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Conserved domains on  [gi|1005261151|ref|NP_001307958|]
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septin-2 isoform d [Homo sapiens]

Protein Classification

septin family protein( domain architecture ID 11107662)

septin family protein similar to septins, which are GTP-binding proteins associated with diverse processes in dividing and non-dividing cells

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 ...
65-336 4.82e-179

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 characteristic 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: 498.36  E-value: 4.82e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151  65 GFEFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGAAEKIERTVQIEASTVEIEERGVKLRLTVVDTPGYGDAINCRDC 144
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151 145 FKTIISYIDEQFERYLHDESGLNRRHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIAKADTLTLKERER 224
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151 225 LKKRILDEIEEHNIKIYHLPDAESDEDEDfKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVEVENPEHNDFL 304
Cdd:pfam00735 161 FKKRIREEIERQNIPIYHFPDEESDEDEE-KELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1005261151 305 KLRTMLI-THMQDLQEVTQDLHYENFRSERLKR 336
Cdd:pfam00735 240 KLRNMLIrTHLQDLKEVTHELHYETYRSEKLSA 272
 
Name Accession Description Interval E-value
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
65-336 4.82e-179

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 characteristic 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: 498.36  E-value: 4.82e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151  65 GFEFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGAAEKIERTVQIEASTVEIEERGVKLRLTVVDTPGYGDAINCRDC 144
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151 145 FKTIISYIDEQFERYLHDESGLNRRHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIAKADTLTLKERER 224
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151 225 LKKRILDEIEEHNIKIYHLPDAESDEDEDfKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVEVENPEHNDFL 304
Cdd:pfam00735 161 FKKRIREEIERQNIPIYHFPDEESDEDEE-KELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1005261151 305 KLRTMLI-THMQDLQEVTQDLHYENFRSERLKR 336
Cdd:pfam00735 240 KLRNMLIrTHLQDLKEVTHELHYETYRSEKLSA 272
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
64-338 2.55e-169

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: 473.96  E-value: 2.55e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151  64 KGFEFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGAAEKIERTVQIEASTVEIEERGVKLRLTVVDTPGYGDAINCRD 143
Cdd:cd01850     1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151 144 CFKTIISYIDEQFERYLHDESGLNR-RHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIAKADTLTLKER 222
Cdd:cd01850    81 CWKPIVDYIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151 223 ERLKKRILDEIEEHNIKIYHLPDAEsdEDEDFKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVEVENPEHND 302
Cdd:cd01850   161 TEFKKRIMEDIEENNIKIYKFPEDE--EDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCD 238
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1005261151 303 FLKLRTMLI-THMQDLQEVTQDLHYENFRSERLKRGG 338
Cdd:cd01850   239 FVKLRNLLIrTHLQDLKETTHNVHYENYRSEKLEALK 275
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
45-362 2.56e-128

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 373.58  E-value: 2.56e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151  45 PGYVGFANLPNQVHRKSVKKGFEFTLMVVGESGLGKSTLINSLFLTDLYPER-VIPGAAEKIERTVQIEASTVEIEERGV 123
Cdd:COG5019     1 NGYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDETeIDDIRAEGTSPTLEIKITKAELEEDGF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151 124 KLRLTVVDTPGYGDAINCRDCFKTIISYIDEQFERYLHDESGLNRRH-IIDNRVHCCFYFISPFGHGLKPLDVAFMKAIH 202
Cdd:COG5019    81 HLNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPkFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151 203 NKVNIVPVIAKADTLTLKERERLKKRILDEIEEHNIKIYHLPDAESDEDEDFkEQTRLLKASIPFSVVGSNQLIEAKGKK 282
Cdd:COG5019   161 KRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESL-EENQDLRSLIPFAIIGSNTEIENGGEQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151 283 VRGRLYPWGVVEVENPEHNDFLKLRTMLI-THMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQILLEKEAELRR 361
Cdd:COG5019   240 VRGRKYPWGVVEIDDEEHSDFKKLRNLLIrTHLQELKETTENLLYENYRTEKLSGLKNSGEPSLKEIHEARLNEEERELK 319

                  .
gi 1005261151 362 M 362
Cdd:COG5019   320 K 320
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
67-134 1.57e-04

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: 41.97  E-value: 1.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005261151  67 EFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGaaekIERTVqieaSTVEIEERGVKLRLTVVDTPG 134
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPG----TTRNY----VTTVIEEDGKTYKFNLLDTAG 60
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
68-134 5.96e-03

Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 37.10  E-value: 5.96e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005261151   68 FTLMVVGESGLGKSTLINSlFLTDLYPERVIPgaaekierTVQIEASTVEIEERGVKLRLTVVDTPG 134
Cdd:smart00175   1 FKIILIGDSGVGKSSLLSR-FTDGKFSEQYKS--------TIGVDFKTKTIEVDGKRVKLQIWDTAG 58
 
Name Accession Description Interval E-value
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
65-336 4.82e-179

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 characteristic 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: 498.36  E-value: 4.82e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151  65 GFEFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGAAEKIERTVQIEASTVEIEERGVKLRLTVVDTPGYGDAINCRDC 144
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151 145 FKTIISYIDEQFERYLHDESGLNRRHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIAKADTLTLKERER 224
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151 225 LKKRILDEIEEHNIKIYHLPDAESDEDEDfKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVEVENPEHNDFL 304
Cdd:pfam00735 161 FKKRIREEIERQNIPIYHFPDEESDEDEE-KELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1005261151 305 KLRTMLI-THMQDLQEVTQDLHYENFRSERLKR 336
Cdd:pfam00735 240 KLRNMLIrTHLQDLKEVTHELHYETYRSEKLSA 272
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
64-338 2.55e-169

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: 473.96  E-value: 2.55e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151  64 KGFEFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGAAEKIERTVQIEASTVEIEERGVKLRLTVVDTPGYGDAINCRD 143
Cdd:cd01850     1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151 144 CFKTIISYIDEQFERYLHDESGLNR-RHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIAKADTLTLKER 222
Cdd:cd01850    81 CWKPIVDYIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151 223 ERLKKRILDEIEEHNIKIYHLPDAEsdEDEDFKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVEVENPEHND 302
Cdd:cd01850   161 TEFKKRIMEDIEENNIKIYKFPEDE--EDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCD 238
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1005261151 303 FLKLRTMLI-THMQDLQEVTQDLHYENFRSERLKRGG 338
Cdd:cd01850   239 FVKLRNLLIrTHLQDLKETTHNVHYENYRSEKLEALK 275
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
45-362 2.56e-128

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 373.58  E-value: 2.56e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151  45 PGYVGFANLPNQVHRKSVKKGFEFTLMVVGESGLGKSTLINSLFLTDLYPER-VIPGAAEKIERTVQIEASTVEIEERGV 123
Cdd:COG5019     1 NGYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDETeIDDIRAEGTSPTLEIKITKAELEEDGF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151 124 KLRLTVVDTPGYGDAINCRDCFKTIISYIDEQFERYLHDESGLNRRH-IIDNRVHCCFYFISPFGHGLKPLDVAFMKAIH 202
Cdd:COG5019    81 HLNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPkFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151 203 NKVNIVPVIAKADTLTLKERERLKKRILDEIEEHNIKIYHLPDAESDEDEDFkEQTRLLKASIPFSVVGSNQLIEAKGKK 282
Cdd:COG5019   161 KRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESL-EENQDLRSLIPFAIIGSNTEIENGGEQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151 283 VRGRLYPWGVVEVENPEHNDFLKLRTMLI-THMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQILLEKEAELRR 361
Cdd:COG5019   240 VRGRKYPWGVVEIDDEEHSDFKKLRNLLIrTHLQELKETTENLLYENYRTEKLSGLKNSGEPSLKEIHEARLNEEERELK 319

                  .
gi 1005261151 362 M 362
Cdd:COG5019   320 K 320
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
73-244 6.86e-07

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: 48.66  E-value: 6.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151  73 VGESGLGKSTLINSLFltdlYPERVI-----PGaaekieRTVQIeaSTVEIEErgvKLRLtvVDTPGYGDA---INCRDC 144
Cdd:cd01876     5 AGRSNVGKSSLINALT----NRKKLArtsktPG------RTQLI--NFFNVGD---KFRL--VDLPGYGYAkvsKEVREK 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151 145 FKTIIsyideqfERYLhdesgLNRR------HIIDNRvhccfyfispfgHGLKPLDVAFMK-AIHNKVNIVPVIAKADTL 217
Cdd:cd01876    68 WGKLI-------EEYL-----ENREnlkgvvLLIDAR------------HGPTPIDLEMLEfLEELGIPFLIVLTKADKL 123
                         170       180
                  ....*....|....*....|....*..
gi 1005261151 218 TLKERERLKKRILDEIEEHNIKIYHLP 244
Cdd:cd01876   124 KKSELAKVLKKIKEELNLFNILPPVIL 150
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
72-237 6.67e-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: 45.91  E-value: 6.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151  72 VVGESGLGKSTLINSLFLTDLYPERVIPGaaekieRTVQIEASTVEIEERGVKLRLtvVDTPGYGDAINCRDCFKTIISY 151
Cdd:cd00882     2 VVGRGGVGKSSLLNALLGGEVGEVSDVPG------TTRDPDVYVKELDKGKVKLVL--VDTPGLDEFGGLGREELARLLL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151 152 ideqferylhdesglnrrhiidNRVHCCFYFISPFGHGLKP--LDVAFMKAIHNKVNIVPVIAKADTLTLKERERLKKRI 229
Cdd:cd00882    74 ----------------------RGADLILLVVDSTDRESEEdaKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLE 131

                  ....*...
gi 1005261151 230 LDEIEEHN 237
Cdd:cd00882   132 ELAKILGV 139
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
68-244 6.93e-06

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: 46.00  E-value: 6.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151  68 FTLMVVGESGLGKSTLINSLFLTDLYPERVIPgaaekiertvqiEASTVEIEERGVKLRLTVVDTPGygdaincrdcfkt 147
Cdd:cd09912     1 FLLAVVGEFSAGKSTLLNALLGEEVLPTGVTP------------TTAVITVLRYGLLKGVVLVDTPG------------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151 148 iisyIDEQFERylHDEsglnrrhIIDNRVHCC--FYFISPFGHGLKPLDVAFMKAI--HNKVNIVPVIAKADTLTLKERE 223
Cdd:cd09912    56 ----LNSTIEH--HTE-------ITESFLPRAdaVIFVLSADQPLTESEREFLKEIlkWSGKKIFFVLNKIDLLSEEELE 122
                         170       180
                  ....*....|....*....|.
gi 1005261151 224 RLKKRILDEIEEHNIKIYHLP 244
Cdd:cd09912   123 EVLEYSREELGVLELGGGEPR 143
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
72-139 5.11e-05

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: 44.51  E-value: 5.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005261151  72 VVGESGLGKSTLINSLFLTDLYPER---------VIPGAAEKIERTVQIEASTVEIEERGVKLrlTVVDTPGYGDAI 139
Cdd:cd04170     4 LVGHSGSGKTTLAEALLYATGAIDRlgrvedgntVSDYDPEEKKRKMSIETSVAPLEWNGHKI--NLIDTPGYADFV 78
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
66-134 8.76e-05

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 [Multi-domain]  Cd Length: 248  Bit Score: 43.46  E-value: 8.76e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005261151  66 FEFTLMVVGESGLGKSTLINSLFltdlyPERVIPGAAEKIE--RTVQIeASTVEieerGVKlrLTVVDTPG 134
Cdd:cd01853    30 FSLTILVLGKTGVGKSSTINSIF-----GERKVSVSAFQSEtlRPREV-SRTVD----GFK--LNIIDTPG 88
YeeP COG3596
Predicted GTPase [General function prediction only];
71-160 1.23e-04

Predicted GTPase [General function prediction only];


Pssm-ID: 226124 [Multi-domain]  Cd Length: 296  Bit Score: 43.63  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261151  71 MVVGESGLGKSTLINSLFLTDLYPervipgaaekiertVQIEASTVEIEERGVKLR----LTVVDTPGYGDAINcRDCfK 146
Cdd:COG3596    43 LLMGATGAGKSSLINALFQGEVKE--------------VSKVGVGTDITTRLRLSYdgenLVLWDTPGLGDGKD-KDA-E 106
                          90
                  ....*....|....
gi 1005261151 147 TIISYIDEQFERYL 160
Cdd:COG3596   107 HRQLYRDYLPKLDL 120
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
67-134 1.57e-04

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: 41.97  E-value: 1.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005261151  67 EFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGaaekIERTVqieaSTVEIEERGVKLRLTVVDTPG 134
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPG----TTRNY----VTTVIEEDGKTYKFNLLDTAG 60
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
73-138 2.39e-04

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: 40.79  E-value: 2.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005261151  73 VGESGLGKSTLINSLFLTDLYPERVIPGAaekierTVQIEASTVEIEERGvklrLTVVDTPGYGDA 138
Cdd:cd11383     3 MGKTGAGKSSLCNALFGTEVAAVGDRRPT------TRAAQAYVWQTGGDG----LVLLDLPGVGER 58
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
67-135 7.76e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 224025 [Multi-domain]  Cd Length: 219  Bit Score: 40.33  E-value: 7.76e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005261151  67 EFTLMVVGESGLGKSTLINSlFLTDLYPERVIPgaaekierTVQIEASTVEIEERGVKLRLTVVDTPGY 135
Cdd:COG1100     5 EFKIVVLGDGGVGKTTLLNR-LVGDEFPEGYPP--------TIGNLDPAKTIEPYRRNIKLQLWDTAGQ 64
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
66-134 1.00e-03

chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K protein originally described is proposed to have three domains. The N-terminal A-domain is acidic, repetitive, weakly conserved, readily removed by proteolysis during chloroplast isolation, and not required for protein translocation. The other domains are designated G (GTPase) and M (membrane anchor); this family includes most of the G domain and all of M. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273381 [Multi-domain]  Cd Length: 763  Bit Score: 41.09  E-value: 1.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005261151  66 FEFTLMVVGESGLGKSTLINSLFltdlypervipgaAEKIERTVQIEASTVEIEE-----RGVKLRltVVDTPG 134
Cdd:TIGR00993 117 FSLNILVLGKSGVGKSATINSIF-------------GEVKFSTDAFGMGTTSVQEieglvQGVKIR--VIDTPG 175
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
69-134 1.22e-03

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 39.69  E-value: 1.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005261151  69 TLMVVGESGLGKSTLINSLFltdlyPERVIPGAA--EKIER----TVQIEAstVEIEERGVklrltVVDTPG 134
Cdd:cd01854    87 TSVLVGQSGVGKSTLLNALL-----PELVLATGEisEKLGRgrhtTTHREL--FPLPGGGL-----IIDTPG 146
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
71-135 1.70e-03

Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 39.17  E-value: 1.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005261151  71 MVVGESGLGKSTLINSLFLTDLYpervIPGAAEKIERTVQ--IEASTVEIEERGVKLRLTVVDTPGY 135
Cdd:cd01855   129 YVVGATNVGKSTLINALLKSNGG----KVQAQALVQRLTVspIPGTTLGLIKIPLGEGKKLYDTPGI 191
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
70-134 2.00e-03

Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.


Pssm-ID: 425451 [Multi-domain]  Cd Length: 162  Bit Score: 38.65  E-value: 2.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005261151  70 LMVVGESGLGKSTLINSlFLTDLYPERVIPgaaekierTVQIE--ASTVEIEERGVKLRLTvvDTPG 134
Cdd:pfam00071   2 LVLVGDGGVGKSSLLIR-FTQNKFPEEYIP--------TIGVDfyTKTIEVDGKTVKLQIW--DTAG 57
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
68-134 5.96e-03

Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 37.10  E-value: 5.96e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005261151   68 FTLMVVGESGLGKSTLINSlFLTDLYPERVIPgaaekierTVQIEASTVEIEERGVKLRLTVVDTPG 134
Cdd:smart00175   1 FKIILIGDSGVGKSSLLSR-FTDGKFSEQYKS--------TIGVDFKTKTIEVDGKRVKLQIWDTAG 58
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
69-134 8.55e-03

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: 426514 [Multi-domain]  Cd Length: 113  Bit Score: 35.67  E-value: 8.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005261151  69 TLMVVGESGLGKSTLINSLFltdlypervipGAAEKIERTVQ--IEASTVEIEERGVKLRLtvVDTPG 134
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALT-----------GAKAIVSDYPGttRDPNEGRLELKGKQIIL--VDTPG 55
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
70-134 8.76e-03

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organisation, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.


Pssm-ID: 430018 [Multi-domain]  Cd Length: 114  Bit Score: 35.95  E-value: 8.76e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005261151  70 LMVVGESGLGKSTLINSlFLTDLYPERVIPgaaekierTVQIEAST---VEIEERGVKLRLTVVDTPG 134
Cdd:pfam08477   2 IVLLGDSGVGKTSLLKR-FVDDTFDPKYQS--------TIGVDFKTktvLENDDNGKKIKLNIWDTAG 60
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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