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Conserved domains on  [gi|1788192|gb|AAC74953|]
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protein-glutamate methylesterase/protein glutamine deamidase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

chemotaxis response regulator protein-glutamate methylesterase( domain architecture ID 11479194)

chemotaxis protein CheB is 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
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1-345 0e+00

chemotaxis-specific protein-glutamate methyltransferase CheB;


:

Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 587.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     1 MSKIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVV 80
Cdd:PRK00742   1 MMKIRVLVVDDSAFMRRLISEILNSDPDIEVVGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRPTPVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    81 MVSSLTGKGSEVTLRALELGAIDFVTKPQLGIREGMLAYNEMIAEKVRTAAKASL---------AAHKPLSAPTTLKAGP 151
Cdd:PRK00742  81 MVSSLTERGAEITLRALELGAVDFVTKPFLGISLGMDEYKEELAEKVRAAARARVralppraaaAARAAAAAPAALAAAP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192   152 LLSSeKLIAIGASTGGTEAIRHVLQPLPLSSPA-LLITQHMPPGFTRSFADRLNKLCQIGVKEAEDGERVLPGHAYIAPG 230
Cdd:PRK00742 161 LLSS-KLVAIGTSTGGPEALQKVLTPLPANFPApILIVQHMPAGFTKSFAERLNRLCQIEVKEAEDGERLKPGHAYIAPG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192   231 DRHMELSRSGANYQIKIHDGPAVNRHRPSVDVLFHSVAKQAGRNAVGVILTGMGNDGAAGMLAMRQAGAWTLAQNEASCV 310
Cdd:PRK00742 240 GKHMMVARSGANYRIKLDDGPPVNRHRPSVDVLFRSAAKAAGRNALGVILTGMGRDGAAGLLEMKQAGATTIAQDEASCV 319
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 1788192   311 VFGMPREAINMGGVCEVVDLSQVSQQMLAKISAGQ 345
Cdd:PRK00742 320 VYGMPKAAIEAGAVDEVLPLDQIAERILKEVAAGR 354
 
Name Accession Description Interval E-value
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1-345 0e+00

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 587.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     1 MSKIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVV 80
Cdd:PRK00742   1 MMKIRVLVVDDSAFMRRLISEILNSDPDIEVVGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRPTPVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    81 MVSSLTGKGSEVTLRALELGAIDFVTKPQLGIREGMLAYNEMIAEKVRTAAKASL---------AAHKPLSAPTTLKAGP 151
Cdd:PRK00742  81 MVSSLTERGAEITLRALELGAVDFVTKPFLGISLGMDEYKEELAEKVRAAARARVralppraaaAARAAAAAPAALAAAP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192   152 LLSSeKLIAIGASTGGTEAIRHVLQPLPLSSPA-LLITQHMPPGFTRSFADRLNKLCQIGVKEAEDGERVLPGHAYIAPG 230
Cdd:PRK00742 161 LLSS-KLVAIGTSTGGPEALQKVLTPLPANFPApILIVQHMPAGFTKSFAERLNRLCQIEVKEAEDGERLKPGHAYIAPG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192   231 DRHMELSRSGANYQIKIHDGPAVNRHRPSVDVLFHSVAKQAGRNAVGVILTGMGNDGAAGMLAMRQAGAWTLAQNEASCV 310
Cdd:PRK00742 240 GKHMMVARSGANYRIKLDDGPPVNRHRPSVDVLFRSAAKAAGRNALGVILTGMGRDGAAGLLEMKQAGATTIAQDEASCV 319
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 1788192   311 VFGMPREAINMGGVCEVVDLSQVSQQMLAKISAGQ 345
Cdd:PRK00742 320 VYGMPKAAIEAGAVDEVLPLDQIAERILKEVAAGR 354
CheB_Rec cd16432
Chemotaxis response regulator protein-glutamate methylesterase, CheB, with N-terminal REC ...
158-339 1.78e-106

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: 309.29  E-value: 1.78e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192  158 LIAIGASTGGTEAIRHVLQPLPLSSPA-LLITQHMPPGFTRSFADRLNKLCQIGVKEAEDGERVLPGHAYIAPGDRHMEL 236
Cdd:cd16432   1 LVAIGASTGGPQALQEILSALPADFPApILIVQHMPPGFTKSFAERLNRLSALPVKEAEDGEPLEPGTVYIAPGGYHLVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192  237 SRSGANYQIKIHDGPAVNRHRPSVDVLFHSVAKQAGRNAVGVILTGMGNDGAAGMLAMRQAGAWTLAQNEASCVVFGMPR 316
Cdd:cd16432  81 ERRGGGGRIRLSDGPPVNGHRPSVDVLFRSAAEVYGARALGVILTGMGRDGAEGLLALKEAGGYTIAQDEASSVVYGMPK 160
                       170       180
                ....*....|....*....|...
gi 1788192  317 EAINMGGVCEVVDLSQVSQQMLA 339
Cdd:cd16432 161 AAIEAGAADEVLPLDEIAAAILR 183
CheB COG2201
Chemotaxis response regulator CheB, contains REC and protein-glutamate methylesterase domains ...
156-346 1.25e-101

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


Pssm-ID: 441803  Cd Length: 193  Bit Score: 297.38  E-value: 1.25e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192  156 EKLIAIGASTGGTEAIRHVLQPLPLSSP-ALLITQHMPPGFTRSFADRLNKLCQIGVKEAEDGERVLPGHAYIAPGDRHM 234
Cdd:COG2201   3 FKVVAIGASTGGPEALEEVLSALPADFPaPIVIVQHMPPGFTSSLAERLNRLTALPVKEAEDGERLEPGHVYIAPGGRHL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192  235 ELSRSGAnYQIKIHDGPAVNRHRPSVDVLFHSVAKQAGRNAVGVILTGMGNDGAAGMLAMRQAGAWTLAQNEASCVVFGM 314
Cdd:COG2201  83 EVERSGG-YRLRLSDGPPVNGHRPSVDVLFRSLAEVYGERAVGVILTGMGSDGAEGLKAIKEAGGLTIAQDEESCVVYGM 161
                       170       180       190
                ....*....|....*....|....*....|..
gi 1788192  315 PREAINMGGVCEVVDLSQVSQQMLAKISAGQA 346
Cdd:COG2201 162 PRAAIEAGAVDEVLPLEEIAAALLRLLRRRAA 193
CheB_methylest pfam01339
CheB methylesterase;
159-337 7.45e-90

CheB methylesterase;


Pssm-ID: 460166  Cd Length: 178  Bit Score: 266.98  E-value: 7.45e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    159 IAIGASTGGTEAIRHVLQPLPLSSP-ALLITQHMPPGFTRSFADRLNKLCQIGVKEAEDGERVLPGHAYIAPGDRHMELS 237
Cdd:pfam01339   1 VAIGASTGGPEALEELLPALPADLPaAIVVVQHMPPGFTSSLAERLNRLSALPVKEAEDGEPLEPGTVYIAPGGYHLLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    238 RSGANYQikiHDGPAVNRHRPSVDVLFHSVAK-QAGRNAVGVILTGMGNDGAAGMLAMRQAGAWTLAQNEASCVVFGMPR 316
Cdd:pfam01339  81 DGRGPYR---SDGPPVNGHRPSIDVLFRSLAEaYGGKRAIGVILTGMGSDGAAGLKAIKEAGGLTIAQDPATAVVYGMPR 157
                         170       180
                  ....*....|....*....|.
gi 1788192    317 EAINMGGVCEVVDLSQVSQQM 337
Cdd:pfam01339 158 AAIEAGAADFVLPLEEIAAEL 178
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
2-108 3.44e-18

sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a transcription factor critical for the initiation of sporulation. It contains a response regulator receiver domain (pfam00072). In Bacillus subtilis, it works together with response regulator Spo0F and the phosphotransferase Spo0B, both of which are missing from at least some sporulating species and thus not part of the endospore forming bacteria minimal gene set. Spo0A, however, is universal among endospore-forming species. [Cellular processes, Sporulation and germination]


Pssm-ID: 131922 [Multi-domain]  Cd Length: 262  Bit Score: 82.92  E-value: 3.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192      2 SKIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMR--LRPMPV 79
Cdd:TIGR02875   1 HKIRIVIADDNKEFCNLLKEYLAAQPDMEVVGVAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNEieLSARPR 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1788192     80 VMVssLTGKGSE-VTLRALELGAIDFVTKP 108
Cdd:TIGR02875  81 VIM--LSAFGQEkITQRAVALGADYYVLKP 108
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
4-60 2.18e-07

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 47.18  E-value: 2.18e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1788192       4 IRVLSVDDSALMRQIMTEIINSHSDMemVATAPDPLVARDLIKKFNPDVLTLDVEMP 60
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYE--VDEATDGEEALELLKEEKPDLILLDIMMP 55
 
Name Accession Description Interval E-value
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1-345 0e+00

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 587.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     1 MSKIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVV 80
Cdd:PRK00742   1 MMKIRVLVVDDSAFMRRLISEILNSDPDIEVVGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRPTPVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    81 MVSSLTGKGSEVTLRALELGAIDFVTKPQLGIREGMLAYNEMIAEKVRTAAKASL---------AAHKPLSAPTTLKAGP 151
Cdd:PRK00742  81 MVSSLTERGAEITLRALELGAVDFVTKPFLGISLGMDEYKEELAEKVRAAARARVralppraaaAARAAAAAPAALAAAP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192   152 LLSSeKLIAIGASTGGTEAIRHVLQPLPLSSPA-LLITQHMPPGFTRSFADRLNKLCQIGVKEAEDGERVLPGHAYIAPG 230
Cdd:PRK00742 161 LLSS-KLVAIGTSTGGPEALQKVLTPLPANFPApILIVQHMPAGFTKSFAERLNRLCQIEVKEAEDGERLKPGHAYIAPG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192   231 DRHMELSRSGANYQIKIHDGPAVNRHRPSVDVLFHSVAKQAGRNAVGVILTGMGNDGAAGMLAMRQAGAWTLAQNEASCV 310
Cdd:PRK00742 240 GKHMMVARSGANYRIKLDDGPPVNRHRPSVDVLFRSAAKAAGRNALGVILTGMGRDGAAGLLEMKQAGATTIAQDEASCV 319
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 1788192   311 VFGMPREAINMGGVCEVVDLSQVSQQMLAKISAGQ 345
Cdd:PRK00742 320 VYGMPKAAIEAGAVDEVLPLDQIAERILKEVAAGR 354
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
4-339 1.28e-149

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 424.68  E-value: 1.28e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     4 IRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVS 83
Cdd:PRK12555   1 MRIGIVNDSPLAVEALRRALARDPDHEVVWVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAERPCPILIVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    84 SLTGKGSEVTLRALELGAIDFVTKPQLGIREGMLAYNEMIAEKVRTAAKASLAAHKPLSAPTTLKAGPLLSSEKLIAIGA 163
Cdd:PRK12555  81 SLTERNASRVFEAMGAGALDAVDTPTLGIGAGLEEYAAELLAKIDQIGRLLGRRLAPAAAPAAASAAPFRTTPRLVAIGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192   164 STGGTEAIRHVLQPLPLSSPA-LLITQHMPPGFTRSFADRLNKLCQIGVKEAEDGERVLPGHAYIAPGDRHMELSRSGAn 242
Cdd:PRK12555 161 SAGGPAALAVLLGGLPADFPAaIVIVQHVDAAFAAGMAEWLDGQTALPVREAREGERPQPGHVLLAPTNDHLRLTRDGA- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192   243 yqIKIHDGPAVNRHRPSVDVLFHSVAKQAGRNAVGVILTGMGNDGAAGMLAMRQAGAWTLAQNEASCVVFGMPREAINMG 322
Cdd:PRK12555 240 --LRYTREPPVNPYRPSVDVFFESVAQHWGGNAIGVLLTGMGRDGARGLKAMRQAGAHTIAQDEASSAVYGMPKAAAALG 317
                        330
                 ....*....|....*..
gi 1788192   323 GVCEVVDLSQVSQQMLA 339
Cdd:PRK12555 318 AASEVLPLERIAPRLIA 334
CheB_Rec cd16432
Chemotaxis response regulator protein-glutamate methylesterase, CheB, with N-terminal REC ...
158-339 1.78e-106

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: 309.29  E-value: 1.78e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192  158 LIAIGASTGGTEAIRHVLQPLPLSSPA-LLITQHMPPGFTRSFADRLNKLCQIGVKEAEDGERVLPGHAYIAPGDRHMEL 236
Cdd:cd16432   1 LVAIGASTGGPQALQEILSALPADFPApILIVQHMPPGFTKSFAERLNRLSALPVKEAEDGEPLEPGTVYIAPGGYHLVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192  237 SRSGANYQIKIHDGPAVNRHRPSVDVLFHSVAKQAGRNAVGVILTGMGNDGAAGMLAMRQAGAWTLAQNEASCVVFGMPR 316
Cdd:cd16432  81 ERRGGGGRIRLSDGPPVNGHRPSVDVLFRSAAEVYGARALGVILTGMGRDGAEGLLALKEAGGYTIAQDEASSVVYGMPK 160
                       170       180
                ....*....|....*....|...
gi 1788192  317 EAINMGGVCEVVDLSQVSQQMLA 339
Cdd:cd16432 161 AAIEAGAADEVLPLDEIAAAILR 183
CheB_like cd16351
methylesterase CheB domain family; This family contains the methylesterase CheB (EC 3.1.1.61; ...
158-340 5.83e-105

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: 305.64  E-value: 5.83e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192  158 LIAIGASTGGTEAIRHVLQPLPLSSP-ALLITQHMPPGFTRSFADRLNKLCQIGVKEAEDGERVLPGHAYIAPGDRHMEL 236
Cdd:cd16351   1 IVGIGASTGGLEALEHLFEQLPIHSGlVYVVIQHMPPGFTSSMAERLGKKTKVGVKEAEDGEPVEPGTIYIAPGDTHINL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192  237 SRSGANYQIKIHDGPAVNRHRPSVDVLFHSVAKQAGRNAVGVILTGMGNDGAAGMLAMRQAGAWTLAQNEASCVVFGMPR 316
Cdd:cd16351  81 ENGKGFKVQELSNDTGINNLRPPVDHFFSSLAKYNKEKSIAVILTGMGNDGSSGLSYVYDTGGTVIAQTEESCVVFGMPN 160
                       170       180
                ....*....|....*....|....
gi 1788192  317 EAINMGGVCEVVDLSQVSQQMLAK 340
Cdd:cd16351 161 YAIQTGKVDHVVRPEEMASLFEQI 184
CheB COG2201
Chemotaxis response regulator CheB, contains REC and protein-glutamate methylesterase domains ...
156-346 1.25e-101

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


Pssm-ID: 441803  Cd Length: 193  Bit Score: 297.38  E-value: 1.25e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192  156 EKLIAIGASTGGTEAIRHVLQPLPLSSP-ALLITQHMPPGFTRSFADRLNKLCQIGVKEAEDGERVLPGHAYIAPGDRHM 234
Cdd:COG2201   3 FKVVAIGASTGGPEALEEVLSALPADFPaPIVIVQHMPPGFTSSLAERLNRLTALPVKEAEDGERLEPGHVYIAPGGRHL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192  235 ELSRSGAnYQIKIHDGPAVNRHRPSVDVLFHSVAKQAGRNAVGVILTGMGNDGAAGMLAMRQAGAWTLAQNEASCVVFGM 314
Cdd:COG2201  83 EVERSGG-YRLRLSDGPPVNGHRPSVDVLFRSLAEVYGERAVGVILTGMGSDGAEGLKAIKEAGGLTIAQDEESCVVYGM 161
                       170       180       190
                ....*....|....*....|....*....|..
gi 1788192  315 PREAINMGGVCEVVDLSQVSQQMLAKISAGQA 346
Cdd:COG2201 162 PRAAIEAGAVDEVLPLEEIAAALLRLLRRRAA 193
CheB_methylest pfam01339
CheB methylesterase;
159-337 7.45e-90

CheB methylesterase;


Pssm-ID: 460166  Cd Length: 178  Bit Score: 266.98  E-value: 7.45e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    159 IAIGASTGGTEAIRHVLQPLPLSSP-ALLITQHMPPGFTRSFADRLNKLCQIGVKEAEDGERVLPGHAYIAPGDRHMELS 237
Cdd:pfam01339   1 VAIGASTGGPEALEELLPALPADLPaAIVVVQHMPPGFTSSLAERLNRLSALPVKEAEDGEPLEPGTVYIAPGGYHLLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    238 RSGANYQikiHDGPAVNRHRPSVDVLFHSVAK-QAGRNAVGVILTGMGNDGAAGMLAMRQAGAWTLAQNEASCVVFGMPR 316
Cdd:pfam01339  81 DGRGPYR---SDGPPVNGHRPSIDVLFRSLAEaYGGKRAIGVILTGMGSDGAAGLKAIKEAGGLTIAQDPATAVVYGMPR 157
                         170       180
                  ....*....|....*....|.
gi 1788192    317 EAINMGGVCEVVDLSQVSQQM 337
Cdd:pfam01339 158 AAIEAGAADFVLPLEEIAAEL 178
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
4-128 1.83e-61

phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate methylesterase CheB and similar chemotaxis proteins; Methylesterase CheB is a chemotaxis response regulator with an N-terminal REC domain and a C-terminal methylesterase domain. Chemotaxis is a behavior known in motile bacteria that directs their movement in response to chemical gradients. CheB is a phosphorylation-activated response regulator involved in the reversible modification of bacterial chemotaxis receptors. It catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. The CheB REC domain packs against the active site of the C-terminal domain and inhibits methylesterase activity by directly restricting access to the active site. Also included in this family is chemotaxis response regulator CheY, which contains a stand-alone REC domain, and an uncharacterized subfamily composed of proteins containing an N-terminal REC domain and a C-terminal CheY-P phosphatase (CheC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 192.61  E-value: 1.83e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    4 IRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVS 83
Cdd:cd17541   1 IRVLIVDDSAVMRKLLSRILESDPDIEVVGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERPTPVVMVS 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 1788192   84 SLTGKGSEVTLRALELGAIDFVTKPQLGIREGMLAYNEMIAEKVR 128
Cdd:cd17541  81 SLTEEGAEITLEALELGAVDFIAKPSGGISLDLEEIAEELIEKIK 125
CheB cd16433
Chemotaxis response regulator protein-glutamate methylesterase, CheB; This family contains the ...
158-332 1.79e-59

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: 189.51  E-value: 1.79e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192  158 LIAIGASTGGTEAIRHVLQPLPLSSPA-LLITQHMPPGFTRSFADRLNKLCQIGVKEAEDGERVLPGHAYIAPGDRHMEL 236
Cdd:cd16433   1 IVVIGASAGGLEALLELLSALPADFPApVLVVLHRPPDSPSVLPELLSRRTPLPVKEAEDGEPIEPGTIYVAPPDYHLLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192  237 SRSGAnyqIKIHDGPAVNRHRPSVDVLFHSVAKQAGRNAVGVILTGMGNDGAAGMLAMRQAGAWTLAQNEASCVVFGMPR 316
Cdd:cd16433  81 EDDGT---FSLSRGPKVNFSRPSIDVLFRSAADAYGPRVIGVVLTGANDDGAAGLAAIKRAGGLTIVQDPATAEVPSMPR 157
                       170
                ....*....|....*.
gi 1788192  317 EAINMGGVCEVVDLSQ 332
Cdd:cd16433 158 AALAAVAVDHVLPLAE 173
CheB-CheR_fusion cd16434
Chemotaxis response regulator protein-glutamate methylesterase, CheB, fused with CheR domain; ...
158-324 4.04e-41

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: 142.12  E-value: 4.04e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192  158 LIAIGASTGGTEAIRHVLQPLPLSSP-ALLITQHMPPGFTRSFADRLNKLCQIGVKEAEDGERVLPGHAYIAPGDRHMEL 236
Cdd:cd16434   1 VVGIGASAGGLEALEEFFSALPADSGmAFVVVQHLSPDHKSLLAELLARHTSMPVVEAEDGMRVEPNHVYVIPPGKDLTI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192  237 SrsgaNYQIKIHDGPAVNRHRPSVDVLFHSVAKQAGRNAVGVILTGMGNDGAAGMLAMRQAGAWTLAQNEASCVVFGMPR 316
Cdd:cd16434  81 E----DGRLRLSPPDEPRGPRLPIDVFFRSLAEDQGERAIGVILSGTGSDGTLGLKAIKEAGGLVLAQDPETAKFDGMPR 156

                ....*...
gi 1788192  317 EAINMGGV 324
Cdd:cd16434 157 SAIATGLV 164
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
5-108 2.14e-26

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 101.00  E-value: 2.14e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    5 RVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP-MPVVMVS 83
Cdd:COG4753   1 KVLIVDDEPLIREGLKRILEWEAGFEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPdTKIIILS 80
                        90       100
                ....*....|....*....|....*
gi 1788192   84 SLTGKgsEVTLRALELGAIDFVTKP 108
Cdd:COG4753  81 GYSDF--EYAQEAIKLGADDYLLKP 103
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
5-108 2.14e-25

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 98.67  E-value: 2.14e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    5 RVLSVDDSALMRQIMTEIINSHSDMEMVATApDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPM---PVVM 81
Cdd:cd17551   2 RILIVDDNPTNLLLLEALLRSAGYLEVVSFT-DPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLedvPIVM 80
                        90       100
                ....*....|....*....|....*..
gi 1788192   82 VSSLTGKgsEVTLRALELGAIDFVTKP 108
Cdd:cd17551  81 ITADTDR--EVRLRALEAGATDFLTKP 105
Spo0A COG5801
Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell ...
1-108 2.65e-25

Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444503 [Multi-domain]  Cd Length: 264  Bit Score: 102.57  E-value: 2.65e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    1 MSKIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKL--MRLRPMP 78
Cdd:COG5801   2 MEKIKVLIADDNREFCELLEEYLSSQPDMEVVGVAYNGLEALELIEEKKPDVVILDIIMPHLDGLGVLEKLreMNLEKRP 81
                        90       100       110
                ....*....|....*....|....*....|.
gi 1788192   79 VVMVssLTGKGSE-VTLRALELGAIDFVTKP 108
Cdd:COG5801  82 KVIM--LTAFGQEdITQRAVELGADYYILKP 110
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
6-108 2.30e-24

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 95.68  E-value: 2.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192      6 VLSVDDSALMRQIMTEIINShSDMEmVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP-MPVVMVss 84
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEK-EGYV-VAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPtTPVIIL-- 76
                          90       100
                  ....*....|....*....|....*
gi 1788192     85 lTGKGSEVT-LRALELGAIDFVTKP 108
Cdd:pfam00072  77 -TAHGDEDDaVEALEAGADDFLSKP 100
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
3-108 3.01e-24

phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the phosphorelay system in the early stage of spore formation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress and may act in the with sigma factor spo0H to control the expression of some genes that are critical to the sporulation process. Spo0A contains a regulatory N-terminal REC domain and a C-terminal DNA-binding transcription activation domain as its effector/output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 95.37  E-value: 3.01e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    3 KIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKL--MRLRPMPVV 80
Cdd:cd17561   1 KIKVLIADDNREFVQLLEEYLNSQPDMEVVGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLrrMRLEKRPKI 80
                        90       100
                ....*....|....*....|....*....
gi 1788192   81 MVssLTGKGSE-VTLRALELGAIDFVTKP 108
Cdd:cd17561  81 IM--LTAFGQEdITQRAVELGASYYILKP 107
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
3-108 3.18e-24

DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction mechanisms];


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 99.12  E-value: 3.18e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    3 KIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMP-VVM 81
Cdd:COG3279   1 MMKILIVDDEPLARERLERLLEKYPDLEVVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPpIIF 80
                        90       100
                ....*....|....*....|....*..
gi 1788192   82 VSSLtgkgSEVTLRALELGAIDFVTKP 108
Cdd:COG3279  81 TTAY----DEYALEAFEVNAVDYLLKP 103
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
9-108 2.60e-23

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 92.68  E-value: 2.60e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    9 VDDSALMRQIMTEIINSHSdmEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP-MPVVMVSSLTG 87
Cdd:cd00156   3 VDDDPAIRELLKSLLEREG--YEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPdIPVIVLTAKAD 80
                        90       100
                ....*....|....*....|.
gi 1788192   88 KGSEVtlRALELGAIDFVTKP 108
Cdd:cd00156  81 EEDAV--RALELGADDYLVKP 99
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
3-108 2.81e-23

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 94.98  E-value: 2.81e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    3 KIRVLSVDDSALMRQIMTEIINSHsDMEmVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKL---MRLRPMPV 79
Cdd:COG3706   1 PARILVVDDDPTNRKLLRRLLEAA-GYE-VVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLradPRTADIPI 78
                        90       100
                ....*....|....*....|....*....
gi 1788192   80 VMVSSLTGKGSEVtlRALELGAIDFVTKP 108
Cdd:COG3706  79 IFLTALDDEEDRA--RALEAGADDYLTKP 105
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1-108 1.37e-21

DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 89.26  E-value: 1.37e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    1 MSKIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKL-MRLRPMPV 79
Cdd:COG4565   1 MKMIRVLIVEDDPMVAELLRRYLERLPGFEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELrARGPDVDV 80
                        90       100
                ....*....|....*....|....*....
gi 1788192   80 VMVSSltGKGSEVTLRALELGAIDFVTKP 108
Cdd:COG4565  81 IVITA--ARDPETVREALRAGVVDYLIKP 107
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
2-108 1.76e-20

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 91.56  E-value: 1.76e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    2 SKIRVLSVDDSALMRQIMTEIINSHsDMEmVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP-MPVV 80
Cdd:COG2204   1 SMARILVVDDDPDIRRLLKELLERA-GYE-VETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPdLPVI 78
                        90       100
                ....*....|....*....|....*....
gi 1788192   81 MvssLTGKGS-EVTLRALELGAIDFVTKP 108
Cdd:COG2204  79 L---LTGYGDvETAVEAIKAGAFDYLTKP 104
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1-108 2.19e-20

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 85.67  E-value: 2.19e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    1 MSKIRVLSVDDSALMRQIMTEIINSHsDMEmVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKL---MRLRPM 77
Cdd:COG0784   3 LGGKRILVVDDNPDNRELLRRLLERL-GYE-VTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIralPRLPDI 80
                        90       100       110
                ....*....|....*....|....*....|.
gi 1788192   78 PVVMVSSLTGKGSEVtlRALELGAIDFVTKP 108
Cdd:COG0784  81 PIIALTAYADEEDRE--RALEAGADDYLTKP 109
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
6-108 3.03e-19

phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response regulators; This family is composed of uncharacterized response regulators that contain a REC domain and a AraC family helix-turn-helix (HTH) DNA-binding output domain, including Bacillus subtilis uncharacterized transcriptional regulatory protein YesN and Staphylococcus aureus uncharacterized response regulatory protein SAR0214. YesN is a member of the two-component regulatory system YesM/YesN and SAR0214 is a member of the probable two-component regulatory system SAR0215/SAR0214. Also included in this family is the AlgR-like group of LytTR/AlgR family response, which includes Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR and Bacillus subtilis sensory transduction protein LytT, among others. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 82.00  E-value: 3.03e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMTEIINSHS-DMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVss 84
Cdd:cd17536   1 VLIVDDEPLIREGLKKLIDWEElGFEVVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIII-- 78
                        90       100       110
                ....*....|....*....|....*....|.
gi 1788192   85 LTG-------KgsevtlRALELGAIDFVTKP 108
Cdd:cd17536  79 LSGyddfeyaQ------KAIRLGVVDYLLKP 103
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
4-108 3.43e-19

phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response regulator CheY contains a stand-alone REC domain. Chemotaxis is a behavior known for motile bacteria that directs their movement in response to chemical gradients. CheY is involved in transmitting sensory signals from chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 81.94  E-value: 3.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    4 IRVLSVDDSALMRQIMTEIINSHSdMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP-MPVVMV 82
Cdd:cd17542   1 KKVLIVDDAAFMRMMLKDILTKAG-YEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPnAKVIMC 79
                        90       100
                ....*....|....*....|....*.
gi 1788192   83 SSLtGKgSEVTLRALELGAIDFVTKP 108
Cdd:cd17542  80 SAM-GQ-EEMVKEAIKAGAKDFIVKP 103
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
3-108 4.90e-19

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 83.85  E-value: 4.90e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    3 KIRVLSVDDSALMRQIMTEIInSHSDMEmVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKL-MRLRPMPVVM 81
Cdd:COG0745   1 MPRILVVEDDPDIRELLADAL-EREGYE-VDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLrARPSDIPIIM 78
                        90       100
                ....*....|....*....|....*...
gi 1788192   82 vssLTGKGSEVT-LRALELGAIDFVTKP 108
Cdd:COG0745  79 ---LTARDDEEDrVRGLEAGADDYLTKP 103
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
2-108 1.69e-18

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 82.91  E-value: 1.69e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    2 SKIRVLSVDDSALMRQIMTEIInsHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKL---MRLRPMP 78
Cdd:COG3437   5 QAPTVLIVDDDPENLELLRQLL--RTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLradPSTRDIP 82
                        90       100       110
                ....*....|....*....|....*....|
gi 1788192   79 VVMVSSLTgkGSEVTLRALELGAIDFVTKP 108
Cdd:COG3437  83 VIFLTALA--DPEDRERALEAGADDYLTKP 110
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
2-108 3.44e-18

sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a transcription factor critical for the initiation of sporulation. It contains a response regulator receiver domain (pfam00072). In Bacillus subtilis, it works together with response regulator Spo0F and the phosphotransferase Spo0B, both of which are missing from at least some sporulating species and thus not part of the endospore forming bacteria minimal gene set. Spo0A, however, is universal among endospore-forming species. [Cellular processes, Sporulation and germination]


Pssm-ID: 131922 [Multi-domain]  Cd Length: 262  Bit Score: 82.92  E-value: 3.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192      2 SKIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMR--LRPMPV 79
Cdd:TIGR02875   1 HKIRIVIADDNKEFCNLLKEYLAAQPDMEVVGVAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNEieLSARPR 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1788192     80 VMVssLTGKGSE-VTLRALELGAIDFVTKP 108
Cdd:TIGR02875  81 VIM--LSAFGQEkITQRAVALGADYYVLKP 108
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
6-108 8.87e-17

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AlgR-like group of LytTR/AlgR family response regulators are Streptococcus agalactiae sensory transduction protein LytR, Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR, Bacillus subtilis sensory transduction protein LytT, and Escherichia coli transcriptional regulatory protein BtsR, which are members of two-component regulatory systems. LytR and LytT are components of regulatory systems that regulate genes involved in cell wall metabolism. AlgR positively regulates the algD gene, which codes for a GDP-mannose dehydrogenase, a key enzyme in the alginate biosynthesis pathway. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 75.27  E-value: 8.87e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMP-VVMVSS 84
Cdd:cd17532   1 ALIVDDEPLAREELRYLLEEHPDIEIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPlIVFVTA 80
                        90       100
                ....*....|....*....|....
gi 1788192   85 LtgkgSEVTLRALELGAIDFVTKP 108
Cdd:cd17532  81 Y----DEYAVEAFELNAVDYLLKP 100
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
6-107 1.06e-16

phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators; The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 75.24  E-value: 1.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP-MPVVMVSS 84
Cdd:cd17535   1 VLIVDDHPLVREGLRRLLESEPDIEVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPdLKVIVLTA 80
                        90       100
                ....*....|....*....|...
gi 1788192   85 LTgkGSEVTLRALELGAIDFVTK 107
Cdd:cd17535  81 HD--DPEYVLRALKAGAAGYLLK 101
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
32-108 5.28e-16

phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 72.44  E-value: 5.28e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1788192   32 VATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP-MPVVMvssLTGKGSEVT-LRALELGAIDFVTKP 108
Cdd:cd17574  24 VDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSdIPIIM---LTAKDEEEDkVLGLELGADDYITKP 99
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
6-108 1.24e-15

phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins; NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 72.14  E-value: 1.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMTEIIN--SHSdmemVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP-MPVVMV 82
Cdd:cd17550   1 ILIVDDEEDIRESLSGILEdeGYE----VDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPdLPVIMI 76
                        90       100
                ....*....|....*....|....*..
gi 1788192   83 SsltGKGS-EVTLRALELGAIDFVTKP 108
Cdd:cd17550  77 S---GHGTiETAVKATKLGAYDFIEKP 100
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
5-108 3.99e-15

first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 70.22  E-value: 3.99e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    5 RVLSVDDSALMRQIMTEIINSHSdmEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLM---RLRPMPVVM 81
Cdd:cd17538   1 KILVVDDEPANRELLEALLSAEG--YEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKedpETRHIPVIM 78
                        90       100
                ....*....|....*....|....*..
gi 1788192   82 VSSLTGKGSEVtlRALELGAIDFVTKP 108
Cdd:cd17538  79 ITALDDREDRI--RGLEAGADDFLSKP 103
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1-108 4.42e-15

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 72.68  E-value: 4.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    1 MSKIRVLSVDDSALMRQIMTEIInSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVV 80
Cdd:COG3707   1 MRGLRVLVVDDEPLRRADLREGL-REAGYEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERPAPVI 79
                        90       100
                ....*....|....*....|....*...
gi 1788192   81 MVSSltGKGSEVTLRALELGAIDFVTKP 108
Cdd:COG3707  80 LLTA--YSDPELIERALEAGVSAYLVKP 105
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
3-71 4.17e-14

DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 68.38  E-value: 4.17e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1788192    3 KIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKL 71
Cdd:COG2197   1 MIRVLIVDDHPLVREGLRALLEAEPDIEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
6-108 5.30e-14

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar domains; Pseudomonas aeruginosa cyclic di-GMP phosphodiesterase PA4781 contains an N-terminal REC domain and a C-terminal catalytic HD-GYP domain, characteristics of RpfG family response regulators. PA4781 is involved in cyclic di-3',5'-GMP (c-di-GMP) hydrolysis/degradation in a two-step reaction via the linear intermediate pGpG to produce GMP. Its unphosphorylated REC domain prevents accessibility of c-di-GMP to the active site. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 67.15  E-value: 5.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMTEIINSHSdmEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLM---RLRPMPVVMV 82
Cdd:cd19920   1 ILIVDDVPDNLRLLSELLRAAG--YRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKadpATRHIPVIFL 78
                        90       100
                ....*....|....*....|....*.
gi 1788192   83 SSLTGKGSEVtlRALELGAIDFVTKP 108
Cdd:cd19920  79 TALTDTEDKV--KGFELGAVDYITKP 102
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
4-108 1.61e-13

phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes Mycobacterium tuberculosis PdtaR, also called Rv1626, and similar proteins containing a REC domain and an ANTAR (AmiR and NasR transcription antitermination regulators) RNA-binding output domain. PdtaR is a response regulator that acts at the level of transcriptional antitermination and is a member of the PdtaR/PdtaS two-component regulatory system. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 66.28  E-value: 1.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    4 IRVLSVDDSALMRQIMTEIINSHSdMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVS 83
Cdd:cd19932   1 VRVLIAEDEALIRMDLREMLEEAG-YEVVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENIAPIVLLT 79
                        90       100
                ....*....|....*....|....*
gi 1788192   84 SLTGKgsEVTLRALELGAIDFVTKP 108
Cdd:cd19932  80 AYSQQ--DLVERAKEAGAMAYLVKP 102
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
4-108 1.92e-13

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 66.21  E-value: 1.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    4 IRVLSVDDSALMRQIMTEIINShSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLM---RLRPMPVV 80
Cdd:cd19923   1 MKVLVVDDFSTMRRIIKNLLKE-LGFNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRadgALSHLPVL 79
                        90       100
                ....*....|....*....|....*...
gi 1788192   81 MVSSLTGKgsEVTLRALELGAIDFVTKP 108
Cdd:cd19923  80 MVTAEAKK--ENVIAAAQAGVNNYIVKP 105
orf27 CHL00148
Ycf27; Reviewed
2-108 4.67e-13

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 67.82  E-value: 4.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     2 SKIRVLSVDDSALMRQIMT---EIINSHsdmemVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMP 78
Cdd:CHL00148   5 SKEKILVVDDEAYIRKILEtrlSIIGYE-----VITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKESDVP 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 1788192    79 VVMVSSLTGKGSEVTlrALELGAIDFVTKP 108
Cdd:CHL00148  80 IIMLTALGDVSDRIT--GLELGADDYVVKP 107
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
6-107 6.71e-13

phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of Bacillus subtilis DesR, Streptococcus pneumoniae response regulator spr1814, and similar proteins, all containing an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. DesR is a response regulator that, together with its cognate sensor kinase DesK, comprises a two-component regulatory system that controls membrane fluidity. Phosphorylation of the REC domain of DesR is allosterically coupled to two distinct exposed surfaces of the protein, controlling noncanonical dimerization/tetramerization, cooperative activation, and DesK binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 64.60  E-value: 6.71e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP-MPVVMVSS 84
Cdd:cd19930   1 VLIAEDQEMVRGALAALLELEDDLEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPdTKVLIVTT 80
                        90       100
                ....*....|....*....|....
gi 1788192   85 LTGKGsevTL-RALELGAIDFVTK 107
Cdd:cd19930  81 FGRPG---YFrRALAAGVDGYVLK 101
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
5-108 1.55e-12

phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; Pseudomonas aeruginosa RssB is an orphan atypical response regulator containing a REC domain and a PP2C-type protein phosphatase output domain. Its function is still unknown. Escherichia RssB, which is not included in this subfamily, is a ClpX adaptor protein which alters ClpX specificity by mediating a specific interaction between ClpX and the substrates such as RpoS, an RNA polymerase sigma factor. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 63.37  E-value: 1.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    5 RVLSVDDSALMRQIMTEIInSHSDMEMVAtAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP-MPVVMVS 83
Cdd:cd17555   2 TILVIDDDEVVRESIAAYL-EDSGFQVLQ-AADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPdTPVIVVS 79
                        90       100
                ....*....|....*....|....*.
gi 1788192   84 sltGKGS-EVTLRALELGAIDFVTKP 108
Cdd:cd17555  80 ---GAGVmSDAVEALRLGAWDYLTKP 102
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
6-108 1.81e-12

phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is part of the CpxA/CpxR two-component regulatory system that mediates envelope stress responses that is key for virulence and antibiotic resistance in several Gram negative pathogens. CpxR is a transcription factor/response regulator that controls the expression of numerous genes, including those of the classical porins OmpF and OmpC. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 63.09  E-value: 1.81e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMTEIINShsDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMvssL 85
Cdd:cd17623   1 ILLIDDDRELTELLTEYLEM--EGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTSQVPVLM---L 75
                        90       100
                ....*....|....*....|....
gi 1788192   86 TGKGSEVT-LRALELGAIDFVTKP 108
Cdd:cd17623  76 TARGDDIDrILGLELGADDYLPKP 99
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
6-108 6.04e-12

phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and similar proteins; C4-dicarboxylic acid transport protein D (DctD) is part of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA. It is an activator of sigma(54)-RNA polymerase holoenzyme that uses the energy released from ATP hydrolysis to stimulate the isomerization of a closed promoter complex to an open complex capable of initiating transcription. DctD is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 62.12  E-value: 6.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMTEIInSHSDMEmVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP-MPVVMVss 84
Cdd:cd17549   1 VLLVDDDADVREALQQTL-ELAGFR-VRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPdLPVILI-- 76
                        90       100
                ....*....|....*....|....*
gi 1788192   85 lTGKGS-EVTLRALELGAIDFVTKP 108
Cdd:cd17549  77 -TGHGDvPMAVEAMRAGAYDFLEKP 100
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
9-108 7.74e-12

phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response regulators contain an N-terminal receiver domain (REC) and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. The Sinorhizobium meliloti two-component system FixL/FixJ regulates nitrogen fixation in response to oxygen during symbiosis. Under microaerobic conditions, the kinase FixL phosphorylates the response regulator FixJ resulting in the regulation of nitrogen fixation genes such as nifA and fixK. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 61.46  E-value: 7.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    9 VDDSALMRQIMTEIINSHS-DMEMVATAPDPLVARDLIKkfnPDVLTLDVEMPRMDGLDFLEKLMRLR-PMPVVMvssLT 86
Cdd:cd17537   6 VDDDEAVRDSLAFLLRSVGlAVKTFTSASAFLAAAPPDQ---PGCLVLDVRMPGMSGLELQDELLARGsNIPIIF---IT 79
                        90       100
                ....*....|....*....|...
gi 1788192   87 GKGS-EVTLRALELGAIDFVTKP 108
Cdd:cd17537  80 GHGDvPMAVEAMKAGAVDFLEKP 102
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
32-114 9.46e-12

phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF appears to play an important role in cell wall integrity in a wide range of gram-positive bacteria, and may also modulate cell membrane integrity. It functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. YycF belongs to the OmpR family of response regulators, which are characterized by a REC domain and a winged helix-turn-helix effector domain involved in DNA binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 61.29  E-value: 9.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192   32 VATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMvssLTGKGSEV-TLRALELGAIDFVTKPqL 110
Cdd:cd17614  25 VVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSNVPIIM---LTAKDSEVdKVLGLELGADDYVTKP-F 100

                ....
gi 1788192  111 GIRE 114
Cdd:cd17614 101 SNRE 104
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
6-108 2.83e-11

phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and similar domains; Type-B ARRs (Arabidopsis response regulators) are a class of MYB-type transcription factors that act as major players in the transcriptional activation of cytokinin-responsive genes. They directly regulate the expression of type-A ARR genes and other downstream target genes. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Cytokinin signaling involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-B ARRs contain a receiver (REC) domain and a large C-terminal extension that has characteristics of an effector or output domain, with a Myb-like DNA binding domain referred to as the GARP domain. The GARP domain is a motif specific to plant transcription factors. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 59.95  E-value: 2.83e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMTEIINSHSDMemVATAPDPLVARDLIKKF--NPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVS 83
Cdd:cd17584   1 VLVVDDDPTCLAILKRMLLRCGYQ--VTTCTDAEEALSMLRENkdEFDLVITDVHMPDMDGFEFLELIRLEMDLPVIMMS 78
                        90       100
                ....*....|....*....|....*
gi 1788192   84 SlTGKGSEVtLRALELGAIDFVTKP 108
Cdd:cd17584  79 A-DGSTSTV-MKGLAHGACDYLLKP 101
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
5-108 2.98e-11

DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 61.47  E-value: 2.98e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    5 RVLSVDDSALMRQIMTEIinshsdMEM----VATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP-MPV 79
Cdd:COG4567   6 SLLLVDDDEAFARVLARA------LERrgfeVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPdARI 79
                        90       100       110
                ....*....|....*....|....*....|
gi 1788192   80 VMvssLTGKGSEVT-LRALELGAIDFVTKP 108
Cdd:COG4567  80 VV---LTGYASIATaVEAIKLGADDYLAKP 106
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
9-108 3.52e-11

DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 61.65  E-value: 3.52e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    9 VDDSALMRQIMTEIINSHS-DMEMVATAPDPLVARDLIKkfnPDVLTLDVEMPRMDGLDFLEKLMRLR-PMPVVMvssLT 86
Cdd:COG4566   5 VDDDEAVRDSLAFLLESAGlRVETFASAEAFLAALDPDR---PGCLLLDVRMPGMSGLELQEELAARGsPLPVIF---LT 78
                        90       100
                ....*....|....*....|...
gi 1788192   87 GKGS-EVTLRALELGAIDFVTKP 108
Cdd:COG4566  79 GHGDvPMAVRAMKAGAVDFLEKP 101
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
32-108 9.60e-11

phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; Sinorhizobium meliloti ChvI is part of the ExoS/ChvI two-component regulatory system (TCS) that is required for nitrogen-fixing symbiosis and exopolysaccharide synthesis. ExoS/ChvI also play important roles in regulating biofilm formation, motility, nutrient utilization, and the viability of free-living bacteria. ChvI belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 57.84  E-value: 9.60e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1788192   32 VATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMvssLTGKGSEV-TLRALELGAIDFVTKP 108
Cdd:cd19936  25 VETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKSTLPVIF---LTSKDDEIdEVFGLRMGADDYITKP 99
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
6-114 1.33e-10

phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is part of the VirA/VirG two-component system that regulates the expression of virulence (vir) genes. The histidine kinase VirA senses a phenolic wound response signal, undergoes autophosphorylation, and phosphorelays to the VirG response regulator, which induces transcription of the vir regulon. VirG belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 57.84  E-value: 1.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKfnPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVSSL 85
Cdd:cd17594   2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRR--VDLVLLDLRLGQESGLDLLRTIRARSDVPIIIISGD 79
                        90       100
                ....*....|....*....|....*....
gi 1788192   86 TGKGSEVTLrALELGAIDFVTKPqLGIRE 114
Cdd:cd17594  80 RRDEIDRVV-GLELGADDYLAKP-FGLRE 106
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
50-108 1.62e-10

phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains; This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 58.20  E-value: 1.62e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1788192   50 PDVLTLDVEMPRMDGLDFLEKLM---RLRPMPVVMVSSlTGKGSEVtLRALELGAIDFVTKP 108
Cdd:cd17557  53 PDLILLDLNMPRMDGFEVLREIKadpDLRRIPVVVLTT-SDAEEDI-ERAYELGANSYIVKP 112
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
4-108 2.13e-10

phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 57.64  E-value: 2.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    4 IRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRL-RPMPVVMV 82
Cdd:cd19925   1 INVLIVEDDPMVAEIHRAYVEQVPGFTVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAgHDVDVIVV 80
                        90       100
                ....*....|....*....|....*.
gi 1788192   83 SSLTGKgsEVTLRALELGAIDFVTKP 108
Cdd:cd19925  81 TAANDV--ETVREALRLGVVDYLIKP 104
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
9-108 2.37e-10

phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar proteins; Bacillus subtilis GlnL is part of the GlnK-GlnL (formerly YcbA-YcbB) two-component system that positively regulates the expression of the glsA-glnT (formerly ybgJ-ybgH) operon in response to glutamine. It contains a REC domain and a DNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 56.90  E-value: 2.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    9 VDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMP-VVMVSSLTG 87
Cdd:cd17565   4 VDDDKNIIKILSDIIEDDDLGEVVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGkFIMISQVSD 83
                        90       100
                ....*....|....*....|.
gi 1788192   88 KgsEVTLRALELGAIDFVTKP 108
Cdd:cd17565  84 K--EMIGKAYQAGIEFFINKP 102
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
4-108 4.41e-10

phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC domain; This subfamily is composed of uncharacterized proteins containing an N-terminal REC domain and a C-terminal CheC domain that may function as the output/effector domain of a response regulator. CheC is a CheY-P phosphatase, affecting the level of phosphorylated CheY which controls the sense of flagella rotation and determine swimming behavior of chemotactic bacteria. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 56.39  E-value: 4.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    4 IRVLSVDDSALMRQIMTEIINSHSDMEmVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLR-PMPVVMV 82
Cdd:cd17593   1 MKVLICDDSSMARKQLARALPADWDVE-ITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQlETKVIVV 79
                        90       100
                ....*....|....*....|....*....
gi 1788192   83 SsltgkG---SEVTLRALELGAIDFVTKP 108
Cdd:cd17593  80 S-----GdvqPEAKERVLELGALAFLKKP 103
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
5-84 5.39e-10

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains; Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 56.08  E-value: 5.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    5 RVLSVDDSALMRQIMTEIInshSDM-EMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP-MPVVMV 82
Cdd:cd17554   2 KILVVDDEENIRELYKEEL---EDEgYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPdLPVIIC 78

                ..
gi 1788192   83 SS 84
Cdd:cd17554  79 TA 80
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
5-108 5.42e-10

phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 56.21  E-value: 5.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    5 RVLSVDDSALMRQIMTeiINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP-MPVVMvs 83
Cdd:cd17615   1 RVLVVDDEPNITELLS--MALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPdVPVLF-- 76
                        90       100
                ....*....|....*....|....*.
gi 1788192   84 sLTGKGS-EVTLRALELGAIDFVTKP 108
Cdd:cd17615  77 -LTAKDSvEDRIAGLTAGGDDYVTKP 101
pleD PRK09581
response regulator PleD; Reviewed
32-108 6.58e-10

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 59.91  E-value: 6.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    32 VATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLM---RLRPMPVVMVSSLTGKGSEVtlRALELGAIDFVTKP 108
Cdd:PRK09581  29 VLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKsdpATTHIPVVMVTALDDPEDRV--RGLEAGADDFLTKP 106
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
5-108 8.73e-10

phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; Rhodobacter sphaeroides RegA, also called response regulator PrrA, is the DNA binding regulatory protein of a redox-responsive two-component regulatory system RegB/RegA that is involved in transactivating anaerobic expression of the photosynthetic apparatus. It contains a REC domain and a DNA-binding helix-turn-helix output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 55.53  E-value: 8.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    5 RVLSVDDSALMRQIMTEIINSHSdmEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP-MPVVMvs 83
Cdd:cd17563   2 SLLLVDDDEVFAERLARALERRG--FEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPdARIVV-- 77
                        90       100
                ....*....|....*....|....*.
gi 1788192   84 sLTGKGSEVT-LRALELGAIDFVTKP 108
Cdd:cd17563  78 -LTGYASIATaVEAIKLGADDYLAKP 102
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
32-114 9.63e-10

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 55.74  E-value: 9.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192   32 VATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMR---LRPMPVVMvssLTGKGSEV-TLRALELGAIDFVTK 107
Cdd:cd19937  24 VVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSdpkTSSIPIIM---LTAKGEEFdKVLGLELGADDYITK 100

                ....*..
gi 1788192  108 PqLGIRE 114
Cdd:cd19937 101 P-FSPRE 106
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
6-108 1.47e-09

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 54.78  E-value: 1.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMTEIINsHSDMEmVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKL----MRLRPMPVVM 81
Cdd:cd17546   1 VLVVDDNPVNRKVLKKLLE-KLGYE-VDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIreleGGGRRTPIIA 78
                        90       100
                ....*....|....*....|....*..
gi 1788192   82 VSSLTGKGSEVtlRALELGAIDFVTKP 108
Cdd:cd17546  79 LTANALEEDRE--KCLEAGMDDYLSKP 103
PRK11697 PRK11697
two-component system response regulator BtsR;
4-108 1.61e-09

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 57.55  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     4 IRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGldfLEKLMRLRP--MP-VV 80
Cdd:PRK11697   2 IKVLIVDDEPLAREELRELLQEEGDIEIVGECSNAIEAIGAIHRLKPDVVFLDIQMPRISG---LELVGMLDPehMPyIV 78
                         90       100
                 ....*....|....*....|....*...
gi 1788192    81 MVSSLtgkgSEVTLRALELGAIDFVTKP 108
Cdd:PRK11697  79 FVTAF----DEYAIKAFEEHAFDYLLKP 102
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
4-108 1.85e-09

second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This family is composed of uncharacterized PleD-like response regulators that contain two N-terminal REC domains and a C-terminal diguanylate cyclase output domain with the characteristic GGDEF motif at the active site. Unlike PleD which contains a REC-like adaptor domain, the second REC domain of these uncharacterized GGDEF domain proteins, described in this model, contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 54.83  E-value: 1.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    4 IRVLSVDDSALMRQIMTEIINSHsdMEMVATAPDPLVARDLIKKfNPD---VLTlDVEMPRMDGLDFLEKLMRLRP---M 77
Cdd:cd17544   1 IKVLVVDDSATSRNHLRALLRRH--NFQVLEAANGQEALEVLEQ-HPDiklVIT-DYNMPEMDGFELVREIRKKYSrdqL 76
                        90       100       110
                ....*....|....*....|....*....|.
gi 1788192   78 PVVMVSSlTGKGSeVTLRALELGAIDFVTKP 108
Cdd:cd17544  77 AIIGISA-SGDNA-LSARFIKAGANDFLTKP 105
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
5-108 2.26e-09

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 54.56  E-value: 2.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    5 RVLSVDDSALMRqimtEIINSHSDME--MVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMR---LRPMPV 79
Cdd:cd17618   2 TILIVEDEPAIR----EMIAFNLERAgfDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRdemTRDIPI 77
                        90       100       110
                ....*....|....*....|....*....|
gi 1788192   80 VMvssLTGKGSEV-TLRALELGAIDFVTKP 108
Cdd:cd17618  78 IM---LTARGEEEdKVRGLEAGADDYITKP 104
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
6-108 2.84e-09

phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase/response regulators; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase/response regulators contain all the elements of a classical TCS in a single polypeptide chain. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 54.25  E-value: 2.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMTEIINSHSdmEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLM---RLRPMPVVMV 82
Cdd:cd17598   1 ILIVEDSPTQAEQLKHILEEQG--YKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKsdpDLKDIPVILL 78
                        90       100
                ....*....|....*....|....*.
gi 1788192   83 SSLTgkGSEVTLRALELGAIDFVTKP 108
Cdd:cd17598  79 TTLS--DPRDVIRGLECGADNFITKP 102
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
6-108 4.24e-09

phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This subfamily includes the REC domains of Bacillus subtilis chemotaxis protein CheV, Myxococcus xanthus gliding motility regulatory protein FrzE, and similar proteins. CheV is a hybrid protein with an N-terminal CheW-like domain and a C-terminal CheY-like REC domain. The CheV pathway is one of three systems employed by B. subtilis for sensory adaptation that contribute to chemotaxis. It is involved in the transmission of sensory signals from chemoreceptors to flagellar motors. Together with CheW, it is involved in the coupling of methyl-accepting chemoreceptors to the central two-component histidine kinase CheA. FrzE is a hybrid sensor histidine kinase/response regulator that is part of the Frz pathway that controls cell reversal frequency to support directional motility during swarming and fruiting body formation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 53.54  E-value: 4.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSAL-MRQIMTEIINSHSDmemVATAPDPLVARDLIKKFNP---------DVLTLDVEMPRMDGLDFLEKLM--- 72
Cdd:cd19924   1 ILVVDDSPTaRKQLRDLLKNLGFE---IAEAVDGEEALNKLENLAKegndlskelDLIITDIEMPKMDGYELTFELRddp 77
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 1788192   73 RLRPMPVVMVSSLTgkGSEVTLRALELGAIDFVTKP 108
Cdd:cd19924  78 RLANIPVILNSSLS--GEFSRARGKKVGADAYLAKF 111
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
6-108 4.96e-09

phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) PatA is necessary for proper patterning of heterocysts along filaments. PatA contains phosphoacceptor REC domain at its C-terminus and an N-terminal PATAN (PatA N-terminus) domain, which was proposed in a bioinformatics study to mediate protein-protein interactions. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members of this group may have an inactive REC domain, lacking canonical metal-binding and active site residues.


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 53.14  E-value: 4.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMTEIINSHSDMEMVATapDPLVARDLIKKFNPDVLTLDVEMPRMDGLD---FLEKLMRLRPMPVVMv 82
Cdd:cd17602   1 VACVDDRPSIQKMIEYFLEKQGFRVVVID--DPLRALTTLLNSKPDLILIDIDMPDLDGYElcsLLRKSSALKDTPIIM- 77
                        90       100
                ....*....|....*....|....*..
gi 1788192   83 ssLTGKGSEVT-LRALELGAIDFVTKP 108
Cdd:cd17602  78 --LTGKDGLVDrIRAKMAGASGYLTKP 102
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
43-108 6.17e-09

phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family response regulators; Streptococcus agalactiae NsrR is a lantibiotic resistance-associated response regulator and is part of the nisin resistance operon. It is a member of the NsrRK two-component system (TCS) that is involved in the regulation of lantibiotic resistance genes such as a membrane-associated lipoprotein of LanI, and the nsr gene cluster which encodes for the resistance protein NSR and the ABC transporter NsrFP, both conferring resistance against nisin. This subfamily also includes Staphylococcus epidermidis GraR, part of the GraR/GraS TCS involved in resistance against cationic antimicrobial peptides, and Bacillus subtilis BceR, part of the BceS/BceR TCS involved in the regulation of bacitracin resistance. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 53.05  E-value: 6.17e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1788192   43 DLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVSSLTGKGSEVtlRALELGAIDFVTKP 108
Cdd:cd18159  36 EEFLQFKPDLVLLDINLPYFDGFYWCREIRQISNVPIIFISSRDDNMDQV--MAINMGGDDYITKP 99
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
5-108 6.58e-09

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and similar domains; Thermotoga maritima RR468 (encoded by gene TM0468) is the cognate response regulator (RR) of the class I histidine kinase HK853 (product of gene TM0853). HK853/RR468 comprise a two-component system (TCS) that couples environmental stimuli to adaptive responses. This subfamily also includes Fremyella diplosiphon complementary adaptation response regulator homolog RcaF, a small RR that is involved in four-step phosphorelays of the complementary chromatic adaptation (CCA) system that occurs in many cyanobacteria. Both RR468 and RcaF are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 53.32  E-value: 6.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    5 RVLSVDDSALMRQIMTEIINSHSDMEmVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLM---RLRPMPVVM 81
Cdd:cd17552   3 RILVIDDEEDIREVVQACLEKLAGWE-VLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQanpETQSIPVIL 81
                        90       100
                ....*....|....*....|....*...
gi 1788192   82 vssLTGKGSEV-TLRALELGAIDFVTKP 108
Cdd:cd17552  82 ---LTAKAQPSdRQRFASLGVAGVIAKP 106
PRK10693 PRK10693
two-component system response regulator RssB;
35-108 7.64e-09

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 56.15  E-value: 7.64e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1788192    35 APDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKL-MRLRPMPVVMVSSlTGKGSEVTlRALELGAIDFVTKP 108
Cdd:PRK10693   3 AANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLrNRGDQTPVLVISA-TENMADIA-KALRLGVQDVLLKP 75
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
1-108 7.85e-09

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 55.58  E-value: 7.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     1 MSKIrvLSVDDSALMRQIMTEIInshsDME--MVATAPDPLVARDLIKKfNPDVLTLDVEMPRMDGLDFLEKLMRLRPMP 78
Cdd:PRK10955   1 MNKI--LLVDDDRELTSLLKELL----EMEgfNVIVAHDGEQALDLLDD-SIDLLLLDVMMPKKNGIDTLKELRQTHQTP 73
                         90       100       110
                 ....*....|....*....|....*....|.
gi 1788192    79 VVMvssLTGKGSEV-TLRALELGAIDFVTKP 108
Cdd:PRK10955  74 VIM---LTARGSELdRVLGLELGADDYLPKP 101
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
6-108 1.11e-08

phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex aeolicus and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include Aquifex aeolicus NtrC1 and Vibrio quorum-sensing signal integrator LuxO. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 52.59  E-value: 1.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMTEIINS-HSDMEMVATAPDplvARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVss 84
Cdd:cd17572   1 VLLVEDSPSLAALYQEYLSDeGYKVTHVETGKE---ALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIV-- 75
                        90       100
                ....*....|....*....|....*
gi 1788192   85 LTGKGS-EVTLRALELGAIDFVTKP 108
Cdd:cd17572  76 ITAHGSvDIAVEAMRLGAYDFLEKP 100
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
5-108 1.60e-08

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 55.62  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     5 RVLSVDDSALMRQIMTEIINSHSdmEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP-MPVVMVS 83
Cdd:PRK11361   6 RILIVDDEDNVRRMLSTAFALQG--FETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETrTPVILMT 83
                         90       100
                 ....*....|....*....|....*
gi 1788192    84 SLTgkGSEVTLRALELGAIDFVTKP 108
Cdd:PRK11361  84 AYA--EVETAVEALRCGAFDYVIKP 106
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
5-151 1.62e-08

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 54.34  E-value: 1.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     5 RVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARdlIKKFNPDVLTLDVEMPRMDGLDFLEKLMR---LRPMPVVM 81
Cdd:PRK10161   4 RILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQ--LNEPWPDLILLDWMLPGGSGIQFIKHLKResmTRDIPVVM 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1788192    82 vssLTGKGSEVT-LRALELGAIDFVTKP------QLGIREGMLAYNEMIAEKVRTAAKASL--AAHKPLSAPTTLKAGP 151
Cdd:PRK10161  82 ---LTARGEEEDrVRGLETGADDYITKPfspkelVARIKAVMRRISPMAVEEVIEMQGLSLdpTSHRVMAGEEPLEMGP 157
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
6-108 1.64e-08

pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response regulators (PRRs), also called APRRs, comprise a core group of clock components that controls the pace of the central oscillator of the circadian clock, an endogenous time-keeping mechanism that enables organisms to adapt to external daily cycles. The coordinated sequential expression of PRR9 (APRR9), PRR7 (APRR7), PRR5 (APRR5), PRR3 (APRR3), and PRR1 (APRR1) results in circadian waves that may be at the basis of the endogenous circadian clock. PRRs contain an N-terminal pseudo receiver (psREC) domain that resembles the receiver domain of a two-component response regulator, but lacks an aspartate residue that accepts a phosphoryl group from the sensor kinase, and a CCT motif at the C-terminus that contains a putative nuclear localization signal. The psREC domain is involved in protein-protein interactions.


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 51.63  E-value: 1.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMTEIINSHSdmEMVATAPDPLVARDLIK--KFNPDVLTLDVEMPRMDGLDFLEKLMR---LRPMPVV 80
Cdd:cd17582   1 VLLVENDDSTRQIVTALLRKCS--YEVTAASDGLQAWDVLEdeQNEIDLILTEVDLPVSSGFKLLSYIMRhkiCKNIPVI 78
                        90       100
                ....*....|....*....|....*...
gi 1788192   81 MVSSLTGKGseVTLRALELGAIDFVTKP 108
Cdd:cd17582  79 MMSSQDSVG--VVFKCLSKGAADYLVKP 104
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
6-108 2.18e-08

phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a component of the KdpD/KdpE two-component system (TCS) and is activated when histidine kinase KdpD senses a drop in external K+ concentration or upshift in ionic osmolarity, resulting in the expression of a heterooligomeric transporter KdpFABC. In addition, the KdpD/KdpE TCS is also an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. KdpE is a member of the OmpR family of DNA-binding response regulators that contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 51.40  E-value: 2.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMTEIINSHSdmEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVSSL 85
Cdd:cd17620   1 ILVIEDEPQIRRFLRTALEAHG--YRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWSAVPVIVLSAR 78
                        90       100
                ....*....|....*....|...
gi 1788192   86 TGKGSEVtlRALELGAIDFVTKP 108
Cdd:cd17620  79 DEESDKI--AALDAGADDYLTKP 99
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
5-108 2.37e-08

phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; Klebsiella pneumoniae RstA (kpRstA) is part of the RstA/RstB two-component regulatory system that may play a regulatory role in virulence. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 51.61  E-value: 2.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    5 RVLSVDDSALMRQIMTEIINSHsDMEmVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVSS 84
Cdd:cd17622   2 RILLVEDDPKLARLIADFLESH-GFN-VVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQGPILLLTA 79
                        90       100
                ....*....|....*....|....*
gi 1788192   85 LtgkGSEVT-LRALELGAIDFVTKP 108
Cdd:cd17622  80 L---DSDIDhILGLELGADDYVVKP 101
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
5-108 2.84e-08

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 51.39  E-value: 2.84e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    5 RVLSVDDSALMRQIMTEIINSHSdmEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLM---RLRPMPVVM 81
Cdd:cd17548   1 KILIVEDNPLNMKLARDLLESAG--YEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKedpATRDIPVIA 78
                        90       100
                ....*....|....*....|....*..
gi 1788192   82 VSSLTGKGSEVtlRALELGAIDFVTKP 108
Cdd:cd17548  79 LTAYAMKGDRE--KILEAGCDGYISKP 103
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
32-108 2.92e-08

phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The Mycobacterium tuberculosis PrrA is part of the PrrA/PrrB two-component system (TCS) that has been implicated in early intracellular multiplication and is essential for viability. Also included in this subfamily is Mycobacterium tuberculosis MprA, part of the MprAB TCS that regulates EspR, a key regulator of the ESX-1 secretion system, and is required for establishment and maintenance of persistent infection in a tissue- and stage-specific fashion. PrrA and MprA belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 51.23  E-value: 2.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192   32 VATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGldfLEKLMRLRPM----PVVMVSSLTGKGSEVTlrALELGAIDFVTK 107
Cdd:cd17627  25 VETAVDGAEALRVISGNRPDAVVLDVMMPRLDG---LEVCRRLRAAgndlPILVLTARDSVSDRVA--GLDAGADDYLVK 99

                .
gi 1788192  108 P 108
Cdd:cd17627 100 P 100
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
5-108 3.05e-08

phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is part of MtrA/MtrB (or MtrAB), a highly conserved two-component system (TCS) implicated in the regulation of cell division in the actinobacteria. In unicellular Mycobacterium tuberculosis, MtrAB coordinates DNA replication with cell division and regulates the transcription of resuscitation-promoting factor B. In filamentous Streptomyces venezuelae, it links antibiotic production to sporulation. MtrA belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 51.32  E-value: 3.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    5 RVLSVDDSALMRQIMTEIInsHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMvss 84
Cdd:cd17626   2 RILVVDDDAALAEMIGIVL--RGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAESGVPIVM--- 76
                        90       100
                ....*....|....*....|....*
gi 1788192   85 LTGKGSEV-TLRALELGAIDFVTKP 108
Cdd:cd17626  77 LTAKSDTVdVVLGLESGADDYVAKP 101
fixJ PRK09390
response regulator FixJ; Provisional
1-139 4.98e-08

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 52.70  E-value: 4.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     1 MSKIRVLSVDDSALMRQIMTEIINShSDMEMV--ATAPDPLvarDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLR-PM 77
Cdd:PRK09390   1 SDKGVVHVVDDDEAMRDSLAFLLDS-AGFEVRlfESAQAFL---DALPGLRFGCVVTDVRMPGIDGIELLRRLKARGsPL 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1788192    78 PVVMvssLTGKGsEVTL--RALELGAIDFVTKPqlgiregmlAYNEMIAEKVRTAAKASLAAHK 139
Cdd:PRK09390  77 PVIV---MTGHG-DVPLavEAMKLGAVDFIEKP---------FEDERLIGAIERALAQAPEAAK 127
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
31-108 8.81e-08

phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; Escherichia coli CusR is part of the CusS/CusR two-component system (TCS) that is involved in response to copper and silver. Other members of this subfamily include Escherichia coli PcoR, Pseudomonas syringae CopR, and Streptomyces coelicolor CutR, which are all transcriptional regulatory proteins and components of TCSs that regulate genes involved in copper resistance and/or metabolism. member of the subfamily is Escherichia coli HprR (hydrogen peroxide response regulator), previously called YdeW, which is part of the HprSR (or YedVW) TCS involved in stress response to hydrogen peroxide, as well as Cupriavidus metallidurans CzcR, which is part of the CzcS/CzcR TCS involved in the control of cobalt, zinc, and cadmium homeostasis. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 49.36  E-value: 8.81e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192   31 MVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRL-RPMPVVMvssLTGKGS-EVTLRALELGAIDFVTKP 108
Cdd:cd19935  24 AVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAgKQTPVLM---LTARDSvEDRVKGLDLGADDYLVKP 100
PRK15479 PRK15479
transcriptional regulator TctD;
32-108 1.40e-07

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 51.65  E-value: 1.40e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1788192    32 VATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKL-MRLRPMPVVMVSSLTGKGSEVtlRALELGAIDFVTKP 108
Cdd:PRK15479  27 VDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLrKRGQTLPVLLLTARSAVADRV--KGLNVGADDYLPKP 102
PRK13856 PRK13856
two-component response regulator VirG; Provisional
6-114 1.42e-07

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 51.74  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     6 VLSVDDSALMRQIMTEIINSHSdmEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVSSL 85
Cdd:PRK13856   4 VLVIDDDVAMRHLIVEYLTIHA--FKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSLATKSDVPIIIISGD 81
                         90       100
                 ....*....|....*....|....*....
gi 1788192    86 TGKGSEVTLrALELGAIDFVTKPqLGIRE 114
Cdd:PRK13856  82 RLEEADKVV-ALELGATDFIAKP-FGTRE 108
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
5-108 1.71e-07

phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone response regulator containing only a REC domain with no output/effector domain, controls sporulation in Bacillus subtilis through the exchange of a phosphoryl group. Bacillus subtilis forms spores when conditions for growth become unfavorable. The initiation of sporulation is controlled by a phosphorelay (an expanded version of the two-component system) that consists of four main components: a histidine kinase (KinA), a secondary messenger (Spo0F), a phosphotransferase (Spo0B), and a transcription factor (Spo0A). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 49.09  E-value: 1.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    5 RVLSVDDSALMRQIMTEIINSHSDMEMvaTAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVSS 84
Cdd:cd17553   2 KILIVDDQYGIRILLNEVFNKEGYQTF--QAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMT 79
                        90       100
                ....*....|....*....|....
gi 1788192   85 LTGKgSEVTLRALELGAIDFVTKP 108
Cdd:cd17553  80 AYGE-LDMIQESKELGALTHFAKP 102
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
4-60 2.18e-07

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 47.18  E-value: 2.18e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1788192       4 IRVLSVDDSALMRQIMTEIINSHSDMemVATAPDPLVARDLIKKFNPDVLTLDVEMP 60
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYE--VDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
10-108 2.74e-07

phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; Escherichia coli PhoP (EcPhoP) is part of the PhoQ/PhoP two-component system (TCS) that regulates virulence genes and plays an essential role in the response of the bacteria to the environment of their mammalian hosts, sensing several stimuli such as extracellular magnesium limitation, low pH, the presence of cationic antimicrobial peptides, and osmotic upshift. This subfamily also includes Brucella suis FeuP, part of the FeuPQ TCS that is involved in the regulation of iron uptake, and Microchaete diplosiphon RcaC, which is required for chromatic adaptation. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 48.82  E-value: 2.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192   10 DDSALMRQIMTEIINSHSDMEMVATAPDplvARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRL-RPMPVVMvssLTGK 88
Cdd:cd19934   6 DDALLAAQLKEQLSDAGYVVDVAEDGEE---ALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEgRATPVLI---LTAR 79
                        90       100
                ....*....|....*....|.
gi 1788192   89 GSEV-TLRALELGAIDFVTKP 108
Cdd:cd19934  80 DSWQdKVEGLDAGADDYLTKP 100
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
6-71 3.15e-07

phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate/nitrite response regulator protein NarL contains an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. Escherichia coli NarL activates the expression of the nitrate reductase (narGHJI) and formate dehydrogenase-N (fdnGHI) operons, and represses the transcription of the fumarate reductase (frdABCD) operon in response to a nitrate/nitrite induction signal. Phosphorylation of the NarL REC domain releases the C-terminal HTH output domain that subsequently binds specific DNA promoter sites to repress or activate gene expression. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 48.50  E-value: 3.15e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1788192    6 VLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKL 71
Cdd:cd19931   1 VLLIDDHPLLRKGIKQLIELDPDFTVVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKAL 66
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
43-108 3.55e-07

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 50.45  E-value: 3.55e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1788192    43 DLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVsslTGKGSEVT-LRALELGAIDFVTKP 108
Cdd:PRK10710  48 PYVRQTPPDLILLDLMLPGTDGLTLCREIRRFSDIPIVMV---TAKIEEIDrLLGLEIGADDYICKP 111
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
5-108 3.66e-07

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 48.45  E-value: 3.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    5 RVLSVDDSALMRQiMTEIINSHSDMEmVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLmRLRP----MPVV 80
Cdd:cd17562   2 KILAVDDSASIRQ-MVSFTLRGAGYE-VVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKEL-RKLPaykfTPIL 78
                        90       100
                ....*....|....*....|....*...
gi 1788192   81 MVSslTGKGSEVTLRALELGAIDFVTKP 108
Cdd:cd17562  79 MLT--TESSDEKKQEGKAAGATGWLVKP 104
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
6-108 4.24e-07

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 47.84  E-value: 4.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMTEIINSHSdmEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVSSL 85
Cdd:cd17580   1 ILVVDDNEDAAEMLALLLELEG--AEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIAL 78
                        90       100
                ....*....|....*....|....
gi 1788192   86 TGKG-SEVTLRALELGAIDFVTKP 108
Cdd:cd17580  79 TGYGqPEDRERALEAGFDAHLVKP 102
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
43-108 6.41e-07

phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is part of the CckA-ChpT-CtrA phosphorelay that is conserved in alphaproteobacteria and is important in orchestrating the cell cycle, polar development, and flagellar biogenesis. CtrA is the master regulator of flagella synthesis genes and also regulates genes involved in the cell cycle, exopolysaccharide synthesis, and cyclic-di-GMP signaling. CtrA is active as a transcription factor when phosphorylated. It is a member of the OmpR family of DNA-binding response regulators, characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 47.40  E-value: 6.41e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1788192   43 DLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLR-PMPVVMVSSLTGKGSEVtlRALELGAIDFVTKP 108
Cdd:cd17616  36 DLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKvKTPILILSGLADIEDKV--KGLGFGADDYMTKP 100
PRK15369 PRK15369
two component system response regulator;
1-109 9.16e-07

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 48.92  E-value: 9.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     1 MSKIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLmrLRPMPVV 80
Cdd:PRK15369   1 MKNYKILLVDDHELIINGIKNMLAPYPRYKIVGQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQL--HQRWPAM 78
                         90       100       110
                 ....*....|....*....|....*....|..
gi 1788192    81 MVSSLTGKGSE-VTLRALELGAIDFVTK--PQ 109
Cdd:PRK15369  79 NILVLTARQEEhMASRTLAAGALGYVLKksPQ 110
PRK10610 PRK10610
chemotaxis protein CheY;
4-108 9.54e-07

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 47.28  E-value: 9.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     4 IRVLSVDDSALMRQIMTEIINSHSdMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLeKLMR----LRPMPV 79
Cdd:PRK10610   6 LKFLVVDDFSTMRRIVRNLLKELG-FNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELL-KTIRadgaMSALPV 83
                         90       100
                 ....*....|....*....|....*....
gi 1788192    80 VMVSSLTGKgsEVTLRALELGAIDFVTKP 108
Cdd:PRK10610  84 LMVTAEAKK--ENIIAAAQAGASGYVVKP 110
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
32-108 1.01e-06

phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 46.60  E-value: 1.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192   32 VATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKL---MRLRPMPVVMvssLTGKGS-EVTLRALELGAIDFVTK 107
Cdd:cd19927  25 VIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLrknADFDTIPVIF---LTAKGMtSDRIKGYNAGCDGYLSK 101

                .
gi 1788192  108 P 108
Cdd:cd19927 102 P 102
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
5-114 1.07e-06

phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; This subfamily includes Escherichia coli TorR and ArcA, both OmpR family response regulators that mediate adaptation to changes in various respiratory growth conditions. The TorS-TorR two-component system (TCS) is responsible for the tight regulation of the torCAD operon, which encodes the trimethylamine N-oxide (TMAO) reductase respiratory system in response to anaerobic conditions and the presence of TMAO. The ArcA-ArcB TCS is involved in cell growth during anaerobiosis. ArcA is a global regulator that controls more than 30 operons involved in redox regulation (the Arc modulon). OmpR family DNA-binding response regulators are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 47.00  E-value: 1.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    5 RVLSVDDSALMRQIMTEIINShsDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVss 84
Cdd:cd17619   2 HILIVEDEPVTRATLKSYFEQ--EGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSEVGIILV-- 77
                        90       100       110
                ....*....|....*....|....*....|.
gi 1788192   85 lTGKGSEV-TLRALELGAIDFVTKPqLGIRE 114
Cdd:cd17619  78 -TGRDDEVdRIVGLEIGADDYVTKP-FNPRE 106
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
5-73 1.60e-06

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 48.31  E-value: 1.60e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1788192     5 RVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMR 73
Cdd:PRK10403   8 QVLIVDDHPLMRRGVRQLLELDPGFEVVAEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRR 76
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
32-108 1.68e-06

phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is a member of the SenX3-RegX3 two-component system that is involved in phosphate-sensing signal transduction. Phosphorylated RegX3 functions as a transcriptional activator of phoA. It induces transcription in phosphate limiting environment and also controls expression of several critical metabolic enzymes in aerobic condition. RegX3 belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 46.04  E-value: 1.68e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1788192   32 VATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVsslTGKGSEV-TLRALELGAIDFVTKP 108
Cdd:cd17621  25 VTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARSNVPVIMV---TAKDSEIdKVVGLELGADDYVTKP 99
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
50-140 1.81e-06

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 48.26  E-value: 1.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    50 PDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVSSLTGKGSEVTlrALELGAIDFVTKPqLGIREgMLAynemiaeKVRT 129
Cdd:PRK10529  46 PDLIILDLGLPDGDGIEFIRDLRQWSAIPVIVLSARSEESDKIA--ALDAGADDYLSKP-FGIGE-LQA-------RLRV 114
                         90
                 ....*....|.
gi 1788192   130 AAKASLAAHKP 140
Cdd:PRK10529 115 ALRRHSATPAP 125
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
4-108 1.89e-06

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains; This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 46.24  E-value: 1.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    4 IRVLSVDD-----SALMRQIMTEIINshsdmemVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMP 78
Cdd:cd17569   1 PTILLVDDepnilKALKRLLRREGYE-------VLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDT 73
                        90       100       110
                ....*....|....*....|....*....|..
gi 1788192   79 VVMVssLTGKGS-EVTLRALELGAID-FVTKP 108
Cdd:cd17569  74 VRIL--LTGYADlDAAIEAINEGEIYrFLTKP 103
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
3-83 1.93e-06

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 48.10  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     3 KIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLmRLRPMP--VV 80
Cdd:PRK10651   6 PATILLIDDHPMLRTGVKQLISMAPDITVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKL-REKSLSgrIV 84

                 ...
gi 1788192    81 MVS 83
Cdd:PRK10651  85 VFS 87
ompR PRK09468
osmolarity response regulator; Provisional
5-108 2.32e-06

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 48.05  E-value: 2.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     5 RVLSVDDSA----LMRQIMTE---IINSHSDMEMVatapDPLVARDLIkkfnpDVLTLDVEMPRMDGLDFLEklmRLR-- 75
Cdd:PRK09468   7 KILVVDDDMrlraLLERYLTEqgfQVRSAANAEQM----DRLLTRESF-----HLMVLDLMLPGEDGLSICR---RLRsq 74
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 1788192    76 --PMPVVMvssLTGKGSEVT-LRALELGAIDFVTKP 108
Cdd:PRK09468  75 nnPTPIIM---LTAKGEEVDrIVGLEIGADDYLPKP 107
PLN03029 PLN03029
type-a response regulator protein; Provisional
2-108 2.83e-06

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 47.72  E-value: 2.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     2 SKIRVLSVDDSALMRQIMTEIINSHSDM-----------------EMVATAPD-PLVARDLIKKFNPDVLTLDVEMPRMD 63
Cdd:PLN03029   7 SQFHVLAVDDSLIDRKLIEKLLKTSSYQvttvdsgskalkflglhEDDRSNPDtPSVSPNSHQEVEVNLIITDYCMPGMT 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 1788192    64 GLDFLEKLMR---LRPMPVVMVSSlTGKGSEVTlRALELGAIDFVTKP 108
Cdd:PLN03029  87 GYDLLKKIKEsssLRNIPVVIMSS-ENVPSRIT-RCLEEGAEEFFLKP 132
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
51-108 3.20e-06

phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 45.67  E-value: 3.20e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 1788192   51 DVLTLDVEMPRMDGLDFLEKLMRLRPM-PVVMVSSLTGKGSEVtlRALELGAIDFVTKP 108
Cdd:cd17625  43 DLIILDIMLPGMDGLEVLKSLREEGIEtPVLLLTALDAVEDRV--KGLDLGADDYLPKP 99
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
5-108 3.67e-06

phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; Acinetobacter baumannii BfmR is part of the BfmR/S two-component system that functions as the master regulator of biofilm initiation. BfmR confers resistance to complement-mediated bactericidal activity, independent of capsular polysaccharide, and also increases resistance to the clinically important antimicrobials meropenem and colistin, making it a potential antimicrobial target. Its inhibition would have the dual benefit of significantly decreasing in vivo survival and increasing sensitivity to selected antimicrobials. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 45.44  E-value: 3.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    5 RVLSVDDSALMRQIMTEIInSHSDMEmVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMvss 84
Cdd:cd19939   1 RILIVEDELELARLTRDYL-IKAGLE-VSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHSHVPILM--- 75
                        90       100
                ....*....|....*....|....*
gi 1788192   85 LTGKGSEV-TLRALELGAIDFVTKP 108
Cdd:cd19939  76 LTARTEEMdRVLGLEMGADDYLCKP 100
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
41-108 5.86e-06

phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; DNA-binding transcriptional regulator NtrC is also called nitrogen regulation protein NR(I) or nitrogen regulator I (NRI). It contains an N-terminal receiver (REC) domain, followed by a sigma-54 interaction domain, and a C-terminal helix-turn-helix DNA-binding domain. It is part of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. DNA-binding response regulator NtrC is phosphorylated by NtrB; phosphorylation of the N-terminal REC domain activates the central sigma-54 interaction domain and leads to the transcriptional activation from promoters that require sigma(54)-containing RNA polymerase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 44.96  E-value: 5.86e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1788192   41 ARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPM-PVVMVSSLTGKGSEVTlrALELGAIDFVTKP 108
Cdd:cd19919  36 ALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDlPVIIMTAHSDLDSAVS--AYQGGAFEYLPKP 102
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
41-108 6.47e-06

phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 44.78  E-value: 6.47e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192   41 ARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPM-PVVMvssLTGK-GSEVTLRALELGAIDFVTKP 108
Cdd:cd17624  34 AEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSlPVLI---LTARdGVDDRVAGLDAGADDYLVKP 100
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
4-108 8.55e-06

phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; This groups includes a modulated diguanylate cyclase containing a PAS sensor domain from Desulfovibrio desulfuricans G20. Members of this group contain N-terminal REC domains and various output domains including the GGDEF, histidine kinase, and helix-turn-helix (HTH) DNA binding domains. Also included in this family is Mycobacterium tuberculosis PdtaR, a transcriptional antiterminator that contains a REC domain and an ANTAR RNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 44.32  E-value: 8.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    4 IRVLSVDDSALMRQIMTEIINS--HSDMEMVATAPDplvARDLIKKFNPDVLTLDVEMP-RMDGLDFLEKLMRLRPMPVV 80
Cdd:cd17534   1 KKILIVEDEAIIALDLKEILESlgYEVVGIADSGEE---AIELAEENKPDLILMDINLKgDMDGIEAAREIREKFDIPVI 77
                        90       100
                ....*....|....*....|....*....
gi 1788192   81 MVSSLTgkgSEVTL-RALELGAIDFVTKP 108
Cdd:cd17534  78 FLTAYS---DEETLeRAKETNPYGYLVKP 103
dpiA PRK10046
two-component response regulator DpiA; Provisional
4-126 9.15e-06

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 46.16  E-value: 9.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     4 IRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRpMPVVMVS 83
Cdd:PRK10046   5 LTLLIVEDETPLAEMHAEYIRHIPGFSQILLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELVQAH-YPGDVVF 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 1788192    84 SLTGKGSEVTLRALELGAIDFVTKP----QLG-------IREGMLAYNEMIAEK 126
Cdd:PRK10046  84 TTAASDMETVSEAVRCGVFDYLIKPiayeRLGqtltrfrQRKHMLESIDSASQK 137
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
50-108 9.54e-06

phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is part of the BaeSR two-component system that is involved in regulating genes that confer multidrug and metal resistance. In Salmonella, BaeSR induces AcrD and MdtABC drug efflux systems, increasing multidrug and metal resistance. In Escherichia coli, BaeR stimulates multidrug resistance via mdtABC (multidrug transporter ABC, formerly known as yegMNO) genes, which encode a resistance-nodulation-cell division (RND) drug efflux system. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 44.29  E-value: 9.54e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192   50 PDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMvssLTGKGSEVT-LRALELGAIDFVTKP 108
Cdd:cd19938  44 PDLILLDLMLPGTDGLTLCREIRRFSDVPIIM---VTARVEEIDrLLGLELGADDYICKP 100
PRK10430 PRK10430
two-component system response regulator DcuR;
4-108 1.33e-05

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 45.87  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     4 IRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIkkFNP----DVLTLDVEMPRMDGLDFLEKLMRL-RPMP 78
Cdd:PRK10430   2 INVLIVDDDAMVAELNRRYVAQIPGFQCCGTASTLEQAKEII--FNSdtpiDLILLDIYMQQENGLDLLPVLHEAgCKSD 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 1788192    79 VVMVSSltgkGSEVTL--RALELGAIDFVTKP 108
Cdd:PRK10430  80 VIVISS----AADAATikDSLHYGVVDYLIKP 107
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
6-108 4.37e-05

phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and similar proteins; Type-A response regulators of Arabidopsis (ARRs) are involved in cytokinin signaling, which involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Type-A ARRs function downstream of and are regulated by type-B ARRs, which are a class of MYB-type transcription factors. As primary cytokinin response genes, type-A ARRs act as redundant negative feedback regulators of cytokinin signaling by inactivating the phosphorelay. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-A ARRs are similar in domain structure to CheY, in that they lack a typical output domain and only contain a stand-alone receiver (REC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 42.35  E-value: 4.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMTEIINSHS----DMEMVATAPDPLVARDLIKKFNPDVLTL-----DVEMPRMDGLDFLEK---LMR 73
Cdd:cd17581   1 VLAVDDSLVDRKVIERLLRISScrvtAVDSGKRALEFLGLEDEEDSSNFNEPKVnmiitDYCMPGMTGYDLLKKvkeSSA 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 1788192   74 LRPMPVVMVSSltGKGSEVTLRALELGAIDFVTKP 108
Cdd:cd17581  81 LKEIPVVIMSS--ENIPTRISRCLEEGAEDFLLKP 113
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
3-184 9.33e-05

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 43.87  E-value: 9.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     3 KIRVLSVDDSALMRQIMTEIINSHSdmEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP-MPVVM 81
Cdd:PRK10365   5 NIDILVVDDDISHCTILQALLRGWG--YNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPaIPVLI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    82 VSSLTGKGSEVtlRALELGAIDFVTKPqlgiregmLAYNEMIAEKVRTAAKASLAAHKPlsapttlkagPLLSSEKLIAI 161
Cdd:PRK10365  83 MTAYSSVETAV--EALKTGALDYLIKP--------LDFDNLQATLEKALAHTHSIDAET----------PAVTASQFGMV 142
                        170       180
                 ....*....|....*....|...
gi 1788192   162 GASTggteAIRHVLQPLPLSSPA 184
Cdd:PRK10365 143 GKSP----AMQHLLSEIALVAPS 161
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
50-147 9.63e-05

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 43.03  E-value: 9.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    50 PDVLTLDVEMPRMDGLDFLEKLMRLRP-MPVVMvssLTGKGSEVT-LRALELGAIDFVTKPqLGIREgmlaynemIAEKV 127
Cdd:PRK11083  48 PDLVILDVGLPDISGFELCRQLLAFHPaLPVIF---LTARSDEVDrLVGLEIGADDYVAKP-FSPRE--------VAARV 115
                         90       100
                 ....*....|....*....|....
gi 1788192   128 RT----AAKASLAAHKPLSAPTTL 147
Cdd:PRK11083 116 RTilrrVKKFAAPSPVIRIGHFEL 139
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
4-128 1.06e-04

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 44.19  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     4 IRVLSVDDSALMRQIMTEIINSHSdmEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRL-RPMPVVMV 82
Cdd:PRK10841 802 MMILVVDDHPINRRLLADQLGSLG--YQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLgLTLPVIGV 879
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 1788192    83 S--SLtgkgSEVTLRALELGAIDFVTKP-QLGIREGMLAYnemIAEKVR 128
Cdd:PRK10841 880 TanAL----AEEKQRCLEAGMDSCLSKPvTLDVLKQTLTV---YAERVR 921
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
1-108 2.06e-04

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 42.94  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     1 MSKIRVLSVDDSALMRQIMTEIInSHSDMEMVATAPDPLVARDLIKKfNPDVLTLDVEMPRMDGLDFLEKLMRLRPM-PV 79
Cdd:PRK10923   1 MQRGIVWVVDDDSSIRWVLERAL-AGAGLTCTTFENGNEVLEALASK-TPDVLLSDIRMPGMDGLALLKQIKQRHPMlPV 78
                         90       100
                 ....*....|....*....|....*....
gi 1788192    80 VMVSSLTGKGSEVTlrALELGAIDFVTKP 108
Cdd:PRK10923  79 IIMTAHSDLDAAVS--AYQQGAFDYLPKP 105
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
5-108 2.26e-04

phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 40.50  E-value: 2.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    5 RVLSVDDSALMRQIMTEIINSHSDMEmVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLR-PMPVVMVS 83
Cdd:cd17530   2 RVLVLDDDPFQCMMAATILEDLGPGN-VDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHsNAAVILMS 80
                        90       100
                ....*....|....*....|....*...
gi 1788192   84 SLTG---KGSEVTLRALELGAIDFVTKP 108
Cdd:cd17530  81 GLDGgilESAETLAGANGLNLLGTLSKP 108
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
9-124 2.54e-04

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 41.80  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     9 VDDSALMRQIMTEIINSHsDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVSS---- 84
Cdd:PRK09958   6 IDDHPLAIAAIRNLLIKN-DIEILAELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIVSaknd 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 1788192    85 -LTGKgsevtlRALELGAIDFVTKpqlgiREGMlayNEMIA 124
Cdd:PRK09958  85 hFYGK------HCADAGANGFVSK-----KEGM---NNIIA 111
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
5-108 4.12e-04

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of this subfamily are response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It belongs to the nitrogen regulatory protein C (NtrC) family of response regulators, which activate transcription by RNA polymerase (RNAP) in response to a change in the environment. HupR is an unusual member of this family as it activates transcription when unphosphorylated, and transcription is inhibited by phosphorylation. Proteins in this subfamily contain an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 40.04  E-value: 4.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    5 RVLSVDDSALMRQIMTEIINSHSDmemVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVss 84
Cdd:cd17596   2 TILVVDDEVRSLEALRRTLEEDFD---VLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRII-- 76
                        90       100
                ....*....|....*....|....*.
gi 1788192   85 LTG-KGSEVTLRALELGAI-DFVTKP 108
Cdd:cd17596  77 ISGyTDSEDIIAGINEAGIyQYLTKP 102
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
6-129 5.83e-04

REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a pseudo receiver (psREC)-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the REC-like adaptor domain D2 of PleD, which is an inactive domain.


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 39.22  E-value: 5.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMTEIINSHSDMEmVATAPDPLVARDLIKKFNPDVLTLDVEmpRMDGLDF---LEKLMRLRPMPVVMV 82
Cdd:cd17539   1 VLLVDDRPSSAERIAAMLSSEHEVV-VEADPDEALFRAAEGPFDLVIVSLALE--DFDGLRLcsqLRSLERTRQLPILAV 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 1788192   83 SSLTGKGSevTLRALELGAIDFVTKPqlgiregmLAYNEMIAeKVRT 129
Cdd:cd17539  78 ADPGDRGR--LIRALEIGVNDYLVRP--------IDPNELLA-RVRT 113
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
4-107 6.62e-04

phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The GGDEF response regulator WspR is part of the Wsp system that is homologous to chemotaxis systems and also includes the membrane-bound receptor protein WspA. In response to growth on surfaces, WspR is phosphorylated by the Wsp signal transduction complex and is activated, functioning as a diguanylate cyclase (DGC) that catalyzes c-di-GMP synthesis. WspR is a hybrid response regulator-diguanylate cyclase, containing an N-terminal REC domain and a C-terminal GGDEF domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 39.31  E-value: 6.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    4 IRVLSVDDSALMRQIMTEIINSHSDMEMVATApDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLeKLMRLRP----MPV 79
Cdd:cd17575   1 IMVLLVDDQAIIGEAVRRALADEEDIDFHYCS-DPTEAIEVASQIKPTVILQDLVMPGVDGLTLV-RFFRANPatrdIPI 78
                        90       100
                ....*....|....*....|....*...
gi 1788192   80 VMVSslTGKGSEVTLRALELGAIDFVTK 107
Cdd:cd17575  79 IVLS--TKEEPEVKSEAFALGANDYLVK 104
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
1-107 7.98e-04

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 40.39  E-value: 7.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     1 MSKIrvLSVDDSALMRQIMTEIINSHsDMEmVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLdfleKLMR-LRPM-- 77
Cdd:PRK10701   1 MNKI--VFVEDDAEVGSLIAAYLAKH-DID-VTVEPRGDRAEATILREQPDLVLLDIMLPGKDGM----TICRdLRPKwq 72
                         90       100       110
                 ....*....|....*....|....*....|.
gi 1788192    78 -PVVMVSSLTGKGSEVTlrALELGAIDFVTK 107
Cdd:PRK10701  73 gPIVLLTSLDSDMNHIL--ALEMGACDYILK 101
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
51-129 9.58e-04

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 40.29  E-value: 9.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    51 DVLTLDVEMPRMDGLDFLEKLMRL-RPMPVVMVSSLtgkGS-EVTLRALELGAIDFVTKPqlgiregmLAYNEMIAeKVR 128
Cdd:PRK09836  46 DLIILDIMLPDVNGWDIVRMLRSAnKGMPILLLTAL---GTiEHRVKGLELGADDYLVKP--------FAFAELLA-RVR 113

                 .
gi 1788192   129 T 129
Cdd:PRK09836 114 T 114
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
1-107 1.35e-03

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 39.47  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     1 MSKIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP-MPV 79
Cdd:PRK09935   1 MKPASVIIMDTHPIIRMSIEVLLQKNSELQIVLKTDDYRITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQStVKV 80
                         90       100
                 ....*....|....*....|....*...
gi 1788192    80 VMVSSLTgkGSEVTLRALELGAIDFVTK 107
Cdd:PRK09935  81 LFLSSKS--ECFYAGRAIQAGANGFVSK 106
PRK09483 PRK09483
response regulator; Provisional
4-107 1.70e-03

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 39.32  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     4 IRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP-MPVVMV 82
Cdd:PRK09483   2 INVLLVDDHELVRAGIRRILEDIKGIKVVGEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKILRYTPdVKIIML 81
                         90       100
                 ....*....|....*....|....*
gi 1788192    83 SSLTgkGSEVTLRALELGAIDFVTK 107
Cdd:PRK09483  82 TVHT--ENPLPAKVMQAGAAGYLSK 104
REC_LytTR_AgrA-like cd17533
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; ...
4-109 2.41e-03

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AgrA-like group of LytTR/AlgR family response regulators are Staphylococcus aureus accessory gene regulator protein A (AgrA) and Streptococcus pneumoniae response regulator ComE, which are members of two-component regulatory systems. AgrA is a global regulator that controls the synthesis of virulence factors and other exoproteins. ComE is part of the ComD-ComE system that is part of a quorum-sensing signaling pathway that controls the development of competence, a physiological state required for genetic transformation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381088 [Multi-domain]  Cd Length: 131  Bit Score: 37.60  E-value: 2.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    4 IRVLSVDDSALMRQIMTEII-------NSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP 76
Cdd:cd17533   1 MNIFILEDDKIQRVRLEEIIenilkieNIEYVIELTGKTEELLEKIKERGKNGIYFLDIDIKMEEKNGLEVAQKIRKYDP 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 1788192   77 -MPVVMVSSLtgkgSEVTLRALE--LGAIDFVTKPQ 109
Cdd:cd17533  81 yAIIIFVTTH----SEFAPLTFEykVAALDFILKPL 112
PRK10816 PRK10816
two-component system response regulator PhoP;
4-108 2.73e-03

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 38.57  E-value: 2.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192     4 IRVLSVDDSALMRQIMTEIINshsDM-EMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEklmRLRP----MP 78
Cdd:PRK10816   1 MRVLVVEDNALLRHHLKVQLQ---DAgHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIR---RWRSndvsLP 74
                         90       100       110
                 ....*....|....*....|....*....|
gi 1788192    79 VVMVSSLTGKGSEVTlrALELGAIDFVTKP 108
Cdd:PRK10816  75 ILVLTARESWQDKVE--VLSAGADDYVTKP 102
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
6-108 3.35e-03

phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C (NtrC) and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include NtrC, also called nitrogen regulator I (NRI), from Rhodobacter capsulatus, Azospirillum brasilense, and Azorhizobium caulinodans. NtrC is part of the NtrB/NtrC two-component system that controls the expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 36.71  E-value: 3.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMTEIInSHSDMEMVATAPDPLVARdLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRP-MPVVMVSS 84
Cdd:cd19928   1 ILVADDDRAIRTVLTQAL-GRAGYEVRTTGNAATLWR-WVEEGEGDLVITDVVMPDENGLDLIPRIKKARPdLPIIVMSA 78
                        90       100
                ....*....|....*....|....
gi 1788192   85 LTGKGSEVtlRALELGAIDFVTKP 108
Cdd:cd19928  79 QNTLMTAV--KAAERGAFEYLPKP 100
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
6-108 4.92e-03

phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR and similar proteins; Pseudomonas aeruginosa PilR is the response regulator of the PilS/PilR two-component regulatory system (PilSR TCS) that acts in conjunction with sigma-54 to regulate the expression of type 4 pilus (T4P) major subunit PilA. In addition, the PilSR TCS regulates flagellum-dependent swimming motility and pilus-dependent twitching motility. PilR contains an N-terminal REC domain, a central sigma-54 interaction domain, and a C-terminal Fis-type helix-turn-helix DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 35.98  E-value: 4.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    6 VLSVDDSALMRQIMtEIINSHSDMEmVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKL-MRLRPMPVVMVss 84
Cdd:cd19926   1 VLVVDDEPDIRELL-EITLGRMGLD-VRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIqQRLPQTPVAVI-- 76
                        90       100
                ....*....|....*....|....*
gi 1788192   85 lTGKGS-EVTLRALELGAIDFVTKP 108
Cdd:cd19926  77 -TAYGSlDTAIEALKAGAFDFLTKP 100
PRK11517 PRK11517
DNA-binding response regulator HprR;
52-143 5.11e-03

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 37.96  E-value: 5.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1788192    52 VLTLDVEMPRMDGLDFLEKLMRLRPMPVVmvsSLTGKGS-EVTLRALELGAIDFVTKPqlgiregmLAYNEMIAeKVRta 130
Cdd:PRK11517  47 LIILDIMLPGMDGWQILQTLRTAKQTPVI---CLTARDSvDDRVRGLDSGANDYLVKP--------FSFSELLA-RVR-- 112
                         90
                 ....*....|...
gi 1788192   131 akASLAAHKPLSA 143
Cdd:PRK11517 113 --AQLRQHHALNS 123
 
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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