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Conserved domains on  [gi|567929123|ref|WP_024031527|]
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MULTISPECIES: diguanylate cyclase [Pseudoalteromonas]

Protein Classification

PleD family two-component system response regulator( domain architecture ID 1003184)

PleD family two-component system response regulator similar to Caulobacter vibrioides response regulator PleD, which is part of a signal transduction pathway controlling cell differentiation in the swarmer-to-stalked cell transition, and catalyzes the condensation of two GTP molecules to the cyclic dinucleotide di-GMP, which the acts as a secondary messenger

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
pleD super family cl35865
response regulator PleD; Reviewed
3-299 4.29e-68

response regulator PleD; Reviewed


The actual alignment was detected with superfamily member PRK09581:

Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 219.00  E-value: 4.29e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   3 KKAKILIVDDDPLNRLVLEKTLGTEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVF 82
Cdd:PRK09581 154 EDGRILLVDDDVSQAERIANILKEEFRVVVVSDPSEALFNAAETNYDLVIVSANFENYDPLRLCSQLRSKERTRYVPILL 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123  83 ISANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQLLIKQKNDLLEM-------LASIDGLTEIPNRRYLDENLSRE 155
Cdd:PRK09581 234 LVDEDDDPRLVKALELGVNDYLMRPIDKNELLARVRTQIRRKRYQDALRNnleqsieMAVTDGLTGLHNRRYFDMHLKNL 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 156 WRRSKRNGSCLSVLLMDIDHFKRYNDCYGHRAGDECLKQVAQALAAqCERSTDFIARYGGEEFAAVLPDVNKQQALAFAQ 235
Cdd:PRK09581 314 IERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRN-NIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAE 392
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567929123 236 KLRKAVNSLNIEHKASLNADHITISIGIASMENGNASAEqALLEQADLGLYAAKDAGRDQVVAL 299
Cdd:PRK09581 393 RIRRKIAEEPFIISDGKERLNVTVSIGVAELRPSGDTIE-ALIKRADKALYEAKNTGRNRVVAL 455
 
Name Accession Description Interval E-value
pleD PRK09581
response regulator PleD; Reviewed
3-299 4.29e-68

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 219.00  E-value: 4.29e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   3 KKAKILIVDDDPLNRLVLEKTLGTEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVF 82
Cdd:PRK09581 154 EDGRILLVDDDVSQAERIANILKEEFRVVVVSDPSEALFNAAETNYDLVIVSANFENYDPLRLCSQLRSKERTRYVPILL 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123  83 ISANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQLLIKQKNDLLEM-------LASIDGLTEIPNRRYLDENLSRE 155
Cdd:PRK09581 234 LVDEDDDPRLVKALELGVNDYLMRPIDKNELLARVRTQIRRKRYQDALRNnleqsieMAVTDGLTGLHNRRYFDMHLKNL 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 156 WRRSKRNGSCLSVLLMDIDHFKRYNDCYGHRAGDECLKQVAQALAAqCERSTDFIARYGGEEFAAVLPDVNKQQALAFAQ 235
Cdd:PRK09581 314 IERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRN-NIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAE 392
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567929123 236 KLRKAVNSLNIEHKASLNADHITISIGIASMENGNASAEqALLEQADLGLYAAKDAGRDQVVAL 299
Cdd:PRK09581 393 RIRRKIAEEPFIISDGKERLNVTVSIGVAELRPSGDTIE-ALIKRADKALYEAKNTGRNRVVAL 455
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
112-297 1.09e-65

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 207.14  E-value: 1.09e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 112 IVKVRVRNQLLIKQKNDLLEMLASIDGLTEIPNRRYLDENLSREWRRSKRNGSCLSVLLMDIDHFKRYNDCYGHRAGDEC 191
Cdd:COG2199   92 LLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEV 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 192 LKQVAQALAAQCeRSTDFIARYGGEEFAAVLPDVNKQQALAFAQKLRKAVNSLNIEHKAslNADHITISIGIASMENGNA 271
Cdd:COG2199  172 LKEVARRLRASL-RESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEG--KELRVTVSIGVALYPEDGD 248
                        170       180
                 ....*....|....*....|....*.
gi 567929123 272 SAEQaLLEQADLGLYAAKDAGRDQVV 297
Cdd:COG2199  249 SAEE-LLRRADLALYRAKRAGRNRVV 273
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
134-295 5.42e-65

Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 201.33  E-value: 5.42e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123  134 ASIDGLTEIPNRRYLDENLSREWRRSKRNGSCLSVLLMDIDHFKRYNDCYGHRAGDECLKQVAQALaAQCERSTDFIARY 213
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRL-SSSLRRSDLVARL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123  214 GGEEFAAVLPDVNKQQALAFAQKLRKAVNSLNIEHKASLNADHITISIGIASMENGNASAEQaLLEQADLGLYAAKDAGR 293
Cdd:pfam00990  80 GGDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPED-LLKRADTALYQAKQAGR 158

                  ..
gi 567929123  294 DQ 295
Cdd:pfam00990 159 NR 160
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
136-297 3.41e-64

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 198.93  E-value: 3.41e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 136 IDGLTEIPNRRYLDENLSREWRRSKRNGSCLSVLLMDIDHFKRYNDCYGHRAGDECLKQVAQALAAQCeRSTDFIARYGG 215
Cdd:cd01949    2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSL-RESDLVARLGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 216 EEFAAVLPDVNKQQALAFAQKLRKAVNSLNIEHKASLnadHITISIGIASMENGNASAEQaLLEQADLGLYAAKDAGRDQ 295
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEI---RVTASIGIATYPEDGEDAEE-LLRRADEALYRAKRSGRNR 156

                 ..
gi 567929123 296 VV 297
Cdd:cd01949  157 VV 158
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
133-297 4.12e-58

diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 183.60  E-value: 4.12e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   133 LASIDGLTEIPNRRYLDENLSREWRRSKRNGSCLSVLLMDIDHFKRYNDCYGHRAGDECLKQVAQALAAQCeRSTDFIAR 212
Cdd:smart00267   2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCL-RPGDLLAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   213 YGGEEFAAVLPDVNKQQALAFAQKLRKAVNSLNIEHKASLnadHITISIGIASMENGNASAEQaLLEQADLGLYAAKDAG 292
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPL---YLTISIGVAAYPNPGEDAED-LLKRADTALYQAKKAG 156

                   ....*
gi 567929123   293 RDQVV 297
Cdd:smart00267 157 RNQVA 161
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
133-299 9.71e-52

diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 167.51  E-value: 9.71e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123  133 LASIDGLTEIPNRRYLDENLSREWRRSKRNGSCLSVLLMDIDHFKRYNDCYGHRAGDECLKQVAQALAAQCeRSTDFIAR 212
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSV-RGSDVVGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123  213 YGGEEFAAVLPDVNKQQALAFAQKLRKAVNSLNIEHKASlNADHITISIGIASMENGNASAEQaLLEQADLGLYAAKDAG 292
Cdd:TIGR00254  80 YGGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGS-ETLTVTVSIGVACYPGHGLTLEE-LLKRADEALYQAKKAG 157

                  ....*..
gi 567929123  293 RDQVVAL 299
Cdd:TIGR00254 158 RNRVVVA 164
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
112-296 1.98e-41

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 143.97  E-value: 1.98e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 112 IVKVRVRNQLLIKQKNDLLEMLASIDGLTEIPNRRYLDENLSREWRRSKRNGSCLSVLLMDIDHFKRYNDCYGHRAGDEC 191
Cdd:NF038266  72 IVRISDRYQRMMRDLNEALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRV 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 192 LKQVAQALAAQCeRSTDFIARYGGEEFAAVLPDVNKQQALAFAQKLRKAVNSLniEHKASLNADHITISIGIASMENGNA 271
Cdd:NF038266 152 LVEIARTLRAEL-REYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRAL--AVRVGDDVLSVTASAGLAEHRPPEE 228
                        170       180
                 ....*....|....*....|....*
gi 567929123 272 SAEQALLeQADLGLYAAKDAGRDQV 296
Cdd:NF038266 229 GLSATLS-RADQALYQAKRAGRDRV 252
 
Name Accession Description Interval E-value
pleD PRK09581
response regulator PleD; Reviewed
3-299 4.29e-68

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 219.00  E-value: 4.29e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   3 KKAKILIVDDDPLNRLVLEKTLGTEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVF 82
Cdd:PRK09581 154 EDGRILLVDDDVSQAERIANILKEEFRVVVVSDPSEALFNAAETNYDLVIVSANFENYDPLRLCSQLRSKERTRYVPILL 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123  83 ISANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQLLIKQKNDLLEM-------LASIDGLTEIPNRRYLDENLSRE 155
Cdd:PRK09581 234 LVDEDDDPRLVKALELGVNDYLMRPIDKNELLARVRTQIRRKRYQDALRNnleqsieMAVTDGLTGLHNRRYFDMHLKNL 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 156 WRRSKRNGSCLSVLLMDIDHFKRYNDCYGHRAGDECLKQVAQALAAqCERSTDFIARYGGEEFAAVLPDVNKQQALAFAQ 235
Cdd:PRK09581 314 IERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRN-NIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAE 392
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567929123 236 KLRKAVNSLNIEHKASLNADHITISIGIASMENGNASAEqALLEQADLGLYAAKDAGRDQVVAL 299
Cdd:PRK09581 393 RIRRKIAEEPFIISDGKERLNVTVSIGVAELRPSGDTIE-ALIKRADKALYEAKNTGRNRVVAL 455
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
112-297 1.09e-65

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 207.14  E-value: 1.09e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 112 IVKVRVRNQLLIKQKNDLLEMLASIDGLTEIPNRRYLDENLSREWRRSKRNGSCLSVLLMDIDHFKRYNDCYGHRAGDEC 191
Cdd:COG2199   92 LLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEV 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 192 LKQVAQALAAQCeRSTDFIARYGGEEFAAVLPDVNKQQALAFAQKLRKAVNSLNIEHKAslNADHITISIGIASMENGNA 271
Cdd:COG2199  172 LKEVARRLRASL-RESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEG--KELRVTVSIGVALYPEDGD 248
                        170       180
                 ....*....|....*....|....*.
gi 567929123 272 SAEQaLLEQADLGLYAAKDAGRDQVV 297
Cdd:COG2199  249 SAEE-LLRRADLALYRAKRAGRNRVV 273
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
134-295 5.42e-65

Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 201.33  E-value: 5.42e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123  134 ASIDGLTEIPNRRYLDENLSREWRRSKRNGSCLSVLLMDIDHFKRYNDCYGHRAGDECLKQVAQALaAQCERSTDFIARY 213
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRL-SSSLRRSDLVARL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123  214 GGEEFAAVLPDVNKQQALAFAQKLRKAVNSLNIEHKASLNADHITISIGIASMENGNASAEQaLLEQADLGLYAAKDAGR 293
Cdd:pfam00990  80 GGDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPED-LLKRADTALYQAKQAGR 158

                  ..
gi 567929123  294 DQ 295
Cdd:pfam00990 159 NR 160
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
136-297 3.41e-64

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 198.93  E-value: 3.41e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 136 IDGLTEIPNRRYLDENLSREWRRSKRNGSCLSVLLMDIDHFKRYNDCYGHRAGDECLKQVAQALAAQCeRSTDFIARYGG 215
Cdd:cd01949    2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSL-RESDLVARLGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 216 EEFAAVLPDVNKQQALAFAQKLRKAVNSLNIEHKASLnadHITISIGIASMENGNASAEQaLLEQADLGLYAAKDAGRDQ 295
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEI---RVTASIGIATYPEDGEDAEE-LLRRADEALYRAKRSGRNR 156

                 ..
gi 567929123 296 VV 297
Cdd:cd01949  157 VV 158
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
133-297 4.12e-58

diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 183.60  E-value: 4.12e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   133 LASIDGLTEIPNRRYLDENLSREWRRSKRNGSCLSVLLMDIDHFKRYNDCYGHRAGDECLKQVAQALAAQCeRSTDFIAR 212
Cdd:smart00267   2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCL-RPGDLLAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   213 YGGEEFAAVLPDVNKQQALAFAQKLRKAVNSLNIEHKASLnadHITISIGIASMENGNASAEQaLLEQADLGLYAAKDAG 292
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPL---YLTISIGVAAYPNPGEDAED-LLKRADTALYQAKKAG 156

                   ....*
gi 567929123   293 RDQVV 297
Cdd:smart00267 157 RNQVA 161
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
4-289 3.09e-53

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: 172.02  E-value: 3.09e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   4 KAKILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVF 82
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAgYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123  83 ISANNSHTDEAKGLELGAMDYITKPFNASIVKVRVrnqllikqkndllemlasidglteipnrryldenlsrewrrskrn 162
Cdd:COG3706   81 LTALDDEEDRARALEAGADDYLTKPFDPEELLARV--------------------------------------------- 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 163 gsclsvllmdidhfkryndcyghragdeclkqvaqalaaqcerstDFIARYGGEEFAAVLPDVNKQQALAFAQKLRKAVn 242
Cdd:COG3706  116 ---------------------------------------------DLVARYGGEEFAILLPGTDLEGALAVAERIREAV- 149
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 567929123 243 slniehkASLNADHITISIGIasmengnasAEQALLEQADlGLYAAK 289
Cdd:COG3706  150 -------AELPSLRVTVSIGV---------AGDSLLKRAD-ALYQAR 179
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
133-299 9.71e-52

diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 167.51  E-value: 9.71e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123  133 LASIDGLTEIPNRRYLDENLSREWRRSKRNGSCLSVLLMDIDHFKRYNDCYGHRAGDECLKQVAQALAAQCeRSTDFIAR 212
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSV-RGSDVVGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123  213 YGGEEFAAVLPDVNKQQALAFAQKLRKAVNSLNIEHKASlNADHITISIGIASMENGNASAEQaLLEQADLGLYAAKDAG 292
Cdd:TIGR00254  80 YGGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGS-ETLTVTVSIGVACYPGHGLTLEE-LLKRADEALYQAKKAG 157

                  ....*..
gi 567929123  293 RDQVVAL 299
Cdd:TIGR00254 158 RNRVVVA 164
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
124-297 8.65e-46

Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];


Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 163.79  E-value: 8.65e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 124 KQKNDLLEMLASIDGLTEIPNRRYLDENLSREWRRSKRNGSCLSVLLMDIDHFKRYNDCYGHRAGDECLKQVAQALAAQC 203
Cdd:COG5001  241 KRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACL 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 204 eRSTDFIARYGGEEFAAVLPDV-NKQQALAFAQKLRKAVN-SLNIEHKaSLnadHITISIGIASMENGNASAEQaLLEQA 281
Cdd:COG5001  321 -REGDTVARLGGDEFAVLLPDLdDPEDAEAVAERILAALAePFELDGH-EL---YVSASIGIALYPDDGADAEE-LLRNA 394
                        170
                 ....*....|....*.
gi 567929123 282 DLGLYAAKDAGRDQVV 297
Cdd:COG5001  395 DLAMYRAKAAGRNRYR 410
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
2-134 9.26e-43

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: 146.46  E-value: 9.26e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   2 SKKAKILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPI 80
Cdd:COG3437    4 GQAPTVLIVDDDPENLELLRQLLRTLgYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPV 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 567929123  81 VFISANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQLLIKQKNDLLEMLA 134
Cdd:COG3437   84 IFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLV 137
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
112-296 1.98e-41

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 143.97  E-value: 1.98e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 112 IVKVRVRNQLLIKQKNDLLEMLASIDGLTEIPNRRYLDENLSREWRRSKRNGSCLSVLLMDIDHFKRYNDCYGHRAGDEC 191
Cdd:NF038266  72 IVRISDRYQRMMRDLNEALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRV 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 192 LKQVAQALAAQCeRSTDFIARYGGEEFAAVLPDVNKQQALAFAQKLRKAVNSLniEHKASLNADHITISIGIASMENGNA 271
Cdd:NF038266 152 LVEIARTLRAEL-REYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRAL--AVRVGDDVLSVTASAGLAEHRPPEE 228
                        170       180
                 ....*....|....*....|....*
gi 567929123 272 SAEQALLeQADLGLYAAKDAGRDQV 296
Cdd:NF038266 229 GLSATLS-RADQALYQAKRAGRDRV 252
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
98-298 3.98e-40

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 147.08  E-value: 3.98e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123  98 LGAMDYITkpfnASIVKVRVRNQLLIKQKndlLEMLASIDGLTEIPNRRYLDENLSREWRRSKRNGSCLSVLLMDIDHFK 177
Cdd:PRK15426 369 FTAMLLIS----WYVIRRMVSNMFVLQSS---LQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFK 441
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 178 RYNDCYGHRAGDECLKQVAQALAAQCeRSTDFIARYGGEEFAAVLPDVNKQQALAFAQKLRKAVNSLNIEHKASLNAdHI 257
Cdd:PRK15426 442 SINDRFGHQAGDRVLSHAAGLISSSL-RAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTTI-RI 519
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 567929123 258 TISIGIASM-ENGNASAEQaLLEQADLGLYAAKDAGRDQVVA 298
Cdd:PRK15426 520 SASLGVSSAeEDGDYDFEQ-LQSLADRRLYLAKQAGRNRVCA 560
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
7-108 1.22e-38

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: 131.86  E-value: 1.22e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVFISA 85
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAgYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTA 80
                         90       100
                 ....*....|....*....|...
gi 567929123  86 NNSHTDEAKGLELGAMDYITKPF 108
Cdd:cd19920   81 LTDTEDKVKGFELGAVDYITKPF 103
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
6-108 1.40e-38

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: 131.47  E-value: 1.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVFIS 84
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEgYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                         90       100
                 ....*....|....*....|....
gi 567929123  85 ANNSHTDEAKGLELGAMDYITKPF 108
Cdd:cd17538   81 ALDDREDRIRGLEAGADDFLSKPI 104
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
4-121 2.86e-37

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: 131.62  E-value: 2.86e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   4 KAKILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPitQSIPIVF 82
Cdd:COG0745    1 MPRILVVEDDPDIRELLADALEREgYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARP--SDIPIIM 78
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 567929123  83 ISANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:COG0745   79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALL 117
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
2-121 5.45e-36

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: 125.73  E-value: 5.45e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   2 SKKAKILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPI 80
Cdd:COG0784    3 LGGKRILVVDDNPDNRELLRRLLERLgYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPI 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 567929123  81 VFISANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:COG0784   83 IALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLL 123
PRK09894 PRK09894
diguanylate cyclase; Provisional
126-297 9.41e-33

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 122.10  E-value: 9.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 126 KNDLLEMLASIDGLTEIPNRRYLDENLSREwrRSKRNGSCLSVLLMDIDHFKRYNDCYGHRAGDECLKQVAQALAAQCeR 205
Cdd:PRK09894 121 KIYLLTIRSNMDVLTGLPGRRVLDESFDHQ--LRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWT-R 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 206 STDFIARYGGEEFAAVLPDVNKQQALAFAQKLRKAVNSLNIEHkaslnADH---ITISIGIASMENGNASAEqaLLEQAD 282
Cdd:PRK09894 198 DYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITH-----SDGrinITATFGVSRAFPEETLDV--VIGRAD 270
                        170
                 ....*....|....*
gi 567929123 283 LGLYAAKDAGRDQVV 297
Cdd:PRK09894 271 RAMYEGKQTGRNRVM 285
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
8-107 4.65e-32

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: 114.43  E-value: 4.65e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   8 LIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITqsIPIVFISAN 86
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEgYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSD--IPIIMLTAK 78
                         90       100
                 ....*....|....*....|.
gi 567929123  87 NSHTDEAKGLELGAMDYITKP 107
Cdd:cd17574   79 DEEEDKVLGLELGADDYITKP 99
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
5-119 4.84e-31

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: 112.54  E-value: 4.84e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   5 AKILIVDDDPLNRLVLEKTLGTEHDVFLVESGE--KALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVF 82
Cdd:cd17551    1 MRILIVDDNPTNLLLLEALLRSAGYLEVVSFTDprEALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVM 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 567929123  83 ISANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRN 119
Cdd:cd17551   81 ITADTDREVRLRALEAGATDFLTKPFDPVELLARVRN 117
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
8-107 4.05e-30

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: 109.62  E-value: 4.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   8 LIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPitQSIPIVFISAN 86
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREgYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELP--PDIPVIVLTAK 78
                         90       100
                 ....*....|....*....|.
gi 567929123  87 NSHTDEAKGLELGAMDYITKP 107
Cdd:cd00156   79 ADEEDAVRALELGADDYLVKP 99
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
3-121 3.24e-29

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: 115.06  E-value: 3.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   3 KKAKILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPitQSIPIV 81
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAgYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALD--PDLPVI 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 567929123  82 FISANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:COG2204   79 LLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERAL 118
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
7-118 6.73e-29

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: 106.85  E-value: 6.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123    7 ILIVDDDPLNRLVLEKTLGTEH-DVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITqsIPIVFISA 85
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGyVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPT--TPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 567929123   86 NNSHTDEAKGLELGAMDYITKPFNASIVKVRVR 118
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
8-118 1.06e-28

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: 106.20  E-value: 1.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   8 LIVDDDP-LNRLV---LEKTlgtEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVFI 83
Cdd:cd19937    1 LVVDDEEdIVELLkynLEKE---GYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIML 77
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 567929123  84 SANNSHTDEAKGLELGAMDYITKPFNASIVKVRVR 118
Cdd:cd19937   78 TAKGEEFDKVLGLELGADDYITKPFSPRELLARVK 112
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
3-129 2.39e-27

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 103.51  E-value: 2.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   3 KKAKILIVDDDP----LNRLVLEKTLGTEHdVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENpiTQSI 78
Cdd:COG4565    2 KMIRVLIVEDDPmvaeLLRRYLERLPGFEV-VGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRAR--GPDV 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 567929123  79 PIVFISANNSHTDEAKGLELGAMDYITKPFNASIVK------VRVRNQLLIKQKNDL 129
Cdd:COG4565   79 DVIVITAARDPETVREALRAGVVDYLIKPFTFERLRealeryLEYRRLLREDQEEDL 135
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
6-109 4.36e-27

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: 102.24  E-value: 4.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLV----LEKTLGTEhdVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIV 81
Cdd:cd17552    3 RILVIDDEEDIREVvqacLEKLAGWE--VLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVI 80
                         90       100
                 ....*....|....*....|....*...
gi 567929123  82 FISANNSHTDEAKGLELGAMDYITKPFN 109
Cdd:cd17552   81 LLTAKAQPSDRQRFASLGVAGVIAKPFD 108
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
1-121 2.08e-26

Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 100.25  E-value: 2.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   1 MSKKakILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKEnpITQSIP 79
Cdd:COG5803    1 MMKK--ILIVDDQAGIRMLLKEVLKKEgYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKE--IDPDIP 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 567929123  80 IVFISA--NNSHTDEAKglELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:COG5803   77 VIMMTAygELDMVEEAK--ELGAKGYFTKPFDIDELREAVNKLL 118
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
7-111 1.34e-25

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: 97.93  E-value: 1.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENP-ITQSIPIVFIS 84
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLgYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEgGGRRTPIIALT 80
                         90       100
                 ....*....|....*....|....*..
gi 567929123  85 ANNSHTDEAKGLELGAMDYITKPFNAS 111
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLD 107
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
6-107 1.99e-25

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: 97.15  E-value: 1.99e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTEHDVFLV---ESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPitQSIPIVF 82
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEWEAGFEVVgeaENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELD--PDTKIII 78
                         90       100
                 ....*....|....*....|....*
gi 567929123  83 ISANNSHTDEAKGLELGAMDYITKP 107
Cdd:COG4753   79 LSGYSDFEYAQEAIKLGADDYLLKP 103
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
134-296 2.16e-25

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 106.30  E-value: 2.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123  134 ASIDGLTEIPNRRYLDENLSREWRRSKRNGSCLSVLLMDIDHFKRYNDCYGHRAGDECLKQVAQaLAAQCERSTDFIARY 213
Cdd:PRK09776  665 ASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELAS-LMLSMLRSSDVLARL 743
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123  214 GGEEFAAVLPDVNKQQALAFAQKLRKAVNSLNIEHKASLNadHITISIGIASMENGNASAEQaLLEQADLGLYAAKDAGR 293
Cdd:PRK09776  744 GGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGRVY--RVGASAGITLIDANNHQASE-VMSQADIACYAAKNAGR 820

                  ...
gi 567929123  294 DQV 296
Cdd:PRK09776  821 GRV 823
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
5-121 3.49e-25

phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response regulator protein acting with PhoR in a 2-component system responding to phosphate ion. PhoB acts as a positive regulator of gene expression for phosphate-related genes such as phoA, phoS, phoE and ugpAB as well as itself. It is often found proximal to genes for the high-affinity phosphate ABC transporter (pstSCAB; GenProp0190) and presumably regulates these as well. [Regulatory functions, DNA interactions, Signal transduction, Two-component systems]


Pssm-ID: 131209 [Multi-domain]  Cd Length: 226  Bit Score: 100.48  E-value: 3.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123    5 AKILIVDDDP----LNRLVLEKTlgtEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPI 80
Cdd:TIGR02154   3 RRILVVEDEPaireLIAYNLEKA---GYDVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRRLRRRPETRAIPI 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 567929123   81 VFISANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:TIGR02154  80 IMLTARGEEEDRVRGLETGADDYITKPFSPRELLARIKAVL 120
orf27 CHL00148
Ycf27; Reviewed
2-121 1.95e-24

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 98.64  E-value: 1.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   2 SKKAKILIVDDDPLNRLVLEKTLG-TEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKenpiTQS-IP 79
Cdd:CHL00148   4 NSKEKILVVDDEAYIRKILETRLSiIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIR----KESdVP 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 567929123  80 IVFISANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:CHL00148  80 IIMLTALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVL 121
adrA PRK10245
diguanylate cyclase AdrA; Provisional
130-295 2.27e-24

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 101.06  E-value: 2.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 130 LEMLASIDGLTEIPNRRYLDENLSREWRRSKRNGSCLSVLLMDIDHFKRYNDCYGHRAGDECLkqvaQALAAQCE---RS 206
Cdd:PRK10245 201 LQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAI----VALTRQLQitlRG 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 207 TDFIARYGGEEFAAVLPDVNKQQALAFAQKLRKAVNSLNIEhkaslNADHIT--ISIGIASMeNGNASAEQALLEQADLG 284
Cdd:PRK10245 277 SDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLP-----NAPQVTlrISVGVAPL-NPQMSHYREWLKSADLA 350
                        170
                 ....*....|.
gi 567929123 285 LYAAKDAGRDQ 295
Cdd:PRK10245 351 LYKAKNAGRNR 361
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
6-109 1.90e-23

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: 92.60  E-value: 1.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVFIS 84
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAgYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALT 80
                         90       100
                 ....*....|....*....|....*
gi 567929123  85 ANNSHTDEAKGLELGAMDYITKPFN 109
Cdd:cd17548   81 AYAMKGDREKILEAGCDGYISKPID 105
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
6-109 4.66e-23

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 94.88  E-value: 4.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTEHDVFLV---ESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPitQSIPIVF 82
Cdd:COG3279    3 KILIVDDEPLARERLERLLEKYPDLEVVgeaSNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELD--PPPPIIF 80
                         90       100
                 ....*....|....*....|....*..
gi 567929123  83 ISANNSHTdeAKGLELGAMDYITKPFN 109
Cdd:COG3279   81 TTAYDEYA--LEAFEVNAVDYLLKPID 105
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
7-107 1.08e-22

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: 89.81  E-value: 1.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITqsIPIVFISA 85
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEgYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQ--TPVLMLTA 78
                         90       100
                 ....*....|....*....|..
gi 567929123  86 NNSHTDEAKGLELGAMDYITKP 107
Cdd:cd19935   79 RDSVEDRVKGLDLGADDYLVKP 100
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
7-119 3.28e-22

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: 88.98  E-value: 3.28e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENpitQSIPIVFISA 85
Cdd:cd17619    3 ILIVEDEPVTRATLKSYFEQEgYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQ---SEVGIILVTG 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 567929123  86 NNSHTDEAKGLELGAMDYITKPFNASIVKVRVRN 119
Cdd:cd17619   80 RDDEVDRIVGLEIGADDYVTKPFNPRELLVRAKN 113
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
7-118 4.64e-22

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: 88.98  E-value: 4.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPItqSIPIVFISA 85
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEgYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGN--DLPILVLTA 78
                         90       100       110
                 ....*....|....*....|....*....|...
gi 567929123  86 NNSHTDEAKGLELGAMDYITKPFNASIVKVRVR 118
Cdd:cd17627   79 RDSVSDRVAGLDAGADDYLVKPFALEELLARVR 111
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
8-118 1.62e-21

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: 87.28  E-value: 1.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   8 LIVDDDP-LNRLVLEKTLGTEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPItqSIPIVFISAN 86
Cdd:cd17625    1 LVVEDEKdLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGI--ETPVLLLTAL 78
                         90       100       110
                 ....*....|....*....|....*....|..
gi 567929123  87 NSHTDEAKGLELGAMDYITKPFNASIVKVRVR 118
Cdd:cd17625   79 DAVEDRVKGLDLGADDYLPKPFSLAELLARIR 110
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
5-118 2.72e-21

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: 86.51  E-value: 2.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   5 AKILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKEnpITQSIPIVFI 83
Cdd:cd17554    1 KKILVVDDEENIRELYKEELEDEgYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIRE--KKPDLPVIIC 78
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 567929123  84 SANNSHTDEAKglELGAMDYITKPFNASIVKVRVR 118
Cdd:cd17554   79 TAYSEYKSDFS--SWAADAYVVKSSDLTELKETIK 111
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
7-122 4.26e-21

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: 86.23  E-value: 4.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVFISA 85
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQgYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 567929123  86 NNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQLL 122
Cdd:cd17598   81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYILV 117
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
5-118 5.95e-21

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: 85.76  E-value: 5.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   5 AKILIVDDDP----LNRLVLEKTlgtEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPI 80
Cdd:cd17618    1 RTILIVEDEPaireMIAFNLERA---GFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPI 77
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 567929123  81 VFISANNSHTDEAKGLELGAMDYITKPFNASIVKVRVR 118
Cdd:cd17618   78 IMLTARGEEEDKVRGLEAGADDYITKPFSPRELVARIK 115
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
6-109 6.01e-21

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: 86.32  E-value: 6.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDP----LNRLVLEKtLGTEHDVFLVESGEKALTFI----KSNQV---DLIILDVVMPGIDGYEVLVQLKENPI 74
Cdd:cd17557    1 TILLVEDNPgdaeLIQEAFKE-AGVPNELHVVRDGEEALDFLrgegEYADAprpDLILLDLNMPRMDGFEVLREIKADPD 79
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 567929123  75 TQSIPIVFISANNSHTDEAKGLELGAMDYITKPFN 109
Cdd:cd17557   80 LRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVD 114
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
6-107 3.34e-20

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: 83.98  E-value: 3.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTEHDVFLV---ESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKEnpiTQSIPIVF 82
Cdd:cd17541    2 RVLIVDDSAVMRKLLSRILESDPDIEVVgtaRDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMA---ERPTPVVM 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 567929123  83 ISannSHTDE-----AKGLELGAMDYITKP 107
Cdd:cd17541   79 VS---SLTEEgaeitLEALELGAVDFIAKP 105
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
5-109 6.79e-20

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: 83.12  E-value: 6.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   5 AKILIVDDDPLNRLVLEKTL-GTEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVFI 83
Cdd:cd17562    1 KKILAVDDSASIRQMVSFTLrGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILML 80
                         90       100
                 ....*....|....*....|....*.
gi 567929123  84 SANNSHTDEAKGLELGAMDYITKPFN 109
Cdd:cd17562   81 TTESSDEKKQEGKAAGATGWLVKPFD 106
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
7-121 6.93e-20

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: 82.93  E-value: 6.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKE-NPitqSIPIVFIS 84
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEgYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEkYP---DLPVIMIS 77
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 567929123  85 ANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:cd17550   78 GHGTIETAVKATKLGAYDFIEKPLSLDRLLLTIERAL 114
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
7-109 7.21e-20

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: 82.89  E-value: 7.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVFISA 85
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEgAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTG 80
                         90       100
                 ....*....|....*....|....
gi 567929123  86 NNSHTDEAKGLELGAMDYITKPFN 109
Cdd:cd17580   81 YGQPEDRERALEAGFDAHLVKPVD 104
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
165-265 1.20e-19

Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.


Pssm-ID: 143637 [Multi-domain]  Cd Length: 133  Bit Score: 82.79  E-value: 1.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 165 CLSVLLMDIDHFKRYNDCYGHRAGDECLKQVAQALAAQCERSTDFIARYGGEEFAAVLPDVNKQQALAFAQKLRKAVNSL 244
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80
                         90       100
                 ....*....|....*....|.
gi 567929123 245 NIEhkaSLNadHITISIGIAS 265
Cdd:cd07556   81 NQS---EGN--PVRVRIGIHT 96
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
6-121 1.74e-19

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: 82.04  E-value: 1.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDP-LNRLVLEKTLGTEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKenPITQSiPIVFIS 84
Cdd:cd17622    2 RILLVEDDPkLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLR--PKYQG-PILLLT 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 567929123  85 ANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:cd17622   79 ALDSDIDHILGLELGADDYVVKPVEPAVLLARLRALL 115
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
7-118 4.19e-19

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: 80.81  E-value: 4.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDD-PLNRLVLEKTLGTEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPitqSIPIVFISA 85
Cdd:cd17623    1 ILLIDDDrELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTS---QVPVLMLTA 77
                         90       100       110
                 ....*....|....*....|....*....|...
gi 567929123  86 NNSHTDEAKGLELGAMDYITKPFNASIVKVRVR 118
Cdd:cd17623   78 RGDDIDRILGLELGADDYLPKPFNPRELVARIR 110
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
7-107 4.46e-19

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: 80.29  E-value: 4.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENpitQSIPIVFISA 85
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHgYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREW---SAVPVIVLSA 77
                         90       100
                 ....*....|....*....|..
gi 567929123  86 NNSHTDEAKGLELGAMDYITKP 107
Cdd:cd17620   78 RDEESDKIAALDAGADDYLTKP 99
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
7-121 4.80e-19

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: 80.93  E-value: 4.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKEnpiTQSIPIVFISA 85
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEgYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRK---TSNVPIIMLTA 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 567929123  86 NNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:cd17614   78 KDSEVDKVLGLELGADDYVTKPFSNRELLARVKANL 113
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
7-121 6.84e-19

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: 80.40  E-value: 6.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGT-EHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKenpiTQS-IPIVFIS 84
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKwGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIR----QISnVPIIFIS 76
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 567929123  85 ANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:cd18159   77 SRDDNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
7-107 8.25e-19

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: 79.73  E-value: 8.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVFISA 85
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQgFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80
                         90       100
                 ....*....|....*....|..
gi 567929123  86 NNSHTDEAKGLELGAMDYITKP 107
Cdd:cd19927   81 KGMTSDRIKGYNAGCDGYLSKP 102
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
5-121 8.28e-19

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: 80.21  E-value: 8.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   5 AKILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKEnpiTQSIPIVFI 83
Cdd:cd17626    1 ARILVVDDDAALAEMIGIVLRGEgFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRA---ESGVPIVML 77
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 567929123  84 SANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:cd17626   78 TAKSDTVDVVLGLESGADDYVAKPFKPKELVARIRARL 115
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
6-114 9.72e-19

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: 79.89  E-value: 9.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTL--GTEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPItqSIPIVFI 83
Cdd:cd17593    2 KVLICDDSSMARKQLARALpaDWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQL--ETKVIVV 79
                         90       100       110
                 ....*....|....*....|....*....|...
gi 567929123  84 SANNShtDEAKG--LELGAMDYITKPFNASIVK 114
Cdd:cd17593   80 SGDVQ--PEAKErvLELGALAFLKKPFDPEKLA 110
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
3-118 1.13e-18

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 82.70  E-value: 1.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   3 KKAKILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPitQSIPIV 81
Cdd:PRK11083   2 QQPTILLVEDEQAIADTLVYALQSEgFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFH--PALPVI 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 567929123  82 FISANNSHTDEAKGLELGAMDYITKPFNASIVKVRVR 118
Cdd:PRK11083  80 FLTARSDEVDRLVGLEIGADDYVAKPFSPREVAARVR 116
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
6-118 1.16e-18

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: 79.70  E-value: 1.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKEnpITQSIPIVFIS 84
Cdd:cd17615    1 RVLVVDDEPNITELLSMALRYEgWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRA--DGPDVPVLFLT 78
                         90       100       110
                 ....*....|....*....|....*....|....
gi 567929123  85 ANNSHTDEAKGLELGAMDYITKPFNASIVKVRVR 118
Cdd:cd17615   79 AKDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLR 112
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
7-109 1.89e-18

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: 79.30  E-value: 1.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKT-----LGTEHdVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKE-NPitqSIPI 80
Cdd:cd17536    1 VLIVDDEPLIREGLKKLidweeLGFEV-VGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRElYP---DIKI 76
                         90       100       110
                 ....*....|....*....|....*....|....
gi 567929123  81 VFISAnnsHTD-----EAkgLELGAMDYITKPFN 109
Cdd:cd17536   77 IILSG---YDDfeyaqKA--IRLGVVDYLLKPVD 105
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
7-121 2.34e-18

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: 79.16  E-value: 2.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITqsIPIVFISA 85
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEgYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLP--TSVIVITA 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 567929123  86 NNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:cd17572   79 HGSVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNAL 114
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
7-109 2.75e-18

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: 78.82  E-value: 2.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTEHD-VFLVESGEKALTFI--KSNQVDLIILDVVMPGIDGYEVLVQLKENPitqSIPIVFI 83
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYqVTTCTDAEEALSMLreNKDEFDLVITDVHMPDMDGFEFLELIRLEM---DLPVIMM 77
                         90       100
                 ....*....|....*....|....*.
gi 567929123  84 SANNSHTDEAKGLELGAMDYITKPFN 109
Cdd:cd17584   78 SADGSTSTVMKGLAHGACDYLLKPVS 103
ompR PRK09468
osmolarity response regulator; Provisional
1-109 3.57e-18

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 81.56  E-value: 3.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   1 MSKKAKILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENpiTQSIP 79
Cdd:PRK09468   2 MQENYKILVVDDDMRLRALLERYLTEQgFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQ--NNPTP 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 567929123  80 IVFISANNSHTDEAKGLELGAMDYITKPFN 109
Cdd:PRK09468  80 IIMLTAKGEEVDRIVGLEIGADDYLPKPFN 109
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
7-111 3.69e-18

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: 78.35  E-value: 3.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTEHDVFLV---ESGEKALTFIKSNQVDLIILDVVMPGIDGYEV---LVQLKENPItqsipI 80
Cdd:cd17532    1 ALIVDDEPLAREELRYLLEEHPDIEIVgeaENGEEALEAIEELKPDVVFLDIQMPGLDGLELakkLSKLAKPPL-----I 75
                         90       100       110
                 ....*....|....*....|....*....|.
gi 567929123  81 VFISANNSHTDEAkgLELGAMDYITKPFNAS 111
Cdd:cd17532   76 VFVTAYDEYAVEA--FELNAVDYLLKPFSEE 104
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
5-107 3.91e-18

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: 78.40  E-value: 3.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   5 AKILIVDDDPLNRLVLEKTL-GTEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQL-KENPITqsiPIVF 82
Cdd:cd17555    1 ATILVIDDDEVVRESIAAYLeDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQItKESPDT---PVIV 77
                         90       100
                 ....*....|....*....|....*
gi 567929123  83 ISANNSHTDEAKGLELGAMDYITKP 107
Cdd:cd17555   78 VSGAGVMSDAVEALRLGAWDYLTKP 102
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
7-107 4.35e-18

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: 78.19  E-value: 4.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGT-EHDVFLVESGEKALTFIK---------SNQVDLIILDVVMPGIDGYEVLVQLKENPITQ 76
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNlGFEIAEAVDGEEALNKLEnlakegndlSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 567929123  77 SIPIVFISANNSHTDEAKGLELGAMDYITKP 107
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
5-115 4.99e-18

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: 78.22  E-value: 4.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   5 AKILIVDDDPLNRLVLEKTLGTE-HDVF-LVESGEKALTFIKSNQVDLIILDVVMPG-IDGYEVLVQLKENpitQSIPIV 81
Cdd:cd17534    1 KKILIVEDEAIIALDLKEILESLgYEVVgIADSGEEAIELAEENKPDLILMDINLKGdMDGIEAAREIREK---FDIPVI 77
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 567929123  82 FISAnnsHTDEA---KGLELGAMDYITKPFNASIVKV 115
Cdd:cd17534   78 FLTA---YSDEEtleRAKETNPYGYLVKPFNERELKA 111
Spo0A COG5801
Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell ...
1-118 5.52e-18

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: 81.77  E-value: 5.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   1 MSKKAKILIVDDDPLNRLVLEKTLGTEHDVFLV---ESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQS 77
Cdd:COG5801    1 MMEKIKVLIADDNREFCELLEEYLSSQPDMEVVgvaYNGLEALELIEEKKPDVVILDIIMPHLDGLGVLEKLREMNLEKR 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 567929123  78 IPIVFISANNSHTDEAKGLELGAMDYITKPFNASIVKVRVR 118
Cdd:COG5801   81 PKVIMLTAFGQEDITQRAVELGADYYILKPFDLDVLAERIR 121
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
6-118 7.33e-18

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: 77.42  E-value: 7.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDP-LNRLVLEKTLGTEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPitqSIPIVFIS 84
Cdd:cd19938    1 RILIVEDEPkLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFS---DVPIIMVT 77
                         90       100       110
                 ....*....|....*....|....*....|....
gi 567929123  85 ANNSHTDEAKGLELGAMDYITKPFNASIVKVRVR 118
Cdd:cd19938   78 ARVEEIDRLLGLELGADDYICKPYSPREVVARVK 111
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
130-295 9.05e-18

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 83.58  E-value: 9.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 130 LEMLASIDGLTEIPNRRYLDENLSREWRRskRNGSCLSVLLMDIDHFKRYNDCYGHRAGDECLKQVAQALAAqCERSTDF 209
Cdd:PRK10060 233 LRILANTDSITGLPNRNAIQELIDHAINA--ADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILS-CLEEDQT 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 210 IARYGGEEFaAVLPDVNKQQAL-AFAQKLrkaVNSLNIEHKASLNADHITISIGIA-SMENGNASaeQALLEQADLGLYA 287
Cdd:PRK10060 310 LARLGGDEF-LVLASHTSQAALeAMASRI---LTRLRLPFRIGLIEVYTGCSIGIAlAPEHGDDS--ESLIRSADTAMYT 383

                 ....*...
gi 567929123 288 AKDAGRDQ 295
Cdd:PRK10060 384 AKEGGRGQ 391
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
7-118 1.35e-17

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: 76.75  E-value: 1.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENpiTQSIPIVFISA 85
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAgYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQ--GQSLPVLILTA 78
                         90       100       110
                 ....*....|....*....|....*....|...
gi 567929123  86 NNSHTDEAKGLELGAMDYITKPFNASIVKVRVR 118
Cdd:cd17624   79 RDGVDDRVAGLDAGADDYLVKPFALEELLARLR 111
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
7-106 1.56e-17

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: 76.78  E-value: 1.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTEHD---VFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKE-NPitqSIPIVF 82
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLESEPDievVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRrYP---DLKVIV 77
                         90       100
                 ....*....|....*....|....
gi 567929123  83 ISANNSHTDEAKGLELGAMDYITK 106
Cdd:cd17535   78 LTAHDDPEYVLRALKAGAAGYLLK 101
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
6-108 1.97e-17

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: 76.54  E-value: 1.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTEH-DVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKEN-PitqSIPIVFI 83
Cdd:cd19919    2 TVWIVDDDSSIRWVLERALAGAGlTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRhP---DLPVIIM 78
                         90       100
                 ....*....|....*....|....*.
gi 567929123  84 SAnNSHTDEA-KGLELGAMDYITKPF 108
Cdd:cd19919   79 TA-HSDLDSAvSAYQGGAFEYLPKPF 103
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
7-114 2.39e-17

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: 76.25  E-value: 2.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTL-GTEHDVFLVESGEKALTFIKSN-----------QVDLIILDVVMPGIDGYEVLVQLKENPI 74
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLrISSCRVTAVDSGKRALEFLGLEdeedssnfnepKVNMIITDYCMPGMTGYDLLKKVKESSA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 567929123  75 TQSIPIVFISANNSHTDEAKGLELGAMDYITKPFNASIVK 114
Cdd:cd17581   81 LKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLADVK 120
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
6-118 3.59e-17

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 78.69  E-value: 3.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNqVDLIILDVVMPGIDGYEVLVQLKENpitQSIPIVFIS 84
Cdd:PRK10955   3 KILLVDDDRELTSLLKELLEMEgFNVIVAHDGEQALDLLDDS-IDLLLLDVMMPKKNGIDTLKELRQT---HQTPVIMLT 78
                         90       100       110
                 ....*....|....*....|....*....|....
gi 567929123  85 ANNSHTDEAKGLELGAMDYITKPFNASIVKVRVR 118
Cdd:PRK10955  79 ARGSELDRVLGLELGADDYLPKPFNDRELVARIR 112
PRK11173 PRK11173
two-component response regulator; Provisional
6-121 5.95e-17

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 78.13  E-value: 5.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENpitQSIPIVFIS 84
Cdd:PRK11173   5 HILIVEDELVTRNTLKSIFEAEgYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQ---ANVALMFLT 81
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 567929123  85 ANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:PRK11173  82 GRDNEVDKILGLEIGADDYITKPFNPRELTIRARNLL 118
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
6-121 1.01e-16

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: 74.72  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDD-PLNRLVLEKTLGTEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENpitQSIPIVFIS 84
Cdd:cd19939    1 RILIVEDElELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREH---SHVPILMLT 77
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 567929123  85 ANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:cd19939   78 ARTEEMDRVLGLEMGADDYLCKPFSPRELLARVRALL 114
PLN03029 PLN03029
type-a response regulator protein; Provisional
7-163 2.79e-16

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 76.23  E-value: 2.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFI------KSN--------------QVDLIILDVVMPGIDGYEV 65
Cdd:PLN03029  11 VLAVDDSLIDRKLIEKLLKTSsYQVTTVDSGSKALKFLglheddRSNpdtpsvspnshqevEVNLIITDYCMPGMTGYDL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123  66 LVQLKENPITQSIPIVFISANNSHTDEAKGLELGAMDYITKPFNAS--------IVKVRVRNQLLIKQKNDLLEMLASID 137
Cdd:PLN03029  91 LKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSdlnrlkphMMKTKSKNQKQENQEKQEKLEESEIQ 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 567929123 138 G------------------LTEIPN---RRYLDENLSREWRRSKRNG 163
Cdd:PLN03029 171 SekqeqpsqqpqsqpqpqqQPQQPNnnkRKAMEEGLSPDRTRPRYNG 217
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
7-107 4.06e-16

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: 72.62  E-value: 4.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKEnpiTQSIPIVFISA 85
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEgFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRA---RSNVPVIMVTA 77
                         90       100
                 ....*....|....*....|..
gi 567929123  86 NNSHTDEAKGLELGAMDYITKP 107
Cdd:cd17621   78 KDSEIDKVVGLELGADDYVTKP 99
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
7-109 9.66e-16

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: 72.14  E-value: 9.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKEnpITQSIPIVFISA 85
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAgFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRE--LDPDLPVILITG 78
                         90       100
                 ....*....|....*....|....*..
gi 567929123  86 nnsHTDEA---KGLELGAMDYITKPFN 109
Cdd:cd17549   79 ---HGDVPmavEAMRAGAYDFLEKPFD 102
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
6-109 1.10e-15

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: 71.78  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTEH-DVFLVESGEKALTFIKSN-QVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVFI 83
Cdd:cd17544    2 KVLVVDDSATSRNHLRALLRRHNfQVLEAANGQEALEVLEQHpDIKLVITDYNMPEMDGFELVREIRKKYSRDQLAIIGI 81
                         90       100
                 ....*....|....*....|....*.
gi 567929123  84 SANNSHTDEAKGLELGAMDYITKPFN 109
Cdd:cd17544   82 SASGDNALSARFIKAGANDFLTKPFL 107
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
6-121 1.94e-15

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: 71.16  E-value: 1.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTE--HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKEnpITQSIPIVFI 83
Cdd:cd17542    2 KVLIVDDAAFMRMMLKDILTKAgyEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKK--IDPNAKVIMC 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 567929123  84 SANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:cd17542   80 SAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
PRK10643 PRK10643
two-component system response regulator PmrA;
6-150 1.94e-15

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 73.92  E-value: 1.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQsiPIVFIS 84
Cdd:PRK10643   2 KILIVEDDTLLLQGLILALQTEgYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTL--PVLILT 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567929123  85 ANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRnqLLIKQKNDLLEMLASIDGLTEIPNRR--YLDE 150
Cdd:PRK10643  80 ARDTLEDRVAGLDVGADDYLVKPFALEELHARIR--ALIRRHQGQGENELQVGNLTLNLGRQqvWLDG 145
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
7-118 2.67e-15

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: 70.77  E-value: 2.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDD-PLNRLVLEKTLGTEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITqsIPIVFISA 85
Cdd:cd19934    1 LLLVEDDaLLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRA--TPVLILTA 78
                         90       100       110
                 ....*....|....*....|....*....|...
gi 567929123  86 NNSHTDEAKGLELGAMDYITKPFNASIVKVRVR 118
Cdd:cd19934   79 RDSWQDKVEGLDAGADDYLTKPFHIEELLARLR 111
PRK11517 PRK11517
DNA-binding response regulator HprR;
6-121 3.36e-15

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 73.01  E-value: 3.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTEHDVF-LVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKenpITQSIPIVFIS 84
Cdd:PRK11517   2 KILLIEDNQRTQEWVTQGLSEAGYVIdAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLR---TAKQTPVICLT 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 567929123  85 ANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:PRK11517  79 ARDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQL 115
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
7-107 4.16e-15

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: 69.70  E-value: 4.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVFISA 85
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQgFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTG 80
                         90       100
                 ....*....|....*....|..
gi 567929123  86 NNSHTDEAKGLELGAMDYITKP 107
Cdd:cd17602   81 KDGLVDRIRAKMAGASGYLTKP 102
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
7-107 4.62e-15

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: 69.40  E-value: 4.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENpitQSIPIVFISA 85
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEgFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQK---STLPVIFLTS 77
                         90       100
                 ....*....|....*....|..
gi 567929123  86 NNSHTDEAKGLELGAMDYITKP 107
Cdd:cd19936   78 KDDEIDEVFGLRMGADDYITKP 99
PRK15479 PRK15479
transcriptional regulator TctD;
6-118 1.21e-14

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 71.68  E-value: 1.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENpiTQSIPIVFIS 84
Cdd:PRK15479   2 RLLLAEDNRELAHWLEKALVQNgFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKR--GQTLPVLLLT 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 567929123  85 ANNSHTDEAKGLELGAMDYITKPFNASIVKVRVR 118
Cdd:PRK15479  80 ARSAVADRVKGLNVGADDYLPKPFELEELDARLR 113
PRK10766 PRK10766
two-component system response regulator TorR;
6-121 2.05e-14

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 70.84  E-value: 2.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKEnpiTQSIPIVFIS 84
Cdd:PRK10766   4 HILVVEDEPVTRARLQGYFEQEgYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRS---RSTVGIILVT 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 567929123  85 ANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:PRK10766  81 GRTDSIDRIVGLEMGADDYVTKPLELRELLVRVKNLL 117
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
3-141 2.58e-14

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: 69.99  E-value: 2.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   3 KKAKILIVDDDPLNRLVLEKTLGTE--HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPItqsIPI 80
Cdd:COG3707    2 RGLRVLVVDDEPLRRADLREGLREAgyEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP---APV 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 567929123  81 VFISANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRnqLLIKQKNDLLEMLASIDGLTE 141
Cdd:COG3707   79 ILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALE--LALARFRELRALRRELAKLRE 137
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
7-130 3.50e-14

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: 67.72  E-value: 3.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVFISAN 86
Cdd:cd17539    1 VLLVDDRPSSAERIAAMLSSEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQLPILAVADP 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 567929123  87 NSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQLLIKQKNDLL 130
Cdd:cd17539   81 GDRGRLIRALEIGVNDYLVRPIDPNELLARVRTQIRRKRYTDYL 124
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
7-118 3.69e-14

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: 67.43  E-value: 3.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPItqSIPIVFISA 85
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEgFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKV--KTPILILSG 78
                         90       100       110
                 ....*....|....*....|....*....|...
gi 567929123  86 NNSHTDEAKGLELGAMDYITKPFNASIVKVRVR 118
Cdd:cd17616   79 LADIEDKVKGLGFGADDYMTKPFHKDELVARIH 111
PRK15347 PRK15347
two component system sensor kinase;
4-155 6.65e-14

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 71.98  E-value: 6.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   4 KAKILIVDDDPLNRLVLEKTLgTE--HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENP--ITQSIP 79
Cdd:PRK15347 690 QLQILLVDDVETNRDIIGMML-VElgQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPnnLDPDCM 768
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 567929123  80 IVFISANNSHTDEAKGLELGAMDYITKPfnasivkvrvrnqLLIKQKNDLLEMLASIDGLTEIPnrryLDENLSRE 155
Cdd:PRK15347 769 IVALTANAAPEEIHRCKKAGMNHYLTKP-------------VTLAQLARALELAAEYQLLRGIE----LSPQDSSC 827
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
7-121 7.35e-14

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 69.71  E-value: 7.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDP-LNRLVLEKTLGTEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKEnpiTQSIPIVFISA 85
Cdd:PRK10710  13 ILIVEDEPkLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRR---FSDIPIVMVTA 89
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 567929123  86 NNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:PRK10710  90 KIEEIDRLLGLEIGADDYICKPYSPREVVARVKTIL 125
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
7-118 9.62e-14

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: 68.59  E-value: 9.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITqsIPIVFISA 85
Cdd:COG4566    2 VYIVDDDEAVRDSLAFLLESAgLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSP--LPVIFLTG 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 567929123  86 nnsHTD-----EAkgLELGAMDYITKPFNASIVKVRVR 118
Cdd:COG4566   80 ---HGDvpmavRA--MKAGAVDFLEKPFDDQALLDAVR 112
PRK09966 PRK09966
diguanylate cyclase DgcN;
120-289 1.01e-13

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 70.81  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 120 QLLIKQKNDLLEMLASIDGLTEIPNRRYLDENLSREWRRSKRNgSCLSVLLMDIDHFKRYNDCYGHRAGDECLKQVAQAL 199
Cdd:PRK09966 234 QLRLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDAR-KTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRL 312
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 200 aAQCERSTDFIARYGGEEFAAVLPDVNKQ-QALAFAQKLRKAVN---SLNIEHKASLnadhiTISIGIAsMENGNASAEQ 275
Cdd:PRK09966 313 -AEFGGLRHKAYRLGGDEFAMVLYDVQSEsEVQQICSALTQIFNlpfDLHNGHQTTM-----TLSIGYA-MTIEHASAEK 385
                        170
                 ....*....|....
gi 567929123 276 aLLEQADLGLYAAK 289
Cdd:PRK09966 386 -LQELADHNMYQAK 398
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
6-114 2.58e-13

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


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 65.44  E-value: 2.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGT--EHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVFI 83
Cdd:cd19923    2 KVLVVDDFSTMRRIIKNLLKElgFNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLMV 81
                         90       100       110
                 ....*....|....*....|....*....|.
gi 567929123  84 SANNSHTDEAKGLELGAMDYITKPFNASIVK 114
Cdd:cd19923   82 TAEAKKENVIAAAQAGVNNYIVKPFTAATLK 112
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
6-118 2.74e-13

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 67.82  E-value: 2.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDD-PLNRLVLEKTLGTEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVFIS 84
Cdd:PRK10161   4 RILVVEDEaPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLT 83
                         90       100       110
                 ....*....|....*....|....*....|....
gi 567929123  85 ANNSHTDEAKGLELGAMDYITKPFNASIVKVRVR 118
Cdd:PRK10161  84 ARGEEEDRVRGLETGADDYITKPFSPKELVARIK 117
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
6-107 3.13e-13

phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and similar proteins; Plant ethylene receptors contain N-terminal transmembrane domains that contain an ethylene binding site and also serve in localization of the receptor to the endoplasmic reticulum or the Golgi apparatus and a C-terminal histidine kinase (HK)-like domain. There are five ethylene receptors (ETR1, ERS1, ETR2, ERS2, and EIN4) in Arabidopsis thaliana. ETR1, ETR2, and EIN4 also contain REC domains C-terminal to the HK domain. ETR1 and ERS1 belong to subfamily 1, and have functional HK domains while ETR2, ERS2, and EIN4 belong to subfamily 2, and lack the necessary residues for HK activity and may function as serine/threonine kinases. The plant hormone ethylene plays an important role in plant growth and development. It regulates seed germination, seedling growth, leaf and petal abscission, fruit ripening, organ senescence, and pathogen responses. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 65.11  E-value: 3.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLV---LEKTLGTEhdVFLVESGEKALTFIKSNQVD--LIILDVVMPGIDGYEVLVQLKENPITQSIP- 79
Cdd:cd19933    2 KVLLVDDNAVNRMVtkgLLEKLGCE--VTTVSSGEECLNLLASAEHSfqLVLLDLCMPEMDGFEVALRIRKLFGRRERPl 79
                         90       100
                 ....*....|....*....|....*...
gi 567929123  80 IVFISANNSHTDEAKGLELGAMDYITKP 107
Cdd:cd19933   80 IVALTANTDDSTREKCLSLGMNGVITKP 107
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
6-108 3.82e-13

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: 64.96  E-value: 3.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDP----LNRLVLEKtLGTEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITqsIPIV 81
Cdd:cd19925    2 NVLIVEDDPmvaeIHRAYVEQ-VPGFTVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHD--VDVI 78
                         90       100
                 ....*....|....*....|....*..
gi 567929123  82 FISANNSHTDEAKGLELGAMDYITKPF 108
Cdd:cd19925   79 VVTAANDVETVREALRLGVVDYLIKPF 105
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
1-149 6.52e-13

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 68.99  E-value: 6.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123    1 MSKKAKILIVDDDPLNRLVLEKTLGT-EHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENpiTQSIP 79
Cdd:PRK09959  955 LPEKLSILIADDHPTNRLLLKRQLNLlGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQ--NSSLP 1032
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   80 IVFISANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNqllikqkndlLEMLASIdglteIPNRRYLD 149
Cdd:PRK09959 1033 IWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQ----------LHQVAHI-----APQYRHLD 1087
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
7-107 9.65e-13

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: 63.19  E-value: 9.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTL-GTEHDVFLVESGEKALTFIK--SNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVFI 83
Cdd:cd17582    1 VLLVENDDSTRQIVTALLrKCSYEVTAASDGLQAWDVLEdeQNEIDLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMM 80
                         90       100
                 ....*....|....*....|....
gi 567929123  84 SANNSHTDEAKGLELGAMDYITKP 107
Cdd:cd17582   81 SSQDSVGVVFKCLSKGAADYLVKP 104
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
6-107 1.28e-12

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 67.21  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGT--EHDVFLVES-GEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQL-KENPitqsIPIV 81
Cdd:PRK12555   2 RIGIVNDSPLAVEALRRALARdpDHEVVWVATdGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRImAERP----CPIL 77
                         90       100       110
                 ....*....|....*....|....*....|
gi 567929123  82 FISA----NNSHTDEAkgLELGAMDYITKP 107
Cdd:PRK12555  78 IVTSlterNASRVFEA--MGAGALDAVDTP 105
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
5-109 1.34e-12

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 63.38  E-value: 1.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   5 AKILIVDDDP-----LNRLVleKTLGTEHDVFlvESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPItqSIP 79
Cdd:cd17537    1 ATVYVVDDDEavrdsLAFLL--RSVGLAVKTF--TSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGS--NIP 74
                         90       100       110
                 ....*....|....*....|....*....|...
gi 567929123  80 IVFISAnnsHTD---EAKGLELGAMDYITKPFN 109
Cdd:cd17537   75 IIFITG---HGDvpmAVEAMKAGAVDFLEKPFR 104
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
6-121 1.52e-12

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 65.72  E-value: 1.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLgTEHDvFLVESGEKALT---FIKSNQVDLIILDVVMPGIDGYEVLVQLKEnpITQSIPIVF 82
Cdd:PRK09836   2 KLLIVEDEKKTGEYLTKGL-TEAG-FVVDLADNGLNgyhLAMTGDYDLIILDIMLPDVNGWDIVRMLRS--ANKGMPILL 77
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 567929123  83 ISANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:PRK09836  78 LTALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLL 116
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
7-117 2.89e-12

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: 62.28  E-value: 2.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGT--EHDVFLVESGEKALTFIKSNQVDLIILDVVM-PGIDGYEVLVQLKENP-ITQSIPIVF 82
Cdd:cd17589    1 FLIVDDQPTFRSMLKSMLRSlgVTRIDTASSGEEALRMCENKTYDIVLCDYNLgKGKNGQQLLEELRHKKlISPSTVFIM 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 567929123  83 ISANNSHTDEAKGLELGAMDYITKPFNASIVKVRV 117
Cdd:cd17589   81 VTGESSRAMVLSALELEPDDYLLKPFTVSELRERL 115
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
6-121 3.24e-12

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: 62.19  E-value: 3.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKEnpITQSIPIVFIS 84
Cdd:cd17553    2 KILIVDDQYGIRILLNEVFNKEgYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKV--IDENIRVIIMT 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 567929123  85 ANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:cd17553   80 AYGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
7-107 3.59e-12

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: 61.75  E-value: 3.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKEnpITQSIPIVFISA 85
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAgYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKK--ARPDLPIIVMSA 78
                         90       100
                 ....*....|....*....|..
gi 567929123  86 NNSHTDEAKGLELGAMDYITKP 107
Cdd:cd19928   79 QNTLMTAVKAAERGAFEYLPKP 100
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
6-71 4.44e-12

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: 61.65  E-value: 4.44e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 567929123   6 KILIVDDDPLNRLVLEKTL-GTEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKE 71
Cdd:cd17569    2 TILLVDDEPNILKALKRLLrREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRE 68
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
3-109 4.80e-12

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 66.05  E-value: 4.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   3 KKAKILIVDDDPLNRLVLEKTL---GTEHDVFlvESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKE-NPItqsI 78
Cdd:PRK10923   2 QRGIVWVVDDDSSIRWVLERALagaGLTCTTF--ENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQrHPM---L 76
                         90       100       110
                 ....*....|....*....|....*....|.
gi 567929123  79 PIVFISANNSHTDEAKGLELGAMDYITKPFN 109
Cdd:PRK10923  77 PVIIMTAHSDLDAAVSAYQQGAFDYLPKPFD 107
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
6-58 5.31e-12

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: 59.89  E-value: 5.31e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 567929123     6 KILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMP 58
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEgYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
7-118 6.69e-12

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 63.67  E-value: 6.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKEnpiTQSIPIVFISA 85
Cdd:PRK10529   4 VLIVEDEQAIRRFLRTALEGDgMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQ---WSAIPVIVLSA 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 567929123  86 NNSHTDEAKGLELGAMDYITKPFNASIVKVRVR 118
Cdd:PRK10529  81 RSEESDKIAALDAGADDYLSKPFGIGELQARLR 113
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
6-143 6.76e-12

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: 63.01  E-value: 6.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGT-EHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKE-NPitqSIPIVFI 83
Cdd:COG4567    6 SLLLVDDDEAFARVLARALERrGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRErDP---DARIVVL 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123  84 SANNSHTDEAKGLELGAMDYITKPFNAsivkvrvrnqllikqkNDLLEMLASIDGLTEIP 143
Cdd:COG4567   83 TGYASIATAVEAIKLGADDYLAKPADA----------------DDLLAALERAEGDAPAP 126
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
130-292 7.27e-12

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 65.95  E-value: 7.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 130 LEMLASIDGLTEIPNR----RYLDENLSREWRrskrngscLSVLLMDIDHFKRYNDCYGHRAGDECLKQVAQALAAQCeR 205
Cdd:PRK11359 372 IEQLIQFDPLTGLPNRnnlhNYLDDLVDKAVS--------PVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKL-K 442
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 206 STDFIARYGGEEFAAVLPDVNKQQALAFAQKLRKAVNslniehKASLNADH---ITISIGIaSMENGnaSAEQALLEQAD 282
Cdd:PRK11359 443 PDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVS------KPIMIDDKpfpLTLSIGI-SYDVG--KNRDYLLSTAH 513
                        170
                 ....*....|.
gi 567929123 283 LGL-YAAKDAG 292
Cdd:PRK11359 514 NAMdYIRKNGG 524
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
1-106 7.56e-12

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 63.51  E-value: 7.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   1 MSKKAKILIVDDDPLNRLVLEKTLGTEHDVFLV---ESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQS 77
Cdd:PRK10651   3 NQEPATILLIDDHPMLRTGVKQLISMAPDITVVgeaSNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGR 82
                         90       100
                 ....*....|....*....|....*....
gi 567929123  78 IpIVFiSANNSHTDEAKGLELGAMDYITK 106
Cdd:PRK10651  83 I-VVF-SVSNHEEDVVTALKRGADGYLLK 109
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
2-109 8.85e-12

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 65.05  E-value: 8.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   2 SKKAKILIVDDDPLNRLVLEKTL-GTEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKE-NPitqSIP 79
Cdd:PRK10365   3 HDNIDILVVDDDISHCTILQALLrGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAlNP---AIP 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 567929123  80 IVFISANNSHTDEAKGLELGAMDYITKPFN 109
Cdd:PRK10365  80 VLIMTAYSSVETAVEALKTGALDYLIKPLD 109
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
4-69 2.52e-11

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: 60.29  E-value: 2.52e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 567929123   4 KAKILIVDDDPLNRLVLEKTLGTEHD---VFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQL 69
Cdd:COG2197    1 MIRVLIVDDHPLVREGLRALLEAEPDievVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
6-107 2.89e-11

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 63.84  E-value: 2.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGT-EHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKEnpITQSIPIVFIS 84
Cdd:PRK10841 803 MILVVDDHPINRRLLADQLGSlGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQ--LGLTLPVIGVT 880
                         90       100
                 ....*....|....*....|....
gi 567929123  85 ANNSHTDEAKGLELGaMDY-ITKP 107
Cdd:PRK10841 881 ANALAEEKQRCLEAG-MDScLSKP 903
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
2-108 3.02e-11

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 63.25  E-value: 3.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   2 SKKAKILIVDDDPLNRLVLEKTLGTEHDVFLVES---GEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQL-KENPItqs 77
Cdd:PRK00742   1 MMKIRVLVVDDSAFMRRLISEILNSDPDIEVVGTapdGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKImRLRPT--- 77
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 567929123  78 iPIVFISA----NNSHTDEAkgLELGAMDYITKPF 108
Cdd:PRK00742  78 -PVVMVSSlterGAEITLRA--LELGAVDFVTKPF 109
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
6-84 3.22e-11

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: 59.05  E-value: 3.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQ-VDLIILDVVMPGIDGYEVLVQLKEnpITQSIPIVFI 83
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLKKAgYAVTEAESGAEALEKLQQGKdIDIVVTDIVMPEMDGIELAREARK--IDPDVKILFI 78

                 .
gi 567929123  84 S 84
Cdd:cd18160   79 S 79
PRK10610 PRK10610
chemotaxis protein CheY;
3-114 3.39e-11

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 59.60  E-value: 3.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   3 KKAKILIVDD-DPLNRLV--LEKTLGTeHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIP 79
Cdd:PRK10610   4 KELKFLVVDDfSTMRRIVrnLLKELGF-NNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALP 82
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 567929123  80 IVFISANNSHTDEAKGLELGAMDYITKPFNASIVK 114
Cdd:PRK10610  83 VLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLE 117
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
6-107 5.29e-11

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 63.33  E-value: 5.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNrLVLEKTLGTE--HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVFI 83
Cdd:PRK11107 669 TVMAVDDNPAN-LKLIGALLEEqvEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHNQNTPIIAV 747
                         90       100
                 ....*....|....*....|....
gi 567929123  84 SANNSHTDEAKGLELGAMDYITKP 107
Cdd:PRK11107 748 TAHAMAGERERLLSAGMDDYLAKP 771
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
1-157 5.67e-11

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 62.56  E-value: 5.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   1 MSKKAKILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKEnpITQSIP 79
Cdd:PRK11361   1 MTAINRILIVDDEDNVRRMLSTAFALQgFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRS--HETRTP 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567929123  80 IVFISANNSHTDEAKGLELGAMDYITKPFNASIVKvrvrnqLLIKQKNDLLEMLASIdglteipnrRYLDENLSREWR 157
Cdd:PRK11361  79 VILMTAYAEVETAVEALRCGAFDYVIKPFDLDELN------LIVQRALQLQSMKKEI---------RHLHQALSTSWQ 141
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
6-111 5.72e-11

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: 58.96  E-value: 5.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTEHDVFLVES--GEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQL-KENPitqsIPIVF 82
Cdd:cd19932    2 RVLIAEDEALIRMDLREMLEEAGYEVVGEAsdGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIItSENI----APIVL 77
                         90       100
                 ....*....|....*....|....*....
gi 567929123  83 ISANNSHTDEAKGLELGAMDYITKPFNAS 111
Cdd:cd19932   78 LTAYSQQDLVERAKEAGAMAYLVKPFSES 106
PRK10336 PRK10336
two-component system response regulator QseB;
6-127 8.42e-11

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 60.68  E-value: 8.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLN----RLVLEKtLGTEHDVFlvESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENpiTQSIPIV 81
Cdd:PRK10336   2 RILLIEDDMLIgdgiKTGLSK-MGFSVDWF--TQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREK--GQREPVL 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 567929123  82 FISANNSHTDEAKGLELGAMDYITKPFnaSIVKVRVRNQLLIKQKN 127
Cdd:PRK10336  77 ILTARDALAERVEGLRLGADDYLCKPF--ALIEVAARLEALMRRTN 120
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
4-108 9.19e-11

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: 58.00  E-value: 9.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   4 KAKILIVDDD-PLNRLvLEKTLGTEHDVFLV---ESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIP 79
Cdd:cd17561    1 KIKVLIADDNrEFVQL-LEEYLNSQPDMEVVgvaHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPK 79
                         90       100
                 ....*....|....*....|....*....
gi 567929123  80 IVFISANNSHTDEAKGLELGAMDYITKPF 108
Cdd:cd17561   80 IIMLTAFGQEDITQRAVELGASYYILKPF 108
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
6-111 1.82e-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: 57.07  E-value: 1.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKE-NPitqSIPIVFI 83
Cdd:cd17563    2 SLLLVDDDEVFAERLARALERRgFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRAlQP---DARIVVL 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 567929123  84 S--ANNSHTDEAkgLELGAMDYITKPFNAS 111
Cdd:cd17563   79 TgyASIATAVEA--IKLGADDYLAKPADAD 106
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
6-121 3.73e-10

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 58.88  E-value: 3.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGtEHDV-FLVES-GEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKenPITQSiPIVFI 83
Cdd:PRK10701   3 KIVFVEDDAEVGSLIAAYLA-KHDIdVTVEPrGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLR--PKWQG-PIVLL 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 567929123  84 SANNSHTDEAKGLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:PRK10701  79 TSLDSDMNHILALEMGACDYILKTTPPAVLLARLRLHL 116
fixJ PRK09390
response regulator FixJ; Provisional
2-108 4.38e-10

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 58.09  E-value: 4.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   2 SKKAKILIVDDDPLNRLVLEKTLGT-EHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITqsIPI 80
Cdd:PRK09390   1 SDKGVVHVVDDDEAMRDSLAFLLDSaGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSP--LPV 78
                         90       100       110
                 ....*....|....*....|....*....|.
gi 567929123  81 VFISAnnsHTDEAKGLE---LGAMDYITKPF 108
Cdd:PRK09390  79 IVMTG---HGDVPLAVEamkLGAVDFIEKPF 106
PRK10816 PRK10816
two-component system response regulator PhoP;
6-136 5.23e-10

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 58.21  E-value: 5.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTL-GTEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITqsIPIVFIS 84
Cdd:PRK10816   2 RVLVVEDNALLRHHLKVQLqDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVS--LPILVLT 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 567929123  85 ANNSHTDEAKGLELGAMDYITKPFNasIVKVRVRNQLLIKQKNDLLEMLASI 136
Cdd:PRK10816  80 ARESWQDKVEVLSAGADDYVTKPFH--IEEVMARMQALMRRNSGLASQVISL 129
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
7-119 6.36e-10

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: 56.22  E-value: 6.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKE---NPITqsipiVFI 83
Cdd:cd17596    3 ILVVDDEVRSLEALRRTLEEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRErwpEVVR-----III 77
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 567929123  84 SANNSHTDEAKGL-ELGAMDYITKPFNASIVKVRVRN 119
Cdd:cd17596   78 SGYTDSEDIIAGInEAGIYQYLTKPWHPDQLLLTVRN 114
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
6-118 1.08e-09

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: 55.15  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENpitQSIPIVFIS 84
Cdd:cd17594    1 HVLVVDDDAAMRHLLILYLRERgFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRAR---SDVPIIIIS 77
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 567929123  85 ANN-SHTDEAKGLELGAMDYITKPFNASIVKVRVR 118
Cdd:cd17594   78 GDRrDEIDRVVGLELGADDYLAKPFGLRELLARVR 112
PRK10693 PRK10693
two-component system response regulator RssB;
32-107 1.94e-09

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 57.31  E-value: 1.94e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 567929123  32 LVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITqsIPIVFISANNSHTDEAKGLELGAMDYITKP 107
Cdd:PRK10693   2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQ--TPVLVISATENMADIAKALRLGVQDVLLKP 75
PRK13856 PRK13856
two-component response regulator VirG; Provisional
7-124 8.76e-09

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 54.82  E-value: 8.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLgTEH--DVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKenpiTQS-IPIVFI 83
Cdd:PRK13856   4 VLVIDDDVAMRHLIVEYL-TIHafKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSLA----TKSdVPIIII 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 567929123  84 SANN-SHTDEAKGLELGAMDYITKPFNASIVKVRVRNQLLIK 124
Cdd:PRK13856  79 SGDRlEEADKVVALELGATDFIAKPFGTREFLARIRVALRVR 120
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
7-109 1.00e-08

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 56.10  E-value: 1.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLN----RLVLEKtLGTEHDVflVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKEN-PITQSIPIV 81
Cdd:PRK11091 528 ILLVEDIELNvivaRSVLEK-LGNSVDV--AMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERyPREDLPPLV 604
                         90       100
                 ....*....|....*....|....*...
gi 567929123  82 FISAnNSHTDEAKGLELGAMDYITKPFN 109
Cdd:PRK11091 605 ALTA-NVLKDKKEYLDAGMDDVLSKPLS 631
PRK14084 PRK14084
DNA-binding response regulator;
6-116 1.40e-08

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 54.37  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLgTEHDVFLV----ESGEKALTFIKSNQVDLIILDVVM---PGIDGYEVLVQLKENPItqsi 78
Cdd:PRK14084   2 KALIVDDEPLARNELTYLL-NEIGGFEEineaENVKETLEALLINQYDIIFLDINLmdeSGIELAAKIQKMKEPPA---- 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 567929123  79 pIVFISANNSHTdeAKGLELGAMDYITKPF-----NASIVKVR 116
Cdd:PRK14084  77 -IIFATAHDQFA--VKAFELNATDYILKPFeqkriEQAVNKVR 116
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
8-106 2.43e-08

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 53.36  E-value: 2.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   8 LIVDDDPLNRLVLEKTLGTEHDVFLVE--SGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVfiSA 85
Cdd:PRK09958   4 IIIDDHPLAIAAIRNLLIKNDIEILAEltEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIV--SA 81
                         90       100
                 ....*....|....*....|.
gi 567929123  86 NNSHTDEAKGLELGAMDYITK 106
Cdd:PRK09958  82 KNDHFYGKHCADAGANGFVSK 102
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
3-106 2.54e-08

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 53.34  E-value: 2.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   3 KKAKILIVDDDPLNRLVLEKTLGTEHDVFLV---ESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKEnpITQSIP 79
Cdd:PRK09935   2 KPASVIIMDTHPIIRMSIEVLLQKNSELQIVlktDDYRITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQ--IQSTVK 79
                         90       100
                 ....*....|....*....|....*..
gi 567929123  80 IVFISANNSHTDEAKGLELGAMDYITK 106
Cdd:PRK09935  80 VLFLSSKSECFYAGRAIQAGANGFVSK 106
PRK11059 PRK11059
regulatory protein CsrD; Provisional
134-288 6.30e-08

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 53.71  E-value: 6.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123 134 ASIDGLTEIPNRRYLD---ENLSREwrrSKRNGSCLSVLLMDIDHFKRYNDCYGHRAGDECLKQVAQALAAQCERSTDFI 210
Cdd:PRK11059 228 AFQDAKTGLGNRLFFDnqlATLLED---QEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRYPGAL 304
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 567929123 211 -ARYGGEEFAAVLPDVNKQQALAFAQKLRKAVNSLNIehKASLNADHItISIGIASMENGNaSAEQaLLEQADLGLYAA 288
Cdd:PRK11059 305 lARYSRSDFAVLLPHRSLKEADSLASQLLKAVDALPP--PKMLDRDDF-LHIGICAYRSGQ-STEQ-VMEEAEMALRSA 378
PRK15115 PRK15115
response regulator GlrR; Provisional
3-107 9.38e-08

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 52.92  E-value: 9.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   3 KKAKILIVDDDPLNRLVLEKTLGTE-HDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQL-KENPitqSIPI 80
Cdd:PRK15115   4 KPAHLLLVDDDPGLLKLLGMRLTSEgYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIqKVQP---GMPV 80
                         90       100
                 ....*....|....*....|....*..
gi 567929123  81 VFISANNSHTDEAKGLELGAMDYITKP 107
Cdd:PRK15115  81 IILTAHGSIPDAVAATQQGVFSFLTKP 107
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
5-106 1.96e-07

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


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 48.94  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   5 AKILIVDDDPLNRLVLEKTLGTEHDVFL--VESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVF 82
Cdd:cd17575    1 IMVLLVDDQAIIGEAVRRALADEEDIDFhyCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPIIV 80
                         90       100
                 ....*....|....*....|....
gi 567929123  83 ISANNSHTDEAKGLELGAMDYITK 106
Cdd:cd17575   81 LSTKEEPEVKSEAFALGANDYLVK 104
REC_LytTR_AgrA-like cd17533
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; ...
6-127 2.18e-07

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


Pssm-ID: 381088 [Multi-domain]  Cd Length: 131  Bit Score: 49.16  E-value: 2.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTL-------GTEHDVFLVESGEKALTFIK---SNQVDLIILDVVMPGIDGYEVLVQLKE-NPI 74
Cdd:cd17533    2 NIFILEDDKIQRVRLEEIIenilkieNIEYVIELTGKTEELLEKIKergKNGIYFLDIDIKMEEKNGLEVAQKIRKyDPY 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 567929123  75 TQsipIVFISannSHTDEA-KGLE--LGAMDYITKPFNASIVKVRVRNQLLIKQKN 127
Cdd:cd17533   82 AI---IIFVT---THSEFApLTFEykVAALDFILKPLKLEEFKKRIEECIKYAQKN 131
PRK11697 PRK11697
two-component system response regulator BtsR;
6-148 3.44e-07

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 50.23  E-value: 3.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTEHDVFLVesGE-----KALTFIKSNQVDLIILDVVMPGIDGYEVLVQLkeNPitQSIP- 79
Cdd:PRK11697   3 KVLIVDDEPLAREELRELLQEEGDIEIV--GEcsnaiEAIGAIHRLKPDVVFLDIQMPRISGLELVGML--DP--EHMPy 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123  80 IVFISANnshtDE--AKGLELGAMDYITKP-----FNASIVKVRvrnQLLIKQKNDLLEMLASidgLTEIP----NRRYL 148
Cdd:PRK11697  77 IVFVTAF----DEyaIKAFEEHAFDYLLKPidparLAKTLARLR---QERSPQDVLLPEAQPP---LKHIPctghNRIKL 146
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
7-117 3.46e-07

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: 47.81  E-value: 3.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDplnrLVLEKTLGTEHDVF-----LVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENpiTQSIPIV 81
Cdd:cd17573    1 ILLIEDD----STLGKEISKGLNEKgyqadVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEK--HPSIVVI 74
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 567929123  82 FISANNSHTDEAKGLELGAMDYITKPFNASIVKVRV 117
Cdd:cd17573   75 VLSDNPKTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
7-71 3.98e-07

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: 48.04  E-value: 3.98e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTEHDVFLVES---GEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKE 71
Cdd:cd19930    1 VLIAEDQEMVRGALAALLELEDDLEVVAQasnGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELRE 68
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
7-106 5.75e-07

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 47.34  E-value: 5.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTEHDVFLV---ESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVFI 83
Cdd:cd19931    1 VLLIDDHPLLRKGIKQLIELDPDFTVVgeaSSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILTV 80
                         90       100
                 ....*....|....*....|...
gi 567929123  84 SanNSHTDEAKGLELGAMDYITK 106
Cdd:cd19931   81 S--DAEDDVVTALRAGADGYLLK 101
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
7-108 1.33e-06

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: 46.19  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLgteHD----VFLVESGEKALTFIKSN-QVDLIILDVVMPG-IDGYEVLVQLKenPITQSIPI 80
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVL---EDlgytVLEAASGDEALDLLESGpDIDLLVTDVIMPGgMNGSQLAEEAR--RRRPDLKV 75
                         90       100       110
                 ....*....|....*....|....*....|
gi 567929123  81 VFIS--ANNShtdEAKGLELGAMDYITKPF 108
Cdd:cd18161   76 LLTSgyAENA---IEGGDLAPGVDVLSKPF 102
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
7-117 1.51e-06

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: 49.36  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123    7 ILIVDDDPLNRLVLEKTLgTEHDVFLVESGEKALTFIKSNQVDLIILDVVMP-----GIDGYEVLVQ-LKENPITQsipI 80
Cdd:TIGR02915   1 LLIVEDDLGLQKQLKWSF-ADYELAVAADRESAIALVRRHEPAVVTLDLGLPpdadgASEGLAALQQiLAIAPDTK---V 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 567929123   81 VFISANNSHTDEAKGLELGAMDYITKPFNASIVKVRV 117
Cdd:TIGR02915  77 IVITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIV 113
PRK09483 PRK09483
response regulator; Provisional
7-106 2.30e-06

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 47.41  E-value: 2.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTEHDVFLV---ESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQ-LKENPitqSIPIVF 82
Cdd:PRK09483   4 VLLVDDHELVRAGIRRILEDIKGIKVVgeaCCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKiLRYTP---DVKIIM 80
                         90       100
                 ....*....|....*....|....
gi 567929123  83 ISANNSHTDEAKGLELGAMDYITK 106
Cdd:PRK09483  81 LTVHTENPLPAKVMQAGAAGYLSK 104
PRK10430 PRK10430
two-component system response regulator DcuR;
7-111 2.54e-06

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 47.80  E-value: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDP----LNRLVLEKTLGTeHDVFLVESGEKALTFIKSNQ--VDLIILDVVMPGIDGYEVLVQLKEnpITQSIPI 80
Cdd:PRK10430   4 VLIVDDDAmvaeLNRRYVAQIPGF-QCCGTASTLEQAKEIIFNSDtpIDLILLDIYMQQENGLDLLPVLHE--AGCKSDV 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 567929123  81 VFISANNSHTDEAKGLELGAMDYITKPFNAS 111
Cdd:PRK10430  81 IVISSAADAATIKDSLHYGVVDYLIKPFQAS 111
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
7-107 2.85e-06

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: 44.96  E-value: 2.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDP-----LNRLVLEKTLGTEhdVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKenPITQSIPIV 81
Cdd:cd17565    1 FYIVDDDKniikiLSDIIEDDDLGEV--VGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLK--DTGSNGKFI 76
                         90       100
                 ....*....|....*....|....*.
gi 567929123  82 FISANNSHTDEAKGLELGAMDYITKP 107
Cdd:cd17565   77 MISQVSDKEMIGKAYQAGIEFFINKP 102
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
6-111 4.16e-06

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: 45.12  E-value: 4.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLG--TEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENpiTQSIPIVFI 83
Cdd:cd17530    2 RVLVLDDDPFQCMMAATILEdlGPGNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAES--HSNAAVILM 79
                         90       100       110
                 ....*....|....*....|....*....|...
gi 567929123  84 SANNS---HTDEAKGLELG--AMDYITKPFNAS 111
Cdd:cd17530   80 SGLDGgilESAETLAGANGlnLLGTLSKPFSPE 112
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
7-107 4.46e-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: 41.75  E-value: 4.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLG-TEHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEvLVQLKENPITQsIPIVFISA 85
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGrMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLE-LVQHIQQRLPQ-TPVAVITA 78
                         90       100
                 ....*....|....*....|..
gi 567929123  86 NNSHTDEAKGLELGAMDYITKP 107
Cdd:cd19926   79 YGSLDTAIEALKAGAFDFLTKP 100
PRK10360 PRK10360
transcriptional regulator UhpA;
6-106 6.93e-05

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 43.04  E-value: 6.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTEHDVFLVE---SGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKenpitQSIPIVF 82
Cdd:PRK10360   3 TVALIDDHLIVRSGFAQLLGLEPDLQVVAefgSGREALAGLPGRGVQVCICDISMPDISGLELLSQLP-----KGMATIM 77
                         90       100
                 ....*....|....*....|....
gi 567929123  83 ISANNSHTDEAKGLELGAMDYITK 106
Cdd:PRK10360  78 LSVHDSPALVEQALNAGARGFLSK 101
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
6-106 9.25e-05

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 42.92  E-value: 9.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPLNRLVLEKTLGTEHDVFLV---ESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKENPITQSIPIVF 82
Cdd:PRK10403   8 QVLIVDDHPLMRRGVRQLLELDPGFEVVaeaGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQIIILT 87
                         90       100
                 ....*....|....*....|....
gi 567929123  83 ISanNSHTDEAKGLELGAMDYITK 106
Cdd:PRK10403  88 VS--DASSDVFALIDAGADGYLLK 109
REC_PFxFATGY cd17586
phosphoacceptor receiver (REC) domain of PFxFATGY motif single-domain (stand-alone) response ...
7-121 3.20e-04

phosphoacceptor receiver (REC) domain of PFxFATGY motif single-domain (stand-alone) response regulators; This subfamily is composed of stand-alone response regulators (RRs) containing the PFxFATG[G/Y] motif; RRs with such a motif are also called ''FAT GUY'' response regulators. Included in this subfamily are Sphingomonas melonis SdrG, Sinorhizobium meliloti Sma0114, and Erythrobacter litoralis EL_LovR. SdrG is involved in the control of the general stress response. Sma0114 is part of the Sma0113/Sma0114 two-component system (TCS) that is involved in catabolite repression and polyhydroxy butyrate synthesis. EL_LovR is involved in a light-regulated TCS. PFxFATG[G/Y] RRs are typically associated with histidine-tryptophan-glutamate (HWE) histidine kinases that constitute a subclass of the larger histidine kinase superfamily characterized by an altered ATP binding site, which lacks the F-box that is normally an integral component of the ATP lid. The PFxFATG[G/Y] motif is involved in conformational changes after phosphorylation that results in the activation of the RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381122 [Multi-domain]  Cd Length: 111  Bit Score: 39.37  E-value: 3.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   7 ILIVDDDPLNRLVLEKTLGTEH--DVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKEnpitQSIPIVFIS 84
Cdd:cd17586    1 VLVLEDEPLIAMNLEDALEDLGgkEVVTAATCAEALRSLADGPIDIAILDVNLGGETSIPVADALKR----RAIPFIFAT 76
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 567929123  85 ANNSHTDEAkgLELGAMDYITKPFNASIVKVRVRNQL 121
Cdd:cd17586   77 GYGDSHGID--SRLIDVPVLRKPFDADSALAALAMLL 111
PRK15369 PRK15369
two component system response regulator;
6-106 5.49e-03

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 37.37  E-value: 5.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929123   6 KILIVDDDPL------NRLVLEKTLgteHDVFLVESGEKALTFIKSNQVDLIILDVVMPGIDGYEVLVQLKenpitQSIP 79
Cdd:PRK15369   5 KILLVDDHELiingikNMLAPYPRY---KIVGQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLH-----QRWP 76
                         90       100       110
                 ....*....|....*....|....*....|
gi 567929123  80 IVFISANNSHTDE---AKGLELGAMDYITK 106
Cdd:PRK15369  77 AMNILVLTARQEEhmaSRTLAAGALGYVLK 106
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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