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Conserved domains on  [gi|119572638|gb|EAW52253|]
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septin 1, isoform CRA_b [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 ...
1-263 1.63e-165

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: 459.84  E-value: 1.63e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638    1 MVAGESGLGKSTLINSLFLTNLYEDRQVPEASARLTQTLAIERRGVEIEEGGVKVKLTLVDTPGFGDSVDCSDCWLPVVK 80
Cdd:pfam00735   7 MVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNCWRPIVE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638   81 FIEEQFEQYLRDESGLNRKNIQDSRVHCCLYFISPFGRGLRPLDVAFLRAVHEKVNIIPVIGKADALMPQETQALKQKIR 160
Cdd:pfam00735  87 YIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQRFKKRIR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638  161 DQLKEEEIHIYQFPECDSDEDEDfKRQDAEMKESIPFAVVGSCEVVRDGGnRPVRGRRYSWGTVEVENPHHCDFLNLRRM 240
Cdd:pfam00735 167 EEIERQNIPIYHFPDEESDEDEE-KELNEQLKSSIPFAIVGSNTVIENDG-EKVRGRKYPWGVVEVENPSHCDFLKLRNM 244
                         250       260
                  ....*....|....*....|...
gi 119572638  241 LVQTHLQDLKEVTHDLLYEGYRA 263
Cdd:pfam00735 245 LIRTHLQDLKEVTHELHYETYRS 267
 
Name Accession Description Interval E-value
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
1-263 1.63e-165

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: 459.84  E-value: 1.63e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638    1 MVAGESGLGKSTLINSLFLTNLYEDRQVPEASARLTQTLAIERRGVEIEEGGVKVKLTLVDTPGFGDSVDCSDCWLPVVK 80
Cdd:pfam00735   7 MVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNCWRPIVE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638   81 FIEEQFEQYLRDESGLNRKNIQDSRVHCCLYFISPFGRGLRPLDVAFLRAVHEKVNIIPVIGKADALMPQETQALKQKIR 160
Cdd:pfam00735  87 YIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQRFKKRIR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638  161 DQLKEEEIHIYQFPECDSDEDEDfKRQDAEMKESIPFAVVGSCEVVRDGGnRPVRGRRYSWGTVEVENPHHCDFLNLRRM 240
Cdd:pfam00735 167 EEIERQNIPIYHFPDEESDEDEE-KELNEQLKSSIPFAIVGSNTVIENDG-EKVRGRKYPWGVVEVENPSHCDFLKLRNM 244
                         250       260
                  ....*....|....*....|...
gi 119572638  241 LVQTHLQDLKEVTHDLLYEGYRA 263
Cdd:pfam00735 245 LIRTHLQDLKEVTHELHYETYRS 267
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
1-263 2.16e-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: 424.27  E-value: 2.16e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638   1 MVAGESGLGKSTLINSLFLTNLYEDRQVPEASARLTQTLAIERRGVEIEEGGVKVKLTLVDTPGFGDSVDCSDCWLPVVK 80
Cdd:cd01850    8 MVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSDCWKPIVD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638  81 FIEEQFEQYLRDESGLNR-KNIQDSRVHCCLYFISPFGRGLRPLDVAFLRAVHEKVNIIPVIGKADALMPQETQALKQKI 159
Cdd:cd01850   88 YIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEELTEFKKRI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638 160 RDQLKEEEIHIYQFPECdsDEDEDFKRQDAEMKESIPFAVVGSCEVVRDGGnRPVRGRRYSWGTVEVENPHHCDFLNLRR 239
Cdd:cd01850  168 MEDIEENNIKIYKFPED--EEDEEEIEENKKLKSLIPFAIVGSNEEVEVNG-KKVRGRKYPWGVVEVENEEHCDFVKLRN 244
                        250       260
                 ....*....|....*....|....
gi 119572638 240 MLVQTHLQDLKEVTHDLLYEGYRA 263
Cdd:cd01850  245 LLIRTHLQDLKETTHNVHYENYRS 268
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
1-265 1.11e-110

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 324.66  E-value: 1.11e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638   1 MVAGESGLGKSTLINSLFLTNLYEDRQVPEASA-RLTQTLAIERRGVEIEEGGVKVKLTLVDTPGFGDSVDCSDCWLPVV 79
Cdd:COG5019   27 MVVGESGLGKTTFINTLFGTSLVDETEIDDIRAeGTSPTLEIKITKAELEEDGFHLNLTVIDTPGFGDFIDNSKCWEPIV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638  80 KFIEEQFEQYLRDESGLNR-KNIQDSRVHCCLYFISPFGRGLRPLDVAFLRAVHEKVNIIPVIGKADALMPQETQALKQK 158
Cdd:COG5019  107 DYIDDQFDQYLDEEQKIKRnPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKRVNLIPVIAKADTLTDDELAEFKER 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638 159 IRDQLKEEEIHIYQFPECDSDEDEDFkRQDAEMKESIPFAVVGSCEVVRDGGnRPVRGRRYSWGTVEVENPHHCDFLNLR 238
Cdd:COG5019  187 IREDLEQYNIPVFDPYDPEDDEDESL-EENQDLRSLIPFAIIGSNTEIENGG-EQVRGRKYPWGVVEIDDEEHSDFKKLR 264
                        250       260
                 ....*....|....*....|....*..
gi 119572638 239 RMLVQTHLQDLKEVTHDLLYEGYRAAV 265
Cdd:COG5019  265 NLLIRTHLQELKETTENLLYENYRTEK 291
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
2-64 2.06e-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: 40.82  E-value: 2.06e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119572638    2 VAGESGLGKSTLINSLfltnLYEDRQVPEASARLTQTLAIErrgvEIEEGGVKVKLTLVDTPG 64
Cdd:TIGR00231   6 IVGHPNVGKSTLLNSL----LGNKGSITEYYPGTTRNYVTT----VIEEDGKTYKFNLLDTAG 60
PRK00098 PRK00098
GTPase RsgA; Reviewed
1-65 1.52e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 39.42  E-value: 1.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119572638   1 MVAGESGLGKSTLINSLfltnlyedrqVPEASARLTQTLAIERRG---------VEIEEGGvkvklTLVDTPGF 65
Cdd:PRK00098 168 VLAGQSGVGKSTLLNAL----------APDLELKTGEISEALGRGkhttthvelYDLPGGG-----LLIDTPGF 226
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
1-64 6.33e-03

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


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 36.72  E-value: 6.33e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119572638     1 MVAGESGLGKSTLINSlFLTNLYEDRQVPeasarltqTLAIERRGVEIEEGGVKVKLTLVDTPG 64
Cdd:smart00175   4 ILIGDSGVGKSSLLSR-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 ...
1-263 1.63e-165

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: 459.84  E-value: 1.63e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638    1 MVAGESGLGKSTLINSLFLTNLYEDRQVPEASARLTQTLAIERRGVEIEEGGVKVKLTLVDTPGFGDSVDCSDCWLPVVK 80
Cdd:pfam00735   7 MVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNCWRPIVE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638   81 FIEEQFEQYLRDESGLNRKNIQDSRVHCCLYFISPFGRGLRPLDVAFLRAVHEKVNIIPVIGKADALMPQETQALKQKIR 160
Cdd:pfam00735  87 YIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQRFKKRIR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638  161 DQLKEEEIHIYQFPECDSDEDEDfKRQDAEMKESIPFAVVGSCEVVRDGGnRPVRGRRYSWGTVEVENPHHCDFLNLRRM 240
Cdd:pfam00735 167 EEIERQNIPIYHFPDEESDEDEE-KELNEQLKSSIPFAIVGSNTVIENDG-EKVRGRKYPWGVVEVENPSHCDFLKLRNM 244
                         250       260
                  ....*....|....*....|...
gi 119572638  241 LVQTHLQDLKEVTHDLLYEGYRA 263
Cdd:pfam00735 245 LIRTHLQDLKEVTHELHYETYRS 267
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
1-263 2.16e-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: 424.27  E-value: 2.16e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638   1 MVAGESGLGKSTLINSLFLTNLYEDRQVPEASARLTQTLAIERRGVEIEEGGVKVKLTLVDTPGFGDSVDCSDCWLPVVK 80
Cdd:cd01850    8 MVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSDCWKPIVD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638  81 FIEEQFEQYLRDESGLNR-KNIQDSRVHCCLYFISPFGRGLRPLDVAFLRAVHEKVNIIPVIGKADALMPQETQALKQKI 159
Cdd:cd01850   88 YIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEELTEFKKRI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638 160 RDQLKEEEIHIYQFPECdsDEDEDFKRQDAEMKESIPFAVVGSCEVVRDGGnRPVRGRRYSWGTVEVENPHHCDFLNLRR 239
Cdd:cd01850  168 MEDIEENNIKIYKFPED--EEDEEEIEENKKLKSLIPFAIVGSNEEVEVNG-KKVRGRKYPWGVVEVENEEHCDFVKLRN 244
                        250       260
                 ....*....|....*....|....
gi 119572638 240 MLVQTHLQDLKEVTHDLLYEGYRA 263
Cdd:cd01850  245 LLIRTHLQDLKETTHNVHYENYRS 268
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
1-265 1.11e-110

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 324.66  E-value: 1.11e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638   1 MVAGESGLGKSTLINSLFLTNLYEDRQVPEASA-RLTQTLAIERRGVEIEEGGVKVKLTLVDTPGFGDSVDCSDCWLPVV 79
Cdd:COG5019   27 MVVGESGLGKTTFINTLFGTSLVDETEIDDIRAeGTSPTLEIKITKAELEEDGFHLNLTVIDTPGFGDFIDNSKCWEPIV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638  80 KFIEEQFEQYLRDESGLNR-KNIQDSRVHCCLYFISPFGRGLRPLDVAFLRAVHEKVNIIPVIGKADALMPQETQALKQK 158
Cdd:COG5019  107 DYIDDQFDQYLDEEQKIKRnPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKRVNLIPVIAKADTLTDDELAEFKER 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638 159 IRDQLKEEEIHIYQFPECDSDEDEDFkRQDAEMKESIPFAVVGSCEVVRDGGnRPVRGRRYSWGTVEVENPHHCDFLNLR 238
Cdd:COG5019  187 IREDLEQYNIPVFDPYDPEDDEDESL-EENQDLRSLIPFAIIGSNTEIENGG-EQVRGRKYPWGVVEIDDEEHSDFKKLR 264
                        250       260
                 ....*....|....*....|....*..
gi 119572638 239 RMLVQTHLQDLKEVTHDLLYEGYRAAV 265
Cdd:COG5019  265 NLLIRTHLQELKETTENLLYENYRTEK 291
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
2-171 2.69e-09

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: 55.16  E-value: 2.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638   2 VAGESGLGKSTLINSLFltnlyeDRQVPEASARLTQTLAIERRGVEIEEGgvKVKLTLVDTPGFGDSVDcsdcwlpvvKF 81
Cdd:cd00882    2 VVGRGGVGKSSLLNALL------GGEVGEVSDVPGTTRDPDVYVKELDKG--KVKLVLVDTPGLDEFGG---------LG 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638  82 IEEQFEQYLRdesglnrkniqdsRVHCCLYFISPfGRGLRPLDVAFLRAVH---EKVNIIPVIGKADaLMPQETQALKQK 158
Cdd:cd00882   65 REELARLLLR-------------GADLILLVVDS-TDRESEEDAKLLILRRlrkEGIPIILVGNKID-LLEEREVEELLR 129
                        170
                 ....*....|...
gi 119572638 159 IRDQLKEEEIHIY 171
Cdd:cd00882  130 LEELAKILGVPVF 142
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
3-174 2.94e-09

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: 55.21  E-value: 2.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638   3 AGESGLGKSTLINSLflTNLyedRQVPEASAR--LTQTLAIerrgVEIEEggvkvKLTLVDTPGFG---DSVDCSDCWLP 77
Cdd:cd01876    5 AGRSNVGKSSLINAL--TNR---KKLARTSKTpgRTQLINF----FNVGD-----KFRLVDLPGYGyakVSKEVREKWGK 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638  78 VVkfieeqfEQYLRdesglNRKNIQ------DSRvhcclyfispfgRGLRPLDVAFLR-AVHEKVNIIPVIGKADALMPQ 150
Cdd:cd01876   71 LI-------EEYLE-----NRENLKgvvlliDAR------------HGPTPIDLEMLEfLEELGIPFLIVLTKADKLKKS 126
                        170       180
                 ....*....|....*....|....
gi 119572638 151 ETQALKQKIRDQLKEEEIHIYQFP 174
Cdd:cd01876  127 ELAKVLKKIKEELNLFNILPPVIL 150
YeeP COG3596
Predicted GTPase [General function prediction only];
1-175 1.27e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 55.16  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638   1 MVAGESGLGKSTLINSLFltnlyeDRQVPEASARLTQTLAIERrgVEIEEGGVKVkLTLVDTPGFGDSVDcsdcwlpvvk 80
Cdd:COG3596   43 ALVGKTGAGKSSLINALF------GAEVAEVGVGRPCTREIQR--YRLESDGLPG-LVLLDTPGLGEVNE---------- 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638  81 fiEEQFEQYLRDESglnrkniqdSRVHCCLYFISPFGRGLRpLDVAFLRAVHEKVNIIPVIG---KADALMP-------- 149
Cdd:COG3596  104 --RDREYRELRELL---------PEADLILWVVKADDRALA-TDEEFLQALRAQYPDPPVLVvltQVDRLEPerewdppy 171
                        170       180
                 ....*....|....*....|....*..
gi 119572638 150 -QETQALKQKIRDQLKEEEIHIYQFPE 175
Cdd:COG3596  172 nWPSPPKEQNIRRALEAIAEQLGVPID 198
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
3-68 1.96e-05

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: 43.48  E-value: 1.96e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119572638   3 AGESGLGKSTLINSLFLTNlyedrqVPEASARLTQTLAIERRGVEIEEGGvkvkLTLVDTPGFGDS 68
Cdd:cd11383    3 MGKTGAGKSSLCNALFGTE------VAAVGDRRPTTRAAQAYVWQTGGDG----LVLLDLPGVGER 58
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
1-70 2.07e-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  Cd Length: 248  Bit Score: 45.00  E-value: 2.07e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638   1 MVAGESGLGKSTLINSLFltnlyeDRQVPEASARLTQTLaierRGVEIEEGGVKVKLTLVDTPGFGDSVD 70
Cdd:cd01853   35 LVLGKTGVGKSSTINSIF------GERKVSVSAFQSETL----RPREVSRTVDGFKLNIIDTPGLLESQD 94
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
2-65 1.57e-04

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 41.37  E-value: 1.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119572638    2 VAGESGLGKSTLINSLfLTNLyeDRQVPEASARL-----TQTlaiERRGVEIEEGGVkvkltLVDTPGF 65
Cdd:pfam03193 111 LAGQSGVGKSTLLNAL-LPEL--DLRTGEISEKLgrgrhTTT---HVELFPLPGGGL-----LIDTPGF 168
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
2-64 2.06e-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: 40.82  E-value: 2.06e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119572638    2 VAGESGLGKSTLINSLfltnLYEDRQVPEASARLTQTLAIErrgvEIEEGGVKVKLTLVDTPG 64
Cdd:TIGR00231   6 IVGHPNVGKSTLLNSL----LGNKGSITEYYPGTTRNYVTT----VIEEDGKTYKFNLLDTAG 60
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
2-65 2.57e-04

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: 41.23  E-value: 2.57e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119572638   2 VAGESGLGKSTLINSLFLTnlyEDRQVPEASARLtqtlaieRRG---------VEIEEGGVkvkltLVDTPGF 65
Cdd:cd01854   90 LVGQSGVGKSTLLNALLPE---LVLATGEISEKL-------GRGrhttthrelFPLPGGGL-----IIDTPGF 147
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
2-70 3.78e-04

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that 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. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 40.31  E-value: 3.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119572638   2 VAGESGLGKSTLINSLFltnlyeDRQVPEASARLTQTLAIERRGVEIEEGGvkvKLTLVDTPGFGDSVD 70
Cdd:cd00880    2 IFGRPNVGKSSLLNALL------GQNVGIVSPIPGTTRDPVRKEWELLPLG---PVVLIDTPGLDEEGG 61
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
1-65 4.46e-04

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 39.14  E-value: 4.46e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119572638    1 MVAGESGLGKSTLINSLFltnlyedRQVPEASARLTQTLAIERRGVEIEEggvkVKLTLVDTPGF 65
Cdd:pfam01926   3 ALVGRPNVGKSTLINALT-------GAKAIVSDYPGTTRDPNEGRLELKG----KQIILVDTPGL 56
RsgA COG1162
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
1-65 1.38e-03

Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440776 [Multi-domain]  Cd Length: 300  Bit Score: 39.71  E-value: 1.38e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119572638   1 MVAGESGLGKSTLINSLfltnlyedrqVPEASARlTQTL-AIERRG---------VEIEEGGVkvkltLVDTPGF 65
Cdd:COG1162  170 VLVGQSGVGKSTLINAL----------LPDADLA-TGEIsEKLGRGrhttthaelYPLPGGGW-----LIDTPGF 228
PRK00098 PRK00098
GTPase RsgA; Reviewed
1-65 1.52e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 39.42  E-value: 1.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119572638   1 MVAGESGLGKSTLINSLfltnlyedrqVPEASARLTQTLAIERRG---------VEIEEGGvkvklTLVDTPGF 65
Cdd:PRK00098 168 VLAGQSGVGKSTLLNAL----------APDLELKTGEISEALGRGkhttthvelYDLPGGG-----LLIDTPGF 226
Rab18 cd01863
Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic ...
4-64 2.84e-03

Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic transport and is expressed most highly in polarized epithelial cells. However, trypanosomal Rab, TbRAB18, is upregulated in the BSF (Blood Stream Form) stage and localized predominantly to elements of the Golgi complex. In human and mouse cells, Rab18 has been identified in lipid droplets, organelles that store neutral lipids. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206656 [Multi-domain]  Cd Length: 161  Bit Score: 37.68  E-value: 2.84e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119572638   4 GESGLGKSTLINSlFLTNLYEDrqvpeasaRLTQTLAIERRGVEIEEGGVKVKLTLVDTPG 64
Cdd:cd01863    7 GDSGVGKSSLLLR-FTDDTFDE--------DLSSTIGVDFKVKTVTVDGKKVKLAIWDTAG 58
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
2-70 5.06e-03

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: 37.14  E-value: 5.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119572638   2 VAGESGLGKSTLINSLFLTNLYEDRQVPEaSARLTqTLAIerrgveieegGVKVKLTLVDTPGFGDSVD 70
Cdd:cd09912    5 VVGEFSAGKSTLLNALLGEEVLPTGVTPT-TAVIT-VLRY----------GLLKGVVLVDTPGLNSTIE 61
PRK12289 PRK12289
small ribosomal subunit biogenesis GTPase RsgA;
2-73 5.60e-03

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237040 [Multi-domain]  Cd Length: 352  Bit Score: 37.69  E-value: 5.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119572638   2 VAGESGLGKSTLINSLfltnlyedrqVPEASARLTQTLAIERRG------VEIEE---GGVkvkltLVDTPGFGD-SVDC 71
Cdd:PRK12289 177 VAGPSGVGKSSLINRL----------IPDVELRVGKVSGKLGRGrhttrhVELFElpnGGL-----LADTPGFNQpDLDC 241

                 ..
gi 119572638  72 SD 73
Cdd:PRK12289 242 SP 243
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
1-64 6.33e-03

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


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 36.72  E-value: 6.33e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119572638     1 MVAGESGLGKSTLINSlFLTNLYEDRQVPeasarltqTLAIERRGVEIEEGGVKVKLTLVDTPG 64
Cdd:smart00175   4 ILIGDSGVGKSSLLSR-FTDGKFSEQYKS--------TIGVDFKTKTIEVDGKRVKLQIWDTAG 58
 
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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