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Conserved domains on  [gi|1009287637|ref|NP_001308425|]
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septin-10 isoform 3 [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 ...
 6-198 3.45e-105

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: 308.32  E-value: 3.45e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287637   6 YQPIVDYIDAQFEAYLQEELKIKRSLFtYHDSRIHVCLYFISPTGHSLKTLDLLTMKNLDSKVNIIPVIAKADTVSKTEL 85
Cdd:cd01850    82 WKPIVDYIDDQFESYLREESRINRNRR-IPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287637  86 QKFKIKLMSELVSNGVQIYQFPTD--DDTIAKVNAAMNGQLPFAVVGSMDEVKVGNKMVKARQYPWGVVQVENENHCDFV 163
Cdd:cd01850   161 TEFKKRIMEDIEENNIKIYKFPEDeeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1009287637 164 KLREMLICTNMEDLREQTHTRHYELYRRCKLEEMG 198
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 ...
 6-198 3.45e-105

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: 308.32  E-value: 3.45e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287637   6 YQPIVDYIDAQFEAYLQEELKIKRSLFtYHDSRIHVCLYFISPTGHSLKTLDLLTMKNLDSKVNIIPVIAKADTVSKTEL 85
Cdd:cd01850    82 WKPIVDYIDDQFESYLREESRINRNRR-IPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287637  86 QKFKIKLMSELVSNGVQIYQFPTD--DDTIAKVNAAMNGQLPFAVVGSMDEVKVGNKMVKARQYPWGVVQVENENHCDFV 163
Cdd:cd01850   161 TEFKKRIMEDIEENNIKIYKFPEDeeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1009287637 164 KLREMLICTNMEDLREQTHTRHYELYRRCKLEEMG 198
Cdd:cd01850   241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
 6-196 8.40e-83

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: 251.45  E-value: 8.40e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287637   6 YQPIVDYIDAQFEAYLQEELKIKRSLFTyhDSRIHVCLYFISPTGHSLKTLDLLTMKNLDSKVNIIPVIAKADTVSKTEL 85
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIK--DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDEL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287637  86 QKFKIKLMSELVSNGVQIYQFP---TDDDTIAKVNAAMNGQLPFAVVGSMDEVKVGNKMVKARQYPWGVVQVENENHCDF 162
Cdd:pfam00735 159 QRFKKRIREEIERQNIPIYHFPdeeSDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDF 238

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1009287637 163 VKLREMLICTNMEDLREQTHTRHYELYRRCKLEE 196
Cdd:pfam00735 239 LKLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 7-264 7.82e-80

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 247.24  E-value: 7.82e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287637   7 QPIVDYIDAQFEAYLQEELKIKRSLFtYHDSRIHVCLYFISPTGHSLKTLDLLTMKNLDSKVNIIPVIAKADTVSKTELQ 86
Cdd:COG5019   103 EPIVDYIDDQFDQYLDEEQKIKRNPK-FKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKRVNLIPVIAKADTLTDDELA 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287637  87 KFKIKLMSELVSNGVQIYQ-FPTDDDTIAKV--NAAMNGQLPFAVVGSMDEVKVGNKMVKARQYPWGVVQVENENHCDFV 163
Cdd:COG5019   182 EFKERIREDLEQYNIPVFDpYDPEDDEDESLeeNQDLRSLIPFAIIGSNTEIENGGEQVRGRKYPWGVVEIDDEEHSDFK 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287637 164 KLREMLICTNMEDLREQTHTRHYELYRRCKLEemgftdvgpenkpvSVQETYEAKRHEFHGERQRKEE-EMKQMFVQRVK 242
Cdd:COG5019   262 KLRNLLIRTHLQELKETTENLLYENYRTEKLS--------------GLKNSGEPSLKEIHEARLNEEErELKKKFTEKIR 327

                         250       260
                  ....*....|....*....|..
gi 1009287637 243 EKEAILKEAERELQAKFEHLKR 264
Cdd:COG5019   328 EKEKRLEELEQNLIEERKELNS 349
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 6-198 3.45e-105

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: 308.32  E-value: 3.45e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287637   6 YQPIVDYIDAQFEAYLQEELKIKRSLFtYHDSRIHVCLYFISPTGHSLKTLDLLTMKNLDSKVNIIPVIAKADTVSKTEL 85
Cdd:cd01850    82 WKPIVDYIDDQFESYLREESRINRNRR-IPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287637  86 QKFKIKLMSELVSNGVQIYQFPTD--DDTIAKVNAAMNGQLPFAVVGSMDEVKVGNKMVKARQYPWGVVQVENENHCDFV 163
Cdd:cd01850   161 TEFKKRIMEDIEENNIKIYKFPEDeeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1009287637 164 KLREMLICTNMEDLREQTHTRHYELYRRCKLEEMG 198
Cdd:cd01850   241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
 6-196 8.40e-83

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: 251.45  E-value: 8.40e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287637   6 YQPIVDYIDAQFEAYLQEELKIKRSLFTyhDSRIHVCLYFISPTGHSLKTLDLLTMKNLDSKVNIIPVIAKADTVSKTEL 85
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIK--DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDEL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287637  86 QKFKIKLMSELVSNGVQIYQFP---TDDDTIAKVNAAMNGQLPFAVVGSMDEVKVGNKMVKARQYPWGVVQVENENHCDF 162
Cdd:pfam00735 159 QRFKKRIREEIERQNIPIYHFPdeeSDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDF 238

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1009287637 163 VKLREMLICTNMEDLREQTHTRHYELYRRCKLEE 196
Cdd:pfam00735 239 LKLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 7-264 7.82e-80

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 247.24  E-value: 7.82e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287637   7 QPIVDYIDAQFEAYLQEELKIKRSLFtYHDSRIHVCLYFISPTGHSLKTLDLLTMKNLDSKVNIIPVIAKADTVSKTELQ 86
Cdd:COG5019   103 EPIVDYIDDQFDQYLDEEQKIKRNPK-FKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKRVNLIPVIAKADTLTDDELA 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287637  87 KFKIKLMSELVSNGVQIYQ-FPTDDDTIAKV--NAAMNGQLPFAVVGSMDEVKVGNKMVKARQYPWGVVQVENENHCDFV 163
Cdd:COG5019   182 EFKERIREDLEQYNIPVFDpYDPEDDEDESLeeNQDLRSLIPFAIIGSNTEIENGGEQVRGRKYPWGVVEIDDEEHSDFK 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287637 164 KLREMLICTNMEDLREQTHTRHYELYRRCKLEemgftdvgpenkpvSVQETYEAKRHEFHGERQRKEE-EMKQMFVQRVK 242
Cdd:COG5019   262 KLRNLLIRTHLQELKETTENLLYENYRTEKLS--------------GLKNSGEPSLKEIHEARLNEEErELKKKFTEKIR 327

                         250       260
                  ....*....|....*....|..
gi 1009287637 243 EKEAILKEAERELQAKFEHLKR 264
Cdd:COG5019   328 EKEKRLEELEQNLIEERKELNS 349
 
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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