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Conserved domains on  [gi|2017541161|emb|CAG0948284|]
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Response regulator PleD [Geobacteraceae bacterium]

Protein Classification

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

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

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
pleD super family cl35865
response regulator PleD; Reviewed
4-301 3.32e-83

response regulator PleD; Reviewed


The actual alignment was detected with superfamily member PRK09581:

Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 258.68  E-value: 3.32e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDsDTLRGE-IFRTLQEVSLFDSYLEARDGLegFKTLLNNrVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPVI 82
Cdd:PRK09581  157 RILLVDD-DVSQAErIANILKEEFRVVVVSDPSEAL--FNAAETN-YDLVIVSANFENYDPLRLCSQLRSKERTRYVPIL 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  83 ILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLKMKSLQDELKRSNEMLRTLSITDPLTHLHNRR----HLME 158
Cdd:PRK09581  233 LLVDEDDDPRLVKALELGVNDYLMRPIDKNELLARVRTQIRRKRYQDALRNNLEQSIEMAVTDGLTGLHNRRyfdmHLKN 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 159 MVERefqrASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIVTRRLRSYDLAARYGGEEFVLLLPETPIHEAL 238
Cdd:PRK09581  313 LIER----ANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAI 388
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017541161 239 SIAERLRLEVQEHVFDGSLQGLVL--TISLGVATYPSSrVESIDSLFRQADEALYRAKQGGRNRV 301
Cdd:PRK09581  389 AVAERIRRKIAEEPFIISDGKERLnvTVSIGVAELRPS-GDTIEALIKRADKALYEAKNTGRNRV 452
 
Name Accession Description Interval E-value
pleD PRK09581
response regulator PleD; Reviewed
4-301 3.32e-83

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 258.68  E-value: 3.32e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDsDTLRGE-IFRTLQEVSLFDSYLEARDGLegFKTLLNNrVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPVI 82
Cdd:PRK09581  157 RILLVDD-DVSQAErIANILKEEFRVVVVSDPSEAL--FNAAETN-YDLVIVSANFENYDPLRLCSQLRSKERTRYVPIL 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  83 ILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLKMKSLQDELKRSNEMLRTLSITDPLTHLHNRR----HLME 158
Cdd:PRK09581  233 LLVDEDDDPRLVKALELGVNDYLMRPIDKNELLARVRTQIRRKRYQDALRNNLEQSIEMAVTDGLTGLHNRRyfdmHLKN 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 159 MVERefqrASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIVTRRLRSYDLAARYGGEEFVLLLPETPIHEAL 238
Cdd:PRK09581  313 LIER----ANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAI 388
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017541161 239 SIAERLRLEVQEHVFDGSLQGLVL--TISLGVATYPSSrVESIDSLFRQADEALYRAKQGGRNRV 301
Cdd:PRK09581  389 AVAERIRRKIAEEPFIISDGKERLnvTVSIGVAELRPS-GDTIEALIKRADKALYEAKNTGRNRV 452
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
44-303 2.39e-69

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: 217.15  E-value: 2.39e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  44 LLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLK 123
Cdd:COG2199    16 LLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 124 MKSLQDELKRSNEMLRTLSITDPLTHLHNRRHLMEMVEREFQRASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTIL 203
Cdd:COG2199    96 ALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEV 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 204 AEIVTRRLRSYDLAARYGGEEFVLLLPETPIHEALSIAERLRLEVQEHVFDGSLQGLVLTISLGVATYPSSRvESIDSLF 283
Cdd:COG2199   176 ARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVALYPEDG-DSAEELL 254
                         250       260
                  ....*....|....*....|
gi 2017541161 284 RQADEALYRAKQGGRNRVEL 303
Cdd:COG2199   255 RRADLALYRAKRAGRNRVVV 274
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
144-301 2.01e-68

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: 210.49  E-value: 2.01e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 144 TDPLTHLHNRRHLMEMVEREFQRASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIVTRRLRSYDLAARYGGE 223
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017541161 224 EFVLLLPETPIHEALSIAERLRLEVQEHVFDGSlQGLVLTISLGVATYPSSrVESIDSLFRQADEALYRAKQGGRNRV 301
Cdd:cd01949    82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDG-QEIRVTASIGIATYPED-GEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
142-300 7.48e-62

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: 194.01  E-value: 7.48e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 142 SITDPLTHLHNRRHLMEMVEREFQRASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIVTRRLRSYDLAARYG 221
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 222 GEEFVLLLPETPIHEALSIAERLRLEVQEH--VFDGSLQGLVLTISLGVATYPSSRvESIDSLFRQADEALYRAKQGGRN 299
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLkiPHTVSGLPLYVTISIGIAAYPNDG-EDPEDLLKRADTALYQAKQAGRN 159

                  .
gi 2017541161 300 R 300
Cdd:pfam00990 160 R 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
141-303 1.38e-59

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: 188.31  E-value: 1.38e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 141 LSITDPLTHLHNRRHLMEMVEREFQRASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIVTRRLRSYDLAARY 220
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 221 GGEEFVLLLPETPIHEALSIAERLRLEVQEHVFDGSLQGLV-LTISLGVATYPSSrVESIDSLFRQADEALYRAKQGGRN 299
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLtVTVSIGVACYPGH-GLTLEELLKRADEALYQAKKAGRN 159

                  ....
gi 2017541161 300 RVEL 303
Cdd:TIGR00254 160 RVVV 163
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
141-303 1.39e-59

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 188.23  E-value: 1.39e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  141 LSITDPLTHLHNRRHLMEMVEREFQRASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIVTRRLRSYDLAARY 220
Cdd:smart00267   2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  221 GGEEFVLLLPETPIHEALSIAERLRLEVQEHVFDGSLQgLVLTISLGVATYPSSrVESIDSLFRQADEALYRAKQGGRNR 300
Cdd:smart00267  82 GGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIP-LYLTISIGVAAYPNP-GEDAEDLLKRADTALYQAKKAGRNQ 159

                   ...
gi 2017541161  301 VEL 303
Cdd:smart00267 160 VAV 162
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
128-301 1.27e-52

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 173.63  E-value: 1.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 128 QDELKRSNEMLRTLSITDPLTHLHNRRHLMEMVEREFQRASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIV 207
Cdd:NF038266   80 QRMMRDLNEALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 208 TRRLRSYDLAARYGGEEFVLLLPETPIHEALSIAERLRLEVQEHVFDGSLQGLVLTISLGVATYPSSRvESIDSLFRQAD 287
Cdd:NF038266  160 RAELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEHRPPE-EGLSATLSRAD 238
                         170
                  ....*....|....
gi 2017541161 288 EALYRAKQGGRNRV 301
Cdd:NF038266  239 QALYQAKRAGRDRV 252
dguan_cyc_DgcA NF041606
diguanylate cyclase DgcA;
134-303 1.82e-47

diguanylate cyclase DgcA;


Pssm-ID: 469490 [Multi-domain]  Cd Length: 340  Bit Score: 162.61  E-value: 1.82e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 134 SNEMLRTLSITDPLTHLHNRRHLMEMVEREFQRASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIVTRRLRS 213
Cdd:NF041606  170 NNALLLEMTTTDMMTHLKLKHYFYTVLMEKLDTINSQGEPLSILMLDIDFFKQINDTYGHACGDLVLQMVASIIQSCTRT 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 214 YDLAARYGGEEFVLLLPETPIHEALSIAERLRLEVQEHVFDGSLQGLVLTISLGVATYpSSRVESIDSLFRQADEALYRA 293
Cdd:NF041606  250 QDMAARYGGEEFVVMLSNTSSKTAKKIAERIRKSIENLSILYDEQHIRVTISIGVAEY-NFDVESAKSLVERADKALYES 328
                         170
                  ....*....|
gi 2017541161 294 KQGGRNRVEL 303
Cdd:NF041606  329 KQNGRNRVSI 338
resp_reg_YycF NF040534
response regulator YycF;
34-165 7.53e-17

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 78.22  E-value: 7.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  34 ARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAReefQDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGE 113
Cdd:NF040534   30 AYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVRKK---YDMPIIMLTAKDSEIDKVLGLELGADDYVTKPFSTRE 106
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2017541161 114 LVARVRVQL---KMKSLQDELKRSNEM-LRTLSITDPLTHLHNRRHLMEMVEREFQ 165
Cdd:NF040534  107 LIARVKANLrrhQQQNTEEEEEENNEIvIGSLTIHPDAYTVKKRGETIELTHREFE 162
 
Name Accession Description Interval E-value
pleD PRK09581
response regulator PleD; Reviewed
4-301 3.32e-83

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 258.68  E-value: 3.32e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDsDTLRGE-IFRTLQEVSLFDSYLEARDGLegFKTLLNNrVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPVI 82
Cdd:PRK09581  157 RILLVDD-DVSQAErIANILKEEFRVVVVSDPSEAL--FNAAETN-YDLVIVSANFENYDPLRLCSQLRSKERTRYVPIL 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  83 ILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLKMKSLQDELKRSNEMLRTLSITDPLTHLHNRR----HLME 158
Cdd:PRK09581  233 LLVDEDDDPRLVKALELGVNDYLMRPIDKNELLARVRTQIRRKRYQDALRNNLEQSIEMAVTDGLTGLHNRRyfdmHLKN 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 159 MVERefqrASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIVTRRLRSYDLAARYGGEEFVLLLPETPIHEAL 238
Cdd:PRK09581  313 LIER----ANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAI 388
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017541161 239 SIAERLRLEVQEHVFDGSLQGLVL--TISLGVATYPSSrVESIDSLFRQADEALYRAKQGGRNRV 301
Cdd:PRK09581  389 AVAERIRRKIAEEPFIISDGKERLnvTVSIGVAELRPS-GDTIEALIKRADKALYEAKNTGRNRV 452
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
44-303 2.39e-69

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: 217.15  E-value: 2.39e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  44 LLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLK 123
Cdd:COG2199    16 LLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 124 MKSLQDELKRSNEMLRTLSITDPLTHLHNRRHLMEMVEREFQRASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTIL 203
Cdd:COG2199    96 ALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEV 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 204 AEIVTRRLRSYDLAARYGGEEFVLLLPETPIHEALSIAERLRLEVQEHVFDGSLQGLVLTISLGVATYPSSRvESIDSLF 283
Cdd:COG2199   176 ARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVALYPEDG-DSAEELL 254
                         250       260
                  ....*....|....*....|
gi 2017541161 284 RQADEALYRAKQGGRNRVEL 303
Cdd:COG2199   255 RRADLALYRAKRAGRNRVVV 274
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
144-301 2.01e-68

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: 210.49  E-value: 2.01e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 144 TDPLTHLHNRRHLMEMVEREFQRASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIVTRRLRSYDLAARYGGE 223
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017541161 224 EFVLLLPETPIHEALSIAERLRLEVQEHVFDGSlQGLVLTISLGVATYPSSrVESIDSLFRQADEALYRAKQGGRNRV 301
Cdd:cd01949    82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDG-QEIRVTASIGIATYPED-GEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
142-300 7.48e-62

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: 194.01  E-value: 7.48e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 142 SITDPLTHLHNRRHLMEMVEREFQRASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIVTRRLRSYDLAARYG 221
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 222 GEEFVLLLPETPIHEALSIAERLRLEVQEH--VFDGSLQGLVLTISLGVATYPSSRvESIDSLFRQADEALYRAKQGGRN 299
Cdd:pfam00990  81 GDEFAILLPETSLEGAQELAERIRRLLAKLkiPHTVSGLPLYVTISIGIAAYPNDG-EDPEDLLKRADTALYQAKQAGRN 159

                  .
gi 2017541161 300 R 300
Cdd:pfam00990 160 R 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
141-303 1.38e-59

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: 188.31  E-value: 1.38e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 141 LSITDPLTHLHNRRHLMEMVEREFQRASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIVTRRLRSYDLAARY 220
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 221 GGEEFVLLLPETPIHEALSIAERLRLEVQEHVFDGSLQGLV-LTISLGVATYPSSrVESIDSLFRQADEALYRAKQGGRN 299
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLtVTVSIGVACYPGH-GLTLEELLKRADEALYQAKKAGRN 159

                  ....
gi 2017541161 300 RVEL 303
Cdd:TIGR00254 160 RVVV 163
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
141-303 1.39e-59

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 188.23  E-value: 1.39e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  141 LSITDPLTHLHNRRHLMEMVEREFQRASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIVTRRLRSYDLAARY 220
Cdd:smart00267   2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  221 GGEEFVLLLPETPIHEALSIAERLRLEVQEHVFDGSLQgLVLTISLGVATYPSSrVESIDSLFRQADEALYRAKQGGRNR 300
Cdd:smart00267  82 GGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIP-LYLTISIGVAAYPNP-GEDAEDLLKRADTALYQAKKAGRNQ 159

                   ...
gi 2017541161  301 VEL 303
Cdd:smart00267 160 VAV 162
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
128-301 1.27e-52

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 173.63  E-value: 1.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 128 QDELKRSNEMLRTLSITDPLTHLHNRRHLMEMVEREFQRASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIV 207
Cdd:NF038266   80 QRMMRDLNEALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 208 TRRLRSYDLAARYGGEEFVLLLPETPIHEALSIAERLRLEVQEHVFDGSLQGLVLTISLGVATYPSSRvESIDSLFRQAD 287
Cdd:NF038266  160 RAELREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEHRPPE-EGLSATLSRAD 238
                         170
                  ....*....|....
gi 2017541161 288 EALYRAKQGGRNRV 301
Cdd:NF038266  239 QALYQAKRAGRDRV 252
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
4-303 1.73e-49

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: 174.96  E-value: 1.73e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRGEIFRTLQEVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPVII 83
Cdd:COG5001   113 LALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLAL 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  84 LTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLKMKSLQDELKRSNEMLRTLSITDPLTHLHNRRHLMEMVERE 163
Cdd:COG5001   193 LLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQA 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 164 FQRASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIVTRRLRSYDLAARYGGEEFVLLLPETP-IHEALSIAE 242
Cdd:COG5001   273 LARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDdPEDAEAVAE 352
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017541161 243 RLRLEVQE-HVFDGslQGLVLTISLGVATYPSSRvESIDSLFRQADEALYRAKQGGRNRVEL 303
Cdd:COG5001   353 RILAALAEpFELDG--HELYVSASIGIALYPDDG-ADAEELLRNADLAMYRAKAAGRNRYRF 411
dguan_cyc_DgcA NF041606
diguanylate cyclase DgcA;
134-303 1.82e-47

diguanylate cyclase DgcA;


Pssm-ID: 469490 [Multi-domain]  Cd Length: 340  Bit Score: 162.61  E-value: 1.82e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 134 SNEMLRTLSITDPLTHLHNRRHLMEMVEREFQRASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIVTRRLRS 213
Cdd:NF041606  170 NNALLLEMTTTDMMTHLKLKHYFYTVLMEKLDTINSQGEPLSILMLDIDFFKQINDTYGHACGDLVLQMVASIIQSCTRT 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 214 YDLAARYGGEEFVLLLPETPIHEALSIAERLRLEVQEHVFDGSLQGLVLTISLGVATYpSSRVESIDSLFRQADEALYRA 293
Cdd:NF041606  250 QDMAARYGGEEFVVMLSNTSSKTAKKIAERIRKSIENLSILYDEQHIRVTISIGVAEY-NFDVESAKSLVERADKALYES 328
                         170
                  ....*....|
gi 2017541161 294 KQGGRNRVEL 303
Cdd:NF041606  329 KQNGRNRVSI 338
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
2-294 6.46e-46

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: 153.91  E-value: 6.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   2 TTTVLVIDDSDTLRGEIFRTLQEVSLfdSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPV 81
Cdd:COG3706     1 PARILVVDDDPTNRKLLRRLLEAAGY--EVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  82 IILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVrvqlkmkslqdelkrsnemlrtlsitdplthlhnrrhlmemve 161
Cdd:COG3706    79 IFLTALDDEEDRARALEAGADDYLTKPFDPEELLARV------------------------------------------- 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 162 refqrasrkgahlslvildidyfkkindtyghqegdrvltilaeivtrrlrsyDLAARYGGEEFVLLLPETPIHEALSIA 241
Cdd:COG3706   116 -----------------------------------------------------DLVARYGGEEFAILLPGTDLEGALAVA 142
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2017541161 242 ERLRLEVQEhvfdgsLQGLVLTISLGVAtypssrvesIDSLFRQADeALYRAK 294
Cdd:COG3706   143 ERIREAVAE------LPSLRVTVSIGVA---------GDSLLKRAD-ALYQAR 179
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
136-301 2.32e-45

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 162.11  E-value: 2.32e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 136 EMLRTLSITDPLTHLHNRRHLMEMVEREFQRASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIVTRRLRSYD 215
Cdd:PRK15426  392 SSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQD 471
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 216 LAARYGGEEFVLLLPETPIHEALSIAERLRLEVQ-EHVFDGSLQGLVLTISLGVATYPSSRVESIDSLFRQADEALYRAK 294
Cdd:PRK15426  472 VAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINeKEILVAKSTTIRISASLGVSSAEEDGDYDFEQLQSLADRRLYLAK 551

                  ....*..
gi 2017541161 295 QGGRNRV 301
Cdd:PRK15426  552 QAGRNRV 558
PRK09894 PRK09894
diguanylate cyclase; Provisional
136-304 1.35e-42

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 148.68  E-value: 1.35e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 136 EMLRTLSITDPLTHLHNRRHLMEMVERefQRASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIVTRRLRSYD 215
Cdd:PRK09894  123 YLLTIRSNMDVLTGLPGRRVLDESFDH--QLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYE 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 216 LAARYGGEEFVLLLPETPIHEALSIAERLRLEVQEHVF---DGSLQglvLTISLGVATypSSRVESIDSLFRQADEALYR 292
Cdd:PRK09894  201 TVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAIthsDGRIN---ITATFGVSR--AFPEETLDVVIGRADRAMYE 275
                         170
                  ....*....|..
gi 2017541161 293 AKQGGRNRVELM 304
Cdd:PRK09894  276 GKQTGRNRVMFI 287
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
1-139 1.57e-34

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: 125.66  E-value: 1.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   1 MTT----TVLVIDDSDTLRgEIFRTLqevsLFDSY---LEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAR 73
Cdd:COG3437     1 MRTgqapTVLIVDDDPENL-ELLRQL----LRTLGydvVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRAD 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017541161  74 EEFQDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLKMKSLQDELKRSNEMLR 139
Cdd:COG3437    76 PSTRDIPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYLK 141
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
4-123 2.32e-31

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: 116.59  E-value: 2.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRGEIFRTLQEvslfDSY--LEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREefQDLPV 81
Cdd:COG0745     3 RILVVEDDPDIRELLADALER----EGYevDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARP--SDIPI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2017541161  82 IILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLK 123
Cdd:COG0745    77 IMLTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLR 118
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
4-123 2.72e-30

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: 111.48  E-value: 2.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRGEIFRTLQEvsLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPVII 83
Cdd:COG0784     7 RILVVDDNPDNRELLRRLLER--LGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPIIA 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2017541161  84 LTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLK 123
Cdd:COG0784    85 LTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLA 124
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
4-119 1.33e-28

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: 106.76  E-value: 1.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDT---LRGEIFRTLQEVSlFDSYLEARDGLEgfkTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLP 80
Cdd:cd17551     2 RILIVDDNPTnllLLEALLRSAGYLE-VVSFTDPREALA---WCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVP 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2017541161  81 VIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:cd17551    78 IVMITADTDREVRLRALEAGATDFLTKPFDPVELLARVR 116
adrA PRK10245
diguanylate cyclase AdrA; Provisional
114-305 2.87e-27

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 109.53  E-value: 2.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 114 LVARVRVQLKMKslqdeLKRSNEMLRTLSITDPLTHLHNRRHLMEMVEREFQRASRKGAHLSLVILDIDYFKKINDTYGH 193
Cdd:PRK10245  182 LFAWVSYQTATK-----LAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGH 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 194 QEGDRVLTILAEIVTRRLRSYDLAARYGGEEFVLLLPETPIHEALSIAERLRLEVQEHVFDGSLQgLVLTISLGVATYpS 273
Cdd:PRK10245  257 DVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQ-VTLRISVGVAPL-N 334
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2017541161 274 SRVESIDSLFRQADEALYRAKQGGRNRVELMA 305
Cdd:PRK10245  335 PQMSHYREWLKSADLALYKAKNAGRNRTEVAA 366
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
5-119 4.35e-27

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: 102.23  E-value: 4.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRgEIFRTLQEVSLFdSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREefQDLPVIIL 84
Cdd:pfam00072   1 VLIVDDDPLIR-ELLRQLLEKEGY-VVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRD--PTTPVIIL 76
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2017541161  85 TGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:pfam00072  77 TAHGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-138 8.21e-26

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: 106.20  E-value: 8.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   1 MTTTVLVIDDSDTLRGEIFRTLQ----EVslfdsyLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAmmRAREEF 76
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLEragyEV------ETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLR--ELRALD 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017541161  77 QDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLKMKSLQDELKRSNEML 138
Cdd:COG2204    73 PDLPVILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSGLI 134
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
4-108 1.20e-25

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


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 98.31  E-value: 1.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRGEIFRTLQEVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAmmRAREEFQDLPVII 83
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEAGFEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLE--AIRELDPDTKIII 78
                          90       100
                  ....*....|....*....|....*
gi 2017541161  84 LTGREDRDTKIRGLEQGASDYVTKP 108
Cdd:COG4753    79 LSGYSDFEYAQEAIKLGADDYLLKP 103
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
6-108 1.35e-25

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: 98.07  E-value: 1.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   6 LVIDDSDTLRGEIFRTLQevSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAmmRAREEFQDLPVIILT 85
Cdd:cd00156     1 LIVDDDPAIRELLKSLLE--REGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLR--KLRELPPDIPVIVLT 76
                          90       100
                  ....*....|....*....|...
gi 2017541161  86 GREDRDTKIRGLEQGASDYVTKP 108
Cdd:cd00156    77 AKADEEDAVRALELGADDYLVKP 99
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
134-301 2.23e-25

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 106.68  E-value: 2.23e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  134 SNEMLRTLSIT---DPLTHLHNRRHLMEMVEREFQRASRKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIVTRR 210
Cdd:PRK09776   654 SRKMLRQLSYSashDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSM 733
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  211 LRSYDLAARYGGEEFVLLLPETPIHEALSIAERLRLEVQEHVFdgSLQGLVLTI--SLGVA-----TYPSSRVESidslf 283
Cdd:PRK09776   734 LRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHF--PWEGRVYRVgaSAGITlidanNHQASEVMS----- 806
                          170
                   ....*....|....*...
gi 2017541161  284 rQADEALYRAKQGGRNRV 301
Cdd:PRK09776   807 -QADIACYAAKNAGRGRV 823
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
130-298 6.36e-25

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 105.15  E-value: 6.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 130 ELKRSNEMLRTLSITDPLTHLHNRRHLMEMVEREFQRASrkGAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIVTR 209
Cdd:PRK10060  225 EERRAQERLRILANTDSITGLPNRNAIQELIDHAINAAD--NNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILS 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 210 RLRSYDLAARYGGEEFVLLLPETPIH--EALS--IAERLRLEvqehvFDGSLQGLVLTISLGVATYPSSRvESIDSLFRQ 285
Cdd:PRK10060  303 CLEEDQTLARLGGDEFLVLASHTSQAalEAMAsrILTRLRLP-----FRIGLIEVYTGCSIGIALAPEHG-DDSESLIRS 376
                         170
                  ....*....|...
gi 2017541161 286 ADEALYRAKQGGR 298
Cdd:PRK10060  377 ADTAMYTAKEGGR 389
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
6-108 2.88e-24

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: 94.40  E-value: 2.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   6 LVIDDSDTLRGEIFRTLQEvslfDSY--LEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRarEEFQDLPVII 83
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEK----EGYevDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLR--EKGSDIPIIM 74
                          90       100
                  ....*....|....*....|....*
gi 2017541161  84 LTGREDRDTKIRGLEQGASDYVTKP 108
Cdd:cd17574    75 LTAKDEEEDKVLGLELGADDYITKP 99
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
4-119 5.04e-24

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: 94.67  E-value: 5.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRGEIFRTLQ----EVslfdsyLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQDL 79
Cdd:cd17562     2 KILAVDDSASIRQMVSFTLRgagyEV------VEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFT 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2017541161  80 PVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:cd17562    76 PILMLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVK 115
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
5-118 1.20e-23

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: 93.56  E-value: 1.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEVSlFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPVIIL 84
Cdd:cd19923     3 VLVVDDFSTMRRIIKNLLKELG-FNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLMV 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2017541161  85 TGREDRDTKIRGLEQGASDYVTKPFDAGELVARV 118
Cdd:cd19923    82 TAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKL 115
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1-133 1.14e-22

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 91.57  E-value: 1.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   1 MTTTVLVIDDSDTLRGEIFRTLQEVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAReeFQDLP 80
Cdd:COG4565     2 KMIRVLIVEDDPMVAELLRRYLERLPGFEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRAR--GPDVD 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2017541161  81 VIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLKMKSLQDELKR 133
Cdd:COG4565    80 VIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQE 132
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
6-123 1.15e-22

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: 90.74  E-value: 1.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   6 LVIDDSDTLRGEIFRTLQEvslfDSYL--EARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEfqDLPVII 83
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKK----EGYTvdVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGI--ETPVLL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2017541161  84 LTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLK 123
Cdd:cd17625    75 LTALDAVEDRVKGLDLGADDYLPKPFSLAELLARIRALLR 114
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
6-123 6.16e-22

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: 88.87  E-value: 6.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   6 LVIDDSDTLRGEIFRTLQ----EVSlfdsylEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPV 81
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEkegyEVV------TAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPI 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2017541161  82 IILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLK 123
Cdd:cd19937    75 IMLTAKGEEFDKVLGLELGADDYITKPFSPRELLARVKAVLR 116
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
3-122 6.68e-22

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: 88.85  E-value: 6.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   3 TTVLVIDDSDTLRgEIFRTLQEVSLFDSyLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPVI 82
Cdd:cd17618     1 RTILIVEDEPAIR-EMIAFNLERAGFDV-VEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPII 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2017541161  83 ILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQL 122
Cdd:cd17618    79 MLTARGEEEDKVRGLEAGADDYITKPFSPRELVARIKAVL 118
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
34-123 2.34e-21

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: 87.15  E-value: 2.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  34 ARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREefQDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGE 113
Cdd:cd17624    28 VRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQG--QSLPVLILTARDGVDDRVAGLDAGADDYLVKPFALEE 105
                          90
                  ....*....|
gi 2017541161 114 LVARVRVQLK 123
Cdd:cd17624   106 LLARLRALLR 115
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
5-109 4.07e-21

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: 86.41  E-value: 4.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDD--------SDTLRGEIFRTLQevslfdsyleARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEF 76
Cdd:cd19920     1 ILIVDDvpdnlrllSELLRAAGYRVLV----------ATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPAT 70
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2017541161  77 QDLPVIILTGREDRDTKIRGLEQGASDYVTKPF 109
Cdd:cd19920    71 RHIPVIFLTALTDTEDKVKGFELGAVDYITKPF 103
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
3-108 5.57e-21

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: 86.49  E-value: 5.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   3 TTVLVIDDSDTLRgEIFRTLQEVSLFDsYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMraREEFQDLPVI 82
Cdd:cd17555     1 ATILVIDDDEVVR-ESIAAYLEDSGFQ-VLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQI--TKESPDTPVI 76
                          90       100
                  ....*....|....*....|....*.
gi 2017541161  83 ILTGREDRDTKIRGLEQGASDYVTKP 108
Cdd:cd17555    77 VVSGAGVMSDAVEALRLGAWDYLTKP 102
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
4-109 1.70e-20

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: 84.47  E-value: 1.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDD--------SDTLRGEIFRTLqevslfdsylEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREE 75
Cdd:cd17538     1 KILVVDDepanrellEALLSAEGYEVL----------TADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPE 70
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2017541161  76 FQDLPVIILTGREDRDTKIRGLEQGASDYVTKPF 109
Cdd:cd17538    71 TRHIPVIMITALDDREDRIRGLEAGADDFLSKPI 104
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
5-123 4.10e-20

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: 83.97  E-value: 4.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQevslFDSY--LEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRflAMMRAREEFQDLPVI 82
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLR----FEGYevETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLE--VCRRLRAAGNDLPIL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2017541161  83 ILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLK 123
Cdd:cd17627    75 VLTARDSVSDRVAGLDAGADDYLVKPFALEELLARVRALLR 115
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
3-119 5.50e-20

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: 83.86  E-value: 5.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   3 TTVLVIDDSDTLRGEIFRTLQEVSL----FDSYLEARDGLEgfktllNNRVDLVLCDLEMPRMDGFRFLAmmRAREEFQD 78
Cdd:cd19919     1 KTVWIVDDDSSIRWVLERALAGAGLtvtsFENAQEALAALA------SSQPDVLISDIRMPGMDGLALLA--QIKQRHPD 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2017541161  79 LPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:cd19919    73 LPVIIMTAHSDLDSAVSAYQGGAFEYLPKPFDIDEAVALVE 113
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
4-119 1.25e-19

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: 83.23  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDtlrGEIF---RTLQEVSLFDSYLEARDGLEGFKTLLNN-------RVDLVLCDLEMPRMDGFRFLAMMRAR 73
Cdd:cd17557     1 TILLVEDNP---GDAEliqEAFKEAGVPNELHVVRDGEEALDFLRGEgeyadapRPDLILLDLNMPRMDGFEVLREIKAD 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2017541161  74 EEFQDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:cd17557    78 PDLRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIR 123
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
5-108 2.04e-19

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: 82.04  E-value: 2.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEVSLfdSYLEARDGLEGFK---------TLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREE 75
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGF--EIAEAVDGEEALNklenlakegNDLSKELDLIITDIEMPKMDGYELTFELRDDPR 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2017541161  76 FQDLPVIILTGREDRDTKIRGLEQGASDYVTKP 108
Cdd:cd19924    79 LANIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
4-123 4.28e-19

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: 81.24  E-value: 4.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRgEIFRTLQEVSLFDSYLeARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAmmRAREEFQDLPVII 83
Cdd:cd17615     1 RVLVVDDEPNIT-ELLSMALRYEGWDVET-AADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLR--RLRADGPDVPVLF 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2017541161  84 LTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLK 123
Cdd:cd17615    77 LTAKDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALLR 116
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
3-118 5.59e-19

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: 81.03  E-value: 5.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   3 TTVLVIDDSDTLRGEIfRTLQEVSLFdSYLEARDGLEGFKTLLNNR-VDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPV 81
Cdd:cd17544     1 IKVLVVDDSATSRNHL-RALLRRHNF-QVLEAANGQEALEVLEQHPdIKLVITDYNMPEMDGFELVREIRKKYSRDQLAI 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2017541161  82 IILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARV 118
Cdd:cd17544    79 IGISASGDNALSARFIKAGANDFLTKPFLPEEFYCRV 115
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
5-119 9.69e-19

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: 80.45  E-value: 9.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEvslfDSY--LEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPVI 82
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEE----QGYkvQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVI 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2017541161  83 ILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:cd17598    77 LLTTLSDPRDVIRGLECGADNFITKPYDEKYLLSRIK 113
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
5-133 1.10e-18

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: 80.61  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQ----EVSLFDSYLEArdgLEGFKTllnNRVDLVLCDLEMPRMDGFRFLAMMRAREEfqDLP 80
Cdd:cd17549     1 VLLVDDDADVREALQQTLElagfRVRAFADAEEA---LAALSP---DFPGVVISDIRMPGMDGLELLAQIRELDP--DLP 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2017541161  81 VIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLKMKSLQDELKR 133
Cdd:cd17549    73 VILITGHGDVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRLVLENRR 125
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
4-140 1.77e-18

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 85.67  E-value: 1.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRGEI--FRTLQEVSLFDsyleARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREefQDLPV 81
Cdd:PRK11361    6 RILIVDDEDNVRRMLstAFALQGFETHC----ANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHE--TRTPV 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2017541161  82 IILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLKMKSLQDELKRSNEMLRT 140
Cdd:PRK11361   80 ILMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALST 138
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
5-116 2.06e-18

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: 79.42  E-value: 2.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDS-DTLrgEIFRTL-----QEVSLfdsyleARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQD 78
Cdd:cd17580     1 ILVVDDNeDAA--EMLALLlelegAEVTT------AHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLAN 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2017541161  79 LPVIILTG---REDRDtkiRGLEQGASDYVTKPFDAGELVA 116
Cdd:cd17580    73 TPAIALTGygqPEDRE---RALEAGFDAHLVKPVDPDELIE 110
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
5-119 2.35e-18

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: 79.36  E-value: 2.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEvslfDSYLE----ARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAReefQDLP 80
Cdd:cd17541     3 VLIVDDSAVMRKLLSRILES----DPDIEvvgtARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAE---RPTP 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2017541161  81 VIILTG--REDRDTKIRGLEQGASDYVTKPF---------DAGELVARVR 119
Cdd:cd17541    76 VVMVSSltEEGAEITLEALELGAVDFIAKPSggisldleeIAEELIEKIK 125
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
5-119 2.98e-18

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: 79.09  E-value: 2.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAmmRAREEFQDLPVIIL 84
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLESEPDIEVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALR--RLRRRYPDLKVIVL 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2017541161  85 TGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:cd17535    79 TAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIR 113
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
4-119 3.73e-18

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: 78.74  E-value: 3.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRgEIFRTLQEVSLFDSyLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPVII 83
Cdd:cd17548     1 KILIVEDNPLNM-KLARDLLESAGYEV-LEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIA 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2017541161  84 LTG---REDRDtkiRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:cd17548    79 LTAyamKGDRE---KILEAGCDGYISKPIDTREFLETVA 114
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
4-120 6.54e-18

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: 77.87  E-value: 6.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRGEIFRTLQEVSLFDSylEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAReefQDLPVII 83
Cdd:cd17594     1 HVLVVDDDAAMRHLLILYLRERGFDVT--AAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRAR---SDVPIII 75
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2017541161  84 LTG-REDRDTKIRGLEQGASDYVTKPFDAGELVARVRV 120
Cdd:cd17594    76 ISGdRRDEIDRVVGLELGADDYLAKPFGLRELLARVRA 113
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
5-122 6.85e-18

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: 77.90  E-value: 6.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDsDTLRGEIFRTLQEVSLFDSYLEArDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAReefQDLPVIIL 84
Cdd:cd17626     3 ILVVDD-DAALAEMIGIVLRGEGFDPAFCG-DGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAE---SGVPIVML 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2017541161  85 TGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQL 122
Cdd:cd17626    78 TAKSDTVDVVLGLESGADDYVAKPFKPKELVARIRARL 115
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
5-119 8.98e-18

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: 77.81  E-value: 8.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGeifrTLQEVSLFDSY--LEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEfqdLPVI 82
Cdd:cd17619     3 ILIVEDEPVTRA----TLKSYFEQEGYdvSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSE---VGII 75
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2017541161  83 ILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:cd17619    76 LVTGRDDEVDRIVGLEIGADDYVTKPFNPRELLVRAK 112
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
5-123 1.04e-17

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 77.35  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDsDTLRGEIFRTLQEVSLFdSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAReefQDLPVIIL 84
Cdd:cd17623     1 ILLIDD-DRELTELLTEYLEMEGF-NVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKT---SQVPVLML 75
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2017541161  85 TGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLK 123
Cdd:cd17623    76 TARGDDIDRILGLELGADDYLPKPFNPRELVARIRAILR 114
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
5-116 1.47e-17

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: 77.12  E-value: 1.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRgEIFRTLQEvSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREE-FQDLPVII 83
Cdd:cd17546     1 VLVVDDNPVNR-KVLKKLLE-KLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGgGRRTPIIA 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2017541161  84 LTGREDRDTKIRGLEQGASDYVTKPFDAGELVA 116
Cdd:cd17546    79 LTANALEEDREKCLEAGMDDYLSKPVKLDQLKE 111
PRK11517 PRK11517
DNA-binding response regulator HprR;
5-123 3.88e-17

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 78.79  E-value: 3.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEVSLFDSYleARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEfqdLPVIIL 84
Cdd:PRK11517    3 ILLIEDNQRTQEWVTQGLSEAGYVIDA--VSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQ---TPVICL 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2017541161  85 TGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLK 123
Cdd:PRK11517   78 TARDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQLR 116
PRK15479 PRK15479
transcriptional regulator TctD;
34-123 5.60e-17

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 78.22  E-value: 5.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  34 ARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREefQDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGE 113
Cdd:PRK15479   30 VFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRG--QTLPVLLLTARSAVADRVKGLNVGADDYLPKPFELEE 107
                          90
                  ....*....|
gi 2017541161 114 LVARVRVQLK 123
Cdd:PRK15479  108 LDARLRALLR 117
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
5-123 7.46e-17

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: 75.45  E-value: 7.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEVSL-FDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGfrfLAMMR-AREEFQDLPVI 82
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIDWEELgFEVVGEAENGEEALELIEEHKPDIVITDIRMPGMDG---LELIEkIRELYPDIKII 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2017541161  83 ILTGRED----RdtkiRGLEQGASDYVTKPFDAGEL---VARVRVQLK 123
Cdd:cd17536    78 ILSGYDDfeyaQ----KAIRLGVVDYLLKPVDEEELeeaLEKAKEELD 121
resp_reg_YycF NF040534
response regulator YycF;
34-165 7.53e-17

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 78.22  E-value: 7.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  34 ARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAReefQDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGE 113
Cdd:NF040534   30 AYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVRKK---YDMPIIMLTAKDSEIDKVLGLELGADDYVTKPFSTRE 106
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2017541161 114 LVARVRVQL---KMKSLQDELKRSNEM-LRTLSITDPLTHLHNRRHLMEMVEREFQ 165
Cdd:NF040534  107 LIARVKANLrrhQQQNTEEEEEENNEIvIGSLTIHPDAYTVKKRGETIELTHREFE 162
PRK10610 PRK10610
chemotaxis protein CheY;
6-114 8.70e-17

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 75.40  E-value: 8.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   6 LVIDDSDTLRgEIFRTLQEVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPVIILT 85
Cdd:PRK10610    9 LVVDDFSTMR-RIVRNLLKELGFNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVT 87
                          90       100
                  ....*....|....*....|....*....
gi 2017541161  86 GREDRDTKIRGLEQGASDYVTKPFDAGEL 114
Cdd:PRK10610   88 AEAKKENIIAAAQAGASGYVVKPFTAATL 116
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
5-108 8.86e-17

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: 74.51  E-value: 8.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEVSLfdSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRareEFQDLPVIIL 84
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGY--RVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLR---EWSAVPVIVL 75
                          90       100
                  ....*....|....*....|....
gi 2017541161  85 TGREDRDTKIRGLEQGASDYVTKP 108
Cdd:cd17620    76 SARDEESDKIAALDAGADDYLTKP 99
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
5-119 1.54e-16

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: 74.24  E-value: 1.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEVSLfdSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAmmRAREEFQDLPVIIL 84
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGY--VVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLR--RWRSEGRATPVLIL 76
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2017541161  85 TGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:cd19934    77 TARDSWQDKVEGLDAGADDYLTKPFHIEELLARLR 111
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
5-108 1.59e-16

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: 73.95  E-value: 1.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEVSLfdSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPVIIL 84
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGF--TVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFL 78
                          90       100
                  ....*....|....*....|....
gi 2017541161  85 TGREDRDTKIRGLEQGASDYVTKP 108
Cdd:cd19927    79 TAKGMTSDRIKGYNAGCDGYLSKP 102
PRK10766 PRK10766
two-component system response regulator TorR;
1-135 1.65e-16

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 77.00  E-value: 1.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   1 MTTTVLVIDDSDTLRGEIFRTLQEvslfDSY--LEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGfrfLAMMRAREEFQD 78
Cdd:PRK10766    1 MSYHILVVEDEPVTRARLQGYFEQ----EGYtvSEAASGAGMREIMQNQHVDLILLDINLPGEDG---LMLTRELRSRST 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017541161  79 LPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARV-----RVQLKMKSLQDELKRSN 135
Cdd:PRK10766   74 VGIILVTGRTDSIDRIVGLEMGADDYVTKPLELRELLVRVknllwRISLARQAQPHAQEEDN 135
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
5-131 1.89e-16

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: 74.27  E-value: 1.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTL---QEVSLfdsyleARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPV 81
Cdd:cd17539     1 VLLVDDRPSSAERIAAMLsseHEVVV------EADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQLPI 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2017541161  82 IILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLKMKSLQDEL 131
Cdd:cd17539    75 LAVADPGDRGRLIRALEIGVNDYLVRPIDPNELLARVRTQIRRKRYTDYL 124
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
5-114 2.39e-16

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: 73.82  E-value: 2.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQ----EVSLFDSYLEARDGLEGFKtllnNRVDLVLCDLEMPRMDGFRFLAmmRAREEFqDLP 80
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLrcgyQVTTCTDAEEALSMLRENK----DEFDLVITDVHMPDMDGFEFLE--LIRLEM-DLP 73
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2017541161  81 VIILTGREDRDTKIRGLEQGASDYVTKPFDAGEL 114
Cdd:cd17584    74 VIMMSADGSTSTVMKGLAHGACDYLLKPVSIEDL 107
PRK11173 PRK11173
two-component response regulator; Provisional
2-139 2.66e-16

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 76.59  E-value: 2.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   2 TTTVLVIDDSDTLRgeifRTLQevSLFDS--Y--LEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGfrflaMMRARE--E 75
Cdd:PRK11173    3 TPHILIVEDELVTR----NTLK--SIFEAegYdvFEATDGAEMHQILSENDINLVIMDINLPGKNG-----LLLARElrE 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017541161  76 FQDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR--VQLKMK-SLQDELKRSNEMLR 139
Cdd:PRK11173   72 QANVALMFLTGRDNEVDKILGLEIGADDYITKPFNPRELTIRARnlLSRTMNlGTVSEERRSVESYK 138
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1-140 3.41e-16

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: 75.38  E-value: 3.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   1 MTTTVLVIDDSDTLRGEIFRTLQEVSlFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAReefQDLP 80
Cdd:COG3707     2 RGLRVLVVDDEPLRRADLREGLREAG-YEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEE---RPAP 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017541161  81 VIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQL----KMKSLQDELKRSNEMLRT 140
Cdd:COG3707    78 VILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALarfrELRALRRELAKLREALEE 141
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
2-119 4.69e-16

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: 72.97  E-value: 4.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   2 TTTVLVIDDSDTLRgEIFRT-LQEVSLFDSyLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLP 80
Cdd:cd17552     1 SKRILVIDDEEDIR-EVVQAcLEKLAGWEV-LTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIP 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2017541161  81 VIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:cd17552    79 VILLTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIA 117
orf27 CHL00148
Ycf27; Reviewed
5-123 7.85e-16

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 75.52  E-value: 7.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRgeifRTLQEVSLFDSY--LEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAReefQDLPVI 82
Cdd:CHL00148    9 ILVVDDEAYIR----KILETRLSIIGYevITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKE---SDVPII 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2017541161  83 ILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLK 123
Cdd:CHL00148   82 MLTALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVLR 122
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
174-296 9.74e-16

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: 72.77  E-value: 9.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 174 LSLVILDIDYFKKINDTYGHQEGDRVLTILAEIVTRRL-RSYDLAARYGGEEFVLLLPETPIHEALSIAERLRLEVQEhv 252
Cdd:cd07556     2 VTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSA-- 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2017541161 253 fDGSLQGLVLTISLGVATYP--------SSRVESIDSLFRQADEALYRAKQG 296
Cdd:cd07556    80 -LNQSEGNPVRVRIGIHTGPvvvgvigsRPQYDVWGALVNLASRMESQAKAG 130
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
3-116 9.80e-16

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: 72.18  E-value: 9.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   3 TTVLVIDDSDTLRGEIFRTLQE---VSLFdsylEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREefQDL 79
Cdd:cd17593     1 MKVLICDDSSMARKQLARALPAdwdVEIT----FAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQ--LET 74
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2017541161  80 PVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVA 116
Cdd:cd17593    75 KVIVVSGDVQPEAKERVLELGALAFLKKPFDPEKLAQ 111
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1-119 1.49e-15

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 76.34  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   1 MTTTVLVIDDSDTLRGEIFRTLQEvslfDSYLE----ARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFL-AMMRARee 75
Cdd:PRK00742    2 MKIRVLVVDDSAFMRRLISEILNS----DPDIEvvgtAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALeKIMRLR-- 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2017541161  76 fqDLPVII---LTGREDRDTkIRGLEQGASDYVTKPFD---------AGELVARVR 119
Cdd:PRK00742   76 --PTPVVMvssLTERGAEIT-LRALELGAVDFVTKPFLgislgmdeyKEELAEKVR 128
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
5-123 1.63e-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: 71.69  E-value: 1.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDD----SDTLRGEIFRTLQEVSLfdsyleARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAReefQDLP 80
Cdd:cd17614     1 ILVVDDekpiSDILKFNLTKEGYEVVT------AYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKT---SNVP 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2017541161  81 VIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLK 123
Cdd:cd17614    72 IIMLTAKDSEVDKVLGLELGADDYVTKPFSNRELLARVKANLR 114
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
1-123 1.98e-15

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 74.37  E-value: 1.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   1 MTTTVLVIDDSDTLRGEIFRTLQEVSLfdSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLP 80
Cdd:PRK10161    1 MARRILVVEDEAPIREMVCFVLEQNGF--QPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIP 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2017541161  81 VIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLK 123
Cdd:PRK10161   79 VVMLTARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMR 121
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
50-119 2.00e-15

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: 71.29  E-value: 2.00e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  50 DLVLCDLEMPRMDGFRFLAMMRAREefQDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:cd17616    44 DIILLDLNLPDMSGYEVLRTLRLAK--VKTPILILSGLADIEDKVKGLGFGADDYMTKPFHKDELVARIH 111
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
124-297 2.17e-15

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 76.73  E-value: 2.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 124 MKSLQDELKRSNEMLRTLSITDPLTHLHNRRHLMEMVEREFQrasrKGAHLSLVILDIDYFKKINDTYGHQEGDRVLTIL 203
Cdd:PRK11359  358 LAALALEQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVD----KAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEV 433
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 204 AEIVTRRLRSYDLAARYGGEEFVLLLPETPIHEALSIAERLRLEVQEHV-FDGslQGLVLTISLGVaTYPSSRveSIDSL 282
Cdd:PRK11359  434 VNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPImIDD--KPFPLTLSIGI-SYDVGK--NRDYL 508
                         170
                  ....*....|....*.
gi 2017541161 283 FRQADEAL-YRAKQGG 297
Cdd:PRK11359  509 LSTAHNAMdYIRKNGG 524
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
4-138 2.64e-15

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 74.08  E-value: 2.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRGEIFRTLQEVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEfqDLPVII 83
Cdd:COG3279     3 KILIVDDEPLARERLERLLEKYPDLEVVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDP--PPPIIF 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2017541161  84 LTGREDRdtKIRGLEQGASDYVTKPFDAGEL---VARVRVQLKMKSLQDELKRSNEML 138
Cdd:COG3279    81 TTAYDEY--ALEAFEVNAVDYLLKPIDEERLakaLEKAKERLEAKAAAEASPEEKDRI 136
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
1-123 3.48e-15

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 73.46  E-value: 3.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   1 MTTTVLVIDD----SDT----LRGEIFrTLQEVSLfdsyleardGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRA 72
Cdd:PRK11083    2 QQPTILLVEDeqaiADTlvyaLQSEGF-TVEWFER---------GLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLA 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2017541161  73 REEfqDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLK 123
Cdd:PRK11083   72 FHP--ALPVIFLTARSDEVDRLVGLEIGADDYVAKPFSPREVAARVRTILR 120
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
5-108 3.51e-15

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: 70.16  E-value: 3.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQE----VSLfdsyleARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREefQDLP 80
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEegyaVDV------AYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAG--KQTP 72
                          90       100
                  ....*....|....*....|....*...
gi 2017541161  81 VIILTGREDRDTKIRGLEQGASDYVTKP 108
Cdd:cd19935    73 VLMLTARDSVEDRVKGLDLGADDYLVKP 100
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
4-119 5.04e-15

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: 72.44  E-value: 5.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRGEIFRTLQ----EVSLFDSyleARDGLEGFKtllNNRVDLVLCDLEMPRMDGFRFLAMMRAREefQDL 79
Cdd:COG4566     1 TVYIVDDDEAVRDSLAFLLEsaglRVETFAS---AEAFLAALD---PDRPGCLLLDVRMPGMSGLELQEELAARG--SPL 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2017541161  80 PVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:COG4566    73 PVIFLTGHGDVPMAVRAMKAGAVDFLEKPFDDQALLDAVR 112
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
4-119 5.79e-15

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: 69.94  E-value: 5.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRgeifrtlqevSLFDSYLE--------ARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREE 75
Cdd:cd17554     2 KILVVDDEENIR----------ELYKEELEdegyevvtAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKP 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2017541161  76 fqDLPVIILTGREDRDTKIRGLEQGAsdYVTKPFDAGELVARVR 119
Cdd:cd17554    72 --DLPVIICTAYSEYKSDFSSWAADA--YVVKSSDLTELKETIK 111
PRK10643 PRK10643
two-component system response regulator PmrA;
34-119 6.99e-15

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 72.38  E-value: 6.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  34 ARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAmmRAREEFQDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGE 113
Cdd:PRK10643   30 ASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLR--RWRQKKYTLPVLILTARDTLEDRVAGLDVGADDYLVKPFALEE 107

                  ....*.
gi 2017541161 114 LVARVR 119
Cdd:PRK10643  108 LHARIR 113
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
5-143 1.01e-14

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 72.14  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRgEIFRTLQEVSLFDSYLeARDGLEGFKtLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEfqdLPVIIL 84
Cdd:PRK10955    4 ILLVDDDRELT-SLLKELLEMEGFNVIV-AHDGEQALD-LLDDSIDLLLLDVMMPKKNGIDTLKELRQTHQ---TPVIML 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2017541161  85 TGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLKMKSLQDELKRSNEMLRTLSI 143
Cdd:PRK10955   78 TARGSELDRVLGLELGADDYLPKPFNDRELVARIRAILRRSHWSEQQQNNDNGSPTLEV 136
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
4-119 1.62e-14

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: 68.97  E-value: 1.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDsdtlrgE--IFRTLQEVSLFDSY--LEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAmmRAREEFQDL 79
Cdd:cd17569     2 TILLVDD------EpnILKALKRLLRREGYevLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLK--RVRERYPDT 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2017541161  80 PVIILTGREDRDTKIRGLEQGA-SDYVTKPFDAGELVARVR 119
Cdd:cd17569    74 VRILLTGYADLDAAIEAINEGEiYRFLTKPWDDEELKETIR 114
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
36-108 1.68e-14

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: 68.16  E-value: 1.68e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017541161  36 DGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPVIILTGREDRDTKIRGLEQGASDYVTKP 108
Cdd:cd17602    30 DPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTGKDGLVDRIRAKMAGASGYLTKP 102
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
3-126 1.94e-14

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 71.37  E-value: 1.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   3 TTVLVIDDSDTLR--------GEIFRTLQEVSLFDSYLEARdglegfktllNNRVDLVLCDLEMPRMDGFRFLAMMRare 74
Cdd:PRK10529    2 TNVLIVEDEQAIRrflrtaleGDGMRVFEAETLQRGLLEAA----------TRKPDLIILDLGLPDGDGIEFIRDLR--- 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2017541161  75 EFQDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLKMKS 126
Cdd:PRK10529   69 QWSAIPVIVLSARSEESDKIAALDAGADDYLSKPFGIGELQARLRVALRRHS 120
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
5-119 2.66e-14

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: 68.29  E-value: 2.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDtlrgEIFRTLQEVsLFD---SYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAmmRAREEFQDLPV 81
Cdd:cd17550     1 ILIVDDEE----DIRESLSGI-LEDegyEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLK--EIKEKYPDLPV 73
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2017541161  82 IILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:cd17550    74 IMISGHGTIETAVKATKLGAYDFIEKPLSLDRLLLTIE 111
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
4-133 2.88e-14

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: 68.55  E-value: 2.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRGEIFRTLQEVslFDsYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAmmRAREEFQDLPVII 83
Cdd:cd17596     2 TILVVDDEVRSLEALRRTLEED--FD-VLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLK--EVRERWPEVVRII 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2017541161  84 LTGREDRDTKIRGL-EQGASDYVTKPFDAGELVARVRVQLKMKSLQDELKR 133
Cdd:cd17596    77 ISGYTDSEDIIAGInEAGIYQYLTKPWHPDQLLLTVRNAARLFELQRENER 127
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
5-129 4.74e-14

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: 67.61  E-value: 4.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGeifrtlqevsLFDSYLEARD--------GLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEf 76
Cdd:cd17572     1 VLLVEDSPSLAA----------LYQEYLSDEGykvthvetGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSL- 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2017541161  77 qDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLKMKSLQD 129
Cdd:cd17572    70 -PTSVIVITAHGSVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRKLTK 121
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
36-123 7.34e-14

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: 67.01  E-value: 7.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  36 DGLEGFKTLLNNRVDLVLCDLEMPRMDGfrfLAMMRAREEFQDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELV 115
Cdd:cd19939    31 DGQRAVRRIIDEQPSLVVLDIMLPGMDG---LTVCREVREHSHVPILMLTARTEEMDRVLGLEMGADDYLCKPFSPRELL 107

                  ....*...
gi 2017541161 116 ARVRVQLK 123
Cdd:cd19939   108 ARVRALLR 115
ompR PRK09468
osmolarity response regulator; Provisional
2-123 7.89e-14

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 70.00  E-value: 7.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   2 TTTVLVIDDSDTLRGEIFRTLQEVSLfdSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRflAMMRAREEFQDLPV 81
Cdd:PRK09468    5 NYKILVVDDDMRLRALLERYLTEQGF--QVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLS--ICRRLRSQNNPTPI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2017541161  82 IILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLK 123
Cdd:PRK09468   81 IMLTAKGEEVDRIVGLEIGADDYLPKPFNPRELLARIRAVLR 122
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
4-122 1.22e-13

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: 66.25  E-value: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLrGEIFRT-LQEVSLFDSYLEarDGLEGFKTLLNNRVDLVLCDLEMPRMDGfrfLAMMRAREEFQDLPVI 82
Cdd:cd19938     1 RILIVEDEPKL-AQLLIDyLRAAGYAPTLLA--HGDQVLPYVRHTPPDLILLDLMLPGTDG---LTLCREIRRFSDVPII 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2017541161  83 ILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQL 122
Cdd:cd19938    75 MVTARVEEIDRLLGLELGADDYICKPYSPREVVARVKAIL 114
PRK13856 PRK13856
two-component response regulator VirG; Provisional
5-154 1.65e-13

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 69.07  E-value: 1.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEVSLFDSylEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGfrfLAMMRAREEFQDLPVIIL 84
Cdd:PRK13856    4 VLVIDDDVAMRHLIVEYLTIHAFKVT--AVADSQQFNRVLASETVDVVVVDLNLGREDG---LEIVRSLATKSDVPIIII 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017541161  85 TG-REDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLKMKSLQDELKRSnemlRTLSITDPLTHLHNRR 154
Cdd:PRK13856   79 SGdRLEEADKVVALELGATDFIAKPFGTREFLARIRVALRVRPNVVRTKDR----RSFCFADWTLNLRQRR 145
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
6-108 9.71e-13

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: 63.23  E-value: 9.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   6 LVIDD-------SDTLRGEIFRTlqevslfDSYLEARDGLEGFKTLLnnrVDLVLCDLEMPRMDGFRFLAMMRAReefQD 78
Cdd:cd19936     3 LVDDDrniltsvSMALEAEGFSV-------ETYTDGASALDGLNARP---PDLAILDIKMPRMDGMELLQRLRQK---ST 69
                          90       100       110
                  ....*....|....*....|....*....|
gi 2017541161  79 LPVIILTGREDRDTKIRGLEQGASDYVTKP 108
Cdd:cd19936    70 LPVIFLTSKDDEIDEVFGLRMGADDYITKP 99
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
34-123 1.01e-12

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: 63.94  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  34 ARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAreeFQDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGE 113
Cdd:cd17622    30 EHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRP---KYQGPILLLTALDSDIDHILGLELGADDYVVKPVEPAV 106
                          90
                  ....*....|
gi 2017541161 114 LVARVRVQLK 123
Cdd:cd17622   107 LLARLRALLR 116
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
5-122 1.49e-12

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


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 63.07  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQ----EVSLFDSYleaRDGLEGFKTLlnnRVDLVLCDLEMPRMDGFRFLAMMRAreeFQDLP 80
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEkwgyEVVLIEDF---EDVLEEFLQF---KPDLVLLDINLPYFDGFYWCREIRQ---ISNVP 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2017541161  81 VIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQL 122
Cdd:cd18159    72 IIFISSRDDNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
5-108 1.74e-12

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 62.80  E-value: 1.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEVSLfdSYLEARDGLEGFKTL--LNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPVI 82
Cdd:cd17582     1 VLLVENDDSTRQIVTALLRKCSY--EVTAASDGLQAWDVLedEQNEIDLILTEVDLPVSSGFKLLSYIMRHKICKNIPVI 78
                          90       100
                  ....*....|....*....|....*.
gi 2017541161  83 ILTGREDRDTKIRGLEQGASDYVTKP 108
Cdd:cd17582    79 MMSSQDSVGVVFKCLSKGAADYLVKP 104
PRK09966 PRK09966
diguanylate cyclase DgcN;
123-295 1.81e-12

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 67.34  E-value: 1.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 123 KMKSLQDELKRSNEMLRTLSITDPLTHLHNRRHLMEMVEREFQRASRKGAHlSLVILDIDYFKKINDTYGHQEGDRVLT- 201
Cdd:PRK09966  229 EMEEWQLRLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRVLIe 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 202 ---ILAEIVTRRLRSYdlaaRYGGEEFVLLLPET-------PIHEALSIAERLRLEVQehvfDGSLqgLVLTISLGVA-T 270
Cdd:PRK09966  308 iakRLAEFGGLRHKAY----RLGGDEFAMVLYDVqsesevqQICSALTQIFNLPFDLH----NGHQ--TTMTLSIGYAmT 377
                         170       180
                  ....*....|....*....|....*
gi 2017541161 271 YPSSRVESIDSLfrqADEALYRAKQ 295
Cdd:PRK09966  378 IEHASAEKLQEL---ADHNMYQAKH 399
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
3-119 2.05e-12

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: 63.07  E-value: 2.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   3 TTVLVIDDSDTLRGEIFRTLQEvSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLammraREEFQDLP-- 80
Cdd:cd17542     1 KKVLIVDDAAFMRMMLKDILTK-AGYEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEAL-----KEIKKIDPna 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2017541161  81 -VIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:cd17542    75 kVIMCSAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVE 114
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
5-169 2.82e-12

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 67.20  E-value: 2.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEVSLFDSYLEarDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFqdLPVIIL 84
Cdd:PRK10923    6 VWVVDDDSSIRWVLERALAGAGLTCTTFE--NGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPM--LPVIIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  85 TGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLKMkslqdelKRSNEMLRTLSITDPLTHLHNRRHLMEMVEREF 164
Cdd:PRK10923   82 TAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISH-------YQEQQQPRNIQVNGPTTDIIGEAPAMQDVFRII 154

                  ....*
gi 2017541161 165 QRASR 169
Cdd:PRK10923  155 GRLSR 159
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
50-131 3.26e-12

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 65.09  E-value: 3.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  50 DLVLCDLEMPRMDGfrfLAMMRAREEFQDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLKMKSLQD 129
Cdd:PRK10710   56 DLILLDLMLPGTDG---LTLCREIRRFSDIPIVMVTAKIEEIDRLLGLEIGADDYICKPYSPREVVARVKTILRRCKPQR 132

                  ..
gi 2017541161 130 EL 131
Cdd:PRK10710  133 EL 134
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
5-118 4.51e-12

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: 61.68  E-value: 4.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEvslFDSYLEARDGLEGFKTLLNNR-VDLVLCDLEMPRMDGFRFLAmmRAREEFQDLPVII 83
Cdd:cd17573     1 ILLIEDDSTLGKEISKGLNE---KGYQADVAESLKDGEYYIDIRnYDLVLVSDKLPDGNGLSIVS--RIKEKHPSIVVIV 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2017541161  84 LTGREDRDTKIRGLEQGASDYVTKPFDAGELVARV 118
Cdd:cd17573    76 LSDNPKTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
34-123 6.51e-12

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 64.18  E-value: 6.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  34 ARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREefQDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGE 113
Cdd:PRK09836   30 ADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSAN--KGMPILLLTALGTIEHRVKGLELGADDYLVKPFAFAE 107
                          90
                  ....*....|
gi 2017541161 114 LVARVRVQLK 123
Cdd:PRK09836  108 LLARVRTLLR 117
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
5-108 8.87e-12

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: 60.67  E-value: 8.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQ----EVSLfdsyleARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAReefQDLP 80
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRkegfEVTV------ATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRAR---SNVP 71
                          90       100
                  ....*....|....*....|....*...
gi 2017541161  81 VIILTGREDRDTKIRGLEQGASDYVTKP 108
Cdd:cd17621    72 VIMVTAKDSEIDKVVGLELGADDYVTKP 99
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
5-123 1.55e-11

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: 60.63  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRareEFQDLPVIIL 84
Cdd:cd17532     1 ALIVDDEPLAREELRYLLEEHPDIEIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLS---KLAKPPLIVF 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2017541161  85 TGREDrDTKIRGLEQGASDYVTKPFDA---GELVARVRVQLK 123
Cdd:cd17532    78 VTAYD-EYAVEAFELNAVDYLLKPFSEerlAEALAKLRKRLS 118
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
4-119 2.10e-11

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


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 61.86  E-value: 2.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRGEIFRTLQ----EVSLFDSYLEARDGLEgfktllNNRVDLVLCDLEMPRMDGFRFLAMMRAREEfqDL 79
Cdd:COG4567     6 SLLLVDDDEAFARVLARALErrgfEVTTAASVEEALALLE------QAPPDYAVLDLRLGDGSGLDLIEALRERDP--DA 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2017541161  80 PVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:COG4567    78 RIVVLTGYASIATAVEAIKLGADDYLAKPADADDLLAALE 117
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
3-119 5.00e-11

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 59.14  E-value: 5.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   3 TTVLVIDDSDTLR---GEIFRTLQ-EVSLFDSyleARDGLEGFKTLLNNrvdLVLCDLEMPRMDGFRFLAMMRAREEfqD 78
Cdd:cd17537     1 ATVYVVDDDEAVRdslAFLLRSVGlAVKTFTS---ASAFLAAAPPDQPG---CLVLDVRMPGMSGLELQDELLARGS--N 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2017541161  79 LPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:cd17537    73 IPIIFITGHGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIE 113
PRK10336 PRK10336
two-component system response regulator QseB;
36-166 5.37e-11

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 61.45  E-value: 5.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  36 DGLEGFKTLLNNRVDLVLCDLEMPRMDGfrfLAMMRA-REEFQDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGEL 114
Cdd:PRK10336   32 QGRQGKEALYSAPYDAVILDLTLPGMDG---RDILREwREKGQREPVLILTARDALAERVEGLRLGADDYLCKPFALIEV 108
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2017541161 115 VARVRVQLKMKSLQ--DELKRSNEMLRTLSIT-----DPLTHLHNRRHLMEMVEREFQR 166
Cdd:PRK10336  109 AARLEALMRRTNGQasNELRHGNVMLDPGKRIatlagEPLTLKPKEFALLELLMRNAGR 167
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
3-119 9.09e-11

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: 58.57  E-value: 9.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   3 TTVLVIDDSDTLRGEIFRTLQEVSLFDSYLEArDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPVI 82
Cdd:cd17575     1 IMVLLVDDQAIIGEAVRRALADEEDIDFHYCS-DPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPII 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2017541161  83 ILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:cd17575    80 VLSTKEEPEVKSEAFALGANDYLVKLPDKIELVARIR 116
PRK10816 PRK10816
two-component system response regulator PhoP;
5-126 1.80e-10

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 59.75  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEVS-LFDSyleARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEfqDLPVII 83
Cdd:PRK10816    3 VLVVEDNALLRHHLKVQLQDAGhQVDA---AEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDV--SLPILV 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2017541161  84 LTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLKMKS 126
Cdd:PRK10816   78 LTARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALMRRNS 120
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
3-117 6.34e-10

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 56.10  E-value: 6.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   3 TTVLVIDDsDTLRGEIFRTLQE-VSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAReeFQDLPV 81
Cdd:cd19925     1 INVLIVED-DPMVAEIHRAYVEqVPGFTVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAA--GHDVDV 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2017541161  82 IILTGREDRDTKIRGLEQGASDYVTKPFDAGELVAR 117
Cdd:cd19925    78 IVVTAANDVETVREALRLGVVDYLIKPFTFERLRQR 113
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
5-109 7.35e-10

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: 55.69  E-value: 7.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLrgeifrtlqeVSLFDSYLE----------ARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRARE 74
Cdd:cd17561     4 VLIADDNREF----------VQLLEEYLNsqpdmevvgvAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMR 73
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2017541161  75 EFQDLPVIILT--GREDRdTKiRGLEQGASDYVTKPF 109
Cdd:cd17561    74 LEKRPKIIMLTafGQEDI-TQ-RAVELGASYYILKPF 108
fixJ PRK09390
response regulator FixJ; Provisional
4-123 1.26e-09

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 56.93  E-value: 1.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRGEIFRTLQ----EVSLFDSyleARDGLEGFKTLLNNrvdLVLCDLEMPRMDGFRFLAMMRAREefQDL 79
Cdd:PRK09390    5 VVHVVDDDEAMRDSLAFLLDsagfEVRLFES---AQAFLDALPGLRFG---CVVTDVRMPGIDGIELLRRLKARG--SPL 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2017541161  80 PVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLK 123
Cdd:PRK09390   77 PVIVMTGHGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIERALA 120
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
34-114 1.62e-09

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


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 54.72  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  34 ARDGLEGFKTLLNNRVDLVLCDLEMP-RMDGFRflAMMRAREEFqDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAG 112
Cdd:cd17534    31 ADSGEEAIELAEENKPDLILMDINLKgDMDGIE--AAREIREKF-DIPVIFLTAYSDEETLERAKETNPYGYLVKPFNER 107

                  ..
gi 2017541161 113 EL 114
Cdd:cd17534   108 EL 109
PRK10693 PRK10693
two-component system response regulator RssB;
33-108 2.74e-09

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 57.31  E-value: 2.74e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2017541161  33 EARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEfqDLPVIILTGREDRDTKIRGLEQGASDYVTKP 108
Cdd:PRK10693    2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGD--QTPVLVISATENMADIAKALRLGVQDVLLKP 75
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
5-108 3.60e-09

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 53.91  E-value: 3.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQ----EVSLFDSYLEA-----RDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREE 75
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLRisscRVTAVDSGKRAleflgLEDEEDSSNFNEPKVNMIITDYCMPGMTGYDLLKKVKESSA 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2017541161  76 FQDLPVIILTGrEDRDTKI-RGLEQGASDYVTKP 108
Cdd:cd17581    81 LKEIPVVIMSS-ENIPTRIsRCLEEGAEDFLLKP 113
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
5-120 4.12e-09

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 53.57  E-value: 4.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIfRTLQEVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEfqdLPVIIL 84
Cdd:cd19932     3 VLIAEDEALIRMDL-REMLEEAGYEVVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENI---APIVLL 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2017541161  85 TGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRV 120
Cdd:cd19932    79 TAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEM 114
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
4-67 5.27e-09

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: 53.60  E-value: 5.27e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017541161   4 TVLVIDDSDTLRgEIFRTLQEVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFL 67
Cdd:cd17530     2 RVLVLDDDPFQC-MMAATILEDLGPGNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFL 64
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
4-108 9.33e-09

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 56.52  E-value: 9.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSdtlrgEIFRTL---QEVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFlaMMRAREEFQDLP 80
Cdd:PRK10841  803 MILVVDDH-----PINRRLladQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRL--TQRLRQLGLTLP 875
                          90       100
                  ....*....|....*....|....*...
gi 2017541161  81 VIILTGREDRDTKIRGLEQGASDYVTKP 108
Cdd:PRK10841  876 VIGVTANALAEEKQRCLEAGMDSCLSKP 903
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
5-122 1.92e-08

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 51.79  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRgeifRTLQEVSLFDSY--LEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREefQDLPVI 82
Cdd:cd17553     3 ILIVDDQYGIR----ILLNEVFNKEGYqtFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVID--ENIRVI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2017541161  83 ILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQL 122
Cdd:cd17553    77 IMTAYGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
5-110 1.96e-08

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 55.42  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDsDTLRGEIFRTLQEVSLFDSYLeARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEfqDLPVIIL 84
Cdd:PRK10365    8 ILVVDD-DISHCTILQALLRGWGYNVAL-ANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNP--AIPVLIM 83
                          90       100
                  ....*....|....*....|....*.
gi 2017541161  85 TGREDRDTKIRGLEQGASDYVTKPFD 110
Cdd:PRK10365   84 TAYSSVETAVEALKTGALDYLIKPLD 109
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
2-88 5.97e-08

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: 50.66  E-value: 5.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   2 TTTVLVIDDSDTLRGEIFRTLQEVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAmmrareefqdlpv 81
Cdd:COG2197     1 MIRVLIVDDHPLVREGLRALLEAEPDIEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALR------------- 67

                  ....*..
gi 2017541161  82 IILTGRE 88
Cdd:COG2197    68 RLLTPRE 74
PRK15115 PRK15115
response regulator GlrR; Provisional
34-141 7.50e-08

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 53.30  E-value: 7.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  34 ARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEfqDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGE 113
Cdd:PRK15115   35 AESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQP--GMPVIILTAHGSIPDAVAATQQGVFSFLTKPVDRDA 112
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2017541161 114 LVARVRVQLKMKS-LQDE------LKRSNEMLRTL 141
Cdd:PRK15115  113 LYKAIDDALEQSApATDErwreaiVTRSPLMLRLL 147
PRK15347 PRK15347
two component system sensor kinase;
5-147 8.67e-08

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 53.49  E-value: 8.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTL----QEVSLfdsyleARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQD-- 78
Cdd:PRK15347  693 ILLVDDVETNRDIIGMMLvelgQQVTT------AASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNLDpd 766
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017541161  79 LPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLKMkslqdELKRSNEMLRTLSITDPL 147
Cdd:PRK15347  767 CMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARALELAAEY-----QLLRGIELSPQDSSCSPL 830
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
4-86 8.91e-08

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


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 49.42  E-value: 8.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRGEIFRTLQEvslfDSYL--EARDGLEGFKTLLNNR-VDLVLCDLEMPRMDGFRFLamMRAREEFQDLP 80
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKK----AGYAvtEAESGAEALEKLQQGKdIDIVVTDIVMPEMDGIELA--REARKIDPDVK 74

                  ....*.
gi 2017541161  81 VIILTG 86
Cdd:cd18160    75 ILFISG 80
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
5-119 1.48e-07

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 52.19  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRgEIfrtLQEVSLFDSYLE----ARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFL-AMMRAREefqdL 79
Cdd:PRK12555    3 IGIVNDSPLAV-EA---LRRALARDPDHEvvwvATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATrRIMAERP----C 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2017541161  80 PVIILTGREDRDTKI--RGLEQGASDYVTKPF---------DAGELVARVR 119
Cdd:PRK12555   75 PILIVTSLTERNASRvfEAMGAGALDAVDTPTlgigagleeYAAELLAKID 125
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
5-119 2.24e-07

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 48.88  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREefQDLPVIIL 84
Cdd:cd19931     1 VLLIDDHPLLRKGIKQLIELDPDFTVVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEG--VSARIVIL 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2017541161  85 TGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:cd19931    79 TVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALK 113
PRK15369 PRK15369
two component system response regulator;
1-145 2.67e-07

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 50.46  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   1 MTTTVLVIDDSDTLRGEIFRTLQEVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAReeFQDLP 80
Cdd:PRK15369    2 KNYKILLVDDHELIINGIKNMLAPYPRYKIVGQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQR--WPAMN 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017541161  81 VIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLKMKSLQDELKRSNEMLRTLSITD 145
Cdd:PRK15369   80 ILVLTARQEEHMASRTLAAGALGYVLKKSPQQILLAAIQTVAVGKRYIDPALNREAILALLNADD 144
PRK11697 PRK11697
two-component system response regulator BtsR;
4-173 2.69e-07

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 50.62  E-value: 2.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRGEIFRTLQEVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMrareEFQDLPVII 83
Cdd:PRK11697    3 KVLIVDDEPLAREELRELLQEEGDIEIVGECSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELVGML----DPEHMPYIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  84 LTGREDrDTKIRGLEQGASDYVTKPFDAGEL---VARVRVQLKMKSLQdelkrsnemlrTLSITDPLTHL----HNRRHL 156
Cdd:PRK11697   79 FVTAFD-EYAIKAFEEHAFDYLLKPIDPARLaktLARLRQERSPQDVL-----------LPEAQPPLKHIpctgHNRIKL 146
                         170
                  ....*....|....*..
gi 2017541161 157 MEMVEREFQRASRKGAH 173
Cdd:PRK11697  147 LPLEEVEFVSSRLSGVH 163
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
4-119 4.36e-07

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 50.03  E-value: 4.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRGEIFRTLQEVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREefQDLPVII 83
Cdd:PRK10651    8 TILLIDDHPMLRTGVKQLISMAPDITVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKS--LSGRIVV 85
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2017541161  84 LTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:PRK10651   86 FSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQ 121
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
5-119 5.39e-07

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 47.65  E-value: 5.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGfrFLAMMRAREEFQDLPVIIL 84
Cdd:cd19930     1 VLIAEDQEMVRGALAALLELEDDLEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTG--LEVAAELREELPDTKVLIV 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2017541161  85 TGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:cd19930    79 TTFGRPGYFRRALAAGVDGYVLKDRPIEELADAIR 113
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
128-311 6.34e-07

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 50.71  E-value: 6.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 128 QDELKRSNEMLRTLSITDPLTHLHNRRHLMEMVEREFQRASRKgAHLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIV 207
Cdd:PRK11829  218 QQLLADAYADMGRISHRFPVTELPNRSLFISLLEKEIASSTRT-DHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRI 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 208 TRRLRSYDLAARYGGEEFVLLLPETP-IHEALSIAERLRLEVQEHVFDGSLqGLVLTISLGVATYPSSRvESIDSLFRQA 286
Cdd:PRK11829  297 EQCIDDSDLLAQLSKTEFAVLARGTRrSFPAMQLARRIMSQVTQPLFFDEI-TLRPSASIGITRYQAQQ-DTAESMMRNA 374
                         170       180
                  ....*....|....*....|....*
gi 2017541161 287 DEALYRAKQGGRNRVELMAGANAER 311
Cdd:PRK11829  375 STAMMAAHHEGRNQIMVFEPHLIEK 399
PRK09483 PRK09483
response regulator; Provisional
4-119 1.33e-06

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 48.56  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRGEIFRTLQEVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGfrfLAMMRAREEFQ-DLPVI 82
Cdd:PRK09483    3 NVLLVDDHELVRAGIRRILEDIKGIKVVGEACCGEDAVKWCRTNAVDVVLMDMNMPGIGG---LEATRKILRYTpDVKII 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2017541161  83 ILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:PRK09483   80 MLTVHTENPLPAKVMQAGAAGYLSKGAAPQEVVSAIR 116
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
4-116 1.45e-06

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: 46.28  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRGEIFRTLQ----EVSLFDSYLEArdglegFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAReeFQDL 79
Cdd:cd17563     2 SLLLVDDDEVFAERLARALErrgfEVETAHSVEEA------LALAREEKPDYAVLDLRLGGDSGLDLIPPLRAL--QPDA 73
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2017541161  80 PVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVA 116
Cdd:cd17563    74 RIVVLTGYASIATAVEAIKLGADDYLAKPADADEILA 110
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
4-59 1.67e-06

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 44.48  E-value: 1.67e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2017541161    4 TVLVIDDSDTLRGEIFRTLQevSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMP 59
Cdd:smart00448   2 RILVVDDDPLLRELLKALLE--KEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
3-122 2.40e-06

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 47.56  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   3 TTVLVIDDSDTLRGEIFRTLQEVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEfqDLPVI 82
Cdd:PRK09935    4 ASVIIMDTHPIIRMSIEVLLQKNSELQIVLKTDDYRITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQS--TVKVL 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2017541161  83 ILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQL 122
Cdd:PRK09935   82 FLSSKSECFYAGRAIQAGANGFVSKCNDQNDIFHAVQMIL 121
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
1-123 5.12e-06

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 46.94  E-value: 5.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   1 MTTTVLVIDDSDTlrGEIFRTLQEVSLFDSYLEARdGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAReeFQDlP 80
Cdd:PRK10701    1 MNKIVFVEDDAEV--GSLIAAYLAKHDIDVTVEPR-GDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPK--WQG-P 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2017541161  81 VIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLK 123
Cdd:PRK10701   75 IVLLTSLDSDMNHILALEMGACDYILKTTPPAVLLARLRLHLR 117
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
128-312 5.54e-06

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 47.79  E-value: 5.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 128 QDELKRSNEMLRTLSITDPLTHLHNRRHLMEMVErefQRASRKGAhLSLVILDIDYFKKINDTYGHQEGDRVLTILAEIV 207
Cdd:PRK13561  217 QQLLQRQYEEQSRNATRFPVSDLPNKALLMALLE---QVVARKQT-TALMIITCETLRDTAGVLKEAQREILLLTLVEKL 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 208 TRRLRSYDLAARYGGEEFVLLLP--ETPIHeALSIAERLRLEVQEHVfdgSLQGLVLT--ISLGVATYPSSrvESIDSLF 283
Cdd:PRK13561  293 KSVLSPRMVLAQISGYDFAIIANgvKEPWH-AITLGQQVLTIINERL---PIQRIQLRpsCSIGIAMFYGD--LTAEQLY 366
                         170       180
                  ....*....|....*....|....*....
gi 2017541161 284 RQADEALYRAKQGGRNRVELMAGANAERS 312
Cdd:PRK13561  367 SRAISAAFTARRKGKNQIQFFDPQQMEAA 395
PLN03029 PLN03029
type-a response regulator protein; Provisional
49-143 7.87e-06

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 46.18  E-value: 7.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  49 VDLVLCDLEMPRMDGFRFLAMMRAREEFQDLPVIILTGrEDRDTKI-RGLEQGASDYVTKPFDAGELvARVR---VQLKM 124
Cdd:PLN03029   73 VNLIITDYCMPGMTGYDLLKKIKESSSLRNIPVVIMSS-ENVPSRItRCLEEGAEEFFLKPVQLSDL-NRLKphmMKTKS 150
                          90
                  ....*....|....*....
gi 2017541161 125 KSLQDELKRSNEMLRTLSI 143
Cdd:PLN03029  151 KNQKQENQEKQEKLEESEI 169
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
50-108 9.37e-06

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


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 43.65  E-value: 9.37e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2017541161  50 DLVLCDLEMPRMDGFRFLAmmRAREEFQDLPVIILTGREDRDTKIRGLEQGASDYVTKP 108
Cdd:cd19928    44 DLVITDVVMPDENGLDLIP--RIKKARPDLPIIVMSAQNTLMTAVKAAERGAFEYLPKP 100
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
5-108 1.36e-05

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


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 43.54  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQ----EVSLFDSyleardGLEGFKTL--LNNRVDLVLCDLEMPRMDGFRFLAMMRAREEFQD 78
Cdd:cd19933     3 VLLVDDNAVNRMVTKGLLEklgcEVTTVSS------GEECLNLLasAEHSFQLVLLDLCMPEMDGFEVALRIRKLFGRRE 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2017541161  79 LPVII-LTGREDRDTKIRGLEQGASDYVTKP 108
Cdd:cd19933    77 RPLIVaLTANTDDSTREKCLSLGMNGVITKP 107
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
5-108 1.39e-05

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 43.30  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEVSLfdSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAReeFQDLPVIIL 84
Cdd:cd19926     1 VLVVDDEPDIRELLEITLGRMGL--DVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQR--LPQTPVAVI 76
                          90       100
                  ....*....|....*....|....
gi 2017541161  85 TGREDRDTKIRGLEQGASDYVTKP 108
Cdd:cd19926    77 TAYGSLDTAIEALKAGAFDFLTKP 100
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
5-109 1.69e-05

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 43.10  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRgeifRTLQEV--SLFDSYLEARDGLEGFKTLLNN-RVDLVLCDLEMPRMDGFRFLAmMRAREEFQDLPV 81
Cdd:cd18161     1 VLVVEDDPDVR----RLTAEVleDLGYTVLEAASGDEALDLLESGpDIDLLVTDVIMPGGMNGSQLA-EEARRRRPDLKV 75
                          90       100
                  ....*....|....*....|....*...
gi 2017541161  82 IILTGREDRDTKIRGLEQGAsDYVTKPF 109
Cdd:cd18161    76 LLTSGYAENAIEGGDLAPGV-DVLSKPF 102
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
6-113 3.03e-05

phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase output domain; This family is composed of uncharacterized fusion proteins containing a REC domain and a thioredoxin reductase domain. Thioredoxin reductase catalyzes the reduction of thioredoxin and is thus a central component in the thioredoxin system. Fusion proteins containing REC and thioredoxin reductase domains could play an important role in the environmental regulation of the cellular dithiol-disulfide ratio. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 43.09  E-value: 3.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   6 LVIDDSDTLR----------GEIFRTLQEvslfDSYLEARDGLEGFKtLLNNRVDLVLCDLEMPRMDGFRFLAmmRAREE 75
Cdd:cd17595     5 TVDDDPQVLRavardlrrqyGKDYRVLRA----DSGAEALDALKELK-LRGEAVALFLVDQRMPEMDGVEFLE--KAMEL 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2017541161  76 FQDLPVIILTGREDRDTKIRGLEQGASD-YVTKPFDAGE 113
Cdd:cd17595    78 FPEAKRVLLTAYADTDAAIRAINDVQLDyYLLKPWDPPE 116
PRK10430 PRK10430
two-component system response regulator DcuR;
5-112 3.04e-05

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 44.71  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDsDTLRGEIFRT-LQEVSLFDSYLEARDgLEGFKTLLNNR---VDLVLCDLEMPRMDGFRFLAMMRAREEFQDlp 80
Cdd:PRK10430    4 VLIVDD-DAMVAELNRRyVAQIPGFQCCGTAST-LEQAKEIIFNSdtpIDLILLDIYMQQENGLDLLPVLHEAGCKSD-- 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2017541161  81 VIILTGREDRDTKIRGLEQGASDYVTKPFDAG 112
Cdd:PRK10430   80 VIVISSAADAATIKDSLHYGVVDYLIKPFQAS 111
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
5-162 6.56e-05

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


Pssm-ID: 274348 [Multi-domain]  Cd Length: 445  Bit Score: 44.35  E-value: 6.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEVSLFdsylEARDGLEGFKTLLNNRVDLVLCDLEMP-----RMDGFRFLAMMRAREEfqDL 79
Cdd:TIGR02915   1 LLIVEDDLGLQKQLKWSFADYELA----VAADRESAIALVRRHEPAVVTLDLGLPpdadgASEGLAALQQILAIAP--DT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161  80 PVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQLKMKSLQDELKRSNEMLRTLSITDPLTHLHNRRHLMEM 159
Cdd:TIGR02915  75 KVIVITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTLETENRRLQSALGGTALRGLITSSPGMQKICRT 154

                  ...
gi 2017541161 160 VER 162
Cdd:TIGR02915 155 IEK 157
REC_1_GGDEF cd19921
first phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
5-107 7.00e-05

first 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 contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the first REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381148 [Multi-domain]  Cd Length: 115  Bit Score: 41.40  E-value: 7.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQ-----EVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDleMPRMDGFRFLAMmrareefQDL 79
Cdd:cd19921     2 VLIVEDSKTFSKVLKHLIAqelglEVDVAETLAEAKALLEEGDDYFAALVDLNLPD--APNGEAVDLVLE-------KGI 72
                          90       100
                  ....*....|....*....|....*...
gi 2017541161  80 PVIILTGREDRDTKIRGLEQGASDYVTK 107
Cdd:cd19921    73 PVIVLTGSFDEDKRETLLSKGVVDYVLK 100
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
4-109 7.28e-05

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 44.73  E-value: 7.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161    4 TVLVIDDSDTLRGEIFRTLQEVSlFDSYlEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFlaMMRAREEFQDLPVII 83
Cdd:PRK09959   960 SILIADDHPTNRLLLKRQLNLLG-YDVD-EATDGVQALHKVSMQHYDLLITDVNMPNMDGFEL--TRKLREQNSSLPIWG 1035
                           90       100
                   ....*....|....*....|....*.
gi 2017541161   84 LTGREDRDTKIRGLEQGASDYVTKPF 109
Cdd:PRK09959  1036 LTANAQANEREKGLSCGMNLCLFKPL 1061
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
4-118 2.39e-04

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 41.42  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDSDTLRGEIfRTLQEVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAReEFQDLpVII 83
Cdd:PRK09958    2 NAIIIDDHPLAIAAI-RNLLIKNDIEILAELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKR-QYSGI-III 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2017541161  84 LTGREDRDTKIRGLEQGASDYVTKPFDAGELVARV 118
Cdd:PRK09958   79 VSAKNDHFYGKHCADAGANGFVSKKEGMNNIIAAI 113
PRK10360 PRK10360
transcriptional regulator UhpA;
3-119 5.76e-04

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 40.35  E-value: 5.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   3 TTVLVIDDSDTLRGEIFRTL------QEVSLFDSYLEARDGLEGfktllnNRVDLVLCDLEMPRMDGFRFLAMMRareef 76
Cdd:PRK10360    2 ITVALIDDHLIVRSGFAQLLglepdlQVVAEFGSGREALAGLPG------RGVQVCICDISMPDISGLELLSQLP----- 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2017541161  77 QDLPVIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:PRK10360   71 KGMATIMLSVHDSPALVEQALNAGARGFLSKRCSPDELIAAVH 113
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
5-118 5.85e-04

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 38.78  E-value: 5.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEVSlFDSYLEARDGLEGFKTLLNNRVDLVLCDLEM-PRMDGFRFLAMMRareEFQDLP--- 80
Cdd:cd17589     1 FLIVDDQPTFRSMLKSMLRSLG-VTRIDTASSGEEALRMCENKTYDIVLCDYNLgKGKNGQQLLEELR---HKKLISpst 76
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2017541161  81 -VIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARV 118
Cdd:cd17589    77 vFIMVTGESSRAMVLSALELEPDDYLLKPFTVSELRERL 115
PRK13557 PRK13557
histidine kinase; Provisional
2-122 2.15e-03

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 39.65  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   2 TTTVLVIDDSDTLrGEIFRTLQE-----VSLFDSYLEARDGLEGfktllNNRVDLVLCDLEMP-RMDGfrflaMMRAREE 75
Cdd:PRK13557  415 TETILIVDDRPDV-AELARMILEdfgyrTLVASNGREALEILDS-----HPEVDLLFTDLIMPgGMNG-----VMLAREA 483
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2017541161  76 FQDLP---VIILTGREDRDTKIRGLEQGASDYVTKPFDAGELVARVRVQL 122
Cdd:PRK13557  484 RRRQPkikVLLTTGYAEASIERTDAGGSEFDILNKPYRRAELARRVRMVL 533
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
4-110 4.28e-03

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 38.68  E-value: 4.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   4 TVLVIDDS-------DTLRGEIfrtLQEVSLFDSyleardGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMRAREEF 76
Cdd:PRK11107  669 TVMAVDDNpanlkliGALLEEQ---VEHVVLCDS------GHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHN 739
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2017541161  77 QDLPVIILTG---REDRDtkiRGLEQGASDYVTKPFD 110
Cdd:PRK11107  740 QNTPIIAVTAhamAGERE---RLLSAGMDDYLAKPID 773
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
5-119 5.45e-03

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 37.52  E-value: 5.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161   5 VLVIDDSDTLRGEIFRTLQEVSLFDSYLEARDGLEGFKTLLNNRVDLVLCDLEMPRMDGFRFLAMMraREEFQDLPVIIL 84
Cdd:PRK10403    9 VLIVDDHPLMRRGVRQLLELDPGFEVVAEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNAL--RRDGVTAQIIIL 86
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2017541161  85 TGREDRDTKIRGLEQGASDYVTKPFDAGELVARVR 119
Cdd:PRK10403   87 TVSDASSDVFALIDAGADGYLLKDSDPEVLLEAIR 121
PRK11059 PRK11059
regulatory protein CsrD; Provisional
110-244 7.20e-03

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 37.92  E-value: 7.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541161 110 DAGElvARVRVqlkmkslqDELKRSNEMLrtlsitDPLTHLHNRRHLMEMVEREFQRASRKGAHLSLVILDIDYFKKIND 189
Cdd:PRK11059  212 DARE--ERSRF--------DTFIRSNAFQ------DAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQE 275
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2017541161 190 TYGHQEGDRVLTILAEIVTRRLRSYD--LAARYGGEEFVLLLPETPIHEALSIAERL 244
Cdd:PRK11059  276 EWGESQVEELLFELINLLSTFVMRYPgaLLARYSRSDFAVLLPHRSLKEADSLASQL 332
 
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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