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Conserved domains on  [gi|807066321|ref|NP_001293076|]
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septin-11 isoform 1 [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 ...
48-316 5.18e-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: 5.18e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321  48 QGFCFNILCVGETGIGKSTLMDTLFNTKF-----ESDPATHNEPGVRLKARSYELQESNVRLKLTIVDTVGFGDQINKDD 122
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLypskyPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321 123 SYKPIVEYIDAQFEAYLQEELKIKRSLfNYHDTRIHACLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADTIAKNE 202
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRNR-RIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321 203 LHKFKSKIMSELVSNGVQIYQFPTDEET--VAEINATMSVHLPFAVVGSTEEVKIGNKMAKARQYPWGVVQVENENHCDF 280
Cdd:cd01850  160 LTEFKKRIMEDIEENNIKIYKFPEDEEDeeEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDF 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 807066321 281 VKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMG 316
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 ...
48-316 5.18e-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: 5.18e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321  48 QGFCFNILCVGETGIGKSTLMDTLFNTKF-----ESDPATHNEPGVRLKARSYELQESNVRLKLTIVDTVGFGDQINKDD 122
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLypskyPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321 123 SYKPIVEYIDAQFEAYLQEELKIKRSLfNYHDTRIHACLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADTIAKNE 202
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRNR-RIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321 203 LHKFKSKIMSELVSNGVQIYQFPTDEET--VAEINATMSVHLPFAVVGSTEEVKIGNKMAKARQYPWGVVQVENENHCDF 280
Cdd:cd01850  160 LTEFKKRIMEDIEENNIKIYKFPEDEEDeeEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDF 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 807066321 281 VKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMG 316
Cdd:cd01850  240 VKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
49-314 1.32e-111

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: 329.26  E-value: 1.32e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321   49 GFCFNILCVGETGIGKSTLMDTLFNTKFESD-----PATHNEPGVRLKARSYELQESNVRLKLTIVDTVGFGDQINKDDS 123
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRArgipgPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321  124 YKPIVEYIDAQFEAYLQEELKIKRSLFNyhDTRIHACLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADTIAKNEL 203
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIK--DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDEL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321  204 HKFKSKIMSELVSNGVQIYQFP-TDEETVAEINATMSVH--LPFAVVGSTEEVKIGNKMAKARQYPWGVVQVENENHCDF 280
Cdd:pfam00735 159 QRFKKRIREEIERQNIPIYHFPdEESDEDEEKELNEQLKssIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDF 238
                         250       260       270
                  ....*....|....*....|....*....|....
gi 807066321  281 VKLREMLIRVNMEDLREQTHTRHYELYRRCKLEE 314
Cdd:pfam00735 239 LKLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
29-351 2.34e-102

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 309.25  E-value: 2.34e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321  29 SGHVGFDSLPDQLVNKSTSQGFCFNILCVGETGIGKSTLMDTLFNTK------FESDPATHNEPGVRLKARSYELQESNV 102
Cdd:COG5019    1 NGYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSlvdeteIDDIRAEGTSPTLEIKITKAELEEDGF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321 103 RLKLTIVDTVGFGDQINKDDSYKPIVEYIDAQFEAYLQEELKIKRSLFnYHDTRIHACLYFIAPTGHSLKSLDLVTMKKL 182
Cdd:COG5019   81 HLNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPK-FKDTRVHACLYFIRPTGHGLKPLDIEAMKRL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321 183 DSKVNIIPIIAKADTIAKNELHKFKSKIMSELVSNGVQIYQ-FPTDEETVAEINATMSVH--LPFAVVGSTEEVKIGNKM 259
Cdd:COG5019  160 SKRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDpYDPEDDEDESLEENQDLRslIPFAIIGSNTEIENGGEQ 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321 260 AKARQYPWGVVQVENENHCDFVKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMGfkdtdpDSKPFSLQETYEAKRNE 339
Cdd:COG5019  240 VRGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSGLK------NSGEPSLKEIHEARLNE 313
                        330
                 ....*....|..
gi 807066321 340 FLGELQKKEEEM 351
Cdd:COG5019  314 EERELKKKFTEK 325
PLN03118 PLN03118
Rab family protein; Provisional
44-113 4.25e-04

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 41.58  E-value: 4.25e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321  44 KSTSQGFCFNILCVGETGIGKSTLMDTLFNTKFESDPAThnePGVRLKARsyELQESNVRLKLTIVDTVG 113
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 ...
48-316 5.18e-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: 5.18e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321  48 QGFCFNILCVGETGIGKSTLMDTLFNTKF-----ESDPATHNEPGVRLKARSYELQESNVRLKLTIVDTVGFGDQINKDD 122
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLypskyPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321 123 SYKPIVEYIDAQFEAYLQEELKIKRSLfNYHDTRIHACLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADTIAKNE 202
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRNR-RIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321 203 LHKFKSKIMSELVSNGVQIYQFPTDEET--VAEINATMSVHLPFAVVGSTEEVKIGNKMAKARQYPWGVVQVENENHCDF 280
Cdd:cd01850  160 LTEFKKRIMEDIEENNIKIYKFPEDEEDeeEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDF 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 807066321 281 VKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMG 316
Cdd:cd01850  240 VKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
49-314 1.32e-111

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: 329.26  E-value: 1.32e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321   49 GFCFNILCVGETGIGKSTLMDTLFNTKFESD-----PATHNEPGVRLKARSYELQESNVRLKLTIVDTVGFGDQINKDDS 123
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRArgipgPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321  124 YKPIVEYIDAQFEAYLQEELKIKRSLFNyhDTRIHACLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADTIAKNEL 203
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIK--DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDEL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321  204 HKFKSKIMSELVSNGVQIYQFP-TDEETVAEINATMSVH--LPFAVVGSTEEVKIGNKMAKARQYPWGVVQVENENHCDF 280
Cdd:pfam00735 159 QRFKKRIREEIERQNIPIYHFPdEESDEDEEKELNEQLKssIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDF 238
                         250       260       270
                  ....*....|....*....|....*....|....
gi 807066321  281 VKLREMLIRVNMEDLREQTHTRHYELYRRCKLEE 314
Cdd:pfam00735 239 LKLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
29-351 2.34e-102

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 309.25  E-value: 2.34e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321  29 SGHVGFDSLPDQLVNKSTSQGFCFNILCVGETGIGKSTLMDTLFNTK------FESDPATHNEPGVRLKARSYELQESNV 102
Cdd:COG5019    1 NGYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSlvdeteIDDIRAEGTSPTLEIKITKAELEEDGF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321 103 RLKLTIVDTVGFGDQINKDDSYKPIVEYIDAQFEAYLQEELKIKRSLFnYHDTRIHACLYFIAPTGHSLKSLDLVTMKKL 182
Cdd:COG5019   81 HLNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPK-FKDTRVHACLYFIRPTGHGLKPLDIEAMKRL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321 183 DSKVNIIPIIAKADTIAKNELHKFKSKIMSELVSNGVQIYQ-FPTDEETVAEINATMSVH--LPFAVVGSTEEVKIGNKM 259
Cdd:COG5019  160 SKRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDpYDPEDDEDESLEENQDLRslIPFAIIGSNTEIENGGEQ 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321 260 AKARQYPWGVVQVENENHCDFVKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMGfkdtdpDSKPFSLQETYEAKRNE 339
Cdd:COG5019  240 VRGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSGLK------NSGEPSLKEIHEARLNE 313
                        330
                 ....*....|..
gi 807066321 340 FLGELQKKEEEM 351
Cdd:COG5019  314 EERELKKKFTEK 325
YeeP COG3596
Predicted GTPase [General function prediction only];
52-131 5.06e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 54.39  E-value: 5.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321  52 FNILCVGETGIGKSTLMDTLFNTkfESDPATHNEPGVRlKARSYELQESNVRLkLTIVDTVGFGDQINKDDSYKPIVEYI 131
Cdd:COG3596   40 PVIALVGKTGAGKSSLINALFGA--EVAEVGVGRPCTR-EIQRYRLESDGLPG-LVLLDTPGLGEVNERDREYRELRELL 115
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
57-217 2.65e-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: 2.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321  57 VGETGIGKSTLMDTLFNTKFesdPATHNEPGVRLKARSYELQESNVRLKLTIVDTVGFGDqinkddsykpiveyidaqfE 136
Cdd:cd00882    3 VGRGGVGKSSLLNALLGGEV---GEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDE-------------------F 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321 137 AYLQEELKIKRSLFnyhdtRIHACLYFIAPTGH-SLKSLDLVTMKKLDS-KVNIIPIIAKADTIAKNELHKFKSKIMSEL 214
Cdd:cd00882   61 GGLGREELARLLLR-----GADLILLVVDSTDReSEEDAKLLILRRLRKeGIPIILVGNKIDLLEEREVEELLRLEELAK 135

                 ...
gi 807066321 215 VSN 217
Cdd:cd00882  136 ILG 138
PLN03118 PLN03118
Rab family protein; Provisional
44-113 4.25e-04

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 41.58  E-value: 4.25e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321  44 KSTSQGFCFNILCVGETGIGKSTLMDTLFNTKFESDPAThnePGVRLKARsyELQESNVRLKLTIVDTVG 113
Cdd:PLN03118   7 QSSGYDLSFKILLIGDSGVGKSSLLVSFISSSVEDLAPT---IGVDFKIK--QLTVGGKRLKLTIWDTAG 71
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
53-114 5.22e-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: 39.52  E-value: 5.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807066321   53 NILCVGETGIGKSTLMDTLFNTKfesdPATHNEPGVRLKARSYELQESNVrlKLTIVDTVGF 114
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK----AIVSDYPGTTRDPNEGRLELKGK--QIILVDTPGL 56
PRK04213 PRK04213
GTP-binding protein EngB;
54-131 3.51e-03

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 38.74  E-value: 3.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066321  54 ILCVGETGIGKSTLMDTLFNTKFEsdpaTHNEPGVRLKARSYELQEsnvrlkLTIVDTVGFG----------DQInKDDs 123
Cdd:PRK04213  12 IVFVGRSNVGKSTLVRELTGKKVR----VGKRPGVTRKPNHYDWGD------FILTDLPGFGfmsgvpkevqEKI-KDE- 79

                 ....*...
gi 807066321 124 ykpIVEYI 131
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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