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Conserved domains on  [gi|24642603|ref|NP_728005|]
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septin 4, isoform D [Drosophila melanogaster]

Protein Classification

septin family protein( domain architecture ID 10110922)

septin family protein, a filament-forming cytoskeletal GTPase, is involved in various cellular processes, including cytoskeleton organization, cytokinesis, and membrane dynamics

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
82-357 1.74e-155

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: 440.44  E-value: 1.74e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603  82 RGFEFTLMVVGESGLGKSTLINSLFLGDLYKNRQMPNVEERIEKTTKVEKKTMDIEERGVRLRLTVVDTPGFGDAINCED 161
Cdd:cd01850   1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603 162 SWRVCTQYIDEQFRQYFTDESGLNR-RNIQDNRVHCCLYFVPPWGHSLRQMDLDLIRRLHRKVNIVLVIGKADCLNKQEV 240
Cdd:cd01850  81 CWKPIVDYIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603 241 RKLKERILQDLEDNHIQLYQFPECdsDEDDDFKQQDRELKASIPFAVVGSNTILEVAGKKVRGRQYPWGVVNVEDPEHSD 320
Cdd:cd01850 161 TEFKKRIMEDIEENNIKIYKFPED--EEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCD 238
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 24642603 321 FIKLRTFLISTHMQDLKDTTQDVHYENFRAQCISQIS 357
Cdd:cd01850 239 FVKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
82-357 1.74e-155

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: 440.44  E-value: 1.74e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603  82 RGFEFTLMVVGESGLGKSTLINSLFLGDLYKNRQMPNVEERIEKTTKVEKKTMDIEERGVRLRLTVVDTPGFGDAINCED 161
Cdd:cd01850   1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603 162 SWRVCTQYIDEQFRQYFTDESGLNR-RNIQDNRVHCCLYFVPPWGHSLRQMDLDLIRRLHRKVNIVLVIGKADCLNKQEV 240
Cdd:cd01850  81 CWKPIVDYIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603 241 RKLKERILQDLEDNHIQLYQFPECdsDEDDDFKQQDRELKASIPFAVVGSNTILEVAGKKVRGRQYPWGVVNVEDPEHSD 320
Cdd:cd01850 161 TEFKKRIMEDIEENNIKIYKFPED--EEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCD 238
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 24642603 321 FIKLRTFLISTHMQDLKDTTQDVHYENFRAQCISQIS 357
Cdd:cd01850 239 FVKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
83-354 1.72e-152

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: 432.49  E-value: 1.72e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603    83 GFEFTLMVVGESGLGKSTLINSLFLGDLYKNRQMPNVEERIEKTTKVEKKTMDIEERGVRLRLTVVDTPGFGDAINCEDS 162
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603   163 WRVCTQYIDEQFRQYFTDESGLNRRNIQDNRVHCCLYFVPPWGHSLRQMDLDLIRRLHRKVNIVLVIGKADCLNKQEVRK 242
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603   243 LKERILQDLEDNHIQLYQFPECDSDEDDDfKQQDRELKASIPFAVVGSNTILEVAGKKVRGRQYPWGVVNVEDPEHSDFI 322
Cdd:pfam00735 161 FKKRIREEIERQNIPIYHFPDEESDEDEE-KELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239
                         250       260       270
                  ....*....|....*....|....*....|..
gi 24642603   323 KLRTFLISTHMQDLKDTTQDVHYENFRAQCIS 354
Cdd:pfam00735 240 KLRNMLIRTHLQDLKEVTHELHYETYRSEKLS 271
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
65-420 5.43e-118

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 348.93  E-value: 5.43e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603  65 YIGFATLPEQVHRKSVKRGFEFTLMVVGESGLGKSTLINSLFLGDLYKNRQMPNVE-ERIEKTTKVEKKTMDIEERGVRL 143
Cdd:COG5019   3 YVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDETEIDDIRaEGTSPTLEIKITKAELEEDGFHL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603 144 RLTVVDTPGFGDAINCEDSWRVCTQYIDEQFRQYFTDESGLNRRN-IQDNRVHCCLYFVPPWGHSLRQMDLDLIRRLHRK 222
Cdd:COG5019  83 NLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPkFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKR 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603 223 VNIVLVIGKADCLNKQEVRKLKERILQDLEDNHIQLYqFPECDSDEDDDFKQQDRELKASIPFAVVGSNTILEVAGKKVR 302
Cdd:COG5019 163 VNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVF-DPYDPEDDEDESLEENQDLRSLIPFAIIGSNTEIENGGEQVR 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603 303 GRQYPWGVVNVEDPEHSDFIKLRTFLISTHMQDLKDTTQDVHYENFRAqciSQISQHALRERGKLKRDSisstngfDAAI 382
Cdd:COG5019 242 GRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRT---EKLSGLKNSGEPSLKEIH-------EARL 311
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 24642603 383 SETDRLLLQK-DEEIRRMQDMLTQMQEKLKQTHLmEMKK 420
Cdd:COG5019 312 NEEERELKKKfTEKIREKEKRLEELEQNLIEERK-ELNS 349
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
82-357 1.74e-155

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: 440.44  E-value: 1.74e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603  82 RGFEFTLMVVGESGLGKSTLINSLFLGDLYKNRQMPNVEERIEKTTKVEKKTMDIEERGVRLRLTVVDTPGFGDAINCED 161
Cdd:cd01850   1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603 162 SWRVCTQYIDEQFRQYFTDESGLNR-RNIQDNRVHCCLYFVPPWGHSLRQMDLDLIRRLHRKVNIVLVIGKADCLNKQEV 240
Cdd:cd01850  81 CWKPIVDYIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603 241 RKLKERILQDLEDNHIQLYQFPECdsDEDDDFKQQDRELKASIPFAVVGSNTILEVAGKKVRGRQYPWGVVNVEDPEHSD 320
Cdd:cd01850 161 TEFKKRIMEDIEENNIKIYKFPED--EEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCD 238
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 24642603 321 FIKLRTFLISTHMQDLKDTTQDVHYENFRAQCISQIS 357
Cdd:cd01850 239 FVKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
83-354 1.72e-152

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: 432.49  E-value: 1.72e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603    83 GFEFTLMVVGESGLGKSTLINSLFLGDLYKNRQMPNVEERIEKTTKVEKKTMDIEERGVRLRLTVVDTPGFGDAINCEDS 162
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603   163 WRVCTQYIDEQFRQYFTDESGLNRRNIQDNRVHCCLYFVPPWGHSLRQMDLDLIRRLHRKVNIVLVIGKADCLNKQEVRK 242
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603   243 LKERILQDLEDNHIQLYQFPECDSDEDDDfKQQDRELKASIPFAVVGSNTILEVAGKKVRGRQYPWGVVNVEDPEHSDFI 322
Cdd:pfam00735 161 FKKRIREEIERQNIPIYHFPDEESDEDEE-KELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239
                         250       260       270
                  ....*....|....*....|....*....|..
gi 24642603   323 KLRTFLISTHMQDLKDTTQDVHYENFRAQCIS 354
Cdd:pfam00735 240 KLRNMLIRTHLQDLKEVTHELHYETYRSEKLS 271
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
65-420 5.43e-118

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 348.93  E-value: 5.43e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603  65 YIGFATLPEQVHRKSVKRGFEFTLMVVGESGLGKSTLINSLFLGDLYKNRQMPNVE-ERIEKTTKVEKKTMDIEERGVRL 143
Cdd:COG5019   3 YVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDETEIDDIRaEGTSPTLEIKITKAELEEDGFHL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603 144 RLTVVDTPGFGDAINCEDSWRVCTQYIDEQFRQYFTDESGLNRRN-IQDNRVHCCLYFVPPWGHSLRQMDLDLIRRLHRK 222
Cdd:COG5019  83 NLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPkFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKR 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603 223 VNIVLVIGKADCLNKQEVRKLKERILQDLEDNHIQLYqFPECDSDEDDDFKQQDRELKASIPFAVVGSNTILEVAGKKVR 302
Cdd:COG5019 163 VNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVF-DPYDPEDDEDESLEENQDLRSLIPFAIIGSNTEIENGGEQVR 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603 303 GRQYPWGVVNVEDPEHSDFIKLRTFLISTHMQDLKDTTQDVHYENFRAqciSQISQHALRERGKLKRDSisstngfDAAI 382
Cdd:COG5019 242 GRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRT---EKLSGLKNSGEPSLKEIH-------EARL 311
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 24642603 383 SETDRLLLQK-DEEIRRMQDMLTQMQEKLKQTHLmEMKK 420
Cdd:COG5019 312 NEEERELKKKfTEKIREKEKRLEELEQNLIEERK-ELNS 349
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
90-255 1.99e-11

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: 62.09  E-value: 1.99e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603  90 VVGESGLGKSTLINSLFlgdlykNRQMPNVEERIEKTTKVEKKTMDIEERGVRLRLtvVDTPGFGDainCEDSWRvctqy 169
Cdd:cd00882   2 VVGRGGVGKSSLLNALL------GGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVL--VDTPGLDE---FGGLGR----- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603 170 iDEQFRQYFtdesglnrrniqdNRVHCCLYFVPP--WGHSLRQMDLDLIRRLHRKVNIVLVIGKADCLNKQEVRKLKERI 247
Cdd:cd00882  66 -EELARLLL-------------RGADLILLVVDStdRESEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLE 131

                ....*...
gi 24642603 248 LQDLEDNH 255
Cdd:cd00882 132 ELAKILGV 139
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
84-259 8.76e-08

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 51.91  E-value: 8.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603  84 FEFTLMVVGESGLGKSTLINSlFLGDlyknrqmpNVEERIEKTT---KVEKKTMDIEERGVRLRLtvVDTPGfgdaince 160
Cdd:COG1100   2 GEKKIVVVGTGGVGKTSLVNR-LVGD--------IFSLEKYLSTngvTIDKKELKLDGLDVDLVI--WDTPG-------- 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603 161 dswrvctQYIDEQFRQYFTDEsgLNRRNIqdnrvhcCLYFV----PPWGHSLRQMdLDLIRRLHRKVNIVLVIGKADCLN 236
Cdd:COG1100  63 -------QDEFRETRQFYARQ--LTGASL-------YLFVVdgtrEETLQSLYEL-LESLRRLGKKSPIILVLNKIDLYD 125
                       170       180
                ....*....|....*....|...
gi 24642603 237 KQEVRKlKERILQDLEDNHIQLY 259
Cdd:COG1100 126 EEEIED-EERLKEALSEDNIVEV 147
YeeP COG3596
Predicted GTPase [General function prediction only];
85-235 2.97e-06

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 48.99  E-value: 2.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603  85 EFTLMVVGESGLGKSTLINSLFlgdlyknrqmpnvEERIEKTTKVEKKTMDIE----ERGVRLRLTVVDTPGFGDAince 160
Cdd:COG3596  39 PPVIALVGKTGAGKSSLINALF-------------GAEVAEVGVGRPCTREIQryrlESDGLPGLVLLDTPGLGEV---- 101
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24642603 161 dswrvctQYIDEQFRQYftdesglnRRNIQdnRVHCCLYFVPPwGHSLRQMDLDLIRRLHRKVN---IVLVIGKADCL 235
Cdd:COG3596 102 -------NERDREYREL--------RELLP--EADLILWVVKA-DDRALATDEEFLQALRAQYPdppVLVVLTQVDRL 161
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
91-259 2.73e-05

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: 44.42  E-value: 2.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603  91 VGESGLGKSTLINSLFlgdlyKNRQMPnveerieKTTKVEKKTMDIEERGVRLRLTVVDTPGFGDAiNCEDSWRvctQYI 170
Cdd:cd01876   5 AGRSNVGKSSLINALT-----NRKKLA-------RTSKTPGRTQLINFFNVGDKFRLVDLPGYGYA-KVSKEVR---EKW 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603 171 DEQFRQYFTdesglNRRNIQ------DNRvhcclyfvppwgHSLRQMDLDLIRRL-HRKVNIVLVIGKADCLNKQEVRKL 243
Cdd:cd01876  69 GKLIEEYLE-----NRENLKgvvlliDAR------------HGPTPIDLEMLEFLeELGIPFLIVLTKADKLKKSELAKV 131
                       170       180
                ....*....|....*....|
gi 24642603 244 ----KERILQDLEDNHIQLY 259
Cdd:cd01876 132 lkkiKEELNLFNILPPVILF 151
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
84-173 4.76e-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  Cd Length: 248  Bit Score: 44.62  E-value: 4.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603  84 FEFTLMVVGESGLGKSTLINSLFlgdlyknrqmpnvEERIEKTTKVEKKTMDIEE-RGVR--LRLTVVDTPGFgdaincE 160
Cdd:cd01853  30 FSLTILVLGKTGVGKSSTINSIF-------------GERKVSVSAFQSETLRPREvSRTVdgFKLNIIDTPGL------L 90
                        90
                ....*....|...
gi 24642603 161 DSWRvctQYIDEQ 173
Cdd:cd01853  91 ESQD---QRVNRK 100
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
90-256 1.03e-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: 42.62  E-value: 1.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603  90 VVGESGLGKSTLINSLFLGDLYKNRQMPNVeeriekTTKVEKKTM-DIEERGVRLrltvVDTPGFGDAINcEDSWRVctq 168
Cdd:cd00880   2 IFGRPNVGKSSLLNALLGQNVGIVSPIPGT------TRDPVRKEWeLLPLGPVVL----IDTPGLDEEGG-LGRERV--- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603 169 yidEQFRQYFtdesglnrrniqdNRVHCCLyFVPPWGHSLRQMDLDLIRRLHRKVNIVLVIGKADCL-NKQEVRKLKERI 247
Cdd:cd00880  68 ---EEARQVA-------------DRADLVL-LVVDSDLTPVEEEAKLGLLRERGKPVLLVLNKIDLVpESEEEELLRERK 130

                ....*....
gi 24642603 248 LQDLEDNHI 256
Cdd:cd00880 131 LELLPDLPV 139
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
87-231 1.39e-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: 41.07  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642603    87 TLMVVGESGLGKSTLINSLFlgdlyknrqmpnveERIEKTTKVEKKTMDIEERGVRL---RLTVVDTPGFgdaincedsw 163
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALT--------------GAKAIVSDYPGTTRDPNEGRLELkgkQIILVDTPGL---------- 56
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24642603   164 rvctqyIDEqfrqyFTDESGLNRRNIQDNRVHCCLYFVPPwGHSLRQMDLDLIRRLHR-KVNIVLVIGK 231
Cdd:pfam01926  57 ------IEG-----ASEGEGLGRAFLAIIEADLILFVVDS-EEGITPLDEELLELLREnKKPIILVLNK 113
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
91-156 2.40e-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: 41.17  E-value: 2.40e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24642603  91 VGESGLGKSTLINSLFLGDLyknrqmPNVEERIEKTTKVEKKTMDIEERGvrlrLTVVDTPGFGDA 156
Cdd:cd11383   3 MGKTGAGKSSLCNALFGTEV------AAVGDRRPTTRAAQAYVWQTGGDG----LVLLDLPGVGER 58
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
87-153 4.11e-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: 4.11e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24642603  87 TLMVVGESGLGKSTLINSLfLGDLykNRQMPNVEERIEK----TTKVEkkTMDIEERGVrlrltVVDTPGF 153
Cdd:cd01854  87 TSVLVGQSGVGKSTLLNAL-LPEL--VLATGEISEKLGRgrhtTTHRE--LFPLPGGGL-----IIDTPGF 147
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
87-153 2.40e-03

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: 38.68  E-value: 2.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24642603    87 TLMVVGESGLGKSTLINSLfLGDLykNRQMPNVEERIEK----TTKVEkkTMDIEERGVrlrltVVDTPGF 153
Cdd:pfam03193 108 TTVLAGQSGVGKSTLLNAL-LPEL--DLRTGEISEKLGRgrhtTTHVE--LFPLPGGGL-----LIDTPGF 168
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
89-153 5.73e-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: 37.63  E-value: 5.73e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24642603  89 MVVGESGLGKSTLINSLfLGDLYKNRQMPNVEERIeKTTKVEKKTMDIEERGVRLRLTVVDTPGF 153
Cdd:cd01855 129 YVVGATNVGKSTLINAL-LKSNGGKVQAQALVQRL-TVSPIPGTTLGLIKIPLGEGKKLYDTPGI 191
 
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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