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Conserved domains on  [gi|153252198|ref|NP_997249|]
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septin-14 [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 ...
 49-317 1.88e-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: 397.30  E-value: 1.88e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198  49 QGFTFNILCVGETGIGKSTLIDTLFNTNLKDNKSS-----HFYSNVGLQIQTYELQESNVQLKLTVVETVGYGDQIDKEA 123
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPpapgeHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 124 SYQPIVDYIDAQFEAYLQEELKIKRSLFeYHDSRVHVCLYFISPTGHSLKSLDLLTMKNLDSKVNIIPLIAKADTISKND 203
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRNRR-IPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 204 LQTFKNKIMSELISNGIQIYQLPTDEET--AAQANSSVSGLLPFAVVGSTDEVKVGKRMVRGRHYPWGVLQVENENHCDF 281
Cdd:cd01850  160 LTEFKKRIMEDIEENNIKIYKFPEDEEDeeEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDF 239

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 153252198 282 VKLRDMLLCTNMENLKEKTHTQHYECYRYQKLQKMG 317
Cdd:cd01850  240 VKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
PRK12704 super family cl36166
phosphodiesterase; Provisional
 335-432 2.80e-04

phosphodiesterase; Provisional


The actual alignment was detected with superfamily member PRK12704:

Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 2.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 335 EAKRQEFYDQCQREEEELKQRFMQRVKEKEATFKEAEKELQDKFEHLKmiqqEEIRKLEEEKKQLEGEIIDFYKMKAASE 414
Cdd:PRK12704  52 EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD----RKLELLEKREEELEKKEKELEQKQQELE 127

                         90
                 ....*....|....*...
gi 153252198 415 ALQTQLstDTKKDKHRKK 432
Cdd:PRK12704 128 KKEEEL--EELIEEQLQE 143
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 49-317 1.88e-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: 397.30  E-value: 1.88e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198  49 QGFTFNILCVGETGIGKSTLIDTLFNTNLKDNKSS-----HFYSNVGLQIQTYELQESNVQLKLTVVETVGYGDQIDKEA 123
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPpapgeHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 124 SYQPIVDYIDAQFEAYLQEELKIKRSLFeYHDSRVHVCLYFISPTGHSLKSLDLLTMKNLDSKVNIIPLIAKADTISKND 203
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRNRR-IPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 204 LQTFKNKIMSELISNGIQIYQLPTDEET--AAQANSSVSGLLPFAVVGSTDEVKVGKRMVRGRHYPWGVLQVENENHCDF 281
Cdd:cd01850  160 LTEFKKRIMEDIEENNIKIYKFPEDEEDeeEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDF 239

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 153252198 282 VKLRDMLLCTNMENLKEKTHTQHYECYRYQKLQKMG 317
Cdd:cd01850  240 VKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 34-403 9.44e-115

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 340.84  E-value: 9.44e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198  34 GFECLPNQLVSRSIRQGFTFNILCVGETGIGKSTLIDTLFNTNLKDNKS------SHFYSNVGLQIQTYELQESNVQLKL 107
Cdd:COG5019    5 GISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDETEiddiraEGTSPTLEIKITKAELEEDGFHLNL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 108 TVVETVGYGDQIDKEASYQPIVDYIDAQFEAYLQEELKIKRSLFeYHDSRVHVCLYFISPTGHSLKSLDLLTMKNLDSKV 187
Cdd:COG5019   85 TVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPK-FKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKRV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 188 NIIPLIAKADTISKNDLQTFKNKIMSELISNGIQIYQlPTDEETAA----QANSSVSGLLPFAVVGSTDEVKVGKRMVRG 263
Cdd:COG5019  164 NLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFD-PYDPEDDEdeslEENQDLRSLIPFAIIGSNTEIENGGEQVRG 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 264 RHYPWGVLQVENENHCDFVKLRDMLLCTNMENLKEKTHTQHYECYRYQKLQKMGftdvgpNNQPVSFQEIFEAKRQEfyd 343
Cdd:COG5019  243 RKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSGLK------NSGEPSLKEIHEARLNE--- 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 344 qcqrEEEELKQRFMQRVKEKEATFKEAEKELQDKFEHLKMIQQEEIRKLEEEKKQLEGEI 403
Cdd:COG5019  314 ----EERELKKKFTEKIREKEKRLEELEQNLIEERKELNSKLEEIQKKLEDLEKRLEKLK 369
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
 50-315 2.50e-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: 330.80  E-value: 2.50e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198   50 GFTFNILCVGETGIGKSTLIDTLFNTNLKDNKSSHFYS-----NVGLQIQTYELQESNVQLKLTVVETVGYGDQIDKEAS 124
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSekikkTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198  125 YQPIVDYIDAQFEAYLQEELKIKRSLFEyhDSRVHVCLYFISPTGHSLKSLDLLTMKNLDSKVNIIPLIAKADTISKNDL 204
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIK--DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDEL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198  205 QTFKNKIMSELISNGIQIYQLP---TDEETAAQANSSVSGLLPFAVVGSTDEVKVGKRMVRGRHYPWGVLQVENENHCDF 281
Cdd:pfam00735 159 QRFKKRIREEIERQNIPIYHFPdeeSDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDF 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 153252198  282 VKLRDMLLCTNMENLKEKTHTQHYECYRYQKLQK 315
Cdd:pfam00735 239 LKLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
PRK12704 PRK12704
phosphodiesterase; Provisional
 335-432 2.80e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 2.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 335 EAKRQEFYDQCQREEEELKQRFMQRVKEKEATFKEAEKELQDKFEHLKmiqqEEIRKLEEEKKQLEGEIIDFYKMKAASE 414
Cdd:PRK12704  52 EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD----RKLELLEKREEELEKKEKELEQKQQELE 127

                         90
                 ....*....|....*...
gi 153252198 415 ALQTQLstDTKKDKHRKK 432
Cdd:PRK12704 128 KKEEEL--EELIEEQLQE 143
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 331-425 1.39e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.22  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 331 QEIFEAKRQefYDQCQREEEELKQRFMQRVKEKEATFKEAEKELQDKFEHLKMIQQEE---IRKLEEEKKQLEGEIIDFY 407
Cdd:COG0542  411 EELDELERR--LEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEkelIEEIQELKEELEQRYGKIP 488

                         90
                 ....*....|....*...
gi 153252198 408 KMKAASEALQTQLSTDTK 425
Cdd:COG0542  489 ELEKELAELEEELAELAP 506
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 328-403 2.09e-03

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 39.59  E-value: 2.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153252198  328 VSFQEIFE--AKRQEFYDQCQREEEELKQRFMQRVKEKEATFKEAEKELQDKFEHLKMIQQEEIRKLEEEKKQLEGEI 403
Cdd:pfam03961 149 VDFPELKEklEELEKELEELEEELEKLKKRLKKLPKKARGQLPPEKREQLEKLLETKNKLSEELEELEEELKELKEEL 226
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 339-432 5.11e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 38.89  E-value: 5.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 339 QEFYDQCQREEEELKQrFMQRVKEKEATFKEAEKELQDKF-EHLKMIQQEEIRKLEEEKKQLEGEIIDfyKMKAASEALQ 417
Cdd:cd22656  131 KKYQDKAAKVVDKLTD-FENQTEKDQTALETLEKALKDLLtDEGGAIARKEIKDLQKELEKLNEEYAA--KLKAKIDELK 207

                         90
                 ....*....|....*
gi 153252198 418 TQLSTDTKKDKHRKK 432
Cdd:cd22656  208 ALIADDEAKLAAALR 222
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 49-317 1.88e-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: 397.30  E-value: 1.88e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198  49 QGFTFNILCVGETGIGKSTLIDTLFNTNLKDNKSS-----HFYSNVGLQIQTYELQESNVQLKLTVVETVGYGDQIDKEA 123
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPpapgeHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 124 SYQPIVDYIDAQFEAYLQEELKIKRSLFeYHDSRVHVCLYFISPTGHSLKSLDLLTMKNLDSKVNIIPLIAKADTISKND 203
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRNRR-IPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 204 LQTFKNKIMSELISNGIQIYQLPTDEET--AAQANSSVSGLLPFAVVGSTDEVKVGKRMVRGRHYPWGVLQVENENHCDF 281
Cdd:cd01850  160 LTEFKKRIMEDIEENNIKIYKFPEDEEDeeEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDF 239

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 153252198 282 VKLRDMLLCTNMENLKEKTHTQHYECYRYQKLQKMG 317
Cdd:cd01850  240 VKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 34-403 9.44e-115

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 340.84  E-value: 9.44e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198  34 GFECLPNQLVSRSIRQGFTFNILCVGETGIGKSTLIDTLFNTNLKDNKS------SHFYSNVGLQIQTYELQESNVQLKL 107
Cdd:COG5019    5 GISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDETEiddiraEGTSPTLEIKITKAELEEDGFHLNL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 108 TVVETVGYGDQIDKEASYQPIVDYIDAQFEAYLQEELKIKRSLFeYHDSRVHVCLYFISPTGHSLKSLDLLTMKNLDSKV 187
Cdd:COG5019   85 TVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPK-FKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKRV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 188 NIIPLIAKADTISKNDLQTFKNKIMSELISNGIQIYQlPTDEETAA----QANSSVSGLLPFAVVGSTDEVKVGKRMVRG 263
Cdd:COG5019  164 NLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFD-PYDPEDDEdeslEENQDLRSLIPFAIIGSNTEIENGGEQVRG 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 264 RHYPWGVLQVENENHCDFVKLRDMLLCTNMENLKEKTHTQHYECYRYQKLQKMGftdvgpNNQPVSFQEIFEAKRQEfyd 343
Cdd:COG5019  243 RKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSGLK------NSGEPSLKEIHEARLNE--- 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 344 qcqrEEEELKQRFMQRVKEKEATFKEAEKELQDKFEHLKMIQQEEIRKLEEEKKQLEGEI 403
Cdd:COG5019  314 ----EERELKKKFTEKIREKEKRLEELEQNLIEERKELNSKLEEIQKKLEDLEKRLEKLK 369
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
 50-315 2.50e-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: 330.80  E-value: 2.50e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198   50 GFTFNILCVGETGIGKSTLIDTLFNTNLKDNKSSHFYS-----NVGLQIQTYELQESNVQLKLTVVETVGYGDQIDKEAS 124
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSekikkTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198  125 YQPIVDYIDAQFEAYLQEELKIKRSLFEyhDSRVHVCLYFISPTGHSLKSLDLLTMKNLDSKVNIIPLIAKADTISKNDL 204
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIK--DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDEL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198  205 QTFKNKIMSELISNGIQIYQLP---TDEETAAQANSSVSGLLPFAVVGSTDEVKVGKRMVRGRHYPWGVLQVENENHCDF 281
Cdd:pfam00735 159 QRFKKRIREEIERQNIPIYHFPdeeSDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDF 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 153252198  282 VKLRDMLLCTNMENLKEKTHTQHYECYRYQKLQK 315
Cdd:pfam00735 239 LKLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
YeeP COG3596
Predicted GTPase [General function prediction only];
45-132 4.30e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 54.39  E-value: 4.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198  45 RSIRQGFTFNILCVGETGIGKSTLIDTLFNTNLkdnksshfySNVGL------QIQTYELQESNVQLkLTVVETVGYGDQ 118
Cdd:COG3596   32 RLLVELPPPVIALVGKTGAGKSSLINALFGAEV---------AEVGVgrpctrEIQRYRLESDGLPG-LVLLDTPGLGEV 101

                         90
                 ....*....|....
gi 153252198 119 IDKEASYQPIVDYI 132
Cdd:COG3596  102 NERDREYRELRELL 115
PRK12704 PRK12704
phosphodiesterase; Provisional
 335-432 2.80e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 2.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 335 EAKRQEFYDQCQREEEELKQRFMQRVKEKEATFKEAEKELQDKFEHLKmiqqEEIRKLEEEKKQLEGEIIDFYKMKAASE 414
Cdd:PRK12704  52 EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD----RKLELLEKREEELEKKEKELEQKQQELE 127

                         90
                 ....*....|....*...
gi 153252198 415 ALQTQLstDTKKDKHRKK 432
Cdd:PRK12704 128 KKEEEL--EELIEEQLQE 143
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 58-218 6.36e-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: 40.13  E-value: 6.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198  58 VGETGIGKSTLIDTLFNTNLKDNKSSHFysnVGLQIQTYELQESNVQLKLTVVETVGYGDqidkeasyqpivdyidaqfE 137
Cdd:cd00882    3 VGRGGVGKSSLLNALLGGEVGEVSDVPG---TTRDPDVYVKELDKGKVKLVLVDTPGLDE-------------------F 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 138 AYLQEELKIKRSLfeyhdSRVHVCLYFISPTGH-SLKSLDLLTMKNLDS-KVNIIPLIAKADTISKNDLQTFKNKIMSEL 215
Cdd:cd00882   61 GGLGREELARLLL-----RGADLILLVVDSTDReSEEDAKLLILRRLRKeGIPIILVGNKIDLLEEREVEELLRLEELAK 135


                 ...
gi 153252198 216 ISN 218
Cdd:cd00882  136 ILG 138
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 331-425 1.39e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.22  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 331 QEIFEAKRQefYDQCQREEEELKQRFMQRVKEKEATFKEAEKELQDKFEHLKMIQQEE---IRKLEEEKKQLEGEIIDFY 407
Cdd:COG0542  411 EELDELERR--LEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEkelIEEIQELKEELEQRYGKIP 488

                         90
                 ....*....|....*...
gi 153252198 408 KMKAASEALQTQLSTDTK 425
Cdd:COG0542  489 ELEKELAELEEELAELAP 506
PRK12704 PRK12704
phosphodiesterase; Provisional
 331-415 1.79e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 331 QEIFEAKRQEFydqcQREEEELKQRfMQRVKEKEATFKEAEKELQDKFEHLKMIQQEEIRK--LEEEKKQLEGEI---ID 405
Cdd:PRK12704 102 LELLEKREEEL----EKKEKELEQK-QQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVEEEARHEAavlIK 176

                         90
                 ....*....|
gi 153252198 406 FYKMKAASEA 415
Cdd:PRK12704 177 EIEEEAKEEA 186
polC PRK00448
DNA polymerase III PolC; Validated
 311-405 1.89e-03

DNA polymerase III PolC; Validated


Pssm-ID: 234767 [Multi-domain]  Cd Length: 1437  Bit Score: 40.59  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198  311 QKLQKMGFtdvgPNNQPVSFQEIFEAKRQEFYDQCQREEEELKQRFMQRVKEKEATFKEAEKELQDKFEHL---KMIQQE 387
Cdd:PRK00448  149 KQYEKFGF----GILKIDFEIDDSKEELEKFEAQKEEEDEKLAKEALEAMKKLEAEKKKQSKNFDPKEGPVqigKKIDKE 224

                          90       100
                  ....*....|....*....|...
gi 153252198  388 EIRKL-----EEEKKQLEGEIID 405
Cdd:PRK00448  225 EITPMkeineEERRVVVEGYVFK 247
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 328-403 2.09e-03

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 39.59  E-value: 2.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153252198  328 VSFQEIFE--AKRQEFYDQCQREEEELKQRFMQRVKEKEATFKEAEKELQDKFEHLKMIQQEEIRKLEEEKKQLEGEI 403
Cdd:pfam03961 149 VDFPELKEklEELEKELEELEEELEKLKKRLKKLPKKARGQLPPEKREQLEKLLETKNKLSEELEELEEELKELKEEL 226
PTZ00121 PTZ00121
MAEBL; Provisional
 335-432 2.27e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198  335 EAKRQEfydQCQREEEELKQRFMQRVKEKEATFKEAEKelQDKFEHLKMIQQEEIRKLEEEKKQLEGEIIDFYKMKAASE 414
Cdd:PTZ00121 1666 EAKKAE---EDKKKAEEAKKAEEDEKKAAEALKKEAEE--AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740

                          90
                  ....*....|....*...
gi 153252198  415 AlQTQLSTDTKKDKHRKK 432
Cdd:PTZ00121 1741 E-DKKKAEEAKKDEEEKK 1757
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 342-403 3.31e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 3.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153252198 342 YDQCQREEEELKQR----------FMQRVKEKEATFKEAEKELQDKFEHLKMIQQE---EIRKLEEEKKQLEGEI 403
Cdd:COG1579   91 YEALQKEIESLKRRisdledeileLMERIEELEEELAELEAELAELEAELEEKKAEldeELAELEAELEELEAER 165
PTZ00121 PTZ00121
MAEBL; Provisional
 347-432 3.32e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198  347 REEEELKQRFMQRVKEKEATFKEAEkELQDKFEHLKMIQQEEIRKLEEEKKQLEGEIIDFYKMKAASEALQTQLSTDTKK 426
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAE-ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704


                  ....*.
gi 153252198  427 DKHRKK 432
Cdd:PTZ00121 1705 EELKKK 1710
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 347-420 4.02e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.21  E-value: 4.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153252198  347 REEEELKQR-FMQRVKEKEATFKEAEKELQDkfehlkmiQQEEIRKLEEEKKQLEGEIIDFYKMKAASEALQTQL 420
Cdd:pfam20492   1 REEAEREKQeLEERLKQYEEETKKAQEELEE--------SEETAEELEEERRQAEEEAERLEQKRQEAEEEKERL 67
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 342-427 4.32e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 38.94  E-value: 4.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 342 YDQCQREEEELKQRFMQRVKEKEATFKEAEkELQDKFEHLkmiqQEEIRKLEEEKKQLEGEiidFYKMKAASEALQTQLS 421
Cdd:COG4026  130 YNELREELLELKEKIDEIAKEKEKLTKENE-ELESELEEL----REEYKKLREENSILEEE---FDNIKSEYSDLKSRFE 201


                 ....*.
gi 153252198 422 TDTKKD 427
Cdd:COG4026  202 ELLKKR 207
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 339-432 5.11e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 38.89  E-value: 5.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 339 QEFYDQCQREEEELKQrFMQRVKEKEATFKEAEKELQDKF-EHLKMIQQEEIRKLEEEKKQLEGEIIDfyKMKAASEALQ 417
Cdd:cd22656  131 KKYQDKAAKVVDKLTD-FENQTEKDQTALETLEKALKDLLtDEGGAIARKEIKDLQKELEKLNEEYAA--KLKAKIDELK 207

                         90
                 ....*....|....*
gi 153252198 418 TQLSTDTKKDKHRKK 432
Cdd:cd22656  208 ALIADDEAKLAAALR 222
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 333-402 7.35e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 36.94  E-value: 7.35e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198  333 IFEAKRQEFYDQCQREEEELKQRFMQRVKEKEATFKEAEKELQDkfehlkmiQQEEIRKLEEEKKQLEGE 402
Cdd:pfam05672  15 ILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERAR--------REEEARRLEEERRREEEE 76
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 336-432 8.15e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 38.25  E-value: 8.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 336 AKRQEFYDQCQREEEELKQ-RFMQRVKEKEatfKEAEKELQDKfehlkmIQQEEIRKLEEEKKQL--EGEIIDFYKMKAA 412
Cdd:PRK09510  78 EEQRKKKEQQQAEELQQKQaAEQERLKQLE---KERLAAQEQK------KQAEEAAKQAALKQKQaeEAAAKAAAAAKAK 148

                         90       100
                 ....*....|....*....|
gi 153252198 413 SEALQTQLSTDTKKDKHRKK 432
Cdd:PRK09510 149 AEAEAKRAAAAAKKAAAEAK 168
PRK12704 PRK12704
phosphodiesterase; Provisional
 331-405 9.40e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.22  E-value: 9.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153252198 331 QEIFEAKRQEFYDQCQREEEELKQ---RFMQR---VKEKEATFKEAEKELQDKFEHLKmIQQEEIRKLEEEKKQLEGEII 404
Cdd:PRK12704  63 KEEIHKLRNEFEKELRERRNELQKlekRLLQKeenLDRKLELLEKREEELEKKEKELE-QKQQELEKKEEELEELIEEQL 141


                 .
gi 153252198 405 D 405
Cdd:PRK12704 142 Q 142
 
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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