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Conserved domains on  [gi|1154885812|ref|NP_001336236|]
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septin-2 isoform h [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P-loop_NTPase super family cl21455
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
1-139 2.94e-80

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 pfam00735:

Pssm-ID: 354812  Cd Length: 273  Bit Score: 239.89  E-value: 2.94e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154885812   1 MKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHNIKIYHLPDAESDEDEDfKEQTRLLKASIPFSVVGSNQLIE 80
Cdd:pfam00735 135 MKKLSEKVNIIPVIAKADTLTPDELQRFKKRIRADIERQNIKIYKFPDEESDEDEE-KELTEQLKSSIPFAIVGSNTEIE 213
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154885812  81 AKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLI-THMQDLQEVTQDLHYENFRSERLKR 139
Cdd:pfam00735 214 NDGKKVRGRKYPWGVVEVENPSHCDFVKLRNLLIrTHLQDLKEVTHELHYENYRSEKLSA 273
 
Name Accession Description Interval E-value
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
1-139 2.94e-80

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 characteristic 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: 307057  Cd Length: 273  Bit Score: 239.89  E-value: 2.94e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154885812   1 MKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHNIKIYHLPDAESDEDEDfKEQTRLLKASIPFSVVGSNQLIE 80
Cdd:pfam00735 135 MKKLSEKVNIIPVIAKADTLTPDELQRFKKRIRADIERQNIKIYKFPDEESDEDEE-KELTEQLKSSIPFAIVGSNTEIE 213
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154885812  81 AKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLI-THMQDLQEVTQDLHYENFRSERLKR 139
Cdd:pfam00735 214 NDGKKVRGRKYPWGVVEVENPSHCDFVKLRNLLIrTHLQDLKEVTHELHYENYRSEKLSA 273
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
1-141 4.26e-77

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: 231.67  E-value: 4.26e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154885812   1 MKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHNIKIYHLPDAEsdEDEDFKEQTRLLKASIPFSVVGSNQLIE 80
Cdd:cd01850   136 MKKLSKKVNIIPVIAKADTLTPEELTEFKKRIMEDIEENNIKIYKFPEDE--EDEEEIEENKKLKSLIPFAIVGSNEEVE 213
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154885812  81 AKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLI-THMQDLQEVTQDLHYENFRSERLKRGG 141
Cdd:cd01850   214 VNGKKVRGRKYPWGVVEVENEEHCDFVKLRNLLIrTHLQDLKETTHNVHYENYRSEKLEALK 275
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
1-165 2.94e-54

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


Pssm-ID: 227352  Cd Length: 373  Bit Score: 176.36  E-value: 2.94e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154885812   1 MKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHNIKIYHLPDAESDEDEDFkEQTRLLKASIPFSVVGSNQLIE 80
Cdd:COG5019   156 MKRLSKRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESL-EENQDLRSLIPFAIIGSNTEIE 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154885812  81 AKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLI-THMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQILLEKE 159
Cdd:COG5019   235 NGGEQVRGRKYPWGVVEIDDEEHSDFKKLRNLLIrTHLQELKETTENLLYENYRTEKLSGLKNSGEPSLKEIHEARLNEE 314

                  ....*.
gi 1154885812 160 AELRRM 165
Cdd:COG5019   315 ERELKK 320
 
Name Accession Description Interval E-value
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
1-139 2.94e-80

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 characteristic 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: 307057  Cd Length: 273  Bit Score: 239.89  E-value: 2.94e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154885812   1 MKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHNIKIYHLPDAESDEDEDfKEQTRLLKASIPFSVVGSNQLIE 80
Cdd:pfam00735 135 MKKLSEKVNIIPVIAKADTLTPDELQRFKKRIRADIERQNIKIYKFPDEESDEDEE-KELTEQLKSSIPFAIVGSNTEIE 213
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154885812  81 AKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLI-THMQDLQEVTQDLHYENFRSERLKR 139
Cdd:pfam00735 214 NDGKKVRGRKYPWGVVEVENPSHCDFVKLRNLLIrTHLQDLKEVTHELHYENYRSEKLSA 273
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
1-141 4.26e-77

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: 231.67  E-value: 4.26e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154885812   1 MKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHNIKIYHLPDAEsdEDEDFKEQTRLLKASIPFSVVGSNQLIE 80
Cdd:cd01850   136 MKKLSKKVNIIPVIAKADTLTPEELTEFKKRIMEDIEENNIKIYKFPEDE--EDEEEIEENKKLKSLIPFAIVGSNEEVE 213
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154885812  81 AKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLI-THMQDLQEVTQDLHYENFRSERLKRGG 141
Cdd:cd01850   214 VNGKKVRGRKYPWGVVEVENEEHCDFVKLRNLLIrTHLQDLKETTHNVHYENYRSEKLEALK 275
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
1-165 2.94e-54

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


Pssm-ID: 227352  Cd Length: 373  Bit Score: 176.36  E-value: 2.94e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154885812   1 MKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHNIKIYHLPDAESDEDEDFkEQTRLLKASIPFSVVGSNQLIE 80
Cdd:COG5019   156 MKRLSKRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESL-EENQDLRSLIPFAIIGSNTEIE 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154885812  81 AKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLI-THMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQILLEKE 159
Cdd:COG5019   235 NGGEQVRGRKYPWGVVEIDDEEHSDFKKLRNLLIrTHLQELKETTENLLYENYRTEKLSGLKNSGEPSLKEIHEARLNEE 314

                  ....*.
gi 1154885812 160 AELRRM 165
Cdd:COG5019   315 ERELKK 320
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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