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Conserved domains on  [gi|1578829357|ref|WP_130208513|]
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MULTISPECIES: protein phosphatase CheZ [unclassified Escherichia]

Protein Classification

protein phosphatase CheZ( domain architecture ID 10013749)

protein phosphatase CheZ functions in the chemotaxis signal transduction complex by controlling the level of phosphorylated CheY through dephosphorylation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11166 PRK11166
chemotaxis regulator CheZ; Provisional
1-214 6.26e-133

chemotaxis regulator CheZ; Provisional


:

Pssm-ID: 236868  Cd Length: 214  Bit Score: 371.95  E-value: 6.26e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578829357   1 MMQPSIKPADENSAGDIIARIGSLTRMLRDSLRELGLDQAIAEAAEAIPDARDRLYYVVQMTAQAAERALNSVEASQPHQ 80
Cdd:PRK11166    1 MMQPSIPAADEASAGDIIARIGQLTRMLRDSLRELGLDQAIEEAAEAIPDARDRLDYVAQMTEQAAERVLNAVEAAQPHQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578829357  81 DHMEKSAKALTQRWDGWFADPIDLADARELVTDTRQFLADVPTHTSFTNAQLLEIMMAQDFQDLTGQVIKRMMDVIQEIE 160
Cdd:PRK11166   81 DQLEKEAKALDARWDEWFANPIELADARELVTDTRAFLADVPEHTSFTNAQLLEIMMAQDFQDLTGQVIKRMMDVIQEIE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1578829357 161 RQLLMVLLENIPEQDARPKRESQSLLNGPQVDTSKAGVVASQDQVDDLLDSLGF 214
Cdd:PRK11166  161 RQLLMVLLENIPEQESRPKRENESLLNGPQINPEKADVVASQDQVDDLLDSLGF 214
 
Name Accession Description Interval E-value
PRK11166 PRK11166
chemotaxis regulator CheZ; Provisional
1-214 6.26e-133

chemotaxis regulator CheZ; Provisional


Pssm-ID: 236868  Cd Length: 214  Bit Score: 371.95  E-value: 6.26e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578829357   1 MMQPSIKPADENSAGDIIARIGSLTRMLRDSLRELGLDQAIAEAAEAIPDARDRLYYVVQMTAQAAERALNSVEASQPHQ 80
Cdd:PRK11166    1 MMQPSIPAADEASAGDIIARIGQLTRMLRDSLRELGLDQAIEEAAEAIPDARDRLDYVAQMTEQAAERVLNAVEAAQPHQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578829357  81 DHMEKSAKALTQRWDGWFADPIDLADARELVTDTRQFLADVPTHTSFTNAQLLEIMMAQDFQDLTGQVIKRMMDVIQEIE 160
Cdd:PRK11166   81 DQLEKEAKALDARWDEWFANPIELADARELVTDTRAFLADVPEHTSFTNAQLLEIMMAQDFQDLTGQVIKRMMDVIQEIE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1578829357 161 RQLLMVLLENIPEQDARPKRESQSLLNGPQVDTSKAGVVASQDQVDDLLDSLGF 214
Cdd:PRK11166  161 RQLLMVLLENIPEQESRPKRENESLLNGPQINPEKADVVASQDQVDDLLDSLGF 214
CheZ pfam04344
Chemotaxis phosphatase, CheZ; This family represents the bacterial chemotaxis phosphatase, ...
16-214 4.97e-102

Chemotaxis phosphatase, CheZ; This family represents the bacterial chemotaxis phosphatase, CheZ. This protein forms a dimer characterized by a long four-helix bundle, composed of two helices from each monomer. CheZ dephosphorylates CheY in a reaction that is essential to maintain a continuous chemotactic response to environmental changes. It is thought that CheZ's conserved residue Gln 147 orientates a water molecule for nucleophilic attack at the CheY active site.


Pssm-ID: 427881  Cd Length: 203  Bit Score: 293.28  E-value: 4.97e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578829357  16 DIIARIGSLTRMLRDSLRELGLDQAIAEAAEAIPDARDRLYYVVQMTAQAAERALNSVEASQPHQDHMEKSAKALTQRWD 95
Cdd:pfam04344   1 ELFQRVGQLTRQLHDALRELGLDRLLELAASEIPDARDRLNYVATMTEQAANRTLNAVEAAQPLQDRLAEEARALSARWQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578829357  96 GWFADPIDLADARELVTDTRQFLADVPTHTSFTNAQLLEIMMAQDFQDLTGQVIKRMMDVIQEIERQLLMVLLENIPEQD 175
Cdd:pfam04344  81 RLMRRELSLDEFRELAHETRAFLDDVPEDTAATNAQLTEIMMAQDFQDLTGQVIKKVIDLVQEVESQLVQLLLDFGPKEE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1578829357 176 ARPKR---ESQSLLNGPQVD-TSKAGVVASQDQVDDLLDSLGF 214
Cdd:pfam04344 161 IIEHEkteEDDSLLNGPQINpEGRDDVVSSQDQVDDLLSSLGF 203
CheZ COG3143
Phosphoaspartate phosphatase CheZ, dephosphorylates CheY~P [Cell motility, Signal transduction ...
6-214 3.01e-87

Phosphoaspartate phosphatase CheZ, dephosphorylates CheY~P [Cell motility, Signal transduction mechanisms];


Pssm-ID: 442377  Cd Length: 235  Bit Score: 257.23  E-value: 3.01e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578829357   6 IKPADENSAGDIIARIGSLTRMLRDSLRELGLDQAIAEAAEAI-PDARDRLYYVVQMTAQAAERALNSVEASQPHQDHME 84
Cdd:COG3143    24 VDELAAAREDELFQEIGQLTRELHDALRELGLDPRLEEAASSEiPDARDRLDYVVEMTEQAANRTLNAVEAAQPLQDRLR 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578829357  85 KSAKALTQRWDGWFADPIDLADARELVTDTRQFLADVPTHTSFTNAQLLEIMMAQDFQDLTGQVIKRMMDVIQEIERQLL 164
Cdd:COG3143   104 EEAAALLARWQRLFARELSLDEFRELVKDTRAFLGEVPELTDALRAQLTEIMMAQDFQDLTGQVIKKVVNLLQEVESRLV 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1578829357 165 MVLLENIPEQDARP--KRESQSLLNGPQVDTSKAGVVASQDQVDDLLDSLGF 214
Cdd:COG3143   184 QLLLEFGPEEEAAPadAREDASLLNGPQINGEGTDVVSSQDDVDDLLSSLGF 235
 
Name Accession Description Interval E-value
PRK11166 PRK11166
chemotaxis regulator CheZ; Provisional
1-214 6.26e-133

chemotaxis regulator CheZ; Provisional


Pssm-ID: 236868  Cd Length: 214  Bit Score: 371.95  E-value: 6.26e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578829357   1 MMQPSIKPADENSAGDIIARIGSLTRMLRDSLRELGLDQAIAEAAEAIPDARDRLYYVVQMTAQAAERALNSVEASQPHQ 80
Cdd:PRK11166    1 MMQPSIPAADEASAGDIIARIGQLTRMLRDSLRELGLDQAIEEAAEAIPDARDRLDYVAQMTEQAAERVLNAVEAAQPHQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578829357  81 DHMEKSAKALTQRWDGWFADPIDLADARELVTDTRQFLADVPTHTSFTNAQLLEIMMAQDFQDLTGQVIKRMMDVIQEIE 160
Cdd:PRK11166   81 DQLEKEAKALDARWDEWFANPIELADARELVTDTRAFLADVPEHTSFTNAQLLEIMMAQDFQDLTGQVIKRMMDVIQEIE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1578829357 161 RQLLMVLLENIPEQDARPKRESQSLLNGPQVDTSKAGVVASQDQVDDLLDSLGF 214
Cdd:PRK11166  161 RQLLMVLLENIPEQESRPKRENESLLNGPQINPEKADVVASQDQVDDLLDSLGF 214
CheZ pfam04344
Chemotaxis phosphatase, CheZ; This family represents the bacterial chemotaxis phosphatase, ...
16-214 4.97e-102

Chemotaxis phosphatase, CheZ; This family represents the bacterial chemotaxis phosphatase, CheZ. This protein forms a dimer characterized by a long four-helix bundle, composed of two helices from each monomer. CheZ dephosphorylates CheY in a reaction that is essential to maintain a continuous chemotactic response to environmental changes. It is thought that CheZ's conserved residue Gln 147 orientates a water molecule for nucleophilic attack at the CheY active site.


Pssm-ID: 427881  Cd Length: 203  Bit Score: 293.28  E-value: 4.97e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578829357  16 DIIARIGSLTRMLRDSLRELGLDQAIAEAAEAIPDARDRLYYVVQMTAQAAERALNSVEASQPHQDHMEKSAKALTQRWD 95
Cdd:pfam04344   1 ELFQRVGQLTRQLHDALRELGLDRLLELAASEIPDARDRLNYVATMTEQAANRTLNAVEAAQPLQDRLAEEARALSARWQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578829357  96 GWFADPIDLADARELVTDTRQFLADVPTHTSFTNAQLLEIMMAQDFQDLTGQVIKRMMDVIQEIERQLLMVLLENIPEQD 175
Cdd:pfam04344  81 RLMRRELSLDEFRELAHETRAFLDDVPEDTAATNAQLTEIMMAQDFQDLTGQVIKKVIDLVQEVESQLVQLLLDFGPKEE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1578829357 176 ARPKR---ESQSLLNGPQVD-TSKAGVVASQDQVDDLLDSLGF 214
Cdd:pfam04344 161 IIEHEkteEDDSLLNGPQINpEGRDDVVSSQDQVDDLLSSLGF 203
CheZ COG3143
Phosphoaspartate phosphatase CheZ, dephosphorylates CheY~P [Cell motility, Signal transduction ...
6-214 3.01e-87

Phosphoaspartate phosphatase CheZ, dephosphorylates CheY~P [Cell motility, Signal transduction mechanisms];


Pssm-ID: 442377  Cd Length: 235  Bit Score: 257.23  E-value: 3.01e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578829357   6 IKPADENSAGDIIARIGSLTRMLRDSLRELGLDQAIAEAAEAI-PDARDRLYYVVQMTAQAAERALNSVEASQPHQDHME 84
Cdd:COG3143    24 VDELAAAREDELFQEIGQLTRELHDALRELGLDPRLEEAASSEiPDARDRLDYVVEMTEQAANRTLNAVEAAQPLQDRLR 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578829357  85 KSAKALTQRWDGWFADPIDLADARELVTDTRQFLADVPTHTSFTNAQLLEIMMAQDFQDLTGQVIKRMMDVIQEIERQLL 164
Cdd:COG3143   104 EEAAALLARWQRLFARELSLDEFRELVKDTRAFLGEVPELTDALRAQLTEIMMAQDFQDLTGQVIKKVVNLLQEVESRLV 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1578829357 165 MVLLENIPEQDARP--KRESQSLLNGPQVDTSKAGVVASQDQVDDLLDSLGF 214
Cdd:COG3143   184 QLLLEFGPEEEAAPadAREDASLLNGPQINGEGTDVVSSQDDVDDLLSSLGF 235
 
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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