 287 ANVVLLVIDAREGISDQDLSLLGFILNSGRSLVIVVNKWDGLSqevKEQVKETLDYRLGFIDFARVHFISALHGSGVGNL 366
Cdd:COG1159   83 VDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLVK---KEELLPLLAEYSELLDFAEIVPISALKGDNVDEL 159

                 ....*.
gi 490246132 367 FESVRE 372
Cdd:COG1159  160 LDEIAK 165
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
205-366 6.05e-30

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 121.76  E-value: 6.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 205 IKLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSIyipmqrdeREYV--------LIDTAGVRKRgkiTDVVEKFS 276
Cdd:PRK05291 216 LKVVIAGRPNVGKSSLLNALLGEERAIVTDIAGTTRDVI--------EEHInldgiplrLIDTAGIRET---DDEVEKIG 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 277 VIKTLQAIEDANVVLLVIDAREGISDQDLSLLgfILNSGRSLVIVVNKWDgLSQEVKEQvketldyrlgFIDFARVHFIS 356
Cdd:PRK05291 285 IERSREAIEEADLVLLVLDASEPLTEEDDEIL--EELKDKPVIVVLNKAD-LTGEIDLE----------EENGKPVIRIS 351
                        170
                 ....*....|
gi 490246132 357 ALHGSGVGNL 366
Cdd:PRK05291 352 AKTGEGIDEL 361
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
5-157 1.99e-29

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: 112.97  E-value: 1.99e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   5 VALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGREFICIDTGGIDGTEEGVEtRMA-EQSLLAIEEAD 83
Cdd:cd04164    6 VVIAGKPNVGKSSLLNALAGRDRAIVSDIAGTTRDVIEEEIDLGGIPVRLIDTAGLRETEDEIE-KIGiERAREAIEEAD 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490246132  84 VVLFMVDARAGLMPADIAIakHLRSREKPTFLVANKtdgIDVDQAMADFWSLGLGDIYPIAASHGRGVTSLLEQ 157
Cdd:cd04164   85 LVLLVVDASEGLDEEDLEI--LELPAKKPVIVVLNK---SDLLSDAEGISELNGKPIIAISAKTGEGIDELKEA 153
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
171-373 2.09e-28

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 117.38  E-value: 2.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 171 EVDEDAEYWAKFEAEQNGEAEEEPEDDFNPQdLPIkLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSIYIPMQRD 250
Cdd:PRK03003   7 EMRADGTWADESDWELDDEDLAELEAAEGGP-LPV-VAVVGRPNVGKSTLVNRILGRREAVVEDVPGVTRDRVSYDAEWN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 251 EREYVLIDTAG--VRKRGKITDVVEKFSViktlqAIEDANVVLLVIDAREGISDQDLSLLGFILNSGRSLVIVVNKWDGL 328
Cdd:PRK03003  85 GRRFTVVDTGGwePDAKGLQASVAEQAEV-----AMRTADAVLFVVDATVGATATDEAVARVLRRSGKPVILAANKVDDE 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 490246132 329 SQEvkeqVKETLDYRLGFIDfarVHFISALHGSGVGNLFESVREA 373
Cdd:PRK03003 160 RGE----ADAAALWSLGLGE---PHPVSALHGRGVGDLLDAVLAA 197
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
5-171 3.84e-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: 116.31  E-value: 3.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   5 VALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGREFICIDTGGIDGTEEGVETRMAEQSLLAIEEADV 84
Cdd:COG0486  216 VVIVGRPNVGKSSLLNALLGEERAIVTDIAGTTRDVIEERINIGGIPVRLIDTAGLRETEDEVEKIGIERAREAIEEADL 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  85 VLFMVDARAGLMPADIAIAKHLrsREKPTFLVANKTDGIDVDQamADFWSLGLGDIYPIAASHGRGVtSLLEQALLPWVD 164
Cdd:COG0486  296 VLLLLDASEPLTEEDEEILEKL--KDKPVIVVLNKIDLPSEAD--GELKSLPGEPVIAISAKTGEGI-DELKEAILELVG 370

                 ....*..
gi 490246132 165 EVNPQEE 171
Cdd:COG0486  371 EGALEGE 377
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
5-160 2.26e-27

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 114.05  E-value: 2.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   5 VALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGREFICIDTGGIDGTEEGVEtRMA-EQSLLAIEEAD 83
Cdd:PRK05291 218 VVIAGRPNVGKSSLLNALLGEERAIVTDIAGTTRDVIEEHINLDGIPLRLIDTAGIRETDDEVE-KIGiERSREAIEEAD 296
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490246132  84 VVLFMVDARAGLMPADIAIAkhLRSREKPTFLVANKtdgIDVDQAMADFWSLGLGDIYpIAASHGRGVtSLLEQALL 160
Cdd:PRK05291 297 LVLLVLDASEPLTEEDDEIL--EELKDKPVIVVLNK---ADLTGEIDLEEENGKPVIR-ISAKTGEGI-DELREAIK 366
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
208-370 1.05e-26

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: 105.62  E-value: 1.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 208 AIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSIYIPMQRDEREY--VLIDTAGVRKRGKITDvvekfsVIKTLQAIE 285
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKELDKGKVklVLVDTPGLDEFGGLGR------EELARLLLR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 286 DANVVLLVIDAREGISDQD--LSLLGFILNSGRSLVIVVNKWDGLSQEVKEQVKETLdyRLGFIDFARVHFISALHGSGV 363
Cdd:cd00882   75 GADLILLVVDSTDRESEEDakLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLE--ELAKILGVPVFEVSAKTGEGV 152

                 ....*..
gi 490246132 364 GNLFESV 370
Cdd:cd00882  153 DELFEKL 159
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
5-157 6.56e-26

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: 103.70  E-value: 6.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   5 VALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGREFICIDTGGIDGTEEGVETRMAEQSLLAIEEADV 84
Cdd:cd04163    6 VAIIGRPNVGKSTLLNALVGQKISIVSPKPQTTRNRIRGIYTDDDAQIIFVDTPGIHKPKKKLGERMVKAAWSALKDVDL 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490246132  85 VLFMVDARAGLMPADIAIAKHLRSREKPTFLVANKTDGI----DVDQAMADFWSLGLG-DIYPIAASHGRGVTSLLEQ 157
Cdd:cd04163   86 VLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLVkdkeDLLPLLEKLKELHPFaEIFPISALKGENVDELLEY 163
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
5-161 8.39e-26

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 106.61  E-value: 8.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   5 VALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGREFICIDTGGIDGTEEGVETRMAEQSLLAIEEADV 84
Cdd:COG1159    6 VAIVGRPNVGKSTLLNALVGQKVSIVSPKPQTTRHRIRGIVTREDAQIVFVDTPGIHKPKRKLGRRMNKAAWSALEDVDV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  85 VLFMVDARAGLMPADIAIAKHLRSREKPTFLVANKTDGIDVDQ---------AMADFWslglgDIYPIAASHGRGVTSLL 155
Cdd:COG1159   86 ILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLVKKEEllpllaeysELLDFA-----EIVPISALKGDNVDELL 160

                 ....*...
gi 490246132 156 EQ--ALLP 161
Cdd:COG1159  161 DEiaKLLP 168
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
5-160 1.00e-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: 107.18  E-value: 1.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132    5 VALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGREFICIDTGGIDGTEEGVETRMAEQSLLAIEEADV 84
Cdd:pfam12631  97 VVIVGKPNVGKSSLLNALLGEERAIVTDIPGTTRDVIEETINIGGIPLRLIDTAGIRETDDEVEKIGIERAREAIEEADL 176
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490246132   85 VLFMVDARAGLMPADIAIAKHLRSReKPTFLVANKTDGIDVDQAMadfWSLGLGDIYPIAASHGRGVtSLLEQALL 160
Cdd:pfam12631 177 VLLVLDASRPLDEEDLEILELLKDK-KPIIVVLNKSDLLGEIDEL---EELKGKPVLAISAKTGEGL-DELEEAIK 247
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
6-157 4.63e-25

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: 101.17  E-value: 4.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   6 ALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEV-EGREFICIDTGGIDgtEEGVETRM-AEQSLLAIEEAD 83
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRKEWELlPLGPVVLIDTPGLD--EEGGLGRErVEEARQVADRAD 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490246132  84 VVLFMVDARAGLMPADIAIAKhLRSREKPTFLVANKTDGIDVDQAMADFWSLGLG-----DIYPIAASHGRGVTSLLEQ 157
Cdd:cd00880   79 LVLLVVDSDLTPVEEEAKLGL-LRERGKPVLLVLNKIDLVPESEEEELLRERKLEllpdlPVIAVSALPGEGIDELRKK 156
era PRK00089
GTPase Era; Reviewed
5-161 9.08e-25

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 103.97  E-value: 9.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   5 VALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGREFICIDTGGIDGTEEGVETRMAEQSLLAIEEADV 84
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQKISIVSPKPQTTRHRIRGIVTEDDAQIIFVDTPGIHKPKRALNRAMNKAAWSSLKDVDL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  85 VLFMVDARAGLMPADIAIAKHLRSREKPTFLVANKTDGI-DVDQAMA--DFWSLGLG--DIYPIAASHGRGVTSLLEQ-- 157
Cdd:PRK00089  88 VLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVkDKEELLPllEELSELMDfaEIVPISALKGDNVDELLDVia 167

                 ....
gi 490246132 158 ALLP 161
Cdd:PRK00089 168 KYLP 171
mnmE_trmE_thdF TIGR00450
tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF ...
204-338 1.58e-23

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: 102.95  E-value: 1.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  204 PIKLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSIYIPMQRDEREYVLIDTAGVRKRgkiTDVVEKFSVIKTLQA 283
Cdd:TIGR00450 203 GFKLAIVGSPNVGKSSLLNALLKQDRAIVSDIKGTTRDVVEGDFELNGILIKLLDTAGIREH---ADFVERLGIEKSFKA 279
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490246132  284 IEDANVVLLVIDAREGISdQDLSLLGFILNSGRSLVIVVNKWDGLSQEVKEQVKE 338
Cdd:TIGR00450 280 IKQADLVIYVLDASQPLT-KDDFLIIDLNKSKKPFILVLNKIDLKINSLEFFVSS 333
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
6-157 9.89e-23

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: 94.45  E-value: 9.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   6 ALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVE--GREFICIDTGGIDgteEGVETRMAEQSLLAIEEAD 83
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKELDkgKVKLVLVDTPGLD---EFGGLGREELARLLLRGAD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  84 VVLFMVDARAGLMPADIA--IAKHLRSREKPTFLVANKTDGIDVDQ----AMADFWSLGLG-DIYPIAASHGRGVTSLLE 156
Cdd:cd00882   78 LILLVVDSTDRESEEDAKllILRRLRKEGIPIILVGNKIDLLEEREveelLRLEELAKILGvPVFEVSAKTGEGVDELFE 157

                 .
gi 490246132 157 Q 157
Cdd:cd00882  158 K 158
mnmE_trmE_thdF TIGR00450
tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF ...
5-121 1.04e-22

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: 100.25  E-value: 1.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132    5 VALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGREFICIDTGGIDGTEEGVETRMAEQSLLAIEEADV 84
Cdd:TIGR00450 206 LAIVGSPNVGKSSLLNALLKQDRAIVSDIKGTTRDVVEGDFELNGILIKLLDTAGIREHADFVERLGIEKSFKAIKQADL 285
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 490246132   85 VLFMVDARAGLMPADIAIAkHLRSREKPTFLVANKTD 121
Cdd:TIGR00450 286 VIYVLDASQPLTKDDFLII-DLNKSKKPFILVLNKID 321
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
204-371 1.80e-22

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: 93.98  E-value: 1.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  204 PIKLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSIYIPMQRDEREYV--LIDTAGVRKRGKItdvvEKFSVIKTL 281
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEDGKTYKfnLLDTAGQEDYDAI----RRLYYPQVE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  282 QAIEDANVVLLVIDAREGISDQDLSLLGFiLNSGRSLVIVVNKWDGLSQEVKEQVKETLDyRLGFIDFARvhfISALHGS 361
Cdd:TIGR00231  77 RSLRVFDIVILVLDVEEILEKQTKEIIHH-ADSGVPIILVGNKIDLKDADLKTHVASEFA-KLNGEPIIP---LSAETGK 151
                         170
                  ....*....|
gi 490246132  362 GVGNLFESVR 371
Cdd:TIGR00231 152 NIDSAFKIVE 161
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
205-380 2.19e-19

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: 87.83  E-value: 2.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  205 IKLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSIYIPMQRDEREYVLIDTAGV-RKRGKITDVVEKfsviKTLQA 283
Cdd:TIGR00436   1 GFVAILGRPNVGKSTLLNQLHGQKISITSPKAQTTRNRISGIHTTGASQIIFIDTPGFhEKKHSLNRLMMK----EARSA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  284 IEDANVVLLVIDAREGISDQDLsLLGFILNSGRSLVIVVNKWDglsQEVKEQVKETLDYRLGFIDFARVHFISALHGSGV 363
Cdd:TIGR00436  77 IGGVDLILFVVDSDQWNGDGEF-VLTKLQNLKRPVVLTRNKLD---NKFKDKLLPLIDKYAILEDFKDIVPISALTGDNT 152
                         170
                  ....*....|....*..
gi 490246132  364 GNLFESVREAYDSATRR 380
Cdd:TIGR00436 153 SFLAAFIEVHLPEGPFR 169
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
6-159 4.09e-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: 84.04  E-value: 4.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   6 ALVGRPNVGKSTLFNRLTRTRdALVADFPGLTRDRKYGRAEVEGREFICIDTGGI---DGTEEgvETRMAEQSLLAiEEA 82
Cdd:cd01879    1 ALVGNPNVGKTTLFNALTGAR-QKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPGTyslTPYSE--DEKVARDFLLG-EEP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  83 DVVLFMVDARaglmpadiAIAKHLR------SREKPTFLVANKTD-----GIDVD-QAMADfwSLGLGdIYPIAASHGRG 150
Cdd:cd01879   77 DLIVNVVDAT--------NLERNLYltlqllELGLPVVVALNMIDeaekrGIKIDlDKLSE--LLGVP-VVPTSARKGEG 145

                 ....*....
gi 490246132 151 VTSLLEQAL 159
Cdd:cd01879  146 IDELLDAIA 154
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-231 1.55e-18

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 88.64  E-value: 1.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   1 MIPVVALVGRPNVGKSTLFNRLTRTRdALVADFPGLTRDRKYGRAEVEGREFICIDTGGI----DGTEEGVETRmaeqSL 76
Cdd:COG0370    2 KMITIALVGNPNVGKTTLFNALTGSR-QKVGNWPGVTVEKKEGKFKLKGKEIELVDLPGTyslsAYSPDEKVAR----DF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  77 LAIEEADVVLFMVDAraglmpadIAIAKHLR------SREKPTFLVANKTD-----GIDVD-QAMADfwSLGLgDIYPIA 144
Cdd:COG0370   77 LLEEKPDVVVNVVDA--------TNLERNLYltlqllELGIPVVLALNMMDeaekkGIKIDvEKLSK--LLGV-PVVPTS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 145 ASHGRGVTSLLEQAL------------LPWVDEVNP-----QEEVDEDAEYWAKFEA----EQNGEAEEEPEDDFN---- 199
Cdd:COG0370  146 ARKGKGIDELKEAIIeaaegkkprplrIDYPEEIEEaieelEELLEEDGPYPSRWLAikllEGDEEVLELLSELLEllee 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490246132 200 ---------PQDLPIKLA-------------IVGRPNVGKSTLTNRIlgeDRVV 231
Cdd:COG0370  226 ireeleeelGEDLESIIAdaryafierilkeVVTKPGEKKLTLTDKI---DRIL 276
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
4-158 1.67e-18

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: 82.50  E-value: 1.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132    4 VVALVGRPNVGKSTLFNRLTRTRDAlVADFPGLTRDRKYGRAEVEGREFICIDTGGI----DGTEEGVETRmaeqSLLAI 79
Cdd:pfam02421   2 TIALVGNPNVGKTTLFNALTGANQH-VGNWPGVTVEKKEGKFKYKGYEIEIVDLPGIyslsPYSEEERVAR----DYLLN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   80 EEADVVLFMVDARaglmpadiAIAKHL------RSREKPTFLVANKTD-----GIDVD-QAMADfwSLGLgDIYPIAASH 147
Cdd:pfam02421  77 EKPDVIVNVVDAT--------NLERNLyltlqlLELGLPVVLALNMMDeaekkGIKIDiKKLSE--LLGV-PVVPTSARK 145
                         170
                  ....*....|.
gi 490246132  148 GRGVTSLLEQA 158
Cdd:pfam02421 146 GEGIDELLDAI 156
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
205-374 1.68e-17

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 80.03  E-value: 1.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 205 IKLAIVGRPNVGKSTLTNRILGED-RVVVYDMP-GTTRDSIYIPMQRDEREYVLIDTAGvrkrgkiTDVVEKF--SVIKT 280
Cdd:COG1100    4 KKIVVVGTGGVGKTSLVNRLVGDIfSLEKYLSTnGVTIDKKELKLDGLDVDLVIWDTPG-------QDEFRETrqFYARQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 281 LQaieDANVVLLVIDAREGISDQDL-SLLGFILNSGRS--LVIVVNKWDGLSQEVKEQvKETLDYRLGFIDFARVHFISA 357
Cdd:COG1100   77 LT---GASLYLFVVDGTREETLQSLyELLESLRRLGKKspIILVLNKIDLYDEEEIED-EERLKEALSEDNIVEVVATSA 152
                        170
                 ....*....|....*..
gi 490246132 358 LHGSGVGNLFESVREAY 374
Cdd:COG1100  153 KTGEGVEELFAALAEIL 169
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
208-372 2.40e-17

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: 79.48  E-value: 2.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 208 AIVGRPNVGKSTLTNRILGEDRVV-VYDMPGTTR--------DSIYipmqrdereyvLIDT-----AGVRK--RGKITDV 271
Cdd:cd01876    3 AFAGRSNVGKSSLINALTNRKKLArTSKTPGRTQlinffnvgDKFR-----------LVDLpgygyAKVSKevREKWGKL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 272 VEKFsvIKTLQAIedaNVVLLVIDAREGISDQDLSLLGFILNSGRSLVIVVNKWDGLSQ-EVKEQVKETLDYRLGFIDFA 350
Cdd:cd01876   72 IEEY--LENRENL---KGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKsELAKVLKKIKEELNLFNILP 146
                        170       180
                 ....*....|....*....|..
gi 490246132 351 RVHFISALHGSGVGNLFESVRE 372
Cdd:cd01876  147 PVILFSSKKGTGIDELRALIAE 168
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
2-154 1.58e-15

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: 73.95  E-value: 1.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132    2 IPVVALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGR--EFICIDTGGIdgtEEGVETR--MAEQSLL 77
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEDGKtyKFNLLDTAGQ---EDYDAIRrlYYPQVER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   78 AIEEADVVLFMVDARAGLMPaDIAIAKHLRSREKPTFLVANKTD--GIDVDQAMADFWS-LGLGDIYPIAASHGRGVTSL 154
Cdd:TIGR00231  78 SLRVFDIVILVLDVEEILEK-QTKEIIHHADSGVPIILVGNKIDlkDADLKTHVASEFAkLNGEPIIPLSAETGKNIDSA 156
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
208-373 3.74e-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: 3.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 208 AIVGRPNVGKSTLTNRILGEDrVVVYDMPGTTRD----SIYIPmqrDEREYVLIDTAG-VRkrgKI-TDVVEKFSVikTL 281
Cdd:cd01878   45 ALVGYTNAGKSTLFNALTGAD-VLAEDQLFATLDpttrRIKLP---GGREVLLTDTVGfIR---DLpHQLVEAFRS--TL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 282 QAIEDANVVLLVIDA----REGISDQDLSLLGFILNSGRSLVIVVNKWDGLSQEVKEQvketldyRLGFIDFARVhFISA 357
Cdd:cd01878  116 EEVAEADLLLHVVDAsdpdREEQIETVEEVLKELGADDIPIILVLNKIDLLDDEELEE-------RLRAGRPDAV-FISA 187
                        170
                 ....*....|....*.
gi 490246132 358 LHGSGVGNLFESVREA 373
Cdd:cd01878  188 KTGEGLDLLKEAIEEL 203
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
9-192 8.17e-14

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: 73.62  E-value: 8.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132    9 GRPNVGKSTLFNRLTRTrDALVADFPGLTRDRKYGRAEVEGREFICIDTGGI-DGTEEGVETRMAeQSLLAIEEADVVLF 87
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGA-NQTVGNWPGVTVEKKEGKLGFQGEDIEIVDLPGIySLTTFSLEEEVA-RDYLLNEKPDLVVN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   88 MVDARAglMPADIAIAKHLRSREKPTFLVANKTD-----GIDVDqamADFWSLGLG-DIYPIAASHGRGVTSLLeqallp 161
Cdd:TIGR00437  79 VVDASN--LERNLYLTLQLLELGIPMILALNLVDeaekkGIRID---EEKLEERLGvPVVPTSATEGRGIERLK------ 147
                         170       180       190
                  ....*....|....*....|....*....|...
gi 490246132  162 wvDEVNPQEEVDEDAEYWAKF--EAEQNGEAEE 192
Cdd:TIGR00437 148 --DAIRKAIGLKELKKRAIEIvpEAYQVVEVVE 178
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
5-177 1.66e-13

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: 70.50  E-value: 1.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132    5 VALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGREFICIDTGGIDGTEEGVETRMAEQSLLAIEEADV 84
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHGQKISITSPKAQTTRNRISGIHTTGASQIIFIDTPGFHEKKHSLNRLMMKEARSAIGGVDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   85 VLFMVDARAGLMPADIAIAKhLRSREKPTFLVANKTDGIDVDQAMADFWSLG----LGDIYPIAASHGRGVTSLLE--QA 158
Cdd:TIGR00436  83 ILFVVDSDQWNGDGEFVLTK-LQNLKRPVVLTRNKLDNKFKDKLLPLIDKYAiledFKDIVPISALTGDNTSFLAAfiEV 161
                         170
                  ....*....|....*....
gi 490246132  159 LLPWVDEVNPQEEVDEDAE 177
Cdd:TIGR00436 162 HLPEGPFRYPEDYVTDQPD 180
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
6-158 3.98e-13

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: 67.42  E-value: 3.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   6 ALVGRPNVGKSTLFNRLTRTrDALVADFPGLTRDRKYGRAE-VEGREFICIDTGG-IDGTEEGVETrmAEQSLLAIEEAD 83
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSA-KVEIASYPFTTLEPNVGVFEfGDGVDIQIIDLPGlLDGASEGRGL--GEQILAHLYRSD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  84 VVLFMVDA--RAGLMPAD--------IAIAKHLRSrEKPTFLVANKTDGIDVDQAMADFWSLGLGDIY--PIAASHGRGV 151
Cdd:cd01881   78 LILHVIDAseDCVGDPLEdqktlneeVSGSFLFLK-NKPEMIVANKIDMASENNLKRLKLDKLKRGIPvvPTSALTRLGL 156

                 ....*..
gi 490246132 152 TSLLEQA 158
Cdd:cd01881  157 DRVIRTI 163
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
71-262 1.17e-12

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: 66.01  E-value: 1.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  71 MAEqSLLAIEE----ADVVLFMVDARAGLMPADIAIAKHLRSreKPTFLVANKTDgiDVDQAMADFW--SLGLGDIYPIA 144
Cdd:cd01856    6 MAK-ALRQIKEklklVDVVIEVRDARIPLSSRNPDLDKILGN--KPRLIVLNKAD--LADPAKTKKWlkYFKSQGEPVLF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 145 --ASHGRGVTSLLEQALlpwvdevnpqeevdedaeywakfeaEQNGEAEEEPEDDFNPqdLPIKLAIVGRPNVGKSTLTN 222
Cdd:cd01856   81 vnAKNGKGVKKLLKKAK-------------------------KLLKENEKLKAKGLLP--RPLRAMVVGIPNVGKSTLIN 133
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 490246132 223 RILGEDRVVVYDMPGTTRDS--IYIPMqrderEYVLIDTAGV 262
Cdd:cd01856  134 RLRGKKVAKVGNKPGVTRGQqwIRIGP-----NIELLDTPGI 170
obgE PRK12298
GTPase CgtA; Reviewed
5-199 2.57e-12

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 68.36  E-value: 2.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   5 VALVGRPNVGKSTLFNRLTRTRDAlVADFPGLTRDRKYGRAEV-EGREFICIDTGG-IDGTEEGVEtrMAEQSLLAIEEA 82
Cdd:PRK12298 162 VGLLGLPNAGKSTFIRAVSAAKPK-VADYPFTTLVPNLGVVRVdDERSFVVADIPGlIEGASEGAG--LGIRFLKHLERC 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  83 DVVLFMVDaragLMPAD--------IAIAKHLRS-----REKPTFLVANKTDGIDVDQAMADF--------WSlglGDIY 141
Cdd:PRK12298 239 RVLLHLID----IAPIDgsdpvenaRIIINELEKyspklAEKPRWLVFNKIDLLDEEEAEERAkaivealgWE---GPVY 311
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490246132 142 PIAASHGRGVTSLLeQALLPWVDEVNPQEEVDEDAE-----YWAKFEAEQNGEAEEEPEDDFN 199
Cdd:PRK12298 312 LISAASGLGVKELC-WDLMTFIEENPREEAEEAEAPekvefMWDDYHREQLEEVEEEDDDDWD 373
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
207-370 7.93e-12

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: 64.08  E-value: 7.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  207 LAIVGRPNVGKSTLTNRIL------GEDRVVVYD-------MP-----GTTRDSIYIPMQRDEREYVLIDTAGVrkrgki 268
Cdd:pfam00009   6 IGIIGHVDHGKTTLTDRLLyytgaiSKRGEVKGEgeagldnLPeererGITIKSAAVSFETKDYLINLIDTPGH------ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  269 tdvvEKFS--VIKTLQAiedANVVLLVIDAREGISDQDLSLLGFILNSGRSLVIVVNKWDGLSQ----EVKEQVKETLDY 342
Cdd:pfam00009  80 ----VDFVkeVIRGLAQ---ADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDGaeleEVVEEVSRELLE 152
                         170       180
                  ....*....|....*....|....*....
gi 490246132  343 RLGF-IDFARVHFISALHGSGVGNLFESV 370
Cdd:pfam00009 153 KYGEdGEFVPVVPGSALKGEGVQTLLDAL 181
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
206-357 9.92e-12

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: 63.72  E-value: 9.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 206 KLAIVGRPNVGKSTLTNRILGED----RVVvydmPGTTRDS-IYIPMQRDereYVLIDTAGvrkrgkiTDVVEKFSVIKT 280
Cdd:cd09912    2 LLAVVGEFSAGKSTLLNALLGEEvlptGVT----PTTAVITvLRYGLLKG---VVLVDTPG-------LNSTIEHHTEIT 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 281 LQAIEDANVVLLVIDAREGISDQDLSLLGFIL-NSGRSLVIVVNKWDGLSQE-----VKEQVKETLDYRLGfIDFARVHF 354
Cdd:cd09912   68 ESFLPRADAVIFVLSADQPLTESEREFLKEILkWSGKKIFFVLNKIDLLSEEeleevLEYSREELGVLELG-GGEPRIFP 146

                 ...
gi 490246132 355 ISA 357
Cdd:cd09912  147 VSA 149
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
83-262 1.56e-11

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: 62.02  E-value: 1.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  83 DVVLFMVDARAGLMPADIAIAKHLRSREKPTFLVANKTDGID---VDQAMADFWSLGLGDIYPIAASHGRGVTSLLEqal 159
Cdd:cd01849    1 DVVVEVVDARDPLSSRNPDIEVLINEKNKKLIMVLNKADLVPkevLRKWVAELSELYGTKTFFISATNGQGILKLKA--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 160 lpwvdEVNPQEEVDEDAEywakfeaeqngeaeeepeddfnpqdlPIKLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTT 239
Cdd:cd01849   78 -----EITKQKLKLKYKK--------------------------GIRVGVVGLPNVGKSSFINALLNKFKLKVGSIPGTT 126
                        170       180
                 ....*....|....*....|...
gi 490246132 240 RDSIYIPmqrDEREYVLIDTAGV 262
Cdd:cd01849  127 KLQQDVK---LDKEIYLYDTPGI 146
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
208-373 1.69e-11

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 65.88  E-value: 1.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 208 AIVGRPNVGKSTLTNRILGEDrVVVYDM------PgTTRdSIYIPmqrDEREYVLIDTAG-VRKrgkiTDVVEKF-Svik 279
Cdd:COG2262  203 ALVGYTNAGKSTLFNRLTGAD-VLAEDKlfatldP-TTR-RLELP---DGRPVLLTDTVGfIRKl--pHQLVEAFrS--- 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 280 TLQAIEDANVVLLVIDAregiSDQD--------LSLLGFILNSGRSLVIVVNKWDGLSQEVKEQVKETLDYRLgfidfar 351
Cdd:COG2262  272 TLEEVREADLLLHVVDA----SDPDfeeqietvNEVLEELGADDKPIILVFNKIDLLDDEELERLRAGYPDAV------- 340
                        170       180
                 ....*....|....*....|..
gi 490246132 352 vhFISALHGSGVGNLFESVREA 373
Cdd:COG2262  341 --FISAKTGEGIDELLEAIEER 360
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
2-156 2.92e-11

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 65.11  E-value: 2.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   2 IPVVALVGRPNVGKSTLFNRLTRTrDALVAD--FPGL---TRdrkygRAEVE-GREFICIDT-GGID-----------GT 63
Cdd:COG2262  199 IPTVALVGYTNAGKSTLFNRLTGA-DVLAEDklFATLdptTR-----RLELPdGRPVLLTDTvGFIRklphqlveafrST 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  64 -EEgvetrmaeqsllaIEEADVVLFMVDAraglmpADIAIAKHLRS----------REKPTFLVANKTDGIDVDQamADF 132
Cdd:COG2262  273 lEE-------------VREADLLLHVVDA------SDPDFEEQIETvnevleelgaDDKPIILVFNKIDLLDDEE--LER 331
                        170       180
                 ....*....|....*....|....
gi 490246132 133 WSLGLGDIYPIAASHGRGVTSLLE 156
Cdd:COG2262  332 LRAGYPDAVFISAKTGEGIDELLE 355
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
83-262 3.16e-11

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 63.97  E-value: 3.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  83 DVVLFMVDARAglmPA-----DIA-IAKHlrsreKPTFLVANKTDgidvdqaMAD----------FWSLGLgDIYPIAAS 146
Cdd:COG1161   25 DLVIEVVDARI---PLssrnpMLDeLVGN-----KPRLLVLNKAD-------LADpsvtkqwlkyFEKQGV-DALAISAK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 147 HGRGVtslleQALLPWVDEVNPqeevdedaeywakfeaeqngeaeeepedDFNPQDLPIKLAIVGRPNVGKSTLTNRILG 226
Cdd:COG1161   89 KGKGI-----KELIEAIRELAP----------------------------EKGIKRRPIRVMIVGIPNVGKSTLINRLAG 135
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 490246132 227 EDRVVVYDMPGTTRDSIYIPMQrDEREyvLIDTAGV 262
Cdd:COG1161  136 KKVAKTGNKPGVTKGQQWIKLD-DGLE--LLDTPGI 168
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
237-363 3.77e-11

CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.


Pssm-ID: 206729 [Multi-domain]  Cd Length: 209  Bit Score: 62.59  E-value: 3.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 237 GTTRDSIYIPMQRDEREYVLIDTAGVRK--RGKITdvvekfsviktlqAIEDANVVLLVIDAREGISDQD------LSLL 308
Cdd:cd04166   63 GITIDVAYRYFSTPKRKFIIADTPGHEQytRNMVT-------------GASTADLAILLVDARKGVLEQTrrhsyiASLL 129
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490246132 309 GFilnsgRSLVIVVNKWD--GLSQEVKEQVKEtlDYR--LGFIDFARVHFI--SALHGSGV 363
Cdd:cd04166  130 GI-----RHVVVAVNKMDlvDYDEEVFEEIKA--DYLafAASLGIEDITFIpiSALEGDNV 183
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
5-121 1.34e-10

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: 59.83  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   5 VALVGRPNVGKSTLFNRLT-RTRDALVADFPGLTR-------DRK--------YGRAEV--EGREFIcidtggIDGTEEG 66
Cdd:cd01876    2 VAFAGRSNVGKSSLINALTnRKKLARTSKTPGRTQlinffnvGDKfrlvdlpgYGYAKVskEVREKW------GKLIEEY 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490246132  67 VETRmaeQSLLAieeadvVLFMVDARAGLMPADIAIAKHLRSREKPTFLVANKTD 121
Cdd:cd01876   76 LENR---ENLKG------VVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKAD 121
obgE PRK12299
GTPase CgtA; Reviewed
5-171 1.45e-10

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 62.40  E-value: 1.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   5 VALVGRPNVGKSTLFNRLTRTRdALVADFPGLTRDRKYGRAEV-EGREFICIDTGG-IDGTEEGVETRMaeQSLLAIEEA 82
Cdd:PRK12299 161 VGLVGLPNAGKSTLISAVSAAK-PKIADYPFTTLHPNLGVVRVdDYKSFVIADIPGlIEGASEGAGLGH--RFLKHIERT 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  83 DVVLFMVDArAGLMPAD--IAIAKHLRS-----REKPTFLVANKTDGIDVD----QAMADFWSLGLGDIYPIAASHGRGV 151
Cdd:PRK12299 238 RLLLHLVDI-EAVDPVEdyKTIRNELEKyspelADKPRILVLNKIDLLDEEeereKRAALELAALGGPVFLISAVTGEGL 316
                        170       180
                 ....*....|....*....|
gi 490246132 152 TSLLeQALLPWVDEVNPQEE 171
Cdd:PRK12299 317 DELL-RALWELLEEARREEE 335
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
5-157 1.51e-10

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 59.99  E-value: 1.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   5 VALVGRPNVGKSTLFNRLTR----TRDALVADfpGLTRDRKYGRAEVEGREFICIDTGGIDgteegvETRMAEQSLL-AI 79
Cdd:COG1100    6 IVVVGTGGVGKTSLVNRLVGdifsLEKYLSTN--GVTIDKKELKLDGLDVDLVIWDTPGQD------EFRETRQFYArQL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  80 EEADVVLFMVDARagLMPADIAIAKHLRS-----REKPTFLVANKTDGIDVDQ------AMADFWSLGLGDIYPIAASHG 148
Cdd:COG1100   78 TGASLYLFVVDGT--REETLQSLYELLESlrrlgKKSPIILVLNKIDLYDEEEiedeerLKEALSEDNIVEVVATSAKTG 155

                 ....*....
gi 490246132 149 RGVTSLLEQ 157
Cdd:COG1100  156 EGVEELFAA 164
YeeP COG3596
Predicted GTPase [General function prediction only];
204-397 2.94e-10

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 61.32  E-value: 2.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 204 PIKLAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSIYIPMQRDEREY-VLIDTAGVrkrgkiTDVVEKF-SVIKTL 281
Cdd:COG3596   39 PPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLESDGLPGlVLLDTPGL------GEVNERDrEYRELR 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 282 QAIEDANVVLLVIDAREGISDQDLSLLGFIL--NSGRSLVIVVNKWDGL-------------SQEVKEQVKETLDYRLGF 346
Cdd:COG3596  113 ELLPEADLILWVVKADDRALATDEEFLQALRaqYPDPPVLVVLTQVDRLeperewdppynwpSPPKEQNIRRALEAIAEQ 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490246132 347 IDFA--RVHFISAL---HGSGVGNLFESVREAYDSATRrvstAMLTRIMNMAAEDH 397
Cdd:COG3596  193 LGVPidRVIPVSAAedrTGYGLEELVDALAEALPEAKR----SRLARLLRAKAIDR 244
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
6-159 5.85e-10

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: 57.35  E-value: 5.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   6 ALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVEGREFICIDTGGIDGTEEgVETRMAEQSLLAIEEADVV 85
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPGVGERGR-RDREYEELYRRLLPEADLV 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490246132  86 LFMVDARAGLMPADIA-IAKHLRSREKPTFLVANKtdgidVDQamadfwslglgdIYPIAASHGRGVTSLLEQAL 159
Cdd:cd11383   80 LWLLDADDRALAADHDfYLLPLAGHDAPLLFVLNQ-----VDP------------VLAVSARTGWGLDELAEALI 137
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
208-363 6.00e-10

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: 58.46  E-value: 6.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 208 AIVGRPNVGKSTLTNRILGED-------RVVVYDMP--------GTTRDSIYIPMQRDEREYVLIDTAGVrkrgkitdvv 272
Cdd:cd00881    3 GVIGHVDHGKTTLTGSLLYQTgaidrrgTRKETFLDtlkeererGITIKTGVVEFEWPKRRINFIDTPGH---------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 273 EKFSvIKTLQAIEDANVVLLVIDAREGISDQDLSLLGFILNSGRSLVIVVNKWDGLSQEVKEQVKETLDYRLGFIDF--- 349
Cdd:cd00881   73 EDFS-KETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGEEDFDEVLREIKELLKLIGFtfl 151
                        170
                 ....*....|....*...
gi 490246132 350 ----ARVHFISALHGSGV 363
Cdd:cd00881  152 kgkdVPIIPISALTGEGI 169
obgE PRK12297
GTPase CgtA; Reviewed
5-198 1.22e-09

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 60.11  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   5 VALVGRPNVGKSTLFNRLTRTRDAlVADFPGLTRDRKYGRAEV-EGREFICIDTGG-IDGTEEGVEtrMAEQSLLAIEEA 82
Cdd:PRK12297 161 VGLVGFPNVGKSTLLSVVSNAKPK-IANYHFTTLVPNLGVVETdDGRSFVMADIPGlIEGASEGVG--LGHQFLRHIERT 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  83 DVVLFMVDArAGLMPAD-----IAIAKHLRS-----REKPTFLVANKTDGIDVDQAMADFWS-LGLgDIYPIAASHGRGV 151
Cdd:PRK12297 238 RVIVHVIDM-SGSEGRDpiedyEKINKELKLynprlLERPQIVVANKMDLPEAEENLEEFKEkLGP-KVFPISALTGQGL 315
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 490246132 152 TSLLEQA--LLPWVDEVNPQEEVDEDAEYWaKFEAEQNGEAEEEPEDDF 198
Cdd:PRK12297 316 DELLYAVaeLLEETPEFPLEEEEVEEEVYY-KFEEEEKDFTITRDEDGV 363
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
3-159 2.20e-09

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: 56.41  E-value: 2.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   3 PVVALVGRPNVGKSTLFNRLTRTrDALVADFPGLTR-------DRKYGRAEVegreficIDTGGI-D-GTEEGVETRMae 73
Cdd:cd01897    1 RTLVIAGYPNVGKSSLVNKLTRA-KPEVAPYPFTTKslfvghfDYKYLRWQV-------IDTPGIlDrPLEERNTIEM-- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  74 QSLLAIEE-ADVVLFMVDA--RAGLMPAD-IAIAKHLRSR-EKPTFLVANKTDGIDVDQAMA--DFWSLGLGDIYPIAAS 146
Cdd:cd01897   71 QAITALAHlRAAVLFFIDPseTCGYSIEEqLSLFKEIKPLfNKPVIVVLNKIDLLTEEDLSEieKELEKEGEEVIKISTL 150
                        170
                 ....*....|...
gi 490246132 147 HGRGVTSLLEQAL 159
Cdd:cd01897  151 TEEGVDELKNKAC 163
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
79-262 2.56e-09

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: 58.29  E-value: 2.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   79 IEE----ADVVLFMVDARAGLMPADIAIAKHLRSreKPTFLVANKTDGIDVDQAMAdfW--SLGLGDIYPIA--ASHGRG 150
Cdd:TIGR03596  15 IKEnlklVDVVIEVLDARIPLSSRNPMIDEIRGN--KPRLIVLNKADLADPAVTKQ--WlkYFEEKGIKALAvnAKKGAG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  151 VTSLLE--QALLPwvdevnpqeevdedaeywAKFEAEQNGEAEeepeddfNPqdlPIKLAIVGRPNVGKSTLTNRILGED 228
Cdd:TIGR03596  91 VKKIIKaaKKLLK------------------EKNEKLKAKGLK-------NR---PIRAMIVGIPNVGKSTLINRLAGKK 142
                         170       180       190
                  ....*....|....*....|....*....|....
gi 490246132  229 RVVVYDMPGTTRDSIYIpmqRDEREYVLIDTAGV 262
Cdd:TIGR03596 143 VAKVGNRPGVTKGQQWI---KLSDNLELLDTPGI 173
PRK04213 PRK04213
GTP-binding protein EngB;
3-148 5.02e-09

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 56.08  E-value: 5.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   3 PVVALVGRPNVGKSTLFNRLTrTRDALVADFPGLTRDrkygRAEVEGREFICIDTGG---IDGTEEGVETRMAEQSLLAI 79
Cdd:PRK04213  10 PEIVFVGRSNVGKSTLVRELT-GKKVRVGKRPGVTRK----PNHYDWGDFILTDLPGfgfMSGVPKEVQEKIKDEIVRYI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  80 EE-ADVVLF---MVDARA-----------GLMPADIAIAKHLRSREKPTFLVANKTDGIDVDQAMADF----------WS 134
Cdd:PRK04213  85 EDnADRILAavlVVDGKSfieiierwegrGEIPIDVEMFDFLRELGIPPIVAVNKMDKIKNRDEVLDEiaerlglyppWR 164
                        170
                 ....*....|....
gi 490246132 135 LGLGDIYPIAASHG 148
Cdd:PRK04213 165 QWQDIIAPISAKKG 178
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
2-157 7.16e-09

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: 55.54  E-value: 7.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   2 IPVVALVGRPNVGKSTLFNRLTRtRDALVAD--FPGL---TRdrkygRAEV-EGREFICIDT-GGIDG--TEEgVEtrmA 72
Cdd:cd01878   41 VPTVALVGYTNAGKSTLFNALTG-ADVLAEDqlFATLdptTR-----RIKLpGGREVLLTDTvGFIRDlpHQL-VE---A 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  73 EQSLLA-IEEADVVLFMVDA----RAGLMPADIAIAKHLRSREKPTFLVANKTDGIDvDQAMADFWSLGLGDIYPIAASH 147
Cdd:cd01878  111 FRSTLEeVAEADLLLHVVDAsdpdREEQIETVEEVLKELGADDIPIILVLNKIDLLD-DEELEERLRAGRPDAVFISAKT 189
                        170
                 ....*....|
gi 490246132 148 GRGVTSLLEQ 157
Cdd:cd01878  190 GEGLDLLKEA 199
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
209-262 8.49e-09

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: 55.35  E-value: 8.49e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490246132 209 IVGRPNVGKSTLTNRILGED-----------RVVVYDMPGTTRDSIYIPMQRDEreyVLIDTAGV 262
Cdd:cd01855  130 VVGATNVGKSTLINALLKSNggkvqaqalvqRLTVSPIPGTTLGLIKIPLGEGK---KLYDTPGI 191
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
5-157 1.22e-08

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


Pssm-ID: 206685 [Multi-domain]  Cd Length: 170  Bit Score: 54.35  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   5 VALVGRPNVGKSTLFNRLTRTRDAlVADFP--------GLTRDRkygraevEGREFICIDTGG-IDGTEEGVEtrMAEQS 75
Cdd:cd01898    3 VGLVGLPNAGKSTLLSAISNAKPK-IADYPfttlvpnlGVVRVD-------DGRSFVIADIPGlIEGASEGKG--LGHRF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  76 LLAIEEADVVLFMVDARAGLMPAD--IAIAKHLRS-----REKPTFLVANKTDGIDVDQAMADFWSL----GLGDIYPIA 144
Cdd:cd01898   73 LRHIERTRVLLHVIDLSGEDDPVEdyETIRNELEAynpglAEKPRIVVLNKIDLLDAEERFEKLKELlkelKGKKVFPIS 152
                        170
                 ....*....|...
gi 490246132 145 ASHGRGVTSLLEQ 157
Cdd:cd01898  153 ALTGEGLDELLKK 165
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
284-402 2.52e-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: 53.09  E-value: 2.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 284 IEDANVVLLVIDAREGISDQDLSLLGFILNSGRSLVIVVNKWDGLSQEVKEQVKETLDyrlgfidfarvhfisalhgsgv 363
Cdd:cd01859    9 IKEADVVLEVVDARDPELTRSRKLERMALELGKKLIIVLNKADLVPREVLEKWKEVFE---------------------- 66
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490246132 364 GNLFESVreaYDSATRRVSTAMLTRIMNMAAEDHQPPLV 402
Cdd:cd01859   67 SEGLPVV---YVSARERLGTRILRRTIKELAIDGKPVIV 102
YeeP COG3596
Predicted GTPase [General function prediction only];
3-121 2.81e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 55.54  E-value: 2.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   3 PVVALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRD-RKYGRAEVEGREFICIDTGGIDGTEEG-VETRMAEQsllAIE 80
Cdd:COG3596   40 PVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREiQRYRLESDGLPGLVLLDTPGLGEVNERdREYRELRE---LLP 116
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 490246132  81 EADVVLFMVDARAGLMPADIAIAKHLRSR--EKPTFLVANKTD 121
Cdd:COG3596  117 EADLILWVVKADDRALATDEEFLQALRAQypDPPVLVVLTQVD 159
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
2-159 3.09e-08

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 55.22  E-value: 3.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   2 IPVVALVGRPNVGKSTLFNRLTRTRDAlVADFPGLTRDRKYGRAEVEGREFICIDTGGIdgteegVETRMAE------QS 75
Cdd:COG1084  160 LPTIVVAGYPNVGKSSLVSKVTSAKPE-IASYPFTTKGIIVGHFERGHGRYQVIDTPGL------LDRPLSErneierQA 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  76 LLAIEE-ADVVLFMVDAR--AGLmpaDIAIAKHLRSR-----EKPTFLVANKTDGIDVDqamaDFWSLGLGDIYPIAASH 147
Cdd:COG1084  233 ILALKHlADVILFLFDPSetCGY---SLEEQLNLLEEirslfDVPVIVVINKIDLSDEE----ELKEAEEEADIKISALT 305
                        170
                 ....*....|..
gi 490246132 148 GRGVTSLLEQAL 159
Cdd:COG1084  306 GEGVDELLDELI 317
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
3-121 4.91e-08

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: 53.15  E-value: 4.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   3 PVVALVGRPNVGKSTLFNRLT-------------RTR---------DALVADFPGltrdrkYGRAEVEG------REFIc 54
Cdd:COG0218   24 PEIAFAGRSNVGKSSLINALTnrkklartsktpgKTQlinfflindKFYLVDLPG------YGYAKVSKaekekwQKLI- 96
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490246132  55 idtggidgtEEGVETRmaeQSLLAIeeadVVLfmVDARAGLMPADIAIAKHLRSREKPTFLVANKTD 121
Cdd:COG0218   97 ---------EDYLEGR---ENLKGV----VLL--IDIRHPPKELDLEMLEWLDEAGIPFLIVLTKAD 145
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
208-372 5.29e-08

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: 52.40  E-value: 5.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 208 AIVGRPNVGKSTLTNrILGEDRVVVYDMPGTTRDSI--YIPMQrDEREYVLIDTAGVRKrGKITDVVEKFSViktLQAIE 285
Cdd:cd01881    1 GLVGLPNVGKSTLLS-ALTSAKVEIASYPFTTLEPNvgVFEFG-DGVDIQIIDLPGLLD-GASEGRGLGEQI---LAHLY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 286 DANVVLLVIDAREG-----ISDQDL---SLLGFILN-SGRSLVIVVNKWDGLSQE-VKEQVKETLDYRLGFIDfarvhfI 355
Cdd:cd01881   75 RSDLILHVIDASEDcvgdpLEDQKTlneEVSGSFLFlKNKPEMIVANKIDMASENnLKRLKLDKLKRGIPVVP------T 148
                        170
                 ....*....|....*..
gi 490246132 356 SALHGSGVGNLFESVRE 372
Cdd:cd01881  149 SALTRLGLDRVIRTIRK 165
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
5-156 5.56e-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: 52.68  E-value: 5.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   5 VALVGRPNVGKSTLFNRLTR---------TRDALVADFPGLTRDR----KYGRAEVE--GREFICIDT-GGIDGTEEGVe 68
Cdd:cd00881    2 VGVIGHVDHGKTTLTGSLLYqtgaidrrgTRKETFLDTLKEERERgitiKTGVVEFEwpKRRINFIDTpGHEDFSKETV- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  69 trmaeqslLAIEEADVVLFMVDARAGLMPADIAIAKHLRSREKPTFLVANKTDGIDVDQAM--------------ADFWS 134
Cdd:cd00881   81 --------RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGEEDFDevlreikellkligFTFLK 152
                        170       180
                 ....*....|....*....|..
gi 490246132 135 LGLGDIYPIAASHGRGVTSLLE 156
Cdd:cd00881  153 GKDVPIIPISALTGEGIEELLD 174
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
5-156 1.02e-07

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


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 52.14  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132    5 VALVGRPNVGKSTLFNRLT-----RTRDALVADFPGLTRDR-------------KYGRAEVEGREFICIDT-GGIDGTEE 65
Cdd:pfam00009   6 IGIIGHVDHGKTTLTDRLLyytgaISKRGEVKGEGEAGLDNlpeerergitiksAAVSFETKDYLINLIDTpGHVDFVKE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   66 gVETRMAEqsllaieeADVVLFMVDARAGLMPADIAIAKHLRSREKPTFLVANKTDGID-------VDQAMADFWSLGLG 138
Cdd:pfam00009  86 -VIRGLAQ--------ADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDgaeleevVEEVSRELLEKYGE 156
                         170       180
                  ....*....|....*....|...
gi 490246132  139 D-----IYPIAASHGRGVTSLLE 156
Cdd:pfam00009 157 DgefvpVVPGSALKGEGVQTLLD 179
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
205-370 2.62e-07

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


Pssm-ID: 460552 [Multi-domain]  Cd Length: 156  Bit Score: 50.14  E-value: 2.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  205 IKLAIVGRPNVGKSTLTNRILGEdRVVVYDMPGTTRDSIYIPMQRDEREYVLIDTAGVRKRGKITD---VVEKFsVIKtl 281
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTGA-NQHVGNWPGVTVEKKEGKFKYKGYEIEIVDLPGIYSLSPYSEeerVARDY-LLN-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  282 qaiEDANVVLLVIDAR--EgisdQDLSLLGFILNSGRSLVIVVNKWDglsqEVKEQ-----VKEtLDYRLGFidfaRVHF 354
Cdd:pfam02421  77 ---EKPDVIVNVVDATnlE----RNLYLTLQLLELGLPVVLALNMMD----EAEKKgikidIKK-LSELLGV----PVVP 140
                         170
                  ....*....|....*.
gi 490246132  355 ISALHGSGVGNLFESV 370
Cdd:pfam02421 141 TSARKGEGIDELLDAI 156
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
208-376 2.80e-07

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


Pssm-ID: 206667 [Multi-domain]  Cd Length: 159  Bit Score: 50.15  E-value: 2.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 208 AIVGRPNVGKSTLTNRILGeDRVVVYDMPGTTRDSIYIPMQRDEREYVLIDTAGVRKRGKITD---VVEKFsVIKtlqai 284
Cdd:cd01879    1 ALVGNPNVGKTTLFNALTG-ARQKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPGTYSLTPYSEdekVARDF-LLG----- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 285 EDANVVLLVIDAregiS--DQDLSLLGFILNSGRSLVIVVNKWDglsqEVKEQ-VK---ETLDYRLGfidfARVHFISAL 358
Cdd:cd01879   74 EEPDLIVNVVDA----TnlERNLYLTLQLLELGLPVVVALNMID----EAEKRgIKidlDKLSELLG----VPVVPTSAR 141
                        170
                 ....*....|....*...
gi 490246132 359 HGSGVGNLFESVREAYDS 376
Cdd:cd01879  142 KGEGIDELLDAIAKLAES 159
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
5-38 3.99e-07

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: 49.83  E-value: 3.99e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 490246132   5 VALVGRPNVGKSTLFNRLTRTRDALVADFPGLTR 38
Cdd:cd01856  118 AMVVGIPNVGKSTLINRLRGKKVAKVGNKPGVTR 151
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
216-370 9.09e-07

LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.


Pssm-ID: 206677 [Multi-domain]  Cd Length: 179  Bit Score: 49.07  E-value: 9.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 216 GKSTLTNRILGEDRVVV-YDMPGTTRDS--------IYIPMQ--------RDEREYV--LIDTAG-VrkrgkitdvveKF 275
Cdd:cd01890   12 GKSTLADRLLELTGTVSeREMKEQVLDSmdlerergITIKAQavrlfykaKDGEEYLlnLIDTPGhV-----------DF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 276 S--VIKTLQAIEDAnvvLLVIDAREGISDQDLSLLGFILNSGRSLVIVVNKWDGLS---QEVKEQVKETLDyrlgfIDFA 350
Cdd:cd01890   81 SyeVSRSLAACEGA---LLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAadpDRVKQEIEDVLG-----LDAS 152
                        170       180
                 ....*....|....*....|
gi 490246132 351 RVHFISALHGSGVGNLFESV 370
Cdd:cd01890  153 EAILVSAKTGLGVEDLLEAI 172
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
5-91 1.96e-06

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 49.80  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   5 VALVGRPNVGKSTLFNRLTRTrDALVADFPGLTRDRKYGRAEVEGREFICIDTGG-IDGTEEGveTRMAEQSLLAIEEAD 83
Cdd:COG1163   66 VVLVGFPSVGKSTLLNKLTNA-KSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGlIEGAASG--KGRGKEVLSVVRNAD 142

                 ....*...
gi 490246132  84 VVLFMVDA 91
Cdd:COG1163  143 LILIVLDV 150
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
208-326 2.27e-06

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: 46.95  E-value: 2.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 208 AIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSIYIPMQRDEREYVLIDTAGVRKRGkITDVVEKFSViktLQAIEDA 287
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPGVGERG-RRDREYEELY---RRLLPEA 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 490246132 288 NVVLLVIDA--REGISDQDLSLLgfILNSGRS-LVIVVNKWD 326
Cdd:cd11383   77 DLVLWLLDAddRALAADHDFYLL--PLAGHDApLLFVLNQVD 116
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
207-366 3.25e-06

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


Pssm-ID: 206684 [Multi-domain]  Cd Length: 167  Bit Score: 47.17  E-value: 3.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 207 LAIVGRPNVGKSTLTNRILGEDrVVVYDMPGTTRdSIYIP-MQRDEREYVLIDTAGVRKRGkitdvVEKFSVIKtLQAIE 285
Cdd:cd01897    3 LVIAGYPNVGKSSLVNKLTRAK-PEVAPYPFTTK-SLFVGhFDYKYLRWQVIDTPGILDRP-----LEERNTIE-MQAIT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 286 D----ANVVLLVIDARE----GISDQdLSLLGFI-LNSGRSLVIVVNKWDgLSQEvkEQVKETLDYrlGFIDFARVHFIS 356
Cdd:cd01897   75 AlahlRAAVLFFIDPSEtcgySIEEQ-LSLFKEIkPLFNKPVIVVLNKID-LLTE--EDLSEIEKE--LEKEGEEVIKIS 148
                        170
                 ....*....|
gi 490246132 357 ALHGSGVGNL 366
Cdd:cd01897  149 TLTEEGVDEL 158
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
8-39 5.79e-06

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 47.80  E-value: 5.79e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 490246132   8 VGRPNVGKSTLFNRLTRTRDALVADFPGLTRD 39
Cdd:COG1161  119 VGIPNVGKSTLINRLAGKKVAKTGNKPGVTKG 150
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
5-91 5.93e-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: 47.54  E-value: 5.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   5 VALVGRPNVGKSTLFNRLTRTrDALVADFPGLTRDRKYGRAEVEGREFICIDTGGI-DGTEEGveTRMAEQSLLAIEEAD 83
Cdd:cd01896    3 VALVGFPSVGKSTLLSKLTNT-KSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIiEGASDG--KGRGRQVIAVARTAD 79

                 ....*...
gi 490246132  84 VVLFMVDA 91
Cdd:cd01896   80 LILIVLDA 87
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
202-379 6.52e-06

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 47.91  E-value: 6.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 202 DLPiklAIV--GRPNVGKSTLTNRILG-EDRVVVYdmPGTTRDSIYIPMQRDEREYVLIDTAGV--R---KRGKItdvvE 273
Cdd:COG1084  159 DLP---TIVvaGYPNVGKSSLVSKVTSaKPEIASY--PFTTKGIIVGHFERGHGRYQVIDTPGLldRplsERNEI----E 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 274 K--FSVIKTLqaiedANVVLLVIDARE----GISDQdLSLLGFILNS-GRSLVIVVNKWDgLSQEVKEQVKETLDYrlgf 346
Cdd:COG1084  230 RqaILALKHL-----ADVILFLFDPSEtcgySLEEQ-LNLLEEIRSLfDVPVIVVINKID-LSDEEELKEAEEEAD---- 298
                        170       180       190
                 ....*....|....*....|....*....|...
gi 490246132 347 idfarvHFISALHGSGVGNLFESVREAYDSATR 379
Cdd:COG1084  299 ------IKISALTGEGVDELLDELIEALEEEPE 325
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
7-60 9.55e-06

Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 46.10  E-value: 9.55e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490246132   7 LVGRPNVGKSTLFNRLTRT-----------RDALVADFPGLTRD-RKYGRaeveGREFICIDTGGI 60
Cdd:cd01855  130 VVGATNVGKSTLINALLKSnggkvqaqalvQRLTVSPIPGTTLGlIKIPL----GEGKKLYDTPGI 191
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
7-37 2.22e-05

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


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 46.55  E-value: 2.22e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 490246132   7 LVGRPNVGKSTLFNRLTRTrDALVADFPGLT 37
Cdd:COG0012    5 IVGLPNVGKSTLFNALTKA-GAEAANYPFCT 34
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
8-34 3.17e-05

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: 45.53  E-value: 3.17e-05
                         10        20
                 ....*....|....*....|....*..
gi 490246132   8 VGRPNVGKSTLFNRLTRTrDALVADFP 34
Cdd:cd01900    4 VGLPNVGKSTLFNALTKS-NAEAANYP 29
PRK04213 PRK04213
GTP-binding protein EngB;
205-346 3.51e-05

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 44.91  E-value: 3.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 205 IKLAIVGRPNVGKSTLTNRILGEDrVVVYDMPGTTRDsiyiPMQRDEREYVLID------TAGV--RKRGKITDvvekfs 276
Cdd:PRK04213  10 PEIVFVGRSNVGKSTLVRELTGKK-VRVGKRPGVTRK----PNHYDWGDFILTDlpgfgfMSGVpkEVQEKIKD------ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 277 viKTLQAIED----ANVVLLVIDARE--GISDQ---------DLSLLGFILNSGRSLVIVVNKWDglsqEVKEqVKETLD 341
Cdd:PRK04213  79 --EIVRYIEDnadrILAAVLVVDGKSfiEIIERwegrgeipiDVEMFDFLRELGIPPIVAVNKMD----KIKN-RDEVLD 151

                 ....*...
gi 490246132 342 Y---RLGF 346
Cdd:PRK04213 152 EiaeRLGL 159
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
5-38 4.67e-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: 45.19  E-value: 4.67e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 490246132    5 VALVGRPNVGKSTLFNRLTRTRDALVADFPGLTR 38
Cdd:TIGR03596 121 AMIVGIPNVGKSTLINRLAGKKVAKVGNRPGVTK 154
infB CHL00189
translation initiation factor 2; Provisional
3-160 4.73e-05

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 45.98  E-value: 4.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   3 PVVALVGRPNVGKSTLFNRLTRTRDAlVADFPGLTRdrKYGRAEVE------GREFICIDTGGIDgTEEGVETRMAEQSl 76
Cdd:CHL00189 245 PIVTILGHVDHGKTTLLDKIRKTQIA-QKEAGGITQ--KIGAYEVEfeykdeNQKIVFLDTPGHE-AFSSMRSRGANVT- 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  77 laieeaDVVLFMVDARAGLMPADIAIAKHLRSREKPtFLVA-NKTDGID-----VDQAMADF----WSLGlGD--IYPIA 144
Cdd:CHL00189 320 ------DIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAiNKIDKANanterIKQQLAKYnlipEKWG-GDtpMIPIS 391
                        170
                 ....*....|....*.
gi 490246132 145 ASHGRGVTSLLEQALL 160
Cdd:CHL00189 392 ASQGTNIDKLLETILL 407
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
4-38 5.62e-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: 43.72  E-value: 5.62e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 490246132   4 VVALVGRPNVGKSTLFNRLTRTRDALVADFPGLTR 38
Cdd:cd04178  118 TVGVVGYPNVGKSSVINSLKRSRACNVGATPGVTK 152
PRK11058 PRK11058
GTPase HflX; Provisional
2-159 6.37e-05

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 45.09  E-value: 6.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   2 IPVVALVGRPNVGKSTLFNRLTrTRDALVADFPGLTRDRKYGRAEVEG-REFICIDTGGIdgteegveTRMAEQSLLA-- 78
Cdd:PRK11058 197 VPTVSLVGYTNAGKSTLFNRIT-EARVYAADQLFATLDPTLRRIDVADvGETVLADTVGF--------IRHLPHDLVAaf 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  79 ------IEEADVVLFMVDARAGLMPADIA----IAKHLRSREKPTFLVANKTDGIDVDQAMADFWSLGLGDIYPIAASHG 148
Cdd:PRK11058 268 katlqeTRQATLLLHVVDAADVRVQENIEavntVLEEIDAHEIPTLLVMNKIDMLDDFEPRIDRDEENKPIRVWLSAQTG 347
                        170
                 ....*....|.
gi 490246132 149 RGVtSLLEQAL 159
Cdd:PRK11058 348 AGI-PLLFQAL 357
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
5-121 1.12e-04

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: 42.92  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   5 VALVGRPNVGKSTLFNRLTRtRDALVADfPGLTRDR----KYGRAEveGREFIciDTGGIDGTEEGvETRMAEQsllAIE 80
Cdd:cd09912    3 LAVVGEFSAGKSTLLNALLG-EEVLPTG-VTPTTAVitvlRYGLLK--GVVLV--DTPGLNSTIEH-HTEITES---FLP 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 490246132  81 EADVVLFMVDARAGLMPADIAIAKHLRSREKPT-FLVANKTD 121
Cdd:cd09912   73 RADAVIFVLSADQPLTESEREFLKEILKWSGKKiFFVLNKID 114
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
5-60 1.32e-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: 1.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490246132   5 VALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKygraEVEGREFI-CIDTGGI 60
Cdd:cd01849   94 VGVVGLPNVGKSSFINALLNKFKLKVGSIPGTTKLQQ----DVKLDKEIyLYDTPGI 146
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
5-44 1.52e-04

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 44.32  E-value: 1.52e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 490246132   5 VALVGRPNVGKSTLFNRLTRTRDAlVADFPGLTRDRKYGR 44
Cdd:PRK09554   6 IGLIGNPNSGKTTLFNQLTGARQR-VGNWAGVTVERKEGQ 44
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
5-34 2.11e-04

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: 43.37  E-value: 2.11e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 490246132   5 VALVGRPNVGKSTLFNRLTRTrDALVADFP 34
Cdd:cd01899    1 IGLVGKPNVGKSTFFNAATLA-DVEIANYP 29
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
79-262 3.35e-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: 41.15  E-value: 3.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  79 IEEADVVLFMVDARAGLMPADIAIAKHLRSREKPTFLVANKTDGI--DV-DQAMADFWSLGLGDIYpIAASHGRGVTSLL 155
Cdd:cd01859    9 IKEADVVLEVVDARDPELTRSRKLERMALELGKKLIIVLNKADLVprEVlEKWKEVFESEGLPVVY-VSARERLGTRILR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 156 EQALlpwvdevnpqeEVDEDAEywakfeaeqngeaeeepeddfnpqdlPIKLAIVGRPNVGKSTLTNRILGEDRVV---V 232
Cdd:cd01859   88 RTIK-----------ELAIDGK--------------------------PVIVGVVGYPKVGKSSIINALKGRHSAStspI 130
                        170       180       190
                 ....*....|....*....|....*....|
gi 490246132 233 YDMPGTTRDsiyIPMQRDEREYVLIDTAGV 262
Cdd:cd01859  131 PGSPGYTKG---IQLVRIDSKIYLIDTPGV 157
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
79-240 4.94e-04

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: 40.29  E-value: 4.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  79 IEEADVVLFMVDARAGLMPADIAIAKHLRS--REKPTFLVANKTDgidvdqamadfwslglgdiypiaashgrgvtslle 156
Cdd:cd01857    9 IERSDVVVQIVDARNPLFFRCPDLEKYVKEvdPSKENVLLLNKAD----------------------------------- 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 157 qaLLPwvdevnpqeevDEDAEYWAKFEAEQNGeaeeepeddfnpqDLPIKLAI-------VGRPNVGKSTLTNRILGEDR 229
Cdd:cd01857   54 --LVT-----------EEQRKAWARYFKKEGI-------------VVLFFSALneatiglVGYPNVGKSSLINALVGSKK 107
                        170
                 ....*....|.
gi 490246132 230 VVVYDMPGTTR 240
Cdd:cd01857  108 VSVSSTPGKTK 118
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
5-197 6.15e-04

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 41.42  E-value: 6.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   5 VALVGRPNVGKSTLFNRLTRTRDAL-----------VADFPGLTRDRKYG------RAEVEGREFICIDT-GGIDGTEEG 66
Cdd:cd04170    2 IALVGHSGSGKTTLAEALLYATGAIdrlgrvedgntVSDYDPEEKKRKMSietsvaPLEWNGHKINLIDTpGYADFVGET 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  67 VETRMAeqsllaieeADVVLFMVDARAGLMPADIAIAKHLRSREKPTFLVANKTD--GIDVD---QAMADFWSLGLGDI- 140
Cdd:cd04170   82 LSALRA---------VDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDraRADFDktlAALREAFGRPVVPIq 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490246132 141 YPIAA-SHGRGVTSLL-EQALLpwVDEVNPQEEVDEDAEYWAKFEA--EQNGEAEEEpEDD 197
Cdd:cd04170  153 LPIGEgDEFTGVVDLLsEKAYR--YDPGEPSVEIEIPEELKEKVAEarEELLEAVAE-TDE 210
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
3-160 7.34e-04

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: 40.15  E-value: 7.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   3 PVVALVGRPNVGKSTLFNRLTRTRdalVAD--FPGLTRdrKYGRAEVE----GREFICIDTggiDGTEEGVETRMAEQSL 76
Cdd:cd01887    1 PVVTVMGHVDHGKTTLLDKIRKTN---VAAgeAGGITQ--HIGAYQVPidvkIPGITFIDT---PGHEAFTNMRARGASV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  77 laieeADVVLFMVDARAGLMPADIAIAKHLRSREKPTFLVANKTD-----GIDVDQAMADFWSLGL------GDIY--PI 143
Cdd:cd01887   73 -----TDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDkpygtEADPERVKNELSELGLvgeewgGDVSivPI 147
                        170
                 ....*....|....*..
gi 490246132 144 AASHGRGVTSLLEQALL 160
Cdd:cd01887  148 SAKTGEGIDDLLEAILL 164
PRK09602 PRK09602
translation-associated GTPase; Reviewed
5-91 7.63e-04

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 41.72  E-value: 7.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   5 VALVGRPNVGKSTLFNRLTRTrDALVADFPGLTRDRK----YGRAEVEGREF---------ICIDT------------GG 59
Cdd:PRK09602   4 IGLVGKPNVGKSTFFNAATLA-DVEIANYPFTTIDPNvgvaYVRVECPCKELgvkcnprngKCIDGtrfipvelidvaGL 82
                         90       100       110
                 ....*....|....*....|....*....|...
gi 490246132  60 IDGTEEGvetR-MAEQSLLAIEEADVVLFMVDA 91
Cdd:PRK09602  83 VPGAHEG---RgLGNQFLDDLRQADALIHVVDA 112
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
4-60 1.20e-03

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: 39.61  E-value: 1.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132   4 VVALVGRPNVGKSTLFNRLTRTRDAL---VADFPGLTRDRKYGRAeveGREFICIDTGGI 60
Cdd:cd01859  101 IVGVVGYPKVGKSSIINALKGRHSAStspIPGSPGYTKGIQLVRI---DSKIYLIDTPGV 157
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
264-384 2.15e-03

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


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 39.13  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 264 KRGKITDVV--EKFsvIKTLQA-IEDANVVLLVIDAREGISDQD------LSLLGFilnsgRSLVIVVNKWDGLSQE--- 331
Cdd:cd04171   50 KRLGFIDVPghEKF--VKNMLAgAGGIDAVLLVVAADEGIMPQTrehleiLELLGI-----KKGLVVLTKADLVDEDrle 122
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490246132 332 -VKEQVKETLdyRLGFIDFARVHFISALHGSGVgnlfESVREAYDSATRRVSTA 384
Cdd:cd04171  123 lVEEEILELL--AGTFLADAPIFPVSSVTGEGI----EELKNYLDELAEPQSKD 170
PRK11058 PRK11058
GTPase HflX; Provisional
199-372 2.57e-03

GTPase HflX; Provisional


Pssm-ID: 182934 [Multi-domain]  Cd Length: 426  Bit Score: 40.09  E-value: 2.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 199 NPQDLPiKLAIVGRPNVGKSTLTNRILgEDRVVVYDMPGTTRDsiyiPMQR-----DEREYVLIDTAGVrKRGKITDVVE 273
Cdd:PRK11058 193 IKADVP-TVSLVGYTNAGKSTLFNRIT-EARVYAADQLFATLD----PTLRridvaDVGETVLADTVGF-IRHLPHDLVA 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 274 KFSVikTLQAIEDANVVLLVIDA-----REGISDQDLSLLGFILNSGRSLViVVNKWDGLSQEVK--EQVKETLDYRLgf 346
Cdd:PRK11058 266 AFKA--TLQETRQATLLLHVVDAadvrvQENIEAVNTVLEEIDAHEIPTLL-VMNKIDMLDDFEPriDRDEENKPIRV-- 340
                        170       180
                 ....*....|....*....|....*.
gi 490246132 347 idfarvhFISALHGSGVGNLFESVRE 372
Cdd:PRK11058 341 -------WLSAQTGAGIPLLFQALTE 359
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
289-382 3.59e-03

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 39.90  E-value: 3.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 289 VVLLVIDAREGISDQD------LSLLGFilnsgRSLVIVVNKWDGLSQE----VKEQVKETLdyRLGFIDFARVHFISAL 358
Cdd:COG3276   77 LVLLVVAADEGVMPQTrehlaiLDLLGI-----KRGIVVLTKADLVDEEwlelVEEEIRELL--AGTFLEDAPIVPVSAV 149
                         90       100
                 ....*....|....*....|....
gi 490246132 359 HGSGVGNLfesvREAYDSATRRVS 382
Cdd:COG3276  150 TGEGIDEL----RAALDALAAAVP 169
SRPRB pfam09439
Signal recognition particle receptor beta subunit; The beta subunit of the signal recognition ...
3-121 4.54e-03

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: 38.19  E-value: 4.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132    3 PVVALVGRPNVGKSTLFNRLT--RTRDALVADFPGLTRDRKygraEVEGREFICIDTGGIDG-TEEGVETRMAEQSLLAI 79
Cdd:pfam09439   4 PAVIIAGLCDSGKTSLFTLLTtdSVRPTVTSQEPSAAYRYM----LNKGNSFTLIDFPGHVKlRYKLLETLKDSSSLKGI 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 490246132   80 eeadvvLFMVDARAglMPADIA-IAKHL--------RSREKPTFLVA-NKTD 121
Cdd:pfam09439  80 ------VFVVDSTI--FPKEVTdTAEFLydilsiteLLKNGIDILIAcNKQE 123
PTZ00258 PTZ00258
GTP-binding protein; Provisional
7-47 5.22e-03

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 39.16  E-value: 5.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 490246132   7 LVGRPNVGKSTLFNRLTRTRdALVADFPGLTRDRKYGRAEV 47
Cdd:PTZ00258  26 IVGLPNVGKSTTFNALCKQQ-VPAENFPFCTIDPNTARVNV 65
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
182-293 5.45e-03

Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like (Translocon at the Outer-envelope membrane of Chloroplasts) family contains several Toc proteins, including Toc34, Toc33, Toc120, Toc159, Toc86, Toc125, and Toc90. The Toc complex at the outer envelope membrane of chloroplasts is a molecular machine of ~500 kDa that contains a single Toc159 protein, four Toc75 molecules, and four or five copies of Toc34. Toc64 and Toc12 are associated with the translocon, but do not appear to be part of the core complex. The Toc translocon initiates the import of nuclear-encoded preproteins from the cytosol into the organelle. Toc34 and Toc159 are both GTPases, while Toc75 is a beta-barrel integral membrane protein. Toc159 is equally distributed between a soluble cytoplasmic form and a membrane-inserted form, suggesting that assembly of the Toc complex is dynamic. Toc34 and Toc75 act sequentially to mediate docking and insertion of Toc159 resulting in assembly of the functional translocon.


Pssm-ID: 206652  Cd Length: 248  Bit Score: 38.45  E-value: 5.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132 182 FEAEQNGEAEEE----PEDDFnpqdlPIKLAIVGRPNVGKSTLTNRILGEDRVVV--YDmPGTTRdSIYIPMQRDEREYV 255
Cdd:cd01853   10 PDATQTKLHELEaklkKELDF-----SLTILVLGKTGVGKSSTINSIFGERKVSVsaFQ-SETLR-PREVSRTVDGFKLN 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 490246132 256 LIDTAGV------RKRGKITDVVEKFSVIKTLqaiedaNVVLLV 293
Cdd:cd01853   83 IIDTPGLlesqdqRVNRKILSIIKRFLKKKTI------DVVLYV 120
PRK01889 PRK01889
GTPase RsgA; Reviewed
207-263 5.68e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 38.76  E-value: 5.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490246132 207 LAIVGRPNVGKSTLTNRILGEDRVVVY-----DMPG----TTRDSIYIPMQRdereyVLIDTAGVR 263
Cdd:PRK01889 198 VALLGSSGVGKSTLVNALLGEEVQKTGavredDSKGrhttTHRELHPLPSGG-----LLIDTPGMR 258
AAA_22 pfam13401
AAA domain;
207-322 6.63e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 36.94  E-value: 6.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246132  207 LAIVGRPNVGKSTLTNRIL-----GEDRVVVYDMP-GTTRDSIYipmqrdeREYVLIDTAGVRKRGKITDVVEKfsVIKT 280
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLeqlpeVRDSVVFVDLPsGTSPKDLL-------RALLRALGLPLSGRLSKEELLAA--LQQL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 490246132  281 LQAIedANVVLLVIDAREGISDQDLSLLGFILNSGRSLVIVV 322
Cdd:pfam13401  79 LLAL--AVAVVLIIDEAQHLSLEALEELRDLLNLSSKLLQLI 118
 
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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