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Conserved domains on  [gi|494759980|ref|WP_007495388|]
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MULTISPECIES: chemotaxis response regulator protein-glutamate methylesterase [Flavonifractor]

Protein Classification

protein-glutamate methylesterase/protein-glutamine glutaminase( domain architecture ID 11479194)

protein-glutamate methylesterase/protein-glutamine glutaminase is part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli; it catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors by CheR and also mediates the irreversible deamidation of specific glutamine residues to glutamic acid

CATH:  3.40.50.180|3.40.50.2300
EC:  3.1.1.61|3.5.1.44
Gene Ontology:  GO:0050568|GO:0006935|GO:0006482|GO:0005737|GO:0000156|GO:0008984|GO:0018277
PubMed:  10966457|16176121|10049806|8218244|9760239|16740923
SCOP:  4003632

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
6-340 3.90e-135

chemotaxis-specific protein-glutamate methyltransferase CheB;


:

Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 388.35  E-value: 3.90e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   6 RKIRVLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVIL 85
Cdd:PRK00742   2 MKIRVLVVDDSAFMRRLISEILNSDPDIEVVGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRPTPVVM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  86 VSSLNLR----VFDALAAGAVDFVRKPDAVESR--ESFLQALTHKIIVASHARL----SRANLPHPAAPAAPLRFGGDGA 155
Cdd:PRK00742  82 VSSLTERgaeiTLRALELGAVDFVTKPFLGISLgmDEYKEELAEKVRAAARARVralpPRAAAAARAAAAAPAALAAAPL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 156 PEQTVIGLGASTGGTEATLNVLRRLPANIPG-MVIVQHMPVGFTKMYAERLNRLCQMEVREAVNGDEIRPGLALVAPADY 234
Cdd:PRK00742 162 LSSKLVAIGTSTGGPEALQKVLTPLPANFPApILIVQHMPAGFTKSFAERLNRLCQIEVKEAEDGERLKPGHAYIAPGGK 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 235 QAKVVRMGPRYTLSCIPGEKVSGHRPSVDVLFSSMAASVRCRMVGIIMTGMGRDGASGLLEMRKAGAYTIGQDKDSCVVY 314
Cdd:PRK00742 242 HMMVARSGANYRIKLDDGPPVNRHRPSVDVLFRSAAKAAGRNALGVILTGMGRDGAAGLLEMKQAGATTIAQDEASCVVY 321

                        330       340
                 ....*....|....*....|....*.
gi 494759980 315 GMPMVAHDIGAVTVQASCDNIASVLM 340
Cdd:PRK00742 322 GMPKAAIEAGAVDEVLPLDQIAERIL 347
 
Name Accession Description Interval E-value
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
6-340 3.90e-135

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 388.35  E-value: 3.90e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   6 RKIRVLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVIL 85
Cdd:PRK00742   2 MKIRVLVVDDSAFMRRLISEILNSDPDIEVVGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRPTPVVM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  86 VSSLNLR----VFDALAAGAVDFVRKPDAVESR--ESFLQALTHKIIVASHARL----SRANLPHPAAPAAPLRFGGDGA 155
Cdd:PRK00742  82 VSSLTERgaeiTLRALELGAVDFVTKPFLGISLgmDEYKEELAEKVRAAARARVralpPRAAAAARAAAAAPAALAAAPL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 156 PEQTVIGLGASTGGTEATLNVLRRLPANIPG-MVIVQHMPVGFTKMYAERLNRLCQMEVREAVNGDEIRPGLALVAPADY 234
Cdd:PRK00742 162 LSSKLVAIGTSTGGPEALQKVLTPLPANFPApILIVQHMPAGFTKSFAERLNRLCQIEVKEAEDGERLKPGHAYIAPGGK 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 235 QAKVVRMGPRYTLSCIPGEKVSGHRPSVDVLFSSMAASVRCRMVGIIMTGMGRDGASGLLEMRKAGAYTIGQDKDSCVVY 314
Cdd:PRK00742 242 HMMVARSGANYRIKLDDGPPVNRHRPSVDVLFRSAAKAAGRNALGVILTGMGRDGAAGLLEMKQAGATTIAQDEASCVVY 321

                        330       340
                 ....*....|....*....|....*.
gi 494759980 315 GMPMVAHDIGAVTVQASCDNIASVLM 340
Cdd:PRK00742 322 GMPKAAIEAGAVDEVLPLDQIAERIL 347
CheB_Rec cd16432
Chemotaxis response regulator protein-glutamate methylesterase, CheB, with N-terminal REC ...
 160-342 1.01e-87

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: 261.53  E-value: 1.01e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 160 VIGLGASTGGTEATLNVLRRLPANIP-GMVIVQHMPVGFTKMYAERLNRLCQMEVREAVNGDEIRPGLALVAPADYQAKV 238
Cdd:cd16432    1 LVAIGASTGGPQALQEILSALPADFPaPILIVQHMPPGFTKSFAERLNRLSALPVKEAEDGEPLEPGTVYIAPGGYHLVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 239 VRMGPRYTLSCIPGEKVSGHRPSVDVLFSSMAASVRCRMVGIIMTGMGRDGASGLLEMRKAGAYTIGQDKDSCVVYGMPM 318
Cdd:cd16432   81 ERRGGGGRIRLSDGPPVNGHRPSVDVLFRSAAEVYGARALGVILTGMGRDGAEGLLALKEAGGYTIAQDEASSVVYGMPK 160

                        170       180
                 ....*....|....*....|....
gi 494759980 319 VAHDIGAVTVQASCDNIASVLMNH 342
Cdd:cd16432  161 AAIEAGAADEVLPLDEIAAAILRL 184
CheB COG2201
Chemotaxis response regulator CheB, contains REC and protein-glutamate methylesterase domains ...
 160-346 1.74e-85

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


Pssm-ID: 441803  Cd Length: 193  Bit Score: 256.17  E-value: 1.74e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 160 VIGLGASTGGTEATLNVLRRLPANIP-GMVIVQHMPVGFTKMYAERLNRLCQMEVREAVNGDEIRPGLALVAPADYQAKV 238
Cdd:COG2201    5 VVAIGASTGGPEALEEVLSALPADFPaPIVIVQHMPPGFTSSLAERLNRLTALPVKEAEDGERLEPGHVYIAPGGRHLEV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 239 VRMGPrYTLSCIPGEKVSGHRPSVDVLFSSMAASVRCRMVGIIMTGMGRDGASGLLEMRKAGAYTIGQDKDSCVVYGMPM 318
Cdd:COG2201   85 ERSGG-YRLRLSDGPPVNGHRPSVDVLFRSLAEVYGERAVGVILTGMGSDGAEGLKAIKEAGGLTIAQDEESCVVYGMPR 163

                        170       180
                 ....*....|....*....|....*...
gi 494759980 319 VAHDIGAVTVQASCDNIASVLMNHLNNR 346
Cdd:COG2201  164 AAIEAGAVDEVLPLEEIAAALLRLLRRR 191
CheB_methylest pfam01339
CheB methylesterase;
161-339 6.62e-74

CheB methylesterase;


Pssm-ID: 460166  Cd Length: 178  Bit Score: 226.15  E-value: 6.62e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  161 IGLGASTGGTEATLNVLRRLPANIPG-MVIVQHMPVGFTKMYAERLNRLCQMEVREAVNGDEIRPGLALVAPADYQAKVV 239
Cdd:pfam01339   1 VAIGASTGGPEALEELLPALPADLPAaIVVVQHMPPGFTSSLAERLNRLSALPVKEAEDGEPLEPGTVYIAPGGYHLLVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  240 RMGPRYTLsciPGEKVSGHRPSVDVLFSSMAASVR-CRMVGIIMTGMGRDGASGLLEMRKAGAYTIGQDKDSCVVYGMPM 318
Cdd:pfam01339  81 DGRGPYRS---DGPPVNGHRPSIDVLFRSLAEAYGgKRAIGVILTGMGSDGAAGLKAIKEAGGLTIAQDPATAVVYGMPR 157

                         170       180
                  ....*....|....*....|.
gi 494759980  319 VAHDIGAVTVQASCDNIASVL 339
Cdd:pfam01339 158 AAIEAGAADFVLPLEEIAAEL 178
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 8-64 3.21e-06

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: 43.71  E-value: 3.21e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 494759980     8 IRVLVVDDSAVARSVIIQGLSASPriEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMP 64
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEG--YEVDEATDGEEALELLKEEKPDLILLDIMMP 55
 
Name Accession Description Interval E-value
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
6-340 3.90e-135

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 388.35  E-value: 3.90e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   6 RKIRVLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVIL 85
Cdd:PRK00742   2 MKIRVLVVDDSAFMRRLISEILNSDPDIEVVGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRPTPVVM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  86 VSSLNLR----VFDALAAGAVDFVRKPDAVESR--ESFLQALTHKIIVASHARL----SRANLPHPAAPAAPLRFGGDGA 155
Cdd:PRK00742  82 VSSLTERgaeiTLRALELGAVDFVTKPFLGISLgmDEYKEELAEKVRAAARARVralpPRAAAAARAAAAAPAALAAAPL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 156 PEQTVIGLGASTGGTEATLNVLRRLPANIPG-MVIVQHMPVGFTKMYAERLNRLCQMEVREAVNGDEIRPGLALVAPADY 234
Cdd:PRK00742 162 LSSKLVAIGTSTGGPEALQKVLTPLPANFPApILIVQHMPAGFTKSFAERLNRLCQIEVKEAEDGERLKPGHAYIAPGGK 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 235 QAKVVRMGPRYTLSCIPGEKVSGHRPSVDVLFSSMAASVRCRMVGIIMTGMGRDGASGLLEMRKAGAYTIGQDKDSCVVY 314
Cdd:PRK00742 242 HMMVARSGANYRIKLDDGPPVNRHRPSVDVLFRSAAKAAGRNALGVILTGMGRDGAAGLLEMKQAGATTIAQDEASCVVY 321

                        330       340
                 ....*....|....*....|....*.
gi 494759980 315 GMPMVAHDIGAVTVQASCDNIASVLM 340
Cdd:PRK00742 322 GMPKAAIEAGAVDEVLPLDQIAERIL 347
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
8-343 7.20e-98

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 292.94  E-value: 7.20e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   8 IRVLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVILVS 87
Cdd:PRK12555   1 MRIGIVNDSPLAVEALRRALARDPDHEVVWVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAERPCPILIVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  88 SL---NL-RVFDALAAGAVDFVRKP--DAVESRESFLQALTHKIIVASHARLSRANLPHPAAPAAPLRFGGDgapeQTVI 161
Cdd:PRK12555  81 SLterNAsRVFEAMGAGALDAVDTPtlGIGAGLEEYAAELLAKIDQIGRLLGRRLAPAAAPAAASAAPFRTT----PRLV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 162 GLGASTGGTEATLNVLRRLPANIPG-MVIVQHMPVGFTKMYAERLNRLCQMEVREAVNGDEIRPGLALVAPADYQakvVR 240
Cdd:PRK12555 157 AIGASAGGPAALAVLLGGLPADFPAaIVIVQHVDAAFAAGMAEWLDGQTALPVREAREGERPQPGHVLLAPTNDH---LR 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 241 MGPRYTLSCIPGEKVSGHRPSVDVLFSSMAASVRCRMVGIIMTGMGRDGASGLLEMRKAGAYTIGQDKDSCVVYGMPMVA 320
Cdd:PRK12555 234 LTRDGALRYTREPPVNPYRPSVDVFFESVAQHWGGNAIGVLLTGMGRDGARGLKAMRQAGAHTIAQDEASSAVYGMPKAA 313

                        330       340
                 ....*....|....*....|...
gi 494759980 321 HDIGAVTVQASCDNIASVLMNHL 343
Cdd:PRK12555 314 AALGAASEVLPLERIAPRLIALF 336
CheB_Rec cd16432
Chemotaxis response regulator protein-glutamate methylesterase, CheB, with N-terminal REC ...
 160-342 1.01e-87

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: 261.53  E-value: 1.01e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 160 VIGLGASTGGTEATLNVLRRLPANIP-GMVIVQHMPVGFTKMYAERLNRLCQMEVREAVNGDEIRPGLALVAPADYQAKV 238
Cdd:cd16432    1 LVAIGASTGGPQALQEILSALPADFPaPILIVQHMPPGFTKSFAERLNRLSALPVKEAEDGEPLEPGTVYIAPGGYHLVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 239 VRMGPRYTLSCIPGEKVSGHRPSVDVLFSSMAASVRCRMVGIIMTGMGRDGASGLLEMRKAGAYTIGQDKDSCVVYGMPM 318
Cdd:cd16432   81 ERRGGGGRIRLSDGPPVNGHRPSVDVLFRSAAEVYGARALGVILTGMGRDGAEGLLALKEAGGYTIAQDEASSVVYGMPK 160

                        170       180
                 ....*....|....*....|....
gi 494759980 319 VAHDIGAVTVQASCDNIASVLMNH 342
Cdd:cd16432  161 AAIEAGAADEVLPLDEIAAAILRL 184
CheB COG2201
Chemotaxis response regulator CheB, contains REC and protein-glutamate methylesterase domains ...
 160-346 1.74e-85

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


Pssm-ID: 441803  Cd Length: 193  Bit Score: 256.17  E-value: 1.74e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 160 VIGLGASTGGTEATLNVLRRLPANIP-GMVIVQHMPVGFTKMYAERLNRLCQMEVREAVNGDEIRPGLALVAPADYQAKV 238
Cdd:COG2201    5 VVAIGASTGGPEALEEVLSALPADFPaPIVIVQHMPPGFTSSLAERLNRLTALPVKEAEDGERLEPGHVYIAPGGRHLEV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 239 VRMGPrYTLSCIPGEKVSGHRPSVDVLFSSMAASVRCRMVGIIMTGMGRDGASGLLEMRKAGAYTIGQDKDSCVVYGMPM 318
Cdd:COG2201   85 ERSGG-YRLRLSDGPPVNGHRPSVDVLFRSLAEVYGERAVGVILTGMGSDGAEGLKAIKEAGGLTIAQDEESCVVYGMPR 163

                        170       180
                 ....*....|....*....|....*...
gi 494759980 319 VAHDIGAVTVQASCDNIASVLMNHLNNR 346
Cdd:COG2201  164 AAIEAGAVDEVLPLEEIAAALLRLLRRR 191
CheB_methylest pfam01339
CheB methylesterase;
161-339 6.62e-74

CheB methylesterase;


Pssm-ID: 460166  Cd Length: 178  Bit Score: 226.15  E-value: 6.62e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  161 IGLGASTGGTEATLNVLRRLPANIPG-MVIVQHMPVGFTKMYAERLNRLCQMEVREAVNGDEIRPGLALVAPADYQAKVV 239
Cdd:pfam01339   1 VAIGASTGGPEALEELLPALPADLPAaIVVVQHMPPGFTSSLAERLNRLSALPVKEAEDGEPLEPGTVYIAPGGYHLLVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  240 RMGPRYTLsciPGEKVSGHRPSVDVLFSSMAASVR-CRMVGIIMTGMGRDGASGLLEMRKAGAYTIGQDKDSCVVYGMPM 318
Cdd:pfam01339  81 DGRGPYRS---DGPPVNGHRPSIDVLFRSLAEAYGgKRAIGVILTGMGSDGAAGLKAIKEAGGLTIAQDPATAVVYGMPR 157

                         170       180
                  ....*....|....*....|.
gi 494759980  319 VAHDIGAVTVQASCDNIASVL 339
Cdd:pfam01339 158 AAIEAGAADFVLPLEEIAAEL 178
CheB_like cd16351
methylesterase CheB domain family; This family contains the methylesterase CheB (EC 3.1.1.61; ...
 160-326 1.01e-49

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: 164.66  E-value: 1.01e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 160 VIGLGASTGGTEATLNVLRRLPANIP-GMVIVQHMPVGFTKMYAERLNRLCQMEVREAVNGDEIRPGLALVAPADYQAKV 238
Cdd:cd16351    1 IVGIGASTGGLEALEHLFEQLPIHSGlVYVVIQHMPPGFTSSMAERLGKKTKVGVKEAEDGEPVEPGTIYIAPGDTHINL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 239 VRMGPRYTLSCIPGEKVSGHRPSVDVLFSSMAASVRCRMVGIIMTGMGRDGASGLLEMRKAGAYTIGQDKDSCVVYGMPM 318
Cdd:cd16351   81 ENGKGFKVQELSNDTGINNLRPPVDHFFSSLAKYNKEKSIAVILTGMGNDGSSGLSYVYDTGGTVIAQTEESCVVFGMPN 160


                 ....*...
gi 494759980 319 VAHDIGAV 326
Cdd:cd16351  161 YAIQTGKV 168
CheB cd16433
Chemotaxis response regulator protein-glutamate methylesterase, CheB; This family contains the ...
 160-339 2.33e-44

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: 150.22  E-value: 2.33e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 160 VIGLGASTGGTEATLNVLRRLPANIPG-MVIVQHMPVGFTKMYAERLNRLCQMEVREAVNGDEIRPGLALVAPADYQAkV 238
Cdd:cd16433    1 IVVIGASAGGLEALLELLSALPADFPApVLVVLHRPPDSPSVLPELLSRRTPLPVKEAEDGEPIEPGTIYVAPPDYHL-L 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 239 VRMGPRYTLSCipGEKVSGHRPSVDVLFSSMAASVRCRMVGIIMTGMGRDGASGLLEMRKAGAYTIGQDKDSCVVYGMPM 318
Cdd:cd16433   80 VEDDGTFSLSR--GPKVNFSRPSIDVLFRSAADAYGPRVIGVVLTGANDDGAAGLAAIKRAGGLTIVQDPATAEVPSMPR 157

                        170       180
                 ....*....|....*....|.
gi 494759980 319 VAHDIGAVTVQASCDNIASVL 339
Cdd:cd16433  158 AALAAVAVDHVLPLAEIAALL 178
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
 8-125 9.56e-43

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: 144.46  E-value: 9.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   8 IRVLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVILVS 87
Cdd:cd17541    1 IRVLIVDDSAVMRKLLSRILESDPDIEVVGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERPTPVVMVS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 494759980  88 SLNLR----VFDALAAGAVDFVRKPDAVESR--ESFLQALTHKI 125
Cdd:cd17541   81 SLTEEgaeiTLEALELGAVDFIAKPSGGISLdlEEIAEELIEKI 124
CheB-CheR_fusion cd16434
Chemotaxis response regulator protein-glutamate methylesterase, CheB, fused with CheR domain; ...
 160-342 5.86e-33

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


Pssm-ID: 319753  Cd Length: 180  Bit Score: 120.55  E-value: 5.86e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 160 VIGLGASTGGTEATLNVLRRLPANiPGM--VIVQHMPVGFTKMYAERLNRLCQMEVREAVNGDEIRPGLALVAPADYQAK 237
Cdd:cd16434    1 VVGIGASAGGLEALEEFFSALPAD-SGMafVVVQHLSPDHKSLLAELLARHTSMPVVEAEDGMRVEPNHVYVIPPGKDLT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980 238 VVrmGPRYTLSciPGEKVSGHRPSVDVLFSSMAASVRCRMVGIIMTGMGRDGASGLLEMRKAGAYTIGQDKDSCVVYGMP 317
Cdd:cd16434   80 IE--DGRLRLS--PPDEPRGPRLPIDVFFRSLAEDQGERAIGVILSGTGSDGTLGLKAIKEAGGLVLAQDPETAKFDGMP 155

                        170       180
                 ....*....|....*....|....*
gi 494759980 318 MVAHDIGAVTVQASCDNIASVLMNH 342
Cdd:cd16434  156 RSAIATGLVDFVLPPEEIAAELLAY 180
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
 7-121 6.20e-24

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 97.96  E-value: 6.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   7 KIRVLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQF-LPSHPLPVIL 85
Cdd:COG3279    1 MMKILIVDDEPLARERLERLLEKYPDLEVVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLrELDPPPPIIF 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 494759980  86 VSSLNLRVFDALAAGAVDFVRKPDaveSRESFLQAL 121
Cdd:COG3279   81 TTAYDEYALEAFEVNAVDYLLKPI---DEERLAKAL 113
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
 9-108 1.78e-22

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: 90.22  E-value: 1.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHP-LPVILVS 87
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEWEAGFEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPdTKIIILS 80

                         90       100
                 ....*....|....*....|...
gi 494759980  88 SLN--LRVFDALAAGAVDFVRKP 108
Cdd:COG4753   81 GYSdfEYAQEAIKLGADDYLLKP 103
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
 6-123 1.22e-19

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 83.87  E-value: 1.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   6 RKIRVLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHP-LPVI 84
Cdd:COG4565    2 KMIRVLIVEDDPMVAELLRRYLERLPGFEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPdVDVI 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 494759980  85 LVSSLNL--RVFDALAAGAVDFVRKPDaveSRESFLQALTH 123
Cdd:COG4565   82 VITAARDpeTVREALRAGVVDYLIKPF---TFERLREALER 119
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
 10-121 9.22e-19

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: 80.63  E-value: 9.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHP-LPVILVSS 88
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLESEPDIEVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPdLKVIVLTA 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 494759980  89 LNLR--VFDALAAGAVDFVRKPdavESRESFLQAL 121
Cdd:cd17535   81 HDDPeyVLRALKAGAAGYLLKD---SSPEELIEAI 112
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 7-108 3.65e-18

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: 80.72  E-value: 3.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   7 KIRVLVVDDSAVARSVIIQGLSASpRIEVVgYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDF---LKQFLPSHPLPV 83
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAA-GYEVV-EAADGEEALELLQEHRPDLILLDLEMPDMDGLELcrrLRADPRTADIPI 78

                         90       100
                 ....*....|....*....|....*..
gi 494759980  84 ILVSSLNLR--VFDALAAGAVDFVRKP 108
Cdd:COG3706   79 IFLTALDDEedRARALEAGADDYLTKP 105
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
 9-112 4.64e-18

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: 78.64  E-value: 4.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLSASPRIEVVGYAvNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQF--LPSHP-LPVIL 85
Cdd:cd17551    2 RILIVDDNPTNLLLLEALLRSAGYLEVVSFT-DPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLraLPGLEdVPIVM 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 494759980  86 VSSLN---LRVfDALAAGAVDFVRKP-DAVE 112
Cdd:cd17551   81 ITADTdreVRL-RALEAGATDFLTKPfDPVE 110
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 6-108 9.50e-18

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: 78.35  E-value: 9.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   6 RKIRVLVVDDSAVARSVIIQGLSASpRIEVVGyAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDF---LKQFLPSHPLP 82
Cdd:COG0784    4 GGKRILVVDDNPDNRELLRRLLERL-GYEVTT-AEDGAEALELLRAGPPDLILLDINMPGMDGLELlrrIRALPRLPDIP 81

                         90       100
                 ....*....|....*....|....*...
gi 494759980  83 VILVSSLNLR--VFDALAAGAVDFVRKP 108
Cdd:COG0784   82 IIALTAYADEedRERALEAGADDYLTKP 109
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
 11-108 1.57e-17

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: 76.88  E-value: 1.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  11 LVVDDSAVARSVIIQGLSASPriEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHP-LPVILVSSL 89
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREG--YEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPdIPVIVLTAK 78

                         90       100
                 ....*....|....*....|.
gi 494759980  90 NLR--VFDALAAGAVDFVRKP 108
Cdd:cd00156   79 ADEedAVRALELGADDYLVKP 99
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
 8-108 1.88e-17

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: 77.32  E-value: 1.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   8 IRVLVVDDSAVARSVIIQGLSASpRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHP-LPVILV 86
Cdd:cd17542    1 KKVLIVDDAAFMRMMLKDILTKA-GYEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPnAKVIMC 79

                         90       100
                 ....*....|....*....|....
gi 494759980  87 SSLNLR--VFDALAAGAVDFVRKP 108
Cdd:cd17542   80 SAMGQEemVKEAIKAGAKDFIVKP 103
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
 7-108 1.03e-16

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: 77.69  E-value: 1.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   7 KIRVLVVDDSAVARSVIIQGLSASprievvGYAV----NAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQF--LPSHp 80
Cdd:COG0745    1 MPRILVVEDDPDIRELLADALERE------GYEVdtaaDGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLraRPSD- 73

                         90       100       110
                 ....*....|....*....|....*....|.
gi 494759980  81 LPVILVSSLN---LRVfDALAAGAVDFVRKP 108
Cdd:COG0745   74 IPIIMLTARDdeeDRV-RGLEAGADDYLTKP 103
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 10-108 1.46e-16

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: 74.50  E-value: 1.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   10 VLVVDDSAVARSVIIQGLsaspRIE--VVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHP-LPVILV 86
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLL----EKEgyVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPtTPVIIL 76

                          90       100
                  ....*....|....*....|....*
gi 494759980   87 SS---LNLRVfDALAAGAVDFVRKP 108
Cdd:pfam00072  77 TAhgdEDDAV-EALEAGADDFLSKP 100
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 6-108 1.59e-16

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: 80.01  E-value: 1.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   6 RKIRVLVVDDSAVARSVIIQGLSASprievvGYAV----NAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHP- 80
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERA------GYEVetaaSGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPd 74

                         90       100       110
                 ....*....|....*....|....*....|.
gi 494759980  81 LPVILVS---SLNLRVfDALAAGAVDFVRKP 108
Cdd:COG2204   75 LPVILLTgygDVETAV-EAIKAGAFDYLTKP 104
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 3-108 3.16e-16

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: 76.74  E-value: 3.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   3 TTNRKIRVLVVDDSAVARSVIIQGLSASPRiEVVGyAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQF--LPSHP 80
Cdd:COG3437    2 RTGQAPTVLIVDDDPENLELLRQLLRTLGY-DVVT-AESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLraDPSTR 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 494759980  81 -LPVILVSSLNLR--VFDALAAGAVDFVRKP 108
Cdd:COG3437   80 dIPVIFLTALADPedRERALEAGADDYLTKP 110
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
 7-76 1.66e-15

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: 72.23  E-value: 1.66e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   7 KIRVLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFL 76
Cdd:COG2197    1 MIRVLIVDDHPLVREGLRALLEAEPDIEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRLL 70
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
 10-126 2.91e-15

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: 71.21  E-value: 2.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLS-ASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHP-LPVILVS 87
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIDwEELGFEVVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPdIKIIILS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 494759980  88 SlnlrvFD-------ALAAGAVDFVRKPdavESRESFLQALtHKII 126
Cdd:cd17536   81 G-----YDdfeyaqkAIRLGVVDYLLKP---VDEEELEEAL-EKAK 117
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
 10-108 3.60e-14

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: 67.95  E-value: 3.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLP-SHPLPVILVSS 88
Cdd:cd17532    1 ALIVDDEPLAREELRYLLEEHPDIEIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKlAKPPLIVFVTA 80

                         90       100
                 ....*....|....*....|....*
gi 494759980  89 lnlrvFD--ALAA---GAVDFVRKP 108
Cdd:cd17532   81 -----YDeyAVEAfelNAVDYLLKP 100
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
 6-108 6.77e-13

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: 66.52  E-value: 6.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   6 RKIRVLVVDDSAVARSVIIQGLSASpRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVIL 85
Cdd:COG3707    2 RGLRVLVVDDEPLRRADLREGLREA-GYEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERPAPVIL 80

                         90       100
                 ....*....|....*....|....*
gi 494759980  86 VSSLNLRVF--DALAAGAVDFVRKP 108
Cdd:COG3707   81 LTAYSDPELieRALEAGVSAYLVKP 105
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
 10-108 1.24e-12

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: 63.30  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSASP-RIEVvgyAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQfLPSHPL----PVI 84
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGyRVLV---ATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRR-LKADPAtrhiPVI 76

                         90       100
                 ....*....|....*....|....*..
gi 494759980  85 LVSSLNlRVFD---ALAAGAVDFVRKP 108
Cdd:cd19920   77 FLTALT-DTEDkvkGFELGAVDYITKP 102
PRK15369 PRK15369
two component system response regulator;
8-120 1.64e-12

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 65.87  E-value: 1.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   8 IRVLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVILV- 86
Cdd:PRK15369   4 YKILLVDDHELIINGIKNMLAPYPRYKIVGQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRWPAMNILVl 83

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 494759980  87 --SSLNLRVFDALAAGAVDFVRKpdavESRESFLQA 120
Cdd:PRK15369  84 taRQEEHMASRTLAAGALGYVLK----KSPQQILLA 115
PRK11697 PRK11697
two-component system response regulator BtsR;
8-84 3.46e-12

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 65.25  E-value: 3.46e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494759980   8 IRVLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHpLPVI 84
Cdd:PRK11697   2 IKVLIVDDEPLAREELRELLQEEGDIEIVGECSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELVGMLDPEH-MPYI 77
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
 10-108 4.38e-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: 62.51  E-value: 4.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSASprievvGYAVNAM-DAKTKLQHLSPD---VMTLDVEMPGINGIDFLKQFLPSHP-LPVI 84
Cdd:cd17549    1 VLLVDDDADVREALQQTLELA------GFRVRAFaDAEEALAALSPDfpgVVISDIRMPGMDGLELLAQIRELDPdLPVI 74

                         90       100
                 ....*....|....*....|....*..
gi 494759980  85 LVSS---LNLRVfDALAAGAVDFVRKP 108
Cdd:cd17549   75 LITGhgdVPMAV-EAMRAGAYDFLEKP 100
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
 8-108 7.21e-12

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: 61.78  E-value: 7.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   8 IRVLVVDDSAVARSVIIQGLSASPRIEVVgYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQfLPSHPLP--VIL 85
Cdd:cd17593    1 MKVLICDDSSMARKQLARALPADWDVEIT-FAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEA-LPVEQLEtkVIV 78

                         90       100
                 ....*....|....*....|....*...
gi 494759980  86 VS-----SLNLRVfdaLAAGAVDFVRKP 108
Cdd:cd17593   79 VSgdvqpEAKERV---LELGALAFLKKP 103
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
 8-108 2.12e-11

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: 60.34  E-value: 2.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   8 IRVLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQfLPS--HPLPVIL 85
Cdd:cd19925    1 INVLIVEDDPMVAEIHRAYVEQVPGFTVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRE-LRAagHDVDVIV 79

                         90       100
                 ....*....|....*....|....*
gi 494759980  86 VSSLN--LRVFDALAAGAVDFVRKP 108
Cdd:cd19925   80 VTAANdvETVREALRLGVVDYLIKP 104
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
 10-101 4.40e-11

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: 59.28  E-value: 4.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQfLPSHPLP---VIL- 85
Cdd:cd19931    1 VLLIDDHPLLRKGIKQLIELDPDFTVVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKA-LREEGVSariVILt 79

                         90
                 ....*....|....*.
gi 494759980  86 VSSLNLRVFDALAAGA 101
Cdd:cd19931   80 VSDAEDDVVTALRAGA 95
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
 10-108 5.12e-11

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: 58.93  E-value: 5.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSAsprievVGY----AVNAMDAKTKLQHLSP---------DVMTLDVEMPGINGIDFLKQfL 76
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKN------LGFeiaeAVDGEEALNKLENLAKegndlskelDLIITDIEMPKMDGYELTFE-L 73

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494759980  77 PSHP----LPVILVSSLNlRVFD---ALAAGAVDFVRKP 108
Cdd:cd19924   74 RDDPrlanIPVILNSSLS-GEFSrarGKKVGADAYLAKF 111
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
 3-74 5.26e-11

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 61.58  E-value: 5.26e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494759980   3 TTNRKIRVLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQ 74
Cdd:PRK10651   2 SNQEPATILLIDDHPMLRTGVKQLISMAPDITVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDK 73
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
 9-101 5.82e-11

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: 58.77  E-value: 5.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLSASprievvGYAV----NAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHP-LPV 83
Cdd:cd17554    2 KILVVDDEENIRELYKEELEDE------GYEVvtagNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPdLPV 75

                         90       100
                 ....*....|....*....|
gi 494759980  84 ILVSSLNLRV--FDALAAGA 101
Cdd:cd17554   76 IICTAYSEYKsdFSSWAADA 95
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
 8-108 7.44e-11

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: 58.89  E-value: 7.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   8 IRVLVVDDSAVARSVIIQGLSAsprievVGY-----AVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPL- 81
Cdd:cd19923    1 MKVLVVDDFSTMRRIIKNLLKE------LGFnnveeAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALs 74

                         90       100       110
                 ....*....|....*....|....*....|.
gi 494759980  82 --PVILVSSLNLR--VFDALAAGAVDFVRKP 108
Cdd:cd19923   75 hlPVLMVTAEAKKenVIAAAQAGVNNYIVKP 105
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
 9-108 1.37e-10

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: 57.98  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLSASprievvGYAV-NAMDAKTKLQHLS---PDVMTLDVEMPGINGIDFLKQFLPSHP-LPV 83
Cdd:cd17555    2 TILVIDDDEVVRESIAAYLEDS------GFQVlQAADGRQGLELFRseqPDLVLCDLRMPEMDGLEVLKQITKESPdTPV 75

                         90       100
                 ....*....|....*....|....*..
gi 494759980  84 ILVSSLNL--RVFDALAAGAVDFVRKP 108
Cdd:cd17555   76 IVVSGAGVmsDAVEALRLGAWDYLTKP 102
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
 9-108 1.79e-10

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: 57.12  E-value: 1.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLSASprievvGYAV----NAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQfLPSHP---- 80
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAE------GYEVltadSGQEALALAEEELPDLILLDVMMPGMDGFEVCRR-LKEDPetrh 73

                         90       100       110
                 ....*....|....*....|....*....|...
gi 494759980  81 LPVILVSSLN-----LRvfdALAAGAVDFVRKP 108
Cdd:cd17538   74 IPVIMITALDdredrIR---GLEAGADDFLSKP 103
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
 10-108 2.70e-10

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: 57.12  E-value: 2.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSvIIQGLsasprIEVVGYAV----NAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHP-LPVI 84
Cdd:cd17550    1 ILIVDDEEDIRE-SLSGI-----LEDEGYEVdtaaDGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPdLPVI 74

                         90       100
                 ....*....|....*....|....*..
gi 494759980  85 LVS---SLNLRVfDALAAGAVDFVRKP 108
Cdd:cd17550   75 MISghgTIETAV-KATKLGAYDFIEKP 100
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
 11-108 4.17e-10

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: 56.26  E-value: 4.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  11 LVVDDSAVARSVIIQGLSASprievvGYAV----NAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQF--LPSHpLPVI 84
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKE------GYEVdtaaDGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLreKGSD-IPII 73

                         90       100
                 ....*....|....*....|....*..
gi 494759980  85 LVSSLNL---RVFdALAAGAVDFVRKP 108
Cdd:cd17574   74 MLTAKDEeedKVL-GLELGADDYITKP 99
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
 8-112 5.08e-10

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: 56.37  E-value: 5.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   8 IRVLVVDDSAVARSVIIQGLSASpRIEVVGyAVNAMDAKTKL-QHlsPDVMTL--DVEMPGINGIDFLK---QFLPSHPL 81
Cdd:cd17544    1 IKVLVVDDSATSRNHLRALLRRH-NFQVLE-AANGQEALEVLeQH--PDIKLVitDYNMPEMDGFELVReirKKYSRDQL 76

                         90       100       110
                 ....*....|....*....|....*....|...
gi 494759980  82 PVILVSSLNLRVFDA--LAAGAVDFVRKPDAVE 112
Cdd:cd17544   77 AIIGISASGDNALSArfIKAGANDFLTKPFLPE 109
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
 9-108 1.04e-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: 55.64  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLSASPRIEVVGyAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQfLPSHP----LPVI 84
Cdd:cd17552    3 RILVIDDEEDIREVVQACLEKLAGWEVLT-ASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKK-LQANPetqsIPVI 80

                         90       100
                 ....*....|....*....|....*...
gi 494759980  85 L----VSSLNLRVFDALAAGAVdfVRKP 108
Cdd:cd17552   81 LltakAQPSDRQRFASLGVAGV--IAKP 106
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
 9-112 1.52e-09

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: 54.97  E-value: 1.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLsASPRIEVVGYAvNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHP-LPVILV- 86
Cdd:cd19919    2 TVWIVDDDSSIRWVLERAL-AGAGLTVTSFE-NAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPdLPVIIMt 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 494759980  87 --SSLNLRVfDALAAGAVDFVRKP----DAVE 112
Cdd:cd19919   80 ahSDLDSAV-SAYQGGAFEYLPKPfdidEAVA 110
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
 10-123 1.83e-09

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 58.73  E-value: 1.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSASPrIEVVGYAvNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHP-LPVILV-- 86
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAG-LTCTTFE-NGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPmLPVIIMta 83

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494759980  87 -SSLNLRVfDALAAGAVDFVRKP-DAVESRESFLQALTH 123
Cdd:PRK10923  84 hSDLDAAV-SAYQQGAFDYLPKPfDIDEAVALVERAISH 121
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
 10-108 2.22e-09

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: 54.56  E-value: 2.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGL-SASPRIEVVGYAVNAMDAKTKLQHlSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVILVSS 88
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLlRCGYQVTTCTDAEEALSMLRENKD-EFDLVITDVHMPDMDGFEFLELIRLEMDLPVIMMSA 79

                         90       100
                 ....*....|....*....|..
gi 494759980  89 LN--LRVFDALAAGAVDFVRKP 108
Cdd:cd17584   80 DGstSTVMKGLAHGACDYLLKP 101
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
 10-108 3.28e-09

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: 54.13  E-value: 3.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSASP-RIEVVGYAVNAMDAktkLQHLSPDVMTLDVEMPGINGIDFLKQFLPSH-PLPVILVS 87
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGyKVTHVETGKEALAF---LSDQPPDVVLLDLKLPDMSGMEILKWIQERSlPTSVIVIT 77

                         90       100
                 ....*....|....*....|....
gi 494759980  88 ---SLNLRVfDALAAGAVDFVRKP 108
Cdd:cd17572   78 ahgSVDIAV-EAMRLGAYDFLEKP 100
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
 8-108 3.75e-09

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: 53.96  E-value: 3.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   8 IRVLVVDDSAVARSVIIQGLSASPRiEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVILVS 87
Cdd:cd19932    1 VRVLIAEDEALIRMDLREMLEEAGY-EVVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENIAPIVLLT 79

                         90       100
                 ....*....|....*....|...
gi 494759980  88 SLNLR--VFDALAAGAVDFVRKP 108
Cdd:cd19932   80 AYSQQdlVERAKEAGAMAYLVKP 102
orf27 CHL00148
Ycf27; Reviewed
 4-114 5.63e-09

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 55.88  E-value: 5.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   4 TNRKIRVLVVDDSAVARSVIiqglsaSPRIEVVGYAV-NAMDAKTKLQHLS---PDVMTLDVEMPGINGIDFLKQFLPSH 79
Cdd:CHL00148   3 ENSKEKILVVDDEAYIRKIL------ETRLSIIGYEViTASDGEEALKLFRkeqPDLVILDVMMPKLDGYGVCQEIRKES 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 494759980  80 PLPVILVSSLNlRVFD---ALAAGAVDFVRKP---DAVESR 114
Cdd:CHL00148  77 DVPIIMLTALG-DVSDritGLELGADDYVVKPfspKELEAR 116
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
 10-108 5.78e-09

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: 53.52  E-value: 5.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSASP-RIEVVGYAVNAM------DAKTKLQHLSPDV-MTL-DVEMPGINGIDFLKQFLPSHP 80
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLRISScRVTAVDSGKRALeflgleDEEDSSNFNEPKVnMIItDYCMPGMTGYDLLKKVKESSA 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 494759980  81 L---PVILVSSLNL--RVFDALAAGAVDFVRKP 108
Cdd:cd17581   81 LkeiPVVIMSSENIptRISRCLEEGAEDFLLKP 113
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
 10-135 1.43e-08

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: 53.95  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSviiqglSASPRIEVVGYAVNA-MDAKTKLQHLSPD---VMTLDVEMPGINGIDFLKQFLPS-HPLPVI 84
Cdd:COG4566    2 VYIVDDDEAVRD------SLAFLLESAGLRVETfASAEAFLAALDPDrpgCLLLDVRMPGMSGLELQEELAARgSPLPVI 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494759980  85 LVS---SLNLRVfDALAAGAVDFVRKP-------DAVE-----SRESFLQALTHKIIVASHARLSR 135
Cdd:COG4566   76 FLTghgDVPMAV-RAMKAGAVDFLEKPfddqallDAVRralarDRARRAERARRAELRARLASLTP 140
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
 10-107 1.92e-08

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: 51.89  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHP-LPVILVSS 88
Cdd:cd19930    1 VLIAEDQEMVRGALAALLELEDDLEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPdTKVLIVTT 80

                         90       100
                 ....*....|....*....|...
gi 494759980  89 LN----LRvfDALAAGAVDFVRK 107
Cdd:cd19930   81 FGrpgyFR--RALAAGVDGYVLK 101
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
 7-74 3.06e-08

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: 51.07  E-value: 3.06e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494759980   7 KIRVLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQ 74
Cdd:cd17561    1 KIKVLIADDNREFVQLLEEYLNSQPDMEVVGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEK 68
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
4-128 4.71e-08

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 54.27  E-value: 4.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   4 TNRKIRVLVVDDSaVARSVIIQGLsasprIEVVGYAV----NAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSH 79
Cdd:PRK10365   2 THDNIDILVVDDD-ISHCTILQAL-----LRGWGYNValanSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALN 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 494759980  80 P-LPVILV---SSLNLRVfDALAAGAVDFVRKP-DAVESRESFLQALTHKIIVA 128
Cdd:PRK10365  76 PaIPVLIMtaySSVETAV-EALKTGALDYLIKPlDFDNLQATLEKALAHTHSID 128
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
 10-108 5.25e-08

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: 50.67  E-value: 5.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSviiqglSASPRIEVVGYAVNAMD-AKTKLQHLSPD---VMTLDVEMPGINGIDFLKQFLPSH-PLPVI 84
Cdd:cd17537    3 VYVVDDDEAVRD------SLAFLLRSVGLAVKTFTsASAFLAAAPPDqpgCLVLDVRMPGMSGLELQDELLARGsNIPII 76

                         90       100
                 ....*....|....*....|....*..
gi 494759980  85 LVSS---LNLRVfDALAAGAVDFVRKP 108
Cdd:cd17537   77 FITGhgdVPMAV-EAMKAGAVDFLEKP 102
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
 10-121 7.07e-08

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: 50.18  E-value: 7.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSASprievvGYAV----NAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHP-LPVI 84
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKA------GYAVdwvrTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQsLPVL 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494759980  85 LVS---SLNLRVfDALAAGAVDFVRKPDAVESRESFLQAL 121
Cdd:cd17624   75 ILTardGVDDRV-AGLDAGADDYLVKPFALEELLARLRAL 113
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
9-108 7.42e-08

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 53.70  E-value: 7.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLSASPrIEVVgyavNAMDAKTKLQHLS---PDVMTLDVEMPGINGIDFLKQFLPSHP-LPVI 84
Cdd:PRK11361   6 RILIVDDEDNVRRMLSTAFALQG-FETH----CANNGRTALHLFAdihPDVVLMDIRMPEMDGIKALKEMRSHETrTPVI 80

                         90       100
                 ....*....|....*....|....*.
gi 494759980  85 LVSSLN--LRVFDALAAGAVDFVRKP 108
Cdd:PRK11361  81 LMTAYAevETAVEALRCGAFDYVIKP 106
PLN03029 PLN03029
type-a response regulator protein; Provisional
 3-108 7.47e-08

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 52.34  E-value: 7.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   3 TTNRKIRVLVVDDSAVARSVIIQGLSASprievvGYAVNAMDAKTK-LQHL--------SPDVMTL------DVE----- 62
Cdd:PLN03029   4 TTESQFHVLAVDDSLIDRKLIEKLLKTS------SYQVTTVDSGSKaLKFLglheddrsNPDTPSVspnshqEVEvnlii 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 494759980  63 ----MPGINGIDFLKQFLPSHPL---PVILVSSLNL--RVFDALAAGAVDFVRKP 108
Cdd:PLN03029  78 tdycMPGMTGYDLLKKIKESSSLrniPVVIMSSENVpsRITRCLEEGAEEFFLKP 132
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
 10-108 7.76e-08

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: 50.16  E-value: 7.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSAS-PRIEVvgyAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQ----FLPSHPLPVI 84
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLgYEVDV---AENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRirelEGGGRRTPII 77

                         90       100
                 ....*....|....*....|....*.
gi 494759980  85 LVS--SLNLRVFDALAAGAVDFVRKP 108
Cdd:cd17546   78 ALTanALEEDREKCLEAGMDDYLSKP 103
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
11-113 1.77e-07

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 51.05  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  11 LVVDDSAVARsVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLP-SHPLPVILVSSL 89
Cdd:PRK09958   4 IIIDDHPLAI-AAIRNLLIKNDIEILAELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKrQYSGIIIIVSAK 82

                         90       100
                 ....*....|....*....|....*.
gi 494759980  90 NLRVFDALAA--GAVDFVRKPDAVES 113
Cdd:PRK09958  83 NDHFYGKHCAdaGANGFVSKKEGMNN 108
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
9-175 1.87e-07

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 51.34  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLsaspriEVVGYAVN-AMDAKTKLQHL--SPDVMTLDVEMPGINGIDFLKQFLPSHPLPVIL 85
Cdd:PRK10955   3 KILLVDDDRELTSLLKELL------EMEGFNVIvAHDGEQALDLLddSIDLLLLDVMMPKKNGIDTLKELRQTHQTPVIM 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  86 V----SSLNlRVFdALAAGAVDFVRKPdaVESREsflqaLTHKIivasHARLSRANLPHPAAPaaplrfGGDGAPEQTVI 161
Cdd:PRK10955  77 LtargSELD-RVL-GLELGADDYLPKP--FNDRE-----LVARI----RAILRRSHWSEQQQN------NDNGSPTLEVD 137

                        170
                 ....*....|....
gi 494759980 162 GLGASTGGTEATLN 175
Cdd:PRK10955 138 ALSLNPGRQEASFD 151
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
9-113 1.93e-07

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 51.01  E-value: 1.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLP---SHPLPVIL 85
Cdd:PRK10403   8 QVLIVDDHPLMRRGVRQLLELDPGFEVVAEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRdgvTAQIIILT 87

                         90       100
                 ....*....|....*....|....*...
gi 494759980  86 VSSLNLRVFDALAAGAVDFVRKPDAVES 113
Cdd:PRK10403  88 VSDASSDVFALIDAGADGYLLKDSDPEV 115
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
 9-121 3.06e-07

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: 48.57  E-value: 3.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLSASP---RIEVVGYAVNAMD----AKTKLQHLSPDVMTLDVEMPGINGIDFLKQfLPSHP- 80
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGvpnELHVVRDGEEALDflrgEGEYADAPRPDLILLDLNMPRMDGFEVLRE-IKADPd 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 494759980  81 ---LPVILVSSLNLR--VFDALAAGAVDFVRKPdavESRESFLQAL 121
Cdd:cd17557   80 lrrIPVVVLTTSDAEedIERAYELGANSYIVKP---VDFEEFVEAI 122
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
 8-112 3.37e-07

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: 48.56  E-value: 3.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   8 IRVLVVDDSAVARSVIIQGLSASPRIEVvGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFlPSHP----LPV 83
Cdd:cd17575    1 IMVLLVDDQAIIGEAVRRALADEEDIDF-HYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFF-RANPatrdIPI 78

                         90       100       110
                 ....*....|....*....|....*....|..
gi 494759980  84 ILVSSLNLRVF--DALAAGAVDF-VRKPDAVE 112
Cdd:cd17575   79 IVLSTKEEPEVksEAFALGANDYlVKLPDKIE 110
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
 10-108 4.19e-07

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: 47.54  E-value: 4.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSASprievvGYAV----NAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVIL 85
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAH------GYRVfeaeTGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWSAVPVIV 74

                         90       100
                 ....*....|....*....|....*
gi 494759980  86 VS--SLNLRVFDALAAGAVDFVRKP 108
Cdd:cd17620   75 LSarDEESDKIAALDAGADDYLTKP 99
fixJ PRK09390
response regulator FixJ; Provisional
 10-108 4.32e-07

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 49.62  E-value: 4.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIiQGLSASPRIEVVGYAvNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPS-HPLPVILVS- 87
Cdd:PRK09390   6 VHVVDDDEAMRDSL-AFLLDSAGFEVRLFE-SAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARgSPLPVIVMTg 83

                         90       100
                 ....*....|....*....|...
gi 494759980  88 --SLNLRVfDALAAGAVDFVRKP 108
Cdd:PRK09390  84 hgDVPLAV-EAMKLGAVDFIEKP 105
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
 10-108 1.04e-06

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: 46.66  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSASprievvGYAV----NAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSH-PLPVI 84
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEE------GYAVdvayDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGkQTPVL 74

                         90       100
                 ....*....|....*....|....*..
gi 494759980  85 LVS---SLNLRVfDALAAGAVDFVRKP 108
Cdd:cd19935   75 MLTardSVEDRV-KGLDLGADDYLVKP 100
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
 10-108 1.15e-06

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: 46.91  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSASprievvGYAV----NAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVIL 85
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEME------GFNVraahDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTSQVPVLM 74

                         90       100
                 ....*....|....*....|....*.
gi 494759980  86 VSSLNL---RVFdALAAGAVDFVRKP 108
Cdd:cd17623   75 LTARGDdidRIL-GLELGADDYLPKP 99
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
 9-121 1.60e-06

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: 46.58  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDsavaRSVIIQGLSASPRIE--VVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHP-LPVIL 85
Cdd:cd17615    1 RVLVVDD----EPNITELLSMALRYEgwDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPdVPVLF 76

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494759980  86 VS---SLNLRVfDALAAGAVDFVRKPDAVESRESFLQAL 121
Cdd:cd17615   77 LTakdSVEDRI-AGLTAGGDDYVTKPFSLEEVVARLRAL 114
PRK10693 PRK10693
two-component system response regulator RssB;
39-121 2.36e-06

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 48.45  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  39 AVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSH-PLPVILVSSLN--LRVFDALAAGAVDFVRKP--DAVES 113
Cdd:PRK10693   3 AANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGdQTPVLVISATEnmADIAKALRLGVQDVLLKPvkDLNRL 82


                 ....*...
gi 494759980 114 RESFLQAL 121
Cdd:PRK10693  83 REMVFACL 90
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
 9-115 2.55e-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: 45.84  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLSASprievvGYAV----NAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVI 84
Cdd:cd17619    2 HILIVEDEPVTRATLKSYFEQE------GYDVseagDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSEVGII 75

                         90       100       110
                 ....*....|....*....|....*....|...
gi 494759980  85 LVSSLNLRV--FDALAAGAVDFVRKPdaVESRE 115
Cdd:cd17619   76 LVTGRDDEVdrIVGLEIGADDYVTKP--FNPRE 106
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 8-64 3.21e-06

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: 43.71  E-value: 3.21e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 494759980     8 IRVLVVDDSAVARSVIIQGLSASPriEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMP 64
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEG--YEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
 10-127 3.22e-06

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: 45.78  E-value: 3.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVarsviiQGLSASPRIEVVGY----AVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQfLPSHP----L 81
Cdd:cd17598    1 ILIVEDSPT------QAEQLKHILEEQGYkvqvARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRK-IKSDPdlkdI 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 494759980  82 PVILVSSLN--LRVFDALAAGAVDFVRKPdaveSRESFLQALTHKIIV 127
Cdd:cd17598   74 PVILLTTLSdpRDVIRGLECGADNFITKP----YDEKYLLSRIKYILV 117
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
 9-138 3.25e-06

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: 46.83  E-value: 3.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLsaspriEVVGYAV----NAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHP-LPV 83
Cdd:COG4567    6 SLLLVDDDEAFARVLARAL------ERRGFEVttaaSVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPdARI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 494759980  84 ILVS---SLNLRVfDALAAGAVDFVRKPDAVESRESFLQALTHKIIVASHARLSRANL 138
Cdd:COG4567   80 VVLTgyaSIATAV-EAIKLGADDYLAKPADADDLLAALERAEGDAPAPPENPMSLDRL 136
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
 9-108 5.79e-06

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: 44.77  E-value: 5.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDD-SAVARSVIIQGLSASPRIEVVGYAVNAMDAktkLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVILVS 87
Cdd:cd17626    2 RILVVDDdAALAEMIGIVLRGEGFDPAFCGDGTQALAA---FREVRPDLVLLDLMLPGIDGIEVCRQIRAESGVPIVMLT 78

                         90       100
                 ....*....|....*....|...
gi 494759980  88 --SLNLRVFDALAAGAVDFVRKP 108
Cdd:cd17626   79 akSDTVDVVLGLESGADDYVAKP 101
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
 10-108 7.34e-06

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: 44.36  E-value: 7.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSASPRIEVVGyAVNAMDAKTkLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVILVSSL 89
Cdd:cd17594    2 VLVVDDDAAMRHLLILYLRERGFDVTAA-ADGAEEARL-MLHRRVDLVLLDLRLGQESGLDLLRTIRARSDVPIIIISGD 79

                         90       100
                 ....*....|....*....|..
gi 494759980  90 NLRVFD---ALAAGAVDFVRKP 108
Cdd:cd17594   80 RRDEIDrvvGLELGADDYLAKP 101
PRK10610 PRK10610
chemotaxis protein CheY;
5-125 8.52e-06

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 44.58  E-value: 8.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   5 NRKIRVLVVDDSAVARSvIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPS---HPL 81
Cdd:PRK10610   3 DKELKFLVVDDFSTMRR-IVRNLLKELGFNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADgamSAL 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 494759980  82 PVILVSSLNLR--VFDALAAGAVDFVRKPDAVESRESFLQALTHKI 125
Cdd:PRK10610  82 PVLMVTAEAKKenIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKL 127
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
 9-108 1.15e-05

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 45.72  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLSASprievvGYAVN----AMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHP-LPV 83
Cdd:PRK11083   5 TILLVEDEQAIADTLVYALQSE------GFTVEwferGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPaLPV 78

                         90       100
                 ....*....|....*....|....*...
gi 494759980  84 ILVSSLNLRVfD---ALAAGAVDFVRKP 108
Cdd:PRK11083  79 IFLTARSDEV-DrlvGLEIGADDYVAKP 105
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
 10-108 1.39e-05

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: 43.26  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSAsprievVGYAV----NAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHP-LPVI 84
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGR------AGYEVrttgNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPdLPII 74

                         90       100
                 ....*....|....*....|....*.
gi 494759980  85 LVSSLN--LRVFDALAAGAVDFVRKP 108
Cdd:cd19928   75 VMSAQNtlMTAVKAAERGAFEYLPKP 100
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
 10-108 1.79e-05

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: 43.52  E-value: 1.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARsVIIQGLSASP-RIEVVGYAVNAMDAktkLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVILVSS 88
Cdd:cd17622    4 LLVEDDPKLAR-LIADFLESHGfNVVVEHRGDRALEV---IAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQGPILLLTA 79

                         90       100
                 ....*....|....*....|..
gi 494759980  89 L--NLRVFDALAAGAVDFVRKP 108
Cdd:cd17622   80 LdsDIDHILGLELGADDYVVKP 101
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
 10-108 1.91e-05

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators similar to Pseudomonas savastanoi blue-light-activated histidine kinase; 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 (HK)/response regulators contain all the elements of a classical TCS in a single polypeptide chain. Pseudomonas savastanoi blue-light-activated histidine kinase is a photosensitive HK and RR that is involved in increased bacterial virulence upon exposure to light. 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: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 43.10  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLsaspriEVVGYAV-NAMDAKTKLQHL----SPDVMTLDVEMPG-INGIDFLKQFLPSHP-LP 82
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVL------EDLGYTVlEAASGDEALDLLesgpDIDLLVTDVIMPGgMNGSQLAEEARRRRPdLK 74

                         90       100
                 ....*....|....*....|....*...
gi 494759980  83 VILVS--SLNLRVFDALAAGaVDFVRKP 108
Cdd:cd18161   75 VLLTSgyAENAIEGGDLAPG-VDVLSKP 101
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
 11-108 1.93e-05

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: 42.82  E-value: 1.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  11 LVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAktkLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVILVSSLN 90
Cdd:cd19936    3 LVDDDRNILTSVSMALEAEGFSVETYTDGASALDG---LNARPPDLAILDIKMPRMDGMELLQRLRQKSTLPVIFLTSKD 79

                         90       100
                 ....*....|....*....|
gi 494759980  91 LRVFD--ALAAGAVDFVRKP 108
Cdd:cd19936   80 DEIDEvfGLRMGADDYITKP 99
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
 10-121 2.17e-05

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: 43.04  E-value: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSASprievvGYAVN-AMDAKTKLQHLS---PDVMTLDVEMPGINGIDFLKQFLPS-HPLPVI 84
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDA------GYVVDvAEDGEEALFQGEeepYDLVVLDLGLPGMDGLSVLRRWRSEgRATPVL 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494759980  85 LV---SSLNLRVfDALAAGAVDFVRKPDAVESRESFLQAL 121
Cdd:cd19934   75 ILtarDSWQDKV-EGLDAGADDYLTKPFHIEELLARLRAL 113
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
 10-121 2.34e-05

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: 43.14  E-value: 2.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSASPRIevVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVILVSSL 89
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYE--VETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTA 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 494759980  90 NLRVFD---ALAAGAVDFVRKPDAVESRESFLQAL 121
Cdd:cd17627   79 RDSVSDrvaGLDAGADDYLVKPFALEELLARVRAL 113
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
 9-108 2.37e-05

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: 42.81  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLSAspRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVILV-- 86
Cdd:cd17563    2 SLLLVDDDEVFAERLARALER--RGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVlt 79

                         90       100
                 ....*....|....*....|....
gi 494759980  87 --SSLNLRVfDALAAGAVDFVRKP 108
Cdd:cd17563   80 gyASIATAV-EAIKLGADDYLAKP 102
PRK10360 PRK10360
transcriptional regulator UhpA;
8-109 2.45e-05

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 44.58  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   8 IRVLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQfLPSHpLPVILVS 87
Cdd:PRK10360   2 ITVALIDDHLIVRSGFAQLLGLEPDLQVVAEFGSGREALAGLPGRGVQVCICDISMPDISGLELLSQ-LPKG-MATIMLS 79

                         90       100
                 ....*....|....*....|....*..
gi 494759980  88 SLN--LRVFDALAAGAVDFVRK---PD 109
Cdd:PRK10360  80 VHDspALVEQALNAGARGFLSKrcsPD 106
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
 10-74 3.16e-05

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: 42.45  E-value: 3.16e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494759980  10 VLVVDDSAVAR---SVIIQGLSAspRIEVVGYAVNAMDAktkLQHLSPDVMTLDVEMPGINGIDFLKQ 74
Cdd:cd17580    1 ILVVDDNEDAAemlALLLELEGA--EVTTAHSGEEALEA---AQRFRPDVILSDIGMPGMDGYELARR 63
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
 9-108 4.04e-05

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: 42.37  E-value: 4.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLSASprievvGYAV----NAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVI 84
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAA------GYAPtllaHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFSDVPII 74

                         90       100
                 ....*....|....*....|....*....
gi 494759980  85 LVSSlnlRVFD-----ALAAGAVDFVRKP 108
Cdd:cd19938   75 MVTA---RVEEidrllGLELGADDYICKP 100
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
 8-88 4.89e-05

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: 42.01  E-value: 4.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   8 IRVLVVDDSAVARSVIIQGLSASPrIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPG-INGIDFLKQFLPSHPLPVILV 86
Cdd:cd17534    1 KKILIVEDEAIIALDLKEILESLG-YEVVGIADSGEEAIELAEENKPDLILMDINLKGdMDGIEAAREIREKFDIPVIFL 79


                 ..
gi 494759980  87 SS 88
Cdd:cd17534   80 TA 81
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
 11-108 1.17e-04

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: 41.10  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  11 LVVDDSAVARSVIIQGLSASprievvGY----AVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQfLPSHP----LP 82
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKE------GYevvtAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRI-LRSDPktssIP 73

                         90       100
                 ....*....|....*....|....*....
gi 494759980  83 VILVSSLNLRvFD---ALAAGAVDFVRKP 108
Cdd:cd19937   74 IIMLTAKGEE-FDkvlGLELGADDYITKP 101
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
 9-101 1.19e-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: 41.27  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIqglSASPRIeVVGYAVNAMDAKTKLQHL---SPDVMTLDVEMPGINGIDFLKQFLPSH-PLPVI 84
Cdd:cd17530    2 RVLVLDDDPFQCMMAA---TILEDL-GPGNVDEADDGREALVILlcnAPDIIICDLKMPDMDGIEFLRHLAESHsNAAVI 77

                         90
                 ....*....|....*..
gi 494759980  85 LVSSLNLRVFDALAAGA 101
Cdd:cd17530   78 LMSGLDGGILESAETLA 94
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
 9-108 1.31e-04

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: 41.13  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLSASprievvGY----AVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQfLPSHP---- 80
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGA------GYevveAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKE-LRKLPaykf 74

                         90       100       110
                 ....*....|....*....|....*....|
gi 494759980  81 LPVILVSSLNLRVF--DALAAGAVDFVRKP 108
Cdd:cd17562   75 TPILMLTTESSDEKkqEGKAAGATGWLVKP 104
pleD PRK09581
response regulator PleD; Reviewed
 9-108 2.01e-04

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 42.97  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLSASpRIEVVgYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQfLPSHPL----PVI 84
Cdd:PRK09581   4 RILVVDDIPANVKLLEAKLLAE-YYTVL-TASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRR-LKSDPAtthiPVV 80

                         90       100
                 ....*....|....*....|....*..
gi 494759980  85 LVSSLNL---RVfDALAAGAVDFVRKP 108
Cdd:PRK09581  81 MVTALDDpedRV-RGLEAGADDFLTKP 106
PRK10643 PRK10643
two-component system response regulator PmrA;
8-121 2.17e-04

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 41.94  E-value: 2.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   8 IRVLVVDDSAVarsvIIQGLSASPRIEvvGYAV----NAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPS-HPLP 82
Cdd:PRK10643   1 MKILIVEDDTL----LLQGLILALQTE--GYACdcasTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKkYTLP 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 494759980  83 VILVS---SLNLRVfDALAAGAVDFVRKPDAVESRESFLQAL 121
Cdd:PRK10643  75 VLILTardTLEDRV-AGLDVGADDYLVKPFALEELHARIRAL 115
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
 9-108 2.55e-04

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: 40.31  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLSASprievvGYAV----NAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQfLPSHP---- 80
Cdd:cd17618    2 TILIVEDEPAIREMIAFNLERA------GFDVveaeDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRR-LKRDEmtrd 74

                         90       100       110
                 ....*....|....*....|....*....|...
gi 494759980  81 LPVILVSSlnlRVFDA-----LAAGAVDFVRKP 108
Cdd:cd17618   75 IPIIMLTA---RGEEEdkvrgLEAGADDYITKP 104
PRK10336 PRK10336
two-component system response regulator QseB;
8-124 2.66e-04

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 41.80  E-value: 2.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   8 IRVLVVDDSAVARSVIIQGLSAsprievVGYAVN----AMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPS-HPLP 82
Cdd:PRK10336   1 MRILLIEDDMLIGDGIKTGLSK------MGFSVDwftqGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKgQREP 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 494759980  83 VILVS---SLNLRVfDALAAGAVDFVRKPDAVESRESFLQALTHK 124
Cdd:PRK10336  75 VLILTardALAERV-EGLRLGADDYLCKPFALIEVAARLEALMRR 118
PRK09483 PRK09483
response regulator; Provisional
 8-111 2.99e-04

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 41.63  E-value: 2.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   8 IRVLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVILVS 87
Cdd:PRK09483   2 INVLLVDDHELVRAGIRRILEDIKGIKVVGEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKILRYTPDVKIIML 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 494759980  88 SLN------LRVFDALAAGAVDFVRKPDAV 111
Cdd:PRK09483  82 TVHtenplpAKVMQAGAAGYLSKGAAPQEV 111
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
 34-108 3.22e-04

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: 39.56  E-value: 3.22e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494759980  34 EVVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLP-VILVSSLNLR--VFDALAAGAVDFVRKP 108
Cdd:cd17565   25 EVVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGkFIMISQVSDKemIGKAYQAGIEFFINKP 102
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
 10-108 3.83e-04

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: 39.57  E-value: 3.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSASpRIEVVGyAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVILVSSL 89
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKW-GYEVVL-IEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISNVPIIFISSR 78

                         90       100
                 ....*....|....*....|.
gi 494759980  90 --NLRVFDALAAGAVDFVRKP 108
Cdd:cd18159   79 ddNMDQVMAINMGGDDYITKP 99
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
 10-108 4.86e-04

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: 39.33  E-value: 4.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAvARSVIIQGLSASPRIEVVgYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVILVSSL 89
Cdd:cd17614    1 ILVVDDEK-PISDILKFNLTKEGYEVV-TAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSNVPIIMLTAK 78

                         90       100
                 ....*....|....*....|.
gi 494759980  90 NLRVFDALA--AGAVDFVRKP 108
Cdd:cd17614   79 DSEVDKVLGleLGADDYVTKP 99
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
 54-108 5.02e-04

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 40.94  E-value: 5.02e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 494759980  54 PDVMTLDVEMPGINGIDFLKQFLPSHPLPVILVSSLNLRV--FDALAAGAVDFVRKP 108
Cdd:PRK10529  46 PDLIILDLGLPDGDGIEFIRDLRQWSAIPVIVLSARSEESdkIAALDAGADDYLSKP 102
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
 10-108 5.14e-04

phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; Helicobacter pylori response regulator hp1043 (HP-RR) is an orphan response regulator which is phosphorylation-independent and is essential for growth. HP-RR functions as a cell growth-associated regulator in the absence of post-translational modification. Members of this subfamily contain REC and DNA-binding output domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 38.95  E-value: 5.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSASprievvGY----AVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVIL 85
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEK------GYqadvAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVI 74

                         90       100
                 ....*....|....*....|....*.
gi 494759980  86 VSSLNLRV---FDALAAGAVDFVRKP 108
Cdd:cd17573   75 VLSDNPKTeqeIEAFKEGADDYIAKP 100
PRK10816 PRK10816
two-component system response regulator PhoP;
8-121 8.82e-04

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 40.11  E-value: 8.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   8 IRVLVVDDSAVAR---SVIIQGLSASprievVGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSH-PLPV 83
Cdd:PRK10816   1 MRVLVVEDNALLRhhlKVQLQDAGHQ-----VDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDvSLPI 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 494759980  84 ILVS---SLNLRVfDALAAGAVDFVRKPDAVESRESFLQAL 121
Cdd:PRK10816  76 LVLTareSWQDKV-EVLSAGADDYVTKPFHIEEVMARMQAL 115
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
 8-121 1.81e-03

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: 37.77  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   8 IRVLVVDDSAVARSVIIQGLSASPrIEVVgYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPV-ILV 86
Cdd:cd17569    1 PTILLVDDEPNILKALKRLLRREG-YEVL-TATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVrILL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494759980  87 ---SSLNLrVFDALAAGAVD-FVRKP-DAVESRESFLQAL 121
Cdd:cd17569   79 tgyADLDA-AIEAINEGEIYrFLTKPwDDEELKETIRQAL 117
PRK15479 PRK15479
transcriptional regulator TctD;
8-121 1.85e-03

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 39.32  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   8 IRVLVVDDSAVARSVIIQGLSASprievvGYAVN----AMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLP-SHPLP 82
Cdd:PRK15479   1 MRLLLAEDNRELAHWLEKALVQN------GFAVDcvfdGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKrGQTLP 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 494759980  83 VILV---SSLNLRVfDALAAGAVDFVRKPDAVESRESFLQAL 121
Cdd:PRK15479  75 VLLLtarSAVADRV-KGLNVGADDYLPKPFELEELDARLRAL 115
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
 36-108 2.00e-03

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: 37.18  E-value: 2.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494759980  36 VGYAVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVILVSSLNLRV--FDALAAGAVDFVRKP 108
Cdd:cd17621   25 VTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARSNVPVIMVTAKDSEIdkVVGLELGADDYVTKP 99
PRK11517 PRK11517
DNA-binding response regulator HprR;
8-108 2.84e-03

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 38.73  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   8 IRVLVVDDSAVARSVIIQGLSASprievvGYAVNAM-DAKTKLqHLSPD----VMTLDVEMPGINGIDFLKQFLPSHPLP 82
Cdd:PRK11517   1 MKILLIEDNQRTQEWVTQGLSEA------GYVIDAVsDGRDGL-YLALKddyaLIILDIMLPGMDGWQILQTLRTAKQTP 73

                         90       100
                 ....*....|....*....|....*....
gi 494759980  83 VILVS---SLNLRVfDALAAGAVDFVRKP 108
Cdd:PRK11517  74 VICLTardSVDDRV-RGLDSGANDYLVKP 101
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
9-125 2.89e-03

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 38.55  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLsaspriEVVGYA-VNAMDAKTKLQHLS---PDVMTLDVEMPGINGIDFLKQF---LPSHPL 81
Cdd:PRK10161   4 RILVVEDEAPIREMVCFVL------EQNGFQpVEAEDYDSAVNQLNepwPDLILLDWMLPGGSGIQFIKHLkreSMTRDI 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 494759980  82 PVILVSSLNL---RVfDALAAGAVDFVRKPDAVESRESFLQALTHKI 125
Cdd:PRK10161  78 PVVMLTARGEeedRV-RGLETGADDYITKPFSPKELVARIKAVMRRI 123
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
 9-123 4.87e-03

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: 36.38  E-value: 4.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSVIIQGLSASprievvGY----AVNAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQflpshplpvI 84
Cdd:cd17553    2 KILIVDDQYGIRILLNEVFNKE------GYqtfqAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKR---------M 66

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494759980  85 LVSSLNLRVFDALAAGAVDFVRkpdavESREsfLQALTH 123
Cdd:cd17553   67 KVIDENIRVIIMTAYGELDMIQ-----ESKE--LGALTH 98
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
 10-108 5.02e-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: 5.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLsASPRIEVVGyAVNAMDAKTKLQHLSPDVMTLDVEMPGINGID---FLKQFLPSHPLPVILV 86
Cdd:cd19926    1 VLVVDDEPDIRELLEITL-GRMGLDVRS-ARNVKEARELLASEPYDLCLTDMRLPDGSGLElvqHIQQRLPQTPVAVITA 78

                         90       100
                 ....*....|....*....|..
gi 494759980  87 SSLNLRVFDALAAGAVDFVRKP 108
Cdd:cd19926   79 YGSLDTAIEALKAGAFDFLTKP 100
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
 9-108 5.21e-03

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: 36.36  E-value: 5.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAV----ARSVIiqglsaspriEVVGYAV-NAMDAKTKLQHLS---PDVMTLDVEMPGINGIDFLKQfLPSHP 80
Cdd:cd17548    1 KILIVEDNPLnmklARDLL----------ESAGYEVlEAADGEEALEIARkekPDLILMDIQLPGMDGLEATRL-LKEDP 69

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 494759980  81 ----LPVILVSSLNLRVfD---ALAAGAVDFVRKP 108
Cdd:cd17548   70 atrdIPVIALTAYAMKG-DrekILEAGCDGYISKP 103
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
 9-87 5.85e-03

phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is a hybrid stress regulator that contains an N-terminal sigma-like (SL) domain and a C-terminal REC domain. Phosphorylation of the REC domain is known to promote binding of the SL domain to an anti-sigma factor. PhyR thus functions as an anti-anti-sigma factor in its phosphorylated state. It is involved in the general stress response. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381095 [Multi-domain]  Cd Length: 117  Bit Score: 36.07  E-value: 5.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVV-DDSAVARSviIQGLSASPRIEVVGYAVNAMDAKTKLQHLSPDVMTLDVEMP-GINGIDFLKQFLPSHPLPVILV 86
Cdd:cd17540    2 RVLIIeDEPLIAMD--LEQIVEDLGHQVVGIARTRDEAVALARRERPDLILADIQLAdGSSGIDAVNEILTTHDVPVIFV 79


                 .
gi 494759980  87 S 87
Cdd:cd17540   80 T 80
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
 8-110 6.96e-03

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 37.60  E-value: 6.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   8 IRVLVVDDSAVARSVIIQGLSASprievvGYAVNAMDAKTKLQHLSP----DVMTLDVEMPGINGIDFLKQFLPSHP-LP 82
Cdd:PRK09836   1 MKLLIVEDEKKTGEYLTKGLTEA------GFVVDLADNGLNGYHLAMtgdyDLIILDIMLPDVNGWDIVRMLRSANKgMP 74

                         90       100       110
                 ....*....|....*....|....*....|.
gi 494759980  83 VILVSSLNL---RVfDALAAGAVDFVRKPDA 110
Cdd:PRK09836  75 ILLLTALGTiehRV-KGLELGADDYLVKPFA 104
PRK10766 PRK10766
two-component system response regulator TorR;
9-115 7.29e-03

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 37.33  E-value: 7.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980   9 RVLVVDDSAVARSViIQGLsasprIEVVGYAV----NAMDAKTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPLPVI 84
Cdd:PRK10766   4 HILVVEDEPVTRAR-LQGY-----FEQEGYTVseaaSGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRSTVGII 77

                         90       100       110
                 ....*....|....*....|....*....|...
gi 494759980  85 LVSSLNLRV--FDALAAGAVDFVRKPdaVESRE 115
Cdd:PRK10766  78 LVTGRTDSIdrIVGLEMGADDYVTKP--LELRE 108
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
 10-108 7.53e-03

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: 35.85  E-value: 7.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSASPRIEVVGYAVNAMDAKTKLQHlspDVMTLDVEMPGINGIDFLKQFLPSH-PLPVILVSS 88
Cdd:cd17616    2 LLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDY---DIILLDLNLPDMSGYEVLRTLRLAKvKTPILILSG 78

                         90       100
                 ....*....|....*....|..
gi 494759980  89 LN--LRVFDALAAGAVDFVRKP 108
Cdd:cd17616   79 LAdiEDKVKGLGFGADDYMTKP 100
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
 10-108 7.55e-03

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: 35.42  E-value: 7.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLSAS-PRIEVVGYAVNAMdakTKLQHLSPDVMTLDVEMPGINGIDFLKQFLPSHPL---PVIL 85
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQgFRVVVIDDPLRAL---TTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALkdtPIIM 77

                         90       100
                 ....*....|....*....|....*.
gi 494759980  86 VSSlNLRVFDALAA---GAVDFVRKP 108
Cdd:cd17602   78 LTG-KDGLVDRIRAkmaGASGYLTKP 102
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
 10-108 7.67e-03

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: 35.45  E-value: 7.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494759980  10 VLVVDDSAVARSVIIQGLS-ASPRIEVVGYAVNAMDAKTKLQHlSPDVMTLDVEMPGINGIDFLKQFLPSHPL---PVIL 85
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRkCSYEVTAASDGLQAWDVLEDEQN-EIDLILTEVDLPVSSGFKLLSYIMRHKICkniPVIM 79

                         90       100
                 ....*....|....*....|....*.
gi 494759980  86 VSS---LNLrVFDALAAGAVDFVRKP 108
Cdd:cd17582   80 MSSqdsVGV-VFKCLSKGAADYLVKP 104
 
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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