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Conserved domains on  [gi|1334072139|ref|XP_004645302|]
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septin-4 isoform X1 [Octodon degus]

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 ...
135-407 0e+00

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: 506.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 135 GFDFTLMVAGESGLGKSTLVNSLFLTDLYRDRKLLNAEERIMQTVEITKHAVDIEEKGVRLRLTIVDTPGFGDALNNTEC 214
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 215 WKPVAEYIDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPLDVEFMKALHQRVNIVPILAKADTLTRPEVDL 294
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 295 KKRKIREDIEHFGIKIYQFPDCDSDEDEDfKLQDQALKESIPFAVIGSNTVVEARGRRVRGRLYPWGIVEVENPGHCDFV 374
Cdd:pfam00735 161 FKKRIREEIERQNIPIYHFPDEESDEDEE-KELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1334072139 375 KLRTMLVRTHMQDLKDVTRETHYENYRAQCIQS 407
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 ...
135-407 0e+00

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: 506.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 135 GFDFTLMVAGESGLGKSTLVNSLFLTDLYRDRKLLNAEERIMQTVEITKHAVDIEEKGVRLRLTIVDTPGFGDALNNTEC 214
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 215 WKPVAEYIDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPLDVEFMKALHQRVNIVPILAKADTLTRPEVDL 294
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 295 KKRKIREDIEHFGIKIYQFPDCDSDEDEDfKLQDQALKESIPFAVIGSNTVVEARGRRVRGRLYPWGIVEVENPGHCDFV 374
Cdd:pfam00735 161 FKKRIREEIERQNIPIYHFPDEESDEDEE-KELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1334072139 375 KLRTMLVRTHMQDLKDVTRETHYENYRAQCIQS 407
Cdd:pfam00735 240 KLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
134-408 5.75e-162

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: 458.55  E-value: 5.75e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 134 KGFDFTLMVAGESGLGKSTLVNSLFLTDLYRDRKLLNAEERIMQTVEITKHAVDIEEKGVRLRLTIVDTPGFGDALNNTE 213
Cdd:cd01850     1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 214 CWKPVAEYIDQQFEQYFRDESGLNR-KNIQDNRVHCCLYFISPFGHGLRPLDVEFMKALHQRVNIVPILAKADTLTRPEV 292
Cdd:cd01850    81 CWKPIVDYIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 293 DLKKRKIREDIEHFGIKIYQFPDCdsDEDEDFKLQDQALKESIPFAVIGSNTVVEARGRRVRGRLYPWGIVEVENPGHCD 372
Cdd:cd01850   161 TEFKKRIMEDIEENNIKIYKFPED--EEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCD 238
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1334072139 373 FVKLRTMLVRTHMQDLKDVTRETHYENYRAQCIQSM 408
Cdd:cd01850   239 FVKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEAL 274
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
117-469 1.66e-133

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 390.15  E-value: 1.66e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 117 YVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVNSLFLTDLYRDRKLLNAE-ERIMQTVEITKHAVDIEEKGVRL 195
Cdd:COG5019     3 YVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDETEIDDIRaEGTSPTLEIKITKAELEEDGFHL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 196 RLTIVDTPGFGDALNNTECWKPVAEYIDQQFEQYFRDESGLNR-KNIQDNRVHCCLYFISPFGHGLRPLDVEFMKALHQR 274
Cdd:COG5019    83 NLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRnPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 275 VNIVPILAKADTLTRPEVDLKKRKIREDIEHFGIKIYQFPDCDSDEDEDFKLqDQALKESIPFAVIGSNTVVEARGRRVR 354
Cdd:COG5019   163 VNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESLEE-NQDLRSLIPFAIIGSNTEIENGGEQVR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 355 GRLYPWGIVEVENPGHCDFVKLRTMLVRTHMQDLKDVTRETHYENYRAQ-----------CIQSMTRLVVKERNRnkLTR 423
Cdd:COG5019   242 GRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEklsglknsgepSLKEIHEARLNEEER--ELK 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1334072139 424 ESgtdfpipavppgtdpETEKlIREKDEELRRMQEMLHKIQRQMKE 469
Cdd:COG5019   320 KK---------------FTEK-IREKEKRLEELEQNLIEERKELNS 349
PRK00098 PRK00098
GTPase RsgA; Reviewed
104-205 1.59e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 40.57  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 104 KLDPYDSSEDDKEYVG-FATLPNQVHRKSVKKGFDF----------TLMVAGESGLGKSTLVNSLfltdlyrdrkllnAE 172
Cdd:PRK00098  120 KIDLLDDLEEARELLAlYRAIGYDVLELSAKEGEGLdelkpllagkVTVLAGQSGVGKSTLLNAL-------------AP 186
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1334072139 173 ERIMQTVEI----------TKHA--VDIEEKGvrlrlTIVDTPGF 205
Cdd:PRK00098  187 DLELKTGEIsealgrgkhtTTHVelYDLPGGG-----LLIDTPGF 226
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
137-204 5.60e-03

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 37.74  E-value: 5.60e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1334072139 137 DFTLMVAGESGLGKSTLVNSLfltdLYRDRKLLNAEERIMQTVEITKhavdIEEKGVRLRLTIVDTPG 204
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSL----LGNKGSITEYYPGTTRNYVTTV----IEEDGKTYKFNLLDTAG 60
 
Name Accession Description Interval E-value
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
135-407 0e+00

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: 506.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 135 GFDFTLMVAGESGLGKSTLVNSLFLTDLYRDRKLLNAEERIMQTVEITKHAVDIEEKGVRLRLTIVDTPGFGDALNNTEC 214
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 215 WKPVAEYIDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPLDVEFMKALHQRVNIVPILAKADTLTRPEVDL 294
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 295 KKRKIREDIEHFGIKIYQFPDCDSDEDEDfKLQDQALKESIPFAVIGSNTVVEARGRRVRGRLYPWGIVEVENPGHCDFV 374
Cdd:pfam00735 161 FKKRIREEIERQNIPIYHFPDEESDEDEE-KELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1334072139 375 KLRTMLVRTHMQDLKDVTRETHYENYRAQCIQS 407
Cdd:pfam00735 240 KLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
134-408 5.75e-162

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: 458.55  E-value: 5.75e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 134 KGFDFTLMVAGESGLGKSTLVNSLFLTDLYRDRKLLNAEERIMQTVEITKHAVDIEEKGVRLRLTIVDTPGFGDALNNTE 213
Cdd:cd01850     1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 214 CWKPVAEYIDQQFEQYFRDESGLNR-KNIQDNRVHCCLYFISPFGHGLRPLDVEFMKALHQRVNIVPILAKADTLTRPEV 292
Cdd:cd01850    81 CWKPIVDYIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 293 DLKKRKIREDIEHFGIKIYQFPDCdsDEDEDFKLQDQALKESIPFAVIGSNTVVEARGRRVRGRLYPWGIVEVENPGHCD 372
Cdd:cd01850   161 TEFKKRIMEDIEENNIKIYKFPED--EEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCD 238
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1334072139 373 FVKLRTMLVRTHMQDLKDVTRETHYENYRAQCIQSM 408
Cdd:cd01850   239 FVKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEAL 274
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
117-469 1.66e-133

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 390.15  E-value: 1.66e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 117 YVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVNSLFLTDLYRDRKLLNAE-ERIMQTVEITKHAVDIEEKGVRL 195
Cdd:COG5019     3 YVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDETEIDDIRaEGTSPTLEIKITKAELEEDGFHL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 196 RLTIVDTPGFGDALNNTECWKPVAEYIDQQFEQYFRDESGLNR-KNIQDNRVHCCLYFISPFGHGLRPLDVEFMKALHQR 274
Cdd:COG5019    83 NLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRnPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 275 VNIVPILAKADTLTRPEVDLKKRKIREDIEHFGIKIYQFPDCDSDEDEDFKLqDQALKESIPFAVIGSNTVVEARGRRVR 354
Cdd:COG5019   163 VNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESLEE-NQDLRSLIPFAIIGSNTEIENGGEQVR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 355 GRLYPWGIVEVENPGHCDFVKLRTMLVRTHMQDLKDVTRETHYENYRAQ-----------CIQSMTRLVVKERNRnkLTR 423
Cdd:COG5019   242 GRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEklsglknsgepSLKEIHEARLNEEER--ELK 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1334072139 424 ESgtdfpipavppgtdpETEKlIREKDEELRRMQEMLHKIQRQMKE 469
Cdd:COG5019   320 KK---------------FTEK-IREKEKRLEELEQNLIEERKELNS 349
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
143-314 4.30e-08

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: 52.51  E-value: 4.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 143 AGESGLGKSTLVNSLFltdlyRDRKLlnAeeRIMQTVEITKHAV--DIEEKgvrlrLTIVDTPGFGDALNNtecwKPVAE 220
Cdd:cd01876     5 AGRSNVGKSSLINALT-----NRKKL--A--RTSKTPGRTQLINffNVGDK-----FRLVDLPGYGYAKVS----KEVRE 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 221 YIDQQFEQYFRdesglNRKNIqdnrvhCCLYFISPFGHGLRPLDVEFMKAL-HQRVNIVPILAKADTLTRPEVDLKKRKI 299
Cdd:cd01876    67 KWGKLIEEYLE-----NRENL------KGVVLLIDARHGPTPIDLEMLEFLeELGIPFLIVLTKADKLKKSELAKVLKKI 135
                         170
                  ....*....|....*
gi 1334072139 300 REDIEHFGIKIYQFP 314
Cdd:cd01876   136 KEELNLFNILPPVIL 150
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
142-208 4.84e-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: 46.68  E-value: 4.84e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1334072139 142 VAGESGLGKSTLVNSLFltdlyrDRKLLNAEERIMQTVEITKHAVDIEEKGVrlRLTIVDTPGFGDA 208
Cdd:cd00882     2 VVGRGGVGKSSLLNALL------GGEVGEVSDVPGTTRDPDVYVKELDKGKV--KLVLVDTPGLDEF 60
YeeP COG3596
Predicted GTPase [General function prediction only];
138-224 2.13e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 46.30  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 138 FTLMVAGESGLGKSTLVNSLFLTDLyrdrkllnAE--ERIMQTVEItkHAVDIEEKGVRLrLTIVDTPGFGDALNNTECW 215
Cdd:COG3596    40 PVIALVGKTGAGKSSLINALFGAEV--------AEvgVGRPCTREI--QRYRLESDGLPG-LVLLDTPGLGEVNERDREY 108

                  ....*....
gi 1334072139 216 KPVAEYIDQ 224
Cdd:COG3596   109 RELRELLPE 117
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
115-205 6.38e-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: 44.23  E-value: 6.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 115 KEYVGFATLPNQVHRK------SVKKGFDFTL--MVAGESGLGKSTLVNSLF-----LTDLYRdrkllNAEERIMQtvei 181
Cdd:cd01853     1 REWVGFQFFPDATQTKlheleaKLKKELDFSLtiLVLGKTGVGKSSTINSIFgerkvSVSAFQ-----SETLRPRE---- 71
                          90       100
                  ....*....|....*....|....
gi 1334072139 182 tkhaVDIEEKGVrlRLTIVDTPGF 205
Cdd:cd01853    72 ----VSRTVDGF--KLNIIDTPGL 89
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
139-205 8.90e-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: 40.46  E-value: 8.90e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1334072139 139 TLMVAGESGLGKSTLVNSLfltdlyrdrkllnAEERIMQTVEI----------TKHA--VDIEEKGVrlrltIVDTPGF 205
Cdd:cd01854    87 TSVLVGQSGVGKSTLLNAL-------------LPELVLATGEIseklgrgrhtTTHRelFPLPGGGL-----IIDTPGF 147
PRK00098 PRK00098
GTPase RsgA; Reviewed
104-205 1.59e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 40.57  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334072139 104 KLDPYDSSEDDKEYVG-FATLPNQVHRKSVKKGFDF----------TLMVAGESGLGKSTLVNSLfltdlyrdrkllnAE 172
Cdd:PRK00098  120 KIDLLDDLEEARELLAlYRAIGYDVLELSAKEGEGLdelkpllagkVTVLAGQSGVGKSTLLNAL-------------AP 186
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1334072139 173 ERIMQTVEI----------TKHA--VDIEEKGvrlrlTIVDTPGF 205
Cdd:PRK00098  187 DLELKTGEIsealgrgkhtTTHVelYDLPGGG-----LLIDTPGF 226
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
143-208 2.45e-03

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


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 38.09  E-value: 2.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1334072139 143 AGESGLGKSTLVNSLFLTDLYRdrkllnAEERIMQTVEITKHAVDIEEKGvrlrLTIVDTPGFGDA 208
Cdd:cd11383     3 MGKTGAGKSSLCNALFGTEVAA------VGDRRPTTRAAQAYVWQTGGDG----LVLLDLPGVGER 58
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
137-204 5.60e-03

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 37.74  E-value: 5.60e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1334072139 137 DFTLMVAGESGLGKSTLVNSLfltdLYRDRKLLNAEERIMQTVEITKhavdIEEKGVRLRLTIVDTPG 204
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSL----LGNKGSITEYYPGTTRNYVTTV----IEEDGKTYKFNLLDTAG 60
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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