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Conserved domains on  [gi|857890029|emb|CDT05333|]
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putative Response regulator [Vibrio coralliirubri]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10693 super family cl32557
two-component system response regulator RssB;
48-252 1.67e-40

two-component system response regulator RssB;


The actual alignment was detected with superfamily member PRK10693:

Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 144.75  E-value: 1.67e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  48 EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTDDMSDVAKALRFGIKDFLAKPLEDHRH 127
Cdd:PRK10693   2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKPVKDLNR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029 128 LGSAIANTLTDSFdnisdqrdFSSQwfcvddggeIPEDQELHWHLNYLQDNPSAAKDLLHALLPEKDTRQGSWRCSYRLL 207
Cdd:PRK10693  82 LREMVFACLYPSM--------FNSR---------VEEEERLFRDWDALVDNPAAAAKLLKQLQPPVQQVIAHCRVNYRQL 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 857890029 208 QSTEMMPLVFDYAWMMNGQFAFYLVDSSSSDNGGSATTLLVRALF 252
Cdd:PRK10693 145 VAADKPGLVLDIAALSDNDLAFYCLDVTRAGDNGVLAALLLRALF 189
 
Name Accession Description Interval E-value
PRK10693 PRK10693
two-component system response regulator RssB;
48-252 1.67e-40

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 144.75  E-value: 1.67e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  48 EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTDDMSDVAKALRFGIKDFLAKPLEDHRH 127
Cdd:PRK10693   2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKPVKDLNR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029 128 LGSAIANTLTDSFdnisdqrdFSSQwfcvddggeIPEDQELHWHLNYLQDNPSAAKDLLHALLPEKDTRQGSWRCSYRLL 207
Cdd:PRK10693  82 LREMVFACLYPSM--------FNSR---------VEEEERLFRDWDALVDNPAAAAKLLKQLQPPVQQVIAHCRVNYRQL 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 857890029 208 QSTEMMPLVFDYAWMMNGQFAFYLVDSSSSDNGGSATTLLVRALF 252
Cdd:PRK10693 145 VAADKPGLVLDIAALSDNDLAFYCLDVTRAGDNGVLAALLLRALF 189
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
 20-132 5.96e-37

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: 129.63  E-value: 5.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  20 KCVMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSG 99
Cdd:cd17555    1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSG 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKPLEDHRHLGSAI 132
Cdd:cd17555   81 AGVMSDAVEALRLGAWDYLTKPIEDLAVLEHAV 113
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 22-136 4.70e-35

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: 124.96  E-value: 4.70e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEEL--SLEYPSLPMIVVSG 99
Cdd:COG0784    8 ILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIraLPRLPDIPIIALTA 87

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKPLeDHRHLGSAIANTL 136
Cdd:COG0784   88 YADEEDRERALEAGADDYLTKPV-DPEELLEALRRLL 123
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 22-121 4.39e-31

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: 113.79  E-value: 4.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029   22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80

                          90       100
                  ....*....|....*....|
gi 857890029  102 DMSDVAKALRFGIKDFLAKP 121
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKP 100
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 22-74 1.42e-14

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: 67.59  E-value: 1.42e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 857890029    22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMP 74
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
 22-123 7.35e-08

sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a transcription factor critical for the initiation of sporulation. It contains a response regulator receiver domain (pfam00072). In Bacillus subtilis, it works together with response regulator Spo0F and the phosphotransferase Spo0B, both of which are missing from at least some sporulating species and thus not part of the endospore forming bacteria minimal gene set. Spo0A, however, is universal among endospore-forming species. [Cellular processes, Sporulation and germination]


Pssm-ID: 131922 [Multi-domain]  Cd Length: 262  Bit Score: 52.87  E-value: 7.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029   22 VMLVDDDPIFRRITSAYLD-KVGYKVVE-AENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELS----LEYPSLPMI 95
Cdd:TIGR02875   5 IVIADDNKEFCNLLKEYLAaQPDMEVVGvAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNeielSARPRVIML 84

                          90       100
                  ....*....|....*....|....*...
gi 857890029   96 VVSGTDDMSDvaKALRFGIKDFLAKPLE 123
Cdd:TIGR02875  85 SAFGQEKITQ--RAVALGADYYVLKPFD 110
 
Name Accession Description Interval E-value
PRK10693 PRK10693
two-component system response regulator RssB;
48-252 1.67e-40

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 144.75  E-value: 1.67e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  48 EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTDDMSDVAKALRFGIKDFLAKPLEDHRH 127
Cdd:PRK10693   2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKPVKDLNR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029 128 LGSAIANTLTDSFdnisdqrdFSSQwfcvddggeIPEDQELHWHLNYLQDNPSAAKDLLHALLPEKDTRQGSWRCSYRLL 207
Cdd:PRK10693  82 LREMVFACLYPSM--------FNSR---------VEEEERLFRDWDALVDNPAAAAKLLKQLQPPVQQVIAHCRVNYRQL 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 857890029 208 QSTEMMPLVFDYAWMMNGQFAFYLVDSSSSDNGGSATTLLVRALF 252
Cdd:PRK10693 145 VAADKPGLVLDIAALSDNDLAFYCLDVTRAGDNGVLAALLLRALF 189
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
 20-132 5.96e-37

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: 129.63  E-value: 5.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  20 KCVMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSG 99
Cdd:cd17555    1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSG 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKPLEDHRHLGSAI 132
Cdd:cd17555   81 AGVMSDAVEALRLGAWDYLTKPIEDLAVLEHAV 113
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 22-136 4.70e-35

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: 124.96  E-value: 4.70e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEEL--SLEYPSLPMIVVSG 99
Cdd:COG0784    8 ILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIraLPRLPDIPIIALTA 87

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKPLeDHRHLGSAIANTL 136
Cdd:COG0784   88 YADEEDRERALEAGADDYLTKPV-DPEELLEALRRLL 123
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 22-124 2.76e-32

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 119.24  E-value: 2.76e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEEL--SLEYPSLPMIVVSG 99
Cdd:COG3706    4 ILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLraDPRTADIPIIFLTA 83

                         90       100
                 ....*....|....*....|....*
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKPLED 124
Cdd:COG3706   84 LDDEEDRARALEAGADDYLTKPFDP 108
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
 22-121 3.69e-32

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: 116.41  E-value: 3.69e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDK-VGYKVV-EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSG 99
Cdd:COG4753    2 VLIVDDEPLIREGLKRILEWeAGFEVVgEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILSG 81

                         90       100
                 ....*....|....*....|..
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKP 121
Cdd:COG4753   82 YSDFEYAQEAIKLGADDYLLKP 103
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 18-136 1.38e-31

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: 123.15  E-value: 1.38e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  18 NQKCVMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVV 97
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 857890029  98 SGTDDMSDVAKALRFGIKDFLAKPLeDHRHLGSAIANTL 136
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPF-DLEELLAAVERAL 118
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
 23-121 1.68e-31

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: 114.63  E-value: 1.68e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  23 MLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTDD 102
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80

                         90
                 ....*....|....*....
gi 857890029 103 MSDVAKALRFGIKDFLAKP 121
Cdd:cd00156   81 EEDAVRALELGADDYLVKP 99
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 22-121 4.39e-31

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: 113.79  E-value: 4.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029   22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80

                          90       100
                  ....*....|....*....|
gi 857890029  102 DMSDVAKALRFGIKDFLAKP 121
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKP 100
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
 18-148 5.93e-30

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 111.99  E-value: 5.93e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  18 NQKCVMLVDDDPIFRRITSAYLDKV-GYKVV-EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMI 95
Cdd:COG4565    2 KMIRVLIVEDDPMVAELLRRYLERLpGFEVVgVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVI 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 857890029  96 VVSGTDDMSDVAKALRFGIKDFLAKPLEDHRhLGSAIANTLTDSFDNISDQRD 148
Cdd:COG4565   82 VITAARDPETVREALRAGVVDYLIKPFTFER-LREALERYLEYRRLLREDQEE 133
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 22-136 4.19e-29

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: 112.18  E-value: 4.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPS--LPMIVVSG 99
Cdd:COG3437    9 VLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTrdIPVIFLTA 88

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKPLeDHRHLGSAIANTL 136
Cdd:COG3437   89 LADPEDRERALEAGADDYLTKPF-DPEELLARVRNAL 124
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
 22-121 7.12e-28

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: 108.50  E-value: 7.12e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:COG0745    4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTARD 83

                         90       100
                 ....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKP 121
Cdd:COG0745   84 DEEDRVRGLEAGADDYLTKP 103
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
 22-124 8.11e-28

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: 105.50  E-value: 8.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLD--KVGYKVV-EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVS 98
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIDweELGFEVVgEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILS 80

                         90       100
                 ....*....|....*....|....*.
gi 857890029  99 GTDDMSDVAKALRFGIKDFLAKPLED 124
Cdd:cd17536   81 GYDDFEYAQKAIRLGVVDYLLKPVDE 106
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
 22-123 6.35e-26

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: 100.24  E-value: 6.35e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVE---ELSLEYPSLPMIVVS 98
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRrirELEGGGRRTPIIALT 80

                         90       100
                 ....*....|....*....|....*
gi 857890029  99 GTDDMSDVAKALRFGIKDFLAKPLE 123
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVK 105
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
 22-132 2.13e-24

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: 96.43  E-value: 2.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKV-GYKVV-EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSG 99
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLESEpDIEVVgEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTA 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKPLEDHrHLGSAI 132
Cdd:cd17535   81 HDDPEYVLRALKAGAAGYLLKDSSPE-ELIEAI 112
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
 23-121 4.25e-23

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: 92.09  E-value: 4.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  23 MLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTDD 102
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80

                         90
                 ....*....|....*....
gi 857890029 103 MSDVAKALRFGIKDFLAKP 121
Cdd:cd17574   81 EEDKVLGLELGADDYITKP 99
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
 22-121 1.93e-21

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 88.31  E-value: 1.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:COG5803    5 ILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPDIPVIMMTAYG 84

                         90       100
                 ....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKP 121
Cdd:COG5803   85 ELDMVEEAKELGAKGYFTKP 104
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
 22-123 2.58e-21

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: 87.94  E-value: 2.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80

                         90       100
                 ....*....|....*....|..
gi 857890029 102 DMSDVAKALRFGIKDFLAKPLE 123
Cdd:cd17550   81 TIETAVKATKLGAYDFIEKPLS 102
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
 22-123 1.09e-20

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: 86.34  E-value: 1.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGY-KVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEEL--SLEYPSLPMIVVS 98
Cdd:cd17551    3 ILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLraLPGLEDVPIVMIT 82

                         90       100
                 ....*....|....*....|....*
gi 857890029  99 GTDDMSDVAKALRFGIKDFLAKPLE 123
Cdd:cd17551   83 ADTDREVRLRALEAGATDFLTKPFD 107
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
 22-133 1.15e-20

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: 88.48  E-value: 1.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVV-EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPsLPMIVVSGT 100
Cdd:COG3707    6 VLVVDDEPLRRADLREGLREAGYEVVaEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP-APVILLTAY 84

                         90       100       110
                 ....*....|....*....|....*....|...
gi 857890029 101 DDMSDVAKALRFGIKDFLAKPLEDHRhLGSAIA 133
Cdd:COG3707   85 SDPELIERALEAGVSAYLVKPLDPED-LLPALE 116
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
 22-121 3.23e-20

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: 84.52  E-value: 3.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSlEYPSLPMIVVSGTD 101
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLR-EWSAVPVIVLSARD 79

                         90       100
                 ....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKP 121
Cdd:cd17620   80 EESDKIAALDAGADDYLTKP 99
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
 22-121 5.88e-20

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


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 83.70  E-value: 5.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEEL--SLEYPSLPMIVVSG 99
Cdd:cd17538    2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLkeDPETRHIPVIMITA 81

                         90       100
                 ....*....|....*....|..
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKP 121
Cdd:cd17538   82 LDDREDRIRGLEAGADDFLSKP 103
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
 22-121 6.86e-20

phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate methylesterase CheB and similar chemotaxis proteins; Methylesterase CheB is a chemotaxis response regulator with an N-terminal REC domain and a C-terminal methylesterase domain. Chemotaxis is a behavior known in motile bacteria that directs their movement in response to chemical gradients. CheB is a phosphorylation-activated response regulator involved in the reversible modification of bacterial chemotaxis receptors. It catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. The CheB REC domain packs against the active site of the C-terminal domain and inhibits methylesterase activity by directly restricting access to the active site. Also included in this family is chemotaxis response regulator CheY, which contains a stand-alone REC domain, and an uncharacterized subfamily composed of proteins containing an N-terminal REC domain and a C-terminal CheY-P phosphatase (CheC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 84.37  E-value: 6.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKV-GYKVV-EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPsLPMIVVSG 99
Cdd:cd17541    3 VLIVDDSAVMRKLLSRILESDpDIEVVgTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERP-TPVVMVSS 81

                         90       100
                 ....*....|....*....|....
gi 857890029 100 -TDDMSDVA-KALRFGIKDFLAKP 121
Cdd:cd17541   82 lTEEGAEITlEALELGAVDFIAKP 105
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
 22-136 7.16e-20

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: 83.87  E-value: 7.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVV-EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGT 100
Cdd:cd17542    3 VLIVDDAAFMRMMLKDILTKAGYEVVgEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCSAM 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 857890029 101 DDMSDVAKALRFGIKDFLAKPLEDHRHLgSAIANTL 136
Cdd:cd17542   83 GQEEMVKEAIKAGAKDFIVKPFQPERVL-EAVEKVL 117
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
 22-131 3.33e-19

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: 82.54  E-value: 3.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKPLEDHRHLGSA 131
Cdd:cd17549   81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVV 110
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
 22-121 5.10e-19

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


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 81.80  E-value: 5.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLrNSAPD--LIVCDLSMPILDGIELVEELSLEYPS--LPMIVV 97
Cdd:cd17544    3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVL-EQHPDikLVITDYNMPEMDGFELVREIRKKYSRdqLAIIGI 81

                         90       100
                 ....*....|....*....|....
gi 857890029  98 SGTDDMSDVAKALRFGIKDFLAKP 121
Cdd:cd17544   82 SASGDNALSARFIKAGANDFLTKP 105
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
 19-121 5.53e-19

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: 83.43  E-value: 5.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  19 QKCVMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVS 98
Cdd:COG4567    4 DRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVLT 83

                         90       100
                 ....*....|....*....|...
gi 857890029  99 GTDDMSDVAKALRFGIKDFLAKP 121
Cdd:COG4567   84 GYASIATAVEAIKLGADDYLAKP 106
orf27 CHL00148
Ycf27; Reviewed
 18-121 6.40e-19

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 84.77  E-value: 6.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  18 NQKCVMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEyPSLPMIVV 97
Cdd:CHL00148   5 SKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKE-SDVPIIML 83

                         90       100
                 ....*....|....*....|....
gi 857890029  98 SGTDDMSDVAKALRFGIKDFLAKP 121
Cdd:CHL00148  84 TALGDVSDRITGLELGADDYVVKP 107
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
 20-121 7.95e-19

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 81.19  E-value: 7.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  20 KCVMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSL--EYPSLPMIVV 97
Cdd:cd17562    1 KKILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKlpAYKFTPILML 80

                         90       100
                 ....*....|....*....|....*.
gi 857890029  98 S--GTDDMSDVAKALrfGIKDFLAKP 121
Cdd:cd17562   81 TteSSDEKKQEGKAA--GATGWLVKP 104
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
 22-123 1.00e-18

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: 80.85  E-value: 1.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYK-VVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEEL--SLEYPSLPMIVVS 98
Cdd:cd19923    3 VLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIraDGALSHLPVLMVT 82

                         90       100
                 ....*....|....*....|....*
gi 857890029  99 GTDDMSDVAKALRFGIKDFLAKPLE 123
Cdd:cd19923   83 AEAKKENVIAAAQAGVNNYIVKPFT 107
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
 22-121 1.12e-18

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


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 80.50  E-value: 1.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAP---------DLIVCDLSMPILDGIELVEELSLE--YP 90
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKegndlskelDLIITDIEMPKMDGYELTFELRDDprLA 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 857890029  91 SLPMIVVSGTDDMSDVAKALRFGIKDFLAKP 121
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
 20-123 3.79e-18

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: 79.52  E-value: 3.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  20 KCVMLVDDDPIFRRITSAYLDKV-GYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEEL--SLEYPSLPMIV 96
Cdd:cd17552    2 KRILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLqaNPETQSIPVIL 81

                         90       100
                 ....*....|....*....|....*..
gi 857890029  97 VSGTDDMSDVAKALRFGIKDFLAKPLE 123
Cdd:cd17552   82 LTAKAQPSDRQRFASLGVAGVIAKPFD 108
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
 22-121 4.20e-18

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: 78.57  E-value: 4.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSL--EYPSLPMIVVSG 99
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKnaDFDTIPVIFLTA 80

                         90       100
                 ....*....|....*....|..
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKP 121
Cdd:cd19927   81 KGMTSDRIKGYNAGCDGYLSKP 102
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
 22-126 1.05e-17

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 78.06  E-value: 1.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKV-GYKVV-EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSG 99
Cdd:cd19925    3 VLIVEDDPMVAEIHRAYVEQVpGFTVIgTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVVTA 82

                         90       100
                 ....*....|....*....|....*..
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKPLEDHR 126
Cdd:cd19925   83 ANDVETVREALRLGVVDYLIKPFTFER 109
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
 20-105 1.40e-17

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: 77.65  E-value: 1.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  20 KCVMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSG 99
Cdd:cd17554    1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTA 80


                 ....*.
gi 857890029 100 TDDMSD 105
Cdd:cd17554   81 YSEYKS 86
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
 23-121 1.69e-17

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 77.31  E-value: 1.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  23 MLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEEL--SLEYPSLPMIVVSGT 100
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILrsDPKTSSIPIIMLTAK 80

                         90       100
                 ....*....|....*....|.
gi 857890029 101 DDMSDVAKALRFGIKDFLAKP 121
Cdd:cd19937   81 GEEFDKVLGLELGADDYITKP 101
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
 21-126 1.88e-17

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: 79.76  E-value: 1.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  21 CVMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGT 100
Cdd:COG4566    1 TVYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGH 80

                         90       100
                 ....*....|....*....|....*.
gi 857890029 101 DDMSDVAKALRFGIKDFLAKPLEDHR 126
Cdd:COG4566   81 GDVPMAVRAMKAGAVDFLEKPFDDQA 106
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
 22-123 1.79e-16

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: 74.73  E-value: 1.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSlEYPSLPMIVVSGTD 101
Cdd:cd17619    3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELR-EQSEVGIILVTGRD 81

                         90       100
                 ....*....|....*....|..
gi 857890029 102 DMSDVAKALRFGIKDFLAKPLE 123
Cdd:cd17619   82 DEVDRIVGLEIGADDYVTKPFN 103
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
 22-123 2.09e-16

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: 74.42  E-value: 2.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYP--SLPMIVVSG 99
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWlaNTPAIALTG 80

                         90       100
                 ....*....|....*....|....
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKPLE 123
Cdd:cd17580   81 YGQPEDRERALEAGFDAHLVKPVD 104
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
22-127 2.79e-16

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 79.04  E-value: 2.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKV-GYKVV-EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPsLPMIVVSG 99
Cdd:PRK00742   6 VLVVDDSAFMRRLISEILNSDpDIEVVgTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRP-TPVVMVSS 84

                         90       100       110
                 ....*....|....*....|....*....|
gi 857890029 100 -TDDMSDVA-KALRFGIKDFLAKPLEDHRH 127
Cdd:PRK00742  85 lTERGAEITlRALELGAVDFVTKPFLGISL 114
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
 22-123 3.08e-16

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: 73.96  E-value: 3.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80

                         90       100
                 ....*....|....*....|..
gi 857890029 102 DMSDVAKALRFGIKDFLAKPLE 123
Cdd:cd17627   81 SVSDRVAGLDAGADDYLVKPFA 102
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
 22-121 3.20e-16

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: 73.31  E-value: 3.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEEL--SLEYPSLPMIVVSG 99
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLkaDPATRHIPVIFLTA 80

                         90       100
                 ....*....|....*....|..
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKP 121
Cdd:cd19920   81 LTDTEDKVKGFELGAVDYITKP 102
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
 22-162 3.82e-16

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 76.78  E-value: 3.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKV-GYKVV-EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSG 99
Cdd:COG3279    4 ILIVDDEPLARERLERLLEKYpDLEVVgEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFTTA 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 857890029 100 TDDMsdVAKALRFGIKDFLAKPLEDHRhLGSAI--ANTLTDSFDNISDQRDfSSQWFCVDDGGEI 162
Cdd:COG3279   84 YDEY--ALEAFEVNAVDYLLKPIDEER-LAKALekAKERLEAKAAAEASPE-EKDRIFVKSGGKL 144
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
 20-136 4.30e-16

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: 73.59  E-value: 4.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  20 KCVMLVDDDP----IFRRItsayLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMI 95
Cdd:cd17569    1 PTILLVDDEPnilkALKRL----LRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRI 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 857890029  96 VVSGTDDMSDVAKALRFG-IKDFLAKPLEDhRHLGSAIANTL 136
Cdd:cd17569   77 LLTGYADLDAAIEAINEGeIYRFLTKPWDD-EELKETIRQAL 117
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
 22-121 4.40e-16

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: 73.15  E-value: 4.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKL-RNSAPDLIVCDLSMP-ILDGIELVEELSLEYPSLPMIVVSG 99
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLeSGPDIDLLVTDVIMPgGMNGSQLAEEARRRRPDLKVLLTSG 80

                         90       100
                 ....*....|....*....|..
gi 857890029 100 TDDMSDVAKALRFGIkDFLAKP 121
Cdd:cd18161   81 YAENAIEGGDLAPGV-DVLSKP 101
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
 22-126 4.86e-16

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: 73.39  E-value: 4.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80

                         90       100
                 ....*....|....*....|....*.
gi 857890029 102 DMsDVA-KALRFGIKDFLAKPLEDHR 126
Cdd:cd17572   81 SV-DIAvEAMRLGAYDFLEKPFDADR 105
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
22-187 5.52e-16

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 78.92  E-value: 5.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:PRK10365   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKPLEDHR---HLGSAIANTLTDSFDNISDQrdfSSQWFCVddgGEIPEDQELHWHLNYLQdn 178
Cdd:PRK10365  88 SVETAVEALKTGALDYLIKPLDFDNlqaTLEKALAHTHSIDAETPAVT---ASQFGMV---GKSPAMQHLLSEIALVA-- 159


                 ....*....
gi 857890029 179 PSAAKDLLH 187
Cdd:PRK10365 160 PSEATVLIH 168
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
 22-121 6.16e-16

phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; DNA-binding transcriptional regulator NtrC is also called nitrogen regulation protein NR(I) or nitrogen regulator I (NRI). It contains an N-terminal receiver (REC) domain, followed by a sigma-54 interaction domain, and a C-terminal helix-turn-helix DNA-binding domain. It is part of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. DNA-binding response regulator NtrC is phosphorylated by NtrB; phosphorylation of the N-terminal REC domain activates the central sigma-54 interaction domain and leads to the transcriptional activation from promoters that require sigma(54)-containing RNA polymerase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 73.08  E-value: 6.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:cd19919    3 VWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTAHS 82

                         90       100
                 ....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKP 121
Cdd:cd19919   83 DLDSAVSAYQGGAFEYLPKP 102
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
 22-133 1.12e-15

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: 72.19  E-value: 1.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSlEYPSL---PMIVVS 98
Cdd:cd17548    2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLK-EDPATrdiPVIALT 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 857890029  99 GTDDMSDVAKALRFGIKDFLAKPLeDHRHLGSAIA 133
Cdd:cd17548   81 AYAMKGDREKILEAGCDGYISKPI-DTREFLETVA 114
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
 22-99 1.51e-15

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: 71.76  E-value: 1.51e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAP-DLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSG 99
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
 22-121 2.33e-15

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: 71.32  E-value: 2.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:cd17563    3 LLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTGYA 82

                         90       100
                 ....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKP 121
Cdd:cd17563   83 SIATAVEAIKLGADDYLAKP 102
PRK15115 PRK15115
response regulator GlrR; Provisional
 22-139 3.75e-15

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 76.41  E-value: 3.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:PRK15115   8 LLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTAHG 87

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 857890029 102 DMSDVAKALRFGIKDFLAKPLeDHRHLGSAIANTLTDS 139
Cdd:PRK15115  88 SIPDAVAATQQGVFSFLTKPV-DRDALYKAIDDALEQS 124
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
 22-121 5.44e-15

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 70.12  E-value: 5.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAP--DLIVCDLSMPILDGIELVEELsLEYPSL---PMIV 96
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNeiDLILTEVDLPVSSGFKLLSYI-MRHKICkniPVIM 79

                         90       100
                 ....*....|....*....|....*
gi 857890029  97 VSGTDDMSDVAKALRFGIKDFLAKP 121
Cdd:cd17582   80 MSSQDSVGVVFKCLSKGAADYLVKP 104
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
22-123 6.75e-15

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 75.66  E-value: 6.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:PRK11361   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAYA 86

                         90       100
                 ....*....|....*....|..
gi 857890029 102 DMSDVAKALRFGIKDFLAKPLE 123
Cdd:PRK11361  87 EVETAVEALRCGAFDYVIKPFD 108
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
 22-121 6.76e-15

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 69.70  E-value: 6.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEEL--SLEYPSLPMIVVSG 99
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLrkSSALKDTPIIMLTG 80

                         90       100
                 ....*....|....*....|..
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKP 121
Cdd:cd17602   81 KDGLVDRIRAKMAGASGYLTKP 102
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
 22-121 6.98e-15

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: 70.14  E-value: 6.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVV-EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSlPMIVVSGT 100
Cdd:cd19932    3 VLIAEDEALIRMDLREMLEEAGYEVVgEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENIA-PIVLLTAY 81

                         90       100
                 ....*....|....*....|.
gi 857890029 101 DDMSDVAKALRFGIKDFLAKP 121
Cdd:cd19932   82 SQQDLVERAKEAGAMAYLVKP 102
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 22-74 1.42e-14

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: 67.59  E-value: 1.42e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 857890029    22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMP 74
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
 22-122 1.72e-14

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: 69.19  E-value: 1.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAP--DLIVCDLSMPILDGIELVEELSLEyPSLPMIVVSG 99
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDefDLVITDVHMPDMDGFEFLELIRLE-MDLPVIMMSA 79

                         90       100
                 ....*....|....*....|...
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKPL 122
Cdd:cd17584   80 DGSTSTVMKGLAHGACDYLLKPV 102
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
 22-122 2.38e-14

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: 68.72  E-value: 2.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYL-DKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGt 100
Cdd:cd17593    3 VLICDDSSMARKQLARALpADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVSG- 81

                         90       100
                 ....*....|....*....|....
gi 857890029 101 dDMSDVAK--ALRFGIKDFLAKPL 122
Cdd:cd17593   82 -DVQPEAKerVLELGALAFLKKPF 104
fixJ PRK09390
response regulator FixJ; Provisional
 22-134 2.60e-14

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 70.80  E-value: 2.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:PRK09390   6 VHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVMTGHG 85

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 857890029 102 DMSDVAKALRFGIKDFLAKPLEDHRHLG---SAIAN 134
Cdd:PRK09390  86 DVPLAVEAMKLGAVDFIEKPFEDERLIGaieRALAQ 121
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
 22-85 2.64e-14

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: 69.15  E-value: 2.64e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 857890029  22 VMLVDDDPIFRRITSAYLDKV-GYKVV-EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEEL 85
Cdd:COG2197    4 VLIVDDHPLVREGLRALLEAEpDIEVVgEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
 22-121 2.74e-14

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: 68.53  E-value: 2.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:cd17615    2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAKD 81

                         90       100
                 ....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKP 121
Cdd:cd17615   82 SVEDRIAGLTAGGDDYVTKP 101
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
 22-123 3.45e-14

phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 68.28  E-value: 3.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80

                         90       100
                 ....*....|....*....|..
gi 857890029 102 DMSDVAKALRFGIKDFLAKPLE 123
Cdd:cd17624   81 GVDDRVAGLDAGADDYLVKPFA 102
PRK10610 PRK10610
chemotaxis protein CheY;
23-122 1.06e-13

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 67.31  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  23 MLVDDDPIFRRITSAYLDKVGY-KVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLE--YPSLPMIVVSG 99
Cdd:PRK10610   9 LVVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADgaMSALPVLMVTA 88

                         90       100
                 ....*....|....*....|...
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKPL 122
Cdd:PRK10610  89 EAKKENIIAAAQAGASGYVVKPF 111
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
 22-124 1.48e-13

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 66.58  E-value: 1.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEyPSL---PMIVVS 98
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSD-PDLkdiPVILLT 79

                         90       100
                 ....*....|....*....|....*.
gi 857890029  99 GTDDMSDVAKALRFGIKDFLAKPLED 124
Cdd:cd17598   80 TLSDPRDVIRGLECGADNFITKPYDE 105
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
 22-121 1.70e-13

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 69.06  E-value: 1.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSlEYPSLPMIVVSGTD 101
Cdd:PRK10529   4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLR-QWSAIPVIVLSARS 82

                         90       100
                 ....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKP 121
Cdd:PRK10529  83 EESDKIAALDAGADDYLSKP 102
PRK10766 PRK10766
two-component system response regulator TorR;
18-123 1.90e-13

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 68.91  E-value: 1.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  18 NQKCVMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSlEYPSLPMIVV 97
Cdd:PRK10766   1 MSYHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELR-SRSTVGIILV 79

                         90       100
                 ....*....|....*....|....*.
gi 857890029  98 SGTDDMSDVAKALRFGIKDFLAKPLE 123
Cdd:PRK10766  80 TGRTDSIDRIVGLEMGADDYVTKPLE 105
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
 23-122 2.17e-13

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: 65.76  E-value: 2.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  23 MLVDDDPIFRRITSAYL--DKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGT 100
Cdd:cd17565    2 YIVDDDKNIIKILSDIIedDDLGEVVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMISQV 81

                         90       100
                 ....*....|....*....|..
gi 857890029 101 DDMSDVAKALRFGIKDFLAKPL 122
Cdd:cd17565   82 SDKEMIGKAYQAGIEFFINKPI 103
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
 23-123 2.47e-13

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: 65.71  E-value: 2.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  23 MLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTDD 102
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80

                         90       100
                 ....*....|....*....|.
gi 857890029 103 MSDVAKALRFGIKDFLAKPLE 123
Cdd:cd17625   81 VEDRVKGLDLGADDYLPKPFS 101
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
 22-121 2.71e-13

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 65.86  E-value: 2.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSlEYPSLPMIVVSGTD 101
Cdd:cd19938    2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIR-RFSDVPIIMVTARV 80

                         90       100
                 ....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKP 121
Cdd:cd19938   81 EEIDRLLGLELGADDYICKP 100
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
 22-121 4.14e-13

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 64.77  E-value: 4.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSlEYPSLPMIVVSGTD 101
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLR-QKSTLPVIFLTSKD 79

                         90       100
                 ....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKP 121
Cdd:cd19936   80 DEIDEVFGLRMGADDYITKP 99
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
 22-121 4.81e-13

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 65.00  E-value: 4.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80

                         90       100
                 ....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKP 121
Cdd:cd19934   81 SWQDKVEGLDAGADDYLTKP 100
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
 22-132 5.02e-13

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: 65.12  E-value: 5.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVE-AENGLDALQKLRNSAPDLIVCDLSMP-ILDGIELVEELSLEYPsLPMIVVSG 99
Cdd:cd17534    3 ILIVEDEAIIALDLKEILESLGYEVVGiADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREKFD-IPVIFLTA 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 857890029 100 TDD---MSDVAKALRFGikdFLAKPLEDhRHLGSAI 132
Cdd:cd17534   82 YSDeetLERAKETNPYG---YLVKPFNE-RELKAAI 113
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
 22-121 5.22e-13

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: 65.02  E-value: 5.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSlEYPSLPMIVVSGTD 101
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELR-KTSQVPVLMLTARG 79

                         90       100
                 ....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKP 121
Cdd:cd17623   80 DDIDRILGLELGADDYLPKP 99
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
 22-123 1.43e-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: 63.97  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDK--VGYKVVEAENGLDALQKLR-------NSAPDLIVCDLSMPILDGIELVEEL--SLEYP 90
Cdd:cd17557    2 ILLVEDNPGDAELIQEAFKEagVPNELHVVRDGEEALDFLRgegeyadAPRPDLILLDLNMPRMDGFEVLREIkaDPDLR 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 857890029  91 SLPMIVVSGTDDMSDVAKALRFGIKDFLAKPLE 123
Cdd:cd17557   82 RIPVVVLTTSDAEEDIERAYELGANSYIVKPVD 114
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
 22-121 1.55e-12

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: 63.60  E-value: 1.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYpSLPMIVVSGTD 101
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTS-NVPIIMLTAKD 79

                         90       100
                 ....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKP 121
Cdd:cd17614   80 SEVDKVLGLELGADDYVTKP 99
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
 22-124 1.69e-12

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 63.38  E-value: 1.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:cd17537    3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGHG 82

                         90       100
                 ....*....|....*....|...
gi 857890029 102 DMSDVAKALRFGIKDFLAKPLED 124
Cdd:cd17537   83 DVPMAVEAMKAGAVDFLEKPFRD 105
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
 22-123 2.30e-12

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: 63.16  E-value: 2.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSlEYPSLPMIVVSGTD 101
Cdd:cd19939    2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVR-EHSHVPILMLTART 80

                         90       100
                 ....*....|....*....|..
gi 857890029 102 DMSDVAKALRFGIKDFLAKPLE 123
Cdd:cd19939   81 EEMDRVLGLEMGADDYLCKPFS 102
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
 22-125 4.08e-12

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 62.40  E-value: 4.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYpSLPMIVVSGTD 101
Cdd:cd17622    3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKY-QGPILLLTALD 81

                         90       100
                 ....*....|....*....|....
gi 857890029 102 DMSDVAKALRFGIKDFLAKPLEDH 125
Cdd:cd17622   82 SDIDHILGLELGADDYVVKPVEPA 105
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
 22-128 1.35e-11

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: 60.92  E-value: 1.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEyPSLPMIVVSG-T 100
Cdd:cd17594    2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRAR-SDVPIIIISGdR 80

                         90       100
                 ....*....|....*....|....*...
gi 857890029 101 DDMSDVAKALRFGIKDFLAKPLEDHRHL 128
Cdd:cd17594   81 RDEIDRVVGLELGADDYLAKPFGLRELL 108
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
 22-121 2.09e-11

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: 60.34  E-value: 2.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLE--YPSLPMIVVSG 99
Cdd:cd17618    3 ILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDemTRDIPIIMLTA 82

                         90       100
                 ....*....|....*....|..
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKP 121
Cdd:cd17618   83 RGEEEDKVRGLEAGADDYITKP 104
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
 22-123 2.12e-11

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 64.89  E-value: 2.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 85

                         90       100
                 ....*....|....*....|..
gi 857890029 102 DMSDVAKALRFGIKDFLAKPLE 123
Cdd:PRK10923  86 DLDAAVSAYQQGAFDYLPKPFD 107
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
 22-101 2.30e-11

phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 60.53  E-value: 2.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYK-VVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGT 100
Cdd:cd17530    3 VLVLDDDPFQCMMAATILEDLGPGnVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMSGL 82


                 .
gi 857890029 101 D 101
Cdd:cd17530   83 D 83
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
 22-121 2.72e-11

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 59.47  E-value: 2.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80

                         90       100
                 ....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKP 121
Cdd:cd19926   81 SLDTAIEALKAGAFDFLTKP 100
pleD PRK09581
response regulator PleD; Reviewed
 22-124 3.25e-11

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 64.15  E-value: 3.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPS--LPMIVVSG 99
Cdd:PRK09581   5 ILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATthIPVVMVTA 84

                         90       100
                 ....*....|....*....|....*
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKPLED 124
Cdd:PRK09581  85 LDDPEDRVRGLEAGADDFLTKPIND 109
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
 22-121 3.53e-11

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: 59.60  E-value: 3.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSlEYPSLPMIVVSGTD 101
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIR-QISNVPIIFISSRD 79

                         90       100
                 ....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKP 121
Cdd:cd18159   80 DNMDQVMAINMGGDDYITKP 99
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
 22-121 4.73e-11

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: 58.75  E-value: 4.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSlEYPSLPMIVVSGTD 101
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLR-ARSNVPVIMVTAKD 79

                         90       100
                 ....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKP 121
Cdd:cd17621   80 SEIDKVVGLELGADDYVTKP 99
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
 22-123 4.99e-11

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 61.58  E-value: 4.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRR------ITSAYLDKVGykvvEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMI 95
Cdd:PRK10651   9 ILLIDDHPMLRTgvkqliSMAPDITVVG----EASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRIV 84

                         90       100
                 ....*....|....*....|....*...
gi 857890029  96 VVSGTDDMSDVAKALRFGIKDFLAKPLE 123
Cdd:PRK10651  85 VFSVSNHEEDVVTALKRGADGYLLKDME 112
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
 22-121 5.11e-11

phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; Escherichia coli CusR is part of the CusS/CusR two-component system (TCS) that is involved in response to copper and silver. Other members of this subfamily include Escherichia coli PcoR, Pseudomonas syringae CopR, and Streptomyces coelicolor CutR, which are all transcriptional regulatory proteins and components of TCSs that regulate genes involved in copper resistance and/or metabolism. member of the subfamily is Escherichia coli HprR (hydrogen peroxide response regulator), previously called YdeW, which is part of the HprSR (or YedVW) TCS involved in stress response to hydrogen peroxide, as well as Cupriavidus metallidurans CzcR, which is part of the CzcS/CzcR TCS involved in the control of cobalt, zinc, and cadmium homeostasis. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 58.61  E-value: 5.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIfrriTSAYLDKV----GYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVV 97
Cdd:cd19935    1 ILVVEDEKK----LAEYLKKGlteeGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLML 76

                         90       100
                 ....*....|....*....|....
gi 857890029  98 SGTDDMSDVAKALRFGIKDFLAKP 121
Cdd:cd19935   77 TARDSVEDRVKGLDLGADDYLVKP 100
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
22-147 5.19e-11

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 62.13  E-value: 5.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDpifRRITS---AYLDKVGYKVVEAENGLDALQKLRNSApDLIVCDLSMPILDGIELVEELSLEYpSLPMIVVS 98
Cdd:PRK10955   4 ILLVDDD---RELTSllkELLEMEGFNVIVAHDGEQALDLLDDSI-DLLLLDVMMPKKNGIDTLKELRQTH-QTPVIMLT 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 857890029  99 GTDDMSDVAKALRFGIKDFLAKPLEDhRHLGSAIANTLTDSfdNISDQR 147
Cdd:PRK10955  79 ARGSELDRVLGLELGADDYLPKPFND-RELVARIRAILRRS--HWSEQQ 124
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
 22-136 7.53e-11

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AlgR-like group of LytTR/AlgR family response regulators are Streptococcus agalactiae sensory transduction protein LytR, Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR, Bacillus subtilis sensory transduction protein LytT, and Escherichia coli transcriptional regulatory protein BtsR, which are members of two-component regulatory systems. LytR and LytT are components of regulatory systems that regulate genes involved in cell wall metabolism. AlgR positively regulates the algD gene, which codes for a GDP-mannose dehydrogenase, a key enzyme in the alginate biosynthesis pathway. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 58.70  E-value: 7.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVV--EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSlEYPSLPMIV-VS 98
Cdd:cd17532    1 ALIVDDEPLAREELRYLLEEHPDIEIvgEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLS-KLAKPPLIVfVT 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 857890029  99 GTDDMSdvAKALRFGIKDFLAKPLEDHRhlgsaIANTL 136
Cdd:cd17532   80 AYDEYA--VEAFELNAVDYLLKPFSEER-----LAEAL 110
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
 22-121 7.92e-11

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: 58.64  E-value: 7.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEyPSLPMIVVSGTD 101
Cdd:cd17626    3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAE-SGVPIVMLTAKS 81

                         90       100
                 ....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKP 121
Cdd:cd17626   82 DTVDVVLGLESGADDYVAKP 101
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
 22-121 9.52e-11

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: 58.56  E-value: 9.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKL--RNSAPDLIVCDLSMPILDGIELVEELSLEYPSL--PMIV- 96
Cdd:cd19933    3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLasAEHSFQLVLLDLCMPEMDGFEVALRIRKLFGRRerPLIVa 82

                         90       100
                 ....*....|....*....|....*.
gi 857890029  97 -VSGTDDMSDvAKALRFGIKDFLAKP 121
Cdd:cd19933   83 lTANTDDSTR-EKCLSLGMNGVITKP 107
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
22-122 1.31e-10

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 63.21  E-value: 1.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029   22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:PRK09959  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040

                          90       100
                  ....*....|....*....|.
gi 857890029  102 DMSDVAKALRFGIKDFLAKPL 122
Cdd:PRK09959 1041 QANEREKGLSCGMNLCLFKPL 1061
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
 22-123 2.50e-10

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 57.56  E-value: 2.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:cd17553    3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAYG 82

                         90       100
                 ....*....|....*....|..
gi 857890029 102 DMSDVAKALRFGIKDFLAKPLE 123
Cdd:cd17553   83 ELDMIQESKELGALTHFAKPFD 104
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
 22-121 3.49e-10

phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is part of the CckA-ChpT-CtrA phosphorelay that is conserved in alphaproteobacteria and is important in orchestrating the cell cycle, polar development, and flagellar biogenesis. CtrA is the master regulator of flagella synthesis genes and also regulates genes involved in the cell cycle, exopolysaccharide synthesis, and cyclic-di-GMP signaling. CtrA is active as a transcription factor when phosphorylated. It is a member of the OmpR family of DNA-binding response regulators, characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 57.03  E-value: 3.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80

                         90       100
                 ....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKP 121
Cdd:cd17616   81 DIEDKVKGLGFGADDYMTKP 100
PRK15479 PRK15479
transcriptional regulator TctD;
22-123 3.59e-10

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 59.35  E-value: 3.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:PRK15479   3 LLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTARS 82

                         90       100
                 ....*....|....*....|..
gi 857890029 102 DMSDVAKALRFGIKDFLAKPLE 123
Cdd:PRK15479  83 AVADRVKGLNVGADDYLPKPFE 104
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
 22-122 4.20e-10

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 56.99  E-value: 4.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKL-----------RNSAPDLIVCDLSMPILDGIEL---VEELSl 87
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLgledeedssnfNEPKVNMIITDYCMPGMTGYDLlkkVKESS- 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 857890029  88 EYPSLPMIVVSGTDDMSDVAKALRFGIKDFLAKPL 122
Cdd:cd17581   80 ALKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPV 114
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
 22-121 8.32e-10

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


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 55.59  E-value: 8.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80

                         90       100
                 ....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKP 121
Cdd:cd19928   81 TLMTAVKAAERGAFEYLPKP 100
ompR PRK09468
osmolarity response regulator; Provisional
 22-121 9.44e-10

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 58.45  E-value: 9.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENG--LDALqkLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSG 99
Cdd:PRK09468   8 ILVVDDDMRLRALLERYLTEQGFQVRSAANAeqMDRL--LTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPIIMLTA 85

                         90       100
                 ....*....|....*....|..
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKP 121
Cdd:PRK09468  86 KGEEVDRIVGLEIGADDYLPKP 107
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
6-90 9.97e-10

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 59.99  E-value: 9.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029   6 SQPVMTSAQEVINQKCVMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVE-- 83
Cdd:PRK10841 788 ALPSTDKAVSDNDDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQrl 867


                 ....*...
gi 857890029  84 -ELSLEYP 90
Cdd:PRK10841 868 rQLGLTLP 875
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
 22-137 1.40e-09

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 55.43  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRR-----ITSAYLDKVgykVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIV 96
Cdd:cd19931    1 VLLIDDHPLLRKgikqlIELDPDFTV---VGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVI 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 857890029  97 VSGTDDMSDVAKALRFGIKDFLAKPLEDHRhLGSAIANTLT 137
Cdd:cd19931   78 LTVSDAEDDVVTALRAGADGYLLKDMEPED-LLEALKQAAS 117
PRK13856 PRK13856
two-component response regulator VirG; Provisional
 20-121 1.90e-09

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 57.52  E-value: 1.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  20 KCVMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEyPSLPMIVVSG 99
Cdd:PRK13856   2 KHVLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSLATK-SDVPIIIISG 80

                         90       100
                 ....*....|....*....|...
gi 857890029 100 TD-DMSDVAKALRFGIKDFLAKP 121
Cdd:PRK13856  81 DRlEEADKVVALELGATDFIAKP 103
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
 22-123 3.09e-09

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: 53.97  E-value: 3.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDA--LQKLRNSapDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSG 99
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGeyYIDIRNY--DLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSD 78

                         90       100
                 ....*....|....*....|....
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKPLE 123
Cdd:cd17573   79 NPKTEQEIEAFKEGADDYIAKPFD 102
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
23-132 3.19e-09

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 56.44  E-value: 3.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  23 MLVDDDPIFRRITSAYLDKVGYKVV-EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:PRK09958   4 IIIDDHPLAIAAIRNLLIKNDIEILaELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIVSAKN 83

                         90       100       110
                 ....*....|....*....|....*....|.
gi 857890029 102 DMSDVAKALRFGIKDFLAKPlEDHRHLGSAI 132
Cdd:PRK09958  84 DHFYGKHCADAGANGFVSKK-EGMNNIIAAI 113
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
 22-121 1.01e-08

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 54.97  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPifrRI--TSAY-LDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVS 98
Cdd:PRK11083   6 ILLVEDEQ---AIadTLVYaLQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFLT 82

                         90       100
                 ....*....|....*....|...
gi 857890029  99 GTDDMSDVAKALRFGIKDFLAKP 121
Cdd:PRK11083  83 ARSDEVDRLVGLEIGADDYVAKP 105
PRK15369 PRK15369
two component system response regulator;
17-113 1.40e-08

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 54.31  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  17 INQKcVMLVDD-DPIFRRITSAYLDKVGYKVV-EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPM 94
Cdd:PRK15369   2 KNYK-ILLVDDhELIINGIKNMLAPYPRYKIVgQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRWPAMNI 80

                         90
                 ....*....|....*....
gi 857890029  95 IVVSGTDDMSDVAKALRFG 113
Cdd:PRK15369  81 LVLTARQEEHMASRTLAAG 99
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
22-122 1.48e-08

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 54.72  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPS--LPMIVVSG 99
Cdd:PRK10161   5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTrdIPVVMLTA 84

                         90       100
                 ....*....|....*....|...
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKPL 122
Cdd:PRK10161  85 RGEEEDRVRGLETGADDYITKPF 107
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
 1-192 2.06e-08

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 56.01  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029   1 MYKTHSQPVMTSAQEVINQKcVMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGI- 79
Cdd:PRK11107 650 CHHKQPPLLPPTDESRLPLT-VMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIr 728

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  80 --ELVEELSLEYpSLPMIVVSGTDDMSDVAKALRFGIKDFLAKPLEDHrhlgsAIANTLTDsfdnISDQRDFSSQWFCVD 157
Cdd:PRK11107 729 acELIRQLPHNQ-NTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEA-----MLKQVLLR----YKPGPKFTSRVVAPE 798

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 857890029 158 DGGEIPEDQE-LHWHLNYLQDN--PSAAKDLLHAL---LPE 192
Cdd:PRK11107 799 PPEPVHFPNAtLDWQLALRQAAgkPDLARDMLQMLldfLPE 839
PRK10336 PRK10336
two-component system response regulator QseB;
22-122 3.08e-08

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 53.75  E-value: 3.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:PRK10336   3 ILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTARD 82

                         90       100
                 ....*....|....*....|.
gi 857890029 102 DMSDVAKALRFGIKDFLAKPL 122
Cdd:PRK10336  83 ALAERVEGLRLGADDYLCKPF 103
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
 10-121 3.29e-08

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 53.92  E-value: 3.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  10 MTSAQEVINQKCVMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSlEY 89
Cdd:PRK10710   1 MTELPIDENTPRILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIR-RF 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 857890029  90 PSLPMIVVSGTDDMSDVAKALRFGIKDFLAKP 121
Cdd:PRK10710  80 SDIPIVMVTAKIEEIDRLLGLEIGADDYICKP 111
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
 22-121 4.88e-08

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


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 51.21  E-value: 4.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKvGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:cd17596    3 ILVVDDEVRSLEALRRTLEE-DFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISGYT 81

                         90       100
                 ....*....|....*....|.
gi 857890029 102 DMSDVAKALR-FGIKDFLAKP 121
Cdd:cd17596   82 DSEDIIAGINeAGIYQYLTKP 102
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
 22-121 5.18e-08

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 50.72  E-value: 5.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGY-KVVEAENGLDALQKLRNSAPDLIVCDLSMPI-LDGIELVEELSLEY---PSLPMIV 96
Cdd:cd17589    1 FLIVDDQPTFRSMLKSMLRSLGVtRIDTASSGEEALRMCENKTYDIVLCDYNLGKgKNGQQLLEELRHKKlisPSTVFIM 80

                         90       100
                 ....*....|....*....|....*
gi 857890029  97 VSGTDDMSDVAKALRFGIKDFLAKP 121
Cdd:cd17589   81 VTGESSRAMVLSALELEPDDYLLKP 105
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
 8-95 5.20e-08

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 54.91  E-value: 5.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029   8 PVMTSAQEV-INQKCVMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAP-DLIVCDLSMPILDGIELVEEL 85
Cdd:PRK11466 669 VPKTVNQAVrLDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNSEPfAAALVDFDLPDYDGITLARQL 748

                         90
                 ....*....|
gi 857890029  86 SLEYPSLPMI 95
Cdd:PRK11466 749 AQQYPSLVLI 758
PRK10816 PRK10816
two-component system response regulator PhoP;
22-133 6.40e-08

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 52.82  E-value: 6.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:PRK10816   3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTARE 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 857890029 102 DMSDVAKALRFGIKDFLAKPLedhrHLGSAIA 133
Cdd:PRK10816  83 SWQDKVEVLSAGADDYVTKPF----HIEEVMA 110
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
 22-121 6.78e-08

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


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 50.30  E-value: 6.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLD-KVGYKVV-EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEEL-SLEYPSLPMIVVS 98
Cdd:cd17561    4 VLIADDNREFVQLLEEYLNsQPDMEVVgVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLrRMRLEKRPKIIML 83

                         90       100
                 ....*....|....*....|....
gi 857890029  99 GTDDMSDVA-KALRFGIKDFLAKP 121
Cdd:cd17561   84 TAFGQEDITqRAVELGASYYILKP 107
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
 22-123 7.35e-08

sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a transcription factor critical for the initiation of sporulation. It contains a response regulator receiver domain (pfam00072). In Bacillus subtilis, it works together with response regulator Spo0F and the phosphotransferase Spo0B, both of which are missing from at least some sporulating species and thus not part of the endospore forming bacteria minimal gene set. Spo0A, however, is universal among endospore-forming species. [Cellular processes, Sporulation and germination]


Pssm-ID: 131922 [Multi-domain]  Cd Length: 262  Bit Score: 52.87  E-value: 7.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029   22 VMLVDDDPIFRRITSAYLD-KVGYKVVE-AENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELS----LEYPSLPMI 95
Cdd:TIGR02875   5 IVIADDNKEFCNLLKEYLAaQPDMEVVGvAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNeielSARPRVIML 84

                          90       100
                  ....*....|....*....|....*...
gi 857890029   96 VVSGTDDMSDvaKALRFGIKDFLAKPLE 123
Cdd:TIGR02875  85 SAFGQEKITQ--RAVALGADYYVLKPFD 110
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
22-144 1.45e-07

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 52.58  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKV-GYKVV-EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPsLPMIVVSG 99
Cdd:PRK12555   3 IGIVNDSPLAVEALRRALARDpDHEVVwVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAERP-CPILIVTS 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 857890029 100 T--DDMSDVAKALRFGIKDFLAKPLEDHRHLGSAIANTLTDSFDNIS 144
Cdd:PRK12555  82 LteRNASRVFEAMGAGALDAVDTPTLGIGAGLEEYAAELLAKIDQIG 128
PRK15347 PRK15347
two component system sensor kinase;
22-122 7.37e-07

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 51.18  E-value: 7.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELV----EELSLEYPSLPMIVV 97
Cdd:PRK15347 693 ILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTqlwrDDPNNLDPDCMIVAL 772

                         90       100
                 ....*....|....*....|....*
gi 857890029  98 SGTDDMSDVAKALRFGIKDFLAKPL 122
Cdd:PRK15347 773 TANAAPEEIHRCKKAGMNHYLTKPV 797
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
22-132 1.01e-06

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 49.08  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLD-KVGYKVV-EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSG 99
Cdd:PRK10403   9 VLIVDDHPLMRRGVRQLLElDPGFEVVaEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQIIILTV 88

                         90       100       110
                 ....*....|....*....|....*....|...
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKPlEDHRHLGSAI 132
Cdd:PRK10403  89 SDASSDVFALIDAGADGYLLKD-SDPEVLLEAI 120
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
 22-132 1.20e-06

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 46.88  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLD-KVGYKVV-EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSG 99
Cdd:cd19930    1 VLIAEDQEMVRGALAALLElEDDLEVVaQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTT 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 857890029 100 TDDMSDVAKALRFGIKDFLAK--PLEdhrHLGSAI 132
Cdd:cd19930   81 FGRPGYFRRALAAGVDGYVLKdrPIE---ELADAI 112
PRK11173 PRK11173
two-component response regulator; Provisional
 22-121 2.50e-06

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 48.09  E-value: 2.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSlEYPSLPMIVVSGTD 101
Cdd:PRK11173   6 ILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELR-EQANVALMFLTGRD 84

                         90       100
                 ....*....|....*....|
gi 857890029 102 DMSDVAKALRFGIKDFLAKP 121
Cdd:PRK11173  85 NEVDKILGLEIGADDYITKP 104
PRK10360 PRK10360
transcriptional regulator UhpA;
22-120 2.57e-06

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 47.66  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRritSAYLDKVGYK-----VVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELsleyPS-LPMI 95
Cdd:PRK10360   4 VALIDDHLIVR---SGFAQLLGLEpdlqvVAEFGSGREALAGLPGRGVQVCICDISMPDISGLELLSQL----PKgMATI 76

                         90       100
                 ....*....|....*....|....*
gi 857890029  96 VVSGTDDMSDVAKALRFGIKDFLAK 120
Cdd:PRK10360  77 MLSVHDSPALVEQALNAGARGFLSK 101
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
 22-122 3.66e-06

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 48.78  E-value: 3.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYP--SLPMIVVSG 99
Cdd:PRK11091 528 ILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPreDLPPLVALT 607

                         90       100
                 ....*....|....*....|...
gi 857890029 100 TDDMSDVAKALRFGIKDFLAKPL 122
Cdd:PRK11091 608 ANVLKDKKEYLDAGMDDVLSKPL 630
pleD PRK09581
response regulator PleD; Reviewed
 22-123 5.21e-06

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 47.97  E-value: 5.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPI-FRRITSAyLDKVgYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEEL-SLEYPS-LPMIVVS 98
Cdd:PRK09581 158 ILLVDDDVSqAERIANI-LKEE-FRVVVVSDPSEALFNAAETNYDLVIVSANFENYDPLRLCSQLrSKERTRyVPILLLV 235

                         90       100
                 ....*....|....*....|....*
gi 857890029  99 GTDDMSDVAKALRFGIKDFLAKPLE 123
Cdd:PRK09581 236 DEDDDPRLVKALELGVNDYLMRPID 260
dpiA PRK10046
two-component response regulator DpiA; Provisional
 22-137 7.64e-06

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 46.55  E-value: 7.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKV-GY-KVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEEL-SLEYPSlPMIVVS 98
Cdd:PRK10046   7 LLIVEDETPLAEMHAEYIRHIpGFsQILLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELvQAHYPG-DVVFTT 85

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 857890029  99 GTDDMSDVAKALRFGIKDFLAKPLEDHRhlgsaIANTLT 137
Cdd:PRK10046  86 AASDMETVSEAVRCGVFDYLIKPIAYER-----LGQTLT 119
PRK11697 PRK11697
two-component system response regulator BtsR;
22-137 7.93e-06

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 46.76  E-value: 7.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVG-YKVV-EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEypSLPMIV-VS 98
Cdd:PRK11697   4 VLIVDDEPLAREELRELLQEEGdIEIVgECSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELVGMLDPE--HMPYIVfVT 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 857890029  99 GTDDmsdvakalrFGIK-------DFLAKPLEDHRhlgsaIANTLT 137
Cdd:PRK11697  82 AFDE---------YAIKafeehafDYLLKPIDPAR-----LAKTLA 113
PRK09483 PRK09483
response regulator; Provisional
 22-120 8.51e-06

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 46.25  E-value: 8.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKV-GYKVV-EAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSG 99
Cdd:PRK09483   4 VLLVDDHELVRAGIRRILEDIkGIKVVgEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKILRYTPDVKIIMLTV 83

                         90       100
                 ....*....|....*....|.
gi 857890029 100 TDDMSDVAKALRFGIKDFLAK 120
Cdd:PRK09483  84 HTENPLPAKVMQAGAAGYLSK 104
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
 22-122 9.87e-06

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 46.07  E-value: 9.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:PRK09836   3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTALG 82

                         90       100
                 ....*....|....*....|.
gi 857890029 102 DMSDVAKALRFGIKDFLAKPL 122
Cdd:PRK09836  83 TIEHRVKGLELGADDYLVKPF 103
PRK11517 PRK11517
DNA-binding response regulator HprR;
22-122 1.09e-05

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 46.04  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSlPMIVVSGTD 101
Cdd:PRK11517   3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQT-PVICLTARD 81

                         90       100
                 ....*....|....*....|.
gi 857890029 102 DMSDVAKALRFGIKDFLAKPL 122
Cdd:PRK11517  82 SVDDRVRGLDSGANDYLVKPF 102
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
 22-125 1.42e-05

REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a pseudo receiver (psREC)-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the REC-like adaptor domain D2 of PleD, which is an inactive domain.


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 43.84  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDP-IFRRITSAYldKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEEL-SLEYP-SLPMIVVS 98
Cdd:cd17539    1 VLLVDDRPsSAERIAAML--SSEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLrSLERTrQLPILAVA 78

                         90       100
                 ....*....|....*....|....*..
gi 857890029  99 GTDDMSDVAKALRFGIKDFLAKPLEDH 125
Cdd:cd17539   79 DPGDRGRLIRALEIGVNDYLVRPIDPN 105
PRK10643 PRK10643
two-component system response regulator PmrA;
22-158 1.83e-05

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 45.41  E-value: 1.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSLPMIVVSGTD 101
Cdd:PRK10643   3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTARD 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 857890029 102 DMSDVAKALRFGIKDFLAKP--LED---------HRHLGSAiANTLTDsfDNISdqRDFSSQWFCVDD 158
Cdd:PRK10643  83 TLEDRVAGLDVGADDYLVKPfaLEElhariraliRRHQGQG-ENELQV--GNLT--LNLGRQQVWLDG 145
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
 22-90 1.95e-05

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


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 43.86  E-value: 1.95e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 857890029  22 VMLVDDDP-----IFRRITSAYLDKvgYKVVEAENGLDALQ-----KLRNSAPDLIVCDLSMPILDGIELVEELSLEYP 90
Cdd:cd17595    3 ILTVDDDPqvlraVARDLRRQYGKD--YRVLRADSGAEALDalkelKLRGEAVALFLVDQRMPEMDGVEFLEKAMELFP 79
PLN03029 PLN03029
type-a response regulator protein; Provisional
 22-123 2.00e-05

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 45.41  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKL-----RNSAPD---------------LIVCDLSMPILDGIEL 81
Cdd:PLN03029  11 VLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLglhedDRSNPDtpsvspnshqevevnLIITDYCMPGMTGYDL 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 857890029  82 VEELSlEYPSL---PMIVVSGTDDMSDVAKALRFGIKDFLAKPLE 123
Cdd:PLN03029  91 LKKIK-ESSSLrniPVVIMSSENVPSRITRCLEEGAEEFFLKPVQ 134
PRK13557 PRK13557
histidine kinase; Provisional
 4-104 3.04e-05

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 45.82  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029   4 THSQPVMTSAQEVINQKCVMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSA-PDLIVCDLSMP-ILDGIEL 81
Cdd:PRK13557 400 NPEQEPKARAIDRGGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHPeVDLLFTDLIMPgGMNGVML 479

                         90       100
                 ....*....|....*....|...
gi 857890029  82 VEELSLEYPSLPMIVVSGTDDMS 104
Cdd:PRK13557 480 AREARRRQPKIKVLLTTGYAEAS 502
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
 22-120 9.01e-04

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 40.39  E-value: 9.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGYKVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELSLEYPSlPMIVVSGTD 101
Cdd:PRK10701   4 IVFVEDDAEVGSLIAAYLAKHDIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPKWQG-PIVLLTSLD 82

                         90       100
                 ....*....|....*....|
gi 857890029 102 -DMSDVAkALRFGIKDFLAK 120
Cdd:PRK10701  83 sDMNHIL-ALEMGACDYILK 101
PRK10430 PRK10430
two-component system response regulator DcuR;
22-152 1.48e-03

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 39.71  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKV-GYKVVEAENGLDALQKLRNSAP---DLIVCDLSMPILDGIELVEELSLEYPSLPMIVV 97
Cdd:PRK10430   4 VLIVDDDAMVAELNRRYVAQIpGFQCCGTASTLEQAKEIIFNSDtpiDLILLDIYMQQENGLDLLPVLHEAGCKSDVIVI 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 857890029  98 SGTDDMSDVAKALRFGIKDFLAKPLEDHRhLGSAIANTLTDSfdNISDQRDFSSQ 152
Cdd:PRK10430  84 SSAADAATIKDSLHYGVVDYLIKPFQASR-FEEALTGWRQKK--MALEKHQYYDQ 135
PRK14084 PRK14084
DNA-binding response regulator;
22-126 2.12e-03

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 39.35  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIFRRITSAYLDKVGY--KVVEAENGLDALQKLRNSAPDLIVCDLSMPILDGIELVEELS-LEYPslPMIVVS 98
Cdd:PRK14084   3 ALIVDDEPLARNELTYLLNEIGGfeEINEAENVKETLEALLINQYDIIFLDINLMDESGIELAAKIQkMKEP--PAIIFA 80

                         90       100
                 ....*....|....*....|....*...
gi 857890029  99 GTDDMSDVaKALRFGIKDFLAKPLEDHR 126
Cdd:PRK14084  81 TAHDQFAV-KAFELNATDYILKPFEQKR 107
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
 22-120 9.50e-03

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: 35.85  E-value: 9.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890029  22 VMLVDDDPIF----RRITSAYLDKVGYKVVEAENGLDALQKLRnsaPDLIVCDLSMPILDGIELVEELSL--EYPSLPMI 95
Cdd:cd17575    3 VLLVDDQAIIgeavRRALADEEDIDFHYCSDPTEAIEVASQIK---PTVILQDLVMPGVDGLTLVRFFRAnpATRDIPII 79

                         90       100
                 ....*....|....*....|....*
gi 857890029  96 VVSGTDDMSDVAKALRFGIKDFLAK 120
Cdd:cd17575   80 VLSTKEEPEVKSEAFALGANDYLVK 104
 
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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