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Conserved domains on  [gi|156602653|ref|NP_061979|]
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neuronal-specific septin-3 isoform B [Homo sapiens]

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

CATH:  3.40.50.300
Gene Ontology:  GO:0005525|GO:0003924|GO:0061640|GO:0060090
PubMed:  14611653|12445407|12111093|18478031

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 ...
 59-333 1.07e-167

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: 468.18  E-value: 1.07e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653  59 GFDFNIMVVGQSGLGKSTLVNTLFKSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENC 138
Cdd:cd01850    2 GFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSDC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653 139 WEPIEKYINEQYEKFLKEEVNIARKKRIPDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKS 218
Cdd:cd01850   82 WKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEELT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653 219 EFKQRVRKELEVNGIEFYPQKEFDEDLEDKTENDKIRqESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEFA 298
Cdd:cd01850  162 EFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLK-SLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 156602653 299 LLRDFVIRTHLQDLKEVTHNIHYETYRAKRLNDNG 333
Cdd:cd01850  241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 59-333 1.07e-167

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: 468.18  E-value: 1.07e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653  59 GFDFNIMVVGQSGLGKSTLVNTLFKSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENC 138
Cdd:cd01850    2 GFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSDC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653 139 WEPIEKYINEQYEKFLKEEVNIARKKRIPDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKS 218
Cdd:cd01850   82 WKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEELT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653 219 EFKQRVRKELEVNGIEFYPQKEFDEDLEDKTENDKIRqESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEFA 298
Cdd:cd01850  162 EFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLK-SLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 156602653 299 LLRDFVIRTHLQDLKEVTHNIHYETYRAKRLNDNG 333
Cdd:cd01850  241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
 59-329 1.11e-142

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: 404.76  E-value: 1.11e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653   59 GFDFNIMVVGQSGLGKSTLVNTLFKSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENC 138
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653  139 WEPIEKYINEQYEKFLKEEVNIARKKRIpDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKS 218
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIK-DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653  219 EFKQRVRKELEVNGIEFYPQKEFDED-LEDKTENDKIRqESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEF 297
Cdd:pfam00735 160 RFKKRIREEIERQNIPIYHFPDEESDeDEEKELNEQLK-SSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDF 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 156602653  298 ALLRDFVIRTHLQDLKEVTHNIHYETYRAKRL 329
Cdd:pfam00735 239 LKLRNMLIRTHLQDLKEVTHELHYETYRSEKL 270
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 39-329 2.30e-128

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 372.04  E-value: 2.30e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653  39 LGYIGIDTIIEQMRKKTMKTGFDFNIMVVGQSGLGKSTLVNTLF-KSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGV 117
Cdd:COG5019    1 NGYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFgTSLVDETEIDDIRAEGTSPTLEIKITKAELEEDGF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653 118 KMKLTVIDTPGFGDQINNENCWEPIEKYINEQYEKFLKEEVNIARKKRIPDTRVHCCLYFISPTGHSLRPLDLEFMKHLS 197
Cdd:COG5019   81 HLNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653 198 KVVNIIPVIAKADTMTLEEKSEFKQRVRKELEVNGIEFYPQKEFDEDLEDKTENDKIRQESMPFAVVGSDKEYQVNGKRV 277
Cdd:COG5019  161 KRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESLEENQDLRSLIPFAIIGSNTEIENGGEQV 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 156602653 278 LGRKTPWGIIEVENLNHCEFALLRDFVIRTHLQDLKEVTHNIHYETYRAKRL 329
Cdd:COG5019  241 RGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKL 292
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
 60-146 2.79e-05

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: 46.10  E-value: 2.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653   60 FDFNIMVVGQSGLGKSTLVNTLFKSQvsrKASSwnrEEKIPKTVEIKAIghvieEGGVK-MKLTVIDTPGF----GDQIN 134
Cdd:TIGR00993 117 FSLNILVLGKSGVGKSATINSIFGEV---KFST---DAFGMGTTSVQEI-----EGLVQgVKIRVIDTPGLkssaSDQSK 185

                          90
                  ....*....|..
gi 156602653  135 NENCWEPIEKYI 146
Cdd:TIGR00993 186 NEKILSSVKKFI 197
PRK00098 PRK00098
GTPase RsgA; Reviewed
 39-129 3.83e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 38.65  E-value: 3.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653  39 LGY----------IGIDTIIEQMRKKTMktgfdfniMVVGQSGLGKSTLVNTLfksqvsrkasswnreekIP----KTVE 104
Cdd:PRK00098 140 IGYdvlelsakegEGLDELKPLLAGKVT--------VLAGQSGVGKSTLLNAL-----------------APdlelKTGE 194

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 156602653 105 I-KAIG-------HV----IEEGGvkmklTVIDTPGF 129
Cdd:PRK00098 195 IsEALGrgkhtttHVelydLPGGG-----LLIDTPGF 226
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 59-333 1.07e-167

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: 468.18  E-value: 1.07e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653  59 GFDFNIMVVGQSGLGKSTLVNTLFKSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENC 138
Cdd:cd01850    2 GFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSDC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653 139 WEPIEKYINEQYEKFLKEEVNIARKKRIPDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKS 218
Cdd:cd01850   82 WKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEELT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653 219 EFKQRVRKELEVNGIEFYPQKEFDEDLEDKTENDKIRqESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEFA 298
Cdd:cd01850  162 EFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLK-SLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 156602653 299 LLRDFVIRTHLQDLKEVTHNIHYETYRAKRLNDNG 333
Cdd:cd01850  241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
 59-329 1.11e-142

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: 404.76  E-value: 1.11e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653   59 GFDFNIMVVGQSGLGKSTLVNTLFKSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENC 138
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653  139 WEPIEKYINEQYEKFLKEEVNIARKKRIpDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKS 218
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIK-DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653  219 EFKQRVRKELEVNGIEFYPQKEFDED-LEDKTENDKIRqESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEF 297
Cdd:pfam00735 160 RFKKRIREEIERQNIPIYHFPDEESDeDEEKELNEQLK-SSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDF 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 156602653  298 ALLRDFVIRTHLQDLKEVTHNIHYETYRAKRL 329
Cdd:pfam00735 239 LKLRNMLIRTHLQDLKEVTHELHYETYRSEKL 270
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 39-329 2.30e-128

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 372.04  E-value: 2.30e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653  39 LGYIGIDTIIEQMRKKTMKTGFDFNIMVVGQSGLGKSTLVNTLF-KSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGV 117
Cdd:COG5019    1 NGYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFgTSLVDETEIDDIRAEGTSPTLEIKITKAELEEDGF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653 118 KMKLTVIDTPGFGDQINNENCWEPIEKYINEQYEKFLKEEVNIARKKRIPDTRVHCCLYFISPTGHSLRPLDLEFMKHLS 197
Cdd:COG5019   81 HLNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653 198 KVVNIIPVIAKADTMTLEEKSEFKQRVRKELEVNGIEFYPQKEFDEDLEDKTENDKIRQESMPFAVVGSDKEYQVNGKRV 277
Cdd:COG5019  161 KRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESLEENQDLRSLIPFAIIGSNTEIENGGEQV 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 156602653 278 LGRKTPWGIIEVENLNHCEFALLRDFVIRTHLQDLKEVTHNIHYETYRAKRL 329
Cdd:COG5019  241 RGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKL 292
YeeP COG3596
Predicted GTPase [General function prediction only];
46-207 1.02e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 55.93  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653  46 TIIEQMRKKTMKTGFDFNIMVVGQSGLGKSTLVNTLFKSQVSRkasswnREEKIPKTVEIKAigHVIEEGGVKMkLTVID 125
Cdd:COG3596   24 ELLAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAE------VGVGRPCTREIQR--YRLESDGLPG-LVLLD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653 126 TPGFGDQINNEncwepiEKYIneQYEKFLKEevniarkkripdtrVHCCLYFISPTGHSLRpLDLEFMKHLSKVVNIIPV 205
Cdd:COG3596   95 TPGLGEVNERD------REYR--ELRELLPE--------------ADLILWVVKADDRALA-TDEEFLQALRAQYPDPPV 151


                 ..
gi 156602653 206 IA 207
Cdd:COG3596  152 LV 153
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
 48-177 1.71e-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: 54.63  E-value: 1.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653  48 IEQMRKKTMKTGFDFNIMVVGQSGLGKSTLVNTLF---KSQVSRKASSWNREEKIPKTVeikaighvieeGGVkmKLTVI 124
Cdd:cd01853   18 HELEAKLKKELDFSLTILVLGKTGVGKSSTINSIFgerKVSVSAFQSETLRPREVSRTV-----------DGF--KLNII 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 156602653 125 DTPGF---GDQINNENCWEPIEKYIneqyekflkeevniarKKRIPDtrvhCCLYF 177
Cdd:cd01853   85 DTPGLlesQDQRVNRKILSIIKRFL----------------KKKTID----VVLYV 120
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 42-129 1.09e-07

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: 51.63  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653  42 IGIDTIIEQMRKKTmktgfdfnIMVVGQSGLGKSTLVNTLFKsqvsrkasswnrEEKIpKTVEI-KAIG----------- 109
Cdd:cd01854   74 EGLDELRELLKGKT--------SVLVGQSGVGKSTLLNALLP------------ELVL-ATGEIsEKLGrgrhttthrel 132

                         90       100
                 ....*....|....*....|
gi 156602653 110 HVIEEGGVkmkltVIDTPGF 129
Cdd:cd01854  133 FPLPGGGL-----IIDTPGF 147
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 66-237 1.90e-07

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: 50.15  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653  66 VVGQSGLGKSTLVNTLFKSQVSRKasswnrEEKIPKTVEIKAIGHVIEEGGVkmKLTVIDTPGFGDqINNENCWEPIEKY 145
Cdd:cd00882    2 VVGRGGVGKSSLLNALLGGEVGEV------SDVPGTTRDPDVYVKELDKGKV--KLVLVDTPGLDE-FGGLGREELARLL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653 146 INeqyekflkeevniarkkripdtRVHCCLYFISPTGH-SLRPLDLEFMKHLSKV-VNIIPVIAKADTMTLEEKSEFKQR 223
Cdd:cd00882   73 LR----------------------GADLILLVVDSTDReSEEDAKLLILRRLRKEgIPIILVGNKIDLLEEREVEELLRL 130

                        170
                 ....*....|....
gi 156602653 224 VRKELEvNGIEFYP 237
Cdd:cd00882  131 EELAKI-LGVPVFE 143
RsgA COG1162
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
42-129 1.59e-06

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


Pssm-ID: 440776 [Multi-domain]  Cd Length: 300  Bit Score: 48.96  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653  42 IGIDTIIEQMRKKTmktgfdfnIMVVGQSGLGKSTLVNTLFKsqvsrkasswnrEEKIpKTVEI-KAIG----------- 109
Cdd:COG1162  155 EGLDELRELLKGKT--------SVLVGQSGVGKSTLINALLP------------DADL-ATGEIsEKLGrgrhttthael 213

                         90       100
                 ....*....|....*....|
gi 156602653 110 HVIEEGGVkmkltVIDTPGF 129
Cdd:COG1162  214 YPLPGGGW-----LIDTPGF 228
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 63-206 1.72e-05

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: 43.38  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653   63 NIMVVGQSGLGKSTLVNTLF--KSQVSRKAsswnreekiPKTVEIkaIGHVIEEGGVKMKLtvIDTPGFgdqinnencwe 140
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTgaKAIVSDYP---------GTTRDP--NEGRLELKGKQIIL--VDTPGL----------- 56

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156602653  141 piekyineqYEKFLKEEVNIARKKRIPDTRVhccLYFISPTGHSLRPLDLEFMKHLSKvvNIIPVI 206
Cdd:pfam01926  57 ---------IEGASEGEGLGRAFLAIIEADL---ILFVVDSEEGITPLDEELLELLRE--NKKPII 108
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
 60-146 2.79e-05

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: 46.10  E-value: 2.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653   60 FDFNIMVVGQSGLGKSTLVNTLFKSQvsrKASSwnrEEKIPKTVEIKAIghvieEGGVK-MKLTVIDTPGF----GDQIN 134
Cdd:TIGR00993 117 FSLNILVLGKSGVGKSATINSIFGEV---KFST---DAFGMGTTSVQEI-----EGLVQgVKIRVIDTPGLkssaSDQSK 185

                          90
                  ....*....|..
gi 156602653  135 NENCWEPIEKYI 146
Cdd:TIGR00993 186 NEKILSSVKKFI 197
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 61-128 1.17e-04

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: 41.97  E-value: 1.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156602653   61 DFNIMVVGQSGLGKSTLVNTLFKSQVSrkasswnrEEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPG 128
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGS--------ITEYYPGTTRNYVTTVIEEDGKTYKFNLLDTAG 60
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 43-129 2.63e-04

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


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 41.48  E-value: 2.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653  43 GIDTIIEQMRKKTMKTGfdfNIMVVGQSGLGKSTLVNTLFKSQVSRKASSWNREE----KIP-KTVEIKAIghvieegGV 117
Cdd:cd01855  110 GVEELIEEIKKLAKYRG---DVYVVGATNVGKSTLINALLKSNGGKVQAQALVQRltvsPIPgTTLGLIKI-------PL 179

                         90
                 ....*....|..
gi 156602653 118 KMKLTVIDTPGF 129
Cdd:cd01855  180 GEGKKLYDTPGI 191
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 66-131 3.57e-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: 40.69  E-value: 3.57e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156602653  66 VVGQSGLGKSTLVNTLFKSQVSrKASSWNREEKIPKTVEIKaighVIEEGGVkmklTVIDTPGFGD 131
Cdd:cd00880    2 IFGRPNVGKSSLLNALLGQNVG-IVSPIPGTTRDPVRKEWE----LLPLGPV----VLIDTPGLDE 58
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
64-236 3.67e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 40.73  E-value: 3.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653  64 IMVVGQSGLGKSTLVNTLFKSQVSrkasswnrEEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGfgdqinnencwepIE 143
Cdd:COG1100    6 IVVVGTGGVGKTSLVNRLVGDIFS--------LEKYLSTNGVTIDKKELKLDGLDVDLVIWDTPG-------------QD 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653 144 KY--INEQYEKFLKEevniarkkripdtrVHCCLYFISPT-GHSLRPLD--LEFMKHLSKVVNIIPVIAKADTMTLEEKS 218
Cdd:COG1100   65 EFreTRQFYARQLTG--------------ASLYLFVVDGTrEETLQSLYelLESLRRLGKKSPIILVLNKIDLYDEEEIE 130

                        170
                 ....*....|....*...
gi 156602653 219 EfKQRVRKELEVNGIEFY 236
Cdd:COG1100  131 D-EERLKEALSEDNIVEV 147
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 42-129 6.78e-04

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


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 39.83  E-value: 6.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653   42 IGIDTIIEQMRKKTmktgfdfnIMVVGQSGLGKSTLVNTLFKSQVSRkasswnreekipkTVEI-KAIG-------HV-- 111
Cdd:pfam03193  95 EGIEALKELLKGKT--------TVLAGQSGVGKSTLLNALLPELDLR-------------TGEIsEKLGrgrhtttHVel 153

                          90       100
                  ....*....|....*....|
gi 156602653  112 --IEEGGVkmkltVIDTPGF 129
Cdd:pfam03193 154 fpLPGGGL-----LIDTPGF 168
PRK00098 PRK00098
GTPase RsgA; Reviewed
 39-129 3.83e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 38.65  E-value: 3.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156602653  39 LGY----------IGIDTIIEQMRKKTMktgfdfniMVVGQSGLGKSTLVNTLfksqvsrkasswnreekIP----KTVE 104
Cdd:PRK00098 140 IGYdvlelsakegEGLDELKPLLAGKVT--------VLAGQSGVGKSTLLNAL-----------------APdlelKTGE 194

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 156602653 105 I-KAIG-------HV----IEEGGvkmklTVIDTPGF 129
Cdd:PRK00098 195 IsEALGrgkhtttHVelydLPGGG-----LLIDTPGF 226
PRK12288 PRK12288
small ribosomal subunit biogenesis GTPase RsgA;
43-81 7.32e-03

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237039 [Multi-domain]  Cd Length: 347  Bit Score: 37.91  E-value: 7.32e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 156602653  43 GIDTIIEQMRKKTmktgfdfNImVVGQSGLGKSTLVNTL 81
Cdd:PRK12288 195 GLEELEAALTGRI-------SI-FVGQSGVGKSSLINAL 225
 
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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