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Conserved domains on  [gi|1490893224|gb|RLE28184|]
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hypothetical protein DRJ65_00500 [Acidobacteria bacterium]

Protein Classification

CheB methylesterase domain-containing protein( domain architecture ID 11611847)

CheB methylesterase domain-containing protein lacking the receiver (REC) domain that is present in chemotaxis protein CheB, a protein-glutamate methylesterase which demethylates gamma-glutamyl methyl ester residues in chemoreceptor proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CheB_Rec cd16432
Chemotaxis response regulator protein-glutamate methylesterase, CheB, with N-terminal REC ...
 143-326 1.76e-64

Chemotaxis response regulator protein-glutamate methylesterase, CheB, with N-terminal REC domain; This family contains the methylesterase CheB (EC 3.1.1.61; also known as CheB methylesterase, chemotaxis-specific methylesterase, methyl-accepting chemotaxis protein methyl-esterase, or protein methyl-esterase) domain with a REC domain at the N-terminus. CheB is a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors. Signaling output of the chemotaxis receptors is modulated by CheB and methyltransferase CheR by controlling the level of receptor methylation. The N-terminal regulatory (REC) domain blocks the active site of the C-terminal domain until it is phosphorylated. Reversible methylation of transmembrane chemoreceptors plays an important role in ligand-dependent signaling and cellular adaptation in bacterial chemotaxis. Phosphorylated CheB catalyzes deamidation of specific glutamine residues in the cytoplasmic region of the chemoreceptors and demethylation of specific methyl glutamate residues introduced into the chemoreceptors by CheR.


:

Pssm-ID: 319751  Cd Length: 184  Bit Score: 201.82  E-value: 1.76e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 143 LIAVGCSAGGPDATGEMLKTIGTSLlKTSVVVVQHIGEDFQAEYVQWLRRVLPwVNVDVGEDGEKLLPGCVRVAGQGAHL 222
Cdd:cd16432     1 LVAIGASTGGPQALQEILSALPADF-PAPILIVQHMPPGFTKSFAERLNRLSA-LPVKEAEDGEPLEPGTVYIAPGGYHL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 223 EVTEGPA---LRLDrNAPPDHGHRPSVDRLFESVARSIPRSSVGVLLSGMGVDGVEGLLSLSRAGCLTLVQDRESSAVFG 299
Cdd:cd16432    79 VVERRGGggrIRLS-DGPPVNGHRPSVDVLFRSAAEVYGARALGVILTGMGRDGAEGLLALKEAGGYTIAQDEASSVVYG 157

                         170       180
                  ....*....|....*....|....*..
gi 1490893224 300 MPRVALERGAAAIVQPPDALGRALKDR 326
Cdd:cd16432   158 MPKAAIEAGAADEVLPLDEIAAAILRL 184
 
Name Accession Description Interval E-value
CheB_Rec cd16432
Chemotaxis response regulator protein-glutamate methylesterase, CheB, with N-terminal REC ...
 143-326 1.76e-64

Chemotaxis response regulator protein-glutamate methylesterase, CheB, with N-terminal REC domain; This family contains the methylesterase CheB (EC 3.1.1.61; also known as CheB methylesterase, chemotaxis-specific methylesterase, methyl-accepting chemotaxis protein methyl-esterase, or protein methyl-esterase) domain with a REC domain at the N-terminus. CheB is a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors. Signaling output of the chemotaxis receptors is modulated by CheB and methyltransferase CheR by controlling the level of receptor methylation. The N-terminal regulatory (REC) domain blocks the active site of the C-terminal domain until it is phosphorylated. Reversible methylation of transmembrane chemoreceptors plays an important role in ligand-dependent signaling and cellular adaptation in bacterial chemotaxis. Phosphorylated CheB catalyzes deamidation of specific glutamine residues in the cytoplasmic region of the chemoreceptors and demethylation of specific methyl glutamate residues introduced into the chemoreceptors by CheR.


Pssm-ID: 319751  Cd Length: 184  Bit Score: 201.82  E-value: 1.76e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 143 LIAVGCSAGGPDATGEMLKTIGTSLlKTSVVVVQHIGEDFQAEYVQWLRRVLPwVNVDVGEDGEKLLPGCVRVAGQGAHL 222
Cdd:cd16432     1 LVAIGASTGGPQALQEILSALPADF-PAPILIVQHMPPGFTKSFAERLNRLSA-LPVKEAEDGEPLEPGTVYIAPGGYHL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 223 EVTEGPA---LRLDrNAPPDHGHRPSVDRLFESVARSIPRSSVGVLLSGMGVDGVEGLLSLSRAGCLTLVQDRESSAVFG 299
Cdd:cd16432    79 VVERRGGggrIRLS-DGPPVNGHRPSVDVLFRSAAEVYGARALGVILTGMGRDGAEGLLALKEAGGYTIAQDEASSVVYG 157

                         170       180
                  ....*....|....*....|....*..
gi 1490893224 300 MPRVALERGAAAIVQPPDALGRALKDR 326
Cdd:cd16432   158 MPKAAIEAGAADEVLPLDEIAAAILRL 184
CheB COG2201
Chemotaxis response regulator CheB, contains REC and protein-glutamate methylesterase domains ...
 143-328 9.98e-63

Chemotaxis response regulator CheB, contains REC and protein-glutamate methylesterase domains [Signal transduction mechanisms];


Pssm-ID: 441803  Cd Length: 193  Bit Score: 197.62  E-value: 9.98e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 143 LIAVGCSAGGPDATGEMLKTIGTSLlKTSVVVVQHIGEDFQAEYVQWLRRVLPwVNVDVGEDGEKLLPGCVRVAGQGAHL 222
Cdd:COG2201     5 VVAIGASTGGPEALEEVLSALPADF-PAPIVIVQHMPPGFTSSLAERLNRLTA-LPVKEAEDGERLEPGHVYIAPGGRHL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 223 EVTEGPALRLD-RNAPPDHGHRPSVDRLFESVARSIPRSSVGVLLSGMGVDGVEGLLSLSRAGCLTLVQDRESSAVFGMP 301
Cdd:COG2201    83 EVERSGGYRLRlSDGPPVNGHRPSVDVLFRSLAEVYGERAVGVILTGMGSDGAEGLKAIKEAGGLTIAQDEESCVVYGMP 162

                         170       180
                  ....*....|....*....|....*..
gi 1490893224 302 RVALERGAAAIVQPPDALGRALKDRIE 328
Cdd:COG2201   163 RAAIEAGAVDEVLPLEEIAAALLRLLR 189
CheB_methylest pfam01339
CheB methylesterase;
144-323 6.73e-58

CheB methylesterase;


Pssm-ID: 460166  Cd Length: 178  Bit Score: 184.94  E-value: 6.73e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 144 IAVGCSAGGPDATGEMLKTIGTSLlKTSVVVVQHIGEDFQAEYVQWLRRVLPwVNVDVGEDGEKLLPGCVRVAGQGAHLE 223
Cdd:pfam01339   1 VAIGASTGGPEALEELLPALPADL-PAAIVVVQHMPPGFTSSLAERLNRLSA-LPVKEAEDGEPLEPGTVYIAPGGYHLL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 224 VTEGpALRLDRNAPPDHGHRPSVDRLFESVARSI-PRSSVGVLLSGMGVDGVEGLLSLSRAGCLTLVQDRESSAVFGMPR 302
Cdd:pfam01339  79 VEDG-RGPYRSDGPPVNGHRPSIDVLFRSLAEAYgGKRAIGVILTGMGSDGAAGLKAIKEAGGLTIAQDPATAVVYGMPR 157

                         170       180
                  ....*....|....*....|.
gi 1490893224 303 VALERGAAAIVQPPDALGRAL 323
Cdd:pfam01339 158 AAIEAGAADFVLPLEEIAAEL 178
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
143-323 7.09e-48

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 163.90  E-value: 7.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 143 LIAVGCSAGGPDATGEMLKTIGTSLlKTSVVVVQHIGEDFQAEYVQWLRRVLPwVNVDVGEDGEKLLPGCVRVAGQGAHL 222
Cdd:PRK12555  155 LVAIGASAGGPAALAVLLGGLPADF-PAAIVIVQHVDAAFAAGMAEWLDGQTA-LPVREAREGERPQPGHVLLAPTNDHL 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 223 EVTEGPALRLDRnAPPDHGHRPSVDRLFESVARSIPRSSVGVLLSGMGVDGVEGLLSLSRAGCLTLVQDRESSAVFGMPR 302
Cdd:PRK12555  233 RLTRDGALRYTR-EPPVNPYRPSVDVFFESVAQHWGGNAIGVLLTGMGRDGARGLKAMRQAGAHTIAQDEASSAVYGMPK 311

                         170       180
                  ....*....|....*....|.
gi 1490893224 303 VALERGAAAIVQPPDALGRAL 323
Cdd:PRK12555  312 AAAALGAASEVLPLERIAPRL 332
 
Name Accession Description Interval E-value
CheB_Rec cd16432
Chemotaxis response regulator protein-glutamate methylesterase, CheB, with N-terminal REC ...
 143-326 1.76e-64

Chemotaxis response regulator protein-glutamate methylesterase, CheB, with N-terminal REC domain; This family contains the methylesterase CheB (EC 3.1.1.61; also known as CheB methylesterase, chemotaxis-specific methylesterase, methyl-accepting chemotaxis protein methyl-esterase, or protein methyl-esterase) domain with a REC domain at the N-terminus. CheB is a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors. Signaling output of the chemotaxis receptors is modulated by CheB and methyltransferase CheR by controlling the level of receptor methylation. The N-terminal regulatory (REC) domain blocks the active site of the C-terminal domain until it is phosphorylated. Reversible methylation of transmembrane chemoreceptors plays an important role in ligand-dependent signaling and cellular adaptation in bacterial chemotaxis. Phosphorylated CheB catalyzes deamidation of specific glutamine residues in the cytoplasmic region of the chemoreceptors and demethylation of specific methyl glutamate residues introduced into the chemoreceptors by CheR.


Pssm-ID: 319751  Cd Length: 184  Bit Score: 201.82  E-value: 1.76e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 143 LIAVGCSAGGPDATGEMLKTIGTSLlKTSVVVVQHIGEDFQAEYVQWLRRVLPwVNVDVGEDGEKLLPGCVRVAGQGAHL 222
Cdd:cd16432     1 LVAIGASTGGPQALQEILSALPADF-PAPILIVQHMPPGFTKSFAERLNRLSA-LPVKEAEDGEPLEPGTVYIAPGGYHL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 223 EVTEGPA---LRLDrNAPPDHGHRPSVDRLFESVARSIPRSSVGVLLSGMGVDGVEGLLSLSRAGCLTLVQDRESSAVFG 299
Cdd:cd16432    79 VVERRGGggrIRLS-DGPPVNGHRPSVDVLFRSAAEVYGARALGVILTGMGRDGAEGLLALKEAGGYTIAQDEASSVVYG 157

                         170       180
                  ....*....|....*....|....*..
gi 1490893224 300 MPRVALERGAAAIVQPPDALGRALKDR 326
Cdd:cd16432   158 MPKAAIEAGAADEVLPLDEIAAAILRL 184
CheB COG2201
Chemotaxis response regulator CheB, contains REC and protein-glutamate methylesterase domains ...
 143-328 9.98e-63

Chemotaxis response regulator CheB, contains REC and protein-glutamate methylesterase domains [Signal transduction mechanisms];


Pssm-ID: 441803  Cd Length: 193  Bit Score: 197.62  E-value: 9.98e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 143 LIAVGCSAGGPDATGEMLKTIGTSLlKTSVVVVQHIGEDFQAEYVQWLRRVLPwVNVDVGEDGEKLLPGCVRVAGQGAHL 222
Cdd:COG2201     5 VVAIGASTGGPEALEEVLSALPADF-PAPIVIVQHMPPGFTSSLAERLNRLTA-LPVKEAEDGERLEPGHVYIAPGGRHL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 223 EVTEGPALRLD-RNAPPDHGHRPSVDRLFESVARSIPRSSVGVLLSGMGVDGVEGLLSLSRAGCLTLVQDRESSAVFGMP 301
Cdd:COG2201    83 EVERSGGYRLRlSDGPPVNGHRPSVDVLFRSLAEVYGERAVGVILTGMGSDGAEGLKAIKEAGGLTIAQDEESCVVYGMP 162

                         170       180
                  ....*....|....*....|....*..
gi 1490893224 302 RVALERGAAAIVQPPDALGRALKDRIE 328
Cdd:COG2201   163 RAAIEAGAVDEVLPLEEIAAALLRLLR 189
CheB_methylest pfam01339
CheB methylesterase;
144-323 6.73e-58

CheB methylesterase;


Pssm-ID: 460166  Cd Length: 178  Bit Score: 184.94  E-value: 6.73e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 144 IAVGCSAGGPDATGEMLKTIGTSLlKTSVVVVQHIGEDFQAEYVQWLRRVLPwVNVDVGEDGEKLLPGCVRVAGQGAHLE 223
Cdd:pfam01339   1 VAIGASTGGPEALEELLPALPADL-PAAIVVVQHMPPGFTSSLAERLNRLSA-LPVKEAEDGEPLEPGTVYIAPGGYHLL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 224 VTEGpALRLDRNAPPDHGHRPSVDRLFESVARSI-PRSSVGVLLSGMGVDGVEGLLSLSRAGCLTLVQDRESSAVFGMPR 302
Cdd:pfam01339  79 VEDG-RGPYRSDGPPVNGHRPSIDVLFRSLAEAYgGKRAIGVILTGMGSDGAAGLKAIKEAGGLTIAQDPATAVVYGMPR 157

                         170       180
                  ....*....|....*....|.
gi 1490893224 303 VALERGAAAIVQPPDALGRAL 323
Cdd:pfam01339 158 AAIEAGAADFVLPLEEIAAEL 178
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
143-323 7.09e-48

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 163.90  E-value: 7.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 143 LIAVGCSAGGPDATGEMLKTIGTSLlKTSVVVVQHIGEDFQAEYVQWLRRVLPwVNVDVGEDGEKLLPGCVRVAGQGAHL 222
Cdd:PRK12555  155 LVAIGASAGGPAALAVLLGGLPADF-PAAIVIVQHVDAAFAAGMAEWLDGQTA-LPVREAREGERPQPGHVLLAPTNDHL 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 223 EVTEGPALRLDRnAPPDHGHRPSVDRLFESVARSIPRSSVGVLLSGMGVDGVEGLLSLSRAGCLTLVQDRESSAVFGMPR 302
Cdd:PRK12555  233 RLTRDGALRYTR-EPPVNPYRPSVDVFFESVAQHWGGNAIGVLLTGMGRDGARGLKAMRQAGAHTIAQDEASSAVYGMPK 311

                         170       180
                  ....*....|....*....|.
gi 1490893224 303 VALERGAAAIVQPPDALGRAL 323
Cdd:PRK12555  312 AAAALGAASEVLPLERIAPRL 332
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
143-331 9.19e-43

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 151.07  E-value: 9.19e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 143 LIAVGCSAGGPDAtgemLKTIGTSLLKTS---VVVVQHIGEDFQAEYVQWLRRvLPWVNVDVGEDGEKLLPGCVRVAGQG 219
Cdd:PRK00742  166 LVAIGTSTGGPEA----LQKVLTPLPANFpapILIVQHMPAGFTKSFAERLNR-LCQIEVKEAEDGERLKPGHAYIAPGG 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 220 AHLEVTE---GPALRLDrNAPPDHGHRPSVDRLFESVARSIPRSSVGVLLSGMGVDGVEGLLSLSRAGCLTLVQDRESSA 296
Cdd:PRK00742  241 KHMMVARsgaNYRIKLD-DGPPVNRHRPSVDVLFRSAAKAAGRNALGVILTGMGRDGAAGLLEMKQAGATTIAQDEASCV 319

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1490893224 297 VFGMPRVALERGAAAIVQPPDALGRALKDRIETGS 331
Cdd:PRK00742  320 VYGMPKAAIEAGAVDEVLPLDQIAERILKEVAAGR 354
CheB cd16433
Chemotaxis response regulator protein-glutamate methylesterase, CheB; This family contains the ...
 143-325 3.58e-42

Chemotaxis response regulator protein-glutamate methylesterase, CheB; This family contains the methylesterase CheB (EC 3.1.1.61; also known as CheB methylesterase, chemotaxis-specific methylesterase, methyl-accepting chemotaxis protein methyl-esterase, or protein methyl-esterase) domain, a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors. Signaling output of the chemotaxis receptors is modulated by CheB and methyltransferase CheR by controlling the level of receptor methylation. cheR and cheB have a strong preference to occur in the same operon, and a subgroup contains multidomain proteins with CheB-CheR fusions. Reversible methylation of transmembrane chemoreceptors plays an important role in ligand-dependent signaling and cellular adaptation in bacterial chemotaxis. Phosphorylated CheB catalyzes deamidation of specific glutamine residues in the cytoplasmic region of the chemoreceptors and demethylation of specific methyl glutamate residues introduced into the chemoreceptors by CheR.


Pssm-ID: 319752  Cd Length: 181  Bit Score: 144.44  E-value: 3.58e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 143 LIAVGCSAGGPDAtgemLKTIGTSL---LKTSVVVVQHIGEDFQAEYVQWLRRVLPwVNVDVGEDGEKLLPGCVRVAGQG 219
Cdd:cd16433     1 IVVIGASAGGLEA----LLELLSALpadFPAPVLVVLHRPPDSPSVLPELLSRRTP-LPVKEAEDGEPIEPGTIYVAPPD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 220 AHLEVTEGPALRLDRnAPPDHGHRPSVDRLFESVARSIPRSSVGVLLSGMGVDGVEGLLSLSRAGCLTLVQDRESSAVFG 299
Cdd:cd16433    76 YHLLVEDDGTFSLSR-GPKVNFSRPSIDVLFRSAADAYGPRVIGVVLTGANDDGAAGLAAIKRAGGLTIVQDPATAEVPS 154

                         170       180
                  ....*....|....*....|....*.
gi 1490893224 300 MPRVALERGAAAIVQPPDALGRALKD 325
Cdd:cd16433   155 MPRAALAAVAVDHVLPLAEIAALLVR 180
CheB-CheR_fusion cd16434
Chemotaxis response regulator protein-glutamate methylesterase, CheB, fused with CheR domain; ...
 143-323 2.17e-33

Chemotaxis response regulator protein-glutamate methylesterase, CheB, fused with CheR domain; This family contains the methylesterase CheB (EC 3.1.1.61; also known as CheB methylesterase, chemotaxis-specific methylesterase, methyl-accepting chemotaxis protein methyl-esterase, or protein methyl-esterase) domain, a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors, fused with a CheR domain as well as other domains. Signaling output of the chemotaxis receptors is modulated by CheB and methyltransferase CheR by controlling the level of receptor methylation. cheB and cheR are typically found in the same operon. However, CheB and CheR are fused in multi-domain proteins in this subgroup. The CheR protein/domain includes an all-alpha N-terminal domain and an S-adenosylmethionine-dependent methyltransferase C-terminal domain. Reversible methylation of transmembrane chemoreceptors plays an important role in ligand-dependent signaling and cellular adaptation in bacterial chemotaxis. Phosphorylated CheB catalyzes deamidation of specific glutamine residues in the cytoplasmic region of the chemoreceptors and demethylation of specific methyl glutamate residues introduced into the chemoreceptors by CheR.


Pssm-ID: 319753  Cd Length: 180  Bit Score: 121.32  E-value: 2.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 143 LIAVGCSAGGPDATGEMLKTIGTSLLkTSVVVVQHIGEDFQAEYVQWLRRV--LPWVNVdvgEDGEKLLPGCVRVAGQGA 220
Cdd:cd16434     1 VVGIGASAGGLEALEEFFSALPADSG-MAFVVVQHLSPDHKSLLAELLARHtsMPVVEA---EDGMRVEPNHVYVIPPGK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 221 HLEVTEGpALRLdRNAPPDHGHRPSVDRLFESVARSIPRSSVGVLLSGMGVDGVEGLLSLSRAGCLTLVQDRESSAVFGM 300
Cdd:cd16434    77 DLTIEDG-RLRL-SPPDEPRGPRLPIDVFFRSLAEDQGERAIGVILSGTGSDGTLGLKAIKEAGGLVLAQDPETAKFDGM 154

                         170       180
                  ....*....|....*....|...
gi 1490893224 301 PRVALERGAAAIVQPPDALGRAL 323
Cdd:cd16434   155 PRSAIATGLVDFVLPPEEIAAEL 177
CheB_like cd16351
methylesterase CheB domain family; This family contains the methylesterase CheB (EC 3.1.1.61; ...
 143-316 3.78e-32

methylesterase CheB domain family; This family contains the methylesterase CheB (EC 3.1.1.61; also known as CheB methylesterase, chemotaxis-specific methylesterase, methyl-accepting chemotaxis protein methyl-esterase, or protein methyl-esterase) domain, a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors. Signaling output of the chemotaxis receptors is modulated by CheB and methyltransferase CheR by controlling the level of receptor methylation. CheB family members may also contain an N-terminal regulatory (REC) domain, which blocks the active site of the C-terminal domain until it is phosphorylated, or a CheR domain; typically cheB and cheR occur in the same operon. Reversible methylation of transmembrane chemoreceptors plays an important role in ligand-dependent signaling and cellular adaptation in bacterial chemotaxis. Phosphorylated CheB catalyzes deamidation of specific glutamine residues in the cytoplasmic region of the chemoreceptors and demethylation of specific methyl glutamate residues introduced into the chemoreceptors by CheR.


Pssm-ID: 319750  Cd Length: 184  Bit Score: 118.44  E-value: 3.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 143 LIAVGCSAGGPDATGEMLKTIGTSLlKTSVVVVQHIGEDFQAEYVQWLRRvLPWVNVDVGEDGEKLLPGCVRVAGQGAHL 222
Cdd:cd16351     1 IVGIGASTGGLEALEHLFEQLPIHS-GLVYVVIQHMPPGFTSSMAERLGK-KTKVGVKEAEDGEPVEPGTIYIAPGDTHI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490893224 223 EVTEGPA---LRLDrNAPPDHGHRPSVDRLFESVARSIPRSSVGVLLSGMGVDGVEGLLSLSRAGCLTLVQDRESSAVFG 299
Cdd:cd16351    79 NLENGKGfkvQELS-NDTGINNLRPPVDHFFSSLAKYNKEKSIAVILTGMGNDGSSGLSYVYDTGGTVIAQTEESCVVFG 157

                         170
                  ....*....|....*..
gi 1490893224 300 MPRVALERGAAAIVQPP 316
Cdd:cd16351   158 MPNYAIQTGKVDHVVRP 174
 
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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