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Conserved domains on  [gi|15608851|ref|NP_216229|]
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GTPase Der [Mycobacterium tuberculosis H37Rv]

Protein Classification

ribosome-associated GTPase EngA( domain architecture ID 11479870)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
1-459 0e+00

GTP-binding protein Der; Reviewed


:

Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 861.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851    1 MTQDGTWVDESDWQLDDSEIAESGAA-----PVVAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDALWTGRR 75
Cdd:PRK03003   8 MRADGTWADESDWELDDEDLAELEAAeggplPVVAVVGRPNVGKSTLVNRILGRREAVVEDVPGVTRDRVSYDAEWNGRR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   76 FVVQDTGGWEPNAKGLQRLVAEQASVAMRTADAVILVVDAGVGATAADEAAARILLRSGKPVFLAANKVDSEKGESDAAA 155
Cdd:PRK03003  88 FTVVDTGGWEPDAKGLQASVAEQAEVAMRTADAVLFVVDATVGATATDEAVARVLRRSGKPVILAANKVDDERGEADAAA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  156 LWSLGLGEPHAISAMHGRGVADLLDGVLAALPEVGESASASGGPRRVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTV 235
Cdd:PRK03003 168 LWSLGLGEPHPVSALHGRGVGDLLDAVLAALPEVPRVGSASGGPRRVALVGKPNVGKSSLLNKLAGEERSVVDDVAGTTV 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  236 DPVDSLIELGGDVWRFVDTAGLRRKVGQASGHEFYASVRTHAAIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVL 315
Cdd:PRK03003 248 DPVDSLIELGGKTWRFVDTAGLRRRVKQASGHEYYASLRTHAAIEAAEVAVVLIDASEPISEQDQRVLSMVIEAGRALVL 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  316 AYNKWDLVDEDRRELLQREIDRELVQVRWAQRVNISAKTGRAVHKLVPAMEDALASWDTRIATGPLNTWLTEVTAATPPP 395
Cdd:PRK03003 328 AFNKWDLVDEDRRYYLEREIDRELAQVPWAPRVNISAKTGRAVDKLVPALETALESWDTRIPTGRLNAWLGELVAATPPP 407
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15608851  396 VRGGKQPRILFATQATARPPTFVLFTTGFLEAGYRRFLERRLRETFGFDGSPIRVNVRVREKRA 459
Cdd:PRK03003 408 VRGGKQPRILFATQASTRPPTFVLFTTGFLEAGYRRFLERRLRETFGFEGSPIRISVRVREKRG 471
 
Name Accession Description Interval E-value
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
1-459 0e+00

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 861.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851    1 MTQDGTWVDESDWQLDDSEIAESGAA-----PVVAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDALWTGRR 75
Cdd:PRK03003   8 MRADGTWADESDWELDDEDLAELEAAeggplPVVAVVGRPNVGKSTLVNRILGRREAVVEDVPGVTRDRVSYDAEWNGRR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   76 FVVQDTGGWEPNAKGLQRLVAEQASVAMRTADAVILVVDAGVGATAADEAAARILLRSGKPVFLAANKVDSEKGESDAAA 155
Cdd:PRK03003  88 FTVVDTGGWEPDAKGLQASVAEQAEVAMRTADAVLFVVDATVGATATDEAVARVLRRSGKPVILAANKVDDERGEADAAA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  156 LWSLGLGEPHAISAMHGRGVADLLDGVLAALPEVGESASASGGPRRVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTV 235
Cdd:PRK03003 168 LWSLGLGEPHPVSALHGRGVGDLLDAVLAALPEVPRVGSASGGPRRVALVGKPNVGKSSLLNKLAGEERSVVDDVAGTTV 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  236 DPVDSLIELGGDVWRFVDTAGLRRKVGQASGHEFYASVRTHAAIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVL 315
Cdd:PRK03003 248 DPVDSLIELGGKTWRFVDTAGLRRRVKQASGHEYYASLRTHAAIEAAEVAVVLIDASEPISEQDQRVLSMVIEAGRALVL 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  316 AYNKWDLVDEDRRELLQREIDRELVQVRWAQRVNISAKTGRAVHKLVPAMEDALASWDTRIATGPLNTWLTEVTAATPPP 395
Cdd:PRK03003 328 AFNKWDLVDEDRRYYLEREIDRELAQVPWAPRVNISAKTGRAVDKLVPALETALESWDTRIPTGRLNAWLGELVAATPPP 407
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15608851  396 VRGGKQPRILFATQATARPPTFVLFTTGFLEAGYRRFLERRLRETFGFDGSPIRVNVRVREKRA 459
Cdd:PRK03003 408 VRGGKQPRILFATQASTRPPTFVLFTTGFLEAGYRRFLERRLRETFGFEGSPIRISVRVREKRG 471
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
26-458 0e+00

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 601.63  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  26 APVVAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDALWTGRRFVVQDTGGWEPNAK-GLQRLVAEQASVAMR 104
Cdd:COG1160   2 SPVVAIVGRPNVGKSTLFNRLTGRRDAIVDDTPGVTRDRIYGEAEWGGREFTLIDTGGIEPDDDdGLEAEIREQAELAIE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 105 TADAVILVVDAGVGATAADEAAARILLRSGKPVFLAANKVDSEKGESDAAALWSLGLGEPHAISAMHGRGVADLLDGVLA 184
Cdd:COG1160  82 EADVILFVVDGRAGLTPLDEEIAKLLRRSGKPVILVVNKVDGPKREADAAEFYSLGLGEPIPISAEHGRGVGDLLDAVLE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 185 ALPEVGESASASGgPRRVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLRRKVGQA 264
Cdd:COG1160 162 LLPEEEEEEEEDD-PIKIAIVGRPNVGKSSLINALLGEERVIVSDIAGTTRDSIDTPFERDGKKYTLIDTAGIRRKGKVD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 265 SGHEFYASVRTHAAIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLVDEDR--RELLQREIDRELVQV 342
Cdd:COG1160 241 EGIEKYSVLRTLRAIERADVVLLVIDATEGITEQDLKIAGLALEAGKALVIVVNKWDLVEKDRktREELEKEIRRRLPFL 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 343 RWAQRVNISAKTGRAVHKLVPAMEDALASWDTRIATGPLNTWLTEVTAATPPPVRGGKQPRILFATQATARPPTFVLFTT 422
Cdd:COG1160 321 DYAPIVFISALTGQGVDKLLEAVDEVYESANKRISTSKLNRVLEEAVERHPPPAVKGRRLKIYYATQVGTRPPTFVLFVN 400
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 15608851 423 --GFLEAGYRRFLERRLRETFGFDGSPIRVNVRVREKR 458
Cdd:COG1160 401 dpELLPFSYKRYLENQLREAFGFEGTPIRIEFRKRKNP 438
GTPase_EngA TIGR03594
ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase ...
29-453 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: 553.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851    29 VAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDALWTGRRFVVQDTGGWEPNAKGLQRLVAEQASVAMRTADA 108
Cdd:TIGR03594   1 VAIVGRPNVGKSTLFNRLTGKRDAIVDDTPGVTRDRIYGDAEWGGREFILIDTGGIEEDDDGIDAQIREQAEIAIEEADV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   109 VILVVDAGVGATAADEAAARILLRSGKPVFLAANKVDSEKGESDAAALWSLGLGEPHAISAMHGRGVADLLDGVLAALPE 188
Cdd:TIGR03594  81 ILFVVDGREGLTPEDEEIAKWLRKSGKPVILVANKIDGPKEDADAAEFYSLGFGEPIPISAEHGRGIGDLLDAILELLPE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   189 VGESASASGGPRRVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLRRKVGQASGHE 268
Cdd:TIGR03594 161 EEEEEEEEEDPIKIAIIGRPNVGKSTLVNALLGEERVIVSDIAGTTRDSIDIPFERDGKKYTLIDTAGIRRKGKVTEGVE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   269 FYASVRTHAAIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLV-DEDRRELLQREIDRELVQVRWAQR 347
Cdd:TIGR03594 241 KYSVLRTLKAIERADVVLLVLDATEGITEQDLRIAGLALEAGKALVIVVNKWDLVeDEKTRKEIKKELRRKLPFLDFAPI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   348 VNISAKTGRAVHKLVPAMEDALASWDTRIATGPLNTWLTEVTAATPPPVRGGKQPRILFATQATARPPTFVLFTT--GFL 425
Cdd:TIGR03594 321 VFISALTGQGVDKLLDAIDKVYESANKRISTSKLNRVLEEAVAAHPPPLVGGRRVKIKYATQVGTNPPTFVLFGNrpELL 400
                         410       420
                  ....*....|....*....|....*...
gi 15608851   426 EAGYRRFLERRLRETFGFDGSPIRVNVR 453
Cdd:TIGR03594 401 PFSYKRYLENQFREAFGFEGTPIRLEFK 428
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
198-368 1.93e-77

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: 238.87  E-value: 1.93e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 198 GPRRVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLRRKVGQASGHEFYASVRTHA 277
Cdd:cd01895   1 DPIKIAIIGRPNVGKSSLLNALLGEERVIVSDIAGTTRDSIDVPFEYDGQKYTLIDTAGIRKKGKVTEGIEKYSVLRTLK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 278 AIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLVDED--RRELLQREIDRELVQVRWAQRVNISAKTG 355
Cdd:cd01895  81 AIERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVEKDekTMKEFEKELRRKLPFLDYAPIVFISALTG 160
                       170
                ....*....|...
gi 15608851 356 RAVHKLVPAMEDA 368
Cdd:cd01895 161 QGVDKLFDAIKEV 173
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
201-374 6.97e-30

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: 118.74  E-value: 6.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   201 RVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLRR------KVGQAsghefyasvR 274
Cdd:pfam12631  96 KVVIVGKPNVGKSSLLNALLGEERAIVTDIPGTTRDVIEETINIGGIPLRLIDTAGIREtddeveKIGIE---------R 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   275 THAAIDSAEVAIVLIDASQPLTEQDLRVISMvIEAGRALVLAYNKWDLVDEDRRELLQREIDrelvqvrwaqRVNISAKT 354
Cdd:pfam12631 167 AREAIEEADLVLLVLDASRPLDEEDLEILEL-LKDKKPIIVVLNKSDLLGEIDELEELKGKP----------VLAISAKT 235
                         170       180
                  ....*....|....*....|
gi 15608851   355 GRAVHKLVPAMEDALASWDT 374
Cdd:pfam12631 236 GEGLDELEEAIKELFLAGEI 255
 
Name Accession Description Interval E-value
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
1-459 0e+00

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 861.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851    1 MTQDGTWVDESDWQLDDSEIAESGAA-----PVVAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDALWTGRR 75
Cdd:PRK03003   8 MRADGTWADESDWELDDEDLAELEAAeggplPVVAVVGRPNVGKSTLVNRILGRREAVVEDVPGVTRDRVSYDAEWNGRR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   76 FVVQDTGGWEPNAKGLQRLVAEQASVAMRTADAVILVVDAGVGATAADEAAARILLRSGKPVFLAANKVDSEKGESDAAA 155
Cdd:PRK03003  88 FTVVDTGGWEPDAKGLQASVAEQAEVAMRTADAVLFVVDATVGATATDEAVARVLRRSGKPVILAANKVDDERGEADAAA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  156 LWSLGLGEPHAISAMHGRGVADLLDGVLAALPEVGESASASGGPRRVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTV 235
Cdd:PRK03003 168 LWSLGLGEPHPVSALHGRGVGDLLDAVLAALPEVPRVGSASGGPRRVALVGKPNVGKSSLLNKLAGEERSVVDDVAGTTV 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  236 DPVDSLIELGGDVWRFVDTAGLRRKVGQASGHEFYASVRTHAAIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVL 315
Cdd:PRK03003 248 DPVDSLIELGGKTWRFVDTAGLRRRVKQASGHEYYASLRTHAAIEAAEVAVVLIDASEPISEQDQRVLSMVIEAGRALVL 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  316 AYNKWDLVDEDRRELLQREIDRELVQVRWAQRVNISAKTGRAVHKLVPAMEDALASWDTRIATGPLNTWLTEVTAATPPP 395
Cdd:PRK03003 328 AFNKWDLVDEDRRYYLEREIDRELAQVPWAPRVNISAKTGRAVDKLVPALETALESWDTRIPTGRLNAWLGELVAATPPP 407
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15608851  396 VRGGKQPRILFATQATARPPTFVLFTTGFLEAGYRRFLERRLRETFGFDGSPIRVNVRVREKRA 459
Cdd:PRK03003 408 VRGGKQPRILFATQASTRPPTFVLFTTGFLEAGYRRFLERRLRETFGFEGSPIRISVRVREKRG 471
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
4-461 0e+00

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 651.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851    4 DGTWVDESDWQL-------DDSEIAESGAAPVVAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDALWTGRRF 76
Cdd:PRK09518 246 EGYELDEGDEDLlegsgfvAGDEKAGPKAVGVVAIVGRPNVGKSTLVNRILGRREAVVEDTPGVTRDRVSYDAEWAGTDF 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   77 VVQDTGGWEPNAKGLQRLVAEQASVAMRTADAVILVVDAGVGATAADEAAARILLRSGKPVFLAANKVDSEKGESDAAAL 156
Cdd:PRK09518 326 KLVDTGGWEADVEGIDSAIASQAQIAVSLADAVVFVVDGQVGLTSTDERIVRMLRRAGKPVVLAVNKIDDQASEYDAAEF 405
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  157 WSLGLGEPHAISAMHGRGVADLLDGVLAALPEVGESAS--ASGGPRRVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTT 234
Cdd:PRK09518 406 WKLGLGEPYPISAMHGRGVGDLLDEALDSLKVAEKTSGflTPSGLRRVALVGRPNVGKSSLLNQLTHEERAVVNDLAGTT 485
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  235 VDPVDSLIELGGDVWRFVDTAGLRRKVGQASGHEFYASVRTHAAIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALV 314
Cdd:PRK09518 486 RDPVDEIVEIDGEDWLFIDTAGIKRRQHKLTGAEYYSSLRTQAAIERSELALFLFDASQPISEQDLKVMSMAVDAGRALV 565
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  315 LAYNKWDLVDEDRRELLQREIDRELVQVRWAQRVNISAKTGRAVHKLVPAMEDALASWDTRIATGPLNTWLTEVTAATPP 394
Cdd:PRK09518 566 LVFNKWDLMDEFRRQRLERLWKTEFDRVTWARRVNLSAKTGWHTNRLAPAMQEALESWDQRIPTGKLNAFLGKIQAEHPH 645
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15608851  395 PVRGGKQPRILFATQATARPPTFVLFTTGFLEAGYRRFLERRLRETFGFDGSPIRVNVRVREKRAGK 461
Cdd:PRK09518 646 PLRGGKQPRILFATQASTRPPRFVIFTTGFLEHGYRRFLERSLREEFGFEGSPIQISVNIREKKKRK 712
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
26-458 0e+00

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 601.63  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  26 APVVAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDALWTGRRFVVQDTGGWEPNAK-GLQRLVAEQASVAMR 104
Cdd:COG1160   2 SPVVAIVGRPNVGKSTLFNRLTGRRDAIVDDTPGVTRDRIYGEAEWGGREFTLIDTGGIEPDDDdGLEAEIREQAELAIE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 105 TADAVILVVDAGVGATAADEAAARILLRSGKPVFLAANKVDSEKGESDAAALWSLGLGEPHAISAMHGRGVADLLDGVLA 184
Cdd:COG1160  82 EADVILFVVDGRAGLTPLDEEIAKLLRRSGKPVILVVNKVDGPKREADAAEFYSLGLGEPIPISAEHGRGVGDLLDAVLE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 185 ALPEVGESASASGgPRRVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLRRKVGQA 264
Cdd:COG1160 162 LLPEEEEEEEEDD-PIKIAIVGRPNVGKSSLINALLGEERVIVSDIAGTTRDSIDTPFERDGKKYTLIDTAGIRRKGKVD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 265 SGHEFYASVRTHAAIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLVDEDR--RELLQREIDRELVQV 342
Cdd:COG1160 241 EGIEKYSVLRTLRAIERADVVLLVIDATEGITEQDLKIAGLALEAGKALVIVVNKWDLVEKDRktREELEKEIRRRLPFL 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 343 RWAQRVNISAKTGRAVHKLVPAMEDALASWDTRIATGPLNTWLTEVTAATPPPVRGGKQPRILFATQATARPPTFVLFTT 422
Cdd:COG1160 321 DYAPIVFISALTGQGVDKLLEAVDEVYESANKRISTSKLNRVLEEAVERHPPPAVKGRRLKIYYATQVGTRPPTFVLFVN 400
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 15608851 423 --GFLEAGYRRFLERRLRETFGFDGSPIRVNVRVREKR 458
Cdd:COG1160 401 dpELLPFSYKRYLENQLREAFGFEGTPIRIEFRKRKNP 438
GTPase_EngA TIGR03594
ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase ...
29-453 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: 553.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851    29 VAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDALWTGRRFVVQDTGGWEPNAKGLQRLVAEQASVAMRTADA 108
Cdd:TIGR03594   1 VAIVGRPNVGKSTLFNRLTGKRDAIVDDTPGVTRDRIYGDAEWGGREFILIDTGGIEEDDDGIDAQIREQAEIAIEEADV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   109 VILVVDAGVGATAADEAAARILLRSGKPVFLAANKVDSEKGESDAAALWSLGLGEPHAISAMHGRGVADLLDGVLAALPE 188
Cdd:TIGR03594  81 ILFVVDGREGLTPEDEEIAKWLRKSGKPVILVANKIDGPKEDADAAEFYSLGFGEPIPISAEHGRGIGDLLDAILELLPE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   189 VGESASASGGPRRVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLRRKVGQASGHE 268
Cdd:TIGR03594 161 EEEEEEEEEDPIKIAIIGRPNVGKSTLVNALLGEERVIVSDIAGTTRDSIDIPFERDGKKYTLIDTAGIRRKGKVTEGVE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   269 FYASVRTHAAIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLV-DEDRRELLQREIDRELVQVRWAQR 347
Cdd:TIGR03594 241 KYSVLRTLKAIERADVVLLVLDATEGITEQDLRIAGLALEAGKALVIVVNKWDLVeDEKTRKEIKKELRRKLPFLDFAPI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   348 VNISAKTGRAVHKLVPAMEDALASWDTRIATGPLNTWLTEVTAATPPPVRGGKQPRILFATQATARPPTFVLFTT--GFL 425
Cdd:TIGR03594 321 VFISALTGQGVDKLLDAIDKVYESANKRISTSKLNRVLEEAVAAHPPPLVGGRRVKIKYATQVGTNPPTFVLFGNrpELL 400
                         410       420
                  ....*....|....*....|....*...
gi 15608851   426 EAGYRRFLERRLRETFGFDGSPIRVNVR 453
Cdd:TIGR03594 401 PFSYKRYLENQFREAFGFEGTPIRLEFK 428
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
27-458 0e+00

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 525.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   27 PVVAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDALWTGRRFVVQDTGGWEPNAKGLQRLVAEQASVAMRTA 106
Cdd:PRK00093   2 PVVAIVGRPNVGKSTLFNRLTGKRDAIVADTPGVTRDRIYGEAEWLGREFILIDTGGIEPDDDGFEKQIREQAELAIEEA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  107 DAVILVVDAGVGATAADEAAARILLRSGKPVFLAANKVDSEKGESDAAALWSLGLGEPHAISAMHGRGVADLLDGVLAAL 186
Cdd:PRK00093  82 DVILFVVDGRAGLTPADEEIAKILRKSNKPVILVVNKVDGPDEEADAYEFYSLGLGEPYPISAEHGRGIGDLLDAILEEL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  187 PEVGESASASGGPrRVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLRR--KVGQA 264
Cdd:PRK00093 162 PEEEEEDEEDEPI-KIAIIGRPNVGKSSLINALLGEERVIVSDIAGTTRDSIDTPFERDGQKYTLIDTAGIRRkgKVTEG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  265 SghEFYASVRTHAAIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLVDEDRRELLQREIDRELVQVRW 344
Cdd:PRK00093 241 V--EKYSVIRTLKAIERADVVLLVIDATEGITEQDLRIAGLALEAGRALVIVVNKWDLVDEKTMEEFKKELRRRLPFLDY 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  345 AQRVNISAKTGRAVHKLVPAMEDALASWDTRIATGPLNTWLTEVTAATPPPVRGGKQPRILFATQATARPPTFVLFTTG- 423
Cdd:PRK00093 319 APIVFISALTGQGVDKLLEAIDEAYENANRRISTSVLNRVLEEAVERHPPPLVKGRRLKIKYATQVGTNPPTFVLFVNDp 398
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 15608851  424 ---------FLEAGYrrflerrlRETFGFDGSPIRVNVRVREKR 458
Cdd:PRK00093 399 ellpfsykrYLENQL--------REAFDFEGTPIRLEFREKKNK 434
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
198-368 1.93e-77

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: 238.87  E-value: 1.93e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 198 GPRRVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLRRKVGQASGHEFYASVRTHA 277
Cdd:cd01895   1 DPIKIAIIGRPNVGKSSLLNALLGEERVIVSDIAGTTRDSIDVPFEYDGQKYTLIDTAGIRKKGKVTEGIEKYSVLRTLK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 278 AIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLVDED--RRELLQREIDRELVQVRWAQRVNISAKTG 355
Cdd:cd01895  81 AIERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVEKDekTMKEFEKELRRKLPFLDYAPIVFISALTG 160
                       170
                ....*....|...
gi 15608851 356 RAVHKLVPAMEDA 368
Cdd:cd01895 161 QGVDKLFDAIKEV 173
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
30-186 7.69e-71

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: 221.54  E-value: 7.69e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  30 AVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDALWTGRRFVVQDTGGWEPNAKGLQRLVAEQASVAMRTADAV 109
Cdd:cd01894   1 AIVGRPNVGKSTLFNRLTGRRDAIVSDTPGVTRDRKYGEAEWGGREFILIDTGGIEPDDEGISKEIREQAEIAIEEADVI 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15608851 110 ILVVDAGVGATAADEAAARILLRSGKPVFLAANKVDSEKGESDAAALWSLGLGEPHAISAMHGRGVADLLDGVLAAL 186
Cdd:cd01894  81 LFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNIKEEEEAAEFYSLGFGEPIPISAEHGRGIGDLLDAILELL 157
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
201-369 3.96e-30

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: 121.71  E-value: 3.96e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 201 RVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLRR------KVGQAsghefyasvR 274
Cdd:COG0486 215 KVVIVGRPNVGKSSLLNALLGEERAIVTDIAGTTRDVIEERINIGGIPVRLIDTAGLREtedeveKIGIE---------R 285
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 275 THAAIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLayNKWDLVDedrrellqrEIDRELVQVRWAQRVNISAKT 354
Cdd:COG0486 286 AREAIEEADLVLLLLDASEPLTEEDEEILEKLKDKPVIVVL--NKIDLPS---------EADGELKSLPGEPVIAISAKT 354
                       170
                ....*....|....*
gi 15608851 355 GRAVHKLVPAMEDAL 369
Cdd:COG0486 355 GEGIDELKEAILELV 369
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
201-374 6.97e-30

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: 118.74  E-value: 6.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   201 RVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLRR------KVGQAsghefyasvR 274
Cdd:pfam12631  96 KVVIVGKPNVGKSSLLNALLGEERAIVTDIPGTTRDVIEETINIGGIPLRLIDTAGIREtddeveKIGIE---------R 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   275 THAAIDSAEVAIVLIDASQPLTEQDLRVISMvIEAGRALVLAYNKWDLVDEDRRELLQREIDrelvqvrwaqRVNISAKT 354
Cdd:pfam12631 167 AREAIEEADLVLLVLDASRPLDEEDLEILEL-LKDKKPIIVVLNKSDLLGEIDELEELKGKP----------VLAISAKT 235
                         170       180
                  ....*....|....*....|
gi 15608851   355 GRAVHKLVPAMEDALASWDT 374
Cdd:pfam12631 236 GEGLDELEEAIKELFLAGEI 255
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
201-370 2.58e-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: 112.20  E-value: 2.58e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 201 RVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLRR------KVGQAsghefyasvR 274
Cdd:cd04164   5 KVVIAGKPNVGKSSLLNALAGRDRAIVSDIAGTTRDVIEEEIDLGGIPVRLIDTAGLREtedeieKIGIE---------R 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 275 THAAIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLayNKWDLVDEDRRELLQREIDrelvqvrwaqRVNISAKT 354
Cdd:cd04164  76 AREAIEEADLVLLVVDASEGLDEEDLEILELPAKKPVIVVL--NKSDLLSDAEGISELNGKP----------IIAISAKT 143
                       170
                ....*....|....*.
gi 15608851 355 GRAVHKLVPAMEDALA 370
Cdd:cd04164 144 GEGIDELKEALLELAG 159
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
201-319 1.62e-28

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 108.48  E-value: 1.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   201 RVALVGKPNVGKSSLLNKLAGdQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLrrkVGQAsgHEFYASVRTHAAID 280
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTG-AKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGL---IEGA--SEGEGLGRAFLAII 74
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 15608851   281 SAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNK 319
Cdd:pfam01926  75 EADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
29-143 2.77e-28

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 108.09  E-value: 2.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851    29 VAVVGRPNVGKSTLVNRILGRReAVVQDIPGVTRDRVCYDALWTGRRFVVQDTGGWEPNAKGLQRLvaEQASVAMRTADA 108
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGAK-AIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEGL--GRAFLAIIEADL 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 15608851   109 VILVVDAGVGATAADEAAARILLRSGKPVFLAANK 143
Cdd:pfam01926  79 ILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
203-361 3.80e-28

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: 109.26  E-value: 3.80e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 203 ALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIEL--GGDVwRFVDTAGLRRKVGQASGHEFyasvRTHAAID 280
Cdd:cd00880   1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRKEWELlpLGPV-VLIDTPGLDEEGGLGRERVE----EARQVAD 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 281 SAEVAIVLIDASQPLTEQDLRVISMvIEAGRALVLAYNKWDLVDEDRRELLQREIDRELVQVrwAQRVNISAKTGRAVHK 360
Cdd:cd00880  76 RADLVLLVVDSDLTPVEEEAKLGLL-RERGKPVLLVLNKIDLVPESEEEELLRERKLELLPD--LPVIAVSALPGEGIDE 152

                .
gi 15608851 361 L 361
Cdd:cd00880 153 L 153
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
201-371 3.37e-25

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 107.50  E-value: 3.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  201 RVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLRR------KVGQAsghefyasvR 274
Cdd:PRK05291 217 KVVIAGRPNVGKSSLLNALLGEERAIVTDIAGTTRDVIEEHINLDGIPLRLIDTAGIREtddeveKIGIE---------R 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  275 THAAIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLayNKWDLVDEDrreLLQREIDRELVQvrwaqrvnISAKT 354
Cdd:PRK05291 288 SREAIEEADLVLLVLDASEPLTEEDDEILEELKDKPVIVVL--NKADLTGEI---DLEEENGKPVIR--------ISAKT 354
                        170
                 ....*....|....*..
gi 15608851  355 GRAVHKLVPAMEDALAS 371
Cdd:PRK05291 355 GEGIDELREAIKELAFG 371
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
30-186 1.51e-24

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: 99.24  E-value: 1.51e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  30 AVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDALW-TGRRFVVQDTGGWEPNAKGLQRLVAEQASVAMRtADA 108
Cdd:cd00880   1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRKEWELlPLGPVVLIDTPGLDEEGGLGRERVEEARQVADR-ADL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 109 VILVVDAGVGATAADEAAARiLLRSGKPVFLAANKVDSEKGESDAAALWSLGLG-----EPHAISAMHGRGVADLLDGVL 183
Cdd:cd00880  80 VLLVVDSDLTPVEEEAKLGL-LRERGKPVLLVLNKIDLVPESEEEELLRERKLEllpdlPVIAVSALPGEGIDELRKKIA 158

                ...
gi 15608851 184 AAL 186
Cdd:cd00880 159 ELL 161
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
29-188 4.50e-24

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 101.60  E-value: 4.50e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  29 VAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCydALWTGRR----FVvqDTGGW-EPNAKgLQRLVAEQASVAM 103
Cdd:COG1159   6 VAIVGRPNVGKSTLLNALVGQKVSIVSPKPQTTRHRIR--GIVTREDaqivFV--DTPGIhKPKRK-LGRRMNKAAWSAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 104 RTADAVILVVDAGVGATAADEAAARILLRSGKPVFLAANKVDSEKGES--DAAALWSlGLGEPHA---ISAMHGRGVADL 178
Cdd:COG1159  81 EDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLVKKEEllPLLAEYS-ELLDFAEivpISALKGDNVDEL 159
                       170
                ....*....|
gi 15608851 179 LDGVLAALPE 188
Cdd:COG1159 160 LDEIAKLLPE 169
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
29-180 5.43e-24

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: 97.92  E-value: 5.43e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  29 VAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVcyDALWTGRR----FVvqDTGG-WEPNAKGLQRLVaEQASVAM 103
Cdd:cd04163   6 VAIIGRPNVGKSTLLNALVGQKISIVSPKPQTTRNRI--RGIYTDDDaqiiFV--DTPGiHKPKKKLGERMV-KAAWSAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 104 RTADAVILVVDAGVGATAADEAAARILLRSGKPVFLAANKVDSEKGESDAAAL--WSLGLGEP---HAISAMHGRGVADL 178
Cdd:cd04163  81 KDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLVKDKEDLLPLleKLKELHPFaeiFPISALKGENVDEL 160

                ..
gi 15608851 179 LD 180
Cdd:cd04163 161 LE 162
era PRK00089
GTPase Era; Reviewed
29-188 1.63e-23

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 100.12  E-value: 1.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   29 VAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVcydalwTG------RRFVVQDTGGW-EPNAKgLQRLVAEQASV 101
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQKISIVSPKPQTTRHRI------RGivteddAQIIFVDTPGIhKPKRA-LNRAMNKAAWS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  102 AMRTADAVILVVDAGVGATAADEAAARILLRSGKPVFLAANKVD--SEKGESDAAALWSLGLGEP---HAISAMHGRGVA 176
Cdd:PRK00089  81 SLKDVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDlvKDKEELLPLLEELSELMDFaeiVPISALKGDNVD 160
                        170
                 ....*....|..
gi 15608851  177 DLLDGVLAALPE 188
Cdd:PRK00089 161 ELLDVIAKYLPE 172
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
30-180 3.53e-21

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: 89.82  E-value: 3.53e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  30 AVVGRPNVGKSTLVNRILGRREAVVQDIPGVTR--DRVCYDALWTGRRFVVQDTGGWEPNAKGLQRLVAEQasvAMRTAD 107
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRdpDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELARL---LLRGAD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 108 AVILVVDAGVGATAADEAAARI--LLRSGKPVFLAANKVD----SEKGESDAAALWSLGLGEP-HAISAMHGRGVADLLD 180
Cdd:cd00882  78 LILLVVDSTDRESEEDAKLLILrrLRKEGIPIILVGNKIDlleeREVEELLRLEELAKILGVPvFEVSAKTGEGVDELFE 157
KH_dom-like pfam14714
KH-domain-like of EngA bacterial GTPase enzymes, C-terminal; The KH-like domain at the ...
375-453 6.46e-21

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: 86.69  E-value: 6.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   375 RIATGPLNTWLTEVTAATPPPVRGGKQPRILFATQATARPPTFVLFT--TGFLEAGYRRFLERRLRETFGFDGSPIRVNV 452
Cdd:pfam14714   1 RISTSELNRVLEEAVARHPPPSVKGKRLKIYYATQVGTRPPTFVLFVndPELVPFSYKRYLENQLREAFGFEGTPIRLIF 80

                  .
gi 15608851   453 R 453
Cdd:pfam14714  81 R 81
mnmE_trmE_thdF TIGR00450
tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF ...
199-330 1.03e-20

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: 94.09  E-value: 1.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   199 PRRVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLRRkvgQASGHEFYASVRTHAA 278
Cdd:TIGR00450 203 GFKLAIVGSPNVGKSSLLNALLKQDRAIVSDIKGTTRDVVEGDFELNGILIKLLDTAGIRE---HADFVERLGIEKSFKA 279
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15608851   279 IDSAEVAIVLIDASQPLTEqDLRVISMVIEAGRALVLAYNKWDLVDEDRREL 330
Cdd:TIGR00450 280 IKQADLVIYVLDASQPLTK-DDFLIIDLNKSKKPFILVLNKIDLKINSLEFF 330
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
203-358 2.27e-20

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: 87.51  E-value: 2.27e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 203 ALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPV---DSLIELGGDVwRFVDTAGLRRKVGQASGHEFYASVRThaai 279
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDvyvKELDKGKVKL-VLVDTPGLDEFGGLGREELARLLLRG---- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 280 dsAEVAIVLIDASQPLTEQDLRVISMVI--EAGRALVLAYNKWDLVDEDRRELLQREIDREL---VQVrwaqrVNISAKT 354
Cdd:cd00882  76 --ADLILLVVDSTDRESEEDAKLLILRRlrKEGIPIILVGNKIDLLEEREVEELLRLEELAKilgVPV-----FEVSAKT 148

                ....
gi 15608851 355 GRAV 358
Cdd:cd00882 149 GEGV 152
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
203-326 1.22e-19

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: 85.56  E-value: 1.22e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 203 ALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLrrkvgQASGHEFYASVR--THAAID 280
Cdd:cd01894   1 AIVGRPNVGKSTLFNRLTGRRDAIVSDTPGVTRDRKYGEAEWGGREFILIDTGGI-----EPDDEGISKEIReqAEIAIE 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15608851 281 SAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLVDED 326
Cdd:cd01894  76 EADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKIDNIKEE 121
GTP_HydF TIGR03918
[FeFe] hydrogenase H-cluster maturation GTPase HydF; This model describes the family of the ...
201-361 1.82e-19

[FeFe] hydrogenase H-cluster maturation GTPase HydF; This model describes the family of the [Fe] hydrogenase maturation protein HypF as characterized in Chlamydomonas reinhardtii and found, in an operon with radical SAM proteins HydE and HydG, in numerous bacteria. It has GTPase activity, can bind an 4Fe-4S cluster, and is essential for hydrogenase activity. [Protein fate, Protein modification and repair]


Pssm-ID: 274853 [Multi-domain]  Cd Length: 391  Bit Score: 89.88  E-value: 1.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   201 RVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELG--GDVwRFVDTAG---------LRRKvgqasghef 269
Cdd:TIGR03918   8 HIGIFGRRNAGKSSLINALTGQDIAIVSDVPGTTTDPVYKAMELLplGPV-VLIDTAGlddegelgeLRVE--------- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   270 yasvRTHAAIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLVDEDrrellqrEIDRELVQVRWAQRVN 349
Cdd:TIGR03918  78 ----KTREVLDKTDLALLVVDAEQGPGEYELELIEELKERKIPYIVVINKIDLGEES-------AEKEKLEKKFGLPPIF 146
                         170
                  ....*....|..
gi 15608851   350 ISAKTGRAVHKL 361
Cdd:TIGR03918 147 VSALTGEGIDEL 158
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
29-186 3.10e-19

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: 84.47  E-value: 3.10e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  29 VAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRD--RVCYDalWTGRRFVVQDTGGW-------EpnAKGLQRlvaeqA 99
Cdd:cd04164   6 VVIAGKPNVGKSSLLNALAGRDRAIVSDIAGTTRDviEEEID--LGGIPVRLIDTAGLretedeiE--KIGIER-----A 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 100 SVAMRTADAVILVVDAGVGatAADEAAARILLRSGKPVFLAANKVDSekgESDAAALWSLGLGEPHAISAMHGRGVADLL 179
Cdd:cd04164  77 REAIEEADLVLLVVDASEG--LDEEDLEILELPAKKPVIVVLNKSDL---LSDAEGISELNGKPIIAISAKTGEGIDELK 151

                ....*..
gi 15608851 180 DGVLAAL 186
Cdd:cd04164 152 EALLELA 158
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
202-369 1.05e-18

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 86.20  E-value: 1.05e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 202 VALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPV-------DS-LIelggdvwrFVDTAGL---RRKVGQASghefy 270
Cdd:COG1159   6 VAIVGRPNVGKSTLLNALVGQKVSIVSPKPQTTRHRIrgivtreDAqIV--------FVDTPGIhkpKRKLGRRM----- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 271 asVRT-HAAIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLVDEDRRELLQREIDRELvqvRWAQRVN 349
Cdd:COG1159  73 --NKAaWSALEDVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLVKKEELLPLLAEYSELL---DFAEIVP 147
                       170       180
                ....*....|....*....|
gi 15608851 350 ISAKTGRAVHKLVPAMEDAL 369
Cdd:COG1159 148 ISALKGDNVDELLDEIAKLL 167
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
199-362 3.47e-18

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: 81.65  E-value: 3.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   199 PRRVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELGGDVWRF--VDTAG--LRRKVGQASGHEFYASVR 274
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEDGKTYKFnlLDTAGqeDYDAIRRLYYPQVERSLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   275 ThaaidsAEVAIVLIDASQPLTEQDlRVISMVIEAGRALVLAYNKWDLVDEDRRELLQREIDrelvqvRWAQR--VNISA 352
Cdd:TIGR00231  81 V------FDIVILVLDVEEILEKQT-KEIIHHADSGVPIILVGNKIDLKDADLKTHVASEFA------KLNGEpiIPLSA 147
                         170
                  ....*....|
gi 15608851   353 KTGRAVHKLV 362
Cdd:TIGR00231 148 ETGKNIDSAF 157
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
29-180 3.95e-18

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: 86.27  E-value: 3.95e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  29 VAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDALWTGRRFVVQDTGGW-------EpnAKGLQRlvAEQasv 101
Cdd:COG0486 216 VVIVGRPNVGKSSLLNALLGEERAIVTDIAGTTRDVIEERINIGGIPVRLIDTAGLretedevE--KIGIER--ARE--- 288
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15608851 102 AMRTADAVILVVDAGVGATAADEAAARILlrSGKPVFLAANKVDseKGESDAAALWSLGLGEPHAISAMHGRGVADLLD 180
Cdd:COG0486 289 AIEEADLVLLLLDASEPLTEEDEEILEKL--KDKPVIVVLNKID--LPSEADGELKSLPGEPVIAISAKTGEGIDELKE 363
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
202-362 6.52e-18

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: 80.97  E-value: 6.52e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 202 VALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPV-------DS-LIelggdvwrFVDTAGL---RRKVGQASghefy 270
Cdd:cd04163   6 VAIIGRPNVGKSTLLNALVGQKISIVSPKPQTTRNRIrgiytddDAqII--------FVDTPGIhkpKKKLGERM----- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 271 asVRT-HAAIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLVDEDRRELLQREIDRELVQvrWAQRVN 349
Cdd:cd04163  73 --VKAaWSALKDVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLVKDKEDLLPLLEKLKELHP--FAEIFP 148
                       170
                ....*....|...
gi 15608851 350 ISAKTGRAVHKLV 362
Cdd:cd04163 149 ISALKGENVDELL 161
era PRK00089
GTPase Era; Reviewed
202-369 2.20e-17

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 82.40  E-value: 2.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  202 VALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPV-------DS-LIelggdvwrFVDTAGL---RRKVGQASghefy 270
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQKISIVSPKPQTTRHRIrgivtedDAqII--------FVDTPGIhkpKRALNRAM----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  271 asVRT-HAAIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLVDeDRRELLQREID-RELVQvrWAQRV 348
Cdd:PRK00089  75 --NKAaWSSLKDVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVK-DKEELLPLLEElSELMD--FAEIV 149
                        170       180
                 ....*....|....*....|.
gi 15608851  349 NISAKTGRAVHKLVPAMEDAL 369
Cdd:PRK00089 150 PISALKGDNVDELLDVIAKYL 170
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
29-180 2.12e-16

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 80.93  E-value: 2.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   29 VAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDALWTGRRFVVQDTGGW-EPNAK----GLQRlvAEQasvAM 103
Cdd:PRK05291 218 VVIAGRPNVGKSSLLNALLGEERAIVTDIAGTTRDVIEEHINLDGIPLRLIDTAGIrETDDEvekiGIER--SRE---AI 292
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15608851  104 RTADAVILVVDAGVGATAADEAAarILLRSGKPVFLAANKVDsekgESDAAALWSLGLGEPHAISAMHGRGVADLLD 180
Cdd:PRK05291 293 EEADLVLLVLDASEPLTEEDDEI--LEELKDKPVIVVLNKAD----LTGEIDLEEENGKPVIRISAKTGEGIDELRE 363
mnmE_trmE_thdF TIGR00450
tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF ...
29-145 1.70e-15

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: 78.30  E-value: 1.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851    29 VAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDALWTGRRFVVQDTGGWEPNAKGLQRLVAEQASVAMRTADA 108
Cdd:TIGR00450 206 LAIVGSPNVGKSSLLNALLKQDRAIVSDIKGTTRDVVEGDFELNGILIKLLDTAGIREHADFVERLGIEKSFKAIKQADL 285
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 15608851   109 VILVVDAGVGATAADEAAARiLLRSGKPVFLAANKVD 145
Cdd:TIGR00450 286 VIYVLDASQPLTKDDFLIID-LNKSKKPFILVLNKID 321
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
29-180 5.05e-15

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: 75.98  E-value: 5.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851    29 VAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDALWTGRRFVVQDTGGW-EPNAK----GLQRlvaeqASVAM 103
Cdd:pfam12631  97 VVIVGKPNVGKSSLLNALLGEERAIVTDIPGTTRDVIEETINIGGIPLRLIDTAGIrETDDEvekiGIER-----AREAI 171
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15608851   104 RTADAVILVVDAGVGATAADEAAArILLRSGKPVFLAANKVDSEKGESdaaALWSLGLGEPHAISAMHGRGVADLLD 180
Cdd:pfam12631 172 EEADLVLLVLDASRPLDEEDLEIL-ELLKDKKPIIVVLNKSDLLGEID---ELEELKGKPVLAISAKTGEGLDELEE 244
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
202-372 1.49e-14

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: 71.39  E-value: 1.49e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 202 VALVGKPNVGKSSLLNKLAGDQrsvvHEA-----AGTTvdpvdSLI---ELGGDvWRFVDTAG---------LRRKVGQA 264
Cdd:cd01876   2 VAFAGRSNVGKSSLINALTNRK----KLArtsktPGRT-----QLInffNVGDK-FRLVDLPGygyakvskeVREKWGKL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 265 SGHefYASVRthaaiDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLVDEDRRELLQREIDRELVQVRW 344
Cdd:cd01876  72 IEE--YLENR-----ENLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLFNI 144
                       170       180
                ....*....|....*....|....*....
gi 15608851 345 AQRV-NISAKTGRAVHKLvpamEDALASW 372
Cdd:cd01876 145 LPPViLFSSKKGTGIDEL----RALIAEW 169
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
27-184 2.53e-14

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: 70.48  E-value: 2.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851    27 PVVAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDALWTGRRFVVQ--DTGGWEPNAKgLQRLVAEQASVAMR 104
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEDGKTYKFNllDTAGQEDYDA-IRRLYYPQVERSLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   105 TADAVILVVDAGVGATAADEAAARiLLRSGKPVFLAANKVD--SEKGESDAAALWSLGLGEPHA-ISAMHGRGVADLLDG 181
Cdd:TIGR00231  81 VFDIVILVLDVEEILEKQTKEIIH-HADSGVPIILVGNKIDlkDADLKTHVASEFAKLNGEPIIpLSAETGKNIDSAFKI 159

                  ...
gi 15608851   182 VLA 184
Cdd:TIGR00231 160 VEA 162
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
29-188 3.32e-14

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: 72.42  E-value: 3.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851    29 VAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDALWTGRRFVVQDTGGWEPNAKGLQRLVAEQASVAMRTADA 108
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHGQKISITSPKAQTTRNRISGIHTTGASQIIFIDTPGFHEKKHSLNRLMMKEARSAIGGVDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   109 VILVVDAGVGATAADEAAAriLLRSGK-PVFLAANKVDS-EKGESDAAALWSLGLGEPHA---ISAMHGRGVADLLDGVL 183
Cdd:TIGR00436  83 ILFVVDSDQWNGDGEFVLT--KLQNLKrPVVLTRNKLDNkFKDKLLPLIDKYAILEDFKDivpISALTGDNTSFLAAFIE 160

                  ....*
gi 15608851   184 AALPE 188
Cdd:TIGR00436 161 VHLPE 165
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
200-371 7.14e-13

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 66.54  E-value: 7.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 200 RRVALVGKPNVGKSSLLNKLAGDQRSVVHEAA--GTTVDPVDslIEL-GGDVW-RFVDTAGLRRkvgQASGHEFYASvrt 275
Cdd:COG1100   4 KKIVVVGTGGVGKTSLVNRLVGDIFSLEKYLStnGVTIDKKE--LKLdGLDVDlVIWDTPGQDE---FRETRQFYAR--- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 276 haAIDSAEVAIVLIDASQPLTEQDLR-VISMVIEAGRA--LVLAYNKWDLVDEDRRELLQReIDRELVQVRWAQRVNISA 352
Cdd:COG1100  76 --QLTGASLYLFVVDGTREETLQSLYeLLESLRRLGKKspIILVLNKIDLYDEEEIEDEER-LKEALSEDNIVEVVATSA 152
                       170
                ....*....|....*....
gi 15608851 353 KTGRAVHKLVPAMEDALAS 371
Cdd:COG1100 153 KTGEGVEELFAALAEILRG 171
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
201-369 7.58e-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: 68.57  E-value: 7.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   201 RVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLRRKvgqasGHEFY--ASVRTHAA 278
Cdd:TIGR00436   2 FVAILGRPNVGKSTLLNQLHGQKISITSPKAQTTRNRISGIHTTGASQIIFIDTPGFHEK-----KHSLNrlMMKEARSA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   279 IDSAEVAIVLIDASQPLTEQDLrVISMVIEAGRALVLAYNKWDLVDEDRRELLqreIDRELVQVRWAQRVNISAKTGRAV 358
Cdd:TIGR00436  77 IGGVDLILFVVDSDQWNGDGEF-VLTKLQNLKRPVVLTRNKLDNKFKDKLLPL---IDKYAILEDFKDIVPISALTGDNT 152
                         170
                  ....*....|.
gi 15608851   359 HKLVPAMEDAL 369
Cdd:TIGR00436 153 SFLAAFIEVHL 163
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
92-290 1.26e-12

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 67.83  E-value: 1.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  92 QRLVAEQasvaMRTADAVILVVDAgvgataadeaaaRIL----------LRSGKPVFLAANKVD-SEKGESDAAALWSLG 160
Cdd:COG1161  14 RRQIKEI----LKLVDLVIEVVDA------------RIPlssrnpmldeLVGNKPRLLVLNKADlADPSVTKQWLKYFEK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 161 LGEP-HAISAMHGRGVADLLDGVLAALPEVGESasasGGPRRVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVD--- 236
Cdd:COG1161  78 QGVDaLAISAKKGKGIKELIEAIRELAPEKGIK----RRPIRVMIVGIPNVGKSTLINRLAGKKVAKTGNKPGVTKGqqw 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15608851 237 -PVDSLIELggdvwrfVDTAG-LRRK-VGQASGhefYASVRTHA----AIDSAEVAIVLID 290
Cdd:COG1161 154 iKLDDGLEL-------LDTPGiLWPKfEDPEVG---YKLAATGAikdeVLDLEEVALFLLG 204
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
203-371 4.22e-12

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: 64.01  E-value: 4.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 203 ALVGKPNVGKSSLLNKLAGDqRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLrrkvgqasghefYaSVRTHA---AI 279
Cdd:cd01879   1 ALVGNPNVGKTTLFNALTGA-RQKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPGT------------Y-SLTPYSedeKV 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 280 -------DSAEVAIVLIDASQPltEQDLRVISMVIEAGRALVLAYNKWDL-------VDEDRrelLQREIDrelVQVrwa 345
Cdd:cd01879  67 ardfllgEEPDLIVNVVDATNL--ERNLYLTLQLLELGLPVVVALNMIDEaekrgikIDLDK---LSELLG---VPV--- 135
                       170       180
                ....*....|....*....|....*.
gi 15608851 346 qrVNISAKTGRAVHKLVPAMEDALAS 371
Cdd:cd01879 136 --VPTSARKGEGIDELLDAIAKLAES 159
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
29-62 1.23e-11

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


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 62.93  E-value: 1.23e-11
                        10        20        30
                ....*....|....*....|....*....|....
gi 15608851  29 VAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTR 62
Cdd:cd01856 118 AMVVGIPNVGKSTLINRLRGKKVAKVGNKPGVTR 151
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
200-364 3.67e-11

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: 61.31  E-value: 3.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   200 RRVALVGKPNVGKSSLLNKLAGdQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAG---LrrkvGQASGHEFYAsvRTH 276
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTG-ANQHVGNWPGVTVEKKEGKFKYKGYEIEIVDLPGiysL----SPYSEEERVA--RDY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   277 AAIDSAEVAIVLIDASQPltEQDLRVISMVIEAGRALVLAYNKWDLVDEDR----RELLQREIDrelVQVrwaqrVNISA 352
Cdd:pfam02421  74 LLNEKPDVIVNVVDATNL--ERNLYLTLQLLELGLPVVLALNMMDEAEKKGikidIKKLSELLG---VPV-----VPTSA 143
                         170
                  ....*....|..
gi 15608851   353 KTGRAVHKLVPA 364
Cdd:pfam02421 144 RKGEGIDELLDA 155
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
92-221 5.44e-11

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: 62.91  E-value: 5.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851    92 QRLVAEQASVAmrtaDAVILVVDAgvgataadeaaaRI----------LLRSGKPVFLAANKVDseKGESDAAALWSLGL 161
Cdd:TIGR03596  12 RREIKENLKLV----DVVIEVLDA------------RIplssrnpmidEIRGNKPRLIVLNKAD--LADPAVTKQWLKYF 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15608851   162 GEPH----AISAMHGRGVADLLDGVLAALPEVGESASASGG---PRRVALVGKPNVGKSSLLNKLAG 221
Cdd:TIGR03596  74 EEKGikalAVNAKKGAGVKKIIKAAKKLLKEKNEKLKAKGLknrPIRAMIVGIPNVGKSTLINRLAG 140
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
201-369 6.32e-11

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: 61.71  E-value: 6.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 201 RVALVGKPNVGKSSLLNKLAGDQRsvvhEAAG---TTVDPVDSLIELGGDvwR---FVDTAGLRRKVgqasGHEFYASVR 274
Cdd:cd01878  43 TVALVGYTNAGKSTLFNALTGADV----LAEDqlfATLDPTTRRIKLPGG--RevlLTDTVGFIRDL----PHQLVEAFR 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 275 -THAAIDSAEVAIVLIDASQPLTEQDLRVISMVIE----AGRALVLAYNKWDLVDEDRRELLQREIDRElvqvrwaqRVN 349
Cdd:cd01878 113 sTLEEVAEADLLLHVVDASDPDREEQIETVEEVLKelgaDDIPIILVLNKIDLLDDEELEERLRAGRPD--------AVF 184
                       170       180
                ....*....|....*....|
gi 15608851 350 ISAKTGRAVHKLVPAMEDAL 369
Cdd:cd01878 185 ISAKTGEGLDLLKEAIEELL 204
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
199-371 1.37e-10

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 63.60  E-value: 1.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 199 PRRVALVGKPNVGKSSLLNKLAG-DQRsvVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLrrkvgqasgHEFYAS----- 272
Cdd:COG0370   3 MITIALVGNPNVGKTTLFNALTGsRQK--VGNWPGVTVEKKEGKFKLKGKEIELVDLPGT---------YSLSAYspdek 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 273 -VRTHAAIDSAEVAIVLIDASQPltEQDLRVISMVIEAGRALVLAYNKWDLVdeDRRELlqrEID-----REL-VQVrwa 345
Cdd:COG0370  72 vARDFLLEEKPDVVVNVVDATNL--ERNLYLTLQLLELGIPVVLALNMMDEA--EKKGI---KIDveklsKLLgVPV--- 141
                       170       180
                ....*....|....*....|....*.
gi 15608851 346 qrVNISAKTGRAVHKLVPAMEDALAS 371
Cdd:COG0370 142 --VPTSARKGKGIDELKEAIIEAAEG 165
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
29-63 2.30e-10

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 61.28  E-value: 2.30e-10
                        10        20        30
                ....*....|....*....|....*....|....*
gi 15608851  29 VAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRD 63
Cdd:COG1161 116 VMIVGIPNVGKSTLINRLAGKKVAKTGNKPGVTKG 150
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
201-353 5.14e-10

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: 58.33  E-value: 5.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 201 RVALVGKPNVGKSSLLNKLAGDQ---RSVVHEAAGTTVdpvdsL-IELGGDVwRFVDTAGLRrkvGQASGHEfyaSVrTH 276
Cdd:cd09912   2 LLAVVGEFSAGKSTLLNALLGEEvlpTGVTPTTAVITV-----LrYGLLKGV-VLVDTPGLN---STIEHHT---EI-TE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 277 AAIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRA-LVLAYNKWDLVDEDRRELLQREIDRELVQVRWAQRVN----IS 351
Cdd:cd09912  69 SFLPRADAVIFVLSADQPLTESEREFLKEILKWSGKkIFFVLNKIDLLSEEELEEVLEYSREELGVLELGGGEPrifpVS 148

                ..
gi 15608851 352 AK 353
Cdd:cd09912 149 AK 150
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
29-192 1.29e-09

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 57.30  E-value: 1.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  29 VAVVGRPNVGKSTLVNRILGRREAVVQDIP--GVTRDRVCYDALWTGRRFVVQDTGGWEpnakgLQRLVAEQASVAMRTA 106
Cdd:COG1100   6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLStnGVTIDKKELKLDGLDVDLVIWDTPGQD-----EFRETRQFYARQLTGA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 107 DAVILVVDAGVGATAADEAA-ARILLRSGK--PVFLAANKVD------SEKGESDAAALWSLGLGEPHAISAMHGRGVAD 177
Cdd:COG1100  81 SLYLFVVDGTREETLQSLYElLESLRRLGKksPIILVLNKIDlydeeeIEDEERLKEALSEDNIVEVVATSAKTGEGVEE 160
                       170
                ....*....|....*
gi 15608851 178 LLDGVLAALPEVGES 192
Cdd:COG1100 161 LFAALAEILRGEGDS 175
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
28-180 3.69e-09

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: 55.53  E-value: 3.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851    28 VVAVVGRPNVGKSTLVNRILGRREaVVQDIPGVTRDR----VCYDalwtGRRFVVQDTGG-WEPNAKGLQRLVAEQAsVA 102
Cdd:pfam02421   2 TIALVGNPNVGKTTLFNALTGANQ-HVGNWPGVTVEKkegkFKYK----GYEIEIVDLPGiYSLSPYSEEERVARDY-LL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   103 MRTADAVILVVDAGVgataadeaaariLLRS----------GKPVFLAANKVD---SEKGESDAAALwSLGLGEP-HAIS 168
Cdd:pfam02421  76 NEKPDVIVNVVDATN------------LERNlyltlqllelGLPVVLALNMMDeaeKKGIKIDIKKL-SELLGVPvVPTS 142
                         170
                  ....*....|..
gi 15608851   169 AMHGRGVADLLD 180
Cdd:pfam02421 143 ARKGEGIDELLD 154
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
201-300 4.26e-09

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: 56.79  E-value: 4.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 201 RVALVGKPNVGKSSLLNKLAGDQrSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLRR--KVGQASGHEFYASVRThaa 278
Cdd:cd01896   2 RVALVGFPSVGKSTLLSKLTNTK-SEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEgaSDGKGRGRQVIAVART--- 77
                        90       100
                ....*....|....*....|..
gi 15608851 279 idsAEVAIVLIDASQPLTEQDL 300
Cdd:cd01896  78 ---ADLILIVLDATKPEGQREI 96
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
29-62 5.45e-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: 57.13  E-value: 5.45e-09
                          10        20        30
                  ....*....|....*....|....*....|....
gi 15608851    29 VAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTR 62
Cdd:TIGR03596 121 AMIVGIPNVGKSTLINRLAGKKVAKVGNRPGVTK 154
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
29-187 9.96e-09

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: 54.61  E-value: 9.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  29 VAVVGRPNVGKSTLVNRIL---------GRREAVVQDIPGVTRDR-----VCYDAL-WTGRRFVVQDTGGWEPNAKGLQR 93
Cdd:cd00881   2 VGVIGHVDHGKTTLTGSLLyqtgaidrrGTRKETFLDTLKEERERgitikTGVVEFeWPKRRINFIDTPGHEDFSKETVR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  94 lvaeqasvAMRTADAVILVVDAGVGATAADEAAARILLRSGKPVFLAANKVDSEkGESDAAAL---------------WS 158
Cdd:cd00881  82 --------GLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRV-GEEDFDEVlreikellkligftfLK 152
                       170       180
                ....*....|....*....|....*....
gi 15608851 159 LGLGEPHAISAMHGRGVADLLDGVLAALP 187
Cdd:cd00881 153 GKDVPIIPISALTGEGIEELLDAIVEHLP 181
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
201-376 1.16e-08

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 57.02  E-value: 1.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 201 RVALVGKPNVGKSSLLNKLAGDQrsvVHEAAG--TTVDPVDSLIELgGDVWRFV--DTAGLRRKVgqasGHEFYASVR-T 275
Cdd:COG2262 201 TVALVGYTNAGKSTLFNRLTGAD---VLAEDKlfATLDPTTRRLEL-PDGRPVLltDTVGFIRKL----PHQLVEAFRsT 272
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 276 HAAIDSAEVAIVLIDASQPLTEQDLRVISMVIE----AGRALVLAYNKWDLVDEDRRELLQReidrelvqvRWAQRVNIS 351
Cdd:COG2262 273 LEEVREADLLLHVVDASDPDFEEQIETVNEVLEelgaDDKPIILVFNKIDLLDDEELERLRA---------GYPDAVFIS 343
                       170       180
                ....*....|....*....|....*
gi 15608851 352 AKTGRAVHKLVPAMEDALASWDTRI 376
Cdd:COG2262 344 AKTGEGIDELLEAIEERLPEDRVEV 368
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
203-335 1.37e-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: 53.94  E-value: 1.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 203 ALVGKPNVGKSSLLNKLAgdqrSVVHEAA---GTTVDPVDSLIELG-GDVWRFVDTAGL--RRKVGQASGHEFYASVRTH 276
Cdd:cd01881   1 GLVGLPNVGKSTLLSALT----SAKVEIAsypFTTLEPNVGVFEFGdGVDIQIIDLPGLldGASEGRGLGEQILAHLYRS 76
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15608851 277 AAIdsaevaIVLIDASQ-----PLTEQDL--RVISMVIEAG--RALVLAYNKWDLVDED-----RRELLQREI 335
Cdd:cd01881  77 DLI------LHVIDASEdcvgdPLEDQKTlnEEVSGSFLFLknKPEMIVANKIDMASENnlkrlKLDKLKRGI 143
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
30-187 1.74e-08

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


Pssm-ID: 206667 [Multi-domain]  Cd Length: 159  Bit Score: 53.61  E-value: 1.74e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  30 AVVGRPNVGKSTLVNRILGRREAVVqDIPGVTRDRVCYDALWTGRRFVVQDTggwePNAKGLQRLVAEQAsVAMR----- 104
Cdd:cd01879   1 ALVGNPNVGKTTLFNALTGARQKVG-NWPGVTVEKKEGEFKLGGKEIEIVDL----PGTYSLTPYSEDEK-VARDfllge 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 105 TADAVILVVDAGvgataadeaaaRI---------LLRSGKPVFLAANKVD--SEKG-ESDAAALWSLgLGEP-HAISAMH 171
Cdd:cd01879  75 EPDLIVNVVDAT-----------NLernlyltlqLLELGLPVVVALNMIDeaEKRGiKIDLDKLSEL-LGVPvVPTSARK 142
                       170
                ....*....|....*.
gi 15608851 172 GRGVADLLDGVLAALP 187
Cdd:cd01879 143 GEGIDELLDAIAKLAE 158
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
202-310 1.83e-08

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 55.96  E-value: 1.83e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 202 VALVGKPNVGKSSLLNKLAGdQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLRRkvGQASG----HEFYASVRTha 277
Cdd:COG1163  66 VVLVGFPSVGKSTLLNKLTN-AKSEVGAYEFTTLDVVPGMLEYKGAKIQILDVPGLIE--GAASGkgrgKEVLSVVRN-- 140
                        90       100       110
                ....*....|....*....|....*....|...
gi 15608851 278 aidsAEVAIVLIDASQPltEQDLRVISMVIEAG 310
Cdd:COG1163 141 ----ADLILIVLDVFEL--EQYDVLKEELYDAG 167
Nog1 COG1084
GTP-binding protein, GTP1/Obg family [General function prediction only];
27-188 2.02e-08

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


Pssm-ID: 440701 [Multi-domain]  Cd Length: 330  Bit Score: 55.61  E-value: 2.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  27 PVVAVVGRPNVGKSTLVNRILGRR-EavVQDIP----GV-----TRDRvcydalwtgRRFVVQDTGGWepnakgLQRLVA 96
Cdd:COG1084 161 PTIVVAGYPNVGKSSLVSKVTSAKpE--IASYPfttkGIivghfERGH---------GRYQVIDTPGL------LDRPLS 223
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  97 E------QASVAMRT-ADAVILVVDA----GVGATAADEAAARILLRSGKPVFLAANKVDsekgESDAAALWSLGLGEPH 165
Cdd:COG1084 224 ErneierQAILALKHlADVILFLFDPsetcGYSLEEQLNLLEEIRSLFDVPVIVVINKID----LSDEEELKEAEEEADI 299
                       170       180
                ....*....|....*....|...
gi 15608851 166 AISAMHGRGVADLLDGVLAALPE 188
Cdd:COG1084 300 KISALTGEGVDELLDELIEALEE 322
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
29-180 2.49e-08

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: 53.28  E-value: 2.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  29 VAVVGRPNVGKSTLVNRILGR-REAVVQDIPGVTRDRVCYDaLWTGRRFVvqDTggwePN---AKGLQRLVAEQASV--- 101
Cdd:cd01876   2 VAFAGRSNVGKSSLINALTNRkKLARTSKTPGRTQLINFFN-VGDKFRLV--DL----PGygyAKVSKEVREKWGKLiee 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 102 --AMRTA-DAVILVVDAGVGATAADEAAARILLRSGKPVFLAANKVDSEKGeSDAAALWS-----LGLGEPH----AISA 169
Cdd:cd01876  75 ylENRENlKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKK-SELAKVLKkikeeLNLFNILppviLFSS 153
                       170
                ....*....|.
gi 15608851 170 MHGRGVADLLD 180
Cdd:cd01876 154 KKGTGIDELRA 164
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
104-256 3.21e-08

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


Pssm-ID: 206752 [Multi-domain]  Cd Length: 157  Bit Score: 52.71  E-value: 3.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 104 RTADAVILVVDAGVGATAADEAAARILLRSGKPVFLAANKVD-SEKGESDAAALWSLGLGEPHA-ISAMHGRGVADLLDG 181
Cdd:cd01859  10 KEADVVLEVVDARDPELTRSRKLERMALELGKKLIIVLNKADlVPREVLEKWKEVFESEGLPVVyVSARERLGTRILRRT 89
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15608851 182 VLAALPEvgesasasGGPRRVALVGKPNVGKSSLLNKLAGDQR---SVVHEAAGTTVDPvdSLIELGGDVWrFVDTAG 256
Cdd:cd01859  90 IKELAID--------GKPVIVGVVGYPKVGKSSIINALKGRHSastSPIPGSPGYTKGI--QLVRIDSKIY-LIDTPG 156
YeeP COG3596
Predicted GTPase [General function prediction only];
175-370 3.62e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 54.77  E-value: 3.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 175 VADLLDGVLAALPEVGESASASGGPRRVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIEL-GGDVWRFVD 253
Cdd:COG3596  15 LKRLPQVLRELLAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLESdGLPGLVLLD 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 254 TAGLrrkvgQASGHEFYASVRTHAAIDSAEVAIVLIDASQPLTEQDLRVISMVIE--AGRALVLAYNKWDLVDEDRRELL 331
Cdd:COG3596  95 TPGL-----GEVNERDREYRELRELLPEADLILWVVKADDRALATDEEFLQALRAqyPDPPVLVVLTQVDRLEPEREWDP 169
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15608851 332 QREIDRElvqvrwAQRVNISAKTGRAVHKLVPAMEDALA 370
Cdd:COG3596 170 PYNWPSP------PKEQNIRRALEAIAEQLGVPIDRVIP 202
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
200-371 4.41e-08

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: 52.91  E-value: 4.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   200 RRVALVGKPNVGKSSLLNKL-----AGDQRSVVHEAAGTTVDPVD-----------SLIELGGDVWRF--VDTAGlrrkv 261
Cdd:pfam00009   4 RNIGIIGHVDHGKTTLTDRLlyytgAISKRGEVKGEGEAGLDNLPeerergitiksAAVSFETKDYLInlIDTPG----- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   262 gqasgHE-FYASVRTHAAIdsAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLVDEDRRELLQREIDRELV 340
Cdd:pfam00009  79 -----HVdFVKEVIRGLAQ--ADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDGAELEEVVEEVSRELL 151
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 15608851   341 QVRWAQRVN-----ISAKTGRAVHKLVPAMEDALAS 371
Cdd:pfam00009 152 EKYGEDGEFvpvvpGSALKGEGVQTLLDALDEYLPS 187
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
88-234 1.92e-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: 50.60  E-value: 1.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  88 AKGLqRLVAEQASVAmrtaDAVILVVDAgvgataadeaaaRILLRS----------GKPVFLAANKVDseKGESDAAALW 157
Cdd:cd01856   7 AKAL-RQIKEKLKLV----DVVIEVRDA------------RIPLSSrnpdldkilgNKPRLIVLNKAD--LADPAKTKKW 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 158 -----SLGLgEPHAISAMHGRGVADLLDGVLAALPEVGESASASGGPR--RVALVGKPNVGKSSLLNKLAGDQRSVVHEA 230
Cdd:cd01856  68 lkyfkSQGE-PVLFVNAKNGKGVKKLLKKAKKLLKENEKLKAKGLLPRplRAMVVGIPNVGKSTLINRLRGKKVAKVGNK 146

                ....
gi 15608851 231 AGTT 234
Cdd:cd01856 147 PGVT 150
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
202-355 2.20e-07

ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other]


Pssm-ID: 274670 [Multi-domain]  Cd Length: 179  Bit Score: 50.94  E-value: 2.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   202 VALVGKPNVGKSSLLNKLAGdQRSVvheaA------GTTVdpvdsLI---ELGGDvWRFVDTAG---------LRRKVGQ 263
Cdd:TIGR03598  21 IAFAGRSNVGKSSLINALTN-RKKL----ArtsktpGRTQ-----LInffEVNDG-FRLVDLPGygyakvskeEKEKWQK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   264 ASGHefYASVRTH-AAIdsaevaIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLVDEDRRELLQREIDRELVQV 342
Cdd:TIGR03598  90 LIEE--YLEKRENlKGV------VLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKALKKD 161
                         170
                  ....*....|....
gi 15608851   343 RWAQRV-NISAKTG 355
Cdd:TIGR03598 162 ADDPSVqLFSSLKK 175
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
25-186 2.84e-07

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 52.81  E-value: 2.84e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  25 AAPVVAVVGRPNVGKSTLVNRILGRREAVVqDIPGVTRDR----VCYDalwtGRRFVVQDTggweP-----NAKGLQRLV 95
Cdd:COG0370   2 KMITIALVGNPNVGKTTLFNALTGSRQKVG-NWPGVTVEKkegkFKLK----GKEIELVDL----PgtyslSAYSPDEKV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  96 AEQAsVAMRTADAVILVVDAgvgataadeaaARI---------LLRSGKPVFLAANKVD--SEKGES-DAAALwSLGLGE 163
Cdd:COG0370  73 ARDF-LLEEKPDVVVNVVDA-----------TNLernlyltlqLLELGIPVVLALNMMDeaEKKGIKiDVEKL-SKLLGV 139
                       170       180
                ....*....|....*....|....
gi 15608851 164 P-HAISAMHGRGVADLLDGVLAAL 186
Cdd:COG0370 140 PvVPTSARKGKGIDELKEAIIEAA 163
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
202-369 4.10e-07

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: 49.73  E-value: 4.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 202 VALVGKPNVGKSSLLNKLAgdqrsvvheAAG--------TTVDPVdslieLG------GDVWRFVDTAGLrrkVGQAS-- 265
Cdd:cd01898   3 VGLVGLPNAGKSTLLSAIS---------NAKpkiadypfTTLVPN-----LGvvrvddGRSFVIADIPGL---IEGASeg 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 266 ---GHEFYASV-RTHaaidsaeVAIVLIDASQPLT-EQDLRVISMVIE------AGRALVLAYNKWDLVDEDRREllqrE 334
Cdd:cd01898  66 kglGHRFLRHIeRTR-------VLLHVIDLSGEDDpVEDYETIRNELEaynpglAEKPRIVVLNKIDLLDAEERF----E 134
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15608851 335 IDRELVQVRWAQRVN-ISAKTGRAVHKLVPAMEDAL 369
Cdd:cd01898 135 KLKELLKELKGKKVFpISALTGEGLDELLKKLAKLL 170
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
29-84 4.60e-07

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: 49.31  E-value: 4.60e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15608851  29 VAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVcyDALWTGRRFVVqDTGGW 84
Cdd:cd01849  94 VGVVGLPNVGKSSFINALLNKFKLKVGSIPGTTKLQQ--DVKLDKEIYLY-DTPGI 146
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
131-257 1.20e-06

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


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 48.80  E-value: 1.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 131 LRSGKPVFLAANKVD------SE-------KGESDAAALWSLGLgepHAISAMHGRGVADLLDgvlaalpevgESASASG 197
Cdd:cd01855  57 LIGAKPVILVGNKIDllpkdvKPnrlkqwvKKRLKIGGLKIKDV---ILVSAKKGWGVEELIE----------EIKKLAK 123
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15608851 198 GPRRVALVGKPNVGKSSLLNKLAGDQRSVVHEAA-----------GTTVDPVDslIELGGDVWRFvDTAGL 257
Cdd:cd01855 124 YRGDVYVVGATNVGKSTLINALLKSNGGKVQAQAlvqrltvspipGTTLGLIK--IPLGEGKKLY-DTPGI 191
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
27-186 1.52e-06

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


Pssm-ID: 206666 [Multi-domain]  Cd Length: 204  Bit Score: 48.61  E-value: 1.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  27 PVVAVVGRPNVGKSTLVNRILGRrEAVVQDIPGVTRD----RVCydaLWTGRRFVVQDTGGWepnAKGLQR-LVA----- 96
Cdd:cd01878  42 PTVALVGYTNAGKSTLFNALTGA-DVLAEDQLFATLDpttrRIK---LPGGREVLLTDTVGF---IRDLPHqLVEafrst 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  97 -EQAsvamRTADAVILVVDAGVGATAADEAAARILLR----SGKPVFLAANKVDSEKGESDAAALwSLGLGEPHAISAMH 171
Cdd:cd01878 115 lEEV----AEADLLLHVVDASDPDREEQIETVEEVLKelgaDDIPIILVLNKIDLLDDEELEERL-RAGRPDAVFISAKT 189
                       170
                ....*....|....*
gi 15608851 172 GRGVADLLDGVLAAL 186
Cdd:cd01878 190 GEGLDLLKEAIEELL 204
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
29-187 1.53e-06

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


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 48.29  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851    29 VAVVGRPNVGKSTLVNRIL------GRREAVVQDIPGVT------RDR-----VCYDAL-WTGRRFVVQDTGGWEPnakg 90
Cdd:pfam00009   6 IGIIGHVDHGKTTLTDRLLyytgaiSKRGEVKGEGEAGLdnlpeeRERgitikSAAVSFeTKDYLINLIDTPGHVD---- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851    91 lqrLVAEqASVAMRTADAVILVVDAGVGATAADEAAARILLRSGKPVFLAANKVD----SEKGESDAAALWSLGLGEPH- 165
Cdd:pfam00009  82 ---FVKE-VIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDrvdgAELEEVVEEVSRELLEKYGEd 157
                         170       180
                  ....*....|....*....|....*....
gi 15608851   166 -------AISAMHGRGVADLLDGVLAALP 187
Cdd:pfam00009 158 gefvpvvPGSALKGEGVQTLLDALDEYLP 186
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
33-236 2.06e-06

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: 50.12  E-value: 2.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851    33 GRPNVGKSTLVNRILGRReAVVQDIPGVTRDRVCYDALWTGRRFVVQDTGG-WEPNAKGLQRLVAeQASVAMRTADAVIL 111
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGAN-QTVGNWPGVTVEKKEGKLGFQGEDIEIVDLPGiYSLTTFSLEEEVA-RDYLLNEKPDLVVN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   112 VVDAGVGATAADEAAAriLLRSGKPVFLAANKVDSEKGES---DAAALWSLgLGEP-HAISAMHGRGVADLLDGVLAALP 187
Cdd:TIGR00437  79 VVDASNLERNLYLTLQ--LLELGIPMILALNLVDEAEKKGiriDEEKLEER-LGVPvVPTSATEGRGIERLKDAIRKAIG 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15608851   188 EVGESASA----SGGPRRVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVD 236
Cdd:TIGR00437 156 LKELKKRAieivPEAYQVVEVVEGLIEIIYSISKRGLEILLGLLEDLSLEIEK 208
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
23-115 4.27e-06

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


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 48.64  E-value: 4.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  23 SGAAPVVaVVGRPNVGKSTLVNRILGRREAV-------VQDIPGVTRDRvcydalwtGRRFVVQDTGGWEPNA---KGLQ 92
Cdd:COG1163  61 SGDATVV-LVGFPSVGKSTLLNKLTNAKSEVgayefttLDVVPGMLEYK--------GAKIQILDVPGLIEGAasgKGRG 131
                        90       100
                ....*....|....*....|...
gi 15608851  93 RLVaeqASVAmRTADAVILVVDA 115
Cdd:COG1163 132 KEV---LSVV-RNADLILIVLDV 150
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
201-355 8.05e-06

Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible.


Pssm-ID: 206640 [Multi-domain]  Cd Length: 159  Bit Score: 45.91  E-value: 8.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 201 RVALVGKPNVGKSSLLNKLAGDQRSVVHEAagtTVDpVDSL---IELGGD-----VWrfvDTAglrrkvgqasGHEFYAS 272
Cdd:cd00154   2 KIVLIGDSGVGKTSLLLRFVDNKFSENYKS---TIG-VDFKsktIEVDGKkvklqIW---DTA----------GQERFRS 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 273 V-----RthaaidSAEVAIVLIDASQPLTEQDLRV-ISMVIEAGR---ALVLAYNKWDLVDedrrellQREIDRELVQvR 343
Cdd:cd00154  65 ItssyyR------GAHGAILVYDVTNRESFENLDKwLNELKEYAPpniPIILVGNKSDLED-------ERQVSTEEAQ-Q 130
                       170
                ....*....|....*..
gi 15608851 344 WAQRVNI-----SAKTG 355
Cdd:cd00154 131 FAKENGLlffetSAKTG 147
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
202-372 1.25e-05

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: 45.83  E-value: 1.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 202 VALVGKPNVGKSSLLNKLAGdQRSVVHeaagttvdpVDS------LI---ELGGDvWRFVDTAG---------LRRKVGQ 263
Cdd:COG0218  26 IAFAGRSNVGKSSLINALTN-RKKLAR---------TSKtpgktqLInffLINDK-FYLVDLPGygyakvskaEKEKWQK 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 264 ASGHefYASVR-THAAIdsaevaIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLVDEDRRELLQREIdRELVQV 342
Cdd:COG0218  95 LIED--YLEGReNLKGV------VLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAI-KKALGK 165
                       170       180       190
                ....*....|....*....|....*....|..
gi 15608851 343 RWAQR--VNISAKTGRAVHKLvpamEDALASW 372
Cdd:COG0218 166 DPAAPevILFSSLKKEGIDEL----RAAIEEW 193
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
30-186 1.68e-05

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: 45.08  E-value: 1.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  30 AVVGRPNVGKSTLVNrILGRREAVVQDIPGVTRDR---VCYDAlwTGRRFVVQDTGGWEPNA-KGlqRLVAEQASVAMRT 105
Cdd:cd01881   1 GLVGLPNVGKSTLLS-ALTSAKVEIASYPFTTLEPnvgVFEFG--DGVDIQIIDLPGLLDGAsEG--RGLGEQILAHLYR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 106 ADAVILVVDA---GVG------ATAADEAAARILLRSGKPVFLAANKVDSekgeSDAAALWSLGLGE------PHAISAM 170
Cdd:cd01881  76 SDLILHVIDAsedCVGdpledqKTLNEEVSGSFLFLKNKPEMIVANKIDM----ASENNLKRLKLDKlkrgipVVPTSAL 151
                       170
                ....*....|....*.
gi 15608851 171 HGRGVADLLDGVLAAL 186
Cdd:cd01881 152 TRLGLDRVIRTIRKLL 167
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
28-62 1.93e-05

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


Pssm-ID: 206753 [Multi-domain]  Cd Length: 171  Bit Score: 44.87  E-value: 1.93e-05
                        10        20        30
                ....*....|....*....|....*....|....*
gi 15608851  28 VVAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTR 62
Cdd:cd04178 118 TVGVVGYPNVGKSSVINSLKRSRACNVGATPGVTK 152
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
201-360 4.35e-05

Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.


Pssm-ID: 425451 [Multi-domain]  Cd Length: 162  Bit Score: 43.66  E-value: 4.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   201 RVALVGKPNVGKSSLLNKLAGDQRSVVHEAagtTVDpVDSL---IELGG-----DVWrfvDTAGLRRkvgqasghefYAS 272
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLIRFTQNKFPEEYIP---TIG-VDFYtktIEVDGktvklQIW---DTAGQER----------FRA 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   273 VRThAAIDSAEVAIVLIDASQPLTEQDLRV----ISMVIEAGRALVLAYNKWDLVDedrrellQREIDRELVQvRWAQRV 348
Cdd:pfam00071  64 LRP-LYYRGADGFLLVYDITSRDSFENVKKwveeILRHADENVPIVLVGNKCDLED-------QRVVSTEEGE-ALAKEL 134
                         170
                  ....*....|....*..
gi 15608851   349 NI-----SAKTGRAVHK 360
Cdd:pfam00071 135 GLpfmetSAKTNENVEE 151
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
200-361 6.25e-05

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: 43.32  E-value: 6.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 200 RRVALVGKPNVGKSSLLNKLagdqrsvvheaagTTVDP--------VDSL----IELGGDVWRFVDTAG-LRRKVGQASG 266
Cdd:cd01897   1 RTLVIAGYPNVGKSSLVNKL-------------TRAKPevapypftTKSLfvghFDYKYLRWQVIDTPGiLDRPLEERNT 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 267 HEFYA-SVRTHAAidsaevAIVL--IDASQ----PLTEQDLRVISMVIEAGRALVLAYNKWDLVDEDRRELLQREIDREL 339
Cdd:cd01897  68 IEMQAiTALAHLR------AAVLffIDPSEtcgySIEEQLSLFKEIKPLFNKPVIVVLNKIDLLTEEDLSEIEKELEKEG 141
                       170       180
                ....*....|....*....|..
gi 15608851 340 VQVrwaqrVNISAKTGRAVHKL 361
Cdd:cd01897 142 EEV-----IKISTLTEEGVDEL 158
obgE PRK12297
GTPase CgtA; Reviewed
202-371 7.71e-05

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 44.71  E-value: 7.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  202 VALVGKPNVGKSSLLNKLAgdqrsvvheAAG--------TTVDPVDSLIELGGDVwRFV--DTAGLrrkVGQAS-----G 266
Cdd:PRK12297 161 VGLVGFPNVGKSTLLSVVS---------NAKpkianyhfTTLVPNLGVVETDDGR-SFVmaDIPGL---IEGASegvglG 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  267 HEFYASV-RTHaaidsaeVAIVLIDAS-----QPLteQDLRVI-------SMVIEAGRALVLAyNKWDLVD-EDRRELLQ 332
Cdd:PRK12297 228 HQFLRHIeRTR-------VIVHVIDMSgsegrDPI--EDYEKInkelklyNPRLLERPQIVVA-NKMDLPEaEENLEEFK 297
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 15608851  333 REIDRELVQvrwaqrvnISAKTGRAVHKLVPAMEDALAS 371
Cdd:PRK12297 298 EKLGPKVFP--------ISALTGQGLDELLYAVAELLEE 328
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
201-327 8.24e-05

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: 43.71  E-value: 8.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 201 RVALVGKPNVGKSSLLNKLAGD------------QRSVVHEAAGTTVDP---VDSL-------IELggDV-WRFVDTAgl 257
Cdd:cd04166   1 RFITCGSVDDGKSTLIGRLLYDsksifedqlaalERSKSSGTQGEKLDLallVDGLqaereqgITI--DVaYRYFSTP-- 76
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15608851 258 RRK--VGQASGHEFYasVR---THAAidSAEVAIVLIDASQPLTEQDLR---VISMV-IeagRALVLAYNKWDLVDEDR 327
Cdd:cd04166  77 KRKfiIADTPGHEQY--TRnmvTGAS--TADLAILLVDARKGVLEQTRRhsyIASLLgI---RHVVVAVNKMDLVDYDE 148
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
31-63 1.09e-04

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


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 43.02  E-value: 1.09e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 15608851  31 VVGRPNVGKSTLVNRILGR-----------REAVVQDIPGVTRD 63
Cdd:cd01855 130 VVGATNVGKSTLINALLKSnggkvqaqalvQRLTVSPIPGTTLG 173
infB CHL00189
translation initiation factor 2; Provisional
26-183 1.29e-04

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 44.44  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   26 APVVAVVGRPNVGKSTLVNRIlgRREAVVQ-DIPGVTRDRVCYDALW----TGRRFVVQDTGGWEpnakglqrlvaeqAS 100
Cdd:CHL00189 244 PPIVTILGHVDHGKTTLLDKI--RKTQIAQkEAGGITQKIGAYEVEFeykdENQKIVFLDTPGHE-------------AF 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  101 VAMRT-----ADAVILVVDAGVGATAADEAAARILLRSGKPVFLAANKVDS-----EKGESDAAA--LWSLGLGEPH--- 165
Cdd:CHL00189 309 SSMRSrganvTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKanantERIKQQLAKynLIPEKWGGDTpmi 388
                        170
                 ....*....|....*...
gi 15608851  166 AISAMHGRGVADLLDGVL 183
Cdd:CHL00189 389 PISASQGTNIDKLLETIL 406
YeeP COG3596
Predicted GTPase [General function prediction only];
19-145 1.53e-04

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 43.60  E-value: 1.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  19 EIAESGAAPVVAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDalW---TGRRFVVQDTGGWEPNAKGLQRlv 95
Cdd:COG3596  32 RLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYR--LesdGLPGLVLLDTPGLGEVNERDRE-- 107
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15608851  96 AEQASVAMRTADAVILVVDAGVGATAADEAAARILLR--SGKPVFLAANKVD 145
Cdd:COG3596 108 YRELRELLPEADLILWVVKADDRALATDEEFLQALRAqyPDPPVLVVLTQVD 159
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
27-50 1.55e-04

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: 42.75  E-value: 1.55e-04
                        10        20
                ....*....|....*....|....
gi 15608851  27 PVVAVVGRPNVGKSTLVNRILGRR 50
Cdd:COG0218  24 PEIAFAGRSNVGKSSLINALTNRK 47
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
19-62 1.76e-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: 41.92  E-value: 1.76e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 15608851  19 EIAESGAAPVVAVVGRPNVGKSTLVNRILGRREAV---VQDIPGVTR 62
Cdd:cd01859  92 ELAIDGKPVIVGVVGYPKVGKSSIINALKGRHSAStspIPGSPGYTK 138
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
211-327 1.78e-04

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 44.15  E-value: 1.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  211 GKSSLLNKLAGDQRSVV--HEAA--------GTTVDPVDSLIELGG-----------DV-WRFVDTAglRRK--VGQASG 266
Cdd:PRK05506  36 GKSTLIGRLLYDSKMIFedQLAAlerdskkvGTQGDEIDLALLVDGlaaereqgitiDVaYRYFATP--KRKfiVADTPG 113
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15608851  267 HEFYA-SVRTHAAidSAEVAIVLIDASQPLTEQDLRVISMVIEAG-RALVLAYNKWDLVDEDR 327
Cdd:PRK05506 114 HEQYTrNMVTGAS--TADLAIILVDARKGVLTQTRRHSFIASLLGiRHVVLAVNKMDLVDYDQ 174
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
27-180 1.83e-04

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: 42.16  E-value: 1.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  27 PVVAVVGRPNVGKSTLVNrILGRREAVVQDIPGVTR-------DRVCYdalwtgrRFVVQDTGGWepnakgLQRLVAE-- 97
Cdd:cd01897   1 RTLVIAGYPNVGKSSLVN-KLTRAKPEVAPYPFTTKslfvghfDYKYL-------RWQVIDTPGI------LDRPLEErn 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  98 ----QASVAMR-TADAVILVVDA----GVGATAADEAAARILLRSGKPVFLAANKVD--SEKGESDAAALWSLGLGEPHA 166
Cdd:cd01897  67 tiemQAITALAhLRAAVLFFIDPsetcGYSIEEQLSLFKEIKPLFNKPVIVVLNKIDllTEEDLSEIEKELEKEGEEVIK 146
                       170
                ....*....|....
gi 15608851 167 ISAMHGRGVADLLD 180
Cdd:cd01897 147 ISTLTEEGVDELKN 160
PRK04213 PRK04213
GTP-binding protein EngB;
27-77 2.47e-04

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 42.21  E-value: 2.47e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15608851   27 PVVAVVGRPNVGKSTLVNRILGRREAVVQDiPGVTRDRVCYDalWTGRRFV 77
Cdd:PRK04213  10 PEIVFVGRSNVGKSTLVRELTGKKVRVGKR-PGVTRKPNHYD--WGDFILT 57
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
202-234 2.85e-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: 41.06  E-value: 2.85e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 15608851 202 VALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTT 234
Cdd:cd01857  85 IGLVGYPNVGKSSLINALVGSKKVSVSSTPGKT 117
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
203-369 3.84e-04

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


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 40.40  E-value: 3.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 203 ALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGlrrkVGQASGHEFYASVRTHAAIDSA 282
Cdd:cd11383   1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPG----VGERGRRDREYEELYRRLLPEA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 283 EVAIVLIDAsqplteQDlrvismvieagRALVlaynkwdlVDEDRRELLQREIDRELV----QVRwaQRVNISAKTGRAV 358
Cdd:cd11383  77 DLVLWLLDA------DD-----------RALA--------ADHDFYLLPLAGHDAPLLfvlnQVD--PVLAVSARTGWGL 129
                       170
                ....*....|.
gi 15608851 359 HKLVPAMEDAL 369
Cdd:cd11383 130 DELAEALITAL 140
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
25-62 5.06e-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: 5.06e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 15608851  25 AAPVVAVVGRPNVGKSTLVNRILGRREAVVQDIPGVTR 62
Cdd:cd01857  81 NEATIGLVGYPNVGKSSLINALVGSKKVSVSSTPGKTK 118
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
107-239 1.00e-03

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


Pssm-ID: 206746 [Multi-domain]  Cd Length: 146  Bit Score: 39.29  E-value: 1.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 107 DAVILVVDAgvgataadeaaaRILLRS------------GKPVFLAANK---VDSEKGESDAAALWSLGLGEPHAISAMH 171
Cdd:cd01849   1 DVVVEVVDA------------RDPLSSrnpdievlinekNKKLIMVLNKadlVPKEVLRKWVAELSELYGTKTFFISATN 68
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15608851 172 GRGVADLldgvlAALPEVGESASASGGPRRVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVD 239
Cdd:cd01849  69 GQGILKL-----KAEITKQKLKLKYKKGIRVGVVGLPNVGKSSFINALLNKFKLKVGSIPGTTKLQQD 131
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
27-189 1.09e-03

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: 39.76  E-value: 1.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  27 PVVAVVGRPNVGKSTLVNRIlgRREAVVQDIPG----------VTRDRvcydalwTGRRFVVQDTGGWEpnakglqrlva 96
Cdd:cd01887   1 PVVTVMGHVDHGKTTLLDKI--RKTNVAAGEAGgitqhigayqVPIDV-------KIPGITFIDTPGHE----------- 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  97 eqASVAMRT-----ADAVILVVDAGVGATAADEAAARILLRSGKPVFLAANKVD--------SEKGESDAAALwsLGLGE 163
Cdd:cd01887  61 --AFTNMRArgasvTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDkpygteadPERVKNELSEL--GLVGE 136
                       170       180       190
                ....*....|....*....|....*....|...
gi 15608851 164 PHA-------ISAMHGRGVADLLDgVLAALPEV 189
Cdd:cd01887 137 EWGgdvsivpISAKTGEGIDDLLE-AILLLAEV 168
RGK cd04148
Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras GTPases; RGK subfamily. The RGK (Rem, Rem2, Rad, ...
201-361 1.18e-03

Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras GTPases; RGK subfamily. The RGK (Rem, Rem2, Rad, Gem/Kir) subfamily of Ras GTPases are expressed in a tissue-specific manner and are dynamically regulated by transcriptional and posttranscriptional mechanisms in response to environmental cues. RGK proteins bind to the beta subunit of L-type calcium channels, causing functional down-regulation of these voltage-dependent calcium channels, and either termination of calcium-dependent secretion or modulation of electrical conduction and contractile function. Inhibition of L-type calcium channels by Rem2 may provide a mechanism for modulating calcium-triggered exocytosis in hormone-secreting cells, and has been proposed to influence the secretion of insulin in pancreatic beta cells. RGK proteins also interact with and inhibit the Rho/Rho kinase pathway to modulate remodeling of the cytoskeleton. Two characteristics of RGK proteins cited in the literature are N-terminal and C-terminal extensions beyond the GTPase domain typical of Ras superfamily members. The N-terminal extension is not conserved among family members; the C-terminal extension is reported to be conserved among the family and lack the CaaX prenylation motif typical of membrane-associated Ras proteins. However, a putative CaaX motif has been identified in the alignment of the C-terminal residues of this CD.


Pssm-ID: 206715 [Multi-domain]  Cd Length: 219  Bit Score: 40.47  E-value: 1.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 201 RVALVGKPNVGKSSLLNKL-AGDQRSVVHEAAGT-------TVDPVDSLIELgGDVWRFVDTAGLRRKVGQaSGHEFYA- 271
Cdd:cd04148   2 RVVLLGDSGVGKSSLANIFtAGVYEDSAYEASGDdtyertvSVDGEEATLVV-YDHWEQEDGMWLEDSCMQ-VGDAYVIv 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 272 -SVRTHAAIDSAEVAIVLIDASQPLteQDLRVIsmvieagralvLAYNKWDLVdedRRELLQREIDRELVQVRWAQRVNI 350
Cdd:cd04148  80 ySVTDRSSFEKASELRIQLRRARQA--EDIPII-----------LVGNKSDLV---RSREVSVQEGRACAVVFDCKFIET 143
                       170
                ....*....|.
gi 15608851 351 SAKTGRAVHKL 361
Cdd:cd04148 144 SAALQHNVDEL 154
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
201-321 1.79e-03

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.


Pssm-ID: 462490 [Multi-domain]  Cd Length: 114  Bit Score: 37.87  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851   201 RVALVGKPNVGKSSLLNKLAGDQRSVVHEA-------AGTTVDPVDSLIELGGDVWrfvDTAglrrkvgqasGHEFYASV 273
Cdd:pfam08477   1 KVVLLGDSGVGKTSLLKRFVDDTFDPKYKStigvdfkTKTVLENDDNGKKIKLNIW---DTA----------GQERFRSL 67
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15608851   274 RTHAAIDSAeVAIVLIDASqplTEQDLR--VISMVIEAGRA-LVLAYNKWD 321
Cdd:pfam08477  68 HPFYYRGAA-AALLVYDSR---TFSNLKywLRELKKYAGNSpVILVGNKID 114
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
133-258 1.80e-03

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


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 39.69  E-value: 1.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 133 SGKPVFLAANKVD---SEKGESDAAALWSLGLgEPHAISAMHGRGVADLLDgVLAalpevgesasasggPRRVALVGKPN 209
Cdd:cd01854  32 SGIEPVIVLNKADlvdDEELEELLEIYEKLGY-PVLAVSAKTGEGLDELRE-LLK--------------GKTSVLVGQSG 95
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15608851 210 VGKSSLLNKLAGDQR---SVVHEAAG------TTVdpvdSLIELGGDVWrFVDTAGLR 258
Cdd:cd01854  96 VGKSTLLNALLPELVlatGEISEKLGrgrhttTHR----ELFPLPGGGL-IIDTPGFR 148
infB CHL00189
translation initiation factor 2; Provisional
202-362 2.04e-03

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 40.59  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  202 VALVGKPNVGKSSLLNKLAGDQrSVVHEAAGTT--VDPVDSLIELGGDVWR--FVDTaglrrkvgqaSGHEFYASVRTHA 277
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKIRKTQ-IAQKEAGGITqkIGAYEVEFEYKDENQKivFLDT----------PGHEAFSSMRSRG 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  278 AiDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLVDEDRRELLQREIDRELVQVRWA---QRVNISAKT 354
Cdd:CHL00189 316 A-NVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQLAKYNLIPEKWGgdtPMIPISASQ 394

                 ....*...
gi 15608851  355 GRAVHKLV 362
Cdd:CHL00189 395 GTNIDKLL 402
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
31-116 3.19e-03

AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 38.74  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851    31 VVGRPNVGKSTLVNRILGRReAVVQDIPGVTRDRVC--YDALWTGRRFVVQDTGG---WEPNAKGLQRLVAEQASVAMRT 105
Cdd:pfam04548   5 LVGKTGNGKSATGNSILGRK-AFESKLRAQGVTKTCqlVSRTWDGRIINVIDTPGlfdLSVSNDFISKEIIRCLLLAEPG 83
                          90
                  ....*....|.
gi 15608851   106 ADAVILVVDAG 116
Cdd:pfam04548  84 PHAVLLVLSLG 94
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
311-380 3.68e-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: 3.68e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15608851 311 RALVLAYNKWDLVDEDRRELLQREIDRELVQVRWAQ--RVNISAKTGRAVHKLVPAMEDALASWDTRIATGP 380
Cdd:COG3276 105 KRGIVVLTKADLVDEEWLELVEEEIRELLAGTFLEDapIVPVSAVTGEGIDELRAALDALAAAVPARDADGP 176
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
278-364 5.99e-03

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: 37.51  E-value: 5.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851 278 AIDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLVDEDRRELLQrEIDrELVQVRWAQRVNISAKTGRA 357
Cdd:cd01890  87 SLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQ-EIE-DVLGLDASEAILVSAKTGLG 164

                ....*..
gi 15608851 358 VHKLVPA 364
Cdd:cd01890 165 VEDLLEA 171
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
279-353 7.10e-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: 37.30  E-value: 7.10e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15608851 279 IDSAEVAIVLIDASQPLTEQDLRVISMVIEAGRALVLAYNKWDLVDEDRRELLQREIDRELVQVrwaqrVNISAK 353
Cdd:cd01859   9 IKEADVVLEVVDARDPELTRSRKLERMALELGKKLIIVLNKADLVPREVLEKWKEVFESEGLPV-----VYVSAR 78
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
30-115 8.14e-03

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: 36.55  E-value: 8.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608851  30 AVVGRPNVGKSTLVNRILGRREAVVQDIPGVTRDRVCYDALWTGRRFVVQDTGGWEPNAKGlQRLVAEQASVAMRTADAV 109
Cdd:cd11383   1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPGVGERGRR-DREYEELYRRLLPEADLV 79

                ....*.
gi 15608851 110 ILVVDA 115
Cdd:cd11383  80 LWLLDA 85
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
201-263 9.11e-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: 37.68  E-value: 9.11e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15608851 201 RVALVGKPNVGKSSLLNKLAGDQRSVVHEAAGTTVDPVDSLIELGGDVWRFVDTAGLRRKVGQ 263
Cdd:cd01853  33 TILVLGKTGVGKSSTINSIFGERKVSVSAFQSETLRPREVSRTVDGFKLNIIDTPGLLESQDQ 95
 
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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