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Conserved domains on  [gi|1958661173|ref|XP_038942880|]
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septin-9 isoform X3 [Rattus norvegicus]

Protein Classification

septin family protein( domain architecture ID 10110922)

septin family protein, a filament-forming cytoskeletal GTPase, is involved in various cellular processes, including cytoskeleton organization, cytokinesis, and membrane dynamics

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
190-464 5.48e-172

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


:

Pssm-ID: 206649  Cd Length: 275  Bit Score: 484.36  E-value: 5.48e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 190 QGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPISEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNEN 269
Cdd:cd01850     1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 270 CWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEER 349
Cdd:cd01850    81 CWKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 350 VYFKQRITSDLLSNGIDVYPQKEFDEDAEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 429
Cdd:cd01850   161 TEFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958661173 430 YLRDLLIRTHMQNIKDITSNIHFEAYRVKRLNEGN 464
Cdd:cd01850   241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
12-169 1.41e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173   12 SSKQVESTASTPGPSRFGLKRAEVLGHKTPEPV---PRRTEITIVKPQESGLrrveTPASKAPEGSAMPVTDAAPKRvei 88
Cdd:PHA03307    44 VSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGteaPANESRSTPTWSLSTL----APASPAREGSPTPPGPSSPDP--- 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173   89 qvPKPAEAPNCPLPPqtlenseaPMSQLQSRLEPRPPVTEVPYRNQEDSEVAPSCVGDMADNPRDAMLKQAPVSRNEKAP 168
Cdd:PHA03307   117 --PPPTPPPASPPPS--------PAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAP 186

                   .
gi 1958661173  169 V 169
Cdd:PHA03307   187 S 187
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
190-464 5.48e-172

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


Pssm-ID: 206649  Cd Length: 275  Bit Score: 484.36  E-value: 5.48e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 190 QGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPISEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNEN 269
Cdd:cd01850     1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 270 CWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEER 349
Cdd:cd01850    81 CWKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 350 VYFKQRITSDLLSNGIDVYPQKEFDEDAEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 429
Cdd:cd01850   161 TEFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958661173 430 YLRDLLIRTHMQNIKDITSNIHFEAYRVKRLNEGN 464
Cdd:cd01850   241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
191-460 2.86e-136

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


Pssm-ID: 395596  Cd Length: 272  Bit Score: 393.59  E-value: 2.86e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 191 GFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPISEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNENC 270
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 271 WQPIMKFINDQYEKYLQEEVNINRKKRIpDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEERV 350
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIK-DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 351 YFKQRITSDLLSNGIDVYPQKEFDED-AEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 429
Cdd:pfam00735 160 RFKKRIREEIERQNIPIYHFPDEESDeDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958661173 430 YLRDLLIRTHMQNIKDITSNIHFEAYRVKRL 460
Cdd:pfam00735 240 KLRNMLIRTHLQDLKEVTHELHYETYRSEKL 270
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
172-477 1.28e-126

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 372.81  E-value: 1.28e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 172 GYVGIDSILEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLFKSKISR-KSVQPISEERIPKTIEIKSITHDIEEKGVR 250
Cdd:COG5019     2 GYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDeTEIDDIRAEGTSPTLEIKITKAELEEDGFH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 251 MKLTVIDTPGFGDHINNENCWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSK 330
Cdd:COG5019    82 LNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 331 VVNIVPVIAKADTLTLEERVYFKQRITSDLLSNGIDVYpqKEFD-EDAEDRLVNE--KFREMIPFAVVGSDHEYQVNGKR 407
Cdd:COG5019   162 RVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVF--DPYDpEDDEDESLEEnqDLRSLIPFAIIGSNTEIENGGEQ 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 408 ILGRKTKWGTIEVENTTHCEFAYLRDLLIRTHMQNIKDITSNIHFEAYRVKRLNEGNSAMANGIEKEPET 477
Cdd:COG5019   240 VRGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSGLKNSGEPSLKEIHEA 309
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
193-260 3.90e-06

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: 46.98  E-value: 3.90e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958661173 193 EFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPiseeripkTIEIKSITHDIEEKGVRMKLTVIDTPG 260
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYP--------GTTRNYVTTVIEEDGKTYKFNLLDTAG 60
PRK00098 PRK00098
GTPase RsgA; Reviewed
178-268 7.21e-04

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 41.34  E-value: 7.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 178 SILEQMRRKAMKQGFEFNI-MVVGQSGLGKSTLINTLfkskisrksvqpISEERIpKTIEI-------KSIT-----HDI 244
Cdd:PRK00098  148 SAKEGEGLDELKPLLAGKVtVLAGQSGVGKSTLLNAL------------APDLEL-KTGEIsealgrgKHTTthvelYDL 214
                          90       100
                  ....*....|....*....|....*...
gi 1958661173 245 EEKGvrmklTVIDTPGFG----DHINNE 268
Cdd:PRK00098  215 PGGG-----LLIDTPGFSsfglHDLEAE 237
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
12-169 1.41e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173   12 SSKQVESTASTPGPSRFGLKRAEVLGHKTPEPV---PRRTEITIVKPQESGLrrveTPASKAPEGSAMPVTDAAPKRvei 88
Cdd:PHA03307    44 VSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGteaPANESRSTPTWSLSTL----APASPAREGSPTPPGPSSPDP--- 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173   89 qvPKPAEAPNCPLPPqtlenseaPMSQLQSRLEPRPPVTEVPYRNQEDSEVAPSCVGDMADNPRDAMLKQAPVSRNEKAP 168
Cdd:PHA03307   117 --PPPTPPPASPPPS--------PAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAP 186

                   .
gi 1958661173  169 V 169
Cdd:PHA03307   187 S 187
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
190-464 5.48e-172

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


Pssm-ID: 206649  Cd Length: 275  Bit Score: 484.36  E-value: 5.48e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 190 QGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPISEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNEN 269
Cdd:cd01850     1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 270 CWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEER 349
Cdd:cd01850    81 CWKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 350 VYFKQRITSDLLSNGIDVYPQKEFDEDAEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 429
Cdd:cd01850   161 TEFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958661173 430 YLRDLLIRTHMQNIKDITSNIHFEAYRVKRLNEGN 464
Cdd:cd01850   241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
191-460 2.86e-136

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


Pssm-ID: 395596  Cd Length: 272  Bit Score: 393.59  E-value: 2.86e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 191 GFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPISEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNENC 270
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 271 WQPIMKFINDQYEKYLQEEVNINRKKRIpDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEERV 350
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIK-DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 351 YFKQRITSDLLSNGIDVYPQKEFDED-AEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 429
Cdd:pfam00735 160 RFKKRIREEIERQNIPIYHFPDEESDeDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958661173 430 YLRDLLIRTHMQNIKDITSNIHFEAYRVKRL 460
Cdd:pfam00735 240 KLRNMLIRTHLQDLKEVTHELHYETYRSEKL 270
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
172-477 1.28e-126

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 372.81  E-value: 1.28e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 172 GYVGIDSILEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLFKSKISR-KSVQPISEERIPKTIEIKSITHDIEEKGVR 250
Cdd:COG5019     2 GYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDeTEIDDIRAEGTSPTLEIKITKAELEEDGFH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 251 MKLTVIDTPGFGDHINNENCWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSK 330
Cdd:COG5019    82 LNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 331 VVNIVPVIAKADTLTLEERVYFKQRITSDLLSNGIDVYpqKEFD-EDAEDRLVNE--KFREMIPFAVVGSDHEYQVNGKR 407
Cdd:COG5019   162 RVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVF--DPYDpEDDEDESLEEnqDLRSLIPFAIIGSNTEIENGGEQ 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 408 ILGRKTKWGTIEVENTTHCEFAYLRDLLIRTHMQNIKDITSNIHFEAYRVKRLNEGNSAMANGIEKEPET 477
Cdd:COG5019   240 VRGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSGLKNSGEPSLKEIHEA 309
YeeP COG3596
Predicted GTPase [General function prediction only];
179-339 8.75e-10

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 59.78  E-value: 8.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 179 ILEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVqpiseeRIPKTIEIKSITHDIEEKGVrmkLTVIDT 258
Cdd:COG3596    25 LLAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGV------GRPCTREIQRYRLESDGLPG---LVLLDT 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 259 PGFGDHINnencwqpimkfiNDQYEKYLQEEVninrkkripdTRVHCCLYFIPATGHSLRpLDIEFMKRLSKVVNIVPVI 338
Cdd:COG3596    96 PGLGEVNE------------RDREYRELRELL----------PEADLILWVVKADDRALA-TDEEFLQALRAQYPDPPVL 152

                  .
gi 1958661173 339 A 339
Cdd:COG3596   153 V 153
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
198-369 1.14e-08

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: 54.38  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 198 VVGQSGLGKSTLINTLFKSKISrksvqpISEERIPKTIEIKSITHDIEEKGVrmKLTVIDTPGFGDhinnencwqpimkf 277
Cdd:cd00882     2 VVGRGGVGKSSLLNALLGGEVG------EVSDVPGTTRDPDVYVKELDKGKV--KLVLVDTPGLDE-------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 278 indqyEKYLQEEvninRKKRIPDTRVHCCLYFIPATG--HSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEERVYFKQR 355
Cdd:cd00882    60 -----FGGLGRE----ELARLLLRGADLILLVVDSTDreSEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRL 130
                         170
                  ....*....|....
gi 1958661173 356 ITSdLLSNGIDVYP 369
Cdd:cd00882   131 EEL-AKILGVPVFE 143
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
180-309 1.49e-07

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: 52.32  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 180 LEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLFkskisrksvqpisEERIPKTIEIKSITHDIEE-----KGVrmKLT 254
Cdd:cd01853    18 HELEAKLKKELDFSLTILVLGKTGVGKSSTINSIF-------------GERKVSVSAFQSETLRPREvsrtvDGF--KLN 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958661173 255 VIDTPGFgdhinNENCWQPIMKFINDQYEKYLqeevninrKKRIPDtrvhCCLYF 309
Cdd:cd01853    83 IIDTPGL-----LESQDQRVNRKILSIIKRFL--------KKKTID----VVLYV 120
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
195-338 6.14e-07

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: 48.00  E-value: 6.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 195 NIMVVGQSGLGKSTLINTLFKSKisrksvqPISEERIPKTIEIksITHDIEEKGVRMKLtvIDTPGFgdhinnencwqpi 274
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK-------AIVSDYPGTTRDP--NEGRLELKGKQIIL--VDTPGL------------- 56
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958661173 275 mkfindqYEKYLQEEVNINRKKRIpdTRVHCCLYFIPATgHSLRPLDIEFMKRLSKvvNIVPVI 338
Cdd:pfam01926  57 -------IEGASEGEGLGRAFLAI--IEADLILFVVDSE-EGITPLDEELLELLRE--NKKPII 108
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
194-369 2.34e-06

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: 47.93  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 194 FNIMVVGQSGLGKSTLINTLFkskisRKSVQPISEerIPKTIEIKSITHDIeEKGVrmklTVIDTPGFGDHINNencwqp 273
Cdd:cd09912     1 FLLAVVGEFSAGKSTLLNALL-----GEEVLPTGV--TPTTAVITVLRYGL-LKGV----VLVDTPGLNSTIEH------ 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 274 imkfindqyekyLQEEVninrKKRIPdtRVHCCLYFIPAtGHSLRPLDIEFMKRLSKVV--NIVPVIAKADTLT---LEE 348
Cdd:cd09912    63 ------------HTEIT----ESFLP--RADAVIFVLSA-DQPLTESEREFLKEILKWSgkKIFFVLNKIDLLSeeeLEE 123
                         170       180
                  ....*....|....*....|...
gi 1958661173 349 RVYFKQRITS--DLLSNGIDVYP 369
Cdd:cd09912   124 VLEYSREELGvlELGGGEPRIFP 146
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
193-260 3.90e-06

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: 46.98  E-value: 3.90e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958661173 193 EFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPiseeripkTIEIKSITHDIEEKGVRMKLTVIDTPG 260
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYP--------GTTRNYVTTVIEEDGKTYKFNLLDTAG 60
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
175-261 7.96e-06

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


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 46.49  E-value: 7.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 175 GIDSILEQMRRKAMKQGfefNIMVVGQSGLGKSTLINTLFKSKISRK----SVQPISEERIPKTieiksiTHDIEEKGVR 250
Cdd:cd01855   110 GVEELIEEIKKLAKYRG---DVYVVGATNVGKSTLINALLKSNGGKVqaqaLVQRLTVSPIPGT------TLGLIKIPLG 180
                          90
                  ....*....|.
gi 1958661173 251 MKLTVIDTPGF 261
Cdd:cd01855   181 EGKKLYDTPGI 191
GTPase_YqeH TIGR03597
ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of ...
175-275 2.65e-05

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


Pssm-ID: 213834 [Multi-domain]  Cd Length: 360  Bit Score: 46.07  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 175 GIDSILEQMRRKAMKQgfefNIMVVGQSGLGKSTLINTLFksKISRKSVQPISEERIPKTieiksiTHDIEEKGVRMKLT 254
Cdd:TIGR03597 140 GIDELLDKIKKARNKK----DVYVVGVTNVGKSSLINKLL--KQNNGDKDVITTSPFPGT------TLDLIEIPLDDGHS 207
                          90       100
                  ....*....|....*....|....*.
gi 1958661173 255 VIDTPGFGD-----HINNENCWQPIM 275
Cdd:TIGR03597 208 LYDTPGIINshqmaHYLDKKDLKYIT 233
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
192-365 2.70e-05

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 44.59  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 192 FEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPiseeripkTIEIKSITHDIEEKGVRMKLTVIDTPGfgdhinnencw 271
Cdd:COG1100     2 GEKKIVVVGTGGVGKTSLVNRLVGDIFSLEKYLS--------TNGVTIDKKELKLDGLDVDLVIWDTPG----------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 272 QPIMKFINDQYEKYLQEevninrkkripdtrVHCCLYFI----PATGHSLrPLDIEFMKRLSKVVNIVPVIAKADtLTLE 347
Cdd:COG1100    63 QDEFRETRQFYARQLTG--------------ASLYLFVVdgtrEETLQSL-YELLESLRRLGKKSPIILVLNKID-LYDE 126
                         170
                  ....*....|....*...
gi 1958661173 348 ERVYFKQRITSDLLSNGI 365
Cdd:COG1100   127 EEIEDEERLKEALSEDNI 144
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
199-262 4.61e-05

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


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 43.10  E-value: 4.61e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958661173 199 VGQSGLGKSTLINTLFKSKISRKSVqpiseeRIPKTIEIKSITHDIEEKGvrmkLTVIDTPGFG 262
Cdd:cd11383     3 MGKTGAGKSSLCNALFGTEVAAVGD------RRPTTRAAQAYVWQTGGDG----LVLLDLPGVG 56
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
175-261 5.20e-05

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: 44.31  E-value: 5.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 175 GIDSILEQMRRKamkqgfefNIMVVGQSGLGKSTLINTLFKSKISRksVQPISEeripKT---------IEIksitHDIE 245
Cdd:cd01854    75 GLDELRELLKGK--------TSVLVGQSGVGKSTLLNALLPELVLA--TGEISE----KLgrgrhttthREL----FPLP 136
                          90
                  ....*....|....*.
gi 1958661173 246 EKGVrmkltVIDTPGF 261
Cdd:cd01854   137 GGGL-----IIDTPGF 147
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
192-278 1.13e-04

chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K protein originally described is proposed to have three domains. The N-terminal A-domain is acidic, repetitive, weakly conserved, readily removed by proteolysis during chloroplast isolation, and not required for protein translocation. The other domains are designated G (GTPase) and M (membrane anchor); this family includes most of the G domain and all of M. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273381 [Multi-domain]  Cd Length: 763  Bit Score: 44.94  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 192 FEFNIMVVGQSGLGKSTLINTLF-KSKISRKSVQPISeeripktieiKSIThDIEEKGVRMKLTVIDTPGF----GDHIN 266
Cdd:TIGR00993 117 FSLNILVLGKSGVGKSATINSIFgEVKFSTDAFGMGT----------TSVQ-EIEGLVQGVKIRVIDTPGLkssaSDQSK 185
                          90
                  ....*....|..
gi 1958661173 267 NENCWQPIMKFI 278
Cdd:TIGR00993 186 NEKILSSVKKFI 197
RsgA COG1162
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
175-261 2.93e-04

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


Pssm-ID: 440776 [Multi-domain]  Cd Length: 300  Bit Score: 42.79  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 175 GIDSILEQMRRKamkqgfefNIMVVGQSGLGKSTLINTLFKSKISRksVQPISE------------ERIPktieiksith 242
Cdd:COG1162   156 GLDELRELLKGK--------TSVLVGQSGVGKSTLINALLPDADLA--TGEISEklgrgrhttthaELYP---------- 215
                          90
                  ....*....|....*....
gi 1958661173 243 dIEEKGVrmkltVIDTPGF 261
Cdd:COG1162   216 -LPGGGW-----LIDTPGF 228
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
195-260 3.49e-04

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


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 41.82  E-value: 3.49e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958661173 195 NIMVVGQSGLGKSTLINTL-----FKSKISRKSVQPISEE--RIPKTIEIKsithdieekgvrmkltVIDTPG 260
Cdd:pfam04548   2 RIVLVGKTGNGKSATGNSIlgrkaFESKLRAQGVTKTCQLvsRTWDGRIIN----------------VIDTPG 58
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
176-260 4.23e-04

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: 40.97  E-value: 4.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 176 IDSILEQMRRKAMKQGF--EFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPiseeRIPKTIEIKSITHDIEekgvrmkl 253
Cdd:cd01856    96 AKKLLKENEKLKAKGLLprPLRAMVVGIPNVGKSTLINRLRGKKVAKVGNKP----GVTRGQQWIRIGPNIE-------- 163

                  ....*..
gi 1958661173 254 tVIDTPG 260
Cdd:cd01856   164 -LLDTPG 169
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
196-349 6.27e-04

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: 40.57  E-value: 6.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 196 IMVVGQSGLGKSTLINTLFKSK-ISRKSVQPiseeriPKTIEIksITHDIEEkgvrmKLTVIDTPGFG----DHINNENc 270
Cdd:cd01876     2 VAFAGRSNVGKSSLINALTNRKkLARTSKTP------GRTQLI--NFFNVGD-----KFRLVDLPGYGyakvSKEVREK- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 271 WQPIMkfindqyEKYLQEEVNINRkkripdtrvhccLYFIPATGHSLRPLDIEFMKRLSKV-VNIVPVIAKADTLTLEER 349
Cdd:cd01876    68 WGKLI-------EEYLENRENLKG------------VVLLIDARHGPTPIDLEMLEFLEELgIPFLIVLTKADKLKKSEL 128
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
195-263 6.57e-04

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


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 41.42  E-value: 6.57e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958661173 195 NIMVVGQSGLGKSTLINT-LFKSK-ISRK-------SVQPISEERIPKTIEIKSITHDIEEKGVrmKLTVIDTPGFGD 263
Cdd:cd04170     1 NIALVGHSGSGKTTLAEAlLYATGaIDRLgrvedgnTVSDYDPEEKKRKMSIETSVAPLEWNGH--KINLIDTPGYAD 76
PRK00098 PRK00098
GTPase RsgA; Reviewed
178-268 7.21e-04

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 41.34  E-value: 7.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 178 SILEQMRRKAMKQGFEFNI-MVVGQSGLGKSTLINTLfkskisrksvqpISEERIpKTIEI-------KSIT-----HDI 244
Cdd:PRK00098  148 SAKEGEGLDELKPLLAGKVtVLAGQSGVGKSTLLNAL------------APDLEL-KTGEIsealgrgKHTTthvelYDL 214
                          90       100
                  ....*....|....*....|....*...
gi 1958661173 245 EEKGvrmklTVIDTPGFG----DHINNE 268
Cdd:PRK00098  215 PGGG-----LLIDTPGFSsfglHDLEAE 237
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
198-261 1.22e-03

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 39.83  E-value: 1.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958661173 198 VVGQSGLGKSTLINTLfKSKISRKsVQPISEeripktieiKS------ITH----DIEEKGVrmkltVIDTPGF 261
Cdd:pfam03193 111 LAGQSGVGKSTLLNAL-LPELDLR-TGEISE---------KLgrgrhtTTHvelfPLPGGGL-----LIDTPGF 168
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
12-169 1.41e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173   12 SSKQVESTASTPGPSRFGLKRAEVLGHKTPEPV---PRRTEITIVKPQESGLrrveTPASKAPEGSAMPVTDAAPKRvei 88
Cdd:PHA03307    44 VSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGteaPANESRSTPTWSLSTL----APASPAREGSPTPPGPSSPDP--- 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173   89 qvPKPAEAPNCPLPPqtlenseaPMSQLQSRLEPRPPVTEVPYRNQEDSEVAPSCVGDMADNPRDAMLKQAPVSRNEKAP 168
Cdd:PHA03307   117 --PPPTPPPASPPPS--------PAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAP 186

                   .
gi 1958661173  169 V 169
Cdd:PHA03307   187 S 187
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
198-263 1.59e-03

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: 39.15  E-value: 1.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958661173 198 VVGQSGLGKSTLINTLFKSKISRKSVQPISeeripkTIEIKSITHDIEEKGvrmKLTVIDTPGFGD 263
Cdd:cd00880     2 IFGRPNVGKSSLLNALLGQNVGIVSPIPGT------TRDPVRKEWELLPLG---PVVLIDTPGLDE 58
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
195-263 1.79e-03

AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 (avrRpt2-induced gene 1) that appears to be involved in plant resistance to bacteria. The Arabidopsis disease resistance gene RPS2 is involved in recognition of bacterial pathogens carrying the avirulence gene avrRpt2. AIG1 exhibits RPS2- and avrRpt1-dependent induction early after infection with Pseudomonas syringae carrying avrRpt2. This subfamily also includes IAN-4 protein, which has GTP-binding activity and shares sequence homology with a novel family of putative GTP-binding proteins: the immuno-associated nucleotide (IAN) family. The evolutionary conservation of the IAN family provides a unique example of a plant pathogen response gene conserved in animals. The IAN/IMAP subfamily has been proposed to regulate apoptosis in vertebrates and angiosperm plants, particularly in relation to cancer, diabetes, and infections. The human IAN genes were renamed GIMAP (GTPase of the immunity associated proteins).


Pssm-ID: 206651 [Multi-domain]  Cd Length: 201  Bit Score: 39.44  E-value: 1.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958661173 195 NIMVVGQSGLGKSTLINTL-----FKSKISRKSVqpiseeripkTIEIKSITHDIEEKgvrmKLTVIDTPGFGD 263
Cdd:cd01852     2 RLVLVGKTGNGKSATGNTIlgrkvFESKLSASGV----------TKTCQKESAVWDGR----RVNVIDTPGLFD 61
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
188-369 2.77e-03

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: 38.60  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 188 MKQGFefnIMVVGQSGLGKSTLINTLFKSKISrksvqPISeeRIPKTieiksiT-HDIeeKGVRMK----LTVIDTPGfg 262
Cdd:cd04163     1 FKSGF---VAIIGRPNVGKSTLLNALVGQKIS-----IVS--PKPQT------TrNRI--RGIYTDddaqIIFVDTPG-- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 263 dhinnencwqpIMKfindqYEKYLQEEVNINRKKRIPDtrVHCCLYFIPATgHSLRPLDIEFMKRLSKV-VNIVPVIAKA 341
Cdd:cd04163    61 -----------IHK-----PKKKLGERMVKAAWSALKD--VDLVLFVVDAS-EWIGEGDEFILELLKKSkTPVILVLNKI 121
                         170       180
                  ....*....|....*....|....*...
gi 1958661173 342 DTLTLEERVyFKQRITSDLLSNGIDVYP 369
Cdd:cd04163   122 DLVKDKEDL-LPLLEKLKELHPFAEIFP 148
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
151-260 3.00e-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: 38.45  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 151 PRDAMLKQAPVSRNEKAPVDF----GYVGIDSILEQMRRKAMKqGFEFNIMVVGQSGLGKSTLINTLfkskiSRKSVQPI 226
Cdd:cd01859    54 PREVLEKWKEVFESEGLPVVYvsarERLGTRILRRTIKELAID-GKPVIVGVVGYPKVGKSSIINAL-----KGRHSAST 127
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958661173 227 SeeRIPKtieIKSITHDIEEKGVRMKLTVIDTPG 260
Cdd:cd01859   128 S--PIPG---SPGYTKGIQLVRIDSKIYLIDTPG 156
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
196-390 3.26e-03

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: 39.29  E-value: 3.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 196 IMVVGQSGLGKSTLINTLFKSKISRKSvqpiseeRIPKTIEIKSITHDIEEKGvrmKLTVIDTPGFGD--HINNENCWQP 273
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHGQKISITS-------PKAQTTRNRISGIHTTGAS---QIIFIDTPGFHEkkHSLNRLMMKE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 274 IMK---------FINDQYEKYLQEEVNINrKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIA--KAD 342
Cdd:TIGR00436  73 ARSaiggvdlilFVVDSDQWNGDGEFVLT-KLQNLKRPVVLTRNKLDNKFKDKLLPLIDKYAILEDFKDIVPISAltGDN 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958661173 343 TLTLEERVYFKqritsdlLSNGIDVYPQKEFDEDAEDRLVNEKFREMI 390
Cdd:TIGR00436 152 TSFLAAFIEVH-------LPEGPFRYPEDYVTDQPDRFKISEIIREKI 192
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
194-260 6.08e-03

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: 37.44  E-value: 6.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958661173 194 FNIMVVGQSGLGKSTLINTLFKSKISRKSVQPISEERIPKTIEIksithdieeKGVRMKLTVIDTPG 260
Cdd:cd00154     1 FKIVLIGDSGVGKTSLLLRFVDNKFSENYKSTIGVDFKSKTIEV---------DGKKVKLQIWDTAG 58
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
199-349 7.37e-03

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: 37.45  E-value: 7.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 199 VGQSGLGKSTLINTLFKSK-ISRKSVQPiseeriPKTIEIksITHDIEEkgvrmKLTVIDTPGFG-------DHINnenc 270
Cdd:TIGR03598  24 AGRSNVGKSSLINALTNRKkLARTSKTP------GRTQLI--NFFEVND-----GFRLVDLPGYGyakvskeEKEK---- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 271 WQPIMkfindqyEKYLQEEVNInrkkripdtrvhCCLYFIPATGHSLRPLDIEFMKRL-SKVVNIVPVIAKADTLTLEER 349
Cdd:TIGR03598  87 WQKLI-------EEYLEKRENL------------KGVVLLMDIRHPLKELDLEMIEWLrERGIPVLIVLTKADKLKKSEL 147
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
180-260 8.01e-03

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: 38.26  E-value: 8.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 180 LEQMRRKAMKQGfEFNIMVVGQSGLGKSTLINTLFKSKISR--------KSVQPIseeRIPKTIEIksithdieekgvrm 251
Cdd:TIGR03596 106 NEKLKAKGLKNR-PIRAMIVGIPNVGKSTLINRLAGKKVAKvgnrpgvtKGQQWI---KLSDNLEL-------------- 167

                  ....*....
gi 1958661173 252 kltvIDTPG 260
Cdd:TIGR03596 168 ----LDTPG 172
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
175-260 8.71e-03

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 38.17  E-value: 8.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661173 175 GIDSILEQMRRKAMKQGFEFN---IMVVGQSGLGKSTLINTLFKSKISR--------KSVQPIseeRIPKTIEIksithd 243
Cdd:COG1161    92 GIKELIEAIRELAPEKGIKRRpirVMIVGIPNVGKSTLINRLAGKKVAKtgnkpgvtKGQQWI---KLDDGLEL------ 162
                          90
                  ....*....|....*..
gi 1958661173 244 ieekgvrmkltvIDTPG 260
Cdd:COG1161   163 ------------LDTPG 167
 
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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