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Conserved domains on  [gi|685887246|ref|WP_031628685|]
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MULTISPECIES: diguanylate cyclase [Pseudomonas]

Protein Classification

sensor domain-containing diguanylate cyclase( domain architecture ID 13413304)

sensor domain-containing diguanylate cyclase (GGDEF) with a GAF family sensor domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
352-503 2.21e-49

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: 166.96  E-value: 2.21e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 352 RRDPLTNLLNHGQFMASAATVLAE----GPPSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVLTDSLRTDDYVGRLGG 427
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARarrsGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685887246 428 EEFGIVMVGANPSQAKMVVDRLRSIFTAIQFqsEDGTSFSCSFSAGVAILN---VSVKEAHRAADEALYSAKRSGRDRV 503
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFF--IDGQEIRVTASIGIATYPedgEDAEELLRRADEALYRAKRSGRNRV 157
COG5001 super family cl34859
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
188-505 4.20e-35

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


The actual alignment was detected with superfamily member COG5001:

Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 139.14  E-value: 4.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 188 RRTATELGQVRILGLDDDIRNLRSLFRSRNRDIEIEGYRVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRF 267
Cdd:COG5001   84 ALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLA 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 268 RPDVLVTDFHMPEANGDVVASIIRQDRDATIPIIFLSRESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISRSKVL 347
Cdd:COG5001  164 LLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRA 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 348 ESRMRR----DPLTNLLNHGQFMASAATVLA----EGPPSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVLTDSLRTD 419
Cdd:COG5001  244 EERLRHlayhDPLTGLPNRRLFLDRLEQALArarrSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREG 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 420 DYVGRLGGEEFGIVMVG-ANPSQAKMVVDRLRSIFTA-IQFqseDGTSFSCSFSAGVAILNVSVKEAH---RAADEALYS 494
Cdd:COG5001  324 DTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAEpFEL---DGHELYVSASIGIALYPDDGADAEellRNADLAMYR 400
                        330
                 ....*....|.
gi 685887246 495 AKRSGRDRVEI 505
Cdd:COG5001  401 AKAAGRNRYRF 411
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
352-503 2.21e-49

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: 166.96  E-value: 2.21e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 352 RRDPLTNLLNHGQFMASAATVLAE----GPPSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVLTDSLRTDDYVGRLGG 427
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARarrsGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685887246 428 EEFGIVMVGANPSQAKMVVDRLRSIFTAIQFqsEDGTSFSCSFSAGVAILN---VSVKEAHRAADEALYSAKRSGRDRV 503
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFF--IDGQEIRVTASIGIATYPedgEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
249-506 1.52e-47

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: 165.92  E-value: 1.52e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 249 LIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRDATIPIIFLSRESNAEKQLLALSRGADGFVQKPL 328
Cdd:COG2199   12 LLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 329 KRGAFIKALKSIISRSKVLESRMRRDPLTNLLNHGQFMASAATVLA----EGPPSSLVLIDIDHFKSVNDTFGHPVGDRV 404
Cdd:COG2199   92 LLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELArarrEGRPLALLLIDLDHFKRINDTYGHAAGDEV 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 405 LVGLAEVLTDSLRTDDYVGRLGGEEFGIVMVGANPSQAKMVVDRLRSIFTAIQFQSeDGTSFSCSFSAGVAILNVSVKEA 484
Cdd:COG2199  172 LKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFEL-EGKELRVTVSIGVALYPEDGDSA 250
                        250       260
                 ....*....|....*....|....*
gi 685887246 485 H---RAADEALYSAKRSGRDRVEIA 506
Cdd:COG2199  251 EellRRADLALYRAKRAGRNRVVVY 275
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
353-502 1.52e-40

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: 143.55  E-value: 1.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246  353 RDPLTNLLNHGQFMASAATVLA----EGPPSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVLTDSLRTDDYVGRLGGE 428
Cdd:pfam00990   3 HDPLTGLPNRRYFEEQLEQELQralrEGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGGD 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685887246  429 EFGIVMVGANPSQAKMVVDRLRSIFTAIQFQ-SEDGTSFSCSFSAGVAIL---NVSVKEAHRAADEALYSAKRSGRDR 502
Cdd:pfam00990  83 EFAILLPETSLEGAQELAERIRRLLAKLKIPhTVSGLPLYVTISIGIAAYpndGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
352-506 6.46e-40

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 142.00  E-value: 6.46e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246   352 RRDPLTNLLNHGQFMASAATVLAEGP----PSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVLTDSLRTDDYVGRLGG 427
Cdd:smart00267   4 FRDPLTGLPNRRYFEEELEQELQRAQrqgsPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLGG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246   428 EEFGIVMVGANPSQAKMVVDRLRSIFTAIQFQseDGTSFSCSFSAGVAILNVSVKEAH---RAADEALYSAKRSGRDRVE 504
Cdd:smart00267  84 DEFALLLPETSLEEAIALAERILQQLREPIII--HGIPLYLTISIGVAAYPNPGEDAEdllKRADTALYQAKKAGRNQVA 161

                   ..
gi 685887246   505 IA 506
Cdd:smart00267 162 VY 163
PRK09894 PRK09894
diguanylate cyclase; Provisional
332-503 5.24e-36

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 135.58  E-value: 5.24e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 332 AFIKALKSIisRSKVLESRMRRDPLTNLLNHGQFMAS--AATVLAEGPPSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLA 409
Cdd:PRK09894 112 SFTAALTDY--KIYLLTIRSNMDVLTGLPGRRVLDESfdHQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLA 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 410 EVLTDSLRTDDYVGRLGGEEFGIVMVGANPSQAKMVVDRLRSIFTAIQFQSEDGtSFSCSFSAGVAIL--NVSVKEAHRA 487
Cdd:PRK09894 190 TYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDG-RINITATFGVSRAfpEETLDVVIGR 268
                        170
                 ....*....|....*.
gi 685887246 488 ADEALYSAKRSGRDRV 503
Cdd:PRK09894 269 ADRAMYEGKQTGRNRV 284
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
353-506 1.55e-35

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: 130.15  E-value: 1.55e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246  353 RDPLTNLLNHGQFMASAATVLA----EGPPSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVLTDSLRTDDYVGRLGGE 428
Cdd:TIGR00254   4 RDPLTGLYNRRYLEEMLDSELKrarrFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246  429 EFGIVMVGANPSQAKMVVDRLRSIFTAIQFQSEDGTSFSCSFSAGVAILN---VSVKEAHRAADEALYSAKRSGRDRVEI 505
Cdd:TIGR00254  84 EFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPghgLTLEELLKRADEALYQAKKAGRNRVVV 163

                  .
gi 685887246  506 A 506
Cdd:TIGR00254 164 A 164
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
188-505 4.20e-35

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: 139.14  E-value: 4.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 188 RRTATELGQVRILGLDDDIRNLRSLFRSRNRDIEIEGYRVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRF 267
Cdd:COG5001   84 ALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLA 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 268 RPDVLVTDFHMPEANGDVVASIIRQDRDATIPIIFLSRESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISRSKVL 347
Cdd:COG5001  164 LLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRA 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 348 ESRMRR----DPLTNLLNHGQFMASAATVLA----EGPPSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVLTDSLRTD 419
Cdd:COG5001  244 EERLRHlayhDPLTGLPNRRLFLDRLEQALArarrSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREG 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 420 DYVGRLGGEEFGIVMVG-ANPSQAKMVVDRLRSIFTA-IQFqseDGTSFSCSFSAGVAILNVSVKEAH---RAADEALYS 494
Cdd:COG5001  324 DTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAEpFEL---DGHELYVSASIGIALYPDDGADAEellRNADLAMYR 400
                        330
                 ....*....|.
gi 685887246 495 AKRSGRDRVEI 505
Cdd:COG5001  401 AKAAGRNRYRF 411
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
228-327 4.26e-19

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: 82.28  E-value: 4.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 228 LLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQdRDATIPIIFLSRES 307
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRE-LPPDIPVIVLTAKA 79
                         90       100
                 ....*....|....*....|
gi 685887246 308 NAEKQLLALSRGADGFVQKP 327
Cdd:cd00156   80 DEEDAVRALELGADDYLVKP 99
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
227-338 5.42e-16

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: 73.72  E-value: 5.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246  227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQdRDATIPIIFLSRE 306
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRR-RDPTTPVIILTAH 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 685887246  307 SNAEKQLLALSRGADGFVQKPLKRGAFIKALK 338
Cdd:pfam00072  80 GDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
PRK10610 PRK10610
chemotaxis protein CheY;
226-343 8.63e-09

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 53.82  E-value: 8.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLivEHIQHPSQVLEALSRFRP---DVLVTDFHMPEANGDVVASIIRQDRD-ATIPII 301
Cdd:PRK10610   7 KFLVVDDFSTMRRIVRNLLKELGF--NNVEEAEDGVDALNKLQAggfGFVISDWNMPNMDGLELLKTIRADGAmSALPVL 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 685887246 302 FLSRESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISR 343
Cdd:PRK10610  85 MVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEK 126
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
225-279 3.35e-07

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 47.18  E-value: 3.35e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 685887246   225 YRVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMP 279
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
 
Name Accession Description Interval E-value
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
352-503 2.21e-49

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: 166.96  E-value: 2.21e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 352 RRDPLTNLLNHGQFMASAATVLAE----GPPSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVLTDSLRTDDYVGRLGG 427
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARarrsGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685887246 428 EEFGIVMVGANPSQAKMVVDRLRSIFTAIQFqsEDGTSFSCSFSAGVAILN---VSVKEAHRAADEALYSAKRSGRDRV 503
Cdd:cd01949   81 DEFAILLPGTDLEEAEALAERLREAIEEPFF--IDGQEIRVTASIGIATYPedgEDAEELLRRADEALYRAKRSGRNRV 157
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
249-506 1.52e-47

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: 165.92  E-value: 1.52e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 249 LIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRDATIPIIFLSRESNAEKQLLALSRGADGFVQKPL 328
Cdd:COG2199   12 LLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 329 KRGAFIKALKSIISRSKVLESRMRRDPLTNLLNHGQFMASAATVLA----EGPPSSLVLIDIDHFKSVNDTFGHPVGDRV 404
Cdd:COG2199   92 LLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELArarrEGRPLALLLIDLDHFKRINDTYGHAAGDEV 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 405 LVGLAEVLTDSLRTDDYVGRLGGEEFGIVMVGANPSQAKMVVDRLRSIFTAIQFQSeDGTSFSCSFSAGVAILNVSVKEA 484
Cdd:COG2199  172 LKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFEL-EGKELRVTVSIGVALYPEDGDSA 250
                        250       260
                 ....*....|....*....|....*
gi 685887246 485 H---RAADEALYSAKRSGRDRVEIA 506
Cdd:COG2199  251 EellRRADLALYRAKRAGRNRVVVY 275
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
353-502 1.52e-40

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: 143.55  E-value: 1.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246  353 RDPLTNLLNHGQFMASAATVLA----EGPPSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVLTDSLRTDDYVGRLGGE 428
Cdd:pfam00990   3 HDPLTGLPNRRYFEEQLEQELQralrEGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGGD 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685887246  429 EFGIVMVGANPSQAKMVVDRLRSIFTAIQFQ-SEDGTSFSCSFSAGVAIL---NVSVKEAHRAADEALYSAKRSGRDR 502
Cdd:pfam00990  83 EFAILLPETSLEGAQELAERIRRLLAKLKIPhTVSGLPLYVTISIGIAAYpndGEDPEDLLKRADTALYQAKQAGRNR 160
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
352-506 6.46e-40

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 142.00  E-value: 6.46e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246   352 RRDPLTNLLNHGQFMASAATVLAEGP----PSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVLTDSLRTDDYVGRLGG 427
Cdd:smart00267   4 FRDPLTGLPNRRYFEEELEQELQRAQrqgsPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLGG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246   428 EEFGIVMVGANPSQAKMVVDRLRSIFTAIQFQseDGTSFSCSFSAGVAILNVSVKEAH---RAADEALYSAKRSGRDRVE 504
Cdd:smart00267  84 DEFALLLPETSLEEAIALAERILQQLREPIII--HGIPLYLTISIGVAAYPNPGEDAEdllKRADTALYQAKKAGRNQVA 161

                   ..
gi 685887246   505 IA 506
Cdd:smart00267 162 VY 163
PRK09894 PRK09894
diguanylate cyclase; Provisional
332-503 5.24e-36

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 135.58  E-value: 5.24e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 332 AFIKALKSIisRSKVLESRMRRDPLTNLLNHGQFMAS--AATVLAEGPPSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLA 409
Cdd:PRK09894 112 SFTAALTDY--KIYLLTIRSNMDVLTGLPGRRVLDESfdHQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLA 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 410 EVLTDSLRTDDYVGRLGGEEFGIVMVGANPSQAKMVVDRLRSIFTAIQFQSEDGtSFSCSFSAGVAIL--NVSVKEAHRA 487
Cdd:PRK09894 190 TYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDG-RINITATFGVSRAfpEETLDVVIGR 268
                        170
                 ....*....|....*.
gi 685887246 488 ADEALYSAKRSGRDRV 503
Cdd:PRK09894 269 ADRAMYEGKQTGRNRV 284
pleD PRK09581
response regulator PleD; Reviewed
221-503 7.07e-36

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 138.88  E-value: 7.07e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 221 EIEGYRVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRfRPDVLVTDFHMPEANGDVVASIIR-QDRDATIP 299
Cdd:PRK09581 152 KDEDGRILLVDDDVSQAERIANILKEEFRVVVVSDPSEALFNAAET-NYDLVIVSANFENYDPLRLCSQLRsKERTRYVP 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 300 IIFLSRESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISRSKV-------LESRMR---RDPLTNLLNH----GQF 365
Cdd:PRK09581 231 ILLLVDEDDDPRLVKALELGVNDYLMRPIDKNELLARVRTQIRRKRYqdalrnnLEQSIEmavTDGLTGLHNRryfdMHL 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 366 MASAATVLAEGPPSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVLTDSLRTDDYVGRLGGEEFGIVMVGANPSQAKMV 445
Cdd:PRK09581 311 KNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAV 390
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685887246 446 VDRLRSIFTAIQFQSEDG-TSFSCSFSAGVAIL---NVSVKEAHRAADEALYSAKRSGRDRV 503
Cdd:PRK09581 391 AERIRRKIAEEPFIISDGkERLNVTVSIGVAELrpsGDTIEALIKRADKALYEAKNTGRNRV 452
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
353-506 1.55e-35

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: 130.15  E-value: 1.55e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246  353 RDPLTNLLNHGQFMASAATVLA----EGPPSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVLTDSLRTDDYVGRLGGE 428
Cdd:TIGR00254   4 RDPLTGLYNRRYLEEMLDSELKrarrFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246  429 EFGIVMVGANPSQAKMVVDRLRSIFTAIQFQSEDGTSFSCSFSAGVAILN---VSVKEAHRAADEALYSAKRSGRDRVEI 505
Cdd:TIGR00254  84 EFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPghgLTLEELLKRADEALYQAKKAGRNRVVV 163

                  .
gi 685887246  506 A 506
Cdd:TIGR00254 164 A 164
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
188-505 4.20e-35

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: 139.14  E-value: 4.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 188 RRTATELGQVRILGLDDDIRNLRSLFRSRNRDIEIEGYRVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRF 267
Cdd:COG5001   84 ALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLA 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 268 RPDVLVTDFHMPEANGDVVASIIRQDRDATIPIIFLSRESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISRSKVL 347
Cdd:COG5001  164 LLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRA 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 348 ESRMRR----DPLTNLLNHGQFMASAATVLA----EGPPSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVLTDSLRTD 419
Cdd:COG5001  244 EERLRHlayhDPLTGLPNRRLFLDRLEQALArarrSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREG 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 420 DYVGRLGGEEFGIVMVG-ANPSQAKMVVDRLRSIFTA-IQFqseDGTSFSCSFSAGVAILNVSVKEAH---RAADEALYS 494
Cdd:COG5001  324 DTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAEpFEL---DGHELYVSASIGIALYPDDGADAEellRNADLAMYR 400
                        330
                 ....*....|.
gi 685887246 495 AKRSGRDRVEI 505
Cdd:COG5001  401 AKAAGRNRYRF 411
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
347-503 1.94e-31

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 127.82  E-value: 1.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 347 LESRMRRDPLTNLLNHG----QFMASAATVLAEGPPSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVLTDSLRTDDYV 422
Cdd:PRK15426 394 LQWQAWHDPLTRLYNRGalfeKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVA 473
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 423 GRLGGEEFGIVMVGANPSQAKMVVDRLRSIFTAIQFQSEDGTSFSCSFSAGVAilnvsvkEAHR-----------AADEA 491
Cdd:PRK15426 474 GRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTTIRISASLGVS-------SAEEdgdydfeqlqsLADRR 546
                        170
                 ....*....|..
gi 685887246 492 LYSAKRSGRDRV 503
Cdd:PRK15426 547 LYLAKQAGRNRV 558
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
225-496 8.90e-28

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: 109.23  E-value: 8.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 225 YRVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQD-RDATIPIIFL 303
Cdd:COG3706    2 ARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADpRTADIPIIFL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 304 SRESNAEKQLLALSRGADGFVQKPLKRGAFIKALksiisrskvlesrmrrdpltnllnhgqfmasaatvlaegppsslvl 383
Cdd:COG3706   82 TALDDEEDRARALEAGADDYLTKPFDPEELLARV---------------------------------------------- 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 384 ididhfksvndtfghpvgdrvlvglaevltdslrtdDYVGRLGGEEFGIVMVGANPSQAKMVVDRLRSIFtaiqfqsEDG 463
Cdd:COG3706  116 ------------------------------------DLVARYGGEEFAILLPGTDLEGALAVAERIREAV-------AEL 152
                        250       260       270
                 ....*....|....*....|....*....|...
gi 685887246 464 TSFSCSFSAGVAILNvsvkeAHRAADeALYSAK 496
Cdd:COG3706  153 PSLRVTVSIGVAGDS-----LLKRAD-ALYQAR 179
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
223-345 2.17e-24

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: 98.00  E-value: 2.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 223 EGYRVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQD-RDATIPII 301
Cdd:COG0784    4 GGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALpRLPDIPII 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 685887246 302 FLSRESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISRSK 345
Cdd:COG0784   84 ALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARAS 127
adrA PRK10245
diguanylate cyclase AdrA; Provisional
379-506 5.27e-24

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 103.37  E-value: 5.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 379 SSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVLTDSLRTDDYVGRLGGEEFGIVMVG--ANPSQAKM--VVDRLRSIft 454
Cdd:PRK10245 237 ATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGtpAESAITAMsrVHEGLNTL-- 314
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685887246 455 aiqfqsedgtSFSCS------FSAGVAILNVSV---KEAHRAADEALYSAKRSGRDRVEIA 506
Cdd:PRK10245 315 ----------RLPNApqvtlrISVGVAPLNPQMshyREWLKSADLALYKAKNAGRNRTEVA 365
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
346-503 2.39e-22

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 101.29  E-value: 2.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246  346 VLESR--MRR-------DPLTNLLNHGQF----MASAATVLAEGPPSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVL 412
Cdd:PRK09776  651 VTESRkmLRQlsysashDALTHLANRASFekqlRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLM 730
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246  413 TDSLRTDDYVGRLGGEEFGIVMVGANPSQAKMVVDRLRSIFTAIQFQSEdGTSFSCSFSAGVAILNVS---VKEAHRAAD 489
Cdd:PRK09776  731 LSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWE-GRVYRVGASAGITLIDANnhqASEVMSQAD 809
                         170
                  ....*....|....
gi 685887246  490 EALYSAKRSGRDRV 503
Cdd:PRK09776  810 IACYAAKNAGRGRV 823
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
228-327 4.26e-19

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: 82.28  E-value: 4.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 228 LLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQdRDATIPIIFLSRES 307
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRE-LPPDIPVIVLTAKA 79
                         90       100
                 ....*....|....*....|
gi 685887246 308 NAEKQLLALSRGADGFVQKP 327
Cdd:cd00156   80 DEEDAVRALELGADDYLVKP 99
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
226-343 4.92e-19

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: 85.99  E-value: 4.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRD-ATIPIIFLS 304
Cdd:COG3437    8 TVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPStRDIPVIFLT 87
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 685887246 305 RESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISR 343
Cdd:COG3437   88 ALADPEDRERALEAGADDYLTKPFDPEELLARVRNALEL 126
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
225-362 4.35e-18

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: 82.70  E-value: 4.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 225 YRVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDrDATIPIIFLS 304
Cdd:COG0745    2 PRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRAR-PSDIPIIMLT 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 685887246 305 RESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISRSKVleSRMRRDPLTNLLNH 362
Cdd:COG0745   81 ARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAA--EVLRVGDLLDLAAR 136
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
226-356 2.82e-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: 83.86  E-value: 2.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQdRDATIPIIFLSR 305
Cdd:COG2204    4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRA-LDPDLPVILLTG 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 685887246 306 ESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISRSKVLESRMRRDPL 356
Cdd:COG2204   83 YGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSGL 133
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
225-354 9.03e-17

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 76.93  E-value: 9.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 225 YRVLLLDDSRTDAYLARKFLTEEGL--IVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQdRDATIPIIF 302
Cdd:COG4565    4 IRVLIVEDDPMVAELLRRYLERLPGfeVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRA-RGPDVDVIV 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 685887246 303 LSRESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISRSKVLESRMRRD 354
Cdd:COG4565   83 ITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQEED 134
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
227-338 5.42e-16

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: 73.72  E-value: 5.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246  227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQdRDATIPIIFLSRE 306
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRR-RDPTTPVIILTAH 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 685887246  307 SNAEKQLLALSRGADGFVQKPLKRGAFIKALK 338
Cdd:pfam00072  80 GDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
347-475 1.29e-15

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 79.81  E-value: 1.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 347 LESRMRRDPLTNLLNHGQFMASAATVLAEGPPSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVLTDSLRTDDYVGRLG 426
Cdd:PRK11359 372 IEQLIQFDPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIE 451
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 685887246 427 GEEFGIVMVGANPSQAKMVVDRLRSIFTA-IQFqseDGTSFSCSFSAGVA 475
Cdd:PRK11359 452 GTQFVLVSLENDVSNITQIADELRNVVSKpIMI---DDKPFPLTLSIGIS 498
PRK09966 PRK09966
diguanylate cyclase DgcN;
354-502 2.08e-15

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 78.12  E-value: 2.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 354 DPLTNLLNHGQFMASAATVLAEGPP---SSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVLTD--SLRTDDYvgRLGGE 428
Cdd:PRK09966 251 DPLTGLANRAAFRSGINTLMNNSDArktSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEfgGLRHKAY--RLGGD 328
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685887246 429 EFGIVMVGANP-SQAKMVVDRLRSIFTaIQFQSEDGTSFSCSFSAGVAIL--NVSVKEAHRAADEALYSAKRSGRDR 502
Cdd:PRK09966 329 EFAMVLYDVQSeSEVQQICSALTQIFN-LPFDLHNGHQTTMTLSIGYAMTieHASAEKLQELADHNMYQAKHQRAEK 404
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
227-342 1.17e-14

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: 70.43  E-value: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRD-ATIPIIFLSR 305
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDlKDIPVILLTT 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 685887246 306 ESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIIS 342
Cdd:cd17598   81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYILV 117
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
226-330 9.99e-14

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: 67.47  E-value: 9.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLI-VEHIQHPSQVLEALSRFRPDVLVTDFHMPEANG-DVVASIIRQDRDATIPIIFL 303
Cdd:cd17551    2 RILIVDDNPTNLLLLEALLRSAGYLeVVSFTDPREALAWCRENPPDLILLDYMMPGMDGlEFIRRLRALPGLEDVPIVMI 81
                         90       100
                 ....*....|....*....|....*..
gi 685887246 304 SRESNAEKQLLALSRGADGFVQKPLKR 330
Cdd:cd17551   82 TADTDREVRLRALEAGATDFLTKPFDP 108
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
354-500 2.93e-13

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 72.41  E-value: 2.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 354 DPLTNLLNHG--QFMASAATVLAEGPPSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVLTDSLRTDDYVGRLGGEEFg 431
Cdd:PRK10060 240 DSITGLPNRNaiQELIDHAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEF- 318
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685887246 432 IVMVgANPSQAKM------VVDRLRSIFTA--IQFQSedgtsfSCSFSAGVAILNVSVKEAH-RAADEALYSAKRSGR 500
Cdd:PRK10060 319 LVLA-SHTSQAALeamasrILTRLRLPFRIglIEVYT------GCSIGIALAPEHGDDSESLiRSADTAMYTAKEGGR 389
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
227-341 4.00e-13

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: 65.77  E-value: 4.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDrdATIPIIFLSRE 306
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQI--SNVPIIFISSR 78
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 685887246 307 SNAEKQLLALSRGADGFVQKPLKRGAFIKALKSII 341
Cdd:cd18159   79 DDNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
226-327 6.23e-13

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: 64.79  E-value: 6.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEG--LIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQdRDATIPIIFL 303
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRE-LDPDTKIIIL 79
                         90       100
                 ....*....|....*....|....
gi 685887246 304 SRESNAEKQLLALSRGADGFVQKP 327
Cdd:COG4753   80 SGYSDFEYAQEAIKLGADDYLLKP 103
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
227-337 7.03e-13

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: 65.18  E-value: 7.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQD--RDATIPIIFLS 304
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELegGGRRTPIIALT 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 685887246 305 RESNAEKQLLALSRGADGFVQKPLKRGAFIKAL 337
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
226-340 5.93e-12

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: 62.82  E-value: 5.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEhIQHPSQVLEAL----------SRFRPDVLVTDFHMPEANGDVVASIIRQDRD 295
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGVPNE-LHVVRDGEEALdflrgegeyaDAPRPDLILLDLNMPRMDGFEVLREIKADPD 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 685887246 296 -ATIPIIFLSrESNAEKQLL-ALSRGADGFVQKPLKRGAFIKALKSI 340
Cdd:cd17557   80 lRRIPVVVLT-TSDAEEDIErAYELGANSYIVKPVDFEEFVEAIRSL 125
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
224-354 2.42e-11

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: 62.67  E-value: 2.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 224 GYRVLLLDDSRTDAYLARKFLTEEG-LIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRDAtiPIIF 302
Cdd:COG3707    3 GLRVLVVDDEPLRRADLREGLREAGyEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERPA--PVIL 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 685887246 303 LSRESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISRSKVLEsRMRRD 354
Cdd:COG3707   81 LTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARFRELR-ALRRE 131
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
228-327 3.17e-11

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: 59.73  E-value: 3.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 228 LLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRdATIPIIFLS-RE 306
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKG-SDIPIIMLTaKD 79
                         90       100
                 ....*....|....*....|.
gi 685887246 307 SNAEKqLLALSRGADGFVQKP 327
Cdd:cd17574   80 EEEDK-VLGLELGADDYITKP 99
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
226-327 7.17e-11

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: 59.66  E-value: 7.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEG-LIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANG-DVVASIIRQDRDATIPIIFL 303
Cdd:cd19923    2 KVLVVDDFSTMRRIIKNLLKELGfNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGlELLKTIRADGALSHLPVLMV 81
                         90       100
                 ....*....|....*....|....
gi 685887246 304 SRESNAEKQLLALSRGADGFVQKP 327
Cdd:cd19923   82 TAEAKKENVIAAAQAGVNNYIVKP 105
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
226-343 9.78e-11

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


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 58.92  E-value: 9.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRDAtiPIIFLSR 305
Cdd:cd19939    1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHSHV--PILMLTA 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 685887246 306 ESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISR 343
Cdd:cd19939   79 RTEEMDRVLGLEMGADDYLCKPFSPRELLARVRALLRR 116
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
226-344 1.35e-09

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: 55.82  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDrDATIPIIFLSR 305
Cdd:cd17615    1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRAD-GPDVPVLFLTA 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 685887246 306 ESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISRS 344
Cdd:cd17615   80 KDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALLRRS 118
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
227-327 1.78e-09

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: 54.82  E-value: 1.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQD-RDATIPIIFLSR 305
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADpATRHIPVIFLTA 80
                         90       100
                 ....*....|....*....|..
gi 685887246 306 ESNAEKQLLALSRGADGFVQKP 327
Cdd:cd19920   81 LTDTEDKVKGFELGAVDYITKP 102
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
226-329 3.30e-09

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: 54.69  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRqdRDATIPIIFLSR 305
Cdd:cd17622    2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLR--PKYQGPILLLTA 79
                         90       100
                 ....*....|....*....|....
gi 685887246 306 ESNAEKQLLALSRGADGFVQKPLK 329
Cdd:cd17622   80 LDSDIDHILGLELGADDYVVKPVE 103
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
227-343 3.50e-09

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: 54.62  E-value: 3.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRDatIPIIFLSRE 306
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTSQ--VPVLMLTAR 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 685887246 307 SNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISR 343
Cdd:cd17623   79 GDDIDRILGLELGADDYLPKPFNPRELVARIRAILRR 115
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
225-327 3.51e-09

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: 54.71  E-value: 3.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 225 YRVLLLDDSRtdayLARKFLTEeglIVE---HIQ------HPSQVLEALSRFRPDVLVTDFHMPEANG-DVVASIIRQDR 294
Cdd:cd17541    1 IRVLIVDDSA----VMRKLLSR---ILEsdpDIEvvgtarDGEEALEKIKELKPDVITLDIEMPVMDGlEALRRIMAERP 73
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 685887246 295 datIPIIFLS--RESNAEKQLLALSRGADGFVQKP 327
Cdd:cd17541   74 ---TPVVMVSslTEEGAEITLEALELGAVDFIAKP 105
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
378-476 5.09e-09

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: 54.67  E-value: 5.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 378 PSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVLTDSL-RTDDYVGRLGGEEFGIVMVGANPSQAKMVVDRLRSIFTAI 456
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80
                         90       100
                 ....*....|....*....|
gi 685887246 457 QFQSEDGTSFSCSFSAGVAI 476
Cdd:cd07556   81 NQSEGNPVRVRIGIHTGPVV 100
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
226-339 5.25e-09

phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC domain; This subfamily is composed of uncharacterized proteins containing an N-terminal REC domain and a C-terminal CheC domain that may function as the output/effector domain of a response regulator. CheC is a CheY-P phosphatase, affecting the level of phosphorylated CheY which controls the sense of flagella rotation and determine swimming behavior of chemotactic bacteria. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 54.08  E-value: 5.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRtdayLARKFLT-----EEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANG-DVVASIirQDRDATIP 299
Cdd:cd17593    2 KVLICDDSS----MARKQLAralpaDWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGyEVLEAL--PVEQLETK 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 685887246 300 IIFLSRESNAEKQLLALSRGADGFVQKPLKRGAFIKALKS 339
Cdd:cd17593   76 VIVVSGDVQPEAKERVLELGALAFLKKPFDPEKLAQLLEE 115
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
226-329 7.62e-09

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: 53.63  E-value: 7.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRDatIPIIFLSR 305
Cdd:cd17626    2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAESG--VPIVMLTA 79
                         90       100
                 ....*....|....*....|....
gi 685887246 306 ESNAEKQLLALSRGADGFVQKPLK 329
Cdd:cd17626   80 KSDTVDVVLGLESGADDYVAKPFK 103
PRK10610 PRK10610
chemotaxis protein CheY;
226-343 8.63e-09

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 53.82  E-value: 8.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLivEHIQHPSQVLEALSRFRP---DVLVTDFHMPEANGDVVASIIRQDRD-ATIPII 301
Cdd:PRK10610   7 KFLVVDDFSTMRRIVRNLLKELGF--NNVEEAEDGVDALNKLQAggfGFVISDWNMPNMDGLELLKTIRADGAmSALPVL 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 685887246 302 FLSRESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISR 343
Cdd:PRK10610  85 MVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEK 126
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
227-327 8.65e-09

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: 53.23  E-value: 8.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRD-ATIPIIFLS- 304
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWlANTPAIALTg 80
                         90       100
                 ....*....|....*....|....*
gi 685887246 305 --RESNAEKqllALSRGADGFVQKP 327
Cdd:cd17580   81 ygQPEDRER---ALEAGFDAHLVKP 102
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
225-340 1.91e-08

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: 52.67  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 225 YRVLLLDDSRTDAYLARKFLTEEGL-IVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDrDATIPIIFL 303
Cdd:cd17542    1 KKVLIVDDAAFMRMMLKDILTKAGYeVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKI-DPNAKVIMC 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 685887246 304 SRESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSI 340
Cdd:cd17542   80 SAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKV 116
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
226-327 2.42e-08

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: 52.00  E-value: 2.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGdvvASIIRQDRDAT-IPIIFLS 304
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDG---LTLCREIRRFSdVPIIMVT 77
                         90       100
                 ....*....|....*....|...
gi 685887246 305 RESNAEKQLLALSRGADGFVQKP 327
Cdd:cd19938   78 ARVEEIDRLLGLELGADDYICKP 100
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
259-342 2.70e-08

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: 52.13  E-value: 2.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 259 QVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQdRDATIPIIFLSRESNAEKQLLALSRGADGFVQKPLKRGAFIKALK 338
Cdd:cd17535   35 EALALLRELRPDVVLMDLSMPGMDGIEALRRLRR-RYPDLKVIVLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIR 113

                 ....
gi 685887246 339 SIIS 342
Cdd:cd17535  114 AVAA 117
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
227-327 3.13e-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: 51.60  E-value: 3.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQD---RDatIPIIFL 303
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSsalKD--TPIIML 78
                         90       100
                 ....*....|....*....|....
gi 685887246 304 SRESNAEKQLLALSRGADGFVQKP 327
Cdd:cd17602   79 TGKDGLVDRIRAKMAGASGYLTKP 102
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
225-354 3.31e-08

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 56.01  E-value: 3.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 225 YRVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQdRDATIPIIFLS 304
Cdd:PRK11361   5 NRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRS-HETRTPVILMT 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 685887246 305 RESNAEKQLLALSRGADGFVQKPLKrgafIKALKSIISRSKVLESrMRRD 354
Cdd:PRK11361  84 AYAEVETAVEALRCGAFDYVIKPFD----LDELNLIVQRALQLQS-MKKE 128
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
198-327 3.52e-08

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: 51.34  E-value: 3.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 198 RILGLDDDIRNLRSLfrsrNRDIEIEGYRVLLLDDSRtdaylarkflteeglivehiqhpsQVLEALSRFRPDVLVTDFH 277
Cdd:cd17538    1 KILVVDDEPANRELL----EALLSAEGYEVLTADSGQ------------------------EALALAEEELPDLILLDVM 52
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 685887246 278 MPEANGDVVASIIRQDRD-ATIPIIFLSRESNAEKQLLALSRGADGFVQKP 327
Cdd:cd17538   53 MPGMDGFEVCRRLKEDPEtRHIPVIMITALDDREDRIRGLEAGADDFLSKP 103
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
227-327 4.91e-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: 50.84  E-value: 4.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRD-ATIPIIFLSR 305
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADfDTIPVIFLTA 80
                         90       100
                 ....*....|....*....|..
gi 685887246 306 ESNAEKQLLALSRGADGFVQKP 327
Cdd:cd19927   81 KGMTSDRIKGYNAGCDGYLSKP 102
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
227-327 6.07e-08

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: 50.52  E-value: 6.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDrdATIPIIFLSRE 306
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQK--STLPVIFLTSK 78
                         90       100
                 ....*....|....*....|.
gi 685887246 307 SNAEKQLLALSRGADGFVQKP 327
Cdd:cd19936   79 DDEIDEVFGLRMGADDYITKP 99
orf27 CHL00148
Ycf27; Reviewed
225-327 7.17e-08

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 53.57  E-value: 7.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 225 YRVLLLDDsrtDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFR---PDVLVTDFHMPEANGDVVASIIRQDRDatIPII 301
Cdd:CHL00148   7 EKILVVDD---EAYIRKILETRLSIIGYEVITASDGEEALKLFRkeqPDLVILDVMMPKLDGYGVCQEIRKESD--VPII 81
                         90       100
                 ....*....|....*....|....*.
gi 685887246 302 FLSRESNAEKQLLALSRGADGFVQKP 327
Cdd:CHL00148  82 MLTALGDVSDRITGLELGADDYVVKP 107
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
227-327 9.14e-08

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: 50.45  E-value: 9.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRP---------DVLVTDFHMPEANGDVVASIIRQD-RDA 296
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKegndlskelDLIITDIEMPKMDGYELTFELRDDpRLA 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 685887246 297 TIPIIFLSRESNAEKQLLALSRGADGFVQKP 327
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
227-353 1.17e-07

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: 50.57  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDsrtDAYL---ARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANG-DVVASIirQDRDATIPIIF 302
Cdd:cd17549    1 VLLVDD---DADVreaLQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGlELLAQI--RELDPDLPVIL 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 685887246 303 LSRESNAEKQLLALSRGADGFVQKPLKRGAFIKALK-SIISRSKVLESRMRR 353
Cdd:cd17549   76 ITGHGDVPMAVEAMRAGAYDFLEKPFDPERLLDVVRrALEKRRLVLENRRLR 127
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
227-343 1.38e-07

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: 50.11  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRDatIPIIFLSRE 306
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSN--VPIIMLTAK 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 685887246 307 SNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISR 343
Cdd:cd17614   79 DSEVDKVLGLELGADDYVTKPFSNRELLARVKANLRR 115
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
227-340 1.72e-07

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


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 49.55  E-value: 1.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRP--DVLVTDFHMPEANGDVVASIIRQDRDatIPIIFLS 304
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDefDLVITDVHMPDMDGFEFLELIRLEMD--LPVIMMS 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 685887246 305 RESNAEKQLLALSRGADGFVQKPLKrgafIKALKSI 340
Cdd:cd17584   79 ADGSTSTVMKGLAHGACDYLLKPVS----IEDLKNI 110
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
226-327 2.53e-07

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: 50.69  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQdRDATIPIIFLSR 305
Cdd:COG4567    6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRE-RDPDARIVVLTG 84
                         90       100
                 ....*....|....*....|..
gi 685887246 306 ESNAEKQLLALSRGADGFVQKP 327
Cdd:COG4567   85 YASIATAVEAIKLGADDYLAKP 106
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
227-327 2.84e-07

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 52.95  E-value: 2.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQdRDATIPIIFLSRE 306
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQ-RHPMLPVIIMTAH 84
                         90       100
                 ....*....|....*....|.
gi 685887246 307 SNAEKQLLALSRGADGFVQKP 327
Cdd:PRK10923  85 SDLDAAVSAYQQGAFDYLPKP 105
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
226-354 2.86e-07

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 51.34  E-value: 2.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRfRPDVLVTDFHMPEANGDVVASIIRQDRDAtiPIIFLSR 305
Cdd:PRK10955   3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDD-SIDLLLLDVMMPKKNGIDTLKELRQTHQT--PVIMLTA 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 685887246 306 ESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISRSKVLESRMRRD 354
Cdd:PRK10955  80 RGSELDRVLGLELGADDYLPKPFNDRELVARIRAILRRSHWSEQQQNND 128
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
225-279 3.35e-07

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 47.18  E-value: 3.35e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 685887246   225 YRVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMP 279
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
228-327 4.59e-07

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: 48.42  E-value: 4.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 228 LLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRD-ATIPIIFLSRE 306
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKtSSIPIIMLTAK 80
                         90       100
                 ....*....|....*....|.
gi 685887246 307 SNAEKQLLALSRGADGFVQKP 327
Cdd:cd19937   81 GEEFDKVLGLELGADDYITKP 101
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
225-328 5.68e-07

phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; This subfamily includes Escherichia coli TorR and ArcA, both OmpR family response regulators that mediate adaptation to changes in various respiratory growth conditions. The TorS-TorR two-component system (TCS) is responsible for the tight regulation of the torCAD operon, which encodes the trimethylamine N-oxide (TMAO) reductase respiratory system in response to anaerobic conditions and the presence of TMAO. The ArcA-ArcB TCS is involved in cell growth during anaerobiosis. ArcA is a global regulator that controls more than 30 operons involved in redox regulation (the Arc modulon). OmpR family DNA-binding response regulators are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 48.15  E-value: 5.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 225 YRVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGdvvASIIRQDRD-ATIPIIFL 303
Cdd:cd17619    1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDG---LSLTRELREqSEVGIILV 77
                         90       100
                 ....*....|....*....|....*
gi 685887246 304 SRESNAEKQLLALSRGADGFVQKPL 328
Cdd:cd17619   78 TGRDDEVDRIVGLEIGADDYVTKPF 102
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
198-326 6.13e-07

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: 47.99  E-value: 6.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 198 RILGLDDDiRNLRSLFRSrnrDIEIEGYRVLLLDDSRtdaylarkflteeglivehiqhpsQVLEALSRFRPDVLVTDFH 277
Cdd:cd17554    2 KILVVDDE-ENIRELYKE---ELEDEGYEVVTAGNGE------------------------EALEKLESEDPDLVILDIK 53
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 685887246 278 MPEANGDVVASIIRQdRDATIPIIFLSRESNAEKQLLALSrgADGFVQK 326
Cdd:cd17554   54 MPGMDGLETLRKIRE-KKPDLPVIICTAYSEYKSDFSSWA--ADAYVVK 99
ompR PRK09468
osmolarity response regulator; Provisional
223-327 8.29e-07

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 50.36  E-value: 8.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 223 EGYRVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGdvvASIIRQDRDA--TIPI 300
Cdd:PRK09468   4 ENYKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDG---LSICRRLRSQnnPTPI 80
                         90       100
                 ....*....|....*....|....*..
gi 685887246 301 IFLSRESNAEKQLLALSRGADGFVQKP 327
Cdd:PRK09468  81 IMLTAKGEEVDRIVGLEIGADDYLPKP 107
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
225-343 9.85e-07

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 49.81  E-value: 9.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 225 YRVLLLDDSRTDAYLARKFLTE-EGL-IVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANG-DVVASIirQDRDATIPII 301
Cdd:COG3279    2 MKILIVDDEPLARERLERLLEKyPDLeVVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGfELARQL--RELDPPPPII 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 685887246 302 FLSreSNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISR 343
Cdd:COG3279   80 FTT--AYDEYALEAFEVNAVDYLLKPIDEERLAKALEKAKER 119
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
226-341 1.19e-06

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: 47.30  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGdvvASIIRQDRD----ATIPII 301
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDG---IELIKELRKlpayKFTPIL 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 685887246 302 FLSRESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSII 341
Cdd:cd17562   79 MLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
226-327 1.57e-06

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: 46.88  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQdRDATIPIIFLSR 305
Cdd:cd19919    2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQ-RHPDLPVIIMTA 80
                         90       100
                 ....*....|....*....|..
gi 685887246 306 ESNAEKQLLALSRGADGFVQKP 327
Cdd:cd19919   81 HSDLDSAVSAYQGGAFEYLPKP 102
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
227-341 1.68e-06

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: 47.02  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGdvvASIIRQDRDATI--PIIFLS 304
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSG---YEVLRTLRLAKVktPILILS 77
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 685887246 305 RESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSII 341
Cdd:cd17616   78 GLADIEDKVKGLGFGADDYMTKPFHKDELVARIHAIV 114
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
226-343 2.03e-06

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: 46.64  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDS---RTDAylaRKFLTEEGL-IVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRDAtiPII 301
Cdd:cd19932    2 RVLIAEDEaliRMDL---REMLEEAGYeVVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENIA--PIV 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 685887246 302 FLSRESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISR 343
Cdd:cd19932   77 LLTAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAIAR 118
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
227-350 2.21e-06

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: 46.61  E-value: 2.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRDaTIPIIFLSRE 306
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGN-DLPILVLTAR 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 685887246 307 SNAEKQLLALSRGADGFVQKPLkrgafikALKSIISRSKVLESR 350
Cdd:cd17627   80 DSVSDRVAGLDAGADDYLVKPF-------ALEELLARVRALLRR 116
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
226-327 2.58e-06

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: 46.36  E-value: 2.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTdaylARKFLTEeglIVEHiqHPSQVLE------ALSRFR--PDV--LVTDFHMPEANGDVVASIIRQ--D 293
Cdd:cd17544    2 KVLVVDDSAT----SRNHLRA---LLRR--HNFQVLEaangqeALEVLEqhPDIklVITDYNMPEMDGFELVREIRKkyS 72
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 685887246 294 RDaTIPIIFLSreSNAEKQLLA--LSRGADGFVQKP 327
Cdd:cd17544   73 RD-QLAIIGIS--ASGDNALSArfIKAGANDFLTKP 105
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
226-339 3.23e-06

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: 45.99  E-value: 3.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRD-ATIPIIFLS 304
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPAtRDIPVIALT 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 685887246 305 R---ESNAEKQLLAlsrGADGFVQKPLKRGAFIKALKS 339
Cdd:cd17548   81 AyamKGDREKILEA---GCDGYISKPIDTREFLETVAK 115
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
225-384 4.01e-06

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 48.99  E-value: 4.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 225 YRVLLLDDSRtdayLARKFLTEeglIVEhiQHP-----------SQVLEALSRFRPDVLVTDFHMPEANG-DVVASIIRQ 292
Cdd:PRK00742   4 IRVLVVDDSA----FMRRLISE---ILN--SDPdievvgtapdgLEAREKIKKLNPDVITLDVEMPVMDGlDALEKIMRL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 293 DRdatIPIIFLSR--ESNAEKQLLALSRGADGFVQKPL--KRGAFIKALKSIISRSKVLESRMRRDPLTNLLNHGQFMAS 368
Cdd:PRK00742  75 RP---TPVVMVSSltERGAEITLRALELGAVDFVTKPFlgISLGMDEYKEELAEKVRAAARARVRALPPRAAAAARAAAA 151
                        170
                 ....*....|....*...
gi 685887246 369 AATVLAEGP--PSSLVLI 384
Cdd:PRK00742 152 APAALAAAPllSSKLVAI 169
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
226-326 5.99e-06

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: 45.48  E-value: 5.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHI-QHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIR---QDRDatIPII 301
Cdd:cd17575    2 MVLLVDDQAIIGEAVRRALADEEDIDFHYcSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRanpATRD--IPII 79
                         90       100
                 ....*....|....*....|....*
gi 685887246 302 FLSRESNAEKQLLALSRGADGFVQK 326
Cdd:cd17575   80 VLSTKEEPEVKSEAFALGANDYLVK 104
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
227-327 7.15e-06

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: 45.27  E-value: 7.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANG-DVVASIirQDRDATIPIIFLSR 305
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGmEILKWI--QERSLPTSVIVITA 78
                         90       100
                 ....*....|....*....|..
gi 685887246 306 ESNAEKQLLALSRGADGFVQKP 327
Cdd:cd17572   79 HGSVDIAVEAMRLGAYDFLEKP 100
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
227-343 8.48e-06

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 47.11  E-value: 8.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIV---EHIQHpsQVLEALSRfRPDVLVTDFHMPEANGdvvASIIRQDRD-ATIPIIF 302
Cdd:PRK10529   4 VLIVEDEQAIRRFLRTALEGDGMRVfeaETLQR--GLLEAATR-KPDLIILDLGLPDGDG---IEFIRDLRQwSAIPVIV 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 685887246 303 LSRESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISR 343
Cdd:PRK10529  78 LSARSEESDKIAALDAGADDYLSKPFGIGELQARLRVALRR 118
PRK15115 PRK15115
response regulator GlrR; Provisional
226-364 9.37e-06

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 47.91  E-value: 9.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIrQDRDATIPIIFLSR 305
Cdd:PRK15115   7 HLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEI-QKVQPGMPVIILTA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 306 ESNAEKQLLALSRGADGFVQKPLKRGAFIKAL----------------KSIISRSKVL-----ESRMRRDPLTNLLNHGQ 364
Cdd:PRK15115  86 HGSIPDAVAATQQGVFSFLTKPVDRDALYKAIddaleqsapatderwrEAIVTRSPLMlrlleQARMVAQSDVSVLINGQ 165
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
259-343 9.90e-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: 44.64  E-value: 9.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 259 QVLEALSRFRPDVLVTDFHMPEANG-DVVASIIRQDRDatIPIIFLS--------REsnaekqllALSRGADGFVQKPLK 329
Cdd:cd17536   36 EALELIEEHKPDIVITDIRMPGMDGlELIEKIRELYPD--IKIIILSgyddfeyaQK--------AIRLGVVDYLLKPVD 105
                         90
                 ....*....|....
gi 685887246 330 RGAFIKALKSIISR 343
Cdd:cd17536  106 EEELEEALEKAKEE 119
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
226-327 1.10e-05

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: 44.42  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRP-DVLVTDFHMPEANGDVVASIIRQdRDATIPIIFLS 304
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELAREARK-IDPDVKILFIS 79
                         90       100
                 ....*....|....*....|...
gi 685887246 305 RESNAEKQLLALSRGADGFVQKP 327
Cdd:cd18160   80 GGAAAAPELLSDAVGDNATLKKP 102
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
231-344 1.21e-05

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: 46.25  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 231 DDSRTDAyLARkFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANG-DVVASIIRqdRDATIPIIFLSRESNA 309
Cdd:COG4566    8 DEAVRDS-LAF-LLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGlELQEELAA--RGSPLPVIFLTGHGDV 83
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 685887246 310 EKQLLALSRGADGFVQKPLKRGAFIKALKSIISRS 344
Cdd:COG4566   84 PMAVRAMKAGAVDFLEKPFDDQALLDAVRRALARD 118
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
226-327 1.50e-05

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 46.11  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDD----SRTDAYLarkfLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANG-DVVASIIRQDRDatIPI 300
Cdd:PRK11083   5 TILLVEDeqaiADTLVYA----LQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGfELCRQLLAFHPA--LPV 78
                         90       100
                 ....*....|....*....|....*..
gi 685887246 301 IFLSRESNAEKQLLALSRGADGFVQKP 327
Cdd:PRK11083  79 IFLTARSDEVDRLVGLEIGADDYVAKP 105
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
228-343 2.17e-05

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: 43.75  E-value: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 228 LLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRDATiPIIFLSRES 307
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIET-PVLLLTALD 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 685887246 308 NAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISR 343
Cdd:cd17625   80 AVEDRVKGLDLGADDYLPKPFSLAELLARIRALLRR 115
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
199-327 3.77e-05

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: 42.54  E-value: 3.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 199 ILGLDDD--IRNLRSLfrsrnrDIEIEGYRVLLLDDSrtdaylarkfltEEGLIvehiqhpsqvlEALSRfRPDVLVTDF 276
Cdd:cd17620    1 ILVIEDEpqIRRFLRT------ALEAHGYRVFEAETG------------QEGLL-----------EAATR-KPDLIILDL 50
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 685887246 277 HMPEANGdvvASIIRQDRD-ATIPIIFLS-RESNAEKqLLALSRGADGFVQKP 327
Cdd:cd17620   51 GLPDMDG---LEVIRRLREwSAVPVIVLSaRDEESDK-IAALDAGADDYLTKP 99
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
226-327 9.74e-05

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: 41.85  E-value: 9.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRD-ATIPIIFLS 304
Cdd:cd17618    2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMtRDIPIIMLT 81
                         90       100
                 ....*....|....*....|...
gi 685887246 305 RESNAEKQLLALSRGADGFVQKP 327
Cdd:cd17618   82 ARGEEEDKVRGLEAGADDYITKP 104
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
227-334 1.12e-04

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: 41.66  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRqdRDATIPIIFLS-R 305
Cdd:cd17594    2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIR--ARSDVPIIIISgD 79
                         90       100
                 ....*....|....*....|....*....
gi 685887246 306 ESNAEKQLLALSRGADGFVQKPLKRGAFI 334
Cdd:cd17594   80 RRDEIDRVVGLELGADDYLAKPFGLRELL 108
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
231-343 1.54e-04

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 43.37  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 231 DDSRTDAYLArKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGdvvASIIRQDRDAT--IPIIFLSRESN 308
Cdd:PRK09836   8 DEKKTGEYLT-KGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNG---WDIVRMLRSANkgMPILLLTALGT 83
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 685887246 309 AEKQLLALSRGADGFVQKPLKRGAFIKALKSIISR 343
Cdd:PRK09836  84 IEHRVKGLELGADDYLVKPFAFAELLARVRTLLRR 118
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
226-343 1.90e-04

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 43.17  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANG-DVVASIIRQDRDATIPIIFLS 304
Cdd:PRK10161   4 RILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGiQFIKHLKRESMTRDIPVVMLT 83
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 685887246 305 RESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISR 343
Cdd:PRK10161  84 ARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMRR 122
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
226-329 1.94e-04

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: 41.03  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRDATiPIIFLSR 305
Cdd:cd17555    2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDT-PVIVVSG 80
                         90       100
                 ....*....|....*....|....
gi 685887246 306 ESNAEKQLLALSRGADGFVQKPLK 329
Cdd:cd17555   81 AGVMSDAVEALRLGAWDYLTKPIE 104
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
226-341 4.01e-04

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: 40.08  E-value: 4.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGL-IVEHIQHPSQVLEALSRFRPDVLVTDFHMP-EANGDVVASIIRQDRDatIPIIFL 303
Cdd:cd17534    2 KILIVEDEAIIALDLKEILESLGYeVVGIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREKFD--IPVIFL 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 685887246 304 SreSNAEKQLL--ALSRGADGFVQKPLKRgafiKALKSII 341
Cdd:cd17534   80 T--AYSDEETLerAKETNPYGYLVKPFNE----RELKAAI 113
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
248-341 5.71e-04

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 39.50  E-value: 5.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 248 GLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQdRDATIPIIFLSRESNAEKQLLALSRGADGFVQKP 327
Cdd:cd17537   24 GLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLA-RGSNIPIIFITGHGDVPMAVEAMKAGAVDFLEKP 102
                         90
                 ....*....|....
gi 685887246 328 LKRGAFIKALKSII 341
Cdd:cd17537  103 FRDQVLLDAIEQAL 116
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
226-368 5.75e-04

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 41.59  E-value: 5.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRDatIPIIFLSR 305
Cdd:PRK10710  12 RILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRFSD--IPIVMVTA 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685887246 306 ESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISRSKVLESRMRRDPLTNLL-NHGQFMAS 368
Cdd:PRK10710  90 KIEEIDRLLGLEIGADDYICKPYSPREVVARVKTILRRCKPQRELQQQDAESPLIiDESRFQAS 153
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
226-298 7.11e-04

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: 39.35  E-value: 7.11e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685887246 226 RVLLLDDSRTDA-YLARKfLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANG-DVVASIIRQDRDATI 298
Cdd:cd17563    2 SLLLVDDDEVFAeRLARA-LERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGlDLIPPLRALQPDARI 75
PRK10693 PRK10693
two-component system response regulator RssB;
258-329 9.63e-04

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 41.13  E-value: 9.63e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685887246 258 SQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQdRDATIPIIFLSRESNAEKQLLALSRGADGFVQKPLK 329
Cdd:PRK10693   7 VDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRN-RGDQTPVLVISATENMADIAKALRLGVQDVLLKPVK 77
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
223-328 9.69e-04

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 42.03  E-value: 9.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246  223 EGYRVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQdRDATIPIIF 302
Cdd:PRK09959  957 EKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLRE-QNSSLPIWG 1035
                          90       100
                  ....*....|....*....|....*.
gi 685887246  303 LSRESNAEKQLLALSRGADGFVQKPL 328
Cdd:PRK09959 1036 LTANAQANEREKGLSCGMNLCLFKPL 1061
PRK15479 PRK15479
transcriptional regulator TctD;
226-344 1.37e-03

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 40.09  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQdRDATIPIIFLSR 305
Cdd:PRK15479   2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRK-RGQTLPVLLLTA 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 685887246 306 ESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISRS 344
Cdd:PRK15479  81 RSAVADRVKGLNVGADDYLPKPFELEELDARLRALLRRS 119
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
229-328 1.43e-03

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 38.02  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 229 LLDDSRTDAYLARKFLTEE--GLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANG-DVVASIirQDRDATIPIIFLSR 305
Cdd:cd17565    3 IVDDDKNIIKILSDIIEDDdlGEVVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGiQLVRKL--KDTGSNGKFIMISQ 80
                         90       100
                 ....*....|....*....|...
gi 685887246 306 ESNAEKQLLALSRGADGFVQKPL 328
Cdd:cd17565   81 VSDKEMIGKAYQAGIEFFINKPI 103
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
227-329 1.51e-03

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: 38.50  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRP-----------DVLVTDFHMPEANG-DVVASIIRQDR 294
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGLEDEedssnfnepkvNMIITDYCMPGMTGyDLLKKVKESSA 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 685887246 295 DATIPIIFLSRESNAEKQLLALSRGADGFVQKPLK 329
Cdd:cd17581   81 LKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVK 115
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
227-304 1.55e-03

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 38.10  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEAL-SRFRPDVLVTDFHMP-EANGDVVASIIRQDRdATIPIIFLS 304
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLeSGPDIDLLVTDVIMPgGMNGSQLAEEARRRR-PDLKVLLTS 79
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
227-302 2.01e-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: 38.29  E-value: 2.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRtdayLAR----KFLTEEG--LIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQdRDATIPI 300
Cdd:cd17532    1 ALIVDDEP----LAReelrYLLEEHPdiEIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSK-LAKPPLI 75

                 ..
gi 685887246 301 IF 302
Cdd:cd17532   76 VF 77
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
227-327 2.17e-03

phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is a member of the SenX3-RegX3 two-component system that is involved in phosphate-sensing signal transduction. Phosphorylated RegX3 functions as a transcriptional activator of phoA. It induces transcription in phosphate limiting environment and also controls expression of several critical metabolic enzymes in aerobic condition. RegX3 belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 37.56  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDD--SRTD--AYLARKflteEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDrdATIPIIF 302
Cdd:cd17621    1 VLVVEDeeSFSDplAYLLRK----EGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRAR--SNVPVIM 74
                         90       100
                 ....*....|....*....|....*
gi 685887246 303 LSRESNAEKQLLALSRGADGFVQKP 327
Cdd:cd17621   75 VTAKDSEIDKVVGLELGADDYVTKP 99
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
226-327 2.32e-03

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: 37.59  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRT-DAYLARKFLTEEGLIVEHIQHPSQ-VLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRDATIP-IIF 302
Cdd:cd17561    3 KVLIADDNREfVQLLEEYLNSQPDMEVVGVAHNGQeALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPkIIM 82
                         90       100
                 ....*....|....*....|....*...
gi 685887246 303 LS---RESNAEKqllALSRGADGFVQKP 327
Cdd:cd17561   83 LTafgQEDITQR---AVELGASYYILKP 107
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
226-336 2.75e-03

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 39.86  E-value: 2.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRtdayLARKFLTEegLIVEHIQH--------PSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQDRDAT 297
Cdd:PRK12555   2 RIGIVNDSP----LAVEALRR--ALARDPDHevvwvatdGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAERPCP 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 685887246 298 IPIIFLSRESNAEKQLLALSRGADGFVQKP-LKRGAFIKA 336
Cdd:PRK12555  76 ILIVTSLTERNASRVFEAMGAGALDAVDTPtLGIGAGLEE 115
PRK11173 PRK11173
two-component response regulator; Provisional
198-344 3.21e-03

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 39.23  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 198 RILGLDDDI--RN-LRSLFrsrnrdiEIEGYRVlllddsrtdaylarkFLTEEGlivehiqhpSQVLEALSRFRPDVLVT 274
Cdd:PRK11173   5 HILIVEDELvtRNtLKSIF-------EAEGYDV---------------FEATDG---------AEMHQILSENDINLVIM 53
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685887246 275 DFHMPEANGDVVASIIRQDRDatIPIIFLSRESNAEKQLLALSRGADGFVQKPLK-RGAFIKAlKSIISRS 344
Cdd:PRK11173  54 DINLPGKNGLLLARELREQAN--VALMFLTGRDNEVDKILGLEIGADDYITKPFNpRELTIRA-RNLLSRT 121
PRK15347 PRK15347
two component system sensor kinase;
226-328 3.59e-03

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 40.01  E-value: 3.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQD---RDATIPIIF 302
Cdd:PRK15347 692 QILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDpnnLDPDCMIVA 771
                         90       100
                 ....*....|....*....|....*.
gi 685887246 303 LSRESNAEKQLLALSRGADGFVQKPL 328
Cdd:PRK15347 772 LTANAAPEEIHRCKKAGMNHYLTKPV 797
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
353-504 4.29e-03

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 39.70  E-value: 4.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 353 RDPLTNLLNHGQFMASAATVLAEGPPSSLVLIDIDHFKSVNDTFGHPVGDRVLVGLAEVLTDSLRTDDYVGRLGGEEFGI 432
Cdd:PRK13561 233 RFPVSDLPNKALLMALLEQVVARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVLAQISGYDFAI 312
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685887246 433 VMVGAN-PSQAkmvVDRLRSIFTAI-QFQSEDGTSFSCSFSAGVAIL--NVSVKEAHRAADEALYSAKRSGRDRVE 504
Cdd:PRK13561 313 IANGVKePWHA---ITLGQQVLTIInERLPIQRIQLRPSCSIGIAMFygDLTAEQLYSRAISAAFTARRKGKNQIQ 385
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
226-327 4.72e-03

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: 37.15  E-value: 4.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFL-TEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQD-RDATIPIIFL 303
Cdd:cd17552    3 RILVIDDEEDIREVVQACLeKLAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANpETQSIPVILL 82
                         90       100
                 ....*....|....*....|....
gi 685887246 304 SRESNAEKQLLALSRGADGFVQKP 327
Cdd:cd17552   83 TAKAQPSDRQRFASLGVAGVIAKP 106
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
226-360 5.47e-03

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 38.47  E-value: 5.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRtdayLARKFL-----TEEGL-IVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRqDRDATIP 299
Cdd:PRK10651   8 TILLIDDHP----MLRTGVkqlisMAPDItVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLR-EKSLSGR 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685887246 300 IIFLSRESNAEKQLLALSRGADGFVQKPLKRGAFIKALKSIISRSKVLEsrmrrDPLTNLL 360
Cdd:PRK10651  83 IVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQAAAGEMVLS-----EALTPVL 138
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
227-329 5.48e-03

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: 36.71  E-value: 5.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 227 VLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASIIRQdRDATIPIIFLSRE 306
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKE-KYPDLPVIMISGH 79
                         90       100
                 ....*....|....*....|...
gi 685887246 307 SNAEKQLLALSRGADGFVQKPLK 329
Cdd:cd17550   80 GTIETAVKATKLGAYDFIEKPLS 102
PRK10816 PRK10816
two-component system response regulator PhoP;
269-354 6.66e-03

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 38.18  E-value: 6.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 269 PDVLVTDFHMPEANGdvvASIIRQDR--DATIPIIFLS-RESNAEKqLLALSRGADGFVQKPLKrgafikaLKSIISRSK 345
Cdd:PRK10816  45 PDIAIVDLGLPDEDG---LSLIRRWRsnDVSLPILVLTaRESWQDK-VEVLSAGADDYVTKPFH-------IEEVMARMQ 113

                 ....*....
gi 685887246 346 VLesrMRRD 354
Cdd:PRK10816 114 AL---MRRN 119
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
226-332 6.99e-03

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: 36.61  E-value: 6.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 226 RVLLLDDSRTDAYLARKFLTEEGLIVEHIQHPSQVLEALSR----FRpdVLVTDFHMPEANGDVVASIIRQDRDATIP-- 299
Cdd:cd19933    2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASaehsFQ--LVLLDLCMPEMDGFEVALRIRKLFGRRERpl 79
                         90       100       110
                 ....*....|....*....|....*....|...
gi 685887246 300 IIFLSRESNAEKQLLALSRGADGFVQKPLKRGA 332
Cdd:cd19933   80 IVALTANTDDSTREKCLSLGMNGVITKPVSLHA 112
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
226-290 7.79e-03

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: 36.79  E-value: 7.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685887246 226 RVLLLDDSR-TDAYLARKFLTEEGL-IVEHIQHPSQVLEALSRFRPDVLVTDFHMPEANGDVVASII 290
Cdd:COG2197    3 RVLIVDDHPlVREGLRALLEAEPDIeVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
198-339 8.50e-03

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains; This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 36.23  E-value: 8.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685887246 198 RILGLDDDIRNLRSL---FRSrnrdieiEGYRVLLLDDSrtdaylarkfltEEGLivehiqhpsqvlEALSRFRPDVLVT 274
Cdd:cd17569    2 TILLVDDEPNILKALkrlLRR-------EGYEVLTATSG------------EEAL------------EILKQEPVDVVIS 50
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685887246 275 DFHMPEANGDVVASIIRQDRDATIPIIfLSreSNAEKQLL--ALSRGA-DGFVQKPLKRGAFIKALKS 339
Cdd:cd17569   51 DQRMPGMDGAELLKRVRERYPDTVRIL-LT--GYADLDAAieAINEGEiYRFLTKPWDDEELKETIRQ 115
PRK13557 PRK13557
histidine kinase; Provisional
216-287 9.56e-03

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 38.50  E-value: 9.56e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685887246 216 RNRDIEIEGYRVLLLDDSRTD-AYLARKFLTEEGLIVEHIQHPSQVLEAL-SRFRPDVLVTDFHMPEA-NGDVVA 287
Cdd:PRK13557 406 KARAIDRGGTETILIVDDRPDvAELARMILEDFGYRTLVASNGREALEILdSHPEVDLLFTDLIMPGGmNGVMLA 480
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
270-334 9.85e-03

phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; Helicobacter pylori response regulator hp1043 (HP-RR) is an orphan response regulator which is phosphorylation-independent and is essential for growth. HP-RR functions as a cell growth-associated regulator in the absence of post-translational modification. Members of this subfamily contain REC and DNA-binding output domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 35.87  E-value: 9.85e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685887246 270 DVLVTDFHMPEANG-DVVASIirQDRDATIPIIFLSRESNAEKQLLALSRGADGFVQKPLKRGAFI 334
Cdd:cd17573   44 DLVLVSDKLPDGNGlSIVSRI--KEKHPSIVVIVLSDNPKTEQEIEAFKEGADDYIAKPFDFKVLV 107
 
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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