NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1674995404|ref|WP_138527384|]
View 

MULTISPECIES: chemotaxis response regulator protein-glutamate methylesterase [unclassified Pseudoalteromonas]

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1-340 1.37e-178

chemotaxis-specific protein-glutamate methyltransferase CheB;


:

Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 498.52  E-value: 1.37e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   1 MINVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMI 80
Cdd:PRK00742    3 KIRVLVVDDSAFMRRLISEILNSDPDIEVVGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRPTPVVMV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404  81 STLTQKGSPITLEALELGAVDFIAKPTSNVRAQMNHYASLVQQKVRIAAGARIRSF-------KKAPPDAKPILTDTKFL 153
Cdd:PRK00742   83 SSLTERGAEITLRALELGAVDFVTKPFLGISLGMDEYKEELAEKVRAAARARVRALppraaaaARAAAAAPAALAAAPLL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 154 LNKVIAIGASTGGTEAIKEVLIKMPVNCP-PIVITQHIPPVFSASFAERMDRTCLINVKEAQHGDKLSSGWAYIAPGGLH 232
Cdd:PRK00742  163 SSKLVAIGTSTGGPEALQKVLTPLPANFPaPILIVQHMPAGFTKSFAERLNRLCQIEVKEAEDGERLKPGHAYIAPGGKH 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 233 LSIQKRGAALYCQLDDSDPVNRHKPAVDVLFDSLVHCGAKNVVATILTGMGADGAKGLLALKQNGAYTLAQDEYSSVVWG 312
Cdd:PRK00742  243 MMVARSGANYRIKLDDGPPVNRHRPSVDVLFRSAAKAAGRNALGVILTGMGRDGAAGLLEMKQAGATTIAQDEASCVVYG 322
                         330       340
                  ....*....|....*....|....*...
gi 1674995404 313 MPKAAIDINAANEVAALDKMAEKLLSHA 340
Cdd:PRK00742  323 MPKAAIEAGAVDEVLPLDQIAERILKEV 350
 
Name Accession Description Interval E-value
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1-340 1.37e-178

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 498.52  E-value: 1.37e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   1 MINVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMI 80
Cdd:PRK00742    3 KIRVLVVDDSAFMRRLISEILNSDPDIEVVGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRPTPVVMV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404  81 STLTQKGSPITLEALELGAVDFIAKPTSNVRAQMNHYASLVQQKVRIAAGARIRSF-------KKAPPDAKPILTDTKFL 153
Cdd:PRK00742   83 SSLTERGAEITLRALELGAVDFVTKPFLGISLGMDEYKEELAEKVRAAARARVRALppraaaaARAAAAAPAALAAAPLL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 154 LNKVIAIGASTGGTEAIKEVLIKMPVNCP-PIVITQHIPPVFSASFAERMDRTCLINVKEAQHGDKLSSGWAYIAPGGLH 232
Cdd:PRK00742  163 SSKLVAIGTSTGGPEALQKVLTPLPANFPaPILIVQHMPAGFTKSFAERLNRLCQIEVKEAEDGERLKPGHAYIAPGGKH 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 233 LSIQKRGAALYCQLDDSDPVNRHKPAVDVLFDSLVHCGAKNVVATILTGMGADGAKGLLALKQNGAYTLAQDEYSSVVWG 312
Cdd:PRK00742  243 MMVARSGANYRIKLDDGPPVNRHRPSVDVLFRSAAKAAGRNALGVILTGMGRDGAAGLLEMKQAGATTIAQDEASCVVYG 322
                         330       340
                  ....*....|....*....|....*...
gi 1674995404 313 MPKAAIDINAANEVAALDKMAEKLLSHA 340
Cdd:PRK00742  323 MPKAAIEAGAVDEVLPLDQIAERILKEV 350
CheB_Rec cd16432
Chemotaxis response regulator protein-glutamate methylesterase, CheB, with N-terminal REC ...
157-339 1.41e-98

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: 289.26  E-value: 1.41e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 157 VIAIGASTGGTEAIKEVLIKMPVNCP-PIVITQHIPPVFSASFAERMDRTCLINVKEAQHGDKLSSGWAYIAPGGLHLSI 235
Cdd:cd16432     1 LVAIGASTGGPQALQEILSALPADFPaPILIVQHMPPGFTKSFAERLNRLSALPVKEAEDGEPLEPGTVYIAPGGYHLVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 236 QKRGAALYCQLDDSDPVNRHKPAVDVLFDSLVHCGAKNVVATILTGMGADGAKGLLALKQNGAYTLAQDEYSSVVWGMPK 315
Cdd:cd16432    81 ERRGGGGRIRLSDGPPVNGHRPSVDVLFRSAAEVYGARALGVILTGMGRDGAEGLLALKEAGGYTIAQDEASSVVYGMPK 160
                         170       180
                  ....*....|....*....|....
gi 1674995404 316 AAIDINAANEVAALDKMAEKLLSH 339
Cdd:cd16432   161 AAIEAGAADEVLPLDEIAAAILRL 184
CheB COG2201
Chemotaxis response regulator CheB, contains REC and protein-glutamate methylesterase domains ...
155-340 2.01e-92

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


Pssm-ID: 441803  Cd Length: 193  Bit Score: 273.89  E-value: 2.01e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 155 NKVIAIGASTGGTEAIKEVLIKMPVNCP-PIVITQHIPPVFSASFAERMDRTCLINVKEAQHGDKLSSGWAYIAPGGLHL 233
Cdd:COG2201     3 FKVVAIGASTGGPEALEEVLSALPADFPaPIVIVQHMPPGFTSSLAERLNRLTALPVKEAEDGERLEPGHVYIAPGGRHL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 234 SIQKRGAaLYCQLDDSDPVNRHKPAVDVLFDSLVHCGAKNVVATILTGMGADGAKGLLALKQNGAYTLAQDEYSSVVWGM 313
Cdd:COG2201    83 EVERSGG-YRLRLSDGPPVNGHRPSVDVLFRSLAEVYGERAVGVILTGMGSDGAEGLKAIKEAGGLTIAQDEESCVVYGM 161
                         170       180
                  ....*....|....*....|....*..
gi 1674995404 314 PKAAIDINAANEVAALDKMAEKLLSHA 340
Cdd:COG2201   162 PRAAIEAGAVDEVLPLEEIAAALLRLL 188
CheB_methylest pfam01339
CheB methylesterase;
158-336 6.73e-81

CheB methylesterase;


Pssm-ID: 460166  Cd Length: 178  Bit Score: 243.87  E-value: 6.73e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 158 IAIGASTGGTEAIKEVLIKMPVNCP-PIVITQHIPPVFSASFAERMDRTCLINVKEAQHGDKLSSGWAYIAPGGLHLSIQ 236
Cdd:pfam01339   1 VAIGASTGGPEALEELLPALPADLPaAIVVVQHMPPGFTSSLAERLNRLSALPVKEAEDGEPLEPGTVYIAPGGYHLLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 237 KRGAALYcqlDDSDPVNRHKPAVDVLFDSLV-HCGAKNVVATILTGMGADGAKGLLALKQNGAYTLAQDEYSSVVWGMPK 315
Cdd:pfam01339  81 DGRGPYR---SDGPPVNGHRPSIDVLFRSLAeAYGGKRAIGVILTGMGSDGAAGLKAIKEAGGLTIAQDPATAVVYGMPR 157
                         170       180
                  ....*....|....*....|.
gi 1674995404 316 AAIDINAANEVAALDKMAEKL 336
Cdd:pfam01339 158 AAIEAGAADFVLPLEEIAAEL 178
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
2-106 4.83e-16

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


Pssm-ID: 131922 [Multi-domain]  Cd Length: 262  Bit Score: 76.76  E-value: 4.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   2 INVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMR--LRPMP-VV 78
Cdd:TIGR02875   3 IRIVIADDNKEFCNLLKEYLAAQPDMEVVGVAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNEieLSARPrVI 82
                          90       100
                  ....*....|....*....|....*...
gi 1674995404  79 MISTLTQKGspITLEALELGAVDFIAKP 106
Cdd:TIGR02875  83 MLSAFGQEK--ITQRAVALGADYYVLKP 108
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
2-58 8.84e-11

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: 56.81  E-value: 8.84e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1674995404    2 INVLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMP 58
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEG--YEVDEATDGEEALELLKEEKPDLILLDIMMP 55
 
Name Accession Description Interval E-value
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1-340 1.37e-178

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 498.52  E-value: 1.37e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   1 MINVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMI 80
Cdd:PRK00742    3 KIRVLVVDDSAFMRRLISEILNSDPDIEVVGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRPTPVVMV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404  81 STLTQKGSPITLEALELGAVDFIAKPTSNVRAQMNHYASLVQQKVRIAAGARIRSF-------KKAPPDAKPILTDTKFL 153
Cdd:PRK00742   83 SSLTERGAEITLRALELGAVDFVTKPFLGISLGMDEYKEELAEKVRAAARARVRALppraaaaARAAAAAPAALAAAPLL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 154 LNKVIAIGASTGGTEAIKEVLIKMPVNCP-PIVITQHIPPVFSASFAERMDRTCLINVKEAQHGDKLSSGWAYIAPGGLH 232
Cdd:PRK00742  163 SSKLVAIGTSTGGPEALQKVLTPLPANFPaPILIVQHMPAGFTKSFAERLNRLCQIEVKEAEDGERLKPGHAYIAPGGKH 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 233 LSIQKRGAALYCQLDDSDPVNRHKPAVDVLFDSLVHCGAKNVVATILTGMGADGAKGLLALKQNGAYTLAQDEYSSVVWG 312
Cdd:PRK00742  243 MMVARSGANYRIKLDDGPPVNRHRPSVDVLFRSAAKAAGRNALGVILTGMGRDGAAGLLEMKQAGATTIAQDEASCVVYG 322
                         330       340
                  ....*....|....*....|....*...
gi 1674995404 313 MPKAAIDINAANEVAALDKMAEKLLSHA 340
Cdd:PRK00742  323 MPKAAIEAGAVDEVLPLDQIAERILKEV 350
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
2-340 2.38e-138

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 395.79  E-value: 2.38e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   2 INVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMIS 81
Cdd:PRK12555    1 MRIGIVNDSPLAVEALRRALARDPDHEVVWVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAERPCPILIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404  82 TLTQKGSPITLEALELGAVDFIAKPTSNVRAQMNHYASLVQQKVRIAAGARIRSFKKAPPDAKPILTDTKfLLNKVIAIG 161
Cdd:PRK12555   81 SLTERNASRVFEAMGAGALDAVDTPTLGIGAGLEEYAAELLAKIDQIGRLLGRRLAPAAAPAAASAAPFR-TTPRLVAIG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 162 ASTGGTEAIKEVLIKMPVNCP-PIVITQHIPPVFSASFAERMDRTCLINVKEAQHGDKLSSGWAYIAPGGLHLSIQKRGA 240
Cdd:PRK12555  160 ASAGGPAALAVLLGGLPADFPaAIVIVQHVDAAFAAGMAEWLDGQTALPVREAREGERPQPGHVLLAPTNDHLRLTRDGA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 241 alyCQLDDSDPVNRHKPAVDVLFDSLVHCGAKNVVATILTGMGADGAKGLLALKQNGAYTLAQDEYSSVVWGMPKAAIDI 320
Cdd:PRK12555  240 ---LRYTREPPVNPYRPSVDVFFESVAQHWGGNAIGVLLTGMGRDGARGLKAMRQAGAHTIAQDEASSAVYGMPKAAAAL 316
                         330       340
                  ....*....|....*....|
gi 1674995404 321 NAANEVAALDKMAEKLLSHA 340
Cdd:PRK12555  317 GAASEVLPLERIAPRLIALF 336
CheB_Rec cd16432
Chemotaxis response regulator protein-glutamate methylesterase, CheB, with N-terminal REC ...
157-339 1.41e-98

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: 289.26  E-value: 1.41e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 157 VIAIGASTGGTEAIKEVLIKMPVNCP-PIVITQHIPPVFSASFAERMDRTCLINVKEAQHGDKLSSGWAYIAPGGLHLSI 235
Cdd:cd16432     1 LVAIGASTGGPQALQEILSALPADFPaPILIVQHMPPGFTKSFAERLNRLSALPVKEAEDGEPLEPGTVYIAPGGYHLVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 236 QKRGAALYCQLDDSDPVNRHKPAVDVLFDSLVHCGAKNVVATILTGMGADGAKGLLALKQNGAYTLAQDEYSSVVWGMPK 315
Cdd:cd16432    81 ERRGGGGRIRLSDGPPVNGHRPSVDVLFRSAAEVYGARALGVILTGMGRDGAEGLLALKEAGGYTIAQDEASSVVYGMPK 160
                         170       180
                  ....*....|....*....|....
gi 1674995404 316 AAIDINAANEVAALDKMAEKLLSH 339
Cdd:cd16432   161 AAIEAGAADEVLPLDEIAAAILRL 184
CheB COG2201
Chemotaxis response regulator CheB, contains REC and protein-glutamate methylesterase domains ...
155-340 2.01e-92

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


Pssm-ID: 441803  Cd Length: 193  Bit Score: 273.89  E-value: 2.01e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 155 NKVIAIGASTGGTEAIKEVLIKMPVNCP-PIVITQHIPPVFSASFAERMDRTCLINVKEAQHGDKLSSGWAYIAPGGLHL 233
Cdd:COG2201     3 FKVVAIGASTGGPEALEEVLSALPADFPaPIVIVQHMPPGFTSSLAERLNRLTALPVKEAEDGERLEPGHVYIAPGGRHL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 234 SIQKRGAaLYCQLDDSDPVNRHKPAVDVLFDSLVHCGAKNVVATILTGMGADGAKGLLALKQNGAYTLAQDEYSSVVWGM 313
Cdd:COG2201    83 EVERSGG-YRLRLSDGPPVNGHRPSVDVLFRSLAEVYGERAVGVILTGMGSDGAEGLKAIKEAGGLTIAQDEESCVVYGM 161
                         170       180
                  ....*....|....*....|....*..
gi 1674995404 314 PKAAIDINAANEVAALDKMAEKLLSHA 340
Cdd:COG2201   162 PRAAIEAGAVDEVLPLEEIAAALLRLL 188
CheB_methylest pfam01339
CheB methylesterase;
158-336 6.73e-81

CheB methylesterase;


Pssm-ID: 460166  Cd Length: 178  Bit Score: 243.87  E-value: 6.73e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 158 IAIGASTGGTEAIKEVLIKMPVNCP-PIVITQHIPPVFSASFAERMDRTCLINVKEAQHGDKLSSGWAYIAPGGLHLSIQ 236
Cdd:pfam01339   1 VAIGASTGGPEALEELLPALPADLPaAIVVVQHMPPGFTSSLAERLNRLSALPVKEAEDGEPLEPGTVYIAPGGYHLLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 237 KRGAALYcqlDDSDPVNRHKPAVDVLFDSLV-HCGAKNVVATILTGMGADGAKGLLALKQNGAYTLAQDEYSSVVWGMPK 315
Cdd:pfam01339  81 DGRGPYR---SDGPPVNGHRPSIDVLFRSLAeAYGGKRAIGVILTGMGSDGAAGLKAIKEAGGLTIAQDPATAVVYGMPR 157
                         170       180
                  ....*....|....*....|.
gi 1674995404 316 AAIDINAANEVAALDKMAEKL 336
Cdd:pfam01339 158 AAIEAGAADFVLPLEEIAAEL 178
CheB_like cd16351
methylesterase CheB domain family; This family contains the methylesterase CheB (EC 3.1.1.61; ...
157-337 9.21e-63

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: 197.79  E-value: 9.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 157 VIAIGASTGGTEAIKEVLIKMPVNCP-PIVITQHIPPVFSASFAERMDRTCLINVKEAQHGDKLSSGWAYIAPGGLHLSI 235
Cdd:cd16351     1 IVGIGASTGGLEALEHLFEQLPIHSGlVYVVIQHMPPGFTSSMAERLGKKTKVGVKEAEDGEPVEPGTIYIAPGDTHINL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 236 QKRGAALYCQLDDSDPVNRHKPAVDVLFDSLVHCGAKNVVATILTGMGADGAKGLLALKQNGAYTLAQDEYSSVVWGMPK 315
Cdd:cd16351    81 ENGKGFKVQELSNDTGINNLRPPVDHFFSSLAKYNKEKSIAVILTGMGNDGSSGLSYVYDTGGTVIAQTEESCVVFGMPN 160
                         170       180
                  ....*....|....*....|..
gi 1674995404 316 AAIDINAANEVAALDKMAEKLL 337
Cdd:cd16351   161 YAIQTGKVDHVVRPEEMASLFE 182
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
2-126 1.29e-59

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: 187.60  E-value: 1.29e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   2 INVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMIS 81
Cdd:cd17541     1 IRVLIVDDSAVMRKLLSRILESDPDIEVVGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERPTPVVMVS 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1674995404  82 TLTQKGSPITLEALELGAVDFIAKPTSNVRAQMNHYASLVQQKVR 126
Cdd:cd17541    81 SLTEEGAEITLEALELGAVDFIAKPSGGISLDLEEIAEELIEKIK 125
CheB cd16433
Chemotaxis response regulator protein-glutamate methylesterase, CheB; This family contains the ...
157-338 4.88e-52

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: 170.25  E-value: 4.88e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 157 VIAIGASTGGTEAIKEVLIKMPVNCP-PIVITQHIPPVFSASFAERMDRTCLINVKEAQHGDKLSSGWAYIAPGGLHLSI 235
Cdd:cd16433     1 IVVIGASAGGLEALLELLSALPADFPaPVLVVLHRPPDSPSVLPELLSRRTPLPVKEAEDGEPIEPGTIYVAPPDYHLLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 236 QKRGaalYCQLDDSDPVNRHKPAVDVLFDSLVHCGAKNVVATILTGMGADGAKGLLALKQNGAYTLAQDEYSSVVWGMPK 315
Cdd:cd16433    81 EDDG---TFSLSRGPKVNFSRPSIDVLFRSAADAYGPRVIGVVLTGANDDGAAGLAAIKRAGGLTIVQDPATAEVPSMPR 157
                         170       180
                  ....*....|....*....|...
gi 1674995404 316 AAIDINAANEVAALDKMAEKLLS 338
Cdd:cd16433   158 AALAAVAVDHVLPLAEIAALLVR 180
CheB-CheR_fusion cd16434
Chemotaxis response regulator protein-glutamate methylesterase, CheB, fused with CheR domain; ...
157-339 3.77e-35

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: 126.33  E-value: 3.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 157 VIAIGASTGGTEAIKEVLIKMPVNCP-PIVITQHIPPVFSASFAERMDRTCLINVKEAQHGDKLSSGWAYIAPGGLHLSI 235
Cdd:cd16434     1 VVGIGASAGGLEALEEFFSALPADSGmAFVVVQHLSPDHKSLLAELLARHTSMPVVEAEDGMRVEPNHVYVIPPGKDLTI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404 236 QKRgaALycQLDDSDPVNRHKPAVDVLFDSLVHCGAKNVVATILTGMGADGAKGLLALKQNGAYTLAQDEYSSVVWGMPK 315
Cdd:cd16434    81 EDG--RL--RLSPPDEPRGPRLPIDVFFRSLAEDQGERAIGVILSGTGSDGTLGLKAIKEAGGLVLAQDPETAKFDGMPR 156
                         170       180
                  ....*....|....*....|....
gi 1674995404 316 AAIDINAANEVAALDKMAEKLLSH 339
Cdd:cd16434   157 SAIATGLVDFVLPPEEIAAELLAY 180
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
3-106 2.03e-28

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: 106.01  E-value: 2.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   3 NVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMIS 81
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEAGFEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPdTKIIILS 80
                          90       100
                  ....*....|....*....|....*
gi 1674995404  82 TLTQKgsPITLEALELGAVDFIAKP 106
Cdd:COG4753    81 GYSDF--EYAQEAIKLGADDYLLKP 103
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
1-106 2.80e-27

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 107.21  E-value: 2.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   1 MINVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMP-VVM 79
Cdd:COG3279     1 MMKILIVDDEPLARERLERLLEKYPDLEVVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPpIIF 80
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  80 ISTLTQKgspiTLEALELGAVDFIAKP 106
Cdd:COG3279    81 TTAYDEY----ALEAFEVNAVDYLLKP 103
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
4-106 2.10e-25

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: 98.38  E-value: 2.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQasDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMIST 82
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEK--EGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPtTPVIILTA 78
                          90       100
                  ....*....|....*....|....
gi 1674995404  83 LTQKgsPITLEALELGAVDFIAKP 106
Cdd:pfam00072  79 HGDE--DDAVEALEAGADDFLSKP 100
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
3-106 2.27e-25

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


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 98.67  E-value: 2.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   3 NVLIIDDSPLIRGLLTEILQQASDINVVGCAeDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPM---PVVM 79
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRSAGYLEVVSFT-DPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLedvPIVM 80
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  80 ISTLTQKgsPITLEALELGAVDFIAKP 106
Cdd:cd17551    81 ITADTDR--EVRLRALEAGATDFLTKP 105
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
2-106 1.80e-24

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: 96.19  E-value: 1.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   2 INVLIIDDSPLIRGLLTEILQQASdINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMI 80
Cdd:cd17542     1 KKVLIVDDAAFMRMMLKDILTKAG-YEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPnAKVIMC 79
                          90       100
                  ....*....|....*....|....*.
gi 1674995404  81 STLTQKgsPITLEALELGAVDFIAKP 106
Cdd:cd17542    80 SAMGQE--EMVKEAIKAGAKDFIVKP 103
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
1-106 2.12e-24

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: 97.67  E-value: 2.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   1 MINVLIIDDSPLIRGLLTEILQQAsDINVVgCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISF---LKNLMRLRPMPV 77
Cdd:COG3706     1 PARILVVDDDPTNRKLLRRLLEAA-GYEVV-EAADGEEALELLQEHRPDLILLDLEMPDMDGLELcrrLRADPRTADIPI 78
                          90       100
                  ....*....|....*....|....*....
gi 1674995404  78 VMISTLTQKGSpiTLEALELGAVDFIAKP 106
Cdd:COG3706    79 IFLTALDDEED--RARALEAGADDYLTKP 105
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1-123 2.36e-24

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 96.58  E-value: 2.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   1 MINVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNL-MRLRPMPVVM 79
Cdd:COG4565     3 MIRVLIVEDDPMVAELLRRYLERLPGFEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELrARGPDVDVIV 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1674995404  80 IStlTQKGSPITLEALELGAVDFIAKPTS--NVRAQMNHYASLVQQ 123
Cdd:COG4565    83 IT--AARDPETVREALRAGVVDYLIKPFTfeRLREALERYLEYRRL 126
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
5-106 7.58e-24

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: 93.83  E-value: 7.58e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   5 LIIDDSPLIRGLLTEILQQASDInvVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMISTL 83
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYE--VDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPdIPVIVLTAK 78
                          90       100
                  ....*....|....*....|...
gi 1674995404  84 TQKgsPITLEALELGAVDFIAKP 106
Cdd:cd00156    79 ADE--EDAVRALELGADDYLVKP 99
Spo0A COG5801
Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell ...
1-106 6.70e-23

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


Pssm-ID: 444503 [Multi-domain]  Cd Length: 264  Bit Score: 96.02  E-value: 6.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   1 MINVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNL--MRLRPMP-V 77
Cdd:COG5801     4 KIKVLIADDNREFCELLEEYLSSQPDMEVVGVAYNGLEALELIEEKKPDVVILDIIMPHLDGLGVLEKLreMNLEKRPkV 83
                          90       100
                  ....*....|....*....|....*....
gi 1674995404  78 VMISTLTQKGspITLEALELGAVDFIAKP 106
Cdd:COG5801    84 IMLTAFGQED--ITQRAVELGADYYILKP 110
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-106 8.92e-23

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: 98.11  E-value: 8.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   1 MINVLIIDDSPLIRGLLTEILQQAsDINVVgCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVM 79
Cdd:COG2204     2 MARILVVDDDPDIRRLLKELLERA-GYEVE-TAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPdLPVIL 79
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  80 ISTLTQkgSPITLEALELGAVDFIAKP 106
Cdd:COG2204    80 LTGYGD--VETAVEAIKAGAFDYLTKP 104
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1-106 1.66e-22

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: 93.48  E-value: 1.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   1 MINVLIIDDSPLIRGLLTEILQQAsDINVVgCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNL-MRLRPMPVVM 79
Cdd:COG0745     1 MPRILVVEDDPDIRELLADALERE-GYEVD-TAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLrARPSDIPIIM 78
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  80 ISTLTQKGSpiTLEALELGAVDFIAKP 106
Cdd:COG0745    79 LTARDDEED--RVRGLEAGADDYLTKP 103
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1-106 4.74e-22

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: 89.91  E-value: 4.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   1 MINVLIIDDSPLIRGLLTEILQQAsDINVVgCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISF---LKNLMRLRPMPV 77
Cdd:COG0784     5 GKRILVVDDNPDNRELLRRLLERL-GYEVT-TAEDGAEALELLRAGPPDLILLDINMPGMDGLELlrrIRALPRLPDIPI 82
                          90       100
                  ....*....|....*....|....*....
gi 1674995404  78 VMISTLTQKGspITLEALELGAVDFIAKP 106
Cdd:COG0784    83 IALTAYADEE--DRERALEAGADDYLTKP 109
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
4-108 1.67e-21

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: 88.16  E-value: 1.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQAS-DINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMIS 81
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIDWEElGFEVVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPdIKIIILS 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1674995404  82 -----TLTQKgspitleALELGAVDFIAKPTS 108
Cdd:cd17536    81 gyddfEYAQK-------AIRLGVVDYLLKPVD 105
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
3-106 1.90e-21

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: 90.99  E-value: 1.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   3 NVLIIDDSPLIRGLLTEILQQAsDINVVgCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISF---LKNLMRLRPMPVVM 79
Cdd:COG3437     8 TVLIVDDDPENLELLRQLLRTL-GYDVV-TAESGEEALELLLEAPPDLILLDVRMPGMDGFELlrlLRADPSTRDIPVIF 85
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  80 ISTLTQKGSpiTLEALELGAVDFIAKP 106
Cdd:COG3437    86 LTALADPED--RERALEAGADDYLTKP 110
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
2-106 9.86e-21

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: 85.74  E-value: 9.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   2 INVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNL--MRLRPMP-VV 78
Cdd:cd17561     2 IKVLIADDNREFVQLLEEYLNSQPDMEVVGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLrrMRLEKRPkII 81
                          90       100
                  ....*....|....*....|....*...
gi 1674995404  79 MISTLTQKGspITLEALELGAVDFIAKP 106
Cdd:cd17561    82 MLTAFGQED--ITQRAVELGASYYILKP 107
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
4-108 1.12e-20

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: 86.03  E-value: 1.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMIST 82
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLESEPDIEVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPdLKVIVLTA 80
                          90       100
                  ....*....|....*....|....*.
gi 1674995404  83 LTQKGspITLEALELGAVDFIAKPTS 108
Cdd:cd17535    81 HDDPE--YVLRALKAGAAGYLLKDSS 104
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
4-111 3.15e-20

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: 84.51  E-value: 3.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMISTL 83
Cdd:cd17532     1 ALIVDDEPLAREELRYLLEEHPDIEIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFVTA 80
                          90       100
                  ....*....|....*....|....*...
gi 1674995404  84 TQKgspITLEALELGAVDFIAKPTSNVR 111
Cdd:cd17532    81 YDE---YAVEAFELNAVDYLLKPFSEER 105
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1-106 8.64e-20

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: 85.78  E-value: 8.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   1 MINVLIIDDSPLIRGLLTEILQQASdINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMi 80
Cdd:COG3707     3 GLRVLVVDDEPLRRADLREGLREAG-YEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERPAPVIL- 80
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  81 stLTQKGSPITLE-ALELGAVDFIAKP 106
Cdd:COG3707    81 --LTAYSDPELIErALEAGVSAYLVKP 105
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
4-108 1.71e-19

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: 82.54  E-value: 1.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQqasDIN-VVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMIS 81
Cdd:cd17550     1 ILIVDDEEDIRESLSGILE---DEGyEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPdLPVIMIS 77
                          90       100
                  ....*....|....*....|....*...
gi 1674995404  82 TltqKGSPIT-LEALELGAVDFIAKPTS 108
Cdd:cd17550    78 G---HGTIETaVKATKLGAYDFIEKPLS 102
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
1-69 2.21e-18

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: 79.94  E-value: 2.21e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1674995404   1 MINVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNL 69
Cdd:COG2197     1 MIRVLIVDDHPLVREGLRALLEAEPDIEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
5-106 1.07e-17

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: 77.06  E-value: 1.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   5 LIIDDSPLIRGLLTEILQQAsDINVVgCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMistL 83
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKE-GYEVD-TAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSdIPIIM---L 75
                          90       100
                  ....*....|....*....|....
gi 1674995404  84 TQKGSPIT-LEALELGAVDFIAKP 106
Cdd:cd17574    76 TAKDEEEDkVLGLELGADDYITKP 99
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
4-108 3.53e-17

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: 76.30  E-value: 3.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMISTL 83
Cdd:cd19932     3 VLIAEDEALIRMDLREMLEEAG-YEVVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENIAPIVLLTAY 81
                          90       100
                  ....*....|....*....|....*
gi 1674995404  84 TQKgsPITLEALELGAVDFIAKPTS 108
Cdd:cd19932    82 SQQ--DLVERAKEAGAMAYLVKPFS 104
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
4-106 5.11e-17

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: 75.80  E-value: 5.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILqqASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMistL 83
Cdd:cd17623     1 ILLIDDDRELTELLTEYL--EMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTSQVPVLM---L 75
                          90       100
                  ....*....|....*....|....
gi 1674995404  84 TQKGSPIT-LEALELGAVDFIAKP 106
Cdd:cd17623    76 TARGDDIDrILGLELGADDYLPKP 99
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
4-109 5.32e-17

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: 76.37  E-value: 5.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQAsDINVVGCAeDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMIst 82
Cdd:cd17549     1 VLLVDDDADVREALQQTLELA-GFRVRAFA-DAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPdLPVILI-- 76
                          90       100
                  ....*....|....*....|....*...
gi 1674995404  83 lTQKGS-PITLEALELGAVDFIAKPTSN 109
Cdd:cd17549    77 -TGHGDvPMAVEAMRAGAYDFLEKPFDP 103
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
4-106 1.11e-16

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: 74.47  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISF---LKNLMRLRPMPVVMI 80
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAG--YRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVcrrLKADPATRHIPVIFL 78
                          90       100
                  ....*....|....*....|....*.
gi 1674995404  81 STLTQKGSpiTLEALELGAVDFIAKP 106
Cdd:cd19920    79 TALTDTED--KVKGFELGAVDYITKP 102
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
2-106 4.83e-16

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


Pssm-ID: 131922 [Multi-domain]  Cd Length: 262  Bit Score: 76.76  E-value: 4.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   2 INVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMR--LRPMP-VV 78
Cdd:TIGR02875   3 IRIVIADDNKEFCNLLKEYLAAQPDMEVVGVAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNEieLSARPrVI 82
                          90       100
                  ....*....|....*....|....*...
gi 1674995404  79 MISTLTQKGspITLEALELGAVDFIAKP 106
Cdd:TIGR02875  83 MLSAFGQEK--ITQRAVALGADYYVLKP 108
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
2-106 4.97e-15

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: 70.44  E-value: 4.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   2 INVLIIDDSPLIRGLLTEILQQAsDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLM---RLRPMPVV 78
Cdd:cd19923     1 MKVLVVDDFSTMRRIIKNLLKEL-GFNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRadgALSHLPVL 79
                          90       100
                  ....*....|....*....|....*...
gi 1674995404  79 MISTLTQKGSPItlEALELGAVDFIAKP 106
Cdd:cd19923    80 MVTAEAKKENVI--AAAQAGVNNYIVKP 105
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
3-109 6.10e-15

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: 70.36  E-value: 6.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   3 NVLIIDDSPLIRGLLTEILQQASdINVVgCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMR---LRPMPVVM 79
Cdd:cd17618     2 TILIVEDEPAIREMIAFNLERAG-FDVV-EAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRdemTRDIPIIM 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1674995404  80 istLTQKGSPI-TLEALELGAVDFIAKPTSN 109
Cdd:cd17618    80 ---LTARGEEEdKVRGLEAGADDYITKPFSP 107
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
4-106 1.40e-14

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: 68.68  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGisF-----LKNLMRLRPMPVV 78
Cdd:cd17538     2 ILVVDDEPANRELLEALLSAEG--YEVLTADSGQEALALAEEELPDLILLDVMMPGMDG--FevcrrLKEDPETRHIPVI 77
                          90       100
                  ....*....|....*....|....*...
gi 1674995404  79 MISTLTQKGSPItlEALELGAVDFIAKP 106
Cdd:cd17538    78 MITALDDREDRI--RGLEAGADDFLSKP 103
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
4-108 1.81e-14

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: 68.84  E-value: 1.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMIstL 83
Cdd:cd19930     1 VLIAEDQEMVRGALAALLELEDDLEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLI--V 78
                          90       100
                  ....*....|....*....|....*.
gi 1674995404  84 TQKGSPITLE-ALELGAVDFIAKPTS 108
Cdd:cd19930    79 TTFGRPGYFRrALAAGVDGYVLKDRP 104
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
2-108 1.85e-14

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: 68.72  E-value: 1.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   2 INVLIIDDSPLIRGLLTEILQQASDINVVGcAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLR-PMPVVMI 80
Cdd:cd17593     1 MKVLICDDSSMARKQLARALPADWDVEITF-AENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQlETKVIVV 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1674995404  81 STLTQKgspitlEA----LELGAVDFIAKPTS 108
Cdd:cd17593    80 SGDVQP------EAkervLELGALAFLKKPFD 105
PRK11697 PRK11697
two-component system response regulator BtsR;
1-106 4.22e-14

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 70.65  E-value: 4.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   1 MINVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKnlMrLRP--MP-V 77
Cdd:PRK11697    1 MIKVLIVDDEPLAREELRELLQEEGDIEIVGECSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELVG--M-LDPehMPyI 77
                          90       100
                  ....*....|....*....|....*....
gi 1674995404  78 VMISTLTQkgspITLEALELGAVDFIAKP 106
Cdd:PRK11697   78 VFVTAFDE----YAIKAFEEHAFDYLLKP 102
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
3-81 1.57e-13

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: 66.09  E-value: 1.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   3 NVLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMIS 81
Cdd:cd17554     2 KILVVDDEENIRELYKEELEDEG--YEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPdLPVIICT 79
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
4-106 2.20e-13

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: 65.69  E-value: 2.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQaSDINVVGcAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMISt 82
Cdd:cd17555     3 ILVIDDDEVVRESIAAYLED-SGFQVLQ-AADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPdTPVIVVS- 79
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  83 ltqkGSPI---TLEALELGAVDFIAKP 106
Cdd:cd17555    80 ----GAGVmsdAVEALRLGAWDYLTKP 102
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
3-108 5.06e-13

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: 66.48  E-value: 5.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   3 NVLIIDDSPLIRGLLTEILQQASDinVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMis 81
Cdd:COG4567     6 SLLLVDDDEAFARVLARALERRGF--EVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPdARIVV-- 81
                          90       100
                  ....*....|....*....|....*...
gi 1674995404  82 tLTQKGSPIT-LEALELGAVDFIAKPTS 108
Cdd:COG4567    82 -LTGYASIATaVEAIKLGADDYLAKPAD 108
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
4-106 1.40e-12

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: 63.64  E-value: 1.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQAsDINVVgCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNL----MRLRPMPVVM 79
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKL-GYEVD-VAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIreleGGGRRTPIIA 78
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  80 ISTLTQKGSpiTLEALELGAVDFIAKP 106
Cdd:cd17546    79 LTANALEED--REKCLEAGMDDYLSKP 103
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
2-106 1.55e-12

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: 63.42  E-value: 1.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   2 INVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMIS 81
Cdd:cd19925     1 INVLIVEDDPMVAEIHRAYVEQVPGFTVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVV 80
                          90       100
                  ....*....|....*....|....*
gi 1674995404  82 TLTQKGSPITlEALELGAVDFIAKP 106
Cdd:cd19925    81 TAANDVETVR-EALRLGVVDYLIKP 104
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
4-159 1.69e-12

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: 65.51  E-value: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQqASDINVVGCAedpyQAREMIKKLNPD---VLTLDVEMPKMDGISFLKNLMRLR-PMPVVM 79
Cdd:COG4566     2 VYIVDDDEAVRDSLAFLLE-SAGLRVETFA----SAEAFLAALDPDrpgCLLLDVRMPGMSGLELQEELAARGsPLPVIF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404  80 IstlTQKGS-PITLEALELGAVDFIAKPTSNV-------RAQMNHYASLVQQKVRIAAGARIRSfkkappdakpiLTD-- 149
Cdd:COG4566    77 L---TGHGDvPMAVRAMKAGAVDFLEKPFDDQalldavrRALARDRARRAERARRAELRARLAS-----------LTPre 142
                         170
                  ....*....|....*..
gi 1674995404 150 -------TKFLLNKVIA 159
Cdd:COG4566   143 revldlvVAGLSNKQIA 159
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
4-109 1.99e-12

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: 63.03  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASDInvVGCAEDPYQAREMI--KKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMIS 81
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQ--VTTCTDAEEALSMLreNKDEFDLVITDVHMPDMDGFEFLELIRLEMDLPVIMMS 78
                          90       100
                  ....*....|....*....|....*....
gi 1674995404  82 TltqKGSPIT-LEALELGAVDFIAKPTSN 109
Cdd:cd17584    79 A---DGSTSTvMKGLAHGACDYLLKPVSI 104
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
5-108 4.91e-12

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: 61.91  E-value: 4.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   5 LIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMR---LRPMPVVMis 81
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEG--YEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSdpkTSSIPIIM-- 76
                          90       100
                  ....*....|....*....|....*...
gi 1674995404  82 tLTQKGSPI-TLEALELGAVDFIAKPTS 108
Cdd:cd19937    77 -LTAKGEEFdKVLGLELGADDYITKPFS 103
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
1-106 5.23e-12

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 64.82  E-value: 5.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   1 MINVLIIDDSPLIRGLLTEILQQASdINVVgCAEDPYQAREMIKKlNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMi 80
Cdd:PRK10955    1 MNKILLVDDDRELTSLLKELLEMEG-FNVI-VAHDGEQALDLLDD-SIDLLLLDVMMPKKNGIDTLKELRQTHQTPVIM- 76
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  81 stLTQKGSPI-TLEALELGAVDFIAKP 106
Cdd:PRK10955   77 --LTARGSELdRVLGLELGADDYLPKP 101
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
4-106 8.07e-12

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: 61.26  E-value: 8.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPD---VLTlDVEMPKMDGISFLKNLMR---LRPMPV 77
Cdd:cd17582     1 VLLVENDDSTRQIVTALLRKCS--YEVTAASDGLQAWDVLEDEQNEidlILT-EVDLPVSSGFKLLSYIMRhkiCKNIPV 77
                          90       100
                  ....*....|....*....|....*....
gi 1674995404  78 VMIStlTQKGSPITLEALELGAVDFIAKP 106
Cdd:cd17582    78 IMMS--SQDSVGVVFKCLSKGAADYLVKP 104
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
4-106 9.07e-12

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: 61.24  E-value: 9.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQAS-DINVVGCAEDPYQAREMIKKLNPDV------LTLDVEMPKMDGISF---LKNLMRLR 73
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGfEIAEAVDGEEALNKLENLAKEGNDLskeldlIITDIEMPKMDGYELtfeLRDDPRLA 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1674995404  74 PMPVVMISTLTqkgSPITLE-ALELGAVDFIAKP 106
Cdd:cd19924    81 NIPVILNSSLS---GEFSRArGKKVGADAYLAKF 111
orf27 CHL00148
Ycf27; Reviewed
4-108 9.64e-12

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 63.97  E-value: 9.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdINVVgCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMISTL 83
Cdd:CHL00148    9 ILVVDDEAYIRKILETRLSIIG-YEVI-TASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKESDVPIIMLTAL 86
                          90       100
                  ....*....|....*....|....*
gi 1674995404  84 TQKGSPITleALELGAVDFIAKPTS 108
Cdd:CHL00148   87 GDVSDRIT--GLELGADDYVVKPFS 109
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
4-106 1.37e-11

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: 60.80  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISF---LKNLMRLRPMPVVMI 80
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQG--YKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELcrkIKSDPDLKDIPVILL 78
                          90       100
                  ....*....|....*....|....*.
gi 1674995404  81 STLTQKGSPItlEALELGAVDFIAKP 106
Cdd:cd17598    79 TTLSDPRDVI--RGLECGADNFITKP 102
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
6-106 1.46e-11

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: 60.36  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   6 IIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMP-VVMISTLT 84
Cdd:cd17565     3 IVDDDKNIIKILSDIIEDDDLGEVVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGkFIMISQVS 82
                          90       100
                  ....*....|....*....|..
gi 1674995404  85 QKgSPITlEALELGAVDFIAKP 106
Cdd:cd17565    83 DK-EMIG-KAYQAGIEFFINKP 102
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
4-106 1.80e-11

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: 60.67  E-value: 1.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEIL-QQASDINVVGCAEDPYQAremIKKLNPDVLTLDVEMPKMDGISFLKNLM-RLRPMPVVMIs 81
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLsDEGYKVTHVETGKEALAF---LSDQPPDVVLLDLKLPDMSGMEILKWIQeRSLPTSVIVI- 76
                          90       100
                  ....*....|....*....|....*.
gi 1674995404  82 tlTQKGS-PITLEALELGAVDFIAKP 106
Cdd:cd17572    77 --TAHGSvDIAVEAMRLGAYDFLEKP 100
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
3-108 3.02e-11

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: 60.12  E-value: 3.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   3 NVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLN-------PDVLTLDVEMPKMDGISFLKNLM---RL 72
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGVPNELHVVRDGEEALDFLRGEGeyadaprPDLILLDLNMPRMDGFEVLREIKadpDL 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1674995404  73 RPMPVVMISTlTQKGSPItLEALELGAVDFIAKPTS 108
Cdd:cd17557    81 RRIPVVVLTT-SDAEEDI-ERAYELGANSYIVKPVD 114
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
4-99 4.17e-11

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 61.97  E-value: 4.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLmRLRPMP--VVMIS 81
Cdd:PRK10651    9 ILLIDDHPMLRTGVKQLISMAPDITVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKL-REKSLSgrIVVFS 87
                          90
                  ....*....|....*...
gi 1674995404  82 TLTQKGSPITleALELGA 99
Cdd:PRK10651   88 VSNHEEDVVT--ALKRGA 103
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
4-108 4.30e-11

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: 59.31  E-value: 4.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMistL 83
Cdd:cd19938     2 ILIVEDEPKLAQLLIDYLRAAG--YAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFSDVPIIM---V 76
                          90       100
                  ....*....|....*....|....*.
gi 1674995404  84 TQKGSPIT-LEALELGAVDFIAKPTS 108
Cdd:cd19938    77 TARVEEIDrLLGLELGADDYICKPYS 102
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
4-106 4.78e-11

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: 59.14  E-value: 4.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdINVVGCAedpyQAREMIKKLNPD---VLTLDVEMPKMDGISFLKNLMRLR-PMPVVM 79
Cdd:cd17537     3 VYVVDDDEAVRDSLAFLLRSVG-LAVKTFT----SASAFLAAAPPDqpgCLVLDVRMPGMSGLELQDELLARGsNIPIIF 77
                          90       100
                  ....*....|....*....|....*...
gi 1674995404  80 IstlTQKGS-PITLEALELGAVDFIAKP 106
Cdd:cd17537    78 I---TGHGDvPMAVEAMKAGAVDFLEKP 102
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
3-106 4.89e-11

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: 59.32  E-value: 4.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   3 NVLIIDDSPLIRGLLTEILQQasDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMIST 82
Cdd:cd17619     2 HILIVEDEPVTRATLKSYFEQ--EGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSEVGIILVTG 79
                          90       100
                  ....*....|....*....|....
gi 1674995404  83 LTQKGSPITleALELGAVDFIAKP 106
Cdd:cd17619    80 RDDEVDRIV--GLEIGADDYVTKP 101
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
4-106 7.95e-11

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: 58.22  E-value: 7.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKnlmRLR----PMPVVM 79
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEG--YAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLR---RLRaagkQTPVLM 75
                          90       100
                  ....*....|....*....|....*...
gi 1674995404  80 istLTQKGSPI-TLEALELGAVDFIAKP 106
Cdd:cd19935    76 ---LTARDSVEdRVKGLDLGADDYLVKP 100
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
2-58 8.84e-11

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: 56.81  E-value: 8.84e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1674995404    2 INVLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMP 58
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEG--YEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
4-106 1.13e-10

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: 58.05  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQAsDINVVGCaEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPM-PVVMIST 82
Cdd:cd19919     3 VWIVDDDSSIRWVLERALAGA-GLTVTSF-ENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDlPVIIMTA 80
                          90       100
                  ....*....|....*....|....
gi 1674995404  83 LTQKGSPITleALELGAVDFIAKP 106
Cdd:cd19919    81 HSDLDSAVS--AYQGGAFEYLPKP 102
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
30-109 2.72e-10

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: 57.05  E-value: 2.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404  30 VGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMistLTQKGSPI-TLEALELGAVDFIAKPTS 108
Cdd:cd17614    25 VVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSNVPIIM---LTAKDSEVdKVLGLELGADDYVTKPFS 101

                  .
gi 1674995404 109 N 109
Cdd:cd17614   102 N 102
fixJ PRK09390
response regulator FixJ; Provisional
3-106 3.28e-10

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 58.86  E-value: 3.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   3 NVLIIDDSPLIRGLLtEILQQASDINVVgcAEDPYQA-REMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLR-PMPVVMI 80
Cdd:PRK09390    5 VVHVVDDDEAMRDSL-AFLLDSAGFEVR--LFESAQAfLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGsPLPVIVM 81
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  81 stlTQKGS-PITLEALELGAVDFIAKP 106
Cdd:PRK09390   82 ---TGHGDvPLAVEAMKLGAVDFIEKP 105
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
4-106 3.45e-10

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: 56.79  E-value: 3.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASDINVVGcAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLM---RLRPMPVVMi 80
Cdd:cd17552     4 ILVIDDEEDIREVVQACLEKLAGWEVLT-ASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQanpETQSIPVIL- 81
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  81 stLTQKGSPI-TLEALELGAVDFIAKP 106
Cdd:cd17552    82 --LTAKAQPSdRQRFASLGVAGVIAKP 106
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
4-106 3.63e-10

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 61.02  E-value: 3.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILqqASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMIST 82
Cdd:PRK11361    7 ILIVDDEDNVRRMLSTAF--ALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETrTPVILMTA 84
                          90       100
                  ....*....|....*....|....
gi 1674995404  83 LTQKGSPItlEALELGAVDFIAKP 106
Cdd:PRK11361   85 YAEVETAV--EALRCGAFDYVIKP 106
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
4-69 3.73e-10

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: 56.59  E-value: 3.73e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNL 69
Cdd:cd19931     1 VLLIDDHPLLRKGIKQLIELDPDFTVVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKAL 66
ompR PRK09468
osmolarity response regulator; Provisional
4-106 4.16e-10

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 59.22  E-value: 4.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKnlmRLR----PMPVVM 79
Cdd:PRK09468    8 ILVVDDDMRLRALLERYLTEQG--FQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICR---RLRsqnnPTPIIM 82
                          90       100
                  ....*....|....*....|....*...
gi 1674995404  80 istLTQKGSPIT-LEALELGAVDFIAKP 106
Cdd:PRK09468   83 ---LTAKGEEVDrIVGLEIGADDYLPKP 107
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
3-108 4.70e-10

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


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 56.30  E-value: 4.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   3 NVLIIDDSPLIRGLLTEILQQaSDINVVgCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMis 81
Cdd:cd17563     2 SLLLVDDDEVFAERLARALER-RGFEVE-TAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPdARIVV-- 77
                          90       100
                  ....*....|....*....|....*...
gi 1674995404  82 tLTQKGS-PITLEALELGAVDFIAKPTS 108
Cdd:cd17563    78 -LTGYASiATAVEAIKLGADDYLAKPAD 104
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
4-106 5.65e-10

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: 55.84  E-value: 5.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQAsdINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDG---ISFLKNLMRLRPMPVVMi 80
Cdd:cd17602     1 VACVDDRPSIQKMIEYFLEKQ--GFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGyelCSLLRKSSALKDTPIIM- 77
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  81 stLTQKGSPIT-LEALELGAVDFIAKP 106
Cdd:cd17602    78 --LTGKDGLVDrIRAKMAGASGYLTKP 102
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
4-106 7.20e-10

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: 55.75  E-value: 7.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQaSDINVVgCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMISTL 83
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEK-WGYEVV-LIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISNVPIIFISSR 78
                          90       100
                  ....*....|....*....|...
gi 1674995404  84 TQKGSPITleALELGAVDFIAKP 106
Cdd:cd18159    79 DDNMDQVM--AINMGGDDYITKP 99
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
4-117 8.42e-10

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: 55.64  E-value: 8.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASDINVVgcAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMISTL 83
Cdd:cd17553     3 ILIVDDQYGIRILLNEVFNKEGYQTFQ--AANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1674995404  84 TQKGSPITlEALELGAVDFIAKP--TSNVRAQMNHY 117
Cdd:cd17553    81 YGELDMIQ-ESKELGALTHFAKPfdIDEIRDAVKKY 115
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
3-106 1.25e-09

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: 55.24  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   3 NVLIIDDSPLIRGLLTEILQqASDINVVGcAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISF---LKNLMRLRPMPVVM 79
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLE-SAGYEVLE-AADGEEALEIARKEKPDLILMDIQLPGMDGLEAtrlLKEDPATRDIPVIA 78
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  80 ISTLTQKGSpiTLEALELGAVDFIAKP 106
Cdd:cd17548    79 LTAYAMKGD--REKILEAGCDGYISKP 103
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
4-106 2.10e-09

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: 54.09  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMISTL 83
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHG--YRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWSAVPVIVLSAR 78
                          90       100
                  ....*....|....*....|...
gi 1674995404  84 TQKGSPItlEALELGAVDFIAKP 106
Cdd:cd17620    79 DEESDKI--AALDAGADDYLTKP 99
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
4-106 2.23e-09

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: 54.70  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASDInvVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKnlmRLRPM----PVVM 79
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYE--VETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCR---RLRAAgndlPILV 75
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  80 ISTLTQKGSPITleALELGAVDFIAKP 106
Cdd:cd17627    76 LTARDSVSDRVA--GLDAGADDYLVKP 100
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
2-106 2.37e-09

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: 54.34  E-value: 2.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   2 INVLIIDDSPLIRGLLTEILQQAsDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMP-KMDGISFLKNLMRLRPMPVVMI 80
Cdd:cd17534     1 KKILIVEDEAIIALDLKEILESL-GYEVVGIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREKFDIPVIFL 79
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  81 STLTQKGspiTLE-ALELGAVDFIAKP 106
Cdd:cd17534    80 TAYSDEE---TLErAKETNPYGYLVKP 103
PRK10693 PRK10693
two-component system response regulator RssB;
32-109 2.49e-09

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 57.69  E-value: 2.49e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1674995404  32 CAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNL-MRLRPMPVVMISTlTQKGSPITlEALELGAVDFIAKPTSN 109
Cdd:PRK10693    2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLrNRGDQTPVLVISA-TENMADIA-KALRLGVQDVLLKPVKD 78
PRK09483 PRK09483
response regulator; Provisional
1-105 2.52e-09

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 56.65  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   1 MINVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVM 79
Cdd:PRK09483    1 MINVLLVDDHELVRAGIRRILEDIKGIKVVGEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKILRYTPdVKIIM 80
                          90       100
                  ....*....|....*....|....*.
gi 1674995404  80 ISTLTQkgSPITLEALELGAVDFIAK 105
Cdd:PRK09483   81 LTVHTE--NPLPAKVMQAGAAGYLSK 104
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
2-106 2.70e-09

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


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 54.45  E-value: 2.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   2 INVLIIDDSPLIRGLLTEILQQaSDINVVGcAEDPYQAREMIKKlNPD---VLTlDVEMPKMDGISFLKNLMRLRP---M 75
Cdd:cd17544     1 IKVLVVDDSATSRNHLRALLRR-HNFQVLE-AANGQEALEVLEQ-HPDiklVIT-DYNMPEMDGFELVREIRKKYSrdqL 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1674995404  76 PVVMIStlTQKGSPITLEALELGAVDFIAKP 106
Cdd:cd17544    77 AIIGIS--ASGDNALSARFIKAGANDFLTKP 105
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
5-108 2.80e-09

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


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 54.15  E-value: 2.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   5 LIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPM-PVVMISTL 83
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEG--YTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIEtPVLLLTAL 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1674995404  84 TQ-----KGspitleaLELGAVDFIAKPTS 108
Cdd:cd17625    79 DAvedrvKG-------LDLGADDYLPKPFS 101
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
4-106 2.95e-09

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: 54.23  E-value: 2.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdINVVGcAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLmRLRP----MPVVM 79
Cdd:cd17562     3 ILAVDDSASIRQMVSFTLRGAG-YEVVE-AADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKEL-RKLPaykfTPILM 79
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  80 IStlTQKGSPITLEALELGAVDFIAKP 106
Cdd:cd17562    80 LT--TESSDEKKQEGKAAGATGWLVKP 104
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
4-108 3.95e-09

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 56.23  E-value: 3.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdinvvgcaedpYQAREM---------IKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP 74
Cdd:PRK10710   13 ILIVEDEPKLGQLLIDYLQAAS-----------YATTLLshgdevlpyVRQTPPDLILLDLMLPGTDGLTLCREIRRFSD 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1674995404  75 MPVVMIstlTQKGSPIT-LEALELGAVDFIAKPTS 108
Cdd:PRK10710   82 IPIVMV---TAKIEEIDrLLGLEIGADDYICKPYS 113
dpiA PRK10046
two-component response regulator DpiA; Provisional
2-138 6.96e-09

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 55.41  E-value: 6.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   2 INVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMIS 81
Cdd:PRK10046    5 LTLLIVEDETPLAEMHAEYIRHIPGFSQILLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELVQAHYPGDVVFT 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1674995404  82 TLTQKGSPITlEALELGAVDFIAKPTSNVRaqMNHYASLVQQKVRIAAGARIRSFKK 138
Cdd:PRK10046   85 TAASDMETVS-EAVRCGVFDYLIKPIAYER--LGQTLTRFRQRKHMLESIDSASQKQ 138
pleD PRK09581
response regulator PleD; Reviewed
4-110 8.03e-09

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 56.83  E-value: 8.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQqASDINVVgCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLM---RLRPMPVVMI 80
Cdd:PRK09581    5 ILVVDDIPANVKLLEAKLL-AEYYTVL-TASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKsdpATTHIPVVMV 82
                          90       100       110
                  ....*....|....*....|....*....|
gi 1674995404  81 STLTQKGSPItlEALELGAVDFIAKPTSNV 110
Cdd:PRK09581   83 TALDDPEDRV--RGLEAGADDFLTKPINDV 110
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
4-108 1.40e-08

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: 52.35  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQ-QASDINVvgcAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMis 81
Cdd:cd17615     2 VLVVDDEPNITELLSMALRyEGWDVET---AADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPdVPVLF-- 76
                          90       100
                  ....*....|....*....|....*...
gi 1674995404  82 tLTQKGS-PITLEALELGAVDFIAKPTS 108
Cdd:cd17615    77 -LTAKDSvEDRIAGLTAGGDDYVTKPFS 103
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
4-106 1.43e-08

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: 52.28  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRL-RPMPVVMist 82
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAG--YVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEgRATPVLI--- 75
                          90       100
                  ....*....|....*....|....*
gi 1674995404  83 LTQKGS-PITLEALELGAVDFIAKP 106
Cdd:cd19934    76 LTARDSwQDKVEGLDAGADDYLTKP 100
PRK10430 PRK10430
two-component system response regulator DcuR;
1-106 1.50e-08

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 54.73  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   1 MINVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMI--KKLNPDVLTLDVEMPKMDGISFLKNLMRL-RPMPV 77
Cdd:PRK10430    1 MINVLIVDDDAMVAELNRRYVAQIPGFQCCGTASTLEQAKEIIfnSDTPIDLILLDIYMQQENGLDLLPVLHEAgCKSDV 80
                          90       100
                  ....*....|....*....|....*....
gi 1674995404  78 VMISTLTQKGSpiTLEALELGAVDFIAKP 106
Cdd:PRK10430   81 IVISSAADAAT--IKDSLHYGVVDYLIKP 107
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
4-106 3.44e-08

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: 50.91  E-value: 3.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASDInVVGCAEDPYQAREMIKKlNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMISTL 83
Cdd:cd17594     2 VLVVDDDAAMRHLLILYLRERGFD-VTAAADGAEEARLMLHR-RVDLVLLDLRLGQESGLDLLRTIRARSDVPIIIISGD 79
                          90       100
                  ....*....|....*....|...
gi 1674995404  84 TQKGSPITLeALELGAVDFIAKP 106
Cdd:cd17594    80 RRDEIDRVV-GLELGADDYLAKP 101
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
4-76 3.52e-08

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: 50.92  E-value: 3.52e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKnlmRLRPMP 76
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEG--AEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELAR---RLRELP 68
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
1-106 3.79e-08

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 53.27  E-value: 3.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   1 MINVLIIDDSPLIRGLLTEILQQAsdinvvGCAedPYQAREMIKKL------NPDVLTLDVEMPKMDGISFLKNLMRLRP 74
Cdd:PRK10529    1 MTNVLIVEDEQAIRRFLRTALEGD------GMR--VFEAETLQRGLleaatrKPDLIILDLGLPDGDGIEFIRDLRQWSA 72
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1674995404  75 MPVVMISTLTQKGSPITleALELGAVDFIAKP 106
Cdd:PRK10529   73 IPVIVLSARSEESDKIA--ALDAGADDYLSKP 102
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
2-105 5.63e-08

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: 50.87  E-value: 5.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   2 INVLIIDDSPLIRGLLTEILQQASDINVVGCAeDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMR---LRPMPVV 78
Cdd:cd17575     1 IMVLLVDDQAIIGEAVRRALADEEDIDFHYCS-DPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRAnpaTRDIPII 79
                          90       100
                  ....*....|....*....|....*...
gi 1674995404  79 MISTltqKGSP-ITLEALELGAVDFIAK 105
Cdd:cd17575    80 VLST---KEEPeVKSEAFALGANDYLVK 104
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
4-106 7.44e-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: 7.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASDInvVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPM-PVVMIS- 81
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYA--VDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSlPVLILTa 78
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  82 --TLTQKgspitLEALELGAVDFIAKP 106
Cdd:cd17624    79 rdGVDDR-----VAGLDAGADDYLVKP 100
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
48-106 1.00e-07

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: 49.37  E-value: 1.00e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404  48 PDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMistLTQKGSPI-TLEALELGAVDFIAKP 106
Cdd:cd19936    43 PDLAILDIKMPRMDGMELLQRLRQKSTLPVIF---LTSKDDEIdEVFGLRMGADDYITKP 99
PRK13856 PRK13856
two-component response regulator VirG; Provisional
1-106 1.01e-07

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 52.12  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   1 MINVLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMI 80
Cdd:PRK13856    1 MKHVLVIDDDVAMRHLIVEYLTIHA--FKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSLATKSDVPIIII 78
                          90       100
                  ....*....|....*....|....*...
gi 1674995404  81 S--TLTQKGSPItleALELGAVDFIAKP 106
Cdd:PRK13856   79 SgdRLEEADKVV---ALELGATDFIAKP 103
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
4-106 1.04e-07

phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR)-containing response regulators; Response regulators share the common phosphoacceptor REC domain and different output domains. This subfamily contains uncharacterized response regulators with TPR repeats as the effector or output domain, which might contain between 3 to 16 TPR repeats (each about 34 amino acids). TPR-containing proteins occur in all domains of life and the abundance of TPR-containing proteins in a bacterial proteome is not indicative of virulence. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members in this subfamily may contain inactive REC domains lacking canonical metal-binding and active site residues.


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 49.57  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPK-MDGISFLKNLMRLRPMP----VV 78
Cdd:cd17589     1 FLIVDDQPTFRSMLKSMLRSLG-VTRIDTASSGEEALRMCENKTYDIVLCDYNLGKgKNGQQLLEELRHKKLISpstvFI 79
                          90       100
                  ....*....|....*....|....*...
gi 1674995404  79 MISTLTQkgSPITLEALELGAVDFIAKP 106
Cdd:cd17589    80 MVTGESS--RAMVLSALELEPDDYLLKP 105
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
4-114 1.58e-07

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: 49.30  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQaSDINVVgCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMISTL 83
Cdd:cd17622     3 ILLVEDDPKLARLIADFLES-HGFNVV-VEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQGPILLLTAL 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1674995404  84 TQKGSPITleALELGAVDFIAKPTS------NVRAQM 114
Cdd:cd17622    81 DSDIDHIL--GLELGADDYVVKPVEpavllaRLRALL 115
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
4-125 2.83e-07

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 50.87  E-value: 2.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASDINVVgcAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMR---LRPMPVVMI 80
Cdd:PRK10161    5 ILVVEDEAPIREMVCFVLEQNGFQPVE--AEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKResmTRDIPVVML 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1674995404  81 STLTQKGSPItlEALELGAVDFIAKPTS------NVRAQMNHYASLVQQKV 125
Cdd:PRK10161   83 TARGEEEDRV--RGLETGADDYITKPFSpkelvaRIKAVMRRISPMAVEEV 131
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
3-69 3.84e-07

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: 48.21  E-value: 3.84e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1674995404   3 NVLIIDDSPLIRGLLTEILQQASDINVVGcAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNL 69
Cdd:cd17530     2 RVLVLDDDPFQCMMAATILEDLGPGNVDE-ADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHL 67
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
3-106 3.91e-07

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 51.41  E-value: 3.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   3 NVLIIDDSPLIRGLLTEILQQASdinvVGCA--EDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPM-PVVM 79
Cdd:PRK10923    5 IVWVVDDDSSIRWVLERALAGAG----LTCTtfENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMlPVII 80
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  80 ISTLTQKGSPITleALELGAVDFIAKP 106
Cdd:PRK10923   81 MTAHSDLDAAVS--AYQQGAFDYLPKP 105
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
2-178 4.60e-07

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 51.18  E-value: 4.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   2 INVLIIDDSpLIRGLLTEILQQASDINVvGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMI 80
Cdd:PRK10365    6 IDILVVDDD-ISHCTILQALLRGWGYNV-ALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPaIPVLIM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404  81 STLTQKGSPItlEALELGAVDFIAKPTSNVRAQmnhyASLVQqkvriaAGARIRSFKKAPPDAkpilTDTKFLLnkviaI 160
Cdd:PRK10365   84 TAYSSVETAV--EALKTGALDYLIKPLDFDNLQ----ATLEK------ALAHTHSIDAETPAV----TASQFGM-----V 142
                         170
                  ....*....|....*...
gi 1674995404 161 GASTGGTEAIKEVLIKMP 178
Cdd:PRK10365  143 GKSPAMQHLLSEIALVAP 160
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
4-88 5.25e-07

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


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 47.37  E-value: 5.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQAsDINVVGCAEDPyQAREMIKKLNPDVLTLDVEMPKMDGISFLKNL---MRLRPMPVVMi 80
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQ-GFTVIAASNGL-EALDLLNQYIPDLIISDIIMPGVDGYSLLGKLrknADFDTIPVIF- 77

                  ....*...
gi 1674995404  81 stLTQKGS 88
Cdd:cd19927    78 --LTAKGM 83
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
3-80 5.35e-07

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 49.51  E-value: 5.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   3 NVLIIDDSPL----IRGLLteilqQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVV 78
Cdd:PRK09958    2 NAIIIDDHPLaiaaIRNLL-----IKNDIEILAELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGII 76

                  ..
gi 1674995404  79 MI 80
Cdd:PRK09958   77 II 78
PRK10840 PRK10840
transcriptional regulator RcsB; Provisional
2-97 6.29e-07

transcriptional regulator RcsB; Provisional


Pssm-ID: 182771 [Multi-domain]  Cd Length: 216  Bit Score: 49.45  E-value: 6.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   2 INVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPK---MDGISFLKNLMrlRPMPVV 78
Cdd:PRK10840    4 MNVIIADDHPIVLFGIRKSLEQIEWVNVVGEFEDSTALINNLPKLDAHVLITDLSMPGdkyGDGITLIKYIK--RHFPSL 81
                          90       100
                  ....*....|....*....|
gi 1674995404  79 MISTLTQKGSPITLEA-LEL 97
Cdd:PRK10840   82 SIIVLTMNNNPAILSAvLDL 101
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
2-106 9.61e-07

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: 47.01  E-value: 9.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   2 INVLIIDDSPLIRGLLTEILQqASDINVVgCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMIs 81
Cdd:cd17569     1 PTILLVDDEPNILKALKRLLR-REGYEVL-TATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRIL- 77
                          90       100
                  ....*....|....*....|....*....
gi 1674995404  82 tLTqkGSP---ITLEALELGAVD-FIAKP 106
Cdd:cd17569    78 -LT--GYAdldAAIEAINEGEIYrFLTKP 103
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
4-114 1.02e-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: 47.08  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQ-QASDINVVGcaeDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMist 82
Cdd:cd17626     3 ILVVDDDAALAEMIGIVLRgEGFDPAFCG---DGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAESGVPIVM--- 76
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1674995404  83 LTQKGSPI-TLEALELGAVDFIAKP------TSNVRAQM 114
Cdd:cd17626    77 LTAKSDTVdVVLGLESGADDYVAKPfkpkelVARIRARL 115
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
4-90 1.32e-06

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 48.70  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMISTL 83
Cdd:PRK10403    9 VLIVDDHPLMRRGVRQLLELDPGFEVVAEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQIIILTV 88

                  ....*..
gi 1674995404  84 TQKGSPI 90
Cdd:PRK10403   89 SDASSDV 95
PRK15115 PRK15115
response regulator GlrR; Provisional
3-106 2.29e-06

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 49.07  E-value: 2.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   3 NVLIIDDSPLIRGLLTeiLQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMis 81
Cdd:PRK15115    7 HLLLVDDDPGLLKLLG--MRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPgMPVII-- 82
                          90       100
                  ....*....|....*....|....*.
gi 1674995404  82 tLTQKGS-PITLEALELGAVDFIAKP 106
Cdd:PRK15115   83 -LTAHGSiPDAVAATQQGVFSFLTKP 107
PRK15369 PRK15369
two component system response regulator;
2-105 2.43e-06

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 47.77  E-value: 2.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   2 INVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMI 80
Cdd:PRK15369    4 YKILLVDDHELIINGIKNMLAPYPRYKIVGQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRWPaMNILVL 83
                          90       100
                  ....*....|....*....|....*
gi 1674995404  81 STLTQKGSpiTLEALELGAVDFIAK 105
Cdd:PRK15369   84 TARQEEHM--ASRTLAAGALGYVLK 106
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
4-108 3.61e-06

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


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 45.44  E-value: 3.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMISTL 83
Cdd:cd19939     2 ILIVEDELELARLTRDYLIKAG--LEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHSHVPILMLTAR 79
                          90       100
                  ....*....|....*....|....*
gi 1674995404  84 TQKGSPITleALELGAVDFIAKPTS 108
Cdd:cd19939    80 TEEMDRVL--GLEMGADDYLCKPFS 102
PRK15479 PRK15479
transcriptional regulator TctD;
4-127 4.37e-06

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 47.02  E-value: 4.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNL-MRLRPMPVVMist 82
Cdd:PRK15479    3 LLLAEDNRELAHWLEKALVQNG--FAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLrKRGQTLPVLL--- 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1674995404  83 LTQKGSPIT-LEALELGAVDFIAKP------TSNVRAQMNHYASLVQQKVRI 127
Cdd:PRK15479   78 LTARSAVADrVKGLNVGADDYLPKPfeleelDARLRALLRRSAGQVQEVQQL 129
PRK10610 PRK10610
chemotaxis protein CheY;
5-106 4.56e-06

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 45.35  E-value: 4.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   5 LIIDDSPLIRGLLTEILQQASdINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLM---RLRPMPVVMIS 81
Cdd:PRK10610    9 LVVDDFSTMRRIVRNLLKELG-FNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRadgAMSALPVLMVT 87
                          90       100
                  ....*....|....*....|....*
gi 1674995404  82 TLTQKGSPITleALELGAVDFIAKP 106
Cdd:PRK10610   88 AEAKKENIIA--AAQAGASGYVVKP 110
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
3-105 5.05e-06

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 46.79  E-value: 5.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   3 NVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMIS 81
Cdd:PRK09935    5 SVIIMDTHPIIRMSIEVLLQKNSELQIVLKTDDYRITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQStVKVLFLS 84
                          90       100
                  ....*....|....*....|....
gi 1674995404  82 TLTQkgSPITLEALELGAVDFIAK 105
Cdd:PRK09935   85 SKSE--CFYAGRAIQAGANGFVSK 106
PRK14084 PRK14084
DNA-binding response regulator;
2-167 1.00e-05

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 46.28  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   2 INVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMIS 81
Cdd:PRK14084    1 MKALIVDDEPLARNELTYLLNEIGGFEEINEAENVKETLEALLINQYDIIFLDINLMDESGIELAAKIQKMKEPPAIIFA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404  82 TLTQKgspITLEALELGAVDFIAKPTSNVR-AQMNHYASLVQQKVRIAAGARIRSFKKAPPDAKPILTDTK-FLLNK--V 157
Cdd:PRK14084   81 TAHDQ---FAVKAFELNATDYILKPFEQKRiEQAVNKVRATKAKDDNNASAIANDMSANFDQSLPIEIDDKiHMLNQqdI 157
                         170
                  ....*....|
gi 1674995404 158 IAIGASTGGT 167
Cdd:PRK14084  158 IAIGVHNGIT 167
PRK10766 PRK10766
two-component system response regulator TorR;
3-106 1.92e-05

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 45.03  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   3 NVLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNlmrLRPMPVVMIST 82
Cdd:PRK10766    4 HILVVEDEPVTRARLQGYFEQEG--YTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRE---LRSRSTVGIIL 78
                          90       100
                  ....*....|....*....|....*
gi 1674995404  83 LTQKGSPI-TLEALELGAVDFIAKP 106
Cdd:PRK10766   79 VTGRTDSIdRIVGLEMGADDYVTKP 103
PRK11517 PRK11517
DNA-binding response regulator HprR;
2-154 2.59e-05

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 44.89  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   2 INVLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVmis 81
Cdd:PRK11517    1 MKILLIEDNQRTQEWVTQGLSEAG--YVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQTPVI--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404  82 TLTQKGS-PITLEALELGAVDFIAKPTS------NVRAQM-NHYASLVQQKVriaAGARIRSFKKAPP-DAKPI-LTDTK 151
Cdd:PRK11517   76 CLTARDSvDDRVRGLDSGANDYLVKPFSfsellaRVRAQLrQHHALNSTLEI---SGLRMDSVSQSVSrDNISItLTRKE 152

                  ...
gi 1674995404 152 FLL 154
Cdd:PRK11517  153 FQL 155
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
4-106 3.52e-05

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


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 43.12  E-value: 3.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQasDINVVgCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMISTL 83
Cdd:cd17596     3 ILVVDDEVRSLEALRRTLEE--DFDVL-TAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISG 79
                          90       100
                  ....*....|....*....|...
gi 1674995404  84 TQKGSPITLEALELGAVDFIAKP 106
Cdd:cd17596    80 YTDSEDIIAGINEAGIYQYLTKP 102
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
4-113 4.19e-05

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


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 42.69  E-value: 4.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASDINVvgcAEDPYQAREMIKKLNPDVLTLDVEMPKMDGI---SFLKNLMRLRPMPVVMI 80
Cdd:cd17539     1 VLLVDDRPSSAERIAAMLSSEHEVVV---EADPDEALFRAAEGPFDLVIVSLALEDFDGLrlcSQLRSLERTRQLPILAV 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1674995404  81 STLTQKGSPITleALELGAVDFIAKP------TSNVRAQ 113
Cdd:cd17539    78 ADPGDRGRLIR--ALEIGVNDYLVRPidpnelLARVRTQ 114
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
38-131 4.29e-05

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 44.24  E-value: 4.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404  38 QAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMISTLTQKGSPITleALELGAVDFIAKPT------SNVR 111
Cdd:PRK10701   36 RAEATILREQPDLVLLDIMLPGKDGMTICRDLRPKWQGPIVLLTSLDSDMNHIL--ALEMGACDYILKTTppavllARLR 113
                          90       100
                  ....*....|....*....|
gi 1674995404 112 AQMNHYASLVQQKVRIAAGA 131
Cdd:PRK10701  114 LHLRQNEQATQTKGLQETSL 133
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
4-106 6.99e-05

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: 41.37  E-value: 6.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLtEILQQASDINVVGcAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNL-MRLRPMPVVMIst 82
Cdd:cd19926     1 VLVVDDEPDIRELL-EITLGRMGLDVRS-ARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIqQRLPQTPVAVI-- 76
                          90       100
                  ....*....|....*....|....*
gi 1674995404  83 lTQKGSPIT-LEALELGAVDFIAKP 106
Cdd:cd19926    77 -TAYGSLDTaIEALKAGAFDFLTKP 100
PRK10816 PRK10816
two-component system response regulator PhoP;
4-106 9.15e-05

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 43.19  E-value: 9.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKnlmRLRPMPVVM-IST 82
Cdd:PRK10816    3 VLVVEDNALLRHHLKVQLQDAG--HQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIR---RWRSNDVSLpILV 77
                          90       100
                  ....*....|....*....|....*
gi 1674995404  83 LT-QKGSPITLEALELGAVDFIAKP 106
Cdd:PRK10816   78 LTaRESWQDKVEVLSAGADDYVTKP 102
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
1-108 1.35e-04

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 42.64  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   1 MINVLIIDDSPLIRGLLTEILQqaSDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVM 79
Cdd:PRK11083    3 QPTILLVEDEQAIADTLVYALQ--SEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPaLPVIF 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1674995404  80 istLTQKGSPIT-LEALELGAVDFIAKPTS 108
Cdd:PRK11083   81 ---LTARSDEVDrLVGLEIGADDYVAKPFS 107
PRK10360 PRK10360
transcriptional regulator UhpA;
1-108 1.40e-04

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 42.27  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   1 MINVLIIDDSPLIRGLLTEILQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMrlRPMPVVMI 80
Cdd:PRK10360    1 MITVALIDDHLIVRSGFAQLLGLEPDLQVVAEFGSGREALAGLPGRGVQVCICDISMPDISGLELLSQLP--KGMATIML 78
                          90       100
                  ....*....|....*....|....*....
gi 1674995404  81 STltqKGSPITLE-ALELGAVDFIAKPTS 108
Cdd:PRK10360   79 SV---HDSPALVEqALNAGARGFLSKRCS 104
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
2-78 2.38e-04

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 43.04  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   2 INVLIIDDSPLIRGLLTEilQQASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFlknLMRLRPM----PV 77
Cdd:PRK10841  802 MMILVVDDHPINRRLLAD--QLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRL---TQRLRQLgltlPV 876

                  .
gi 1674995404  78 V 78
Cdd:PRK10841  877 I 877
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
4-106 3.01e-04

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: 39.64  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQasdinvVGC----AEDPYQAREMIKK-LNPDVLTLDVEMP-KMDGISFLKNLMRLRP-MP 76
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLED------LGYtvleAASGDEALDLLESgPDIDLLVTDVIMPgGMNGSQLAEEARRRRPdLK 74
                          90       100       110
                  ....*....|....*....|....*....|
gi 1674995404  77 VVMISTLTQKGspITLEALELGaVDFIAKP 106
Cdd:cd18161    75 VLLTSGYAENA--IEGGDLAPG-VDVLSKP 101
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
4-106 3.35e-04

PEP-CTERM-box response regulator transcription factor; Members of this protein family share full-length homology with (but do not include) the acetoacetate metabolism regulatory protein AtoC (see SP|Q06065). These proteins have a Fis family DNA binding sequence (pfam02954), a response regulator receiver domain (pfam00072), and sigma-54 interaction domain (pfam00158). [Regulatory functions, DNA interactions]


Pssm-ID: 274348 [Multi-domain]  Cd Length: 445  Bit Score: 42.43  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdinvVGCAEDPYQAREMIKKLNPDVLTLDVEMPK-----MDGISFLKNLMRLRPMPVV 78
Cdd:TIGR02915   1 LLIVEDDLGLQKQLKWSFADYE----LAVAADRESAIALVRRHEPAVVTLDLGLPPdadgaSEGLAALQQILAIAPDTKV 76
                          90       100
                  ....*....|....*....|....*...
gi 1674995404  79 MISTlTQKGSPITLEALELGAVDFIAKP 106
Cdd:TIGR02915  77 IVIT-GNDDRENAVKAIGLGAYDFYQKP 103
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
4-106 3.40e-04

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: 39.41  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQAS-DINVVGCAEDPYQareMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMIS 81
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGyEVRTTGNAATLWR---WVEEGEGDLVITDVVMPDENGLDLIPRIKKARPdLPIIVMS 77
                          90       100
                  ....*....|....*....|....*
gi 1674995404  82 tlTQKGSPITLEALELGAVDFIAKP 106
Cdd:cd19928    78 --AQNTLMTAVKAAERGAFEYLPKP 100
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
4-106 3.42e-04

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: 40.04  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMI-----------KKLNPDVLTLDVEMPKMDGISFL---KNL 69
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLRISS--CRVTAVDSGKRALEFLgledeedssnfNEPKVNMIITDYCMPGMTGYDLLkkvKES 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1674995404  70 MRLRPMPVVMISTltqKGSPITL-EALELGAVDFIAKP 106
Cdd:cd17581    79 SALKEIPVVIMSS---ENIPTRIsRCLEEGAEDFLLKP 113
PRK13435 PRK13435
response regulator; Provisional
4-119 6.04e-04

response regulator; Provisional


Pssm-ID: 184052 [Multi-domain]  Cd Length: 145  Bit Score: 39.65  E-value: 6.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASDiNVVGCAEDPYQAREMIKKLNPDVLTLDVEmpKMDG---ISFLKNLMRLRPMPVVMI 80
Cdd:PRK13435    8 VLIVEDEALIALELEKLVEEAGH-EVVGIAMSSEQAIALGRRRQPDVALVDVH--LADGptgVEVARRLSADGGVEVVFM 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1674995404  81 StltqkGSPITLEALELGAVDFIAKP-TSNVRAQMNHYAS 119
Cdd:PRK13435   85 T-----GNPERVPHDFAGALGVIAKPySPRGVARALSYLS 119
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
2-64 9.12e-04

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 40.99  E-value: 9.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1674995404   2 INVLIIDDSP----LIRGLLTEILQQasdinVVGCaEDPYQAREMIKKLNPDVLTLDVEMPKMDGIS 64
Cdd:PRK11107  668 LTVMAVDDNPanlkLIGALLEEQVEH-----VVLC-DSGHQAVEQAKQRPFDLILMDIQMPGMDGIR 728
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
4-106 1.27e-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: 38.16  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILqqASDINVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLR-PMPVVMIST 82
Cdd:cd17616     1 VLLIEDDSATAQSIELML--KSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKvKTPILILSG 78
                          90       100
                  ....*....|....*....|....
gi 1674995404  83 LTQKGSPITleALELGAVDFIAKP 106
Cdd:cd17616    79 LADIEDKVK--GLGFGADDYMTKP 100
pleD PRK09581
response regulator PleD; Reviewed
3-106 1.42e-03

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 40.27  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   3 NVLIIDDSPLIRGLLTEILQQASDINVVGcaeDPYQAREMIKKLNPDVLTLDVEMPKMDGI---SFLKNLMRLRPMPVVM 79
Cdd:PRK09581  157 RILLVDDDVSQAERIANILKEEFRVVVVS---DPSEALFNAAETNYDLVIVSANFENYDPLrlcSQLRSKERTRYVPILL 233
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  80 ISTltQKGSPITLEALELGAVDFIAKP 106
Cdd:PRK09581  234 LVD--EDDDPRLVKALELGVNDYLMRP 258
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
4-106 2.61e-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: 36.79  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMistL 83
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEG--FEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARSNVPVIM---V 75
                          90       100
                  ....*....|....*....|....
gi 1674995404  84 TQKGSPI-TLEALELGAVDFIAKP 106
Cdd:cd17621    76 TAKDSEIdKVVGLELGADDYVTKP 99
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
4-81 3.93e-03

phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 36.33  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNP-DVLTLDVEMPKMDGISFLKNLMRLRP-MPVVMIS 81
Cdd:cd18160     2 ILLADDEPSVRKFIVTTLKKAG--YAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELAREARKIDPdVKILFIS 79
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
4-106 6.29e-03

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: 35.87  E-value: 6.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQA---SDInvvgcAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRP-MPVVM 79
Cdd:cd17573     1 ILLIEDDSTLGKEISKGLNEKgyqADV-----AESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPsIVVIV 75
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  80 ISTLTQKGSPItlEALELGAVDFIAKP 106
Cdd:cd17573    76 LSDNPKTEQEI--EAFKEGADDYIAKP 100
PRK10643 PRK10643
two-component system response regulator PmrA;
4-106 6.77e-03

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 37.32  E-value: 6.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1674995404   4 VLIIDDSPLIRGLLTEILQQASdiNVVGCAEDPYQAREMIKKLNPDVLTLDVEMPKMDGISFLKNLMRLRPMPVVMIstL 83
Cdd:PRK10643    3 ILIVEDDTLLLQGLILALQTEG--YACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLI--L 78
                          90       100
                  ....*....|....*....|....*..
gi 1674995404  84 TQKGspiTLE----ALELGAVDFIAKP 106
Cdd:PRK10643   79 TARD---TLEdrvaGLDVGADDYLVKP 102
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH