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Conserved domains on  [gi|545478822|ref|NP_001269902|]
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septin-2 isoform c [Homo sapiens]

Protein Classification

septin family protein( domain architecture ID 11107662)

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
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
35-316 3.36e-175

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: 487.96  E-value: 3.36e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822   35 GFEFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGAAalntrktllwEKIERTVQIEASTVEIEERGVKLRLTVVDTPG 114
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPS----------EKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822  115 YGDAINCRDCFKTIISYIDEQFERYLHDESGLNRRHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIAKA 194
Cdd:pfam00735  71 FGDAIDNSNCWRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822  195 DTLTLKERERLKKRILDEIEEHNIKIYHLPDAESDEDEDfKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVE 274
Cdd:pfam00735 151 DTLTPDELQRFKKRIREEIERQNIPIYHFPDEESDEDEE-KELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVE 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 545478822  275 VENPEHNDFLKLRTMLI-THMQDLQEVTQDLHYENFRSERLKR 316
Cdd:pfam00735 230 VENPSHCDFLKLRNMLIrTHLQDLKEVTHELHYETYRSEKLSA 272
 
Name Accession Description Interval E-value
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
35-316 3.36e-175

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: 487.96  E-value: 3.36e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822   35 GFEFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGAAalntrktllwEKIERTVQIEASTVEIEERGVKLRLTVVDTPG 114
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPS----------EKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822  115 YGDAINCRDCFKTIISYIDEQFERYLHDESGLNRRHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIAKA 194
Cdd:pfam00735  71 FGDAIDNSNCWRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822  195 DTLTLKERERLKKRILDEIEEHNIKIYHLPDAESDEDEDfKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVE 274
Cdd:pfam00735 151 DTLTPDELQRFKKRIREEIERQNIPIYHFPDEESDEDEE-KELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVE 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 545478822  275 VENPEHNDFLKLRTMLI-THMQDLQEVTQDLHYENFRSERLKR 316
Cdd:pfam00735 230 VENPSHCDFLKLRNMLIrTHLQDLKEVTHELHYETYRSEKLSA 272
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
34-318 3.40e-165

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: 462.79  E-value: 3.40e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822  34 KGFEFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGAAalntrktllwEKIERTVQIEASTVEIEERGVKLRLTVVDTP 113
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPG----------EHITKTVEIKISKAELEENGVKLKLTVIDTP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822 114 GYGDAINCRDCFKTIISYIDEQFERYLHDESGLNR-RHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIA 192
Cdd:cd01850   71 GFGDNINNSDCWKPIVDYIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822 193 KADTLTLKERERLKKRILDEIEEHNIKIYHLPDAEsdEDEDFKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGV 272
Cdd:cd01850  151 KADTLTPEELTEFKKRIMEDIEENNIKIYKFPEDE--EDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGV 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 545478822 273 VEVENPEHNDFLKLRTMLI-THMQDLQEVTQDLHYENFRSERLKRGG 318
Cdd:cd01850  229 VEVENEEHCDFVKLRNLLIrTHLQDLKETTHNVHYENYRSEKLEALK 275
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
15-342 3.52e-126

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 367.42  E-value: 3.52e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822  15 PGYVGFANLPNQVHRKSVKKGFEFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGAAALNTRKTllwekiertVQIEAS 94
Cdd:COG5019    1 NGYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDETEIDDIRAEGTSPT---------LEIKIT 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822  95 TVEIEERGVKLRLTVVDTPGYGDAINCRDCFKTIISYIDEQFERYLHDESGLNRRH-IIDNRVHCCFYFISPFGHGLKPL 173
Cdd:COG5019   72 KAELEEDGFHLNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPkFKDTRVHACLYFIRPTGHGLKPL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822 174 DVAFMKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHNIKIYHLPDAESDEDEDFkEQTRLLKASIPFSVVGSN 253
Cdd:COG5019  152 DIEAMKRLSKRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESL-EENQDLRSLIPFAIIGSN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822 254 QLIEAKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLI-THMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQIL 332
Cdd:COG5019  231 TEIENGGEQVRGRKYPWGVVEIDDEEHSDFKKLRNLLIrTHLQELKETTENLLYENYRTEKLSGLKNSGEPSLKEIHEAR 310
                        330
                 ....*....|
gi 545478822 333 LEKEAELRRM 342
Cdd:COG5019  311 LNEEERELKK 320
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
37-114 4.61e-03

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 37.35  E-value: 4.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545478822   37 EFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGaaalntrktllwekIERTVqieaSTVEIEERGVKLRLTVVDTPG 114
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPG--------------TTRNY----VTTVIEEDGKTYKFNLLDTAG 60
 
Name Accession Description Interval E-value
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
35-316 3.36e-175

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: 487.96  E-value: 3.36e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822   35 GFEFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGAAalntrktllwEKIERTVQIEASTVEIEERGVKLRLTVVDTPG 114
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPS----------EKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822  115 YGDAINCRDCFKTIISYIDEQFERYLHDESGLNRRHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIAKA 194
Cdd:pfam00735  71 FGDAIDNSNCWRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822  195 DTLTLKERERLKKRILDEIEEHNIKIYHLPDAESDEDEDfKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVE 274
Cdd:pfam00735 151 DTLTPDELQRFKKRIREEIERQNIPIYHFPDEESDEDEE-KELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVE 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 545478822  275 VENPEHNDFLKLRTMLI-THMQDLQEVTQDLHYENFRSERLKR 316
Cdd:pfam00735 230 VENPSHCDFLKLRNMLIrTHLQDLKEVTHELHYETYRSEKLSA 272
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
34-318 3.40e-165

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: 462.79  E-value: 3.40e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822  34 KGFEFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGAAalntrktllwEKIERTVQIEASTVEIEERGVKLRLTVVDTP 113
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPG----------EHITKTVEIKISKAELEENGVKLKLTVIDTP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822 114 GYGDAINCRDCFKTIISYIDEQFERYLHDESGLNR-RHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIA 192
Cdd:cd01850   71 GFGDNINNSDCWKPIVDYIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822 193 KADTLTLKERERLKKRILDEIEEHNIKIYHLPDAEsdEDEDFKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGV 272
Cdd:cd01850  151 KADTLTPEELTEFKKRIMEDIEENNIKIYKFPEDE--EDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGV 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 545478822 273 VEVENPEHNDFLKLRTMLI-THMQDLQEVTQDLHYENFRSERLKRGG 318
Cdd:cd01850  229 VEVENEEHCDFVKLRNLLIrTHLQDLKETTHNVHYENYRSEKLEALK 275
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
15-342 3.52e-126

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 367.42  E-value: 3.52e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822  15 PGYVGFANLPNQVHRKSVKKGFEFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGAAALNTRKTllwekiertVQIEAS 94
Cdd:COG5019    1 NGYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDETEIDDIRAEGTSPT---------LEIKIT 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822  95 TVEIEERGVKLRLTVVDTPGYGDAINCRDCFKTIISYIDEQFERYLHDESGLNRRH-IIDNRVHCCFYFISPFGHGLKPL 173
Cdd:COG5019   72 KAELEEDGFHLNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPkFKDTRVHACLYFIRPTGHGLKPL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822 174 DVAFMKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHNIKIYHLPDAESDEDEDFkEQTRLLKASIPFSVVGSN 253
Cdd:COG5019  152 DIEAMKRLSKRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESL-EENQDLRSLIPFAIIGSN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822 254 QLIEAKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLI-THMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQIL 332
Cdd:COG5019  231 TEIENGGEQVRGRKYPWGVVEIDDEEHSDFKKLRNLLIrTHLQELKETTENLLYENYRTEKLSGLKNSGEPSLKEIHEAR 310
                        330
                 ....*....|
gi 545478822 333 LEKEAELRRM 342
Cdd:COG5019  311 LNEEERELKK 320
YeeP COG3596
Predicted GTPase [General function prediction only];
37-120 4.88e-06

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 47.84  E-value: 4.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822  37 EFTLMVVGESGLGKSTLINSLFLtdlypervipgaaalntrktllwEKIERTVQIEASTVEIE----ERGVKLRLTVVDT 112
Cdd:COG3596   39 PPVIALVGKTGAGKSSLINALFG-----------------------AEVAEVGVGRPCTREIQryrlESDGLPGLVLLDT 95

                 ....*...
gi 545478822 113 PGYGDAIN 120
Cdd:COG3596   96 PGLGEVNE 103
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
43-224 6.44e-06

YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 45.96  E-value: 6.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822  43 VGESGLGKSTLINSLFltdlypervipgaaalnTRKtllweKIERTVQIEASTVEIEERGVKLRLTVVDTPGYGDA---I 119
Cdd:cd01876    5 AGRSNVGKSSLINALT-----------------NRK-----KLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAkvsK 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822 120 NCRDCFKTIIsyideqfERYLHDESGLNRR-HIIDNRvhccfyfispfgHGLKPLDVAFMK-AIHNKVNIVPVIAKADTL 197
Cdd:cd01876   63 EVREKWGKLI-------EEYLENRENLKGVvLLIDAR------------HGPTPIDLEMLEfLEELGIPFLIVLTKADKL 123
                        170       180
                 ....*....|....*....|....*..
gi 545478822 198 TLKERERLKKRILDEIEEHNIKIYHLP 224
Cdd:cd01876  124 KKSELAKVLKKIKEELNLFNILPPVIL 150
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
42-217 2.11e-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: 41.29  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822  42 VVGESGLGKSTLINSLFLTDLYPERVIPGaaalntrktllwekieRTVQIEASTVEIEERGVKLRLtvVDTPGYGDAINC 121
Cdd:cd00882    2 VVGRGGVGKSSLLNALLGGEVGEVSDVPG----------------TTRDPDVYVKELDKGKVKLVL--VDTPGLDEFGGL 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822 122 RDCFKTIISYideqferylhdesglnrrhiidNRVHCCFYFISPFGHGLKP--LDVAFMKAIHNKVNIVPVIAKADTLTL 199
Cdd:cd00882   64 GREELARLLL----------------------RGADLILLVVDSTDRESEEdaKLLILRRLRKEGIPIILVGNKIDLLEE 121
                        170
                 ....*....|....*...
gi 545478822 200 KERERLKKRILDEIEEHN 217
Cdd:cd00882  122 REVEELLRLEELAKILGV 139
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
38-224 2.61e-04

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 41.38  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822  38 FTLMVVGESGLGKSTLINSLFLTDLYPERVIPGAAALntrkTLLwekiertvqieastveieERGVKLRLTVVDTPGygd 117
Cdd:cd09912    1 FLLAVVGEFSAGKSTLLNALLGEEVLPTGVTPTTAVI----TVL------------------RYGLLKGVVLVDTPG--- 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822 118 aincrdcfktiisyIDEQFERylHDEsglnrrhIIDNRVHCC--FYFISPFGHGLKPLDVAFMKAI--HNKVNIVPVIAK 193
Cdd:cd09912   56 --------------LNSTIEH--HTE-------ITESFLPRAdaVIFVLSADQPLTESEREFLKEIlkWSGKKIFFVLNK 112
                        170       180       190
                 ....*....|....*....|....*....|.
gi 545478822 194 ADTLTLKERERLKKRILDEIEEHNIKIYHLP 224
Cdd:cd09912  113 IDLLSEEELEEVLEYSREELGVLELGGGEPR 143
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
42-119 4.44e-04

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 41.42  E-value: 4.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822  42 VVGESGLGKSTLINS-LFLTDLY--PERVIPGaaalNTRKTLLWEKIERTVQIEASTVEIEERGVKLrlTVVDTPGYGDA 118
Cdd:cd04170    4 LVGHSGSGKTTLAEAlLYATGAIdrLGRVEDG----NTVSDYDPEEKKRKMSIETSVAPLEWNGHKI--NLIDTPGYADF 77

                 .
gi 545478822 119 I 119
Cdd:cd04170   78 V 78
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
36-237 8.11e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 39.96  E-value: 8.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822  36 FEFTLMVVGESGLGKSTLINSLfltdlypervipgaaalnTRKTLLWEKIERTVQIEASTVEIEERGVKLRLTVVDTPGy 115
Cdd:COG1100    2 GEKKIVVVGTGGVGKTSLVNRL------------------VGDIFSLEKYLSTNGVTIDKKELKLDGLDVDLVIWDTPG- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545478822 116 gdaincrdcfKTIISYIDEQFERYLHDESGLnrrhI--IDNRVHCCFYFIspfghgLKPLDVAFMKAIhnKVNIVPVIAK 193
Cdd:COG1100   63 ----------QDEFRETRQFYARQLTGASLY----LfvVDGTREETLQSL------YELLESLRRLGK--KSPIILVLNK 120
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 545478822 194 ADTLTLKERERlKKRILDEIEEHNIKIYHLPDAESDED-EDFKEQ 237
Cdd:COG1100  121 IDLYDEEEIED-EERLKEALSEDNIVEVVATSAKTGEGvEELFAA 164
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
36-114 1.04e-03

Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like (Translocon at the Outer-envelope membrane of Chloroplasts) family contains several Toc proteins, including Toc34, Toc33, Toc120, Toc159, Toc86, Toc125, and Toc90. The Toc complex at the outer envelope membrane of chloroplasts is a molecular machine of ~500 kDa that contains a single Toc159 protein, four Toc75 molecules, and four or five copies of Toc34. Toc64 and Toc12 are associated with the translocon, but do not appear to be part of the core complex. The Toc translocon initiates the import of nuclear-encoded preproteins from the cytosol into the organelle. Toc34 and Toc159 are both GTPases, while Toc75 is a beta-barrel integral membrane protein. Toc159 is equally distributed between a soluble cytoplasmic form and a membrane-inserted form, suggesting that assembly of the Toc complex is dynamic. Toc34 and Toc75 act sequentially to mediate docking and insertion of Toc159 resulting in assembly of the functional translocon.


Pssm-ID: 206652  Cd Length: 248  Bit Score: 40.38  E-value: 1.04e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545478822  36 FEFTLMVVGESGLGKSTLINSLFltdlyPERVIPGAAALNTrkTLLWEKIERTVQieastveieerGVKlrLTVVDTPG 114
Cdd:cd01853   30 FSLTILVLGKTGVGKSSTINSIF-----GERKVSVSAFQSE--TLRPREVSRTVD-----------GFK--LNIIDTPG 88
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
43-118 1.70e-03

YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 38.48  E-value: 1.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545478822  43 VGESGLGKSTLINSLFLTDLypervipgAAALNTRKTllwekierTVQIEASTVEIEERGvklrLTVVDTPGYGDA 118
Cdd:cd11383    3 MGKTGAGKSSLCNALFGTEV--------AAVGDRRPT--------TRAAQAYVWQTGGDG----LVLLDLPGVGER 58
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
37-114 4.61e-03

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 37.35  E-value: 4.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545478822   37 EFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGaaalntrktllwekIERTVqieaSTVEIEERGVKLRLTVVDTPG 114
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPG--------------TTRNY----VTTVIEEDGKTYKFNLLDTAG 60
 
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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