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Conserved domains on  [gi|15598897|ref|NP_252391|]
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two-component response regulator [Pseudomonas aeruginosa PAO1]

Protein Classification

response regulator( domain architecture ID 11467115)

response regulator receives the signal from a sensor partner in two-component systems through its receiver (REC) domain

CATH:  3.40.50.2300
Gene Ontology:  GO:0000160|GO:0000156
PubMed:  20226724|31100988
SCOP:  4003632

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
19-146 3.76e-87

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: 258.11  E-value: 3.76e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  19 VMVLLVDDQAMIGEAVRRSLASEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIV 98
Cdd:cd17575   1 IMVLLVDDQAIIGEAVRRALADEEDIDFHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPIIV 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15598897  99 LSTKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRYHSRSYIALQQR 146
Cdd:cd17575  81 LSTKEEPEVKSEAFALGANDYLVKLPDKIELVARIRYHSRSYINLLQR 128
pleD super family cl35865
response regulator PleD; Reviewed
21-334 4.69e-71

response regulator PleD; Reviewed


The actual alignment was detected with superfamily member PRK09581:

Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 228.25  E-value: 4.69e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLASEAGIDFHfcSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLS 100
Cdd:PRK09581 158 ILLVDDDVSQAERIANILKEEFRVVVV--SDPSEALFNAAETNYDLVIVSANFENYDPLRLCSQLRSKERTRYVPILLLV 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRyhsrsyiaLQQRDEAYR-ALRESQQQLLEtnlvlqrLMNSDGLTGL 179
Cdd:PRK09581 236 DEDDDPRLVKALELGVNDYLMRPIDKNELLARVR--------TQIRRKRYQdALRNNLEQSIE-------MAVTDGLTGL 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  180 SNRRHFDEYLEMEWRRSLREQSQLSLLMIDVDYFKSYNDTFGHVAGDEALRQVAGAIREgCSRSSDLAARYGGEEFAMVL 259
Cdd:PRK09581 301 HNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRN-NIRGTDLIARYGGEEFVVVM 379
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598897  260 PGTSPGGARLLAEKVRRTVESLQISHDQPRPGSHLTVSIGVSTLvpGGGGQTFRVLIEMADQALYQAKNNGRNQV 334
Cdd:PRK09581 380 PDTDIEDAIAVAERIRRKIAEEPFIISDGKERLNVTVSIGVAEL--RPSGDTIEALIKRADKALYEAKNTGRNRV 452
 
Name Accession Description Interval E-value
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
19-146 3.76e-87

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: 258.11  E-value: 3.76e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  19 VMVLLVDDQAMIGEAVRRSLASEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIV 98
Cdd:cd17575   1 IMVLLVDDQAIIGEAVRRALADEEDIDFHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPIIV 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15598897  99 LSTKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRYHSRSYIALQQR 146
Cdd:cd17575  81 LSTKEEPEVKSEAFALGANDYLVKLPDKIELVARIRYHSRSYINLLQR 128
pleD PRK09581
response regulator PleD; Reviewed
21-334 4.69e-71

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 228.25  E-value: 4.69e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLASEAGIDFHfcSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLS 100
Cdd:PRK09581 158 ILLVDDDVSQAERIANILKEEFRVVVV--SDPSEALFNAAETNYDLVIVSANFENYDPLRLCSQLRSKERTRYVPILLLV 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRyhsrsyiaLQQRDEAYR-ALRESQQQLLEtnlvlqrLMNSDGLTGL 179
Cdd:PRK09581 236 DEDDDPRLVKALELGVNDYLMRPIDKNELLARVR--------TQIRRKRYQdALRNNLEQSIE-------MAVTDGLTGL 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  180 SNRRHFDEYLEMEWRRSLREQSQLSLLMIDVDYFKSYNDTFGHVAGDEALRQVAGAIREgCSRSSDLAARYGGEEFAMVL 259
Cdd:PRK09581 301 HNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRN-NIRGTDLIARYGGEEFVVVM 379
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598897  260 PGTSPGGARLLAEKVRRTVESLQISHDQPRPGSHLTVSIGVSTLvpGGGGQTFRVLIEMADQALYQAKNNGRNQV 334
Cdd:PRK09581 380 PDTDIEDAIAVAERIRRKIAEEPFIISDGKERLNVTVSIGVAEL--RPSGDTIEALIKRADKALYEAKNTGRNRV 452
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
174-334 1.56e-67

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: 209.34  E-value: 1.56e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897 174 DGLTGLSNRRHFDEYLEMEWRRSLREQSQLSLLMIDVDYFKSYNDTFGHVAGDEALRQVAGAIREgCSRSSDLAARYGGE 253
Cdd:cd01949   3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRS-SLRESDLVARLGGD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897 254 EFAMVLPGTSPGGARLLAEKVRRTVESLQISHDQPRpgsHLTVSIGVSTLVPggGGQTFRVLIEMADQALYQAKNNGRNQ 333
Cdd:cd01949  82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEI---RVTASIGIATYPE--DGEDAEELLRRADEALYRAKRSGRNR 156

                .
gi 15598897 334 V 334
Cdd:cd01949 157 V 157
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
172-333 3.93e-66

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: 205.56  E-value: 3.93e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   172 NSDGLTGLSNRRHFDEYLEMEWRRSLREQSQLSLLMIDVDYFKSYNDTFGHVAGDEALRQVAGAIREgCSRSSDLAARYG 251
Cdd:pfam00990   2 AHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSS-SLRRSDLVARLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   252 GEEFAMVLPGTSPGGARLLAEKVRRTVESLQISHDQPRPGSHLTVSIGVSTLVPggGGQTFRVLIEMADQALYQAKNNGR 331
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPN--DGEDPEDLLKRADTALYQAKQAGR 158

                  ..
gi 15598897   332 NQ 333
Cdd:pfam00990 159 NR 160
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
65-334 9.29e-66

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: 209.06  E-value: 9.29e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  65 TVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLSTKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRYHSRSYIALQ 144
Cdd:COG2199   2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897 145 QRDEAYRALR------ESQQQLLETNLVLQRLMNSDGLTGLSNRRHFDEYLEMEWRRSLREQSQLSLLMIDVDYFKSYND 218
Cdd:COG2199  82 ELLLLLLALLllllalEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIND 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897 219 TFGHVAGDEALRQVAGAIREGCsRSSDLAARYGGEEFAMVLPGTSPGGARLLAEKVRRTVESLQISHDQPRPgsHLTVSI 298
Cdd:COG2199 162 TYGHAAGDEVLKEVARRLRASL-RESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKEL--RVTVSI 238
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15598897 299 GVSTLVPggGGQTFRVLIEMADQALYQAKNNGRNQV 334
Cdd:COG2199 239 GVALYPE--DGDSAEELLRRADLALYRAKRAGRNRV 272
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
169-334 3.42e-58

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 185.53  E-value: 3.42e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897    169 RLMNSDGLTGLSNRRHFDEYLEMEWRRSLREQSQLSLLMIDVDYFKSYNDTFGHVAGDEALRQVAGAIREgCSRSSDLAA 248
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSS-CLRPGDLLA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897    249 RYGGEEFAMVLPGTSPGGARLLAEKVRRTVESLQISHDQPRpgsHLTVSIGVSTLVPggGGQTFRVLIEMADQALYQAKN 328
Cdd:smart00267  80 RLGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPL---YLTISIGVAAYPN--PGEDAEDLLKRADTALYQAKK 154

                   ....*.
gi 15598897    329 NGRNQV 334
Cdd:smart00267 155 AGRNQV 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
174-334 1.50e-57

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: 184.08  E-value: 1.50e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   174 DGLTGLSNRRHFDEYLEMEWRRSLREQSQLSLLMIDVDYFKSYNDTFGHVAGDEALRQVAGAIREGCsRSSDLAARYGGE 253
Cdd:TIGR00254   5 DPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSV-RGSDVVGRYGGE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   254 EFAMVLPGTSPGGARLLAEKVRRTVESLQISHdQPRPGSHLTVSIGVSTLVPggGGQTFRVLIEMADQALYQAKNNGRNQ 333
Cdd:TIGR00254  84 EFVVILPGTPLEDALSKAERLRDAINSKPIEV-AGSETLTVTVSIGVACYPG--HGLTLEELLKRADEALYQAKKAGRNR 160

                  .
gi 15598897   334 V 334
Cdd:TIGR00254 161 V 161
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
21-327 2.48e-42

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: 145.05  E-value: 2.48e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLS 100
Cdd:COG3706   4 ILVVDDDPTNRKLLRRLL-EAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIFLT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIryhsrsyialqqrdeayralresqqqlletnlvlqrlmnsdgltgls 180
Cdd:COG3706  83 ALDDEEDRARALEAGADDYLTKPFDPEELLARV----------------------------------------------- 115
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897 181 nrrhfdeylemewrrslreqsqlsllmidvdyfksyndtfghvagdealrqvagairegcsrssDLAARYGGEEFAMVLP 260
Cdd:COG3706 116 ----------------------------------------------------------------DLVARYGGEEFAILLP 131
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598897 261 GTSPGGARLLAEKVRRTVESLqishdqprPGSHLTVSIGVStlvpgggGQTfrvLIEMADqALYQAK 327
Cdd:COG3706 132 GTDLEGALAVAERIREAVAEL--------PSLRVTVSIGVA-------GDS---LLKRAD-ALYQAR 179
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
21-134 4.28e-20

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: 84.13  E-value: 4.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897    21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPAtrDIPIIVLS 100
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKE-GYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDP--TTPVIILT 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 15598897   101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:pfam00072  78 AHGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
21-147 5.03e-12

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 64.83  E-value: 5.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPAtrdIPIIVLS 100
Cdd:PRK10529   4 VLIVEDEQAIRRFLRTALEGD-GMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQWSA---IPVIVLS 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15598897  101 TKEEPTVKSAAFAAGANDYLVKlPDAI-ELVARIRYHSRSYIALQQRD 147
Cdd:PRK10529  80 ARSEESDKIAALDAGADDYLSK-PFGIgELQARLRVALRRHSATPAPD 126
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
21-74 4.23e-07

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 46.41  E-value: 4.23e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 15598897     21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMP 74
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKE-GYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
 
Name Accession Description Interval E-value
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
19-146 3.76e-87

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: 258.11  E-value: 3.76e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  19 VMVLLVDDQAMIGEAVRRSLASEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIV 98
Cdd:cd17575   1 IMVLLVDDQAIIGEAVRRALADEEDIDFHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPIIV 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15598897  99 LSTKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRYHSRSYIALQQR 146
Cdd:cd17575  81 LSTKEEPEVKSEAFALGANDYLVKLPDKIELVARIRYHSRSYINLLQR 128
pleD PRK09581
response regulator PleD; Reviewed
21-334 4.69e-71

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 228.25  E-value: 4.69e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLASEAGIDFHfcSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLS 100
Cdd:PRK09581 158 ILLVDDDVSQAERIANILKEEFRVVVV--SDPSEALFNAAETNYDLVIVSANFENYDPLRLCSQLRSKERTRYVPILLLV 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRyhsrsyiaLQQRDEAYR-ALRESQQQLLEtnlvlqrLMNSDGLTGL 179
Cdd:PRK09581 236 DEDDDPRLVKALELGVNDYLMRPIDKNELLARVR--------TQIRRKRYQdALRNNLEQSIE-------MAVTDGLTGL 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  180 SNRRHFDEYLEMEWRRSLREQSQLSLLMIDVDYFKSYNDTFGHVAGDEALRQVAGAIREgCSRSSDLAARYGGEEFAMVL 259
Cdd:PRK09581 301 HNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRN-NIRGTDLIARYGGEEFVVVM 379
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598897  260 PGTSPGGARLLAEKVRRTVESLQISHDQPRPGSHLTVSIGVSTLvpGGGGQTFRVLIEMADQALYQAKNNGRNQV 334
Cdd:PRK09581 380 PDTDIEDAIAVAERIRRKIAEEPFIISDGKERLNVTVSIGVAEL--RPSGDTIEALIKRADKALYEAKNTGRNRV 452
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
174-334 1.56e-67

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: 209.34  E-value: 1.56e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897 174 DGLTGLSNRRHFDEYLEMEWRRSLREQSQLSLLMIDVDYFKSYNDTFGHVAGDEALRQVAGAIREgCSRSSDLAARYGGE 253
Cdd:cd01949   3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRS-SLRESDLVARLGGD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897 254 EFAMVLPGTSPGGARLLAEKVRRTVESLQISHDQPRpgsHLTVSIGVSTLVPggGGQTFRVLIEMADQALYQAKNNGRNQ 333
Cdd:cd01949  82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEI---RVTASIGIATYPE--DGEDAEELLRRADEALYRAKRSGRNR 156

                .
gi 15598897 334 V 334
Cdd:cd01949 157 V 157
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
172-333 3.93e-66

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: 205.56  E-value: 3.93e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   172 NSDGLTGLSNRRHFDEYLEMEWRRSLREQSQLSLLMIDVDYFKSYNDTFGHVAGDEALRQVAGAIREgCSRSSDLAARYG 251
Cdd:pfam00990   2 AHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSS-SLRRSDLVARLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   252 GEEFAMVLPGTSPGGARLLAEKVRRTVESLQISHDQPRPGSHLTVSIGVSTLVPggGGQTFRVLIEMADQALYQAKNNGR 331
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPN--DGEDPEDLLKRADTALYQAKQAGR 158

                  ..
gi 15598897   332 NQ 333
Cdd:pfam00990 159 NR 160
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
65-334 9.29e-66

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: 209.06  E-value: 9.29e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  65 TVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLSTKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRYHSRSYIALQ 144
Cdd:COG2199   2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897 145 QRDEAYRALR------ESQQQLLETNLVLQRLMNSDGLTGLSNRRHFDEYLEMEWRRSLREQSQLSLLMIDVDYFKSYND 218
Cdd:COG2199  82 ELLLLLLALLllllalEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIND 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897 219 TFGHVAGDEALRQVAGAIREGCsRSSDLAARYGGEEFAMVLPGTSPGGARLLAEKVRRTVESLQISHDQPRPgsHLTVSI 298
Cdd:COG2199 162 TYGHAAGDEVLKEVARRLRASL-RESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKEL--RVTVSI 238
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15598897 299 GVSTLVPggGGQTFRVLIEMADQALYQAKNNGRNQV 334
Cdd:COG2199 239 GVALYPE--DGDSAEELLRRADLALYRAKRAGRNRV 272
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
169-334 3.42e-58

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 185.53  E-value: 3.42e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897    169 RLMNSDGLTGLSNRRHFDEYLEMEWRRSLREQSQLSLLMIDVDYFKSYNDTFGHVAGDEALRQVAGAIREgCSRSSDLAA 248
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSS-CLRPGDLLA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897    249 RYGGEEFAMVLPGTSPGGARLLAEKVRRTVESLQISHDQPRpgsHLTVSIGVSTLVPggGGQTFRVLIEMADQALYQAKN 328
Cdd:smart00267  80 RLGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPL---YLTISIGVAAYPN--PGEDAEDLLKRADTALYQAKK 154

                   ....*.
gi 15598897    329 NGRNQV 334
Cdd:smart00267 155 AGRNQV 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
174-334 1.50e-57

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: 184.08  E-value: 1.50e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   174 DGLTGLSNRRHFDEYLEMEWRRSLREQSQLSLLMIDVDYFKSYNDTFGHVAGDEALRQVAGAIREGCsRSSDLAARYGGE 253
Cdd:TIGR00254   5 DPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSV-RGSDVVGRYGGE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   254 EFAMVLPGTSPGGARLLAEKVRRTVESLQISHdQPRPGSHLTVSIGVSTLVPggGGQTFRVLIEMADQALYQAKNNGRNQ 333
Cdd:TIGR00254  84 EFVVILPGTPLEDALSKAERLRDAINSKPIEV-AGSETLTVTVSIGVACYPG--HGLTLEELLKRADEALYQAKKAGRNR 160

                  .
gi 15598897   334 V 334
Cdd:TIGR00254 161 V 161
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
10-334 7.48e-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: 165.72  E-value: 7.48e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  10 DLGAPLDGAVMVLLVDDQAMIGEAVRRSLASEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNP 89
Cdd:COG5001  97 LALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLL 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  90 ATRDIPIIVLSTKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRYHSRSYIALQQRDEAYRALRESQQQLletnlvlQR 169
Cdd:COG5001 177 LLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERL-------RH 249
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897 170 LMNSDGLTGLSNRRHFDEYLEMEWRRSLREQSQLSLLMIDVDYFKSYNDTFGHVAGDEALRQVAGAIREgCSRSSDLAAR 249
Cdd:COG5001 250 LAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRA-CLREGDTVAR 328
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897 250 YGGEEFAMVLPG-TSPGGARLLAEKVRRTV-ESLQISHDQPrpgsHLTVSIGVStLVPgGGGQTFRVLIEMADQALYQAK 327
Cdd:COG5001 329 LGGDEFAVLLPDlDDPEDAEAVAERILAALaEPFELDGHEL----YVSASIGIA-LYP-DDGADAEELLRNADLAMYRAK 402

                ....*..
gi 15598897 328 NNGRNQV 334
Cdd:COG5001 403 AAGRNRY 409
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
21-327 2.48e-42

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: 145.05  E-value: 2.48e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLS 100
Cdd:COG3706   4 ILVVDDDPTNRKLLRRLL-EAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIFLT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIryhsrsyialqqrdeayralresqqqlletnlvlqrlmnsdgltgls 180
Cdd:COG3706  83 ALDDEEDRARALEAGADDYLTKPFDPEELLARV----------------------------------------------- 115
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897 181 nrrhfdeylemewrrslreqsqlsllmidvdyfksyndtfghvagdealrqvagairegcsrssDLAARYGGEEFAMVLP 260
Cdd:COG3706 116 ----------------------------------------------------------------DLVARYGGEEFAILLP 131
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598897 261 GTSPGGARLLAEKVRRTVESLqishdqprPGSHLTVSIGVStlvpgggGQTfrvLIEMADqALYQAK 327
Cdd:COG3706 132 GTDLEGALAVAERIREAVAEL--------PSLRVTVSIGVA-------GDS---LLKRAD-ALYQAR 179
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
150-345 1.12e-41

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 152.86  E-value: 1.12e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  150 YRALRESQQQLLETnlvlqrlmnsDGLTGLSNRRHFDEYLEMEWRRSLREQSQLSLLMIDVDYFKSYNDTFGHVAGDEAL 229
Cdd:PRK15426 387 MFVLQSSLQWQAWH----------DPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVL 456
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  230 RQVAGAIREGCsRSSDLAARYGGEEFAMVLPGTSPGGARLLAEKVRRTVESLQISHDQPRPgSHLTVSIGVSTLVPGGGG 309
Cdd:PRK15426 457 SHAAGLISSSL-RAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTT-IRISASLGVSSAEEDGDY 534
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15598897  310 qTFRVLIEMADQALYQAKNNGRNQVGLMEQPVPPAP 345
Cdd:PRK15426 535 -DFEQLQSLADRRLYLAKQAGRNRVCASDNAHEREV 569
PRK09894 PRK09894
diguanylate cyclase; Provisional
126-337 2.63e-40

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 143.67  E-value: 2.63e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  126 AIELVARI---RYHSRSYIALQQRDEAYR-ALRESQQQLLETnlvlqrLMNSDGLTGLSNRRHFDEYLEMEwrRSLREQS 201
Cdd:PRK09894  86 ARELLLAIvegHWQDAHFDAFQEGLLSFTaALTDYKIYLLTI------RSNMDVLTGLPGRRVLDESFDHQ--LRNREPQ 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  202 QLSLLMIDVDYFKSYNDTFGHVAGDEALRQVAGAIREGcSRSSDLAARYGGEEFAMVLPGTSPGGARLLAEKVRRTVESL 281
Cdd:PRK09894 158 NLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASW-TRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANH 236
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15598897  282 QISHDQPRpgSHLTVSIGVSTLVPgggGQTFRVLIEMADQALYQAKNNGRNQVGLM 337
Cdd:PRK09894 237 AITHSDGR--INITATFGVSRAFP---EETLDVVIGRADRAMYEGKQTGRNRVMFI 287
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
202-329 1.16e-37

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: 131.32  E-value: 1.16e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897 202 QLSLLMIDVDYFKSYNDTFGHVAGDEALRQVAGAIREGCSRSSDLAARYGGEEFAMVLPGTSPGGARLLAEKVRRTVESL 281
Cdd:cd07556   1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15598897 282 QIShdqprPGSHLTVSIGVSTLVPGGGG-------QTFRVLIEMADQALYQAKNN 329
Cdd:cd07556  81 NQS-----EGNPVRVRIGIHTGPVVVGVigsrpqyDVWGALVNLASRMESQAKAG 130
adrA PRK10245
diguanylate cyclase AdrA; Provisional
159-333 5.73e-32

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 123.02  E-value: 5.73e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  159 QLLETNLVLQRLMNSDGLTGLSNRRHFDEYLEMEWRRSLREQSQLSLLMIDVDYFKSYNDTFGHVAGDEAL----RQVAG 234
Cdd:PRK10245 193 KLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIvaltRQLQI 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  235 AIregcsRSSDLAARYGGEEFAMVLPGTSPGGARLLAEKVRRTVESLQISHdqpRPGSHLTVSIGVSTLVPGGGgqTFRV 314
Cdd:PRK10245 273 TL-----RGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPN---APQVTLRISVGVAPLNPQMS--HYRE 342
                        170
                 ....*....|....*....
gi 15598897  315 LIEMADQALYQAKNNGRNQ 333
Cdd:PRK10245 343 WLKSADLALYKAKNAGRNR 361
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
21-134 3.96e-29

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: 108.68  E-value: 3.96e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLS 100
Cdd:cd17551   3 ILIVDDNPTNLLLLEALLRSAGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVMIT 82
                        90       100       110
                ....*....|....*....|....*....|....
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd17551  83 ADTDREVRLRALEAGATDFLTKPFDPVELLARVR 116
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
21-155 1.66e-28

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: 110.25  E-value: 1.66e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLS 100
Cdd:COG3437   9 VLIVDDDPENLELLRQLL-RTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPVIFLT 87
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRYHSRSYiALQQRDEAYRALRE 155
Cdd:COG3437  88 ALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELR-RLQRELDDLVLYLK 141
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
21-134 2.07e-26

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: 101.85  E-value: 2.07e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLS 100
Cdd:COG0784   8 ILVVDDNPDNRELLRRLL-ERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPIIALT 86
                        90       100       110
                ....*....|....*....|....*....|....
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:COG0784  87 AYADEEDRERALEAGADDYLTKPVDPEELLEALR 120
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
21-138 2.63e-26

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: 103.88  E-value: 2.63e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPatRDIPIIVLS 100
Cdd:COG0745   4 ILVVEDDPDIRELLADAL-EREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARP--SDIPIIMLT 80
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKlP-DAIELVARIRYHSR 138
Cdd:COG0745  81 ARDDEEDRVRGLEAGADDYLTK-PfDPEELLARIRALLR 118
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
22-122 2.55e-23

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 92.29  E-value: 2.55e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  22 LLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPatRDIPIIVLST 101
Cdd:cd00156   1 LIVDDDPAIRELLKSLLERE-GYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELP--PDIPVIVLTA 77
                        90       100
                ....*....|....*....|.
gi 15598897 102 KEEPTVKSAAFAAGANDYLVK 122
Cdd:cd00156  78 KADEEDAVRALELGADDYLVK 98
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
158-339 2.82e-22

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 98.21  E-value: 2.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   158 QQLLETNLVLQRLMNS---DGLTGLSNRRHFDEYLemewRRSLRE----QSQLSLLMIDVDYFKSYNDTFGHVAGDEALR 230
Cdd:PRK09776  649 QDVTESRKMLRQLSYSashDALTHLANRASFEKQL----RRLLQTvnstHQRHALVFIDLDRFKAVNDSAGHAAGDALLR 724
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   231 QVAGAIReGCSRSSDLAARYGGEEFAMVLPGTSPGGARLLAEKVRRTVESLQIS-----HDqprpgshLTVSIGVsTLVP 305
Cdd:PRK09776  725 ELASLML-SMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPwegrvYR-------VGASAGI-TLID 795
                         170       180       190
                  ....*....|....*....|....*....|....
gi 15598897   306 GGGGQTFRVLIEmADQALYQAKNNGRNQVGLMEQ 339
Cdd:PRK09776  796 ANNHQASEVMSQ-ADIACYAAKNAGRGRVTVYEP 828
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
21-132 1.86e-21

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: 87.95  E-value: 1.86e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEAGIDFHF-CSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGnpATRDIPIIVL 99
Cdd:cd17535   1 VLIVDDHPLVREGLRRLLESEPDIEVVGeAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRR--RYPDLKVIVL 78
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15598897 100 STKEEPTVKSAAFAAGANDYLVK------LPDAIELVAR 132
Cdd:cd17535  79 TAHDDPEYVLRALKAGAAGYLLKdsspeeLIEAIRAVAA 117
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
22-122 2.79e-21

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: 87.08  E-value: 2.79e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  22 LLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPatRDIPIIVLST 101
Cdd:cd17574   1 LVVEDDEEIAELLSDYL-EKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKG--SDIPIIMLTA 77
                        90       100
                ....*....|....*....|.
gi 15598897 102 KEEPTVKSAAFAAGANDYLVK 122
Cdd:cd17574  78 KDEEEDKVLGLELGADDYITK 98
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
21-133 7.65e-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: 86.70  E-value: 7.65e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLAsEAGI--DFHFCSDPQQAVA-------VANQIKPTVILQDLVMPGVDGLTLLAAYRGNPAT 91
Cdd:cd17557   2 ILLVEDNPGDAELIQEAFK-EAGVpnELHVVRDGEEALDflrgegeYADAPRPDLILLDLNMPRMDGFEVLREIKADPDL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15598897  92 RDIPIIVLSTKEEPTVKSAAFAAGANDYLVK---LPDAIELVARI 133
Cdd:cd17557  81 RRIPVVVLTTSDAEEDIERAYELGANSYIVKpvdFEEFVEAIRSL 125
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
21-134 4.28e-20

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: 84.13  E-value: 4.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897    21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPAtrDIPIIVLS 100
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKE-GYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDP--TTPVIILT 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 15598897   101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:pfam00072  78 AHGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
21-161 1.43e-19

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 83.48  E-value: 1.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEAGID-FHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGnpATRDIPIIVL 99
Cdd:COG4565   6 VLIVEDDPMVAELLRRYLERLPGFEvVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRA--RGPDVDVIVI 83
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598897 100 STKEEPTVKSAAFAAGANDYLVKlP-DAIELVARIRYHSRsyialqqrdeAYRALRESQQQLL 161
Cdd:COG4565  84 TAARDPETVREALRAGVVDYLIK-PfTFERLREALERYLE----------YRRLLREDQEEDL 135
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
21-163 2.31e-19

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: 88.48  E-value: 2.31e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPatRDIPIIVLS 100
Cdd:COG2204   5 ILVVDDDPDIRRLLKELL-ERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALD--PDLPVILLT 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRYHSRSYIALQQRDEAYRALRESQ--QQLLET 163
Cdd:COG2204  82 GYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSGLIGRSPamQEVRRL 146
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
21-134 3.04e-19

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: 81.96  E-value: 3.04e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLAsEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLS 100
Cdd:cd17562   3 ILAVDDSASIRQMVSFTLR-GAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILMLT 81
                        90       100       110
                ....*....|....*....|....*....|....
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd17562  82 TESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVK 115
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
21-122 3.21e-19

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: 81.36  E-value: 3.21e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEAGID-FHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPatRDIPIIVL 99
Cdd:COG4753   2 VLIVDDEPLIREGLKRILEWEAGFEvVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELD--PDTKIIIL 79
                        90       100
                ....*....|....*....|...
gi 15598897 100 STKEEPTVKSAAFAAGANDYLVK 122
Cdd:COG4753  80 SGYSDFEYAQEAIKLGADDYLLK 102
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
21-134 7.52e-19

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: 80.89  E-value: 7.52e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGnpATRDIPIIVLS 100
Cdd:cd17627   1 ILVVDDDRAVRESLRRSLRFE-GYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRA--AGNDLPILVLT 77
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKlPDAI-ELVARIR 134
Cdd:cd17627  78 ARDSVSDRVAGLDAGADDYLVK-PFALeELLARVR 111
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
154-333 2.48e-18

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 85.89  E-value: 2.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  154 RESQQQLLEtnlvlqrLMNSDGLTGLSNRRHFDEYLEMEWRRslREQSQLSLLMIDVDYFKSYNDTFGHVAGDEALRQVA 233
Cdd:PRK10060 227 RRAQERLRI-------LANTDSITGLPNRNAIQELIDHAINA--ADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVS 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  234 GAIReGCSRSSDLAARYGGEEFAMVLPGTSPGGARLLAEkvrRTVESLQishdQP-RPG---SHLTVSIGVStLVPgGGG 309
Cdd:PRK10060 298 LAIL-SCLEEDQTLARLGGDEFLVLASHTSQAALEAMAS---RILTRLR----LPfRIGlieVYTGCSIGIA-LAP-EHG 367
                        170       180
                 ....*....|....*....|....
gi 15598897  310 QTFRVLIEMADQALYQAKNNGRNQ 333
Cdd:PRK10060 368 DDSESLIRSADTAMYTAKEGGRGQ 391
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
21-134 5.13e-18

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: 78.83  E-value: 5.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLS 100
Cdd:cd17618   3 ILIVEDEPAIREMIAFNL-ERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIMLT 81
                        90       100       110
                ....*....|....*....|....*....|....
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd17618  82 ARGEEEDKVRGLEAGADDYITKPFSPRELVARIK 115
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
21-122 7.17e-18

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: 77.94  E-value: 7.17e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLS 100
Cdd:cd19920   1 ILIVDDVPDNLRLLSELL-RAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLT 79
                        90       100
                ....*....|....*....|..
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVK 122
Cdd:cd19920  80 ALTDTEDKVKGFELGAVDYITK 101
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
21-138 7.42e-18

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: 78.30  E-value: 7.42e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGnpATRDIPIIVLS 100
Cdd:cd17624   1 ILLVEDDALLGDGLKTGL-RKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRR--QGQSLPVLILT 77
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRYHSR 138
Cdd:cd17624  78 ARDGVDDRVAGLDAGADDYLVKPFALEELLARLRALLR 115
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
22-134 2.34e-17

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: 76.93  E-value: 2.34e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  22 LLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLST 101
Cdd:cd19937   1 LVVDDEEDIVELLKYNLEKE-GYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTA 79
                        90       100       110
                ....*....|....*....|....*....|...
gi 15598897 102 KEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd19937  80 KGEEFDKVLGLELGADDYITKPFSPRELLARVK 112
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
21-134 3.37e-17

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: 76.44  E-value: 3.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLS 100
Cdd:cd17552   4 ILVIDDEEDIREVVQACLEKLAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVILLT 83
                        90       100       110
                ....*....|....*....|....*....|....
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd17552  84 AKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIA 117
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
21-134 6.80e-17

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: 75.58  E-value: 6.80e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRgnpATRDIPIIVLS 100
Cdd:cd17626   3 ILVVDDDAALAEMIGIVLRGE-GFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIR---AESGVPIVMLT 78
                        90       100       110
                ....*....|....*....|....*....|....
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd17626  79 AKSDTVDVVLGLESGADDYVAKPFKPKELVARIR 112
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
124-332 7.95e-17

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 81.74  E-value: 7.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  124 PDA-IELVARIRYHSRSyIALQQRdeayralrESQQQLletnlvlQRLMNSDGLTGLSNRRHFDEYLEmewrRSLREQSQ 202
Cdd:PRK11359 344 TSAfIERVADISQHLAA-LALEQE--------KSRQHI-------EQLIQFDPLTGLPNRNNLHNYLD----DLVDKAVS 403
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  203 LSLLMIDVDYFKSYNDTFGHVAGDEALRQVAGAIREGCsRSSDLAARYGGEEFAMVLPGTSPGGARLLAEKVRRTVESLQ 282
Cdd:PRK11359 404 PVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKL-KPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPI 482
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15598897  283 ISHDQPRPgshLTVSIGVSTlvpgGGGQTFRVLIEMADQALYQAKNNGRN 332
Cdd:PRK11359 483 MIDDKPFP---LTLSIGISY----DVGKNRDYLLSTAHNAMDYIRKNGGN 525
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
21-132 1.54e-16

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: 74.62  E-value: 1.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASeAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPAtrDIPIIVLS 100
Cdd:cd19919   3 VWIVDDDSSIRWVLERALAG-AGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHP--DLPVIIMT 79
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVK---LPDAIELVAR 132
Cdd:cd19919  80 AHSDLDSAVSAYQGGAFEYLPKpfdIDEAVALVER 114
PRK09966 PRK09966
diguanylate cyclase DgcN;
153-328 9.42e-16

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 77.74  E-value: 9.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  153 LRESQQQLLETNLVLQRLMNSDGLTGLSNRRHFDEYL-EMEWRRSLREQSqlSLLMIDVDYFKSYNDTFGHVAGDEALRQ 231
Cdd:PRK09966 230 MEEWQLRLQAKNAQLLRTALHDPLTGLANRAAFRSGInTLMNNSDARKTS--ALLFLDGDNFKYINDTWGHATGDRVLIE 307
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  232 VAGAIRE-GCSRSSdlAARYGGEEFAMVLPGTSPggarllAEKVRRTVESLQISHDQP---RPG--SHLTVSIGVSTLVP 305
Cdd:PRK09966 308 IAKRLAEfGGLRHK--AYRLGGDEFAMVLYDVQS------ESEVQQICSALTQIFNLPfdlHNGhqTTMTLSIGYAMTIE 379
                        170       180
                 ....*....|....*....|...
gi 15598897  306 GGGGQTfrvLIEMADQALYQAKN 328
Cdd:PRK09966 380 HASAEK---LQELADHNMYQAKH 399
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
21-122 1.46e-15

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


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 71.37  E-value: 1.46e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLS 100
Cdd:cd17538   2 ILVVDDEPANRELLEALLSAE-GYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                        90       100
                ....*....|....*....|..
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVK 122
Cdd:cd17538  81 ALDDREDRIRGLEAGADDFLSK 102
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
21-122 2.29e-15

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: 71.35  E-value: 2.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASeAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPAT-RDIPIIVL 99
Cdd:cd17546   1 VLVVDDNPVNRKVLKKLLEK-LGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGgRRTPIIAL 79
                        90       100
                ....*....|....*....|...
gi 15598897 100 STKEEPTVKSAAFAAGANDYLVK 122
Cdd:cd17546  80 TANALEEDREKCLEAGMDDYLSK 102
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
21-134 3.92e-15

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: 70.88  E-value: 3.92e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEAGIDF-HFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRgnpATRDIPIIVL 99
Cdd:cd17541   3 VLIVDDSAVMRKLLSRILESDPDIEVvGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIM---AERPTPVVMV 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15598897 100 S--TKEEPTVKSAAFAAGANDYLVK---------LPDAIELVARIR 134
Cdd:cd17541  80 SslTEEGAEITLEALELGAVDFIAKpsggisldlEEIAEELIEKIK 125
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
21-134 5.14e-15

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: 70.41  E-value: 5.14e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPatrDIPIIVLS 100
Cdd:cd17623   1 ILLIDDDRELTELLTEYLEME-GFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTS---QVPVLMLT 76
                        90       100       110
                ....*....|....*....|....*....|....
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd17623  77 ARGDDIDRILGLELGADDYLPKPFNPRELVARIR 110
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
21-134 9.29e-15

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: 69.69  E-value: 9.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGnpATRDIPIIVLS 100
Cdd:cd17615   2 VLVVDDEPNITELLSMALRYE-GWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRA--DGPDVPVLFLT 78
                        90       100       110
                ....*....|....*....|....*....|....
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd17615  79 AKDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLR 112
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
21-138 9.43e-15

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: 69.76  E-value: 9.43e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRgnpATRDIPIIVLS 100
Cdd:cd17614   1 ILVVDDEKPISDILKFNLTKE-GYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVR---KTSNVPIIMLT 76
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRYHSR 138
Cdd:cd17614  77 AKDSEVDKVLGLELGADDYVTKPFSNRELLARVKANLR 114
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
22-134 2.46e-14

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: 68.40  E-value: 2.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  22 LLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNpaTRDIPIIVLST 101
Cdd:cd17625   1 LVVEDEKDLSEAITKHLKKE-GYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREE--GIETPVLLLTA 77
                        90       100       110
                ....*....|....*....|....*....|...
gi 15598897 102 KEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd17625  78 LDAVEDRVKGLDLGADDYLPKPFSLAELLARIR 110
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
21-122 3.31e-14

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: 67.57  E-value: 3.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNpatRDIPIIVLS 100
Cdd:cd17620   1 ILVIEDEPQIRRFLRTALEAH-GYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREW---SAVPVIVLS 76
                        90       100
                ....*....|....*....|..
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVK 122
Cdd:cd17620  77 ARDEESDKIAALDAGADDYLTK 98
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
20-134 9.26e-14

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: 66.79  E-value: 9.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  20 MVLLVDDQAMIGEAVRRSLASeAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVL 99
Cdd:cd17548   1 KILIVEDNPLNMKLARDLLES-AGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIAL 79
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15598897 100 S---TKEEptvKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd17548  80 TayaMKGD---REKILEAGCDGYISKPIDTREFLETVA 114
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
21-199 6.62e-13

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


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 66.52  E-value: 6.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLAsEAGID-FHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPAtrdIPIIVL 99
Cdd:COG3707   6 VLVVDDEPLRRADLREGLR-EAGYEvVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP---APVILL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897 100 STKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRyhsrsyIALQQRDEaYRALRESQQQL---LETNLVLQR----LMn 172
Cdd:COG3707  82 TAYSDPELIERALEAGVSAYLVKPLDPEDLLPALE------LALARFRE-LRALRRELAKLreaLEERKLIERakgiLM- 153
                       170       180       190
                ....*....|....*....|....*....|....*
gi 15598897 173 sdgltglsNRRHFDE-----YLE---MEWRRSLRE 199
Cdd:COG3707 154 --------ERRGLSEdeayrLLRkqaMDRRVKLAE 180
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
53-135 7.90e-13

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: 64.27  E-value: 7.90e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  53 QQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLSTKEEPTVKSAAFAAGANDYLVKLPDAIELVAR 132
Cdd:cd17598  32 REALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTTLSDPRDVIRGLECGADNFITKPYDEKYLLSR 111

                ...
gi 15598897 133 IRY 135
Cdd:cd17598 112 IKY 114
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
21-122 4.15e-12

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


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 62.01  E-value: 4.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAV-----------AVANQIKptVILQDLVMPGVDGLTLLAAYRGNP 89
Cdd:cd19924   1 ILVVDDSPTARKQLRDLL-KNLGFEIAEAVDGEEALnklenlakegnDLSKELD--LIITDIEMPKMDGYELTFELRDDP 77
                        90       100       110
                ....*....|....*....|....*....|...
gi 15598897  90 ATRDIPIIVLSTKEEPTVKSAAFAAGANDYLVK 122
Cdd:cd19924  78 RLANIPVILNSSLSGEFSRARGKKVGADAYLAK 110
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
21-147 5.03e-12

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 64.83  E-value: 5.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPAtrdIPIIVLS 100
Cdd:PRK10529   4 VLIVEDEQAIRRFLRTALEGD-GMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQWSA---IPVIVLS 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15598897  101 TKEEPTVKSAAFAAGANDYLVKlPDAI-ELVARIRYHSRSYIALQQRD 147
Cdd:PRK10529  80 ARSEESDKIAALDAGADDYLSK-PFGIgELQARLRVALRRHSATPAPD 126
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
21-133 6.92e-12

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: 61.32  E-value: 6.92e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLS 100
Cdd:cd17580   1 ILVVDDNEDAAEMLALLLELE-GAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALT 79
                        90       100       110
                ....*....|....*....|....*....|...
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARI 133
Cdd:cd17580  80 GYGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
21-134 1.15e-11

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: 61.18  E-value: 1.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEAGIDFHfcSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLS 100
Cdd:cd17539   1 VLLVDDRPSSAERIAAMLSSEHEVVVE--ADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQLPILAVA 78
                        90       100       110
                ....*....|....*....|....*....|....
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd17539  79 DPGDRGRLIRALEIGVNDYLVRPIDPNELLARVR 112
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
21-134 1.36e-11

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: 60.85  E-value: 1.36e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNpatRDIPIIVLS 100
Cdd:cd19939   2 ILIVEDELELARLTRDYL-IKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREH---SHVPILMLT 77
                        90       100       110
                ....*....|....*....|....*....|....
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd19939  78 ARTEEMDRVLGLEMGADDYLCKPFSPRELLARVR 111
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
21-122 1.39e-11

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: 60.47  E-value: 1.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLS 100
Cdd:cd19927   1 ILLVDDDPGIRLAVKDYL-EDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLT 79
                        90       100
                ....*....|....*....|..
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVK 122
Cdd:cd19927  80 AKGMTSDRIKGYNAGCDGYLSK 101
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
21-134 1.93e-11

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 60.47  E-value: 1.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLAsEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRgnpATRDIPIIVLS 100
Cdd:cd19938   2 ILIVEDEPKLAQLLIDYLR-AAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIR---RFSDVPIIMVT 77
                        90       100       110
                ....*....|....*....|....*....|....
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd19938  78 ARVEEIDRLLGLELGADDYICKPYSPREVVARVK 111
PRK11517 PRK11517
DNA-binding response regulator HprR;
21-146 2.81e-11

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 62.61  E-value: 2.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATrdiPIIVLS 100
Cdd:PRK11517   3 ILLIEDNQRTQEWVTQGL-SEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQT---PVICLT 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 15598897  101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRYHSRSYIALQQR 146
Cdd:PRK11517  79 ARDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQLRQHHALNST 124
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
21-156 4.82e-11

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: 59.81  E-value: 4.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPAtrDIPIIVLS 100
Cdd:cd17549   1 VLLVDDDADVREALQQTL-ELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDP--DLPVILIT 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVK--LPDA-IELVARiryhsrsyiALQQRDEAY--RALRES 156
Cdd:cd17549  78 GHGDVPMAVEAMRAGAYDFLEKpfDPERlLDVVRR---------ALEKRRLVLenRRLRQQ 129
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
21-134 7.41e-11

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: 58.83  E-value: 7.41e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASeAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNpaTRDIPIIVLS 100
Cdd:cd19934   1 LLLVEDDALLAAQLKEQLSD-AGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSE--GRATPVLILT 77
                        90       100       110
                ....*....|....*....|....*....|....
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd19934  78 ARDSWQDKVEGLDAGADDYLTKPFHIEELLARLR 111
orf27 CHL00148
Ycf27; Reviewed
21-134 7.98e-11

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 61.27  E-value: 7.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRgnpATRDIPIIVLS 100
Cdd:CHL00148   9 ILVVDDEAYIRKILETRL-SIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIR---KESDVPIIMLT 84
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15598897  101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:CHL00148  85 ALGDVSDRITGLELGADDYVVKPFSPKELEARIR 118
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
20-160 9.35e-11

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


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 60.50  E-value: 9.35e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  20 MVLLVDDQamigEAVRRSLA---SEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPatRDIPI 96
Cdd:COG4566   1 TVYIVDDD----EAVRDSLAfllESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARG--SPLPV 74
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598897  97 IVLStkEEPTVKSA--AFAAGANDYLVKLPDAIELVARIRyhsRSYIALQQRDEAYRALRESQQQL 160
Cdd:COG4566  75 IFLT--GHGDVPMAvrAMKAGAVDFLEKPFDDQALLDAVR---RALARDRARRAERARRAELRARL 135
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
21-183 9.41e-11

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 60.64  E-value: 9.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLASEAGIDF-HFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDipIIVL 99
Cdd:PRK10403   9 VLIVDDHPLMRRGVRQLLELDPGFEVvAEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQ--IIIL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  100 STKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRYHSRSYIALQQRDEAYRALRESQQQ-------LLETNL-VLQRLM 171
Cdd:PRK10403  87 TVSDASSDVFALIDAGADGYLLKDSDPEVLLEAIRAGAKGSKVFSERVNQYLREREMFGAeedpfsvLTERELdVLHELA 166
                        170
                 ....*....|..
gi 15598897  172 NsdgltGLSNRR 183
Cdd:PRK10403 167 Q-----GLSNKQ 173
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
13-184 1.16e-10

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 60.43  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   13 APLDGAVMVLLVDDQAMIGEAVRRSLASEAGIDF-HFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPAT 91
Cdd:PRK10651   1 MSNQEPATILLIDDHPMLRTGVKQLISMAPDITVvGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   92 RDIPIIVLSTKEEPTVksAAFAAGANDYLVKLPDAIELVAriryhsrsyiALQQRDEAYRALRESQQQLLETNLVLQRLM 171
Cdd:PRK10651  81 GRIVVFSVSNHEEDVV--TALKRGADGYLLKDMEPEDLLK----------ALQQAAAGEMVLSEALTPVLAASLRANRAT 148
                        170
                 ....*....|...
gi 15598897  172 NSDGLTGLSNRRH 184
Cdd:PRK10651 149 TERDVNQLTPRER 161
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
21-162 1.67e-10

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: 59.16  E-value: 1.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLAsEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRG-NPATRdipIIVL 99
Cdd:COG4567   7 LLLVDDDEAFARVLARALE-RRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRErDPDAR---IVVL 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598897 100 S-TKEEPTVkSAAFAAGANDYLVKLPDAIELVARI-RYHSRSYIALQQRDEAYRALRESQQQLLE 162
Cdd:COG4567  83 TgYASIATA-VEAIKLGADDYLAKPADADDLLAALeRAEGDAPAPPENPMSLDRLEWEHIQRVLA 146
Spo0A COG5801
Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell ...
21-134 2.14e-10

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: 60.58  E-value: 2.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEAgiDFHFC---SDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPII 97
Cdd:COG5801   7 VLIADDNREFCELLEEYLSSQP--DMEVVgvaYNGLEALELIEEKKPDVVILDIIMPHLDGLGVLEKLREMNLEKRPKVI 84
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15598897  98 VLSTKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:COG5801  85 MLTAFGQEDITQRAVELGADYYILKPFDLDVLAERIR 121
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
18-134 2.59e-10

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 59.73  E-value: 2.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   18 AVMVLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPII 97
Cdd:PRK10161   2 ARRILVVEDEAPIREMVCFVL-EQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVV 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15598897   98 VLSTKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:PRK10161  81 MLTARGEEEDRVRGLETGADDYITKPFSPKELVARIK 117
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
21-118 3.27e-10

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 60.66  E-value: 3.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLASEAGIDFHFC-SDPQQAVAVANQIKPTVILQDLVMPGVDGLTllaayrgnpATRDI----- 94
Cdd:PRK12555   3 IGIVNDSPLAVEALRRALARDPDHEVVWVaTDGAQAVERCAAQPPDVILMDLEMPRMDGVE---------ATRRImaerp 73
                         90       100
                 ....*....|....*....|....*..
gi 15598897   95 -PIIVLS--TKEEPTVKSAAFAAGAND 118
Cdd:PRK12555  74 cPILIVTslTERNASRVFEAMGAGALD 100
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
21-138 3.69e-10

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: 56.62  E-value: 3.69e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEagiDFHFCSDPQ--QAVAVANQIKPTVILQDLVMPGVDGLTLLaayRGNPATRDIPIIV 98
Cdd:cd17622   3 ILLVEDDPKLARLIADFLESH---GFNVVVEHRgdRALEVIAREKPDAVLLDIMLPGIDGLTLC---RDLRPKYQGPILL 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15598897  99 LSTKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRYHSR 138
Cdd:cd17622  77 LTALDSDIDHILGLELGADDYVVKPVEPAVLLARLRALLR 116
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
21-122 4.18e-10

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 56.22  E-value: 4.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLS 100
Cdd:cd17602   1 VACVDDRPSIQKMIEYFLEKQ-GFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLT 79
                        90       100
                ....*....|....*....|..
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVK 122
Cdd:cd17602  80 GKDGLVDRIRAKMAGASGYLTK 101
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
21-122 4.39e-10

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: 56.61  E-value: 4.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDD----QAMIGEAVRRS----LASEAG---IDFhFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNP 89
Cdd:cd17581   1 VLAVDDslvdRKVIERLLRISscrvTAVDSGkraLEF-LGLEDEEDSSNFNEPKVNMIITDYCMPGMTGYDLLKKVKESS 79
                        90       100       110
                ....*....|....*....|....*....|...
gi 15598897  90 ATRDIPIIVLSTKEEPTVKSAAFAAGANDYLVK 122
Cdd:cd17581  80 ALKEIPVVIMSSENIPTRISRCLEEGAEDFLLK 112
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
21-84 5.67e-10

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: 56.82  E-value: 5.67e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEAGIDF-HFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAA 84
Cdd:COG2197   4 VLIVDDHPLVREGLRALLEAEPDIEVvGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRR 68
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
21-134 8.96e-10

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: 55.81  E-value: 8.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEA-GIDF-HFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRG-NPatrDIPII 97
Cdd:cd17536   1 VLIVDDEPLIREGLKKLIDWEElGFEVvGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRElYP---DIKII 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15598897  98 VLS-------TKEeptvksaAFAAGANDYLVK---LPDAIELVARIR 134
Cdd:cd17536  78 ILSgyddfeyAQK-------AIRLGVVDYLLKpvdEEELEEALEKAK 117
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
21-136 9.52e-10

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


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 55.69  E-value: 9.52e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGnpATRDIPIIVLS 100
Cdd:cd17554   3 ILVVDDEENIRELYKEEL-EDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIRE--KKPDLPVIICT 79
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15598897 101 TKeePTVKSAAFAAGANDYLVKLPDAIELVARIRYH 136
Cdd:cd17554  80 AY--SEYKSDFSSWAADAYVVKSSDLTELKETIKRL 113
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
19-133 1.01e-09

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: 55.81  E-value: 1.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  19 VMVLLVDDQAMIGEAVRRSLaSEAGI-DFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPII 97
Cdd:cd19923   1 MKVLVVDDFSTMRRIIKNLL-KELGFnNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVL 79
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15598897  98 VLSTKEEPTVKSAAFAAGANDYLVKLPDAIELVARI 133
Cdd:cd19923  80 MVTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKL 115
PRK09483 PRK09483
response regulator; Provisional
21-142 1.38e-09

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 57.42  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLASEAGIDF-HFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTllaayrgnpATR------- 92
Cdd:PRK09483   4 VLLVDDHELVRAGIRRILEDIKGIKVvGEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLE---------ATRkilrytp 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15598897   93 DIPIIVLSTKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR--YHSRSYIA 142
Cdd:PRK09483  75 DVKIIMLTVHTENPLPAKVMQAGAAGYLSKGAAPQEVVSAIRsvHSGQRYIA 126
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
21-122 1.43e-09

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: 54.90  E-value: 1.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQamigEAVRRSLA---SEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGnpATRDIPII 97
Cdd:cd17555   3 ILVIDDD----EVVRESIAaylEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITK--ESPDTPVI 76
                        90       100
                ....*....|....*....|....*...
gi 15598897  98 VLSTKeepTVKSAAFAA---GANDYLVK 122
Cdd:cd17555  77 VVSGA---GVMSDAVEAlrlGAWDYLTK 101
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
21-122 1.56e-09

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: 54.37  E-value: 1.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGnpATRDIPIIVLS 100
Cdd:cd19935   1 ILVVEDEKKLAEYLKKGL-TEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRA--AGKQTPVLMLT 77
                        90       100
                ....*....|....*....|..
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVK 122
Cdd:cd19935  78 ARDSVEDRVKGLDLGADDYLVK 99
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
21-134 2.04e-09

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: 54.59  E-value: 2.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLaSEAGidFHF---CSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRG-NPATRdipI 96
Cdd:cd17542   3 VLIVDDAAFMRMMLKDIL-TKAG--YEVvgeAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKiDPNAK---V 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15598897  97 IVLST--KEEPTVKsaAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd17542  77 IMCSAmgQEEMVKE--AIKAGAKDFIVKPFQPERVLEAVE 114
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
21-134 3.20e-09

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: 54.28  E-value: 3.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEAGID-FHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVL 99
Cdd:cd19931   1 VLLIDDHPLLRKGIKQLIELDPDFTvVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILTV 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15598897 100 STKEEPTVksAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd19931  81 SDAEDDVV--TALRAGADGYLLKDMEPEDLLEALK 113
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
21-122 3.45e-09

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


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 54.06  E-value: 3.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLAS------EAgidfhfcSDPQQAVAVANQ---IKptVILQDLVMPGVDGLTLLAAYRGNPAT 91
Cdd:cd17544   3 VLVVDDSATSRNHLRALLRRhnfqvlEA-------ANGQEALEVLEQhpdIK--LVITDYNMPEMDGFELVREIRKKYSR 73
                        90       100       110
                ....*....|....*....|....*....|..
gi 15598897  92 RDIPIIVLSTKEEPTVkSAAF-AAGANDYLVK 122
Cdd:cd17544  74 DQLAIIGISASGDNAL-SARFiKAGANDFLTK 104
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
21-134 3.66e-09

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 56.62  E-value: 3.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLASeAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGnpaTRDIPIIVLS 100
Cdd:PRK10710  13 ILIVEDEPKLGQLLIDYLQA-ASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRR---FSDIPIVMVT 88
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15598897  101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:PRK10710  89 AKIEEIDRLLGLEIGADDYICKPYSPREVVARVK 122
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
21-131 4.97e-09

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: 53.69  E-value: 4.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPatRDIPIIVLS 100
Cdd:cd17593   3 VLICDDSSMARKQLARALPADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQ--LETKVIVVS 80
                        90       100       110
                ....*....|....*....|....*....|.
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVA 131
Cdd:cd17593  81 GDVQPEAKERVLELGALAFLKKPFDPEKLAQ 111
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
21-134 6.08e-09

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: 53.18  E-value: 6.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGnpATRDIPIIVLS 100
Cdd:cd17616   1 VLLIEDDSATAQSIELMLKSE-GFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRL--AKVKTPILILS 77
                        90       100       110
                ....*....|....*....|....*....|....
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd17616  78 GLADIEDKVKGLGFGADDYMTKPFHKDELVARIH 111
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
21-122 1.16e-08

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 54.82  E-value: 1.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEAGIDF-HFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPatRDIPIIVL 99
Cdd:COG3279   4 ILIVDDEPLARERLERLLEKYPDLEVvGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELD--PPPPIIFT 81
                        90       100
                ....*....|....*....|...
gi 15598897 100 STKEEPTVKsaAFAAGANDYLVK 122
Cdd:COG3279  82 TAYDEYALE--AFEVNAVDYLLK 102
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
21-129 1.47e-08

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 56.01  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQamigEAVRRSLA---SEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNpaTRDIPII 97
Cdd:PRK11361   7 ILIVDDE----DNVRRMLStafALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSH--ETRTPVI 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 15598897   98 VLSTKEEPTVKSAAFAAGANDYLVKLPDAIEL 129
Cdd:PRK11361  81 LMTAYAEVETAVEALRCGAFDYVIKPFDLDEL 112
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
21-154 1.78e-08

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 54.26  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNpatRDIPIIVLS 100
Cdd:PRK10701   4 IVFVEDDAEVGSLIAAYLAKH-DIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPK---WQGPIVLLT 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598897  101 TKEEPTVKSAAFAAGANDYLVKL-PDAIeLVARIRYHSRSYIALQQRDEA-------YRALR 154
Cdd:PRK10701  80 SLDSDMNHILALEMGACDYILKTtPPAV-LLARLRLHLRQNEQATQTKGLqetsltpYKALH 140
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
18-134 2.07e-08

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 55.16  E-value: 2.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   18 AVMVLLVDDQAMIGEAVRRSLASEAGIDF-HFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLaayrgnP---ATRD 93
Cdd:PRK00742   3 KIRVLVVDDSAFMRRLISEILNSDPDIEVvGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDAL------EkimRLRP 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15598897   94 IPIIVLS--TKEEPTVKSAAFAAGANDYLVK--------LPDAI-ELVARIR 134
Cdd:PRK00742  77 TPVVMVSslTERGAEITLRALELGAVDFVTKpflgislgMDEYKeELAEKVR 128
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
21-138 2.45e-08

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 55.26  E-value: 2.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLASeAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATrdIPIIVLS 100
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAG-AGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPM--LPVIIMT 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 15598897  101 TKEEPTVKSAAFAAGANDYLVK---LPDAIELVARIRYHSR 138
Cdd:PRK10923  83 AHSDLDAAVSAYQQGAFDYLPKpfdIDEAVALVERAISHYQ 123
ompR PRK09468
osmolarity response regulator; Provisional
21-134 3.04e-08

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 53.82  E-value: 3.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGnpATRDIPIIVLS 100
Cdd:PRK09468   8 ILVVDDDMRLRALLERYL-TEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRS--QNNPTPIIMLT 84
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15598897  101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:PRK09468  85 AKGEEVDRIVGLEIGADDYLPKPFNPRELLARIR 118
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
21-134 3.77e-08

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: 51.00  E-value: 3.77e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEAGIDF-HFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATrdiPIIVL 99
Cdd:cd17532   1 ALIVDDEPLAREELRYLLEEHPDIEIvGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKP---PLIVF 77
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15598897 100 STK-EEPTVKsaAFAAGANDYLVKLPDA---IELVARIR 134
Cdd:cd17532  78 VTAyDEYAVE--AFELNAVDYLLKPFSEerlAEALAKLR 114
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
19-122 5.06e-08

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: 50.88  E-value: 5.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  19 VMVLLVDDQAMIGEAVRRSLASEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRG-NPAtrdiPII 97
Cdd:cd19932   1 VRVLIAEDEALIRMDLREMLEEAGYEVVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSeNIA----PIV 76
                        90       100
                ....*....|....*....|....*
gi 15598897  98 VLSTKEEPTVKSAAFAAGANDYLVK 122
Cdd:cd19932  77 LLTAYSQQDLVERAKEAGAMAYLVK 101
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
21-83 5.07e-08

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: 50.86  E-value: 5.07e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLA 83
Cdd:cd17569   3 ILLVDDEPNILKALKRLLRRE-GYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLK 64
PRK10336 PRK10336
two-component system response regulator QseB;
21-166 5.11e-08

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 52.98  E-value: 5.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNpaTRDIPIIVLS 100
Cdd:PRK10336   3 ILLIEDDMLIGDGIKTGL-SKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREK--GQREPVLILT 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598897  101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRyhsrsyiALQQRD--EAYRALRESQQQLLETNLV 166
Cdd:PRK10336  80 ARDALAERVEGLRLGADDYLCKPFALIEVAARLE-------ALMRRTngQASNELRHGNVMLDPGKRI 140
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
50-122 8.00e-08

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 49.71  E-value: 8.00e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598897  50 SDPQQAVAVANQIKPTV--ILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLSTKEEPTVKSAAFAAGANDYLVK 122
Cdd:cd17582  29 SDGLQAWDVLEDEQNEIdlILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMMSSQDSVGVVFKCLSKGAADYLVK 103
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
21-134 9.99e-08

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 49.96  E-value: 9.99e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEAGID-FHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYR-GNPATRdipIIV 98
Cdd:cd19930   1 VLIAEDQEMVRGALAALLELEDDLEvVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELReELPDTK---VLI 77
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15598897  99 LSTKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd19930  78 VTTFGRPGYFRRALAAGVDGYVLKDRPIEELADAIR 113
PRK10643 PRK10643
two-component system response regulator PmrA;
21-147 1.13e-07

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 51.96  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLASEAgidfhFCSDPQQAVAVANQIKPT-----VILqDLVMPGVDGLTLLAAYRGNpaTRDIP 95
Cdd:PRK10643   3 ILIVEDDTLLLQGLILALQTEG-----YACDCASTAREAEALLESghyslVVL-DLGLPDEDGLHLLRRWRQK--KYTLP 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15598897   96 IIVLSTKEEPTVKSAAFAAGANDYLVKlPDAI-ELVARI-----RYHSRSYIALQQRD 147
Cdd:PRK10643  75 VLILTARDTLEDRVAGLDVGADDYLVK-PFALeELHARIralirRHQGQGENELQVGN 131
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
21-122 1.63e-07

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: 49.16  E-value: 1.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASeAGIDFHFCSDPQQAVAVANQIKPT--VILQDLVMPGVDGLTLLAAYRGNPatrDIPIIV 98
Cdd:cd17584   1 VLVVDDDPTCLAILKRMLLR-CGYQVTTCTDAEEALSMLRENKDEfdLVITDVHMPDMDGFEFLELIRLEM---DLPVIM 76
                        90       100
                ....*....|....*....|....
gi 15598897  99 LSTKEEPTVKSAAFAAGANDYLVK 122
Cdd:cd17584  77 MSADGSTSTVMKGLAHGACDYLLK 100
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
21-134 1.69e-07

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: 49.31  E-value: 1.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRgnpATRDIPIIVLS 100
Cdd:cd17619   3 ILIVEDEPVTRATLKSYFEQE-GYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELR---EQSEVGIILVT 78
                        90       100       110
                ....*....|....*....|....*....|....
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd17619  79 GRDDEVDRIVGLEIGADDYVTKPFNPRELLVRAK 112
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
21-122 1.75e-07

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 48.60  E-value: 1.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRgnpATRDIPIIVLS 100
Cdd:cd19936   1 IALVDDDRNILTSVSMALEAE-GFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLR---QKSTLPVIFLT 76
                        90       100
                ....*....|....*....|..
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVK 122
Cdd:cd19936  77 SKDDEIDEVFGLRMGADDYITK 98
PRK15347 PRK15347
two component system sensor kinase;
21-133 1.76e-07

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 53.11  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRD--IPIIV 98
Cdd:PRK15347 693 ILLVDDVETNRDIIGMML-VELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNLDpdCMIVA 771
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 15598897   99 LSTKEEPTVKSAAFAAGANDYLVK------LPDAIELVARI 133
Cdd:PRK15347 772 LTANAAPEEIHRCKKAGMNHYLTKpvtlaqLARALELAAEY 812
PRK10816 PRK10816
two-component system response regulator PhoP;
21-134 2.77e-07

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 50.51  E-value: 2.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATrdIPIIVLS 100
Cdd:PRK10816   3 VLVVEDNALLRHHLKVQL-QDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVS--LPILVLT 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15598897  101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:PRK10816  80 ARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQ 113
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
21-131 3.37e-07

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: 48.21  E-value: 3.37e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRG-NPATRdipIIVL 99
Cdd:cd17563   3 LLLVDDDEVFAERLARALERR-GFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRAlQPDAR---IVVL 78
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15598897 100 ------STkeepTVksAAFAAGANDYLVKLPDAIELVA 131
Cdd:cd17563  79 tgyasiAT----AV--EAIKLGADDYLAKPADADEILA 110
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
21-74 4.23e-07

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 46.41  E-value: 4.23e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 15598897     21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMP 74
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKE-GYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
21-134 4.81e-07

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: 47.83  E-value: 4.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRgnpATRDIPIIVLS 100
Cdd:cd17594   2 VLVVDDDAAMRHLLILYL-RERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIR---ARSDVPIIIIS 77
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15598897 101 T-KEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd17594  78 GdRRDEIDRVVGLELGADDYLAKPFGLRELLARVR 112
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
21-122 5.16e-07

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: 48.01  E-value: 5.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEAGidFHFC---SDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGnpATRDIPII 97
Cdd:cd19925   3 VLIVEDDPMVAEIHRAYVEQVPG--FTVIgtaGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRA--AGHDVDVI 78
                        90       100
                ....*....|....*....|....*
gi 15598897  98 VLSTKEEPTVKSAAFAAGANDYLVK 122
Cdd:cd19925  79 VVTAANDVETVREALRLGVVDYLIK 103
PRK10610 PRK10610
chemotaxis protein CheY;
16-122 1.17e-06

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 47.28  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   16 DGAVMVLLVDDQAMIGEAVRrSLASEAGidFHFCSDPQQAVAVANQIKPT---VILQDLVMPGVDGLTLLAAYRGNPATR 92
Cdd:PRK10610   3 DKELKFLVVDDFSTMRRIVR-NLLKELG--FNNVEEAEDGVDALNKLQAGgfgFVISDWNMPNMDGLELLKTIRADGAMS 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 15598897   93 DIPIIVLSTKEEPTVKSAAFAAGANDYLVK 122
Cdd:PRK10610  80 ALPVLMVTAEAKKENIIAAAQAGASGYVVK 109
PLN03029 PLN03029
type-a response regulator protein; Provisional
61-159 1.25e-06

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 48.88  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   61 QIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLSTKEEPTVKSAAFAAGANDYLVKlPDAIELVARIRYH---S 137
Cdd:PLN03029  70 EVEVNLIITDYCMPGMTGYDLLKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLK-PVQLSDLNRLKPHmmkT 148
                         90       100
                 ....*....|....*....|..
gi 15598897  138 RSYIALQQRDEAYRALRESQQQ 159
Cdd:PLN03029 149 KSKNQKQENQEKQEKLEESEIQ 170
PRK15369 PRK15369
two component system response regulator;
21-122 1.29e-06

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 48.54  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLASEAgiDFHFCSDPQQAVAVAN---QIKPTVILQDLVMPGVDGLTLLAAYRGN-PATRdipI 96
Cdd:PRK15369   6 ILLVDDHELIINGIKNMLAPYP--RYKIVGQVDNGLEVYNacrQLEPDIVILDLGLPGMNGLDVIPQLHQRwPAMN---I 80
                         90       100
                 ....*....|....*....|....*.
gi 15598897   97 IVLSTKEEPTVKSAAFAAGANDYLVK 122
Cdd:PRK15369  81 LVLTARQEEHMASRTLAAGALGYVLK 106
PRK10430 PRK10430
two-component system response regulator DcuR;
21-122 1.47e-06

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 48.57  E-value: 1.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLASEAGidFHFC---SDPQQAVAV--ANQIKPTVILQDLVMPGVDGLTLLAAYRGnpATRDIP 95
Cdd:PRK10430   4 VLIVDDDAMVAELNRRYVAQIPG--FQCCgtaSTLEQAKEIifNSDTPIDLILLDIYMQQENGLDLLPVLHE--AGCKSD 79
                         90       100
                 ....*....|....*....|....*..
gi 15598897   96 IIVLSTKEEPTVKSAAFAAGANDYLVK 122
Cdd:PRK10430  80 VIVISSAADAATIKDSLHYGVVDYLIK 106
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
21-146 2.25e-06

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 48.26  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQiKPTVILQDLVMPGVDGLTLLAAYRGNPATrdiPIIVLS 100
Cdd:PRK10955   4 ILLVDDDRELTSLLKELLEME-GFNVIVAHDGEQALDLLDD-SIDLLLLDVMMPKKNGIDTLKELRQTHQT---PVIMLT 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 15598897  101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR-YHSRSYIALQQR 146
Cdd:PRK10955  79 ARGSELDRVLGLELGADDYLPKPFNDRELVARIRaILRRSHWSEQQQ 125
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
21-100 2.90e-06

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: 45.57  E-value: 2.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQamigEAVRRSLA---SEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRG-NPatrDIPI 96
Cdd:cd17550   1 ILIVDDE----EDIRESLSgilEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEkYP---DLPV 73

                ....
gi 15598897  97 IVLS 100
Cdd:cd17550  74 IMIS 77
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
51-122 5.96e-06

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: 44.52  E-value: 5.96e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598897  51 DPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIVLSTKEEPTVKSAAFAAGANDYLVK 122
Cdd:cd17561  35 NGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPKIIMLTAFGQEDITQRAVELGASYYILK 106
PRK11697 PRK11697
two-component system response regulator BtsR;
21-134 6.55e-06

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 46.76  E-value: 6.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLASEAGIDF-HFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYrgNPATRdiPIIVL 99
Cdd:PRK11697   4 VLIVDDEPLAREELRELLQEEGDIEIvGECSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELVGML--DPEHM--PYIVF 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 15598897  100 STK-EEPTVKsaAFAAGANDYLVKLPDAIEL---VARIR 134
Cdd:PRK11697  80 VTAfDEYAIK--AFEEHAFDYLLKPIDPARLaktLARLR 116
PRK11059 PRK11059
regulatory protein CsrD; Provisional
174-326 1.49e-05

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 46.78  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  174 DGLTGLSNRRHFDEYLEmewrrSLREQSQL-----SLLMIDVDYFKSYNDTFGHVAGDEALRQVAGAIREGCSRSSD-LA 247
Cdd:PRK11059 231 DAKTGLGNRLFFDNQLA-----TLLEDQEMvgahgVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRYPGaLL 305
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598897  248 ARYGGEEFAMVLPGTSPGGARLLAEKVRRTVESLQISHDQPRPGshlTVSIGVSTLVpggGGQTFRVLIEMADQALYQA 326
Cdd:PRK11059 306 ARYSRSDFAVLLPHRSLKEADSLASQLLKAVDALPPPKMLDRDD---FLHIGICAYR---SGQSTEQVMEEAEMALRSA 378
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
21-122 1.78e-05

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: 42.96  E-value: 1.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRgnpATRDIPIIVLS 100
Cdd:cd17621   1 VLVVEDEESFSDPLAYLLRKE-GFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLR---ARSNVPVIMVT 76
                        90       100
                ....*....|....*....|..
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVK 122
Cdd:cd17621  77 AKDSEIDKVVGLELGADDYVTK 98
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
21-134 5.92e-05

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 43.76  E-value: 5.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGnpATRDIPIIVLS 100
Cdd:PRK09836   3 LLIVEDEKKTGEYLTKGL-TEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRS--ANKGMPILLLT 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15598897  101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:PRK09836  80 ALGTIEHRVKGLELGADDYLVKPFAFAELLARVR 113
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
66-133 6.53e-05

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: 41.65  E-value: 6.53e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598897  66 VILQDLVMPGVDGLTLLAAYRGNpaTRDIPIIVLSTKEEPTVKSAAFAAGANDYLVKLPDAIELVARI 133
Cdd:cd17573  45 LVLVSDKLPDGNGLSIVSRIKEK--HPSIVVIVLSDNPKTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
21-134 1.52e-04

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: 40.65  E-value: 1.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQamigEAVRRSLAS---EAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPAtrDIPII 97
Cdd:cd17537   3 VYVVDDD----EAVRDSLAFllrSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGS--NIPII 76
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15598897  98 VLSTKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd17537  77 FITGHGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIE 113
PRK15479 PRK15479
transcriptional regulator TctD;
21-134 1.71e-04

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 42.40  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNpaTRDIPIIVLS 100
Cdd:PRK15479   3 LLLAEDNRELAHWLEKAL-VQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKR--GQTLPVLLLT 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15598897  101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:PRK15479  80 ARSAVADRVKGLNVGADDYLPKPFELEELDARLR 113
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
21-122 2.28e-04

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


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 39.79  E-value: 2.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLaSEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAayRGNPATRDIPIIVLS 100
Cdd:cd19928   1 ILVADDDRAIRTVLTQAL-GRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIP--RIKKARPDLPIIVMS 77
                        90       100
                ....*....|....*....|..
gi 15598897 101 TKEEPTVKSAAFAAGANDYLVK 122
Cdd:cd19928  78 AQNTLMTAVKAAERGAFEYLPK 99
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
21-134 2.45e-04

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 41.87  E-value: 2.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPAtrDIPIIVLS 100
Cdd:PRK11083   6 ILLVEDEQAIADTLVYALQSE-GFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHP--ALPVIFLT 82
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15598897  101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:PRK11083  83 ARSDEVDRLVGLEIGADDYVAKPFSPREVAARVR 116
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
135-338 2.71e-04

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 42.62  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  135 YHSRSYIALQQRDEA---YRALRESQQQLLETNLVLQRLMNSDGLTGLSNRRHFDEYLEMEWRRSLREQSQlSLLMIDVD 211
Cdd:PRK11829 193 HHQLTLPAHHQDDELgvlVRNYNRNQQLLADAYADMGRISHRFPVTELPNRSLFISLLEKEIASSTRTDHF-HLLVIGIE 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  212 YFKSYNDTFGHVAGDEALRQVAGAIREGCSRSSdLAARYGGEEFAMVLPGTS-PGGARLLAEKVRRTV-ESLQISHDQPR 289
Cdd:PRK11829 272 TLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSD-LLAQLSKTEFAVLARGTRrSFPAMQLARRIMSQVtQPLFFDEITLR 350
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15598897  290 PgshlTVSIGVSTLVPGGggQTFRVLIEMADQALYQAKNNGRNQVGLME 338
Cdd:PRK11829 351 P----SASIGITRYQAQQ--DTAESMMRNASTAMMAAHHEGRNQIMVFE 393
PRK13856 PRK13856
two-component response regulator VirG; Provisional
21-151 3.25e-04

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 41.72  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIGEAVRRSLASEAgIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLaayRGNPATRDIPIIVLS 100
Cdd:PRK13856   4 VLVIDDDVAMRHLIVEYLTIHA-FKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIV---RSLATKSDVPIIIIS 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15598897  101 -TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRyhsrsyIALQQRDEAYR 151
Cdd:PRK13856  80 gDRLEEADKVVALELGATDFIAKPFGTREFLARIR------VALRVRPNVVR 125
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
49-122 3.37e-04

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 42.53  E-value: 3.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   49 CSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRDIPIIvlstkeepTVKSAAFA--------AGANDYL 120
Cdd:PRK11107 697 CDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHNQNTPII--------AVTAHAMAgererllsAGMDDYL 768

                 ..
gi 15598897  121 VK 122
Cdd:PRK11107 769 AK 770
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
21-149 3.58e-04

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


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 40.04  E-value: 3.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLasEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGN-PATrdIPIIVL 99
Cdd:cd17596   3 ILVVDDEVRSLEALRRTL--EEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERwPEV--VRIIIS 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15598897 100 STKEEPTVKSAAFAAGANDYLVK--LPDaiELVARIRYHSRSYiALQQRDEA 149
Cdd:cd17596  79 GYTDSEDIIAGINEAGIYQYLTKpwHPD--QLLLTVRNAARLF-ELQRENER 127
fixJ PRK09390
response regulator FixJ; Provisional
16-157 3.68e-04

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 41.14  E-value: 3.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   16 DGAVMVLLVDDQamigEAVRRSLA---SEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATr 92
Cdd:PRK09390   1 SDKGVVHVVDDD----EAMRDSLAfllDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSP- 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598897   93 dIPIIVLSTKEEPTVKSAAFAAGANDYLVKLPDAIELVARIRyhsrsyIALQQRDEAYRALRESQ 157
Cdd:PRK09390  76 -LPVIVMTGHGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIE------RALAQAPEAAKSEAVAA 133
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
21-134 3.93e-04

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: 39.49  E-value: 3.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEaGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPAtrDIPIIVLS 100
Cdd:cd17572   1 VLLVEDSPSLAALYQEYLSDE-GYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSL--PTSVIVIT 77
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15598897 101 TkeEPTVKSA--AFAAGANDYLVKLPDAIELVARIR 134
Cdd:cd17572  78 A--HGSVDIAveAMRLGAYDFLEKPFDADRLRVTVR 111
PRK10766 PRK10766
two-component system response regulator TorR;
21-134 1.16e-03

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 39.64  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   21 VLLVDDQAMIgEAVRRSLASEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRgnpATRDIPIIVLS 100
Cdd:PRK10766   5 ILVVEDEPVT-RARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELR---SRSTVGIILVT 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15598897  101 TKEEPTVKSAAFAAGANDYLVKLPDAIELVARIR 134
Cdd:PRK10766  81 GRTDSIDRIVGLEMGADDYVTKPLELRELLVRVK 114
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
50-122 1.49e-03

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: 37.64  E-value: 1.49e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598897  50 SDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRgnPATRDIPIIVLSTKEEPTVKSAAFAAGANDYLVK 122
Cdd:cd17565  31 DNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLK--DTGSNGKFIMISQVSDKEMIGKAYQAGIEFFINK 101
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
22-163 2.51e-03

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 38.72  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   22 LLVDDQAMIGEAVRRSLASEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLAAYRGNPATRdiPIIVLST 101
Cdd:PRK09958   4 IIIDDHPLAIAAIRNLLIKNDIEILAELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSG--IIIIVSA 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598897  102 KEEPTVKSAAFAAGANDYLVKLPDAIELVARIRYHSRSYIALQQRDEAYRALRESQQQLLET 163
Cdd:PRK09958  82 KNDHFYGKHCADAGANGFVSKKEGMNNIIAAIEAAKNGYCYFPFSLNRFVGSLTSDQQKLDS 143
PRK10693 PRK10693
two-component system response regulator RssB;
47-122 3.03e-03

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 38.82  E-value: 3.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598897   47 HFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLLA--AYRGNpatrDIPIIVLSTKEEPTVKSAAFAAGANDYLVK 122
Cdd:PRK10693   1 VLAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEhlRNRGD----QTPVLVISATENMADIAKALRLGVQDVLLK 74
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
21-117 4.68e-03

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: 36.65  E-value: 4.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897  21 VLLVDDQAMIGEAVRRSLASEAGIDFHFCSDPQQAVAVANQIKPTVILQDLVMPGVDGLTLL--AAYRGNPATrdipIIV 98
Cdd:cd17530   3 VLVLDDDPFQCMMAATILEDLGPGNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLrhLAESHSNAA----VIL 78
                        90
                ....*....|....*....
gi 15598897  99 LSTKEEPTVKSAAFAAGAN 117
Cdd:cd17530  79 MSGLDGGILESAETLAGAN 97
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
66-125 4.72e-03

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 37.93  E-value: 4.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598897   66 VILQDLVMPGVDGLTLLAayRGNPATRDIPIIVLSTKEEPTVKSAAFAAGANDYLVKLPD 125
Cdd:PRK09935  52 LIIMDIDLPGTDGFTFLK--RIKQIQSTVKVLFLSSKSECFYAGRAIQAGANGFVSKCND 109
 
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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