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Conserved domains on  [gi|156120821|ref|NP_001095557|]
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septin-14 [Bos taurus]

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 ...
 49-313 2.41e-138

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: 396.92  E-value: 2.41e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821  49 QGFFFNILCVGETGIGKSTLIDTLFNTSLKDKKSS-----HFYASVGLKIQTYELQENNVQLKLTVVKTVGYGDQINKEA 123
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPpapgeHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821 124 SYQPIVDYLDAQFESYLQEELKIKRSlGNYRDSRVHVCLYFISPTGHSLKSLDILTMKNIDSKVNIIPVIAKADAISKSD 203
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRN-RRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821 204 LQTFKCAIMNELISNGIQMYQFPTDNETSTHM--NSSMNGLLPFAVVGSTEEVKVGKRTVRGRQYPWGILQVENENHCDF 281
Cdd:cd01850  160 LTEFKKRIMEDIEENNIKIYKFPEDEEDEEEIeeNKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDF 239

                        250       260       270
                 ....*....|....*....|....*....|..
gi 156120821 282 VKLRDMLLCTNREDLKEQTHTRHYERYRRNRL 313
Cdd:cd01850  240 VKLRNLLIRTHLQDLKETTHNVHYENYRSEKL 271
GBP_C super family cl46256
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 335-388 8.43e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


The actual alignment was detected with superfamily member cd16269:

Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 37.94  E-value: 8.43e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 156120821 335 EAKRQELLEQCQREEEELKHKFMQRVKEKETAFKEAEKELQDKFEHLKKVQQEE 388
Cdd:cd16269  203 ERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKE 256
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 49-313 2.41e-138

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: 396.92  E-value: 2.41e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821  49 QGFFFNILCVGETGIGKSTLIDTLFNTSLKDKKSS-----HFYASVGLKIQTYELQENNVQLKLTVVKTVGYGDQINKEA 123
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPpapgeHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821 124 SYQPIVDYLDAQFESYLQEELKIKRSlGNYRDSRVHVCLYFISPTGHSLKSLDILTMKNIDSKVNIIPVIAKADAISKSD 203
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRN-RRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821 204 LQTFKCAIMNELISNGIQMYQFPTDNETSTHM--NSSMNGLLPFAVVGSTEEVKVGKRTVRGRQYPWGILQVENENHCDF 281
Cdd:cd01850  160 LTEFKKRIMEDIEENNIKIYKFPEDEEDEEEIeeNKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDF 239

                        250       260       270
                 ....*....|....*....|....*....|..
gi 156120821 282 VKLRDMLLCTNREDLKEQTHTRHYERYRRNRL 313
Cdd:cd01850  240 VKLRNLLIRTHLQDLKETTHNVHYENYRSEKL 271
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
 50-313 3.21e-112

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: 330.42  E-value: 3.21e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821   50 GFFFNILCVGETGIGKSTLIDTLFNTSLKDKKSsHFYAS------VGLKIQTYELQENNVQLKLTVVKTVGYGDQINKEA 123
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARG-IPGPSekikktVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821  124 SYQPIVDYLDAQFESYLQEELKIKRSlgNYRDSRVHVCLYFISPTGHSLKSLDILTMKNIDSKVNIIPVIAKADAISKSD 203
Cdd:pfam00735  80 CWRPIVEYIDEQYEQYLRDESGLNRK--SIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821  204 LQTFKCAIMNELISNGIQMYQFP---TDNETSTHMNSSMNGLLPFAVVGSTEEVKVGKRTVRGRQYPWGILQVENENHCD 280
Cdd:pfam00735 158 LQRFKKRIREEIERQNIPIYHFPdeeSDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCD 237

                         250       260       270
                  ....*....|....*....|....*....|...
gi 156120821  281 FVKLRDMLLCTNREDLKEQTHTRHYERYRRNRL 313
Cdd:pfam00735 238 FLKLRNMLIRTHLQDLKEVTHELHYETYRSEKL 270
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 34-390 1.13e-109

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 327.74  E-value: 1.13e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821  34 GFDCLAHQLVDKSVQQGFFFNILCVGETGIGKSTLIDTLFNTSLKDKKS----SHFYASVGLKIQTY--ELQENNVQLKL 107
Cdd:COG5019    5 GISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDETEiddiRAEGTSPTLEIKITkaELEEDGFHLNL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821 108 TVVKTVGYGDQINKEASYQPIVDYLDAQFESYLQEELKIKRSlGNYRDSRVHVCLYFISPTGHSLKSLDILTMKNIDSKV 187
Cdd:COG5019   85 TVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRN-PKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKRV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821 188 NIIPVIAKADAISKSDLQTFKCAIMNELISNGIQMYqFPTDNET----STHMNSSMNGLLPFAVVGSTEEVKVGKRTVRG 263
Cdd:COG5019  164 NLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVF-DPYDPEDdedeSLEENQDLRSLIPFAIIGSNTEIENGGEQVRG 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821 264 RQYPWGILQVENENHCDFVKLRDMLLCTNREDLKEQTHTRHYERYRRNRLHMMGftdmgpNNQPVSFQEIYEAKRQElle 343
Cdd:COG5019  243 RKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSGLK------NSGEPSLKEIHEARLNE--- 313

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 156120821 344 qcqrEEEELKHKFMQRVKEKETAFKEAEKELQDKFEHL--------KKVQQEETM 390
Cdd:COG5019  314 ----EERELKKKFTEKIREKEKRLEELEQNLIEERKELnskleeiqKKLEDLEKR 364
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 335-388 8.43e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 37.94  E-value: 8.43e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 156120821 335 EAKRQELLEQCQREEEELKHKFMQRVKEKETAFKEAEKELQDKFEHLKKVQQEE 388
Cdd:cd16269  203 ERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKE 256
PRK12704 PRK12704
phosphodiesterase; Provisional
 335-383 8.69e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.22  E-value: 8.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 156120821 335 EAKRQELLEQCQREEEELKHKFMQRVKEKETAFKEAEKELQDKFEHLKK 383
Cdd:PRK12704  52 EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR 100
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 49-313 2.41e-138

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: 396.92  E-value: 2.41e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821  49 QGFFFNILCVGETGIGKSTLIDTLFNTSLKDKKSS-----HFYASVGLKIQTYELQENNVQLKLTVVKTVGYGDQINKEA 123
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPpapgeHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821 124 SYQPIVDYLDAQFESYLQEELKIKRSlGNYRDSRVHVCLYFISPTGHSLKSLDILTMKNIDSKVNIIPVIAKADAISKSD 203
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRN-RRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821 204 LQTFKCAIMNELISNGIQMYQFPTDNETSTHM--NSSMNGLLPFAVVGSTEEVKVGKRTVRGRQYPWGILQVENENHCDF 281
Cdd:cd01850  160 LTEFKKRIMEDIEENNIKIYKFPEDEEDEEEIeeNKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDF 239

                        250       260       270
                 ....*....|....*....|....*....|..
gi 156120821 282 VKLRDMLLCTNREDLKEQTHTRHYERYRRNRL 313
Cdd:cd01850  240 VKLRNLLIRTHLQDLKETTHNVHYENYRSEKL 271
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
 50-313 3.21e-112

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: 330.42  E-value: 3.21e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821   50 GFFFNILCVGETGIGKSTLIDTLFNTSLKDKKSsHFYAS------VGLKIQTYELQENNVQLKLTVVKTVGYGDQINKEA 123
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARG-IPGPSekikktVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821  124 SYQPIVDYLDAQFESYLQEELKIKRSlgNYRDSRVHVCLYFISPTGHSLKSLDILTMKNIDSKVNIIPVIAKADAISKSD 203
Cdd:pfam00735  80 CWRPIVEYIDEQYEQYLRDESGLNRK--SIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821  204 LQTFKCAIMNELISNGIQMYQFP---TDNETSTHMNSSMNGLLPFAVVGSTEEVKVGKRTVRGRQYPWGILQVENENHCD 280
Cdd:pfam00735 158 LQRFKKRIREEIERQNIPIYHFPdeeSDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCD 237

                         250       260       270
                  ....*....|....*....|....*....|...
gi 156120821  281 FVKLRDMLLCTNREDLKEQTHTRHYERYRRNRL 313
Cdd:pfam00735 238 FLKLRNMLIRTHLQDLKEVTHELHYETYRSEKL 270
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 34-390 1.13e-109

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 327.74  E-value: 1.13e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821  34 GFDCLAHQLVDKSVQQGFFFNILCVGETGIGKSTLIDTLFNTSLKDKKS----SHFYASVGLKIQTY--ELQENNVQLKL 107
Cdd:COG5019    5 GISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDETEiddiRAEGTSPTLEIKITkaELEEDGFHLNL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821 108 TVVKTVGYGDQINKEASYQPIVDYLDAQFESYLQEELKIKRSlGNYRDSRVHVCLYFISPTGHSLKSLDILTMKNIDSKV 187
Cdd:COG5019   85 TVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRN-PKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKRV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821 188 NIIPVIAKADAISKSDLQTFKCAIMNELISNGIQMYqFPTDNET----STHMNSSMNGLLPFAVVGSTEEVKVGKRTVRG 263
Cdd:COG5019  164 NLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVF-DPYDPEDdedeSLEENQDLRSLIPFAIIGSNTEIENGGEQVRG 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821 264 RQYPWGILQVENENHCDFVKLRDMLLCTNREDLKEQTHTRHYERYRRNRLHMMGftdmgpNNQPVSFQEIYEAKRQElle 343
Cdd:COG5019  243 RKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSGLK------NSGEPSLKEIHEARLNE--- 313

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 156120821 344 qcqrEEEELKHKFMQRVKEKETAFKEAEKELQDKFEHL--------KKVQQEETM 390
Cdd:COG5019  314 ----EERELKKKFTEKIREKEKRLEELEQNLIEERKELnskleeiqKKLEDLEKR 364
YeeP COG3596
Predicted GTPase [General function prediction only];
53-132 6.56e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 54.00  E-value: 6.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821  53 FNILCVGETGIGKSTLIDTLFNTSLkdkksshfyASVGL------KIQTYELQENNVQLkLTVVKTVGYGDQINKEASYQ 126
Cdd:COG3596   40 PVIALVGKTGAGKSSLINALFGAEV---------AEVGVgrpctrEIQRYRLESDGLPG-LVLLDTPGLGEVNERDREYR 109


                 ....*.
gi 156120821 127 PIVDYL 132
Cdd:COG3596  110 ELRELL 115
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 58-218 1.15e-04

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: 42.44  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821  58 VGETGIGKSTLIDTLFNTSLKDKKSSHfyaSVGLKIQTYELQENNVQLKLTVVKTVGYGDqinkeasyqpivdyldaqfE 137
Cdd:cd00882    3 VGRGGVGKSSLLNALLGGEVGEVSDVP---GTTRDPDVYVKELDKGKVKLVLVDTPGLDE-------------------F 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156120821 138 SYLQEELKIKRSLgnyrdSRVHVCLYFISPTGH-SLKSLDILTMKNIDS-KVNIIPVIAKADAISKSDLQTFKCAIMNEL 215
Cdd:cd00882   61 GGLGREELARLLL-----RGADLILLVVDSTDReSEEDAKLLILRRLRKeGIPIILVGNKIDLLEEREVEELLRLEELAK 135


                 ...
gi 156120821 216 ISN 218
Cdd:cd00882  136 ILG 138
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 335-388 8.43e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 37.94  E-value: 8.43e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 156120821 335 EAKRQELLEQCQREEEELKHKFMQRVKEKETAFKEAEKELQDKFEHLKKVQQEE 388
Cdd:cd16269  203 ERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKE 256
PRK12704 PRK12704
phosphodiesterase; Provisional
 335-383 8.69e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.22  E-value: 8.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 156120821 335 EAKRQELLEQCQREEEELKHKFMQRVKEKETAFKEAEKELQDKFEHLKK 383
Cdd:PRK12704  52 EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR 100
 
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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