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Conserved domains on  [gi|1034640533|ref|XP_016863892|]
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septin-11 isoform X4 [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

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 ...
38-306 3.34e-151

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: 429.66  E-value: 3.34e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533  38 QGFCFNILCVGETGIGKSTLMDTLFNTKF-----ESDPATHNEPGVRLKARSYELQESNVRLKLTIVDTVGFGDQINKDD 112
Cdd:cd01850     1 RGFQFNIMVVGESGLGKSTFINTLFGTKLypskyPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533 113 SYKPIVEYIDAQFEAYLQEELKIKRSLfNYHDTRIHACLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADTIAKNE 192
Cdd:cd01850    81 CWKPIVDYIDDQFESYLREESRINRNR-RIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533 193 LHKFKSKIMSELVSNGVQIYQFPTDEET--VAEINATMSVHLPFAVVGSTEEVKIGNKMAKARQYPWGVVQVENENHCDF 270
Cdd:cd01850   160 LTEFKKRIMEDIEENNIKIYKFPEDEEDeeEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDF 239
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034640533 271 VKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMG 306
Cdd:cd01850   240 VKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
38-306 3.34e-151

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: 429.66  E-value: 3.34e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533  38 QGFCFNILCVGETGIGKSTLMDTLFNTKF-----ESDPATHNEPGVRLKARSYELQESNVRLKLTIVDTVGFGDQINKDD 112
Cdd:cd01850     1 RGFQFNIMVVGESGLGKSTFINTLFGTKLypskyPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533 113 SYKPIVEYIDAQFEAYLQEELKIKRSLfNYHDTRIHACLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADTIAKNE 192
Cdd:cd01850    81 CWKPIVDYIDDQFESYLREESRINRNR-RIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533 193 LHKFKSKIMSELVSNGVQIYQFPTDEET--VAEINATMSVHLPFAVVGSTEEVKIGNKMAKARQYPWGVVQVENENHCDF 270
Cdd:cd01850   160 LTEFKKRIMEDIEENNIKIYKFPEDEEDeeEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDF 239
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034640533 271 VKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMG 306
Cdd:cd01850   240 VKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
39-304 7.33e-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: 329.65  E-value: 7.33e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533  39 GFCFNILCVGETGIGKSTLMDTLFNTKFESD-----PATHNEPGVRLKARSYELQESNVRLKLTIVDTVGFGDQINKDDS 113
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRArgipgPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533 114 YKPIVEYIDAQFEAYLQEELKIKRSLFNyhDTRIHACLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADTIAKNEL 193
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIK--DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDEL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533 194 HKFKSKIMSELVSNGVQIYQFP-TDEETVAEINATMSVH--LPFAVVGSTEEVKIGNKMAKARQYPWGVVQVENENHCDF 270
Cdd:pfam00735 159 QRFKKRIREEIERQNIPIYHFPdEESDEDEEKELNEQLKssIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDF 238
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034640533 271 VKLREMLIRVNMEDLREQTHTRHYELYRRCKLEE 304
Cdd:pfam00735 239 LKLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
19-341 5.59e-103

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 310.41  E-value: 5.59e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533  19 SGHVGFDSLPDQLVNKSTSQGFCFNILCVGETGIGKSTLMDTLFNTK------FESDPATHNEPGVRLKARSYELQESNV 92
Cdd:COG5019     1 NGYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSlvdeteIDDIRAEGTSPTLEIKITKAELEEDGF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533  93 RLKLTIVDTVGFGDQINKDDSYKPIVEYIDAQFEAYLQEELKIKRSLFnYHDTRIHACLYFIAPTGHSLKSLDLVTMKKL 172
Cdd:COG5019    81 HLNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPK-FKDTRVHACLYFIRPTGHGLKPLDIEAMKRL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533 173 DSKVNIIPIIAKADTIAKNELHKFKSKIMSELVSNGVQIYQ-FPTDEETVAEINATMSVH--LPFAVVGSTEEVKIGNKM 249
Cdd:COG5019   160 SKRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDpYDPEDDEDESLEENQDLRslIPFAIIGSNTEIENGGEQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533 250 AKARQYPWGVVQVENENHCDFVKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMGfkdtdpDSKPFSLQETYEAKRNE 329
Cdd:COG5019   240 VRGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSGLK------NSGEPSLKEIHEARLNE 313
                         330
                  ....*....|..
gi 1034640533 330 FLGELQKKEEEM 341
Cdd:COG5019   314 EERELKKKFTEK 325
PLN03118 PLN03118
Rab family protein; Provisional
34-103 4.12e-04

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 41.58  E-value: 4.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533  34 KSTSQGFCFNILCVGETGIGKSTLMDTLFNTKFESDPAThnePGVRLKARsyELQESNVRLKLTIVDTVG 103
Cdd:PLN03118    7 QSSGYDLSFKILLIGDSGVGKSSLLVSFISSSVEDLAPT---IGVDFKIK--QLTVGGKRLKLTIWDTAG 71
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
38-306 3.34e-151

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: 429.66  E-value: 3.34e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533  38 QGFCFNILCVGETGIGKSTLMDTLFNTKF-----ESDPATHNEPGVRLKARSYELQESNVRLKLTIVDTVGFGDQINKDD 112
Cdd:cd01850     1 RGFQFNIMVVGESGLGKSTFINTLFGTKLypskyPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533 113 SYKPIVEYIDAQFEAYLQEELKIKRSLfNYHDTRIHACLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADTIAKNE 192
Cdd:cd01850    81 CWKPIVDYIDDQFESYLREESRINRNR-RIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533 193 LHKFKSKIMSELVSNGVQIYQFPTDEET--VAEINATMSVHLPFAVVGSTEEVKIGNKMAKARQYPWGVVQVENENHCDF 270
Cdd:cd01850   160 LTEFKKRIMEDIEENNIKIYKFPEDEEDeeEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDF 239
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034640533 271 VKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMG 306
Cdd:cd01850   240 VKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
39-304 7.33e-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: 329.65  E-value: 7.33e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533  39 GFCFNILCVGETGIGKSTLMDTLFNTKFESD-----PATHNEPGVRLKARSYELQESNVRLKLTIVDTVGFGDQINKDDS 113
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRArgipgPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533 114 YKPIVEYIDAQFEAYLQEELKIKRSLFNyhDTRIHACLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADTIAKNEL 193
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIK--DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDEL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533 194 HKFKSKIMSELVSNGVQIYQFP-TDEETVAEINATMSVH--LPFAVVGSTEEVKIGNKMAKARQYPWGVVQVENENHCDF 270
Cdd:pfam00735 159 QRFKKRIREEIERQNIPIYHFPdEESDEDEEKELNEQLKssIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDF 238
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034640533 271 VKLREMLIRVNMEDLREQTHTRHYELYRRCKLEE 304
Cdd:pfam00735 239 LKLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
19-341 5.59e-103

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 310.41  E-value: 5.59e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533  19 SGHVGFDSLPDQLVNKSTSQGFCFNILCVGETGIGKSTLMDTLFNTK------FESDPATHNEPGVRLKARSYELQESNV 92
Cdd:COG5019     1 NGYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSlvdeteIDDIRAEGTSPTLEIKITKAELEEDGF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533  93 RLKLTIVDTVGFGDQINKDDSYKPIVEYIDAQFEAYLQEELKIKRSLFnYHDTRIHACLYFIAPTGHSLKSLDLVTMKKL 172
Cdd:COG5019    81 HLNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPK-FKDTRVHACLYFIRPTGHGLKPLDIEAMKRL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533 173 DSKVNIIPIIAKADTIAKNELHKFKSKIMSELVSNGVQIYQ-FPTDEETVAEINATMSVH--LPFAVVGSTEEVKIGNKM 249
Cdd:COG5019   160 SKRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDpYDPEDDEDESLEENQDLRslIPFAIIGSNTEIENGGEQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533 250 AKARQYPWGVVQVENENHCDFVKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMGfkdtdpDSKPFSLQETYEAKRNE 329
Cdd:COG5019   240 VRGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSGLK------NSGEPSLKEIHEARLNE 313
                         330
                  ....*....|..
gi 1034640533 330 FLGELQKKEEEM 341
Cdd:COG5019   314 EERELKKKFTEK 325
YeeP COG3596
Predicted GTPase [General function prediction only];
42-121 4.86e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 54.39  E-value: 4.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533  42 FNILCVGETGIGKSTLMDTLFNTkfESDPATHNEPGVRlKARSYELQESNVRLkLTIVDTVGFGDQINKDDSYKPIVEYI 121
Cdd:COG3596    40 PVIALVGKTGAGKSSLINALFGA--EVAEVGVGRPCTR-EIQRYRLESDGLPG-LVLLDTPGLGEVNERDREYRELRELL 115
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
47-207 3.27e-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: 47.07  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533  47 VGETGIGKSTLMDTLFNTKFesdPATHNEPGVRLKARSYELQESNVRLKLTIVDTVGFGDqinkddsykpiveyidaqfE 126
Cdd:cd00882     3 VGRGGVGKSSLLNALLGGEV---GEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDE-------------------F 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533 127 AYLQEELKIKRSLFnyhdtRIHACLYFIAPTGH-SLKSLDLVTMKKLDS-KVNIIPIIAKADTIAKNELHKFKSKIMSEL 204
Cdd:cd00882    61 GGLGREELARLLLR-----GADLILLVVDSTDReSEEDAKLLILRRLRKeGIPIILVGNKIDLLEEREVEELLRLEELAK 135

                  ...
gi 1034640533 205 VSN 207
Cdd:cd00882   136 ILG 138
PLN03118 PLN03118
Rab family protein; Provisional
34-103 4.12e-04

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 41.58  E-value: 4.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533  34 KSTSQGFCFNILCVGETGIGKSTLMDTLFNTKFESDPAThnePGVRLKARsyELQESNVRLKLTIVDTVG 103
Cdd:PLN03118    7 QSSGYDLSFKILLIGDSGVGKSSLLVSFISSSVEDLAPT---IGVDFKIK--QLTVGGKRLKLTIWDTAG 71
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
43-104 5.88e-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: 5.88e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034640533  43 NILCVGETGIGKSTLMDTLFNTKfesdPATHNEPGVRLKARSYELQESNVrlKLTIVDTVGF 104
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK----AIVSDYPGTTRDPNEGRLELKGK--QIILVDTPGL 56
PRK04213 PRK04213
GTP-binding protein EngB;
44-121 3.67e-03

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 38.36  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640533  44 ILCVGETGIGKSTLMDTLFNTKFEsdpaTHNEPGVRLKARSYELQEsnvrlkLTIVDTVGFG----------DQInKDDs 113
Cdd:PRK04213   12 IVFVGRSNVGKSTLVRELTGKKVR----VGKRPGVTRKPNHYDWGD------FILTDLPGFGfmsgvpkevqEKI-KDE- 79

                  ....*...
gi 1034640533 114 ykpIVEYI 121
Cdd:PRK04213   80 ---IVRYI 84
 
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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