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Conserved domains on  [gi|971380264|ref|XP_015137034|]
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septin-7 isoform X5 [Gallus gallus]

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 ...
27-297 2.26e-168

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: 472.80  E-value: 2.26e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264  27 RGFEFTLMVVGESGLGKSTLINSLFLTELYSPEYPG-PSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSN 105
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPaPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264 106 CWQPVIDYIDSKFEDYLNAESRVNR-RQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEEC 184
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264 185 QQFKKQIMKEIQEHKIKIYEFPETD-DEEENKIVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFT 263
Cdd:cd01850  161 TEFKKRIMEDIEENNIKIYKFPEDEeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 971380264 264 ILRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAV 297
Cdd:cd01850  241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKLEAL 274
PRK12704 super family cl36166
phosphodiesterase; Provisional
324-420 5.65e-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: 5.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264 324 AQMEEERREHVAKMKKMEMEMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEaqhkELEEKRRQFEDEKASWEAQQR 403
Cdd:PRK12704  49 KEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE----LLEKREEELEKKEKELEQKQQ 124
                         90
                 ....*....|....*..
gi 971380264 404 ILEQQNSsrTLEKNKKK 420
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 ...
27-297 2.26e-168

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: 472.80  E-value: 2.26e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264  27 RGFEFTLMVVGESGLGKSTLINSLFLTELYSPEYPG-PSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSN 105
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPaPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264 106 CWQPVIDYIDSKFEDYLNAESRVNR-RQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEEC 184
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264 185 QQFKKQIMKEIQEHKIKIYEFPETD-DEEENKIVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFT 263
Cdd:cd01850  161 TEFKKRIMEDIEENNIKIYKFPEDEeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 971380264 264 ILRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAV 297
Cdd:cd01850  241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKLEAL 274
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
28-296 4.79e-161

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: 454.06  E-value: 4.79e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264   28 GFEFTLMVVGESGLGKSTLINSLFLTELYSPE-YPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNC 106
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARgIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264  107 WQPVIDYIDSKFEDYLNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQ 186
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264  187 FKKQIMKEIQEHKIKIYEFP--ETDDEEENKIVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTI 264
Cdd:pfam00735 161 FKKRIREEIERQNIPIYHFPdeESDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFLK 240
                         250       260       270
                  ....*....|....*....|....*....|..
gi 971380264  265 LRNMLIRTHMQDLKDVTNNVHYENYRSRKLAA 296
Cdd:pfam00735 241 LRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
9-397 7.69e-141

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 406.71  E-value: 7.69e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264   9 GYVGFANLPNQVYRKSVKRGFEFTLMVVGESGLGKSTLINSLFLTELYS--PEYPGPSHRIKKTVQVEQSKVLIKEGGVQ 86
Cdd:COG5019    2 GYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDetEIDDIRAEGTSPTLEIKITKAELEEDGFH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264  87 LLLTIVDTPGFGDAVDNSNCWQPVIDYIDSKFEDYLNAESRVNR-RQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHE 165
Cdd:COG5019   82 LNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRnPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264 166 KVNIIPLIAKADTLTPEECQQFKKQIMKEIQEHKIKIYE--FPETDDEEENKIVKKIKDRLPLAVVGSNTIIEVNGKRVR 243
Cdd:COG5019  162 RVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDpyDPEDDEDESLEENQDLRSLIPFAIIGSNTEIENGGEQVR 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264 244 GRQYPWGVAEVENGEHCDFTILRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAvtyngvDNNKNKGQLTKFDTvegmspl 323
Cdd:COG5019  242 GRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSG------LKNSGEPSLKEIHE------- 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971380264 324 AQMEEERREhvakmkkmemeMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEDEKAS 397
Cdd:COG5019  309 ARLNEEERE-----------LKKKFTEKIREKEKRLEELEQNLIEERKELNSKLEEIQKKLEDLEKRLEKLKSN 371
PRK12704 PRK12704
phosphodiesterase; Provisional
324-420 5.65e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 5.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264 324 AQMEEERREHVAKMKKMEMEMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEaqhkELEEKRRQFEDEKASWEAQQR 403
Cdd:PRK12704  49 KEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE----LLEKREEELEKKEKELEQKQQ 124
                         90
                 ....*....|....*..
gi 971380264 404 ILEQQNSsrTLEKNKKK 420
Cdd:PRK12704 125 ELEKKEE--ELEELIEE 139
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
351-423 6.14e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 6.14e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971380264 351 KVKEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEDEKASWEAQQRILEQQNSSRTLEKNKKKGKI 423
Cdd:COG3883  140 ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
30-96 7.55e-04

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 40.05  E-value: 7.55e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 971380264   30 EFTLMVVGESGLGKSTLINSLFLTELYSPEYpgpshriKKTVQVEQSKVLIKEGGVQLLLTIVDTPG 96
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEY-------YPGTTRNYVTTVIEEDGKTYKFNLLDTAG 60
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
353-422 4.01e-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: 39.65  E-value: 4.01e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 971380264   353 KEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQF-EDEKASWEAQQRILEQQNSSRTLEKNKKKGK 422
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVsELEEEIEELQKELYALANEISRLEQQKQILR 308
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
325-420 5.27e-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: 39.16  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264  325 QMEEERREHVAKMKKMEMEMEQ--VFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQ----HKEL----EEKR------ 388
Cdd:pfam15709 403 QEEEERKQRLQLQAAQERARQQqeEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQlaeeQKRLmemaEEERleyqrq 482
                          90       100       110
                  ....*....|....*....|....*....|..
gi 971380264  389 RQFEDEKASWEAQQRILEQQNSSRTLEKNKKK 420
Cdd:pfam15709 483 KQEAEEKARLEAEERRQKEEEAARLALEEAMK 514
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
27-297 2.26e-168

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: 472.80  E-value: 2.26e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264  27 RGFEFTLMVVGESGLGKSTLINSLFLTELYSPEYPG-PSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSN 105
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPaPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264 106 CWQPVIDYIDSKFEDYLNAESRVNR-RQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEEC 184
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264 185 QQFKKQIMKEIQEHKIKIYEFPETD-DEEENKIVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFT 263
Cdd:cd01850  161 TEFKKRIMEDIEENNIKIYKFPEDEeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 971380264 264 ILRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAV 297
Cdd:cd01850  241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKLEAL 274
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
28-296 4.79e-161

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: 454.06  E-value: 4.79e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264   28 GFEFTLMVVGESGLGKSTLINSLFLTELYSPE-YPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNC 106
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARgIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264  107 WQPVIDYIDSKFEDYLNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQ 186
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264  187 FKKQIMKEIQEHKIKIYEFP--ETDDEEENKIVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTI 264
Cdd:pfam00735 161 FKKRIREEIERQNIPIYHFPdeESDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFLK 240
                         250       260       270
                  ....*....|....*....|....*....|..
gi 971380264  265 LRNMLIRTHMQDLKDVTNNVHYENYRSRKLAA 296
Cdd:pfam00735 241 LRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
9-397 7.69e-141

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 406.71  E-value: 7.69e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264   9 GYVGFANLPNQVYRKSVKRGFEFTLMVVGESGLGKSTLINSLFLTELYS--PEYPGPSHRIKKTVQVEQSKVLIKEGGVQ 86
Cdd:COG5019    2 GYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDetEIDDIRAEGTSPTLEIKITKAELEEDGFH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264  87 LLLTIVDTPGFGDAVDNSNCWQPVIDYIDSKFEDYLNAESRVNR-RQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHE 165
Cdd:COG5019   82 LNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRnPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264 166 KVNIIPLIAKADTLTPEECQQFKKQIMKEIQEHKIKIYE--FPETDDEEENKIVKKIKDRLPLAVVGSNTIIEVNGKRVR 243
Cdd:COG5019  162 RVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDpyDPEDDEDESLEENQDLRSLIPFAIIGSNTEIENGGEQVR 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264 244 GRQYPWGVAEVENGEHCDFTILRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAvtyngvDNNKNKGQLTKFDTvegmspl 323
Cdd:COG5019  242 GRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSG------LKNSGEPSLKEIHE------- 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971380264 324 AQMEEERREhvakmkkmemeMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEDEKAS 397
Cdd:COG5019  309 ARLNEEERE-----------LKKKFTEKIREKEKRLEELEQNLIEERKELNSKLEEIQKKLEDLEKRLEKLKSN 371
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
35-220 4.06e-09

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


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 55.16  E-value: 4.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264  35 VVGESGLGKSTLINSLFLTelyspEYPGPSHRIKKTVQVEQSKVLIKEGGVQllLTIVDTPGFGDAvdnsncwqpvidyi 114
Cdd:cd00882    2 VVGRGGVGKSSLLNALLGG-----EVGEVSDVPGTTRDPDVYVKELDKGKVK--LVLVDTPGLDEF-------------- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264 115 dskfedylNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKP--LDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQIM 192
Cdd:cd00882   61 --------GGLGREELARLLLRGADLILLVVDSTDRESEEdaKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEE 132
                        170       180
                 ....*....|....*....|....*...
gi 971380264 193 KEiQEHKIKIYEFPETDDEEENKIVKKI 220
Cdd:cd00882  133 LA-KILGVPVFEVSAKTGEGVDELFEKL 159
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
36-198 2.39e-07

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 439988 [Multi-domain]  Cd Length: 194  Bit Score: 50.84  E-value: 2.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264  36 VGESGLGKSTLINSLFltelyspeypgpshRIKKTVQVeqSKvliKEGGVQLL--------LTIVDTPGFG------DAV 101
Cdd:COG0218   29 AGRSNVGKSSLINALT--------------NRKKLART--SK---TPGKTQLInfflindkFYLVDLPGYGyakvskAEK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264 102 DNsncWQPVIdyidskfEDYLNaesrvNRRQMpdnrvqCCLYFIAPSGHGLKPLDIEFMKRLHE-KVNIIPLIAKADTLT 180
Cdd:COG0218   90 EK---WQKLI-------EDYLE-----GRENL------KGVVLLIDIRHPPKELDLEMLEWLDEaGIPFLIVLTKADKLK 148
                        170
                 ....*....|....*...
gi 971380264 181 PEECQQFKKQIMKEIQEH 198
Cdd:COG0218  149 KSELAKQLKAIKKALGKD 166
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
36-207 3.09e-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: 47.12  E-value: 3.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264  36 VGESGLGKSTLINSLFltelyspeypgpshRIKKTVQVeqSKvliKEGGVQLL--------LTIVDTPGFG-----DAVD 102
Cdd:cd01876    5 AGRSNVGKSSLINALT--------------NRKKLART--SK---TPGRTQLInffnvgdkFRLVDLPGYGyakvsKEVR 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264 103 NSncWQPVIdyidskfEDYLNaesrvNRRQMpdnrvqCCLYFIAPSGHGLKPLDIEFMKRL-HEKVNIIPLIAKADTLTP 181
Cdd:cd01876   66 EK--WGKLI-------EEYLE-----NRENL------KGVVLLIDARHGPTPIDLEMLEFLeELGIPFLIVLTKADKLKK 125
                        170       180
                 ....*....|....*....|....*.
gi 971380264 182 EEcqqfKKQIMKEIQEHKIKIYEFPE 207
Cdd:cd01876  126 SE----LAKVLKKIKEELNLFNILPP 147
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
29-96 4.68e-06

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 46.90  E-value: 4.68e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 971380264  29 FEFTLMVVGESGLGKSTLINSlFLTELYSPEYPGPSHRikktVQVEQSKVLIKEGGVQLLltIVDTPG 96
Cdd:COG1100    2 GEKKIVVVGTGGVGKTSLVNR-LVGDIFSLEKYLSTNG----VTIDKKELKLDGLDVDLV--IWDTPG 62
YeeP COG3596
Predicted GTPase [General function prediction only];
30-183 1.50e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 46.68  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264  30 EFTLMVVGESGLGKSTLINSLFLTELYSpeypgPSHRIKKTVQVEQskVLIKEGGVQlLLTIVDTPGFGDAVDNsncwqp 109
Cdd:COG3596   39 PPVIALVGKTGAGKSSLINALFGAEVAE-----VGVGRPCTREIQR--YRLESDGLP-GLVLLDTPGLGEVNER------ 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264 110 viDYIDSKFEDYLNaESR----VNRRQMPDNRVqcclyfiapsghglkplDIEFMKRLHEKVNIIPLIA---KADTLTPE 182
Cdd:COG3596  105 --DREYRELRELLP-EADlilwVVKADDRALAT-----------------DEEFLQALRAQYPDPPVLVvltQVDRLEPE 164

                 .
gi 971380264 183 E 183
Cdd:COG3596  165 R 165
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
29-102 1.97e-05

Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like (Translocon at the Outer-envelope membrane of Chloroplasts) family contains several Toc proteins, including Toc34, Toc33, Toc120, Toc159, Toc86, Toc125, and Toc90. The Toc complex at the outer envelope membrane of chloroplasts is a molecular machine of ~500 kDa that contains a single Toc159 protein, four Toc75 molecules, and four or five copies of Toc34. Toc64 and Toc12 are associated with the translocon, but do not appear to be part of the core complex. The Toc translocon initiates the import of nuclear-encoded preproteins from the cytosol into the organelle. Toc34 and Toc159 are both GTPases, while Toc75 is a beta-barrel integral membrane protein. Toc159 is equally distributed between a soluble cytoplasmic form and a membrane-inserted form, suggesting that assembly of the Toc complex is dynamic. Toc34 and Toc75 act sequentially to mediate docking and insertion of Toc159 resulting in assembly of the functional translocon.


Pssm-ID: 206652  Cd Length: 248  Bit Score: 45.77  E-value: 1.97e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 971380264  29 FEFTLMVVGESGLGKSTLINSLF-----LTELYSPEYPGPsHRIKKTVQveqskvlikegGVQllLTIVDTPGFGDAVD 102
Cdd:cd01853   30 FSLTILVLGKTGVGKSSTINSIFgerkvSVSAFQSETLRP-REVSRTVD-----------GFK--LNIIDTPGLLESQD 94
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
31-203 2.10e-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: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264  31 FTLMVVGESGLGKSTLINSLfLTELYSPEYPGP--------SHRIKKTVqveqskvlikeggvqlllTIVDTPGFGDAVD 102
Cdd:cd09912    1 FLLAVVGEFSAGKSTLLNAL-LGEEVLPTGVTPttavitvlRYGLLKGV------------------VLVDTPGLNSTIE 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264 103 nsncwqpvidyidskfedylnAESRVNRRQMPDnrvqCCL-YFIAPSGHGLKPLDIEFMK--RLHEKVNIIPLIAKADTL 179
Cdd:cd09912   62 ---------------------HHTEITESFLPR----ADAvIFVLSADQPLTESEREFLKeiLKWSGKKIFFVLNKIDLL 116
                        170       180
                 ....*....|....*....|....*....
gi 971380264 180 TPEECQQ-----FKKQIMKEIQEHKIKIY 203
Cdd:cd09912  117 SEEELEEvleysREELGVLELGGGEPRIF 145
PRK12704 PRK12704
phosphodiesterase; Provisional
324-420 5.65e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 5.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264 324 AQMEEERREHVAKMKKMEMEMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEaqhkELEEKRRQFEDEKASWEAQQR 403
Cdd:PRK12704  49 KEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE----LLEKREEELEKKEKELEQKQQ 124
                         90
                 ....*....|....*..
gi 971380264 404 ILEQQNSsrTLEKNKKK 420
Cdd:PRK12704 125 ELEKKEE--ELEELIEE 139
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
351-423 6.14e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 6.14e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971380264 351 KVKEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEDEKASWEAQQRILEQQNSSRTLEKNKKKGKI 423
Cdd:COG3883  140 ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
32-97 6.32e-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: 40.84  E-value: 6.32e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 971380264  32 TLMVVGESGLGKSTLINSLFltelyspeyPGP-------SHRIKK----TVQVEqskvLIK--EGGVqllltIVDTPGF 97
Cdd:cd01854   87 TSVLVGQSGVGKSTLLNALL---------PELvlatgeiSEKLGRgrhtTTHRE----LFPlpGGGL-----IIDTPGF 147
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
30-96 7.55e-04

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 40.05  E-value: 7.55e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 971380264   30 EFTLMVVGESGLGKSTLINSLFLTELYSPEYpgpshriKKTVQVEQSKVLIKEGGVQLLLTIVDTPG 96
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEY-------YPGTTRNYVTTVIEEDGKTYKFNLLDTAG 60
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
32-173 1.18e-03

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: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264   32 TLMVVGESGLGKSTLINSLFLTELYSPEYPGpshrikKTVQVEQSKVLIKEGGVQLlltiVDTPGFgdavdnsncwqpvi 111
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPG------TTRDPNEGRLELKGKQIIL----VDTPGL-------------- 56
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 971380264  112 dyIDSKFEDYLNAESRVNRRqmpdnRVQCCLYFIaPSGHGLKPLDIEFMKRLHEkvNIIPLI 173
Cdd:pfam01926  57 --IEGASEGEGLGRAFLAII-----EADLILFVV-DSEEGITPLDEELLELLRE--NKKPII 108
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
29-97 1.18e-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: 41.09  E-value: 1.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 971380264   29 FEFTLMVVGESGLGKSTLINSLFLTELYSPEYPGPShrikkTVQVEQSKVLIKegGVQllLTIVDTPGF 97
Cdd:TIGR00993 117 FSLNILVLGKSGVGKSATINSIFGEVKFSTDAFGMG-----TTSVQEIEGLVQ--GVK--IRVIDTPGL 176
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
353-422 4.01e-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: 39.65  E-value: 4.01e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 971380264   353 KEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQF-EDEKASWEAQQRILEQQNSSRTLEKNKKKGK 422
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVsELEEEIEELQKELYALANEISRLEQQKQILR 308
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
356-408 4.92e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 4.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 971380264 356 VQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEDEKASWEAQQRILEQQ 408
Cdd:COG3883  124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
325-420 5.27e-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: 39.16  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264  325 QMEEERREHVAKMKKMEMEMEQ--VFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQ----HKEL----EEKR------ 388
Cdd:pfam15709 403 QEEEERKQRLQLQAAQERARQQqeEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQlaeeQKRLmemaEEERleyqrq 482
                          90       100       110
                  ....*....|....*....|....*....|..
gi 971380264  389 RQFEDEKASWEAQQRILEQQNSSRTLEKNKKK 420
Cdd:pfam15709 483 KQEAEEKARLEAEERRQKEEEAARLALEEAMK 514
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
35-102 6.05e-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: 37.23  E-value: 6.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971380264  35 VVGESGLGKSTLINSL-----FLTElyspEYPGpshrikkTVQVEQSKVLIKEGGVQllLTIVDTPGFGDAVD 102
Cdd:cd00880    2 IFGRPNVGKSSLLNALlgqnvGIVS----PIPG-------TTRDPVRKEWELLPLGP--VVLIDTPGLDEEGG 61
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
324-416 7.50e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 38.57  E-value: 7.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971380264  324 AQMEEERREHVAKMKKMEMEMEQVF---EMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQhKELEEKRRQFEdEKASWEA 400
Cdd:pfam17380 427 AEQEEARQREVRRLEEERAREMERVrleEQERQQQVERLRQQEEERKRKKLELEKEKRDR-KRAEEQRRKIL-EKELEER 504
                          90
                  ....*....|....*.
gi 971380264  401 QQRILEQQNSSRTLEK 416
Cdd:pfam17380 505 KQAMIEEERKRKLLEK 520
PTZ00121 PTZ00121
MAEBL; Provisional
353-420 8.57e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 8.57e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 971380264  353 KEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEDEKASWEAQQRILEQQNSSRTLEKNKKK 420
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
PTZ00121 PTZ00121
MAEBL; Provisional
349-422 9.10e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 9.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 971380264  349 EMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQH-KELEEKRRQFEDEKASWEAQQRILEQQNSSRTLEKNKKKGK 422
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
 
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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