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Conserved domains on  [gi|499657480|ref|WP_011338214|]
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diguanylate cyclase [Cereibacter sphaeroides]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
pleD super family cl35865
response regulator PleD; Reviewed
1-453 9.58e-100

response regulator PleD; Reviewed


The actual alignment was detected with superfamily member PRK09581:

Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 306.44  E-value: 9.58e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   1 MGGKVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVI 80
Cdd:PRK09581   1 MTARILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  81 MISASRDPAIRLQALAEGADDFLAKPLDDPVLMARLRSLLRLRDSSGEGAVRGAALRALGLAER-----AESFEGpGLIA 155
Cdd:PRK09581  81 MVTALDDPEDRVRGLEAGADDFLTKPINDVALFARVKSLTRLKMVIDELRLRASTNAEIGVTALmimayANKDED-GRIL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 156 LVAARPETGLRWRKELQALMPDRIVLQTREEALAEAGPVPDIFVIDADLDGPGGgLRLMSDLRSRAGSRHAAVCIVRGQM 235
Cdd:PRK09581 160 LVDDDVSQAERIANILKEEFRVVVVSDPSEALFNAAETNYDLVIVSANFENYDP-LRLCSQLRSKERTRYVPILLLVDED 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 236 GGEGAAMIYDLGANDLLPAAFDPREARLRLRNLLRRKRRGDEMRATLQNGLRLAVVDPLTGLYNRRYAGAHLAAVAERAR 315
Cdd:PRK09581 239 DDPRLVKALELGVNDYLMRPIDKNELLARVRTQIRRKRYQDALRNNLEQSIEMAVTDGLTGLHNRRYFDMHLKNLIERAN 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 316 AADERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHANLRPGDLIARIGGEEFLVALPDVPrPEDAHAVAERLREA 395
Cdd:PRK09581 319 ERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTD-IEDAIAVAERIRRK 397
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499657480 396 VEEEPVPLPGGGS-LRVTISVGLAlspdEAGRRAEPVDAVVQRADSALLLAKSAGRNQV 453
Cdd:PRK09581 398 IAEEPFIISDGKErLNVTVSIGVA----ELRPSGDTIEALIKRADKALYEAKNTGRNRV 452
 
Name Accession Description Interval E-value
pleD PRK09581
response regulator PleD; Reviewed
1-453 9.58e-100

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 306.44  E-value: 9.58e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   1 MGGKVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVI 80
Cdd:PRK09581   1 MTARILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  81 MISASRDPAIRLQALAEGADDFLAKPLDDPVLMARLRSLLRLRDSSGEGAVRGAALRALGLAER-----AESFEGpGLIA 155
Cdd:PRK09581  81 MVTALDDPEDRVRGLEAGADDFLTKPINDVALFARVKSLTRLKMVIDELRLRASTNAEIGVTALmimayANKDED-GRIL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 156 LVAARPETGLRWRKELQALMPDRIVLQTREEALAEAGPVPDIFVIDADLDGPGGgLRLMSDLRSRAGSRHAAVCIVRGQM 235
Cdd:PRK09581 160 LVDDDVSQAERIANILKEEFRVVVVSDPSEALFNAAETNYDLVIVSANFENYDP-LRLCSQLRSKERTRYVPILLLVDED 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 236 GGEGAAMIYDLGANDLLPAAFDPREARLRLRNLLRRKRRGDEMRATLQNGLRLAVVDPLTGLYNRRYAGAHLAAVAERAR 315
Cdd:PRK09581 239 DDPRLVKALELGVNDYLMRPIDKNELLARVRTQIRRKRYQDALRNNLEQSIEMAVTDGLTGLHNRRYFDMHLKNLIERAN 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 316 AADERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHANLRPGDLIARIGGEEFLVALPDVPrPEDAHAVAERLREA 395
Cdd:PRK09581 319 ERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTD-IEDAIAVAERIRRK 397
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499657480 396 VEEEPVPLPGGGS-LRVTISVGLAlspdEAGRRAEPVDAVVQRADSALLLAKSAGRNQV 453
Cdd:PRK09581 398 IAEEPFIISDGKErLNVTVSIGVA----ELRPSGDTIEALIKRADKALYEAKNTGRNRV 452
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
292-453 2.74e-57

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: 186.22  E-value: 2.74e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 292 DPLTGLYNRRYAGAHLAAVAERARAADERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHANLRPGDLIARIGGEE 371
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 372 FLVALPDVPrPEDAHAVAERLREAVEEEpvPLPGGGSLRVTISVGLALSPDEagrrAEPVDAVVQRADSALLLAKSAGRN 451
Cdd:cd01949   83 FAILLPGTD-LEEAEALAERLREAIEEP--FFIDGQEIRVTASIGIATYPED----GEDAEELLRRADEALYRAKRSGRN 155

                 ..
gi 499657480 452 QV 453
Cdd:cd01949  156 RV 157
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
177-455 1.27e-55

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: 186.34  E-value: 1.27e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 177 DRIVLQTREEALAEAGPVPDIFVIDADLDGPGGGLRLMSDLRSRAGSRHAAVCIVRGQMGGEGAAMIYDLGANDLLPAAF 256
Cdd:COG2199    2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 257 DPREARLRLRNLLRRKRRGDEMRATLQNGLRLAVVDPLTGLYNRRYAGAHLAAVAERARAADERFAVMVIDLDRFKSVND 336
Cdd:COG2199   82 ELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIND 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 337 RWGHGAGDAVLVAVARRLHANLRPGDLIARIGGEEFLVALPDVPrPEDAHAVAERLREAVEEEPVPLpGGGSLRVTISVG 416
Cdd:COG2199  162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTD-LEEAEALAERLREALEQLPFEL-EGKELRVTVSIG 239
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 499657480 417 LALSPDEagrrAEPVDAVVQRADSALLLAKSAGRNQVTI 455
Cdd:COG2199  240 VALYPED----GDSAEELLRRADLALYRAKRAGRNRVVV 274
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
289-452 2.25e-51

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: 170.90  E-value: 2.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  289 AVVDPLTGLYNRRYAGAHLAAVAERARAADERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHANLRPGDLIARIG 368
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  369 GEEFLVALPDVPRpEDAHAVAERLREAVEEEPVPLPGGG-SLRVTISVGLALSPDEagrrAEPVDAVVQRADSALLLAKS 447
Cdd:pfam00990  81 GDEFAILLPETSL-EGAQELAERIRRLLAKLKIPHTVSGlPLYVTISIGIAAYPND----GEDPEDLLKRADTALYQAKQ 155

                  ....*
gi 499657480  448 AGRNQ 452
Cdd:pfam00990 156 AGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
287-453 1.43e-49

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 166.27  E-value: 1.43e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   287 RLAVVDPLTGLYNRRYAGAHLAAVAERARAADERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHANLRPGDLIAR 366
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   367 IGGEEFLVALPDVPrPEDAHAVAERLREAVEEEpvPLPGGGSLRVTISVGLALSPDEagrrAEPVDAVVQRADSALLLAK 446
Cdd:smart00267  81 LGGDEFALLLPETS-LEEAIALAERILQQLREP--IIIHGIPLYLTISIGVAAYPNP----GEDAEDLLKRADTALYQAK 153

                   ....*..
gi 499657480   447 SAGRNQV 453
Cdd:smart00267 154 KAGRNQV 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
288-453 3.16e-46

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: 157.88  E-value: 3.16e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  288 LAVVDPLTGLYNRRYAGAHLAAVAERARAADERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHANLRPGDLIARI 367
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  368 GGEEFLVALPDVPRpEDAHAVAERLREAVEEEPVPLPGGGSLRVTISVGLALSPDEagrrAEPVDAVVQRADSALLLAKS 447
Cdd:TIGR00254  81 GGEEFVVILPGTPL-EDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPGH----GLTLEELLKRADEALYQAKK 155

                  ....*.
gi 499657480  448 AGRNQV 453
Cdd:TIGR00254 156 AGRNRV 161
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
292-453 7.50e-41

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 146.28  E-value: 7.50e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 292 DPLTGLYNRRYAGAHLAAVAERARAADERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHANLRPGDLIARIGGEE 371
Cdd:NF038266  97 DPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGEE 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 372 FLVALPDVPrPEDAHAVAERLREAVEEEPVPlPGGGSLRVTISVGLA-LSPDEagrraEPVDAVVQRADSALLLAKSAGR 450
Cdd:NF038266 177 FLLLLPETG-LEEAQVVLERLREAVRALAVR-VGDDVLSVTASAGLAeHRPPE-----EGLSATLSRADQALYQAKRAGR 249

                 ...
gi 499657480 451 NQV 453
Cdd:NF038266 250 DRV 252
 
Name Accession Description Interval E-value
pleD PRK09581
response regulator PleD; Reviewed
1-453 9.58e-100

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 306.44  E-value: 9.58e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   1 MGGKVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVI 80
Cdd:PRK09581   1 MTARILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  81 MISASRDPAIRLQALAEGADDFLAKPLDDPVLMARLRSLLRLRDSSGEGAVRGAALRALGLAER-----AESFEGpGLIA 155
Cdd:PRK09581  81 MVTALDDPEDRVRGLEAGADDFLTKPINDVALFARVKSLTRLKMVIDELRLRASTNAEIGVTALmimayANKDED-GRIL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 156 LVAARPETGLRWRKELQALMPDRIVLQTREEALAEAGPVPDIFVIDADLDGPGGgLRLMSDLRSRAGSRHAAVCIVRGQM 235
Cdd:PRK09581 160 LVDDDVSQAERIANILKEEFRVVVVSDPSEALFNAAETNYDLVIVSANFENYDP-LRLCSQLRSKERTRYVPILLLVDED 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 236 GGEGAAMIYDLGANDLLPAAFDPREARLRLRNLLRRKRRGDEMRATLQNGLRLAVVDPLTGLYNRRYAGAHLAAVAERAR 315
Cdd:PRK09581 239 DDPRLVKALELGVNDYLMRPIDKNELLARVRTQIRRKRYQDALRNNLEQSIEMAVTDGLTGLHNRRYFDMHLKNLIERAN 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 316 AADERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHANLRPGDLIARIGGEEFLVALPDVPrPEDAHAVAERLREA 395
Cdd:PRK09581 319 ERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTD-IEDAIAVAERIRRK 397
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499657480 396 VEEEPVPLPGGGS-LRVTISVGLAlspdEAGRRAEPVDAVVQRADSALLLAKSAGRNQV 453
Cdd:PRK09581 398 IAEEPFIISDGKErLNVTVSIGVA----ELRPSGDTIEALIKRADKALYEAKNTGRNRV 452
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
292-453 2.74e-57

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: 186.22  E-value: 2.74e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 292 DPLTGLYNRRYAGAHLAAVAERARAADERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHANLRPGDLIARIGGEE 371
Cdd:cd01949    3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 372 FLVALPDVPrPEDAHAVAERLREAVEEEpvPLPGGGSLRVTISVGLALSPDEagrrAEPVDAVVQRADSALLLAKSAGRN 451
Cdd:cd01949   83 FAILLPGTD-LEEAEALAERLREAIEEP--FFIDGQEIRVTASIGIATYPED----GEDAEELLRRADEALYRAKRSGRN 155

                 ..
gi 499657480 452 QV 453
Cdd:cd01949  156 RV 157
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
177-455 1.27e-55

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: 186.34  E-value: 1.27e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 177 DRIVLQTREEALAEAGPVPDIFVIDADLDGPGGGLRLMSDLRSRAGSRHAAVCIVRGQMGGEGAAMIYDLGANDLLPAAF 256
Cdd:COG2199    2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 257 DPREARLRLRNLLRRKRRGDEMRATLQNGLRLAVVDPLTGLYNRRYAGAHLAAVAERARAADERFAVMVIDLDRFKSVND 336
Cdd:COG2199   82 ELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIND 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 337 RWGHGAGDAVLVAVARRLHANLRPGDLIARIGGEEFLVALPDVPrPEDAHAVAERLREAVEEEPVPLpGGGSLRVTISVG 416
Cdd:COG2199  162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTD-LEEAEALAERLREALEQLPFEL-EGKELRVTVSIG 239
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 499657480 417 LALSPDEagrrAEPVDAVVQRADSALLLAKSAGRNQVTI 455
Cdd:COG2199  240 VALYPED----GDSAEELLRRADLALYRAKRAGRNRVVV 274
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
39-453 1.14e-52

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: 188.06  E-value: 1.14e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  39 LSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMISASRDPAIRLQALAEGADDFLAKPLDDPVLMARLRS 118
Cdd:COG5001    1 LLALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 119 LLRLRDSSGEGAVRGAALRALGLAERAESFEGPGLIALVAARPETGLRWRKELQALMPDRIVLQTREEALAEAGPVPDIF 198
Cdd:COG5001   81 LLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 199 VIDADLDGPGGGLRLMSDLRSRAGSRHAAVCIVRGQMGGEGAAMIYDLGANDLLPAAFDPREARLRLRNLLRRKRRGDEM 278
Cdd:COG5001  161 LLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITER 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 279 RATLQNGLRLAVVDPLTGLYNRRYAGAHLAAVAERARAADERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHANL 358
Cdd:COG5001  241 KRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 359 RPGDLIARIGGEEFLVALPDVPRPEDAHAVAERLREAVeEEPVPLpGGGSLRVTISVGLALSPDEAGRraepVDAVVQRA 438
Cdd:COG5001  321 REGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAAL-AEPFEL-DGHELYVSASIGIALYPDDGAD----AEELLRNA 394
                        410
                 ....*....|....*
gi 499657480 439 DSALLLAKSAGRNQV 453
Cdd:COG5001  395 DLAMYRAKAAGRNRY 409
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
289-452 2.25e-51

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: 170.90  E-value: 2.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  289 AVVDPLTGLYNRRYAGAHLAAVAERARAADERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHANLRPGDLIARIG 368
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  369 GEEFLVALPDVPRpEDAHAVAERLREAVEEEPVPLPGGG-SLRVTISVGLALSPDEagrrAEPVDAVVQRADSALLLAKS 447
Cdd:pfam00990  81 GDEFAILLPETSL-EGAQELAERIRRLLAKLKIPHTVSGlPLYVTISIGIAAYPND----GEDPEDLLKRADTALYQAKQ 155

                  ....*
gi 499657480  448 AGRNQ 452
Cdd:pfam00990 156 AGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
287-453 1.43e-49

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 166.27  E-value: 1.43e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   287 RLAVVDPLTGLYNRRYAGAHLAAVAERARAADERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHANLRPGDLIAR 366
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   367 IGGEEFLVALPDVPrPEDAHAVAERLREAVEEEpvPLPGGGSLRVTISVGLALSPDEagrrAEPVDAVVQRADSALLLAK 446
Cdd:smart00267  81 LGGDEFALLLPETS-LEEAIALAERILQQLREP--IIIHGIPLYLTISIGVAAYPNP----GEDAEDLLKRADTALYQAK 153

                   ....*..
gi 499657480   447 SAGRNQV 453
Cdd:smart00267 154 KAGRNQV 160
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
288-453 3.16e-46

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: 157.88  E-value: 3.16e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  288 LAVVDPLTGLYNRRYAGAHLAAVAERARAADERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHANLRPGDLIARI 367
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  368 GGEEFLVALPDVPRpEDAHAVAERLREAVEEEPVPLPGGGSLRVTISVGLALSPDEagrrAEPVDAVVQRADSALLLAKS 447
Cdd:TIGR00254  81 GGEEFVVILPGTPL-EDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPGH----GLTLEELLKRADEALYQAKK 155

                  ....*.
gi 499657480  448 AGRNQV 453
Cdd:TIGR00254 156 AGRNRV 161
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
292-453 7.50e-41

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 146.28  E-value: 7.50e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 292 DPLTGLYNRRYAGAHLAAVAERARAADERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHANLRPGDLIARIGGEE 371
Cdd:NF038266  97 DPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYDLCGRWGGEE 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 372 FLVALPDVPrPEDAHAVAERLREAVEEEPVPlPGGGSLRVTISVGLA-LSPDEagrraEPVDAVVQRADSALLLAKSAGR 450
Cdd:NF038266 177 FLLLLPETG-LEEAQVVLERLREAVRALAVR-VGDDVLSVTASAGLAeHRPPE-----EGLSATLSRADQALYQAKRAGR 249

                 ...
gi 499657480 451 NQV 453
Cdd:NF038266 250 DRV 252
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
281-461 9.69e-40

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 150.55  E-value: 9.69e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 281 TLQNGLR-LAVVDPLTGLYNRRyAGAHLAAVAERARAADER-FAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHANL 358
Cdd:PRK15426 389 VLQSSLQwQAWHDPLTRLYNRG-ALFEKARALAKRCQRDQQpFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSL 467
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 359 RPGDLIARIGGEEFLVALPDVPRpEDAHAVAERLREAVEEEPVPLPGGGSLRVTISVGLAlspdEAGRRAE-PVDAVVQR 437
Cdd:PRK15426 468 RAQDVAGRVGGEEFCVVLPGASL-AEAAQVAERIRLRINEKEILVAKSTTIRISASLGVS----SAEEDGDyDFEQLQSL 542
                        170       180
                 ....*....|....*....|....
gi 499657480 438 ADSALLLAKSAGRNQVTIERSAVA 461
Cdd:PRK15426 543 ADRRLYLAKQAGRNRVCASDNAHE 566
PRK09894 PRK09894
diguanylate cyclase; Provisional
291-453 6.56e-39

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 142.51  E-value: 6.56e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 291 VDPLTGLYNRRYAGAHLAAVAERARaaDERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHANLRPGDLIARIGGE 370
Cdd:PRK09894 131 MDVLTGLPGRRVLDESFDHQLRNRE--PQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGE 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 371 EFLVALPDVpRPEDAHAVAERLREAVEEEPVPLPgGGSLRVTISVGLAlspdEAgRRAEPVDAVVQRADSALLLAKSAGR 450
Cdd:PRK09894 209 EFIICLKAA-TDEEACRAGERIRQLIANHAITHS-DGRINITATFGVS----RA-FPEETLDVVIGRADRAMYEGKQTGR 281

                 ...
gi 499657480 451 NQV 453
Cdd:PRK09894 282 NRV 284
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
4-114 1.48e-32

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: 121.94  E-value: 1.48e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMIS 83
Cdd:COG3706    3 RILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIFLT 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 499657480  84 ASRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:COG3706   83 ALDDEEDRARALEAGADDYLTKPFDPEELLA 113
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
4-106 3.20e-30

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: 112.98  E-value: 3.20e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMIS 83
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                         90       100
                 ....*....|....*....|...
gi 499657480  84 ASRDPAIRLQALAEGADDFLAKP 106
Cdd:cd17538   81 ALDDREDRIRGLEAGADDFLSKP 103
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
4-114 3.54e-28

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 111.41  E-value: 3.54e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMIS 83
Cdd:COG3437    8 TVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPVIFLT 87
                         90       100       110
                 ....*....|....*....|....*....|.
gi 499657480  84 ASRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:COG3437   88 ALADPEDRERALEAGADDYLTKPFDPEELLA 118
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
4-108 6.98e-27

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: 104.45  E-value: 6.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMA-GDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMI 82
Cdd:cd17551    2 RILIVDDNPTNLLLLEALLRSAGYLEVVSfTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVMI 81
                         90       100
                 ....*....|....*....|....*.
gi 499657480  83 SASRDPAIRLQALAEGADDFLAKPLD 108
Cdd:cd17551   82 TADTDREVRLRALEAGATDFLTKPFD 107
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1-114 5.55e-26

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 102.24  E-value: 5.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   1 MGGKVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVI 80
Cdd:COG0784    4 GGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPII 83
                         90       100       110
                 ....*....|....*....|....*....|....
gi 499657480  81 MISASRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:COG0784   84 ALTAYADEEDRERALEAGADDYLTKPVDPEELLE 117
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
4-114 3.55e-25

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: 102.34  E-value: 3.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPatRDIPVIMIS 83
Cdd:COG0745    3 RILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARP--SDIPIIMLT 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 499657480  84 ASRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:COG0745   81 ARDDEEDRVRGLEAGADDYLTKPFDPEELLA 111
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
5-106 9.69e-25

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: 97.97  E-value: 9.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   5 VLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMISA 84
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTA 80
                         90       100
                 ....*....|....*....|..
gi 499657480  85 SRDPAIRLQALAEGADDFLAKP 106
Cdd:cd19920   81 LTDTEDKVKGFELGAVDYITKP 102
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
277-457 1.95e-24

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 107.07  E-value: 1.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  277 EMRATLQNGLRLAVVDPLTGLYNRRYAGAHLAAVAERARAADERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHA 356
Cdd:PRK09776  653 ESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLS 732
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  357 NLRPGDLIARIGGEEFLVALPDVPRPEdAHAVAERLREAVEEepVPLPGGGSL-RVTISVGLALSPDEAGRRAEpvdaVV 435
Cdd:PRK09776  733 MLRSSDVLARLGGDEFGLLLPDCNVES-ARFIATRIISAIND--YHFPWEGRVyRVGASAGITLIDANNHQASE----VM 805
                         170       180
                  ....*....|....*....|..
gi 499657480  436 QRADSALLLAKSAGRNQVTIER 457
Cdd:PRK09776  806 SQADIACYAAKNAGRGRVTVYE 827
adrA PRK10245
diguanylate cyclase AdrA; Provisional
292-455 5.28e-23

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 99.90  E-value: 5.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 292 DPLTGLYNRRYAGAHLAAVAERARAADERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHANLRPGDLIARIGGEE 371
Cdd:PRK10245 208 DGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDE 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 372 FLVALPDVPrPEDAHAVAERLREAVEEepVPLPGGGSLRVTISVGLALSPDEAGRRAEPVDAvvqrADSALLLAKSAGRN 451
Cdd:PRK10245 288 FAVIMSGTP-AESAITAMSRVHEGLNT--LRLPNAPQVTLRISVGVAPLNPQMSHYREWLKS----ADLALYKAKNAGRN 360

                 ....
gi 499657480 452 QVTI 455
Cdd:PRK10245 361 RTEV 364
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
6-106 3.41e-22

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: 90.75  E-value: 3.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   6 LITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPatRDIPVIMISAS 85
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELP--PDIPVIVLTAK 78
                         90       100
                 ....*....|....*....|.
gi 499657480  86 RDPAIRLQALAEGADDFLAKP 106
Cdd:cd00156   79 ADEEDAVRALELGADDYLVKP 99
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
15-106 1.42e-21

phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 89.00  E-value: 1.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  15 RIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPatRDIPVIMISASRDPAIRLQA 94
Cdd:cd17574   10 AELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKG--SDIPIIMLTAKDEEEDKVLG 87
                         90
                 ....*....|..
gi 499657480  95 LAEGADDFLAKP 106
Cdd:cd17574   88 LELGADDYITKP 99
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
4-114 2.49e-21

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 88.85  E-value: 2.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMIS 83
Cdd:cd17618    2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIMLT 81
                         90       100       110
                 ....*....|....*....|....*....|.
gi 499657480  84 ASRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:cd17618   82 ARGEEEDKVRGLEAGADDYITKPFSPRELVA 112
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
4-108 1.29e-20

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: 86.83  E-value: 1.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMIS 83
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALT 80
                         90       100
                 ....*....|....*....|....*
gi 499657480  84 ASRDPAIRLQALAEGADDFLAKPLD 108
Cdd:cd17548   81 AYAMKGDREKILEAGCDGYISKPID 105
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
4-114 2.72e-19

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 83.87  E-value: 2.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLK--VKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADpaTRDIPVIM 81
Cdd:COG4565    5 RVLIVEDDPMVAELLRryLERLPGFEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRAR--GPDVDVIV 82
                         90       100       110
                 ....*....|....*....|....*....|...
gi 499657480  82 ISASRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:COG4565   83 ITAARDPETVREALRAGVVDYLIKPFTFERLRE 115
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
42-108 8.35e-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: 82.08  E-value: 8.35e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499657480  42 ARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMISASRDPAIRLQALAEGADDFLAKPLD 108
Cdd:cd17557   48 ADAPRPDLILLDLNMPRMDGFEVLREIKADPDLRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVD 114
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
6-114 1.72e-18

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: 80.78  E-value: 1.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   6 LITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMISAS 85
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAK 80
                         90       100
                 ....*....|....*....|....*....
gi 499657480  86 RDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:cd19937   81 GEEFDKVLGLELGADDYITKPFSPRELLA 109
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
276-455 6.32e-18

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 86.66  E-value: 6.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 276 DEMRAtlQNGLR-LAVVDPLTGLYNRRyaGAHLAAVAERARAADERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRL 354
Cdd:PRK10060 225 EERRA--QERLRiLANTDSITGLPNRN--AIQELIDHAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAI 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 355 HANLRPGDLIARIGGEEFLVALPDVPRPE---DAHAVAERLReaveeEPVPLpggGSLRV--TISVGLALSPdeagRRAE 429
Cdd:PRK10060 301 LSCLEEDQTLARLGGDEFLVLASHTSQAAleaMASRILTRLR-----LPFRI---GLIEVytGCSIGIALAP----EHGD 368
                        170       180
                 ....*....|....*....|....*.
gi 499657480 430 PVDAVVQRADSALLLAKSAGRNQVTI 455
Cdd:PRK10060 369 DSESLIRSADTAMYTAKEGGRGQFCV 394
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
5-112 1.18e-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: 78.28  E-value: 1.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   5 VLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPAT-RDIPVIMIS 83
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGgRRTPIIALT 80
                         90       100
                 ....*....|....*....|....*....
gi 499657480  84 ASRDPAIRLQALAEGADDFLAKPLDDPVL 112
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLDQL 109
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
5-114 1.47e-17

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: 77.96  E-value: 1.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480    5 VLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPAtrDIPVIMISA 84
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDP--TTPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 499657480   85 SRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLA 108
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1-114 1.81e-17

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: 84.24  E-value: 1.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   1 MGGKVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPatRDIPVI 80
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALD--PDLPVI 78
                         90       100       110
                 ....*....|....*....|....*....|....
gi 499657480  81 MISASRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:COG2204   79 LLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLA 112
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
4-114 5.44e-17

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: 76.57  E-value: 5.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMIS 83
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILMLT 81
                         90       100       110
                 ....*....|....*....|....*....|.
gi 499657480  84 ASRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:cd17562   82 TESSDEKKQEGKAAGATGWLVKPFDPEQLLE 112
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
287-451 8.37e-17

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 83.28  E-value: 8.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 287 RLAVVDPLTGLYNRRYAGAHLAAVAERaraaDERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHANLRPGDLIAR 366
Cdd:PRK11359 374 QLIQFDPLTGLPNRNNLHNYLDDLVDK----AVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCR 449
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 367 IGGEEFLVALPDVpRPEDAHAVAERLREAVeEEPVPLpGGGSLRVTISVGlaLSPDEAGRRaepvDAVVQRADSALLLAK 446
Cdd:PRK11359 450 IEGTQFVLVSLEN-DVSNITQIADELRNVV-SKPIMI-DDKPFPLTLSIG--ISYDVGKNR----DYLLSTAHNAMDYIR 520

                 ....*
gi 499657480 447 SAGRN 451
Cdd:PRK11359 521 KNGGN 525
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
4-108 1.46e-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: 75.67  E-value: 1.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLA-AACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMI 82
Cdd:cd17552    3 RILVIDDEEDIREVVQACLEkLAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVILL 82
                         90       100
                 ....*....|....*....|....*.
gi 499657480  83 SASRDPAIRLQALAEGADDFLAKPLD 108
Cdd:cd17552   83 TAKAQPSDRQRFASLGVAGVIAKPFD 108
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
1-114 2.14e-16

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 78.22  E-value: 2.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   1 MGGKVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVI 80
Cdd:PRK10161   1 MARRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVV 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 499657480  81 MISASRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:PRK10161  81 MLTARGEEEDRVRGLETGADDYITKPFSPKELVA 114
orf27 CHL00148
Ycf27; Reviewed
4-106 1.12e-15

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 76.29  E-value: 1.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADpatRDIPVIMIS 83
Cdd:CHL00148   8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKE---SDVPIIMLT 84
                         90       100
                 ....*....|....*....|...
gi 499657480  84 ASRDPAIRLQALAEGADDFLAKP 106
Cdd:CHL00148  85 ALGDVSDRITGLELGADDYVVKP 107
PRK09966 PRK09966
diguanylate cyclase DgcN;
276-424 1.53e-15

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 78.12  E-value: 1.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 276 DEM-----RATLQNG--LRLAVVDPLTGLYNRryaGAHLAAVAERARAADER--FAVMVIDLDRFKSVNDRWGHGAGDAV 346
Cdd:PRK09966 228 DEMeewqlRLQAKNAqlLRTALHDPLTGLANR---AAFRSGINTLMNNSDARktSALLFLDGDNFKYINDTWGHATGDRV 304
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499657480 347 LVAVARRLHANLRPGDLIARIGGEEFLVALPDVPRPEDAHAVAERLREAVeEEPVPLPGGGSLRVTISVGLALSPDEA 424
Cdd:PRK09966 305 LIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQQICSALTQIF-NLPFDLHNGHQTTMTLSIGYAMTIEHA 381
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
5-114 3.29e-15

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: 71.59  E-value: 3.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   5 VLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMISA 84
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 499657480  85 SRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:cd17598   81 LSDPRDVIRGLECGADNFITKPYDEKYLLS 110
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
4-106 5.98e-15

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: 70.57  E-value: 5.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLK--VKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPatRDIPVIM 81
Cdd:COG4753    1 KVLIVDDEPLIREGLKriLEWEAGFEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELD--PDTKIII 78
                         90       100
                 ....*....|....*....|....*
gi 499657480  82 ISASRDPAIRLQALAEGADDFLAKP 106
Cdd:COG4753   79 LSGYSDFEYAQEAIKLGADDYLLKP 103
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
4-112 9.98e-15

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


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 70.44  E-value: 9.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLM-AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMI 82
Cdd:cd19923    2 KVLVVDDFSTMRRIIKNLLKELGFNNVEeAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLMV 81
                         90       100       110
                 ....*....|....*....|....*....|
gi 499657480  83 SASRDPAIRLQALAEGADDFLAKPLDDPVL 112
Cdd:cd19923   82 TAEAKKENVIAAAQAGVNNYIVKPFTAATL 111
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
5-106 5.99e-14

phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a component of the KdpD/KdpE two-component system (TCS) and is activated when histidine kinase KdpD senses a drop in external K+ concentration or upshift in ionic osmolarity, resulting in the expression of a heterooligomeric transporter KdpFABC. In addition, the KdpD/KdpE TCS is also an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. KdpE is a member of the OmpR family of DNA-binding response regulators that contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 67.57  E-value: 5.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   5 VLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRadpATRDIPVIMISA 84
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLR---EWSAVPVIVLSA 77
                         90       100
                 ....*....|....*....|..
gi 499657480  85 SRDPAIRLQALAEGADDFLAKP 106
Cdd:cd17620   78 RDEESDKIAALDAGADDYLTKP 99
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
18-114 6.82e-14

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: 67.90  E-value: 6.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  18 LKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRAdpATRDIPVIMISASRDPAIRLQALAE 97
Cdd:cd17624   14 LKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRR--QGQSLPVLILTARDGVDDRVAGLDA 91
                         90
                 ....*....|....*..
gi 499657480  98 GADDFLAKPLDDPVLMA 114
Cdd:cd17624   92 GADDYLVKPFALEELLA 108
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
32-114 7.62e-14

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: 67.72  E-value: 7.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  32 AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPatrDIPVIMISASRDPAIRLQALAEGADDFLAKPLDDPV 111
Cdd:cd17623   28 AHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTS---QVPVLMLTARGDDIDRILGLELGADDYLPKPFNPRE 104

                 ...
gi 499657480 112 LMA 114
Cdd:cd17623  105 LVA 107
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
4-114 1.22e-13

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: 67.30  E-value: 1.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACY-LPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRA-DPATRdipVIM 81
Cdd:cd17542    2 KVLIVDDAAFMRMMLKDILTKAGYeVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKiDPNAK---VIM 78
                         90       100       110
                 ....*....|....*....|....*....|...
gi 499657480  82 ISASRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:cd17542   79 CSAMGQEEMVKEAIKAGAKDFIVKPFQPERVLE 111
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
4-106 2.63e-13

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: 66.22  E-value: 2.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADpaTRDIPVIMIS 83
Cdd:cd17615    1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRAD--GPDVPVLFLT 78
                         90       100
                 ....*....|....*....|...
gi 499657480  84 ASRDPAIRLQALAEGADDFLAKP 106
Cdd:cd17615   79 AKDSVEDRIAGLTAGGDDYVTKP 101
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
32-106 3.28e-13

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: 65.54  E-value: 3.28e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499657480  32 AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRAdpATRDIPVIMISASRDPAIRLQALAEGADDFLAKP 106
Cdd:cd19935   28 AYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRA--AGKQTPVLMLTARDSVEDRVKGLDLGADDYLVKP 100
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
5-106 8.50e-13

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: 64.71  E-value: 8.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   5 VLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRAdpATRDIPVIMISA 84
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRA--AGNDLPILVLTA 78
                         90       100
                 ....*....|....*....|..
gi 499657480  85 SRDPAIRLQALAEGADDFLAKP 106
Cdd:cd17627   79 RDSVSDRVAGLDAGADDYLVKP 100
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
47-111 1.12e-12

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: 64.74  E-value: 1.12e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499657480  47 PDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMISASRDPAIRLQALAEGADDFLAKpLDDPV 111
Cdd:cd17575   46 PTVILQDLVMPGVDGLTLVRFFRANPATRDIPIIVLSTKEEPEVKSEAFALGANDYLVK-LPDKI 109
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
4-106 1.42e-12

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: 64.34  E-value: 1.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAAcylPLM-----AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRadpATRDIP 78
Cdd:cd17541    2 RVLIVDDSAVMRKLLSRILESD---PDIevvgtARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIM---AERPTP 75
                         90       100       110
                 ....*....|....*....|....*....|
gi 499657480  79 VIMISA--SRDPAIRLQALAEGADDFLAKP 106
Cdd:cd17541   76 VVMVSSltEEGAEITLEALELGAVDFIAKP 105
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
31-114 1.68e-12

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: 63.78  E-value: 1.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  31 MAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRAdpATRDIPVIMISASRDPAIRLQALAEGADDFLAKPLDDP 110
Cdd:cd17625   26 VCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLRE--EGIETPVLLLTALDAVEDRVKGLDLGADDYLPKPFSLA 103

                 ....
gi 499657480 111 VLMA 114
Cdd:cd17625  104 ELLA 107
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
32-105 2.14e-12

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: 63.69  E-value: 2.14e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499657480  32 AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPatRDIPVIMISASRDPAIRLQALAEGADDFLAK 105
Cdd:cd17535   30 AADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRY--PDLKVIVLTAHDDPEYVLRALKAGAAGYLLK 101
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
4-109 3.28e-12

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: 62.99  E-value: 3.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADpaTRDIPVIMIS 83
Cdd:cd17555    2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKE--SPDTPVIVVS 79
                         90       100
                 ....*....|....*....|....*.
gi 499657480  84 ASRDPAIRLQALAEGADDFLAKPLDD 109
Cdd:cd17555   80 GAGVMSDAVEALRLGAWDYLTKPIED 105
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
4-106 5.40e-12

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: 62.40  E-value: 5.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPatrDIPVIMIS 83
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFS---DVPIIMVT 77
                         90       100
                 ....*....|....*....|...
gi 499657480  84 ASRDPAIRLQALAEGADDFLAKP 106
Cdd:cd19938   78 ARVEEIDRLLGLELGADDYICKP 100
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
4-84 6.41e-12

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: 62.24  E-value: 6.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRAdpATRDIPVIMIS 83
Cdd:cd17554    2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIRE--KKPDLPVIICT 79

                 .
gi 499657480  84 A 84
Cdd:cd17554   80 A 80
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
4-114 6.50e-12

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: 62.10  E-value: 6.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADpatRDIPVIMIS 83
Cdd:cd17626    2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAE---SGVPIVMLT 78
                         90       100       110
                 ....*....|....*....|....*....|.
gi 499657480  84 ASRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:cd17626   79 AKSDTVDVVLGLESGADDYVAKPFKPKELVA 109
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
27-107 1.55e-11

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: 60.97  E-value: 1.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  27 YLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRA-DPatrDIPVIMIS--ASRDPAIRlqALAEGADDFL 103
Cdd:cd17550   23 YEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEkYP---DLPVIMISghGTIETAVK--ATKLGAYDFI 97

                 ....
gi 499657480 104 AKPL 107
Cdd:cd17550   98 EKPL 101
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
17-114 1.63e-11

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: 60.90  E-value: 1.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  17 VLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRadpATRDIPVIMISASRDPAIRLQALA 96
Cdd:cd17614   13 ILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVR---KTSNVPIIMLTAKDSEVDKVLGLE 89
                         90
                 ....*....|....*...
gi 499657480  97 EGADDFLAKPLDDPVLMA 114
Cdd:cd17614   90 LGADDYVTKPFSNRELLA 107
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
5-108 1.78e-11

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: 60.93  E-value: 1.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   5 VLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMISA 84
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTG 80
                         90       100
                 ....*....|....*....|....
gi 499657480  85 SRDPAIRLQALAEGADDFLAKPLD 108
Cdd:cd17580   81 YGQPEDRERALEAGFDAHLVKPVD 104
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
323-418 6.31e-11

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: 60.06  E-value: 6.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 323 VMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHANL-RPGDLIARIGGEEFLVALPDVpRPEDAHAVAERLREAVEEEPV 401
Cdd:cd07556    4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVSGLD-HPAAAVAFAEDMREAVSALNQ 82
                         90
                 ....*....|....*..
gi 499657480 402 PLPGGGSLRVTISVGLA 418
Cdd:cd07556   83 SEGNPVRVRIGIHTGPV 99
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
18-106 8.81e-11

phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; Escherichia coli PhoP (EcPhoP) is part of the PhoQ/PhoP two-component system (TCS) that regulates virulence genes and plays an essential role in the response of the bacteria to the environment of their mammalian hosts, sensing several stimuli such as extracellular magnesium limitation, low pH, the presence of cationic antimicrobial peptides, and osmotic upshift. This subfamily also includes Brucella suis FeuP, part of the FeuPQ TCS that is involved in the regulation of iron uptake, and Microchaete diplosiphon RcaC, which is required for chromatic adaptation. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 58.83  E-value: 8.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  18 LKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRAdpATRDIPVIMISASRDPAIRLQALAE 97
Cdd:cd19934   14 LKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRS--EGRATPVLILTARDSWQDKVEGLDA 91

                 ....*....
gi 499657480  98 GADDFLAKP 106
Cdd:cd19934   92 GADDYLTKP 100
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
48-114 1.23e-10

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: 58.60  E-value: 1.23e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499657480  48 DLILLDWALPDVPGLEVLRHLRADpaTRDIPVIMISASRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:cd17573   44 DLVLVSDKLPDGNGLSIVSRIKEK--HPSIVVIVLSDNPKTEQEIEAFKEGADDYIAKPFDFKVLVA 108
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
319-453 1.45e-10

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 63.42  E-value: 1.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 319 ERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLHANLRPGDLIARIGGEEFLVALPDVPRPEDAHAVAERLREAVeE 398
Cdd:PRK11829 261 DHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSFPAMQLARRIMSQV-T 339
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499657480 399 EPVPLpGGGSLRVTISVGLALspdeagRRA--EPVDAVVQRADSALLLAKSAGRNQV 453
Cdd:PRK11829 340 QPLFF-DEITLRPSASIGITR------YQAqqDTAESMMRNASTAMMAAHHEGRNQI 389
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
32-112 2.05e-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: 58.02  E-value: 2.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  32 AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRAdpATRDIPVIMISASRDPAIRLQALAEGADDFLAKPLDDPV 111
Cdd:cd19925   32 AGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRA--AGHDVDVIVVTAANDVETVREALRLGVVDYLIKPFTFER 109

                 .
gi 499657480 112 L 112
Cdd:cd19925  110 L 110
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
4-106 2.61e-10

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


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 57.91  E-value: 2.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARgELPD--LILLDWALPDVPGLEVLRHLRADPATRDIPVIM 81
Cdd:cd17544    2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLE-QHPDikLVITDYNMPEMDGFELVREIRKKYSRDQLAIIG 80
                         90       100
                 ....*....|....*....|....*
gi 499657480  82 ISASRDPAIRLQALAEGADDFLAKP 106
Cdd:cd17544   81 ISASGDNALSARFIKAGANDFLTKP 105
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
3-108 3.66e-10

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 57.18  E-value: 3.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   3 GKVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRA-DPatrDIPVIM 81
Cdd:cd17553    1 EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKViDE---NIRVII 77
                         90       100
                 ....*....|....*....|....*..
gi 499657480  82 ISASRDPAIRLQALAEGADDFLAKPLD 108
Cdd:cd17553   78 MTAYGELDMIQESKELGALTHFAKPFD 104
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
362-446 4.03e-10

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: 58.77  E-value: 4.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 362 DLIARIGGEEFLVALPDVPRpEDAHAVAERLREAVEEEPvplpgggSLRVTISVGLAlspdeagrraepVDAVVQRADsA 441
Cdd:COG3706  116 DLVARYGGEEFAILLPGTDL-EGALAVAERIREAVAELP-------SLRVTVSIGVA------------GDSLLKRAD-A 174

                 ....*
gi 499657480 442 LLLAK 446
Cdd:COG3706  175 LYQAR 179
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
5-114 4.48e-10

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: 57.03  E-value: 4.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   5 VLITDNVATNRIVlKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRAdpATRDIPVIMISA 84
Cdd:cd17616    2 LLIEDDSATAQSI-ELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRL--AKVKTPILILSG 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 499657480  85 SRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:cd17616   79 LADIEDKVKGLGFGADDYMTKPFHKDELVA 108
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
4-114 4.61e-10

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: 56.69  E-value: 4.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPatrDIPVIMIS 83
Cdd:cd17594    1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARS---DVPIIIIS 77
                         90       100       110
                 ....*....|....*....|....*....|..
gi 499657480  84 ASRDPAI-RLQALAEGADDFLAKPLDDPVLMA 114
Cdd:cd17594   78 GDRRDEIdRVVGLELGADDYLAKPFGLRELLA 109
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1-114 5.24e-10

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: 58.81  E-value: 5.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   1 MGGKVLITDNVATNRIVLKVKLAAACYLPL-MAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPAtrdIPV 79
Cdd:COG3707    2 RGLRVLVVDDEPLRRADLREGLREAGYEVVaEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP---APV 78
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499657480  80 IMISASRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:COG3707   79 ILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLP 113
ompR PRK09468
osmolarity response regulator; Provisional
4-114 5.91e-10

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 59.60  E-value: 5.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRAdpATRDIPVIMIS 83
Cdd:PRK09468   7 KILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRS--QNNPTPIIMLT 84
                         90       100       110
                 ....*....|....*....|....*....|.
gi 499657480  84 ASRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:PRK09468  85 AKGEEVDRIVGLEIGADDYLPKPFNPRELLA 115
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
32-108 6.75e-10

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: 56.44  E-value: 6.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  32 AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHL--RADPatrdIPVIMISA--SRDPAIrlQALAEGADDFLAKPL 107
Cdd:cd17572   28 VETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIqeRSLP----TSVIVITAhgSVDIAV--EAMRLGAYDFLEKPF 101

                 .
gi 499657480 108 D 108
Cdd:cd17572  102 D 102
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
22-106 8.59e-10

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 58.93  E-value: 8.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  22 LAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRAdpaTRDIPVIMISASRDPAIRLQALAEGADD 101
Cdd:PRK10710  30 LQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRR---FSDIPIVMVTAKIEEIDRLLGLEIGADD 106

                 ....*
gi 499657480 102 FLAKP 106
Cdd:PRK10710 107 YICKP 111
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
4-108 1.16e-09

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: 57.23  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRA-DPATRdipVIMI 82
Cdd:COG4567    6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRErDPDAR---IVVL 82
                         90       100
                 ....*....|....*....|....*.
gi 499657480  83 SASRDPAIRLQALAEGADDFLAKPLD 108
Cdd:COG4567   83 TGYASIATAVEAIKLGADDYLAKPAD 108
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
34-106 1.55e-09

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: 54.76  E-value: 1.55e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499657480  34 DGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADpatRDIPVIMISASRDPAIRLQALAEGADDFLAKP 106
Cdd:cd19936   30 DGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQK---STLPVIFLTSKDDEIDEVFGLRMGADDYITKP 99
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
35-106 1.65e-09

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 58.05  E-value: 1.65e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499657480  35 GASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPAtrDIPVIMISASRDPAIRLQALAEGADDFLAKP 106
Cdd:PRK11083  36 GLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHP--ALPVIFLTARSDEVDRLVGLEIGADDYVAKP 105
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
47-106 1.69e-09

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 57.89  E-value: 1.69e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  47 PDLILLDWALPDVPGLEVLRHLRADPAtrdIPVIMISASRDPAIRLQALAEGADDFLAKP 106
Cdd:PRK10529  46 PDLIILDLGLPDGDGIEFIRDLRQWSA---IPVIVLSARSEESDKIAALDAGADDYLSKP 102
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
39-114 2.68e-09

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: 54.91  E-value: 2.68e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499657480  39 LSLARGELPDLILLDWALPDVPGLEVLRHLRAdpATRDIPVIMISASRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:cd17537   37 LAAAPPDQPGCLVLDVRMPGMSGLELQDELLA--RGSNIPIIFITGHGDVPMAVEAMKAGAVDFLEKPFRDQVLLD 110
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
32-114 3.46e-09

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: 54.80  E-value: 3.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  32 AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRA-DPatrDIPVIMISASRDPAIRLQALAEGADDFLAKPLDDP 110
Cdd:cd17549   28 FADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRElDP---DLPVILITGHGDVPMAVEAMRAGAYDFLEKPFDPE 104

                 ....
gi 499657480 111 VLMA 114
Cdd:cd17549  105 RLLD 108
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
33-114 5.44e-09

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: 55.88  E-value: 5.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  33 GDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPatRDIPVIMISASRDPAIRLQALAEGADDFLAKPLDDPVL 112
Cdd:COG4566   30 ASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARG--SPLPVIFLTGHGDVPMAVRAMKAGAVDFLEKPFDDQAL 107

                 ..
gi 499657480 113 MA 114
Cdd:COG4566  108 LD 109
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
48-108 6.43e-09

phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and similar domains; Type-B ARRs (Arabidopsis response regulators) are a class of MYB-type transcription factors that act as major players in the transcriptional activation of cytokinin-responsive genes. They directly regulate the expression of type-A ARR genes and other downstream target genes. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Cytokinin signaling involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-B ARRs contain a receiver (REC) domain and a large C-terminal extension that has characteristics of an effector or output domain, with a Myb-like DNA binding domain referred to as the GARP domain. The GARP domain is a motif specific to plant transcription factors. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 53.79  E-value: 6.43e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499657480  48 DLILLDWALPDVPGLEVLRHLRADPatrDIPVIMISASRDPAIRLQALAEGADDFLAKPLD 108
Cdd:cd17584   46 DLVITDVHMPDMDGFEFLELIRLEM---DLPVIMMSADGSTSTVMKGLAHGACDYLLKPVS 103
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
47-114 6.71e-09

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: 53.44  E-value: 6.71e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499657480  47 PDLILLDWALPDVPGLEVLRHLRAdpaTRDIPVIMISASRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:cd18159   43 PDLVLLDINLPYFDGFYWCREIRQ---ISNVPIIFISSRDDNMDQVMAINMGGDDYITKPFDLDVLLA 107
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
32-108 7.01e-09

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 55.98  E-value: 7.01e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499657480  32 AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPatRDIPVIMISASRDPAIrlQALAEGADDFLAKPLD 108
Cdd:COG3279   33 ASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELD--PPPPIIFTTAYDEYAL--EAFEVNAVDYLLKPID 105
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
4-114 7.89e-09

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 55.96  E-value: 7.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELpDLILLDWALPDVPGLEVLRHLRADPATrdiPVIMIS 83
Cdd:PRK10955   3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDSI-DLLLLDVMMPKKNGIDTLKELRQTHQT---PVIMLT 78
                         90       100       110
                 ....*....|....*....|....*....|.
gi 499657480  84 ASRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:PRK10955  79 ARGSELDRVLGLELGADDYLPKPFNDRELVA 109
PRK10693 PRK10693
two-component system response regulator RssB;
32-109 1.02e-08

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 56.54  E-value: 1.02e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499657480  32 AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATrdIPVIMISASRDPAIRLQALAEGADDFLAKPLDD 109
Cdd:PRK10693   3 AANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQ--TPVLVISATENMADIAKALRLGVQDVLLKPVKD 78
PRK10610 PRK10610
chemotaxis protein CheY;
4-107 1.03e-08

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 53.44  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLM-AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMI 82
Cdd:PRK10610   7 KFLVVDDFSTMRRIVRNLLKELGFNNVEeAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMV 86
                         90       100
                 ....*....|....*....|....*
gi 499657480  83 SASRDPAIRLQALAEGADDFLAKPL 107
Cdd:PRK10610  87 TAEAKKENIIAAAQAGASGYVVKPF 111
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
31-106 1.52e-08

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: 52.20  E-value: 1.52e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499657480  31 MAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRAdpaTRDIPVIMISASRDPAIRLQALAEGADDFLAKP 106
Cdd:cd17621   27 VATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRA---RSNVPVIMVTAKDSEIDKVVGLELGADDYVTKP 99
PRK10766 PRK10766
two-component system response regulator TorR;
1-108 1.66e-08

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 54.66  E-value: 1.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   1 MGGKVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRAdpaTRDIPVI 80
Cdd:PRK10766   1 MSYHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRS---RSTVGII 77
                         90       100
                 ....*....|....*....|....*...
gi 499657480  81 MISASRDPAIRLQALAEGADDFLAKPLD 108
Cdd:PRK10766  78 LVTGRTDSIDRIVGLEMGADDYVTKPLE 105
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
5-106 1.67e-08

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 52.02  E-value: 1.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   5 VLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELP--DLILLDWALPDVPGLEVLRHLRADPATRDIPVIMI 82
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNeiDLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMM 80
                         90       100
                 ....*....|....*....|....
gi 499657480  83 SASRDPAIRLQALAEGADDFLAKP 106
Cdd:cd17582   81 SSQDSVGVVFKCLSKGAADYLVKP 104
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
48-107 1.76e-08

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: 52.75  E-value: 1.76e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  48 DLILLDWALPDVPGLEVLRHLRADPATRDIPVIMISASRDPAIRLQALAEGADDFLAKPL 107
Cdd:cd17581   55 NMIITDYCMPGMTGYDLLKKVKESSALKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPV 114
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
4-114 1.77e-08

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 54.93  E-value: 1.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLIT-DNVATNRIVLKvKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRAdpATRDIPVIMI 82
Cdd:PRK09836   2 KLLIVeDEKKTGEYLTK-GLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRS--ANKGMPILLL 78
                         90       100       110
                 ....*....|....*....|....*....|..
gi 499657480  83 SASRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:PRK09836  79 TALGTIEHRVKGLELGADDYLVKPFAFAELLA 110
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
4-112 1.95e-08

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: 52.15  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRivlkvKLAAACyLP-------LMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRAdpatRD 76
Cdd:cd17593    2 KVLICDDSSMAR-----KQLARA-LPadwdveiTFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPV----EQ 71
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 499657480  77 IP--VIMISASRDPAIRLQALAEGADDFLAKPLDDPVL 112
Cdd:cd17593   72 LEtkVIVVSGDVQPEAKERVLELGALAFLKKPFDPEKL 109
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
5-108 3.07e-08

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: 51.62  E-value: 3.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   5 VLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLS-LARGELpDLILLDWALPDVPGLEVLRHLRAdpaTRDIPVIMIS 83
Cdd:cd17619    3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQiLARQDI-DLVLLDINLPGKDGLSLTRELRE---QSEVGIILVT 78
                         90       100
                 ....*....|....*....|....*
gi 499657480  84 ASRDPAIRLQALAEGADDFLAKPLD 108
Cdd:cd17619   79 GRDDEVDRIVGLEIGADDYVTKPFN 103
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
32-106 5.33e-08

phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the phosphorelay system in the early stage of spore formation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress and may act in the with sigma factor spo0H to control the expression of some genes that are critical to the sporulation process. Spo0A contains a regulatory N-terminal REC domain and a C-terminal DNA-binding transcription activation domain as its effector/output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 50.68  E-value: 5.33e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499657480  32 AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMISASRDPAIRLQALAEGADDFLAKP 106
Cdd:cd17561   33 AHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPKIIMLTAFGQEDITQRAVELGASYYILKP 107
PRK15347 PRK15347
two component system sensor kinase;
4-107 5.92e-08

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 55.42  E-value: 5.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRD--IPVIM 81
Cdd:PRK15347 692 QILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNLDpdCMIVA 771
                         90       100
                 ....*....|....*....|....*.
gi 499657480  82 ISASRDPAIRLQALAEGADDFLAKPL 107
Cdd:PRK15347 772 LTANAAPEEIHRCKKAGMNHYLTKPV 797
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
47-106 6.29e-08

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: 50.44  E-value: 6.29e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  47 PDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMISASRDPAIRLQALAEGADDFLAKP 106
Cdd:cd17602   43 PDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTGKDGLVDRIRAKMAGASGYLTKP 102
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
5-106 6.56e-08

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: 50.45  E-value: 6.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   5 VLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMISA 84
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80
                         90       100
                 ....*....|....*....|..
gi 499657480  85 SRDPAIRLQALAEGADDFLAKP 106
Cdd:cd19927   81 KGMTSDRIKGYNAGCDGYLSKP 102
PRK15479 PRK15479
transcriptional regulator TctD;
32-108 7.25e-08

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 52.80  E-value: 7.25e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499657480  32 AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRAdpATRDIPVIMISASRDPAIRLQALAEGADDFLAKPLD 108
Cdd:PRK15479  30 VFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRK--RGQTLPVLLLTARSAVADRVKGLNVGADDYLPKPFE 104
PRK11517 PRK11517
DNA-binding response regulator HprR;
5-114 7.55e-08

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 52.98  E-value: 7.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   5 VLITDNVATNRIVLKvKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATrdiPVIMISA 84
Cdd:PRK11517   4 LLIEDNQRTQEWVTQ-GLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQT---PVICLTA 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 499657480  85 SRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:PRK11517  80 RDSVDDRVRGLDSGANDYLVKPFSFSELLA 109
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
32-114 8.14e-08

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 52.72  E-value: 8.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  32 AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRAdpATRDIPVIMISASRDPAIRLQALAEGADDFLAKPLDDPV 111
Cdd:PRK10651  38 ASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLRE--KSLSGRIVVFSVSNHEEDVVTALKRGADGYLLKDMEPED 115

                 ...
gi 499657480 112 LMA 114
Cdd:PRK10651 116 LLK 118
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
4-108 8.74e-08

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 54.08  E-value: 8.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRA-DPATrdiPVIMI 82
Cdd:PRK11361   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRShETRT---PVILM 82
                         90       100
                 ....*....|....*....|....*.
gi 499657480  83 SASRDPAIRLQALAEGADDFLAKPLD 108
Cdd:PRK11361  83 TAYAEVETAVEALRCGAFDYVIKPFD 108
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
31-114 9.02e-08

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: 50.45  E-value: 9.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  31 MAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADpatRDIPVIMISASRDPAIRLQALAEGADDFLAKPLDDP 110
Cdd:cd19939   28 VFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREH---SHVPILMLTARTEEMDRVLGLEMGADDYLCKPFSPR 104

                 ....
gi 499657480 111 VLMA 114
Cdd:cd19939  105 ELLA 108
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
3-108 1.54e-07

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: 49.58  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   3 GKVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPAtrDIPVIMI 82
Cdd:cd19919    1 KTVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHP--DLPVIIM 78
                         90       100
                 ....*....|....*....|....*.
gi 499657480  83 SASRDPAIRLQALAEGADDFLAKPLD 108
Cdd:cd19919   79 TAHSDLDSAVSAYQGGAFEYLPKPFD 104
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
5-108 2.00e-07

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 53.11  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   5 VLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRA-DPAtrdIPVIMIS 83
Cdd:PRK10365   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAlNPA---IPVLIMT 84
                         90       100
                 ....*....|....*....|....*
gi 499657480  84 ASRDPAIRLQALAEGADDFLAKPLD 108
Cdd:PRK10365  85 AYSSVETAVEALKTGALDYLIKPLD 109
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
34-116 2.19e-07

phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; Klebsiella pneumoniae RstA (kpRstA) is part of the RstA/RstB two-component regulatory system that may play a regulatory role in virulence. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 49.30  E-value: 2.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  34 DGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRAdpaTRDIPVIMISASRDPAIRLQALAEGADDFLAKPLDDPVLM 113
Cdd:cd17622   32 RGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRP---KYQGPILLLTALDSDIDHILGLELGADDYVVKPVEPAVLL 108

                 ...
gi 499657480 114 ARL 116
Cdd:cd17622  109 ARL 111
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
276-453 3.11e-07

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 52.79  E-value: 3.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 276 DEMRatlqnglRLAVVDPLTGLYNRryagAHLAAVAERARAADERFAVMVIDLDRFKSVNDRWGHGAGDAVLVAVARRLH 355
Cdd:PRK13561 225 EEQS-------RNATRFPVSDLPNK----ALLMALLEQVVARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLK 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480 356 ANLRPGDLIARIGGEEFLVALPDVPRPEDAHAVAERLREAVEEePVPLPGGgSLRVTISVGLALSpdEAGRRAEpvdAVV 435
Cdd:PRK13561 294 SVLSPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINE-RLPIQRI-QLRPSCSIGIAMF--YGDLTAE---QLY 366
                        170
                 ....*....|....*...
gi 499657480 436 QRADSALLLAKSAGRNQV 453
Cdd:PRK13561 367 SRAISAAFTARRKGKNQI 384
PLN03029 PLN03029
type-a response regulator protein; Provisional
48-107 3.39e-07

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 50.80  E-value: 3.39e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  48 DLILLDWALPDVPGLEVLRHLRADPATRDIPVIMISASRDPAIRLQALAEGADDFLAKPL 107
Cdd:PLN03029  74 NLIITDYCMPGMTGYDLLKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPV 133
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
5-106 7.00e-07

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: 47.76  E-value: 7.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   5 VLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELP---------DLILLDWALPDVPGLEVLRHLRADPATR 75
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKegndlskelDLIITDIEMPKMDGYELTFELRDDPRLA 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 499657480  76 DIPVIMISASRDPAIRLQALAEGADDFLAKP 106
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
32-114 1.04e-06

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: 47.33  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  32 AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRA-DPatrDIPVIMISASRD-----PAIRLqalaeGADDFLAK 105
Cdd:cd17536   31 AENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRElYP---DIKIIILSGYDDfeyaqKAIRL-----GVVDYLLK 102

                 ....*....
gi 499657480 106 PLDDPVLMA 114
Cdd:cd17536  103 PVDEEELEE 111
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
31-114 2.97e-06

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: 45.86  E-value: 2.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  31 MAGDGASCLSLARGELPDLILLDWALP-DVPGLEVLRHLRADpatRDIPVIMISASRDPAIRLQALAEGADDFLAKPLDD 109
Cdd:cd17534   30 IADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREK---FDIPVIFLTAYSDEETLERAKETNPYGYLVKPFNE 106

                 ....*
gi 499657480 110 PVLMA 114
Cdd:cd17534  107 RELKA 111
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
32-108 4.45e-06

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: 45.42  E-value: 4.45e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499657480  32 AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMISASRDPAIRlqALAEGADDFLAKPLD 108
Cdd:cd19931   30 ASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILTVSDAEDDVVT--ALRAGADGYLLKDME 104
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
3-108 4.89e-06

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 48.71  E-value: 4.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   3 GKVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATrdIPVIMI 82
Cdd:PRK10923   4 GIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPM--LPVIIM 81
                         90       100
                 ....*....|....*....|....*.
gi 499657480  83 SASRDPAIRLQALAEGADDFLAKPLD 108
Cdd:PRK10923  82 TAHSDLDAAVSAYQQGAFDYLPKPFD 107
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
32-114 5.31e-06

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 47.15  E-value: 5.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  32 AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMISASRDPAIRLqaLAEGADDFLAKPLDDPV 111
Cdd:PRK10403  38 AGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQIIILTVSDASSDVFAL--IDAGADGYLLKDSDPEV 115

                 ...
gi 499657480 112 LMA 114
Cdd:PRK10403 116 LLE 118
fixJ PRK09390
response regulator FixJ; Provisional
3-114 6.02e-06

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 46.92  E-value: 6.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   3 GKVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATrdIPVIMI 82
Cdd:PRK09390   4 GVVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSP--LPVIVM 81
                         90       100       110
                 ....*....|....*....|....*....|..
gi 499657480  83 SASRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:PRK09390  82 TGHGDVPLAVEAMKLGAVDFIEKPFEDERLIG 113
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
4-108 7.56e-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: 44.74  E-value: 7.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRA-DPATRdipVIMI 82
Cdd:cd17563    2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRAlQPDAR---IVVL 78
                         90       100       110
                 ....*....|....*....|....*....|.
gi 499657480  83 S-----ASRDPAIRLqalaeGADDFLAKPLD 108
Cdd:cd17563   79 TgyasiATAVEAIKL-----GADDYLAKPAD 104
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
5-112 1.41e-05

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 47.81  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480    5 VLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATrdIPVIMISA 84
Cdd:PRK09959  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSS--LPIWGLTA 1038
                          90       100
                  ....*....|....*....|....*...
gi 499657480   85 SRDPAIRLQALAEGADDFLAKPLDDPVL 112
Cdd:PRK09959 1039 NAQANEREKGLSCGMNLCLFKPLTLDVL 1066
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
34-112 1.68e-05

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 47.54  E-value: 1.68e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499657480  34 DGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPVIMISASRDPAIRLQALAEGADDFLAKPLDDPVL 112
Cdd:PRK11107 699 SGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAML 777
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
4-106 4.30e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 45.26  E-value: 4.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLM--AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRadpATRDIPVIM 81
Cdd:PRK12555   2 RIGIVNDSPLAVEALRRALARDPDHEVVwvATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIM---AERPCPILI 78
                         90       100
                 ....*....|....*....|....*..
gi 499657480  82 ISAS--RDPAIRLQALAEGADDFLAKP 106
Cdd:PRK12555  79 VTSLteRNASRVFEAMGAGALDAVDTP 105
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
5-106 4.67e-05

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


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 42.11  E-value: 4.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   5 VLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLrhLRADPATRDIPVIMISA 84
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLI--PRIKKARPDLPIIVMSA 78
                         90       100
                 ....*....|....*....|..
gi 499657480  85 SRDPAIRLQALAEGADDFLAKP 106
Cdd:cd19928   79 QNTLMTAVKAAERGAFEYLPKP 100
PRK10643 PRK10643
two-component system response regulator PmrA;
32-106 4.92e-05

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 44.64  E-value: 4.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  32 AGDGASCLSLARGELP----DLILLDWALPDVPGLEVLRHLRADpaTRDIPVIMISAsRDpAI--RLQALAEGADDFLAK 105
Cdd:PRK10643  26 ACDCASTAREAEALLEsghySLVVLDLGLPDEDGLHLLRRWRQK--KYTLPVLILTA-RD-TLedRVAGLDVGADDYLVK 101

                 .
gi 499657480 106 P 106
Cdd:PRK10643 102 P 102
PRK10430 PRK10430
two-component system response regulator DcuR;
5-106 8.35e-05

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 43.94  E-value: 8.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   5 VLITDNVAT----NRivlkvklaaaCYLPLMAG----DGASCLSLAR-----GELP-DLILLDWALPDVPGLEVLRHLRA 70
Cdd:PRK10430   4 VLIVDDDAMvaelNR----------RYVAQIPGfqccGTASTLEQAKeiifnSDTPiDLILLDIYMQQENGLDLLPVLHE 73
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499657480  71 dpATRDIPVIMISASRDPAIRLQALAEGADDFLAKP 106
Cdd:PRK10430  74 --AGCKSDVIVISSAADAATIKDSLHYGVVDYLIKP 107
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
4-106 8.82e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 44.37  E-value: 8.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAAcylPLM-----AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRAdpaTRDIP 78
Cdd:PRK00742   5 RVLVVDDSAFMRRLISEILNSD---PDIevvgtAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMR---LRPTP 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 499657480  79 VIMISA--SRDPAIRLQALAEGADDFLAKP 106
Cdd:PRK00742  79 VVMVSSltERGAEITLRALELGAVDFVTKP 108
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
32-114 9.94e-05

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 44.93  E-value: 9.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  32 AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIPvimisasrdPAIRLQA---------LAEGADDF 102
Cdd:PRK11091 555 AMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPREDLP---------PLVALTAnvlkdkkeyLDAGMDDV 625
                         90
                 ....*....|..
gi 499657480 103 LAKPLDDPVLMA 114
Cdd:PRK11091 626 LSKPLSVPALTA 637
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
47-107 1.01e-04

phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar proteins; Bacillus subtilis GlnL is part of the GlnK-GlnL (formerly YcbA-YcbB) two-component system that positively regulates the expression of the glsA-glnT (formerly ybgJ-ybgH) operon in response to glutamine. It contains a REC domain and a DNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 41.49  E-value: 1.01e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499657480  47 PDLILLDWALPDVPGLEVLRHLRadPATRDIPVIMISASRDPAIRLQALAEGADDFLAKPL 107
Cdd:cd17565   45 PDIVLIDLLMPGMDGIQLVRKLK--DTGSNGKFIMISQVSDKEMIGKAYQAGIEFFINKPI 103
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
48-114 1.57e-04

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: 41.15  E-value: 1.57e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499657480  48 DLILLDWALPDVPGLEVLRHLRADPATRDIPVIMISASRDPAIRLQALAEGADDFLAKPLDDPVLMA 114
Cdd:cd17539   43 DLVIVSLALEDFDGLRLCSQLRSLERTRQLPILAVADPGDRGRLIRALEIGVNDYLVRPIDPNELLA 109
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
4-106 1.87e-04

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: 40.86  E-value: 1.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPL-MAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADpatRDIPVIMI 82
Cdd:cd19932    2 RVLIAEDEALIRMDLREMLEEAGYEVVgEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSE---NIAPIVLL 78
                         90       100
                 ....*....|....*....|....
gi 499657480  83 SASRDPAIRLQALAEGADDFLAKP 106
Cdd:cd19932   79 TAYSQQDLVERAKEAGAMAYLVKP 102
PRK13856 PRK13856
two-component response regulator VirG; Provisional
5-106 3.94e-04

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 42.11  E-value: 3.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   5 VLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLradPATRDIPVIMISA 84
Cdd:PRK13856   4 VLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSL---ATKSDVPIIIISG 80
                         90       100
                 ....*....|....*....|...
gi 499657480  85 SR-DPAIRLQALAEGADDFLAKP 106
Cdd:PRK13856  81 DRlEEADKVVALELGATDFIAKP 103
PRK10336 PRK10336
two-component system response regulator QseB;
48-107 4.29e-04

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 41.80  E-value: 4.29e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  48 DLILLDWALPDVPGLEVLRHLRADpaTRDIPVIMISASRDPAIRLQALAEGADDFLAKPL 107
Cdd:PRK10336  46 DAVILDLTLPGMDGRDILREWREK--GQREPVLILTARDALAERVEGLRLGADDYLCKPF 103
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
48-106 4.50e-04

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: 39.44  E-value: 4.50e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499657480  48 DLILLDWALPDVPGLEVLRHLRADPAtrDIPVIMISASRDPAIRLQALAEGADDFLAKP 106
Cdd:cd19926   44 DLCLTDMRLPDGSGLELVQHIQQRLP--QTPVAVITAYGSLDTAIEALKAGAFDFLTKP 100
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
4-112 4.79e-04

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: 39.69  E-value: 4.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLS-LARGELP-DLILLDWALPDVPGLEVLRHLRADPATRDIPVIM 81
Cdd:cd19933    2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNlLASAEHSfQLVLLDLCMPEMDGFEVALRIRKLFGRRERPLIV 81
                         90       100       110
                 ....*....|....*....|....*....|..
gi 499657480  82 I-SASRDPAIRLQALAEGADDFLAKPLDDPVL 112
Cdd:cd19933   82 AlTANTDDSTREKCLSLGMNGVITKPVSLHAL 113
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
4-68 5.37e-04

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: 39.88  E-value: 5.37e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLM--AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHL 68
Cdd:COG2197    3 RVLIVDDHPLVREGLRALLEAEPDIEVVgeAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
PRK10360 PRK10360
transcriptional regulator UhpA;
33-105 6.97e-04

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 40.73  E-value: 6.97e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499657480  33 GDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLradpaTRDIPVIMISASRDPAIRLQALAEGADDFLAK 105
Cdd:PRK10360  34 GSGREALAGLPGRGVQVCICDISMPDISGLELLSQL-----PKGMATIMLSVHDSPALVEQALNAGARGFLSK 101
PRK15369 PRK15369
two component system response regulator;
34-114 1.31e-03

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 40.06  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  34 DGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRAD-PATRdipVIMISASRDPAIRLQALAEGADDFLAKPLDDPVL 112
Cdd:PRK15369  37 NGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRwPAMN---ILVLTARQEEHMASRTLAAGALGYVLKKSPQQIL 113

                 ..
gi 499657480 113 MA 114
Cdd:PRK15369 114 LA 115
PRK10816 PRK10816
two-component system response regulator PhoP;
4-106 1.66e-03

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 39.72  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATrdIPVIMIS 83
Cdd:PRK10816   2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVS--LPILVLT 79
                         90       100
                 ....*....|....*....|...
gi 499657480  84 ASRDPAIRLQALAEGADDFLAKP 106
Cdd:PRK10816  80 ARESWQDKVEVLSAGADDYVTKP 102
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
4-106 2.35e-03

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


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 37.48  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480   4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLS-LARGELPDLILLDWALPDVPGLEVLRHLRA-DPatrDIPVIM 81
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEkLQQGKDIDIVVTDIVMPEMDGIELAREARKiDP---DVKILF 77
                         90       100
                 ....*....|....*....|....*
gi 499657480  82 ISASRDPAIRLQALAEGADDFLAKP 106
Cdd:cd18160   78 ISGGAAAAPELLSDAVGDNATLKKP 102
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
32-108 2.42e-03

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: 37.90  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499657480  32 AGDGASCLSLARGELPDLILLDWALPDVPGLEV---LRHLRADPAtrdipVIMISASRDPAirLQALAEGADDFLAKPLD 108
Cdd:cd17532   30 AENGEEALEAIEELKPDVVFLDIQMPGLDGLELakkLSKLAKPPL-----IVFVTAYDEYA--VEAFELNAVDYLLKPFS 102
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
34-105 3.18e-03

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 38.72  E-value: 3.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499657480  34 DGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDIpvIMISASRDPAIRLQALAEGADDFLAK 105
Cdd:PRK09958  33 EGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGII--IIVSAKNDHFYGKHCADAGANGFVSK 102
dpiA PRK10046
two-component response regulator DpiA; Provisional
30-107 4.63e-03

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 38.46  E-value: 4.63e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499657480  30 LMAGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRADPATRDipVIMISASRDPAIRLQALAEGADDFLAKPL 107
Cdd:PRK10046  34 LLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELVQAHYPGD--VVFTTAASDMETVSEAVRCGVFDYLIKPI 109
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
32-105 6.08e-03

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: 36.48  E-value: 6.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499657480  32 AGDGASCLSLARGELPDLILLDWALPDVPGLEVLRHLRAD-PATRdipVIMISASRDPAIRLQALAEGADDFLAK 105
Cdd:cd19930   30 ASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREElPDTK---VLIVTTFGRPGYFRRALAAGVDGYVLK 101
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
4-57 7.94e-03

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: 34.47  E-value: 7.94e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 499657480     4 KVLITDNVATNRIVLKVKLAAACYLPLMAGDGASCLSLARGELPDLILLDWALP 57
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
 
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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