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Conserved domains on  [gi|1478051111|ref|NP_443070|]
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septin-1 [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 ...
28-301 2.16e-171

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: 478.33  E-value: 2.16e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111  28 GFDFTLMVAGESGLGKSTLINSLFLTNLYEDRQVPEASARLTQTLAIERRGVEIEEGGVKVKLTLVDTPGFGDSVDCSDC 107
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111 108 WLPVVKFIEEQFEQYLRDESGLNRKNIQDSRVHCCLYFISPFGRGLRPLDVAFLRAVHEKVNIIPVIGKADALMPQETQA 187
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111 188 LKQKIRDQLKEEEIHIYQFPECDSDEDEDfKRQDAEMKESIPFAVVGSCEVVRDGGnRPVRGRRYSWGTVEVENPHHCDF 267
Cdd:pfam00735 161 FKKRIREEIERQNIPIYHFPDEESDEDEE-KELNEQLKSSIPFAIVGSNTVIENDG-EKVRGRKYPWGVVEVENPSHCDF 238
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1478051111 268 LNLRRMLVQTHLQDLKEVTHDLLYEGYRARCLQS 301
Cdd:pfam00735 239 LKLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
 
Name Accession Description Interval E-value
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
28-301 2.16e-171

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: 478.33  E-value: 2.16e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111  28 GFDFTLMVAGESGLGKSTLINSLFLTNLYEDRQVPEASARLTQTLAIERRGVEIEEGGVKVKLTLVDTPGFGDSVDCSDC 107
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111 108 WLPVVKFIEEQFEQYLRDESGLNRKNIQDSRVHCCLYFISPFGRGLRPLDVAFLRAVHEKVNIIPVIGKADALMPQETQA 187
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111 188 LKQKIRDQLKEEEIHIYQFPECDSDEDEDfKRQDAEMKESIPFAVVGSCEVVRDGGnRPVRGRRYSWGTVEVENPHHCDF 267
Cdd:pfam00735 161 FKKRIREEIERQNIPIYHFPDEESDEDEE-KELNEQLKSSIPFAIVGSNTVIENDG-EKVRGRKYPWGVVEVENPSHCDF 238
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1478051111 268 LNLRRMLVQTHLQDLKEVTHDLLYEGYRARCLQS 301
Cdd:pfam00735 239 LKLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
27-302 2.62e-157

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: 442.76  E-value: 2.62e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111  27 KGFDFTLMVAGESGLGKSTLINSLFLTNLYEDRQVPEASARLTQTLAIERRGVEIEEGGVKVKLTLVDTPGFGDSVDCSD 106
Cdd:cd01850     1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111 107 CWLPVVKFIEEQFEQYLRDESGLNR-KNIQDSRVHCCLYFISPFGRGLRPLDVAFLRAVHEKVNIIPVIGKADALMPQET 185
Cdd:cd01850    81 CWKPIVDYIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111 186 QALKQKIRDQLKEEEIHIYQFPECdsDEDEDFKRQDAEMKESIPFAVVGSCEVVRDGGnRPVRGRRYSWGTVEVENPHHC 265
Cdd:cd01850   161 TEFKKRIMEDIEENNIKIYKFPED--EEDEEEIEENKKLKSLIPFAIVGSNEEVEVNG-KKVRGRKYPWGVVEVENEEHC 237
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1478051111 266 DFLNLRRMLVQTHLQDLKEVTHDLLYEGYRARCLQSL 302
Cdd:cd01850   238 DFVKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEAL 274
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
10-354 3.49e-123

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 360.10  E-value: 3.49e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111  10 YVGFAALPNQLHRKSVKKGFDFTLMVAGESGLGKSTLINSLFLTNLYEDRQVPEASA-RLTQTLAIERRGVEIEEGGVKV 88
Cdd:COG5019     3 YVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDETEIDDIRAeGTSPTLEIKITKAELEEDGFHL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111  89 KLTLVDTPGFGDSVDCSDCWLPVVKFIEEQFEQYLRDESGLNR-KNIQDSRVHCCLYFISPFGRGLRPLDVAFLRAVHEK 167
Cdd:COG5019    83 NLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRnPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111 168 VNIIPVIGKADALMPQETQALKQKIRDQLKEEEIHIYQFPECDSDEDEDFkRQDAEMKESIPFAVVGSCEVVRDGGnRPV 247
Cdd:COG5019   163 VNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESL-EENQDLRSLIPFAIIGSNTEIENGG-EQV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111 248 RGRRYSWGTVEVENPHHCDFLNLRRMLVQTHLQDLKEVTHDLLYEGYRARCLQSLAR-PGARDRASRSKLSRQSATEIPl 326
Cdd:COG5019   241 RGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSGLKNsGEPSLKEIHEARLNEEERELK- 319
                         330       340
                  ....*....|....*....|....*...
gi 1478051111 327 pmlplADTEKLIREKDEELRRMQEMLEK 354
Cdd:COG5019   320 -----KKFTEKIREKEKRLEELEQNLIE 342
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
30-97 1.85e-04

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 41.59  E-value: 1.85e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1478051111  30 DFTLMVAGESGLGKSTLINSLfltnLYEDRQVPEASARLTQTLAIErrgvEIEEGGVKVKLTLVDTPG 97
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSL----LGNKGSITEYYPGTTRNYVTT----VIEEDGKTYKFNLLDTAG 60
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
31-97 1.34e-03

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


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 39.03  E-value: 1.34e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1478051111   31 FTLMVAGESGLGKSTLINSlFLTNLYEDRQVPeasarltqTLAIERRGVEIEEGGVKVKLTLVDTPG 97
Cdd:smart00175   1 FKIILIGDSGVGKSSLLSR-FTDGKFSEQYKS--------TIGVDFKTKTIEVDGKRVKLQIWDTAG 58
PLN03118 PLN03118
Rab family protein; Provisional
28-97 1.92e-03

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 39.27  E-value: 1.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1478051111  28 GFD--FTLMVAGESGLGKSTLINSlFLTNLYEDrqvpeasarLTQTLAIERRGVEIEEGGVKVKLTLVDTPG 97
Cdd:PLN03118   10 GYDlsFKILLIGDSGVGKSSLLVS-FISSSVED---------LAPTIGVDFKIKQLTVGGKRLKLTIWDTAG 71
 
Name Accession Description Interval E-value
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
28-301 2.16e-171

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: 478.33  E-value: 2.16e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111  28 GFDFTLMVAGESGLGKSTLINSLFLTNLYEDRQVPEASARLTQTLAIERRGVEIEEGGVKVKLTLVDTPGFGDSVDCSDC 107
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111 108 WLPVVKFIEEQFEQYLRDESGLNRKNIQDSRVHCCLYFISPFGRGLRPLDVAFLRAVHEKVNIIPVIGKADALMPQETQA 187
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111 188 LKQKIRDQLKEEEIHIYQFPECDSDEDEDfKRQDAEMKESIPFAVVGSCEVVRDGGnRPVRGRRYSWGTVEVENPHHCDF 267
Cdd:pfam00735 161 FKKRIREEIERQNIPIYHFPDEESDEDEE-KELNEQLKSSIPFAIVGSNTVIENDG-EKVRGRKYPWGVVEVENPSHCDF 238
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1478051111 268 LNLRRMLVQTHLQDLKEVTHDLLYEGYRARCLQS 301
Cdd:pfam00735 239 LKLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
27-302 2.62e-157

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: 442.76  E-value: 2.62e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111  27 KGFDFTLMVAGESGLGKSTLINSLFLTNLYEDRQVPEASARLTQTLAIERRGVEIEEGGVKVKLTLVDTPGFGDSVDCSD 106
Cdd:cd01850     1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111 107 CWLPVVKFIEEQFEQYLRDESGLNR-KNIQDSRVHCCLYFISPFGRGLRPLDVAFLRAVHEKVNIIPVIGKADALMPQET 185
Cdd:cd01850    81 CWKPIVDYIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111 186 QALKQKIRDQLKEEEIHIYQFPECdsDEDEDFKRQDAEMKESIPFAVVGSCEVVRDGGnRPVRGRRYSWGTVEVENPHHC 265
Cdd:cd01850   161 TEFKKRIMEDIEENNIKIYKFPED--EEDEEEIEENKKLKSLIPFAIVGSNEEVEVNG-KKVRGRKYPWGVVEVENEEHC 237
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1478051111 266 DFLNLRRMLVQTHLQDLKEVTHDLLYEGYRARCLQSL 302
Cdd:cd01850   238 DFVKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEAL 274
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
10-354 3.49e-123

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 360.10  E-value: 3.49e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111  10 YVGFAALPNQLHRKSVKKGFDFTLMVAGESGLGKSTLINSLFLTNLYEDRQVPEASA-RLTQTLAIERRGVEIEEGGVKV 88
Cdd:COG5019     3 YVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDETEIDDIRAeGTSPTLEIKITKAELEEDGFHL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111  89 KLTLVDTPGFGDSVDCSDCWLPVVKFIEEQFEQYLRDESGLNR-KNIQDSRVHCCLYFISPFGRGLRPLDVAFLRAVHEK 167
Cdd:COG5019    83 NLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRnPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111 168 VNIIPVIGKADALMPQETQALKQKIRDQLKEEEIHIYQFPECDSDEDEDFkRQDAEMKESIPFAVVGSCEVVRDGGnRPV 247
Cdd:COG5019   163 VNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESL-EENQDLRSLIPFAIIGSNTEIENGG-EQV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111 248 RGRRYSWGTVEVENPHHCDFLNLRRMLVQTHLQDLKEVTHDLLYEGYRARCLQSLAR-PGARDRASRSKLSRQSATEIPl 326
Cdd:COG5019   241 RGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSGLKNsGEPSLKEIHEARLNEEERELK- 319
                         330       340
                  ....*....|....*....|....*...
gi 1478051111 327 pmlplADTEKLIREKDEELRRMQEMLEK 354
Cdd:COG5019   320 -----KKFTEKIREKEKRLEELEQNLIE 342
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
36-207 6.68e-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: 54.44  E-value: 6.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111  36 AGESGLGKSTLINSLflTNLyedRQVPEASAR--LTQTLAIerrgVEIEEggvkvKLTLVDTPGFG---DSVDCSDCWLP 110
Cdd:cd01876     5 AGRSNVGKSSLINAL--TNR---KKLARTSKTpgRTQLINF----FNVGD-----KFRLVDLPGYGyakVSKEVREKWGK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111 111 VVkfieeqfEQYLRdesglNRKNIQ------DSRvhcclyfispfgRGLRPLDVAFLR-AVHEKVNIIPVIGKADALMPQ 183
Cdd:cd01876    71 LI-------EEYLE-----NRENLKgvvlliDAR------------HGPTPIDLEMLEfLEELGIPFLIVLTKADKLKKS 126
                         170       180
                  ....*....|....*....|....
gi 1478051111 184 ETQALKQKIRDQLKEEEIHIYQFP 207
Cdd:cd01876   127 ELAKVLKKIKEELNLFNILPPVIL 150
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
35-204 7.76e-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: 54.38  E-value: 7.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111  35 VAGESGLGKSTLINSLFltnlyeDRQVPEASARLTQTLAIERRGVEIEEGgvKVKLTLVDTPGFGDSVDcsdcwlpvvKF 114
Cdd:cd00882     2 VVGRGGVGKSSLLNALL------GGEVGEVSDVPGTTRDPDVYVKELDKG--KVKLVLVDTPGLDEFGG---------LG 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111 115 IEEQFEQYLRdesglnrkniqdsRVHCCLYFISPfGRGLRPLDVAFLRAVH---EKVNIIPVIGKADaLMPQETQALKQK 191
Cdd:cd00882    65 REELARLLLR-------------GADLILLVVDS-TDRESEEDAKLLILRRlrkEGIPIILVGNKID-LLEEREVEELLR 129
                         170
                  ....*....|...
gi 1478051111 192 IRDQLKEEEIHIY 204
Cdd:cd00882   130 LEELAKILGVPVF 142
YeeP COG3596
Predicted GTPase [General function prediction only];
31-208 1.63e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 55.54  E-value: 1.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111  31 FTLMVAGESGLGKSTLINSLFltnlyeDRQVPEASARLTQTLAIERrgVEIEEGGVKVkLTLVDTPGFGDSVDcsdcwlp 110
Cdd:COG3596    40 PVIALVGKTGAGKSSLINALF------GAEVAEVGVGRPCTREIQR--YRLESDGLPG-LVLLDTPGLGEVNE------- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111 111 vvkfiEEQFEQYLRDESglnrkniqdSRVHCCLYFISPFGRGLRpLDVAFLRAVHEKVNIIPVIG---KADALMP----- 182
Cdd:COG3596   104 -----RDREYRELRELL---------PEADLILWVVKADDRALA-TDEEFLQALRAQYPDPPVLVvltQVDRLEPerewd 168
                         170       180       190
                  ....*....|....*....|....*....|
gi 1478051111 183 ----QETQALKQKIRDQLKEEEIHIYQFPE 208
Cdd:COG3596   169 ppynWPSPPKEQNIRRALEAIAEQLGVPID 198
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
8-103 3.17e-08

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: 53.86  E-value: 3.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111   8 KEYVGFAALPNQLHRK------SVKKGFDFTL--MVAGESGLGKSTLINSLFltnlyeDRQVPEASARLTQTLaierRGV 79
Cdd:cd01853     1 REWVGFQFFPDATQTKlheleaKLKKELDFSLtiLVLGKTGVGKSSTINSIF------GERKVSVSAFQSETL----RPR 70
                          90       100
                  ....*....|....*....|....
gi 1478051111  80 EIEEGGVKVKLTLVDTPGFGDSVD 103
Cdd:cd01853    71 EVSRTVDGFKLNIIDTPGLLESQD 94
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
36-101 3.35e-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: 3.35e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1478051111  36 AGESGLGKSTLINSLFLTNlyedrqVPEASARLTQTLAIERRGVEIEEGGvkvkLTLVDTPGFGDS 101
Cdd:cd11383     3 MGKTGAGKSSLCNALFGTE------VAAVGDRRPTTRAAQAYVWQTGGDG----LVLLDLPGVGER 58
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
32-98 1.14e-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: 42.77  E-value: 1.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1478051111  32 TLMVAGESGLGKSTLINSLFLTnlyEDRQVPEASARLtqtlaieRRG---------VEIEEGGVkvkltLVDTPGF 98
Cdd:cd01854    87 TSVLVGQSGVGKSTLLNALLPE---LVLATGEISEKL-------GRGrhttthrelFPLPGGGL-----IIDTPGF 147
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
30-98 1.28e-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: 42.14  E-value: 1.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1478051111  30 DFTLMVAGESGLGKSTLINSLfLTNLyeDRQVPEASARL-----TQTlaiERRGVEIEEGGVkvkltLVDTPGF 98
Cdd:pfam03193 106 GKTTVLAGQSGVGKSTLLNAL-LPEL--DLRTGEISEKLgrgrhTTT---HVELFPLPGGGL-----LIDTPGF 168
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
30-97 1.85e-04

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 41.59  E-value: 1.85e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1478051111  30 DFTLMVAGESGLGKSTLINSLfltnLYEDRQVPEASARLTQTLAIErrgvEIEEGGVKVKLTLVDTPG 97
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSL----LGNKGSITEYYPGTTRNYVTT----VIEEDGKTYKFNLLDTAG 60
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
31-103 2.19e-04

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


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 41.76  E-value: 2.19e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1478051111  31 FTLMVAGESGLGKSTLINSLFLTNLYEDRQVPEaSARLTqTLAIerrgveieegGVKVKLTLVDTPGFGDSVD 103
Cdd:cd09912     1 FLLAVVGEFSAGKSTLLNALLGEEVLPTGVTPT-TAVIT-VLRY----------GLLKGVVLVDTPGLNSTIE 61
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
32-98 5.49e-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: 5.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1478051111  32 TLMVAGESGLGKSTLINSLFltnlyedRQVPEASARLTQTLAIERRGVEIEEggvkVKLTLVDTPGF 98
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALT-------GAKAIVSDYPGTTRDPNEGRLELKG----KQIILVDTPGL 56
RsgA COG1162
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
32-98 6.62e-04

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


Pssm-ID: 440776 [Multi-domain]  Cd Length: 300  Bit Score: 41.25  E-value: 6.62e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1478051111  32 TLMVAGESGLGKSTLINSLfltnlyedrqVPEASARlTQTL-AIERRG---------VEIEEGGVkvkltLVDTPGF 98
Cdd:COG1162   168 TSVLVGQSGVGKSTLINAL----------LPDADLA-TGEIsEKLGRGrhttthaelYPLPGGGW-----LIDTPGF 228
Rab18 cd01863
Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic ...
31-97 1.02e-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: 39.22  E-value: 1.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1478051111  31 FTLMVAGESGLGKSTLINSlFLTNLYEDrqvpeasaRLTQTLAIERRGVEIEEGGVKVKLTLVDTPG 97
Cdd:cd01863     1 LKILLIGDSGVGKSSLLLR-FTDDTFDE--------DLSSTIGVDFKVKTVTVDGKKVKLAIWDTAG 58
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
35-103 1.06e-03

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: 39.15  E-value: 1.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1478051111  35 VAGESGLGKSTLINSLFltnlyeDRQVPEASARLTQTLAIERRGVEIEEGGvkvKLTLVDTPGFGDSVD 103
Cdd:cd00880     2 IFGRPNVGKSSLLNALL------GQNVGIVSPIPGTTRDPVRKEWELLPLG---PVVLIDTPGLDEEGG 61
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
31-97 1.34e-03

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


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 39.03  E-value: 1.34e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1478051111   31 FTLMVAGESGLGKSTLINSlFLTNLYEDRQVPeasarltqTLAIERRGVEIEEGGVKVKLTLVDTPG 97
Cdd:smart00175   1 FKIILIGDSGVGKSSLLSR-FTDGKFSEQYKS--------TIGVDFKTKTIEVDGKRVKLQIWDTAG 58
PLN03118 PLN03118
Rab family protein; Provisional
28-97 1.92e-03

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 39.27  E-value: 1.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1478051111  28 GFD--FTLMVAGESGLGKSTLINSlFLTNLYEDrqvpeasarLTQTLAIERRGVEIEEGGVKVKLTLVDTPG 97
Cdd:PLN03118   10 GYDlsFKILLIGDSGVGKSSLLVS-FISSSVED---------LAPTIGVDFKIKQLTVGGKRLKLTIWDTAG 71
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
29-101 2.17e-03

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


Pssm-ID: 273381 [Multi-domain]  Cd Length: 763  Bit Score: 39.94  E-value: 2.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1478051111  29 FDFTLMVAGESGLGKSTLINSLFltnlyeDRQVPEASARLTQTLAIErrgvEIeEGGVK-VKLTLVDTPGFGDS 101
Cdd:TIGR00993 117 FSLNILVLGKSGVGKSATINSIF------GEVKFSTDAFGMGTTSVQ----EI-EGLVQgVKIRVIDTPGLKSS 179
PRK00098 PRK00098
GTPase RsgA; Reviewed
34-98 2.58e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 39.42  E-value: 2.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1478051111  34 MVAGESGLGKSTLINSLfltnlyedrqVPEASARLTQTLAIERRG---------VEIEEGGvkvklTLVDTPGF 98
Cdd:PRK00098  168 VLAGQSGVGKSTLLNAL----------APDLELKTGEISEALGRGkhttthvelYDLPGGG-----LLIDTPGF 226
PRK12289 PRK12289
small ribosomal subunit biogenesis GTPase RsgA;
35-106 9.89e-03

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237040 [Multi-domain]  Cd Length: 352  Bit Score: 37.69  E-value: 9.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051111  35 VAGESGLGKSTLINSLfltnlyedrqVPEASARLTQTLAIERRG------VEIEE---GGVkvkltLVDTPGFGD-SVDC 104
Cdd:PRK12289  177 VAGPSGVGKSSLINRL----------IPDVELRVGKVSGKLGRGrhttrhVELFElpnGGL-----LADTPGFNQpDLDC 241

                  ..
gi 1478051111 105 SD 106
Cdd:PRK12289  242 SP 243
 
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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