NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1009287641|ref|NP_001308428|]
View 

septin-10 isoform 5 [Homo sapiens]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 32-164 3.47e-67

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd01850:

Pssm-ID: 476819  Cd Length: 275  Bit Score: 210.09  E-value: 3.47e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287641  32 QIVNIIPVIAKADTVSKTELQKFKIKLMSELVSNGVQIYQFPTD--DDTIAKVNAAMNGQLPFAVVGSMDEVKVGNKMVK 109
Cdd:cd01850   141 KKVNIIPVIAKADTLTPEELTEFKKRIMEDIEENNIKIYKFPEDeeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVR 220

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1009287641 110 ARQYPWGVVQVENENHCDFVKLREMLICTNMEDLREQTHTRHYELYRRCKLEEMG 164
Cdd:cd01850   221 GRKYPWGVVEVENEEHCDFVKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 32-164 3.47e-67

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: 210.09  E-value: 3.47e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287641  32 QIVNIIPVIAKADTVSKTELQKFKIKLMSELVSNGVQIYQFPTD--DDTIAKVNAAMNGQLPFAVVGSMDEVKVGNKMVK 109
Cdd:cd01850   141 KKVNIIPVIAKADTLTPEELTEFKKRIMEDIEENNIKIYKFPEDeeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVR 220

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1009287641 110 ARQYPWGVVQVENENHCDFVKLREMLICTNMEDLREQTHTRHYELYRRCKLEEMG 164
Cdd:cd01850   221 GRKYPWGVVEVENEEHCDFVKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
 32-162 2.25e-50

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: 167.09  E-value: 2.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287641  32 QIVNIIPVIAKADTVSKTELQKFKIKLMSELVSNGVQIYQFP---TDDDTIAKVNAAMNGQLPFAVVGSMDEVKVGNKMV 108
Cdd:pfam00735 139 EKVNIIPVIAKADTLTPDELQRFKKRIREEIERQNIPIYHFPdeeSDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKV 218

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1009287641 109 KARQYPWGVVQVENENHCDFVKLREMLICTNMEDLREQTHTRHYELYRRCKLEE 162
Cdd:pfam00735 219 RGRKYPWGVVEVENPSHCDFLKLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 32-230 2.85e-49

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 167.11  E-value: 2.85e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287641  32 QIVNIIPVIAKADTVSKTELQKFKIKLMSELVSNGVQIYQ-FPTDDDTIAKV--NAAMNGQLPFAVVGSMDEVKVGNKMV 108
Cdd:COG5019   161 KRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDpYDPEDDEDESLeeNQDLRSLIPFAIIGSNTEIENGGEQV 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287641 109 KARQYPWGVVQVENENHCDFVKLREMLICTNMEDLREQTHTRHYELYRRCKLEemgftdvgpenkpvSVQETYEAKRHEF 188
Cdd:COG5019   241 RGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLS--------------GLKNSGEPSLKEI 306

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1009287641 189 HGERQRKEE-EMKQMFVQRVKEKEAILKEAERELQAKFEHLKR 230
Cdd:COG5019   307 HEARLNEEErELKKKFTEKIREKEKRLEELEQNLIEERKELNS 349
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 32-164 3.47e-67

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: 210.09  E-value: 3.47e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287641  32 QIVNIIPVIAKADTVSKTELQKFKIKLMSELVSNGVQIYQFPTD--DDTIAKVNAAMNGQLPFAVVGSMDEVKVGNKMVK 109
Cdd:cd01850   141 KKVNIIPVIAKADTLTPEELTEFKKRIMEDIEENNIKIYKFPEDeeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVR 220

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1009287641 110 ARQYPWGVVQVENENHCDFVKLREMLICTNMEDLREQTHTRHYELYRRCKLEEMG 164
Cdd:cd01850   221 GRKYPWGVVEVENEEHCDFVKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
 32-162 2.25e-50

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: 167.09  E-value: 2.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287641  32 QIVNIIPVIAKADTVSKTELQKFKIKLMSELVSNGVQIYQFP---TDDDTIAKVNAAMNGQLPFAVVGSMDEVKVGNKMV 108
Cdd:pfam00735 139 EKVNIIPVIAKADTLTPDELQRFKKRIREEIERQNIPIYHFPdeeSDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKV 218

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1009287641 109 KARQYPWGVVQVENENHCDFVKLREMLICTNMEDLREQTHTRHYELYRRCKLEE 162
Cdd:pfam00735 219 RGRKYPWGVVEVENPSHCDFLKLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 32-230 2.85e-49

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 167.11  E-value: 2.85e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287641  32 QIVNIIPVIAKADTVSKTELQKFKIKLMSELVSNGVQIYQ-FPTDDDTIAKV--NAAMNGQLPFAVVGSMDEVKVGNKMV 108
Cdd:COG5019   161 KRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDpYDPEDDEDESLeeNQDLRSLIPFAIIGSNTEIENGGEQV 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287641 109 KARQYPWGVVQVENENHCDFVKLREMLICTNMEDLREQTHTRHYELYRRCKLEemgftdvgpenkpvSVQETYEAKRHEF 188
Cdd:COG5019   241 RGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLS--------------GLKNSGEPSLKEI 306

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1009287641 189 HGERQRKEE-EMKQMFVQRVKEKEAILKEAERELQAKFEHLKR 230
Cdd:COG5019   307 HEARLNEEErELKKKFTEKIREKEKRLEELEQNLIEERKELNS 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH