septin-12 isoform 1 [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
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 ... |
45-272 | 1.51e-122 | ||||
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: 352.23 E-value: 1.51e-122
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| Name | Accession | Description | Interval | E-value | |||||
| CDC_Septin | cd01850 | CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ... |
45-272 | 1.51e-122 | |||||
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: 352.23 E-value: 1.51e-122
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| Septin | pfam00735 | Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ... |
45-272 | 1.62e-102 | |||||
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: 301.53 E-value: 1.62e-102
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| CDC3 | COG5019 | Septin family protein [Cell cycle control, cell division, chromosome partitioning, ... |
26-272 | 6.14e-98 | |||||
Septin family protein [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]; Pssm-ID: 227352 [Multi-domain] Cd Length: 373 Bit Score: 293.46 E-value: 6.14e-98
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| 3a0901s04IAP86 | TIGR00993 | chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ... |
46-122 | 2.19e-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: 43.02 E-value: 2.19e-04
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| PRK00098 | PRK00098 | GTPase RsgA; Reviewed |
51-114 | 4.22e-04 | |||||
GTPase RsgA; Reviewed Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 41.34 E-value: 4.22e-04
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| Name | Accession | Description | Interval | E-value | |||||
| CDC_Septin | cd01850 | CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ... |
45-272 | 1.51e-122 | |||||
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: 352.23 E-value: 1.51e-122
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| Septin | pfam00735 | Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ... |
45-272 | 1.62e-102 | |||||
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: 301.53 E-value: 1.62e-102
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| CDC3 | COG5019 | Septin family protein [Cell cycle control, cell division, chromosome partitioning, ... |
26-272 | 6.14e-98 | |||||
Septin family protein [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton]; Pssm-ID: 227352 [Multi-domain] Cd Length: 373 Bit Score: 293.46 E-value: 6.14e-98
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| YeeP | COG3596 | Predicted GTPase [General function prediction only]; |
30-141 | 1.69e-09 | |||||
Predicted GTPase [General function prediction only]; Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 57.85 E-value: 1.69e-09
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| Toc34_like | cd01853 | Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ... |
46-131 | 3.85e-06 | |||||
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: 47.31 E-value: 3.85e-06
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| Ras_like_GTPase | cd00882 | Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
52-217 | 3.93e-06 | |||||
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: 46.30 E-value: 3.93e-06
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| 3a0901s04IAP86 | TIGR00993 | chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ... |
46-122 | 2.19e-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: 43.02 E-value: 2.19e-04
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| small_GTP | TIGR00231 | small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
47-113 | 3.04e-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: 40.82 E-value: 3.04e-04
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| PRK00098 | PRK00098 | GTPase RsgA; Reviewed |
51-114 | 4.22e-04 | |||||
GTPase RsgA; Reviewed Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 41.34 E-value: 4.22e-04
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| MMR_HSR1 | pfam01926 | 50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
49-114 | 4.67e-04 | |||||
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: 39.14 E-value: 4.67e-04
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| AIG1 | pfam04548 | AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria. |
49-113 | 8.57e-04 | |||||
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria. Pssm-ID: 398307 [Multi-domain] Cd Length: 200 Bit Score: 39.90 E-value: 8.57e-04
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| Era_like | cd00880 | E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
52-116 | 1.25e-03 | |||||
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 38.77 E-value: 1.25e-03
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| DLP_2 | cd09912 | Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
48-121 | 3.37e-03 | |||||
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: 37.91 E-value: 3.37e-03
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| NOG | cd01897 | Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ... |
48-204 | 7.23e-03 | |||||
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in eukaryotes ranging from trypanosomes to humans. NOG1 is functionally linked to ribosome biogenesis and found in association with the nuclear pore complexes and identified in many preribosomal complexes. Thus, defects in NOG1 can lead to defects in 60S biogenesis. The S. cerevisiae NOG1 gene is essential for cell viability, and mutations in the predicted G motifs abrogate function. It is a member of the ODN family of GTP-binding proteins that also includes the bacterial Obg and DRG proteins. Pssm-ID: 206684 [Multi-domain] Cd Length: 167 Bit Score: 36.77 E-value: 7.23e-03
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