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Conserved domains on  [gi|164698481|ref|NP_001106959|]
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septin-9 isoform b [Mus musculus]

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 ...
286-560 3.38e-173

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: 491.29  E-value: 3.38e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 286 QGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNEN 365
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 366 CWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEER 445
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 446 VYFKQRITADLLSNGIDVYPQKEFDEDAEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 525
Cdd:cd01850  161 TEFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 164698481 526 YLRDLLIRTHMQNIKDITSNIHFEAYRVKRLNEGN 560
Cdd:cd01850  241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
PHA03247 super family cl33720
large tegument protein UL36; Provisional
31-225 1.94e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481   31 PPNSTPPRRVQTPLLRATVAS--SSQKFQDLGvKNSEPAARLVDSLSQRSPKP-SLRRVELAGAKAPEPMSRRTEISIDI 107
Cdd:PHA03247 2674 AQASSPPQRPRRRAARPTVGSltSLADPPPPP-PTPEPAPHALVSATPLPPGPaAARQASPALPAAPAPPAVPAGPATPG 2752
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481  108 SSKQVESTASAAGPSRFGLKRAEVLGHKTPEPVPRRTEITIVKPQESVLRRVETPASKIP------EGSAVPATDAAPKR 181
Cdd:PHA03247 2753 GPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLapaaalPPAASPAGPLPPPT 2832
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 164698481  182 VEIQVPkPAEAPNCPLPSQTLENSEAPMSQLQSRLEPRPSVAEV 225
Cdd:PHA03247 2833 SAQPTA-PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKP 2875
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
286-560 3.38e-173

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: 491.29  E-value: 3.38e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 286 QGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNEN 365
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 366 CWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEER 445
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 446 VYFKQRITADLLSNGIDVYPQKEFDEDAEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 525
Cdd:cd01850  161 TEFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 164698481 526 YLRDLLIRTHMQNIKDITSNIHFEAYRVKRLNEGN 560
Cdd:cd01850  241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
287-556 5.40e-137

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: 398.98  E-value: 5.40e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481  287 GFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNENC 366
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481  367 WQPIMKFINDQYEKYLQEEVNINRKKRIpDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEERV 446
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIK-DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481  447 YFKQRITADLLSNGIDVYPQKEFDED-AEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 525
Cdd:pfam00735 160 RFKKRIREEIERQNIPIYHFPDEESDeDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 164698481  526 YLRDLLIRTHMQNIKDITSNIHFEAYRVKRL 556
Cdd:pfam00735 240 KLRNMLIRTHLQDLKEVTHELHYETYRSEKL 270
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
268-573 2.34e-126

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 375.51  E-value: 2.34e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 268 GYVGIDSILEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLFKSKISR-KSVQPTSEERIPKTIEIKSITHDIEEKGVR 346
Cdd:COG5019    2 GYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDeTEIDDIRAEGTSPTLEIKITKAELEEDGFH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 347 MKLTVIDTPGFGDHINNENCWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSK 426
Cdd:COG5019   82 LNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 427 VVNIVPVIAKADTLTLEERVYFKQRITADLLSNGIDVYpqKEFD-EDAEDRLVNE--KFREMIPFAVVGSDHEYQVNGKR 503
Cdd:COG5019  162 RVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVF--DPYDpEDDEDESLEEnqDLRSLIPFAIIGSNTEIENGGEQ 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 504 ILGRKTKWGTIEVENTTHCEFAYLRDLLIRTHMQNIKDITSNIHFEAYRVKRLNEGNSAMANGIEKEPEA 573
Cdd:COG5019  240 VRGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSGLKNSGEPSLKEIHEA 309
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
289-356 2.01e-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: 48.14  E-value: 2.01e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164698481  289 EFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIpktieiksITHDIEEKGVRMKLTVIDTPG 356
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNY--------VTTVIEEDGKTYKFNLLDTAG 60
PHA03247 PHA03247
large tegument protein UL36; Provisional
31-225 1.94e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481   31 PPNSTPPRRVQTPLLRATVAS--SSQKFQDLGvKNSEPAARLVDSLSQRSPKP-SLRRVELAGAKAPEPMSRRTEISIDI 107
Cdd:PHA03247 2674 AQASSPPQRPRRRAARPTVGSltSLADPPPPP-PTPEPAPHALVSATPLPPGPaAARQASPALPAAPAPPAVPAGPATPG 2752
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481  108 SSKQVESTASAAGPSRFGLKRAEVLGHKTPEPVPRRTEITIVKPQESVLRRVETPASKIP------EGSAVPATDAAPKR 181
Cdd:PHA03247 2753 GPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLapaaalPPAASPAGPLPPPT 2832
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 164698481  182 VEIQVPkPAEAPNCPLPSQTLENSEAPMSQLQSRLEPRPSVAEV 225
Cdd:PHA03247 2833 SAQPTA-PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKP 2875
PLN03118 PLN03118
Rab family protein; Provisional
290-356 7.85e-04

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 41.19  E-value: 7.85e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164698481 290 FNIMVVGQSGLGKSTLINTLFKSKIsrKSVQPTseerIPKTIEIKSITHDieekGVRMKLTVIDTPG 356
Cdd:PLN03118  15 FKILLIGDSGVGKSSLLVSFISSSV--EDLAPT----IGVDFKIKQLTVG----GKRLKLTIWDTAG 71
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
286-560 3.38e-173

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: 491.29  E-value: 3.38e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 286 QGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNEN 365
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 366 CWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEER 445
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 446 VYFKQRITADLLSNGIDVYPQKEFDEDAEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 525
Cdd:cd01850  161 TEFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 164698481 526 YLRDLLIRTHMQNIKDITSNIHFEAYRVKRLNEGN 560
Cdd:cd01850  241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
287-556 5.40e-137

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: 398.98  E-value: 5.40e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481  287 GFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNENC 366
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481  367 WQPIMKFINDQYEKYLQEEVNINRKKRIpDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEERV 446
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIK-DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481  447 YFKQRITADLLSNGIDVYPQKEFDED-AEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 525
Cdd:pfam00735 160 RFKKRIREEIERQNIPIYHFPDEESDeDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 164698481  526 YLRDLLIRTHMQNIKDITSNIHFEAYRVKRL 556
Cdd:pfam00735 240 KLRNMLIRTHLQDLKEVTHELHYETYRSEKL 270
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
268-573 2.34e-126

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 375.51  E-value: 2.34e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 268 GYVGIDSILEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLFKSKISR-KSVQPTSEERIPKTIEIKSITHDIEEKGVR 346
Cdd:COG5019    2 GYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDeTEIDDIRAEGTSPTLEIKITKAELEEDGFH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 347 MKLTVIDTPGFGDHINNENCWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSK 426
Cdd:COG5019   82 LNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 427 VVNIVPVIAKADTLTLEERVYFKQRITADLLSNGIDVYpqKEFD-EDAEDRLVNE--KFREMIPFAVVGSDHEYQVNGKR 503
Cdd:COG5019  162 RVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVF--DPYDpEDDEDESLEEnqDLRSLIPFAIIGSNTEIENGGEQ 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 504 ILGRKTKWGTIEVENTTHCEFAYLRDLLIRTHMQNIKDITSNIHFEAYRVKRLNEGNSAMANGIEKEPEA 573
Cdd:COG5019  240 VRGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSGLKNSGEPSLKEIHEA 309
YeeP COG3596
Predicted GTPase [General function prediction only];
275-359 3.47e-09

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 58.62  E-value: 3.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 275 ILEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVqptseeRIPKTIEIKSITHDIEEKGVrmkLTVIDT 354
Cdd:COG3596   25 LLAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGV------GRPCTREIQRYRLESDGLPG---LVLLDT 95

                 ....*
gi 164698481 355 PGFGD 359
Cdd:COG3596   96 PGLGE 100
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
294-465 8.15e-09

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: 54.77  E-value: 8.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 294 VVGQSGLGKSTLINTLFKSKISrksvqPTSEERIPkTIEIKSITHDIEEKGVrmKLTVIDTPGFGDhinnencwqpimkf 373
Cdd:cd00882    2 VVGRGGVGKSSLLNALLGGEVG-----EVSDVPGT-TRDPDVYVKELDKGKV--KLVLVDTPGLDE-------------- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 374 indqyEKYLQEEvninRKKRIPDTRVHCCLYFIPATG--HSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEERVYFKQR 451
Cdd:cd00882   60 -----FGGLGRE----ELARLLLRGADLILLVVDSTDreSEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRL 130
                        170
                 ....*....|....
gi 164698481 452 ITAdLLSNGIDVYP 465
Cdd:cd00882  131 EEL-AKILGVPVFE 143
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
276-405 9.89e-08

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: 53.48  E-value: 9.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 276 LEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLF---KSKISRKSVQPTSEERIPKTIeiksithdieeKGVrmKLTVI 352
Cdd:cd01853   18 HELEAKLKKELDFSLTILVLGKTGVGKSSTINSIFgerKVSVSAFQSETLRPREVSRTV-----------DGF--KLNII 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 164698481 353 DTPGFgdhinNENCWQPIMKFINDQYEKYLqeevninrKKRIPDtrvhCCLYF 405
Cdd:cd01853   85 DTPGL-----LESQDQRVNRKILSIIKRFL--------KKKTID----VVLYV 120
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
290-465 6.13e-07

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: 49.85  E-value: 6.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 290 FNIMVVGQSGLGKSTLINTLFkskisRKSVQPTSEerIPKTIEIKSITHDIeEKGVrmklTVIDTPGFGDHINNencwqp 369
Cdd:cd09912    1 FLLAVVGEFSAGKSTLLNALL-----GEEVLPTGV--TPTTAVITVLRYGL-LKGV----VLVDTPGLNSTIEH------ 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 370 imkfindqyekyLQEEVninrKKRIPdtRVHCCLYFIPAtGHSLRPLDIEFMKRLSKVV--NIVPVIAKADTLT---LEE 444
Cdd:cd09912   63 ------------HTEIT----ESFLP--RADAVIFVLSA-DQPLTESEREFLKEILKWSgkKIFFVLNKIDLLSeeeLEE 123
                        170       180
                 ....*....|....*....|...
gi 164698481 445 RVYFKQRITA--DLLSNGIDVYP 465
Cdd:cd09912  124 VLEYSREELGvlELGGGEPRIFP 146
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
291-434 1.16e-06

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: 47.61  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481  291 NIMVVGQSGLGKSTLINTLF--KSKISRKSvqptseeriPKTIEIksITHDIEEKGVRMKLtvIDTPGFgdhinnencwq 368
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTgaKAIVSDYP---------GTTRDP--NEGRLELKGKQIIL--VDTPGL----------- 56
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164698481  369 pimkfindqYEKYLQEEVNINRKKRIpdTRVHCCLYFIPATgHSLRPLDIEFMKRLSKvvNIVPVI 434
Cdd:pfam01926  57 ---------IEGASEGEGLGRAFLAI--IEADLILFVVDSE-EGITPLDEELLELLRE--NKKPII 108
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
289-356 2.01e-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: 48.14  E-value: 2.01e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164698481  289 EFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIpktieiksITHDIEEKGVRMKLTVIDTPG 356
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNY--------VTTVIEEDGKTYKFNLLDTAG 60
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
271-357 1.29e-05

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


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 46.10  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 271 GIDSILEQMRRKAMKQGfefNIMVVGQSGLGKSTLINTLFKSKisRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLT 350
Cdd:cd01855  110 GVEELIEEIKKLAKYRG---DVYVVGATNVGKSTLINALLKSN--GGKVQAQALVQRLTVSPIPGTTLGLIKIPLGEGKK 184

                 ....*..
gi 164698481 351 VIDTPGF 357
Cdd:cd01855  185 LYDTPGI 191
GTPase_YqeH TIGR03597
ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of ...
271-371 1.77e-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: 47.23  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481  271 GIDSILEQMRRKAMKQgfefNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSeeRIPKTieiksiTHDIEEKGVRMKLT 350
Cdd:TIGR03597 140 GIDELLDKIKKARNKK----DVYVVGVTNVGKSSLINKLLKQNNGDKDVITTS--PFPGT------TLDLIEIPLDDGHS 207
                          90       100
                  ....*....|....*....|....*.
gi 164698481  351 VIDTPGFGD-----HINNENCWQPIM 371
Cdd:TIGR03597 208 LYDTPGIINshqmaHYLDKKDLKYIT 233
PHA03247 PHA03247
large tegument protein UL36; Provisional
31-225 1.94e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481   31 PPNSTPPRRVQTPLLRATVAS--SSQKFQDLGvKNSEPAARLVDSLSQRSPKP-SLRRVELAGAKAPEPMSRRTEISIDI 107
Cdd:PHA03247 2674 AQASSPPQRPRRRAARPTVGSltSLADPPPPP-PTPEPAPHALVSATPLPPGPaAARQASPALPAAPAPPAVPAGPATPG 2752
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481  108 SSKQVESTASAAGPSRFGLKRAEVLGHKTPEPVPRRTEITIVKPQESVLRRVETPASKIP------EGSAVPATDAAPKR 181
Cdd:PHA03247 2753 GPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLapaaalPPAASPAGPLPPPT 2832
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 164698481  182 VEIQVPkPAEAPNCPLPSQTLENSEAPMSQLQSRLEPRPSVAEV 225
Cdd:PHA03247 2833 SAQPTA-PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKP 2875
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
288-461 3.58e-05

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 44.59  E-value: 3.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 288 FEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPtseeripkTIEIKSITHDIEEKGVRMKLTVIDTPGfgdhinnencw 367
Cdd:COG1100    2 GEKKIVVVGTGGVGKTSLVNRLVGDIFSLEKYLS--------TNGVTIDKKELKLDGLDVDLVIWDTPG----------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 368 QPIMKFINDQYEKYLQEevninrkkripdtrVHCCLYFI----PATGHSLrPLDIEFMKRLSKVVNIVPVIAKADtLTLE 443
Cdd:COG1100   63 QDEFRETRQFYARQLTG--------------ASLYLFVVdgtrEETLQSL-YELLESLRRLGKKSPIILVLNKID-LYDE 126
                        170
                 ....*....|....*...
gi 164698481 444 ERVYFKQRITADLLSNGI 461
Cdd:COG1100  127 EEIEDEERLKEALSEDNI 144
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
295-358 5.70e-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: 5.70e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164698481 295 VGQSGLGKSTLINTLFKSKISRKSVqptseeRIPKTIEIKSITHDIEEKGvrmkLTVIDTPGFG 358
Cdd:cd11383    3 MGKTGAGKSSLCNALFGTEVAAVGD------RRPTTRAAQAYVWQTGGDG----LVLLDLPGVG 56
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
291-356 6.57e-05

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


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 44.14  E-value: 6.57e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164698481  291 NIMVVGQSGLGKSTLINTL-----FKSKISRKSVQPTSEE--RIPKTIEIKsithdieekgvrmkltVIDTPG 356
Cdd:pfam04548   2 RIVLVGKTGNGKSATGNSIlgrkaFESKLRAQGVTKTCQLvsRTWDGRIIN----------------VIDTPG 58
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
271-357 1.08e-04

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: 43.54  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 271 GIDSILEQMRRKamkqgfefNIMVVGQSGLGKSTLINTLFKskisrKSVQPTSEERipktieiKSI-------TH----D 339
Cdd:cd01854   75 GLDELRELLKGK--------TSVLVGQSGVGKSTLLNALLP-----ELVLATGEIS-------EKLgrgrhttTHrelfP 134
                         90
                 ....*....|....*...
gi 164698481 340 IEEKGVrmkltVIDTPGF 357
Cdd:cd01854  135 LPGGGL-----IIDTPGF 147
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
288-374 1.17e-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: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481  288 FEFNIMVVGQSGLGKSTLINTLF-KSKISRKSVQPTSeeripktieiKSIThDIEEKGVRMKLTVIDTPGF----GDHIN 362
Cdd:TIGR00993 117 FSLNILVLGKSGVGKSATINSIFgEVKFSTDAFGMGT----------TSVQ-EIEGLVQGVKIRVIDTPGLkssaSDQSK 185
                          90
                  ....*....|..
gi 164698481  363 NENCWQPIMKFI 374
Cdd:TIGR00993 186 NEKILSSVKKFI 197
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
294-359 2.09e-04

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: 42.23  E-value: 2.09e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164698481 294 VVGQSGLGKSTLINTLFKSKISRKSVQP-TSEERIPKTIEIKSIThdieekgvrmKLTVIDTPGFGD 359
Cdd:cd00880    2 IFGRPNVGKSSLLNALLGQNVGIVSPIPgTTRDPVRKEWELLPLG----------PVVLIDTPGLDE 58
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
272-356 2.56e-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: 42.13  E-value: 2.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 272 IDSILEQMRRKAMKQGF--EFNIMVVGQSGLGKSTLINTLFKSKISRKSVQP--TseeripKTIEIKSITHDIEekgvrm 347
Cdd:cd01856   96 AKKLLKENEKLKAKGLLprPLRAMVVGIPNVGKSTLINRLRGKKVAKVGNKPgvT------RGQQWIRIGPNIE------ 163

                 ....*....
gi 164698481 348 kltVIDTPG 356
Cdd:cd01856  164 ---LLDTPG 169
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
292-445 4.49e-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: 41.34  E-value: 4.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 292 IMVVGQSGLGKSTLINTLFKskisRKSVQPTSeeRIP-KTIEIksITHDIEEkgvrmKLTVIDTPGFG----DHINNENc 366
Cdd:cd01876    2 VAFAGRSNVGKSSLINALTN----RKKLARTS--KTPgRTQLI--NFFNVGD-----KFRLVDLPGYGyakvSKEVREK- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 367 WQPIMkfindqyEKYLQEEVNINRkkripdtrvhccLYFIPATGHSLRPLDIEFMKRLSKV-VNIVPVIAKADTLTLEER 445
Cdd:cd01876   68 WGKLI-------EEYLENRENLKG------------VVLLIDARHGPTPIDLEMLEFLEELgIPFLIVLTKADKLKKSEL 128
PHA03247 PHA03247
large tegument protein UL36; Provisional
31-258 5.09e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 5.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481   31 PPNSTPPrrvQTPLLRATVASSSQKFQDLGvkNSEPAARLVDSLSQRSPKP---SLRRVELAGAKAPEPMSRRTEISIDI 107
Cdd:PHA03247 2613 PPSPLPP---DTHAPDPPPPSPSPAANEPD--PHPPPTVPPPERPRDDPAPgrvSRPRRARRLGRAAQASSPPQRPRRRA 2687
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481  108 SSKQVESTASAAGPSRFGlkraevlghKTPEPVPRRTEITIVKPQESVLRRVETPASKI-------PEGSAVPATDAAPK 180
Cdd:PHA03247 2688 ARPTVGSLTSLADPPPPP---------PTPEPAPHALVSATPLPPGPAAARQASPALPAapappavPAGPATPGGPARPA 2758
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164698481  181 RveiqvPKPAEAPNCPLPSQtlenseAPMSQLQSRLEPRPSVAEVPYRNQEDSEVTPSCVGDMADNPRDAM-LKQAPAS 258
Cdd:PHA03247 2759 R-----PPTTAGPPAPAPPA------APAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALpPAASPAG 2826
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
284-465 6.72e-04

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: 40.52  E-value: 6.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 284 MKQGFefnIMVVGQSGLGKSTLINTLFKSKISrksvqPTSeeRIPKTieiksiT-HDIeeKGVRMK----LTVIDTPGfg 358
Cdd:cd04163    1 FKSGF---VAIIGRPNVGKSTLLNALVGQKIS-----IVS--PKPQT------TrNRI--RGIYTDddaqIIFVDTPG-- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 359 dhinnencwqpIMKfindqYEKYLQEEVNINRKKRIPDtrVHCCLYFIPATgHSLRPLDIEFMKRLSKV-VNIVPVIAKA 437
Cdd:cd04163   61 -----------IHK-----PKKKLGERMVKAAWSALKD--VDLVLFVVDAS-EWIGEGDEFILELLKKSkTPVILVLNKI 121
                        170       180
                 ....*....|....*....|....*...
gi 164698481 438 DTLTLEERVyFKQRITADLLSNGIDVYP 465
Cdd:cd04163  122 DLVKDKEDL-LPLLEKLKELHPFAEIFP 148
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
271-356 7.34e-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: 40.38  E-value: 7.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 271 GIDSILEQMRRKAMKqGFEFNIMVVGQSGLGKSTLINTLfkskiSRKSVQPTSeeRIPKtieIKSITHDIEEKGVRMKLT 350
Cdd:cd01859   82 GTRILRRTIKELAID-GKPVIVGVVGYPKVGKSSIINAL-----KGRHSASTS--PIPG---SPGYTKGIQLVRIDSKIY 150

                 ....*.
gi 164698481 351 VIDTPG 356
Cdd:cd01859  151 LIDTPG 156
PLN03118 PLN03118
Rab family protein; Provisional
290-356 7.85e-04

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 41.19  E-value: 7.85e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164698481 290 FNIMVVGQSGLGKSTLINTLFKSKIsrKSVQPTseerIPKTIEIKSITHDieekGVRMKLTVIDTPG 356
Cdd:PLN03118  15 FKILLIGDSGVGKSSLLVSFISSSV--EDLAPT----IGVDFKIKQLTVG----GKRLKLTIWDTAG 71
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
291-359 1.13e-03

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: 41.04  E-value: 1.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164698481 291 NIMVVGQSGLGKSTLINT-LFKSK-ISRK-------SVQPTSEERIPKTIEIKSITHDIEEKGVrmKLTVIDTPGFGD 359
Cdd:cd04170    1 NIALVGHSGSGKTTLAEAlLYATGaIDRLgrvedgnTVSDYDPEEKKRKMSIETSVAPLEWNGH--KINLIDTPGYAD 76
RsgA COG1162
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
271-357 1.35e-03

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


Pssm-ID: 440776 [Multi-domain]  Cd Length: 300  Bit Score: 40.87  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 271 GIDSILEQMRRKamkqgfefNIMVVGQSGLGKSTLINTLFKskisrKSVQPTSE--ERIPK----TieiksiTH----DI 340
Cdd:COG1162  156 GLDELRELLKGK--------TSVLVGQSGVGKSTLINALLP-----DADLATGEisEKLGRgrhtT------THaelyPL 216
                         90
                 ....*....|....*..
gi 164698481 341 EEKGVrmkltVIDTPGF 357
Cdd:COG1162  217 PGGGW-----LIDTPGF 228
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
294-357 1.78e-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: 39.45  E-value: 1.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164698481  294 VVGQSGLGKSTLINTLfkskisrksvQPTSEERipktieiksiTHDIEEKGVRMKLT--------------VIDTPGF 357
Cdd:pfam03193 111 LAGQSGVGKSTLLNAL----------LPELDLR----------TGEISEKLGRGRHTtthvelfplpggglLIDTPGF 168
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
291-359 1.82e-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: 39.83  E-value: 1.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164698481 291 NIMVVGQSGLGKSTLINTL-----FKSKISRKSVqptseeripkTIEIKSITHDIEEKgvrmKLTVIDTPGFGD 359
Cdd:cd01852    2 RLVLVGKTGNGKSATGNTIlgrkvFESKLSASGV----------TKTCQKESAVWDGR----RVNVIDTPGLFD 61
PRK00098 PRK00098
GTPase RsgA; Reviewed
274-364 2.32e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 40.19  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481 274 SILEQMRRKAMKQGFEFNI-MVVGQSGLGKSTLINTLfkskisrksvqptseerIPKtIEIKsiTHDIEEKGVRMKLT-- 350
Cdd:PRK00098 148 SAKEGEGLDELKPLLAGKVtVLAGQSGVGKSTLLNAL-----------------APD-LELK--TGEISEALGRGKHTtt 207
                         90       100       110
                 ....*....|....*....|....*....|
gi 164698481 351 ------------VIDTPGFG----DHINNE 364
Cdd:PRK00098 208 hvelydlpggglLIDTPGFSsfglHDLEAE 237
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
292-486 2.97e-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: 39.68  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481  292 IMVVGQSGLGKSTLINTLFKSKISRKSvqptseeRIPKTIEIKSITHDIEEKGvrmKLTVIDTPGFGD--HINNENCWQP 369
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHGQKISITS-------PKAQTTRNRISGIHTTGAS---QIIFIDTPGFHEkkHSLNRLMMKE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481  370 IMK---------FINDQYEKYLQEEVNINrKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIA--KAD 438
Cdd:TIGR00436  73 ARSaiggvdlilFVVDSDQWNGDGEFVLT-KLQNLKRPVVLTRNKLDNKFKDKLLPLIDKYAILEDFKDIVPISAltGDN 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 164698481  439 TLTLEERVYFKqritadlLSNGIDVYPQKEFDEDAEDRLVNEKFREMI 486
Cdd:TIGR00436 152 TSFLAAFIEVH-------LPEGPFRYPEDYVTDQPDRFKISEIIREKI 192
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
295-445 7.70e-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: 37.84  E-value: 7.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481  295 VGQSGLGKSTLINTLFKSK-ISRKSVQPTseeripKTIEIksITHDIEEkgvrmKLTVIDTPGFG-------DHINnenc 366
Cdd:TIGR03598  24 AGRSNVGKSSLINALTNRKkLARTSKTPG------RTQLI--NFFEVND-----GFRLVDLPGYGyakvskeEKEK---- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698481  367 WQPIMkfindqyEKYLQEEVNInrkkripdtrvhCCLYFIPATGHSLRPLDIEFMKRL-SKVVNIVPVIAKADTLTLEER 445
Cdd:TIGR03598  87 WQKLI-------EEYLEKRENL------------KGVVLLMDIRHPLKELDLEMIEWLrERGIPVLIVLTKADKLKKSEL 147
 
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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