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Conserved domains on  [gi|1768365543|ref|NP_001362228|]
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septin-7 isoform 4 [Homo sapiens]

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 ...
1-264 5.27e-163

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: 457.78  E-value: 5.27e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543   1 MVVGESGLGKSTLINSLFLTDLYSPEYPG-PSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVID 79
Cdd:cd01850     8 MVVGESGLGKSTFINTLFGTKLYPSKYPPaPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSDCWKPIVD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543  80 YIDSKFEDYLNAESRVNR-RQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQI 158
Cdd:cd01850    88 YIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEELTEFKKRI 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543 159 MKEIQEHKIKIYEFPETD-DEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNMLI 237
Cdd:cd01850   168 MEDIEENNIKIYKFPEDEeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFVKLRNLLI 247
                         250       260
                  ....*....|....*....|....*..
gi 1768365543 238 RTHMQDLKDVTNNVHYENYRSRKLAAV 264
Cdd:cd01850   248 RTHLQDLKETTHNVHYENYRSEKLEAL 274
PRK12704 super family cl36166
phosphodiesterase; Provisional
284-380 4.61e-04

phosphodiesterase; Provisional


The actual alignment was detected with superfamily member PRK12704:

Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543 284 AQMEEERREHVAKMKKMEMEMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEaqhkELEEKRRQFEDEKANWEAQQR 363
Cdd:PRK12704   49 KEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE----LLEKREEELEKKEKELEQKQQ 124
                          90
                  ....*....|....*..
gi 1768365543 364 ILEQQNSsrTLEKNKKK 380
Cdd:PRK12704  125 ELEKKEE--ELEELIEE 139
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
1-264 5.27e-163

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: 457.78  E-value: 5.27e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543   1 MVVGESGLGKSTLINSLFLTDLYSPEYPG-PSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVID 79
Cdd:cd01850     8 MVVGESGLGKSTFINTLFGTKLYPSKYPPaPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSDCWKPIVD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543  80 YIDSKFEDYLNAESRVNR-RQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQI 158
Cdd:cd01850    88 YIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEELTEFKKRI 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543 159 MKEIQEHKIKIYEFPETD-DEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNMLI 237
Cdd:cd01850   168 MEDIEENNIKIYKFPEDEeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFVKLRNLLI 247
                         250       260
                  ....*....|....*....|....*..
gi 1768365543 238 RTHMQDLKDVTNNVHYENYRSRKLAAV 264
Cdd:cd01850   248 RTHLQDLKETTHNVHYENYRSEKLEAL 274
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
1-263 3.83e-157

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: 442.89  E-value: 3.83e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543   1 MVVGESGLGKSTLINSLFLTDLYSPE-YPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVID 79
Cdd:pfam00735   7 MVVGESGLGKTTFINTLFLTDLYRARgIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNCWRPIVE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543  80 YIDSKFEDYLNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQIM 159
Cdd:pfam00735  87 YIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQRFKKRIR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543 160 KEIQEHKIKIYEFP--ETDDEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNMLI 237
Cdd:pfam00735 167 EEIERQNIPIYHFPdeESDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFLKLRNMLI 246
                         250       260
                  ....*....|....*....|....*.
gi 1768365543 238 RTHMQDLKDVTNNVHYENYRSRKLAA 263
Cdd:pfam00735 247 RTHLQDLKEVTHELHYETYRSEKLSA 272
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
1-357 1.97e-129

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 376.28  E-value: 1.97e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543   1 MVVGESGLGKSTLINSLFLTDLYS--PEYPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVI 78
Cdd:COG5019    27 MVVGESGLGKTTFINTLFGTSLVDetEIDDIRAEGTSPTLEIKITKAELEEDGFHLNLTVIDTPGFGDFIDNSKCWEPIV 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543  79 DYIDSKFEDYLNAESRVNR-RQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQ 157
Cdd:COG5019   107 DYIDDQFDQYLDEEQKIKRnPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKRVNLIPVIAKADTLTDDELAEFKER 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543 158 IMKEIQEHKIKIYE--FPETDDEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNM 235
Cdd:COG5019   187 IREDLEQYNIPVFDpyDPEDDEDESLEENQDLRSLIPFAIIGSNTEIENGGEQVRGRKYPWGVVEIDDEEHSDFKKLRNL 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543 236 LIRTHMQDLKDVTNNVHYENYRSRKLAAvtyngvDNNKNKGQLTKSPLAQMEEERREhvakmkkmemeMEQVFEMKVKEK 315
Cdd:COG5019   267 LIRTHLQELKETTENLLYENYRTEKLSG------LKNSGEPSLKEIHEARLNEEERE-----------LKKKFTEKIREK 329
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1768365543 316 VQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEDEKAN 357
Cdd:COG5019   330 EKRLEELEQNLIEERKELNSKLEEIQKKLEDLEKRLEKLKSN 371
PRK12704 PRK12704
phosphodiesterase; Provisional
284-380 4.61e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543 284 AQMEEERREHVAKMKKMEMEMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEaqhkELEEKRRQFEDEKANWEAQQR 363
Cdd:PRK12704   49 KEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE----LLEKREEELEKKEKELEQKQQ 124
                          90
                  ....*....|....*..
gi 1768365543 364 ILEQQNSsrTLEKNKKK 380
Cdd:PRK12704  125 ELEKKEE--ELEELIEE 139
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
311-383 6.63e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 6.63e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1768365543 311 KVKEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEDEKANWEAQQRILEQQNSSRTLEKNKKKGKI 383
Cdd:COG3883   140 ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
2-63 1.54e-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: 38.89  E-value: 1.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1768365543   2 VVGESGLGKSTLINSLFLTDLYSPEYpgpshriKKTVQVEQSKVLIKEGGVQLLLTIVDTPG 63
Cdd:TIGR00231   6 IVGHPNVGKSTLLNSLLGNKGSITEY-------YPGTTRNYVTTVIEEDGKTYKFNLLDTAG 60
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
275-380 1.98e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.32  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543 275 KGQLTKSPLAQMEEERREHVAKMKKMEMEMEQ--VFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQ----HKEL---- 344
Cdd:pfam15709 393 KQRLEEERQRQEEEERKQRLQLQAAQERARQQqeEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQlaeeQKRLmema 472
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1768365543 345 EEKR------RQFEDEKANWEAQQRILEQQNSSRTLEKNKKK 380
Cdd:pfam15709 473 EEERleyqrqKQEAEEKARLEAEERRQKEEEAARLALEEAMK 514
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
313-382 9.92e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.11  E-value: 9.92e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1768365543  313 KEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQF-EDEKANWEAQQRILEQQNSSRTLEKNKKKGK 382
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVsELEEEIEELQKELYALANEISRLEQQKQILR 308
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
1-264 5.27e-163

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: 457.78  E-value: 5.27e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543   1 MVVGESGLGKSTLINSLFLTDLYSPEYPG-PSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVID 79
Cdd:cd01850     8 MVVGESGLGKSTFINTLFGTKLYPSKYPPaPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSDCWKPIVD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543  80 YIDSKFEDYLNAESRVNR-RQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQI 158
Cdd:cd01850    88 YIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEELTEFKKRI 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543 159 MKEIQEHKIKIYEFPETD-DEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNMLI 237
Cdd:cd01850   168 MEDIEENNIKIYKFPEDEeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFVKLRNLLI 247
                         250       260
                  ....*....|....*....|....*..
gi 1768365543 238 RTHMQDLKDVTNNVHYENYRSRKLAAV 264
Cdd:cd01850   248 RTHLQDLKETTHNVHYENYRSEKLEAL 274
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
1-263 3.83e-157

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: 442.89  E-value: 3.83e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543   1 MVVGESGLGKSTLINSLFLTDLYSPE-YPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVID 79
Cdd:pfam00735   7 MVVGESGLGKTTFINTLFLTDLYRARgIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNCWRPIVE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543  80 YIDSKFEDYLNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQIM 159
Cdd:pfam00735  87 YIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQRFKKRIR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543 160 KEIQEHKIKIYEFP--ETDDEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNMLI 237
Cdd:pfam00735 167 EEIERQNIPIYHFPdeESDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFLKLRNMLI 246
                         250       260
                  ....*....|....*....|....*.
gi 1768365543 238 RTHMQDLKDVTNNVHYENYRSRKLAA 263
Cdd:pfam00735 247 RTHLQDLKEVTHELHYETYRSEKLSA 272
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
1-357 1.97e-129

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 376.28  E-value: 1.97e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543   1 MVVGESGLGKSTLINSLFLTDLYS--PEYPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVI 78
Cdd:COG5019    27 MVVGESGLGKTTFINTLFGTSLVDetEIDDIRAEGTSPTLEIKITKAELEEDGFHLNLTVIDTPGFGDFIDNSKCWEPIV 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543  79 DYIDSKFEDYLNAESRVNR-RQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQ 157
Cdd:COG5019   107 DYIDDQFDQYLDEEQKIKRnPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKRVNLIPVIAKADTLTDDELAEFKER 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543 158 IMKEIQEHKIKIYE--FPETDDEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNM 235
Cdd:COG5019   187 IREDLEQYNIPVFDpyDPEDDEDESLEENQDLRSLIPFAIIGSNTEIENGGEQVRGRKYPWGVVEIDDEEHSDFKKLRNL 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543 236 LIRTHMQDLKDVTNNVHYENYRSRKLAAvtyngvDNNKNKGQLTKSPLAQMEEERREhvakmkkmemeMEQVFEMKVKEK 315
Cdd:COG5019   267 LIRTHLQELKETTENLLYENYRTEKLSG------LKNSGEPSLKEIHEARLNEEERE-----------LKKKFTEKIREK 329
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1768365543 316 VQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEDEKAN 357
Cdd:COG5019   330 EKRLEELEQNLIEERKELNSKLEEIQKKLEDLEKRLEKLKSN 371
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
2-187 2.33e-09

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 55.93  E-value: 2.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543   2 VVGESGLGKSTLINSLFLTdlyspEYPGPSHRIKKTVQVEQSKVLIKEGGVQllLTIVDTPGFGDAvdnsncwqpvidyi 81
Cdd:cd00882     2 VVGRGGVGKSSLLNALLGG-----EVGEVSDVPGTTRDPDVYVKELDKGKVK--LVLVDTPGLDEF-------------- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543  82 dskfedylNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKP--LDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQIM 159
Cdd:cd00882    61 --------GGLGREELARLLLRGADLILLVVDSTDRESEEdaKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEE 132
                         170       180
                  ....*....|....*....|....*...
gi 1768365543 160 KEiQEHKIKIYEFPETDDEEENKLVKKI 187
Cdd:cd00882   133 LA-KILGVPVFEVSAKTGEGVDELFEKL 159
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
3-174 3.22e-06

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: 46.73  E-value: 3.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543   3 VGESGLGKSTLINSLFltdlyspeypgpshRIKKTVQVeqSKvliKEGGVQLL--------LTIVDTPGFG-----DAVD 69
Cdd:cd01876     5 AGRSNVGKSSLINALT--------------NRKKLART--SK---TPGRTQLInffnvgdkFRLVDLPGYGyakvsKEVR 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543  70 NSncWQPVIdyidskfEDYLNaesrvNRRQMpdnrvqCCLYFIAPSGHGLKPLDIEFMKRL-HEKVNIIPLIAKADTLTP 148
Cdd:cd01876    66 EK--WGKLI-------EEYLE-----NRENL------KGVVLLIDARHGPTPIDLEMLEFLeELGIPFLIVLTKADKLKK 125
                         170       180
                  ....*....|....*....|....*.
gi 1768365543 149 EEcqqfKKQIMKEIQEHKIKIYEFPE 174
Cdd:cd01876   126 SE----LAKVLKKIKEELNLFNILPP 147
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
2-191 5.39e-06

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 46.51  E-value: 5.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543   2 VVGESGLGKSTLINSlFLTDLYSPEYPGPSHRikktVQVEQSKVLIKEGGVQLLltIVDTPGfgdavdnsncwQPVIDYI 81
Cdd:COG1100     8 VVGTGGVGKTSLVNR-LVGDIFSLEKYLSTNG----VTIDKKELKLDGLDVDLV--IWDTPG-----------QDEFRET 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543  82 DSKFEDYLNAESRV-----NRRqmPDNRVQccLYFIapsghglkpldIEFMKRLHEKVNIIPLIAKADtLTPEECQQFKK 156
Cdd:COG1100    70 RQFYARQLTGASLYlfvvdGTR--EETLQS--LYEL-----------LESLRRLGKKSPIILVLNKID-LYDEEEIEDEE 133
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1768365543 157 QIMKEIQEHKIK-IYEFPETDDEEENKLVKKIKDRL 191
Cdd:COG1100   134 RLKEALSEDNIVeVVATSAKTGEGVEELFAALAEIL 169
YeeP COG3596
Predicted GTPase [General function prediction only];
1-150 6.28e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 44.37  E-value: 6.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543   1 MVVGESGLGKSTLINSLF-----LTDLYSPEypgpshrikkTVQVEQskVLIKEGGVQlLLTIVDTPGFGDAVDNsncwq 75
Cdd:COG3596    43 ALVGKTGAGKSSLINALFgaevaEVGVGRPC----------TREIQR--YRLESDGLP-GLVLLDTPGLGEVNER----- 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543  76 pviDYIDSKFEDYLNaESR----VNRRQMPDNRVqcclyfiapsghglkplDIEFMKRLHEKVNIIPLIA---KADTLTP 148
Cdd:COG3596   105 ---DREYRELRELLP-EADlilwVVKADDRALAT-----------------DEEFLQALRAQYPDPPVLVvltQVDRLEP 163

                  ..
gi 1768365543 149 EE 150
Cdd:COG3596   164 ER 165
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
1-69 1.01e-04

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: 43.46  E-value: 1.01e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1768365543   1 MVVGESGLGKSTLINSLF-----LTDLYSPEYPGPsHRIKKTVQveqskvlikegGVQllLTIVDTPGFGDAVD 69
Cdd:cd01853    35 LVLGKTGVGKSSTINSIFgerkvSVSAFQSETLRP-REVSRTVD-----------GFK--LNIIDTPGLLESQD 94
PRK12704 PRK12704
phosphodiesterase; Provisional
284-380 4.61e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543 284 AQMEEERREHVAKMKKMEMEMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEaqhkELEEKRRQFEDEKANWEAQQR 363
Cdd:PRK12704   49 KEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE----LLEKREEELEKKEKELEQKQQ 124
                          90
                  ....*....|....*..
gi 1768365543 364 ILEQQNSsrTLEKNKKK 380
Cdd:PRK12704  125 ELEKKEE--ELEELIEE 139
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
311-383 6.63e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 6.63e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1768365543 311 KVKEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEDEKANWEAQQRILEQQNSSRTLEKNKKKGKI 383
Cdd:COG3883   140 ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
1-64 9.52e-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: 38.37  E-value: 9.52e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1768365543   1 MVVGESGLGKSTLINSLFLTDLYSPEYPGpshrikKTVQVEQSKVLIKEGGVQLlltiVDTPGF 64
Cdd:pfam01926   3 ALVGRPNVGKSTLINALTGAKAIVSDYPG------TTRDPNEGRLELKGKQIIL----VDTPGL 56
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
2-63 1.54e-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: 38.89  E-value: 1.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1768365543   2 VVGESGLGKSTLINSLFLTDLYSPEYpgpshriKKTVQVEQSKVLIKEGGVQLLLTIVDTPG 63
Cdd:TIGR00231   6 IVGHPNVGKSTLLNSLLGNKGSITEY-------YPGTTRNYVTTVIEEDGKTYKFNLLDTAG 60
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
2-64 1.82e-03

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


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 39.30  E-value: 1.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1768365543   2 VVGESGLGKSTLINSLFltdlyspeyPGP-------SHRIKK----TVQVEqskvLIK--EGGVqllltIVDTPGF 64
Cdd:cd01854    90 LVGQSGVGKSTLLNALL---------PELvlatgeiSEKLGRgrhtTTHRE----LFPlpGGGL-----IIDTPGF 147
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
275-380 1.98e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.32  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543 275 KGQLTKSPLAQMEEERREHVAKMKKMEMEMEQ--VFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQ----HKEL---- 344
Cdd:pfam15709 393 KQRLEEERQRQEEEERKQRLQLQAAQERARQQqeEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQlaeeQKRLmema 472
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1768365543 345 EEKR------RQFEDEKANWEAQQRILEQQNSSRTLEKNKKK 380
Cdd:pfam15709 473 EEERleyqrqKQEAEEKARLEAEERRQKEEEAARLALEEAMK 514
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
2-69 4.43e-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: 37.61  E-value: 4.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1768365543   2 VVGESGLGKSTLINSL-----FLTDlyspEYPGpshrikkTVQVEQSKVLIKEGGVQllLTIVDTPGFGDAVD 69
Cdd:cd00880     2 IFGRPNVGKSSLLNALlgqnvGIVS----PIPG-------TTRDPVRKEWELLPLGP--VVLIDTPGLDEEGG 61
PTZ00121 PTZ00121
MAEBL; Provisional
269-380 6.09e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 6.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1768365543  269 VDNNKNKGQLTKSPLAQMEEERREHVAKMKKMEMEMEQVFEMKVKE-----KVQKLKDSEAELQRRHEQMKKNLEAQHKE 343
Cdd:PTZ00121  1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEaeeakKAEELKKKEAEEKKKAEELKKAEEENKIK 1731
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1768365543  344 LEEKRRQFEDEKANWEAQQRILEQQNSSRTLEKNKKK 380
Cdd:PTZ00121  1732 AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
316-368 6.54e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.27  E-value: 6.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1768365543 316 VQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEDEKANWEAQQRILEQQ 368
Cdd:COG3883   124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
313-382 9.92e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.11  E-value: 9.92e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1768365543  313 KEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQF-EDEKANWEAQQRILEQQNSSRTLEKNKKKGK 382
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVsELEEEIEELQKELYALANEISRLEQQKQILR 308
 
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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