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Conserved domains on  [gi|15599592|ref|NP_253086|]
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two-component response regulator [Pseudomonas aeruginosa PAO1]

Protein Classification

response regulator( domain architecture ID 11467115)

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
51-173 9.19e-27

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: 104.61  E-value: 9.19e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  51 LSILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESinHYTYI 130
Cdd:COG3706   2 ARILVVDDDPTNRKLLRRLLEAAGYE-VVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRT--ADIPI 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15599592 131 VLLTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYAADRL 173
Cdd:COG3706  79 IFLTALDDEEDRARALEAGADDYLTKPFDPEELLARVDLVARY 121
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
98-356 2.36e-11

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


:

Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 63.46  E-value: 2.36e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  98 VLLADWLMPEMDGLELTARVRQLDESINHYTYIVLLTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYAADRLCNTL 177
Cdd:COG2199  14 LLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592 178 QRLLVENRLLTENIARMEERNLVDTLTGLGNPRYLRQKLADSLRQVETRGGALCYLLVGMPEAPVLRQRHGEAFHRELLL 257
Cdd:COG2199  94 LLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLK 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592 258 GVARRLQQLVRPLDVLVRLDEQHFALITLVEDLHECSSSSfKRLHDGLNLKAFKTSEGFISLKA--GIAMLGLDSGalpl 335
Cdd:COG2199 174 EVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALA-ERLREALEQLPFELEGKELRVTVsiGVALYPEDGD---- 248
                       250       260
                ....*....|....*....|.
gi 15599592 336 GIDELLQRTEALLPDAYASGR 356
Cdd:COG2199 249 SAEELLRRADLALYRAKRAGR 269
 
Name Accession Description Interval E-value
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
51-173 9.19e-27

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: 104.61  E-value: 9.19e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  51 LSILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESinHYTYI 130
Cdd:COG3706   2 ARILVVDDDPTNRKLLRRLLEAAGYE-VVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRT--ADIPI 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15599592 131 VLLTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYAADRL 173
Cdd:COG3706  79 IFLTALDDEEDRARALEAGADDYLTKPFDPEELLARVDLVARY 121
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
54-156 1.99e-22

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: 90.16  E-value: 1.99e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  54 LVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLdesiNHYTYIVLL 133
Cdd:cd17574   1 LVVEDDEEIAELLSDYLEKEGYE-VDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREK----GSDIPIIML 75
                        90       100
                ....*....|....*....|...
gi 15599592 134 TGKEGENVLGEAFDRGVDDFVSK 156
Cdd:cd17574  76 TAKDEEEDKVLGLELGADDYITK 98
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
53-156 2.95e-19

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: 82.20  E-value: 2.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592    53 ILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESinhyTYIVL 132
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGY-VVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPT----TPVII 75
                          90       100
                  ....*....|....*....|....
gi 15599592   133 LTGKEGENVLGEAFDRGVDDFVSK 156
Cdd:pfam00072  76 LTAHGDEDDAVEALEAGADDFLSK 99
PRK15347 PRK15347
two component system sensor kinase;
51-220 2.22e-11

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 65.43  E-value: 2.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   51 LSILVVDDAKFSSAMIGRALSQAGyQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINHYTYI 130
Cdd:PRK15347 691 LQILLVDDVETNRDIIGMMLVELG-QQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNLDPDCMI 769
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  131 VLLTGkegeNVLGEAFDR----GVDDFVSKAAMNEQLVPRI-YAADrlcntLQrllvenrlLTENIARMEERNLVDTLTG 205
Cdd:PRK15347 770 VALTA----NAAPEEIHRckkaGMNHYLTKPVTLAQLARALeLAAE-----YQ--------LLRGIELSPQDSSCSPLLD 832
                        170
                 ....*....|....*
gi 15599592  206 LGNPRyLRQKLADSL 220
Cdd:PRK15347 833 TDDMA-LNSKLYQSL 846
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
98-356 2.36e-11

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 63.46  E-value: 2.36e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  98 VLLADWLMPEMDGLELTARVRQLDESINHYTYIVLLTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYAADRLCNTL 177
Cdd:COG2199  14 LLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592 178 QRLLVENRLLTENIARMEERNLVDTLTGLGNPRYLRQKLADSLRQVETRGGALCYLLVGMPEAPVLRQRHGEAFHRELLL 257
Cdd:COG2199  94 LLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLK 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592 258 GVARRLQQLVRPLDVLVRLDEQHFALITLVEDLHECSSSSfKRLHDGLNLKAFKTSEGFISLKA--GIAMLGLDSGalpl 335
Cdd:COG2199 174 EVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALA-ERLREALEQLPFELEGKELRVTVsiGVALYPEDGD---- 248
                       250       260
                ....*....|....*....|.
gi 15599592 336 GIDELLQRTEALLPDAYASGR 356
Cdd:COG2199 249 SAEELLRRADLALYRAKRAGR 269
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
196-356 3.87e-11

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 60.72  E-value: 3.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592    196 ERNLVDTLTGLGNPRYLRQKLADSLRQVETRGGALCYLLVGMPEAPVLRQRHGEAFHRELLLGVARRLQQLVRPLDVLVR 275
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592    276 LDEQHFALITLVEDLHECSSSSfKRLHDGLNLKAF-KTSEGFISLKAGIAMLGLDsgalPLGIDELLQRTEALLPDAYAS 354
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALA-ERILQQLREPIIiHGIPLYLTISIGVAAYPNP----GEDAEDLLKRADTALYQAKKA 155

                   ..
gi 15599592    355 GR 356
Cdd:smart00267 156 GR 157
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
201-356 4.51e-10

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 57.57  E-value: 4.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592 201 DTLTGLGNPRYLRQKLADSLRQVETRGGALCYLLVGMPEapvLRQ---RHGEAFHRELLLGVARRLQQLVRPLDVLVRL- 276
Cdd:cd01949   3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDH---FKQindTYGHAAGDEVLKEVAERLRSSLRESDLVARLg 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592 277 -DEqhFALITLVEDLHECSSSSfKRLHDGLNLKAFKTSEGF-ISLKAGIAMLGLDSGAlplgIDELLQRTEALLPDAYAS 354
Cdd:cd01949  80 gDE--FAILLPGTDLEEAEALA-ERLREAIEEPFFIDGQEIrVTASIGIATYPEDGED----AEELLRRADEALYRAKRS 152

                ..
gi 15599592 355 GR 356
Cdd:cd01949 153 GR 154
pleD PRK09581
response regulator PleD; Reviewed
52-356 2.44e-08

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 55.29  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   52 SILVVDDAKFSSAMIGRALSQAGYQDIrfASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESinHYTYIV 131
Cdd:PRK09581 157 RILLVDDDVSQAERIANILKEEFRVVV--VSDPSEALFNAAETNYDLVIVSANFENYDPLRLCSQLRSKERT--RYVPIL 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  132 LLTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIyaadrlcNTLQRLLVENRLLTENIARMEERNLVDTLTGLGNPRY 211
Cdd:PRK09581 233 LLVDEDDDPRLVKALELGVNDYLMRPIDKNELLARV-------RTQIRRKRYQDALRNNLEQSIEMAVTDGLTGLHNRRY 305
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  212 LRQKLADSLRQVETRGGALCYLLVGMPEAPVLRQRHGEAFHRELLLGVARRLQQLVRPLDVLVRLDEQHFaLITLVE-DL 290
Cdd:PRK09581 306 FDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEF-VVVMPDtDI 384
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599592  291 HECSSSSfKRLHDGLNLKAFKTSEG--FISLKAGIAMLGLDSGALPlgIDELLQRTEALLPDAYASGR 356
Cdd:PRK09581 385 EDAIAVA-ERIRRKIAEEPFIISDGkeRLNVTVSIGVAELRPSGDT--IEALIKRADKALYEAKNTGR 449
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
199-325 3.10e-08

Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 52.64  E-value: 3.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   199 LVDTLTGLGNPRYLRQKLADSLRQVETRGGALCYLLVGMPEAPVLRQRHGEAFHRELLLGVARRLQQLVRPLDVLVRLDE 278
Cdd:pfam00990   2 AHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGG 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15599592   279 QHFALItLVEDLHECSSSSFKRLHDGLNLKAF----KTSEGFISLKAGIAM 325
Cdd:pfam00990  82 DEFAIL-LPETSLEGAQELAERIRRLLAKLKIphtvSGLPLYVTISIGIAA 131
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
51-106 6.02e-06

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 42.94  E-value: 6.02e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 15599592     51 LSILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMP 106
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYE-VDEATDGEEALELLKEEKPDLILLDIMMP 55
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
201-356 9.87e-06

diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 45.41  E-value: 9.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   201 DTLTGLGNPRYLRQKLaDSLRQVETRGG-ALCYLLVGMPEAPVLRQRHGEAFHRELLLGVARRLQQLVRPLDVLVRLDEQ 279
Cdd:TIGR00254   5 DPLTGLYNRRYLEEML-DSELKRARRFQrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGE 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599592   280 HFALITLVEDLHECSSSSfKRLHDGLNLKAFKTSEG-FISLKAGIAMLGLDSGALPLGidELLQRTEALLPDAYASGR 356
Cdd:TIGR00254  84 EFVVILPGTPLEDALSKA-ERLRDAINSKPIEVAGSeTLTVTVSIGVACYPGHGLTLE--ELLKRADEALYQAKKAGR 158
 
Name Accession Description Interval E-value
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
51-173 9.19e-27

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: 104.61  E-value: 9.19e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  51 LSILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESinHYTYI 130
Cdd:COG3706   2 ARILVVDDDPTNRKLLRRLLEAAGYE-VVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRT--ADIPI 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15599592 131 VLLTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYAADRL 173
Cdd:COG3706  79 IFLTALDDEEDRARALEAGADDYLTKPFDPEELLARVDLVARY 121
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
46-181 2.40e-23

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: 93.76  E-value: 2.40e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  46 MPNPDLSILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDEsiN 125
Cdd:COG0784   1 PPLGGKRILVVDDNPDNRELLRRLLERLGYE-VTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPR--L 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15599592 126 HYTYIVLLTGKEGENVLGEAFDRGVDDFVSKaamneqlvPriYAADRLCNTLQRLL 181
Cdd:COG0784  78 PDIPIIALTAYADEEDRERALEAGADDYLTK--------P--VDPEELLEALRRLL 123
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
54-156 1.99e-22

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: 90.16  E-value: 1.99e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  54 LVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLdesiNHYTYIVLL 133
Cdd:cd17574   1 LVVEDDEEIAELLSDYLEKEGYE-VDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREK----GSDIPIIML 75
                        90       100
                ....*....|....*....|...
gi 15599592 134 TGKEGENVLGEAFDRGVDDFVSK 156
Cdd:cd17574  76 TAKDEEEDKVLGLELGADDYITK 98
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
52-156 2.04e-22

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: 90.60  E-value: 2.04e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  52 SILVVDDAKFSSAMIGRALSQ-AGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINhytyI 130
Cdd:COG4753   1 KVLIVDDEPLIREGLKRILEWeAGFEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTK----I 76
                        90       100
                ....*....|....*....|....*.
gi 15599592 131 VLLTGKEGENVLGEAFDRGVDDFVSK 156
Cdd:COG4753  77 IILSGYSDFEYAQEAIKLGADDYLLK 102
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
47-187 2.53e-22

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: 93.69  E-value: 2.53e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  47 PNPDLSILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESInh 126
Cdd:COG3437   3 TGQAPTVLIVDDDPENLELLRQLLRTLGY-DVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTR-- 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599592 127 YTYIVLLTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYAADRLCNTLQRLLVENRLL 187
Cdd:COG3437  80 DIPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYL 140
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
53-156 1.22e-20

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: 85.98  E-value: 1.22e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLdESINHYTYIVL 132
Cdd:cd17546   1 VLVVDDNPVNRKVLKKLLEKLGYE-VDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIREL-EGGGRRTPIIA 78
                        90       100
                ....*....|....*....|....
gi 15599592 133 LTGKEGENVLGEAFDRGVDDFVSK 156
Cdd:cd17546  79 LTANALEEDREKCLEAGMDDYLSK 102
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
52-195 1.13e-19

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 89.64  E-value: 1.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  52 SILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINhytyIV 131
Cdd:COG2204   4 RILVVDDDPDIRRLLKELLERAGYE-VETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLP----VI 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599592 132 LLTGKEGENVLGEAFDRGVDDFVSKaamneqlvPriYAADRLCNTLQRLLVENRLLTENIARME 195
Cdd:COG2204  79 LLTGYGDVETAVEAIKAGAFDYLTK--------P--FDLEELLAAVERALERRRLRRENAEDSG 132
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
53-172 1.75e-19

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: 85.39  E-value: 1.75e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESInhytYIVL 132
Cdd:COG0745   4 ILVVEDDPDIRELLADALEREGYE-VDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDI----PIIM 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15599592 133 LTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYAADR 172
Cdd:COG0745  79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLR 118
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
53-156 2.95e-19

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: 82.20  E-value: 2.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592    53 ILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESinhyTYIVL 132
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGY-VVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPT----TPVII 75
                          90       100
                  ....*....|....*....|....
gi 15599592   133 LTGKEGENVLGEAFDRGVDDFVSK 156
Cdd:pfam00072  76 LTAHGDEDDAVEALEAGADDFLSK 99
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
54-156 6.66e-19

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 80.73  E-value: 6.66e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  54 LVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESInhytYIVLL 133
Cdd:cd00156   1 LIVDDDPAIRELLKSLLEREGYE-VDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDI----PVIVL 75
                        90       100
                ....*....|....*....|...
gi 15599592 134 TGKEGENVLGEAFDRGVDDFVSK 156
Cdd:cd00156  76 TAKADEEDAVRALELGADDYLVK 98
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
51-168 2.39e-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: 80.07  E-value: 2.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  51 LSILVVDDAKFSSAMIGRALSQAGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQlDESINHYTYI 130
Cdd:cd19923   1 MKVLVVDDFSTMRRIIKNLLKELGFNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRA-DGALSHLPVL 79
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15599592 131 VLLTGKEGENVLgEAFDRGVDDFVSKAAMNEQLVPRIY 168
Cdd:cd19923  80 MVTAEAKKENVI-AAAQAGVNNYIVKPFTAATLKEKLE 116
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
53-156 2.63e-17

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: 77.10  E-value: 2.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDEsiNHYTYIVL 132
Cdd:cd17551   3 ILIVDDNPTNLLLLEALLRSAGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPG--LEDVPIVM 80
                        90       100
                ....*....|....*....|....
gi 15599592 133 LTGKEGENVLGEAFDRGVDDFVSK 156
Cdd:cd17551  81 ITADTDREVRLRALEAGATDFLTK 104
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
51-190 7.05e-16

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 73.47  E-value: 7.05e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  51 LSILVVDDAKFSSAMIGRALSQ-AGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINhyty 129
Cdd:COG4565   4 IRVLIVEDDPMVAELLRRYLERlPGFEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVD---- 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599592 130 IVLLTGKEGENVLGEAFDRGVDDFVSKaamneqlvPriYAADRLCNTLQRLLVENRLLTEN 190
Cdd:COG4565  80 VIVITAARDPETVREALRAGVVDYLIK--------P--FTFERLREALERYLEYRRLLRED 130
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
53-167 4.52e-15

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: 70.77  E-value: 4.52e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINhytyIVL 132
Cdd:cd17542   3 VLIVDDAAFMRMMLKDILTKAGYEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAK----VIM 78
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15599592 133 LTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRI 167
Cdd:cd17542  79 CSAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAV 113
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
53-170 5.08e-15

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: 70.62  E-value: 5.08e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDakfsSAMIGRAL-----SQAGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINhy 127
Cdd:cd17535   1 VLIVDD----HPLVREGLrrlleSEPDIEVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLK-- 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15599592 128 tyIVLLTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYAA 170
Cdd:cd17535  75 --VIVLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAV 115
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
53-169 1.60e-14

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: 69.20  E-value: 1.60e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQDIRfASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQlDESINHyTYIVL 132
Cdd:cd17618   3 ILIVEDEPAIREMIAFNLERAGFDVVE-AEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKR-DEMTRD-IPIIM 79
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15599592 133 LTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYA 169
Cdd:cd17618  80 LTARGEEEDKVRGLEAGADDYITKPFSPRELVARIKA 116
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
52-170 3.44e-14

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


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 68.20  E-value: 3.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  52 SILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESinhyTYIV 131
Cdd:cd17569   2 TILLVDDEPNILKALKRLLRREGY-EVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPD----TVRI 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15599592 132 LLTGKEGENVLGEAFDRG-VDDFVSKAAMNEQLVPRIYAA 170
Cdd:cd17569  77 LLTGYADLDAAIEAINEGeIYRFLTKPWDDEELKETIRQA 116
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
49-201 8.28e-14

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: 69.22  E-value: 8.28e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  49 PDLSILVVDDAKFSSAMIGRALSQAGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESInhyt 128
Cdd:COG3707   2 RGLRVLVVDDEPLRRADLREGLREAGYEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERPAP---- 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599592 129 yIVLLTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYAADRLCNTLQRLLVENRLLTEniaRMEERNLVD 201
Cdd:COG3707  78 -VILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARFRELRALRRELAKLRE---ALEERKLIE 146
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
53-119 4.08e-13

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: 65.23  E-value: 4.08e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQDIRfASSASEALQQLEQRP-VSVLLADWLMPEMDGLELTARVRQ 119
Cdd:cd17544   3 VLVVDDSATSRNHLRALLRRHNFQVLE-AANGQEALEVLEQHPdIKLVITDYNMPEMDGFELVREIRK 69
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
53-181 5.16e-13

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: 64.82  E-value: 5.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINhytyIVL 132
Cdd:COG5803   5 ILIVDDQAGIRMLLKEVLKKEGYE-VFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPDIP----VIM 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15599592 133 LTGKEGENVLGEAFDRGVDDFVSKaamneqlvPriYAADRLCNTLQRLL 181
Cdd:COG5803  80 MTAYGELDMVEEAKELGAKGYFTK--------P--FDIDELREAVNKLL 118
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
53-172 1.18e-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: 63.98  E-value: 1.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQldesiNHYTYIVL 132
Cdd:cd17614   1 ILVVDDEKPISDILKFNLTKEGY-EVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRK-----TSNVPIIM 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15599592 133 LTGKEGE--NVLGeaFDRGVDDFVSKAAMNEQLVPRIYAADR 172
Cdd:cd17614  75 LTAKDSEvdKVLG--LELGADDYVTKPFSNRELLARVKANLR 114
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
53-135 1.86e-12

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 63.25  E-value: 1.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDEsiNHYTYIVL 132
Cdd:cd17580   1 ILVVDDNEDAAEMLALLLELEGAE-VTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPW--LANTPAIA 77

                ...
gi 15599592 133 LTG 135
Cdd:cd17580  78 LTG 80
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
53-156 3.33e-12

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: 62.13  E-value: 3.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQlDESINHYTyIVL 132
Cdd:cd17538   2 ILVVDDEPANRELLEALLSAEGYE-VLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKE-DPETRHIP-VIM 78
                        90       100
                ....*....|....*....|....
gi 15599592 133 LTGKEGENVLGEAFDRGVDDFVSK 156
Cdd:cd17538  79 ITALDDREDRIRGLEAGADDFLSK 102
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
47-158 7.36e-12

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: 63.40  E-value: 7.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  47 PNPDLSILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESinh 126
Cdd:COG4567   1 SAEDRSLLLVDDDEAFARVLARALERRGF-EVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPD--- 76
                        90       100       110
                ....*....|....*....|....*....|..
gi 15599592 127 yTYIVLLTGKEGENVLGEAFDRGVDDFVSKAA 158
Cdd:COG4567  77 -ARIVVLTGYASIATAVEAIKLGADDYLAKPA 107
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
54-172 1.19e-11

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: 61.14  E-value: 1.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  54 LVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINhyTYIVLL 133
Cdd:cd19937   1 LVVDDEEDIVELLKYNLEKEGYE-VVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSS--IPIIML 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15599592 134 TGKegenvlGEAFDR------GVDDFVSKAAMNEQLVPRIYAADR 172
Cdd:cd19937  78 TAK------GEEFDKvlglelGADDYITKPFSPRELLARVKAVLR 116
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
52-134 1.46e-11

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: 60.78  E-value: 1.46e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  52 SILVVDDAKFSSAMIGRALSQAGYQDIRfASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESinHYTYIV 131
Cdd:cd17562   2 KILAVDDSASIRQMVSFTLRGAGYEVVE-AADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAY--KFTPIL 78

                ...
gi 15599592 132 LLT 134
Cdd:cd17562  79 MLT 81
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
53-135 2.07e-11

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: 60.43  E-value: 2.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKfssaMIGRALSQA------GYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLdesiNH 126
Cdd:cd17536   1 VLIVDDEP----LIREGLKKLidweelGFEVVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIREL----YP 72

                ....*....
gi 15599592 127 YTYIVLLTG 135
Cdd:cd17536  73 DIKIIILSG 81
PRK15347 PRK15347
two component system sensor kinase;
51-220 2.22e-11

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 65.43  E-value: 2.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   51 LSILVVDDAKFSSAMIGRALSQAGyQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINHYTYI 130
Cdd:PRK15347 691 LQILLVDDVETNRDIIGMMLVELG-QQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNLDPDCMI 769
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  131 VLLTGkegeNVLGEAFDR----GVDDFVSKAAMNEQLVPRI-YAADrlcntLQrllvenrlLTENIARMEERNLVDTLTG 205
Cdd:PRK15347 770 VALTA----NAAPEEIHRckkaGMNHYLTKPVTLAQLARALeLAAE-----YQ--------LLRGIELSPQDSSCSPLLD 832
                        170
                 ....*....|....*
gi 15599592  206 LGNPRyLRQKLADSL 220
Cdd:PRK15347 833 TDDMA-LNSKLYQSL 846
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
53-191 2.34e-11

phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and similar proteins; C4-dicarboxylic acid transport protein D (DctD) is part of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA. It is an activator of sigma(54)-RNA polymerase holoenzyme that uses the energy released from ATP hydrolysis to stimulate the isomerization of a closed promoter complex to an open complex capable of initiating transcription. DctD is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 60.58  E-value: 2.34e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQDIRFASsASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINhytyIVL 132
Cdd:cd17549   1 VLLVDDDADVREALQQTLELAGFRVRAFAD-AEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLP----VIL 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599592 133 LTGKegenvlG------EAFDRGVDDFVSKAAMNEQLVPriyAADRLCNtLQRLLVENRLLTENI 191
Cdd:cd17549  76 ITGH------GdvpmavEAMRAGAYDFLEKPFDPERLLD---VVRRALE-KRRLVLENRRLRQQL 130
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
98-356 2.36e-11

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 63.46  E-value: 2.36e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  98 VLLADWLMPEMDGLELTARVRQLDESINHYTYIVLLTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYAADRLCNTL 177
Cdd:COG2199  14 LLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592 178 QRLLVENRLLTENIARMEERNLVDTLTGLGNPRYLRQKLADSLRQVETRGGALCYLLVGMPEAPVLRQRHGEAFHRELLL 257
Cdd:COG2199  94 LLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLK 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592 258 GVARRLQQLVRPLDVLVRLDEQHFALITLVEDLHECSSSSfKRLHDGLNLKAFKTSEGFISLKA--GIAMLGLDSGalpl 335
Cdd:COG2199 174 EVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALA-ERLREALEQLPFELEGKELRVTVsiGVALYPEDGD---- 248
                       250       260
                ....*....|....*....|.
gi 15599592 336 GIDELLQRTEALLPDAYASGR 356
Cdd:COG2199 249 SAEELLRRADLALYRAKRAGR 269
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
196-356 3.87e-11

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 60.72  E-value: 3.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592    196 ERNLVDTLTGLGNPRYLRQKLADSLRQVETRGGALCYLLVGMPEAPVLRQRHGEAFHRELLLGVARRLQQLVRPLDVLVR 275
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592    276 LDEQHFALITLVEDLHECSSSSfKRLHDGLNLKAF-KTSEGFISLKAGIAMLGLDsgalPLGIDELLQRTEALLPDAYAS 354
Cdd:smart00267  81 LGGDEFALLLPETSLEEAIALA-ERILQQLREPIIiHGIPLYLTISIGVAAYPNP----GEDAEDLLKRADTALYQAKKA 155

                   ..
gi 15599592    355 GR 356
Cdd:smart00267 156 GR 157
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
53-156 5.17e-11

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: 59.33  E-value: 5.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGyqDIR---FASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDEsinhyTY 129
Cdd:cd17541   3 VLIVDDSAVMRKLLSRILESDP--DIEvvgTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERP-----TP 75
                        90       100       110
                ....*....|....*....|....*....|
gi 15599592 130 IVL---LTGKEGENVLgEAFDRGVDDFVSK 156
Cdd:cd17541  76 VVMvssLTEEGAEITL-EALELGAVDFIAK 104
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
52-179 9.06e-11

phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The GGDEF response regulator WspR is part of the Wsp system that is homologous to chemotaxis systems and also includes the membrane-bound receptor protein WspA. In response to growth on surfaces, WspR is phosphorylated by the Wsp signal transduction complex and is activated, functioning as a diguanylate cyclase (DGC) that catalyzes c-di-GMP synthesis. WspR is a hybrid response regulator-diguanylate cyclase, containing an N-terminal REC domain and a C-terminal GGDEF domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 58.96  E-value: 9.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  52 SILVVDDAKFSSAMIGRALSQAGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINhyTYIV 131
Cdd:cd17575   2 MVLLVDDQAIIGEAVRRALADEEDIDFHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRD--IPII 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15599592 132 LLTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRI-YAADRLCNTLQR 179
Cdd:cd17575  80 VLSTKEEPEVKSEAFALGANDYLVKLPDKIELVARIrYHSRSYINLLQR 128
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
51-165 1.32e-10

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: 58.32  E-value: 1.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  51 LSILVVDDAKFSSAMIGRALSQAGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDesinHYTYI 130
Cdd:cd17593   1 MKVLICDDSSMARKQLARALPADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQ----LETKV 76
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15599592 131 VLLTGkegeNVLGEAFDR----GVDDFVSKAAMNEQLVP 165
Cdd:cd17593  77 IVVSG----DVQPEAKERvlelGALAFLKKPFDPEKLAQ 111
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
53-156 1.56e-10

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: 57.52  E-value: 1.56e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQlDESINHYTYIVL 132
Cdd:cd19920   1 ILIVDDVPDNLRLLSELLRAAGY-RVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKA-DPATRHIPVIFL 78
                        90       100
                ....*....|....*....|....*.
gi 15599592 133 --LTGKEGENvlgEAFDRGVDDFVSK 156
Cdd:cd19920  79 taLTDTEDKV---KGFELGAVDYITK 101
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
53-167 1.63e-10

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: 58.11  E-value: 1.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRqLDESINHYTYIVL 132
Cdd:cd17598   1 ILIVEDSPTQAEQLKHILEEQGYK-VQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIK-SDPDLKDIPVILL 78
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15599592 133 LTGKEGENVLgEAFDRGVDDFVSKAAMNEQLVPRI 167
Cdd:cd17598  79 TTLSDPRDVI-RGLECGADNFITKPYDEKYLLSRI 112
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
53-156 1.90e-10

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: 57.17  E-value: 1.90e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDEsinhyTYIVL 132
Cdd:cd17620   1 ILVIEDEPQIRRFLRTALEAHGYR-VFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWSA-----VPVIV 74
                        90       100
                ....*....|....*....|....
gi 15599592 133 LTGKEGENVLGEAFDRGVDDFVSK 156
Cdd:cd17620  75 LSARDEESDKIAALDAGADDYLTK 98
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
53-156 3.58e-10

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: 56.62  E-value: 3.58e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQ---------RPVSVLLADWLMPEMDGLELTARVRQLDES 123
Cdd:cd19924   1 ILVVDDSPTARKQLRDLLKNLGF-EIAEAVDGEEALNKLENlakegndlsKELDLIITDIEMPKMDGYELTFELRDDPRL 79
                        90       100       110
                ....*....|....*....|....*....|...
gi 15599592 124 INhyTYIVLLTGKEGENVLGEAFDRGVDDFVSK 156
Cdd:cd19924  80 AN--IPVILNSSLSGEFSRARGKKVGADAYLAK 110
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
53-169 3.73e-10

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: 56.91  E-value: 3.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESinhyTYIVL 132
Cdd:cd19934   1 LLLVEDDALLAAQLKEQLSDAGYV-VDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRA----TPVLI 75
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15599592 133 LTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYA 169
Cdd:cd19934  76 LTARDSWQDKVEGLDAGADDYLTKPFHIEELLARLRA 112
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
201-356 4.51e-10

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 57.57  E-value: 4.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592 201 DTLTGLGNPRYLRQKLADSLRQVETRGGALCYLLVGMPEapvLRQ---RHGEAFHRELLLGVARRLQQLVRPLDVLVRL- 276
Cdd:cd01949   3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDH---FKQindTYGHAAGDEVLKEVAERLRSSLRESDLVARLg 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592 277 -DEqhFALITLVEDLHECSSSSfKRLHDGLNLKAFKTSEGF-ISLKAGIAMLGLDSGAlplgIDELLQRTEALLPDAYAS 354
Cdd:cd01949  80 gDE--FAILLPGTDLEEAEALA-ERLREAIEEPFFIDGQEIrVTASIGIATYPEDGED----AEELLRRADEALYRAKRS 152

                ..
gi 15599592 355 GR 356
Cdd:cd01949 153 GR 154
PRK10610 PRK10610
chemotaxis protein CheY;
46-168 4.92e-10

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 56.91  E-value: 4.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   46 MPNPDLSILVVDDAKFSSAMIGRALSQAGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQlDESIN 125
Cdd:PRK10610   1 MADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRA-DGAMS 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 15599592  126 HYTYIVLLTGKEGENVLGEAfDRGVDDFVSK---AAMNEQLVPRIY 168
Cdd:PRK10610  80 ALPVLMVTAEAKKENIIAAA-QAGASGYVVKpftAATLEEKLNKIF 124
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
52-119 5.06e-10

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: 56.51  E-value: 5.06e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599592  52 SILVVDDAKFSSAMIGRALSQAGYQDIRFASsASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQ 119
Cdd:cd19919   2 TVWIVDDDSSIRWVLERALAGAGLTVTSFEN-AQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQ 68
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
53-172 1.15e-09

phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 55.44  E-value: 1.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQldesINHYTYIVL 132
Cdd:cd17615   2 VLVVDDEPNITELLSMALRYEGW-DVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRA----DGPDVPVLF 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15599592 133 LTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYAADR 172
Cdd:cd17615  77 LTAKDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALLR 116
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
53-169 1.32e-09

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: 55.47  E-value: 1.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINhytyIVL 132
Cdd:cd17627   1 ILVVDDDRAVRESLRRSLRFEGY-EVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLP----ILV 75
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15599592 133 LTGKE--GENVLGeaFDRGVDDFVSKAAMNEQLVPRIYA 169
Cdd:cd17627  76 LTARDsvSDRVAG--LDAGADDYLVKPFALEELLARVRA 112
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
53-156 2.60e-09

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


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 53.98  E-value: 2.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQ-DIrfASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQldesINHYTYIV 131
Cdd:cd19935   1 ILVVEDEKKLAEYLKKGLTEEGYAvDV--AYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRA----AGKQTPVL 74
                        90       100
                ....*....|....*....|....*..
gi 15599592 132 LLTGKEG--ENVLGeaFDRGVDDFVSK 156
Cdd:cd19935  75 MLTARDSveDRVKG--LDLGADDYLVK 99
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
53-169 2.80e-09

phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is part of MtrA/MtrB (or MtrAB), a highly conserved two-component system (TCS) implicated in the regulation of cell division in the actinobacteria. In unicellular Mycobacterium tuberculosis, MtrAB coordinates DNA replication with cell division and regulates the transcription of resuscitation-promoting factor B. In filamentous Streptomyces venezuelae, it links antibiotic production to sporulation. MtrA belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 54.40  E-value: 2.80e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQL-EQRPVSVLLaDWLMPEMDGLELTARVRqlDESinhYTYIV 131
Cdd:cd17626   3 ILVVDDDAALAEMIGIVLRGEGF-DPAFCGDGTQALAAFrEVRPDLVLL-DLMLPGIDGIEVCRQIR--AES---GVPIV 75
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15599592 132 LLTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYA 169
Cdd:cd17626  76 MLTAKSDTVDVVLGLESGADDYVAKPFKPKELVARIRA 113
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
52-135 3.17e-09

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: 54.15  E-value: 3.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  52 SILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLE-QRPVSVLLaDWLMPEMDGLELTARVRQLDESINhytyI 130
Cdd:cd17554   2 KILVVDDEENIRELYKEELEDEGY-EVVTAGNGEEALEKLEsEDPDLVIL-DIKMPGMDGLETLRKIREKKPDLP----V 75

                ....*
gi 15599592 131 VLLTG 135
Cdd:cd17554  76 IICTA 80
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
53-135 3.37e-09

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: 53.66  E-value: 3.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQ-RPVSVLLADWLMPEMDGLELTARVRQLDESINhytyIV 131
Cdd:cd18160   2 ILLADDEPSVRKFIVTTLKKAGYA-VTEAESGAEALEKLQQgKDIDIVVTDIVMPEMDGIELAREARKIDPDVK----IL 76

                ....
gi 15599592 132 LLTG 135
Cdd:cd18160  77 FISG 80
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
53-135 6.30e-09

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: 53.27  E-value: 6.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQldesINHYTYIVL 132
Cdd:cd17550   1 ILIVDDEEDIRESLSGILEDEGYE-VDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKE----KYPDLPVIM 75

                ...
gi 15599592 133 LTG 135
Cdd:cd17550  76 ISG 78
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
51-181 1.03e-08

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 55.21  E-value: 1.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  51 LSILVVDDAKFSSAMIGRALSQ-AGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESinhyTY 129
Cdd:COG3279   2 MKILIVDDEPLARERLERLLEKyPDLEVVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPP----PP 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15599592 130 IVLLTGKEgENVLgEAFDRGVDDFVSKaamneqlvPriYAADRLCNTLQRLL 181
Cdd:COG3279  78 IIFTTAYD-EYAL-EAFEVNAVDYLLK--------P--IDEERLAKALEKAK 117
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
53-189 1.28e-08

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: 52.59  E-value: 1.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQldesiNHY-TYIV 131
Cdd:cd17572   1 VLLVEDSPSLAALYQEYLSDEGY-KVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQE-----RSLpTSVI 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15599592 132 LLTGKEGENVLGEAFDRGVDDFVSKAAMneqlvpriyaADRLCNTLQRLLvENRLLTE 189
Cdd:cd17572  75 VITAHGSVDIAVEAMRLGAYDFLEKPFD----------ADRLRVTVRNAL-KHRKLTK 121
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
53-172 1.33e-08

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 54.72  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   53 ILVVDDAKFSSAMIGRALSQAGYQDIRfASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQldESINHYTYIVL 132
Cdd:PRK10161   5 ILVVEDEAPIREMVCFVLEQNGFQPVE-AEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKR--ESMTRDIPVVM 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 15599592  133 LTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYAADR 172
Cdd:PRK10161  82 LTARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMR 121
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
52-135 1.40e-08

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: 52.06  E-value: 1.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  52 SILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESinhyTYIV 131
Cdd:cd17563   2 SLLLVDDDEVFAERLARALERRGFE-VETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPD----ARIV 76

                ....
gi 15599592 132 LLTG 135
Cdd:cd17563  77 VLTG 80
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
53-175 1.59e-08

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 54.42  E-value: 1.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   53 ILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQRpVSVLLADWLMPEMDGLELTARVRQldesiNHYTYIVL 132
Cdd:PRK10955   4 ILLVDDDRELTSLLKELLEMEGF-NVIVAHDGEQALDLLDDS-IDLLLLDVMMPKKNGIDTLKELRQ-----THQTPVIM 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 15599592  133 LT--GKEGENVLGeaFDRGVDDFVSKAAMNEQLVPRIYAADRLCN 175
Cdd:PRK10955  77 LTarGSELDRVLG--LELGADDYLPKPFNDRELVARIRAILRRSH 119
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
53-169 2.36e-08

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: 51.72  E-value: 2.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINhytyIVL 132
Cdd:cd17624   1 ILLVEDDALLGDGLKTGLRKAGYA-VDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLP----VLI 75
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15599592 133 LTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYA 169
Cdd:cd17624  76 LTARDGVDDRVAGLDAGADDYLVKPFALEELLARLRA 112
pleD PRK09581
response regulator PleD; Reviewed
52-356 2.44e-08

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 55.29  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   52 SILVVDDAKFSSAMIGRALSQAGYQDIrfASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESinHYTYIV 131
Cdd:PRK09581 157 RILLVDDDVSQAERIANILKEEFRVVV--VSDPSEALFNAAETNYDLVIVSANFENYDPLRLCSQLRSKERT--RYVPIL 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  132 LLTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIyaadrlcNTLQRLLVENRLLTENIARMEERNLVDTLTGLGNPRY 211
Cdd:PRK09581 233 LLVDEDDDPRLVKALELGVNDYLMRPIDKNELLARV-------RTQIRRKRYQDALRNNLEQSIEMAVTDGLTGLHNRRY 305
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  212 LRQKLADSLRQVETRGGALCYLLVGMPEAPVLRQRHGEAFHRELLLGVARRLQQLVRPLDVLVRLDEQHFaLITLVE-DL 290
Cdd:PRK09581 306 FDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEF-VVVMPDtDI 384
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599592  291 HECSSSSfKRLHDGLNLKAFKTSEG--FISLKAGIAMLGLDSGALPlgIDELLQRTEALLPDAYASGR 356
Cdd:PRK09581 385 EDAIAVA-ERIRRKIAEEPFIISDGkeRLNVTVSIGVAELRPSGDT--IEALIKRADKALYEAKNTGR 449
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
81-156 2.64e-08

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: 51.12  E-value: 2.64e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599592  81 ASSASEALQQLEQRPVSVLLADWLMPEMDGLELtarVRQLdESINHYTYIVLLTGKEGENVLGEAFDRGVDDFVSK 156
Cdd:cd17565  30 ADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQL---VRKL-KDTGSNGKFIMISQVSDKEMIGKAYQAGIEFFINK 101
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
54-169 2.72e-08

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: 51.45  E-value: 2.72e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  54 LVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQldESINhyTYIVLL 133
Cdd:cd17625   1 LVVEDEKDLSEAITKHLKKEGY-TVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLRE--EGIE--TPVLLL 75
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15599592 134 TGKEGEN--VLGeaFDRGVDDFVSKAAMNEQLVPRIYA 169
Cdd:cd17625  76 TALDAVEdrVKG--LDLGADDYLPKPFSLAELLARIRA 111
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
199-325 3.10e-08

Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 52.64  E-value: 3.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   199 LVDTLTGLGNPRYLRQKLADSLRQVETRGGALCYLLVGMPEAPVLRQRHGEAFHRELLLGVARRLQQLVRPLDVLVRLDE 278
Cdd:pfam00990   2 AHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGG 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15599592   279 QHFALItLVEDLHECSSSSFKRLHDGLNLKAF----KTSEGFISLKAGIAM 325
Cdd:pfam00990  82 DEFAIL-LPETSLEGAQELAERIRRLLAKLKIphtvSGLPLYVTISIGIAA 131
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
52-188 4.68e-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: 4.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  52 SILVVDDAKFSSAMIGRALSQAgyQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVR-QLDESINhytyi 130
Cdd:cd17596   2 TILVVDDEVRSLEALRRTLEED--FDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVReRWPEVVR----- 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15599592 131 VLLTG-KEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYAADRLcNTLQRllvENRLLT 188
Cdd:cd17596  75 IIISGyTDSEDIIAGINEAGIYQYLTKPWHPDQLLLTVRNAARL-FELQR---ENERLS 129
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
52-120 5.95e-08

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: 50.66  E-value: 5.95e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599592  52 SILVVDDAKFSSAMIGRALSQAGYQDIRfASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQL 120
Cdd:cd17555   2 TILVIDDDEVVRESIAAYLEDSGFQVLQ-AADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKE 69
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
53-172 6.58e-08

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: 50.38  E-value: 6.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQldesiNHYTYIVL 132
Cdd:cd17623   1 ILLIDDDRELTELLTEYLEMEGF-NVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRK-----TSQVPVLM 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15599592 133 LTGKegenvlGEAFDR------GVDDFVSKAAMNEQLVPRIYAADR 172
Cdd:cd17623  75 LTAR------GDDIDRilglelGADDYLPKPFNPRELVARIRAILR 114
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
52-166 7.36e-08

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 50.08  E-value: 7.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  52 SILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDEsinhyTYIV 131
Cdd:cd17619   2 HILIVEDEPVTRATLKSYFEQEGY-DVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSE-----VGII 75
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15599592 132 LLTGKEGE--NVLGeaFDRGVDDFVSKAAMNEQLVPR 166
Cdd:cd17619  76 LVTGRDDEvdRIVG--LEIGADDYVTKPFNPRELLVR 110
ompR PRK09468
osmolarity response regulator; Provisional
46-172 8.29e-08

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 52.67  E-value: 8.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   46 MPNPDLSILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLdesiN 125
Cdd:PRK09468   1 MMQENYKILVVDDDMRLRALLERYLTEQGFQ-VRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQ----N 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15599592  126 HYTYIVLLTGKegenvlGEAFDR------GVDDFVSKAAMNEQLVPRIYAADR 172
Cdd:PRK09468  76 NPTPIIMLTAK------GEEVDRivgleiGADDYLPKPFNPRELLARIRAVLR 122
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
24-156 1.17e-07

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 53.82  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   24 PPATNRALAGSVPAPILFSSPFMP------NPDLSILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVS 97
Cdd:PRK10841 769 PALLARIYRIELESDDSANALPSTdkavsdNDDMMILVVDDHPINRRLLADQLGSLGYQ-CKTANDGVDALNVLSKNHID 847
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599592   98 VLLADWLMPEMDGLELTARVRQLdesiNHYTYIVLLTGkegeNVLGEAFDR----GVDDFVSK 156
Cdd:PRK10841 848 IVLTDVNMPNMDGYRLTQRLRQL----GLTLPVIGVTA----NALAEEKQRcleaGMDSCLSK 902
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
53-156 1.95e-07

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: 49.08  E-value: 1.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQDIRfASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQlDESINHyTYIVL 132
Cdd:cd17548   2 ILIVEDNPLNMKLARDLLESAGYEVLE-AADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKE-DPATRD-IPVIA 78
                        90       100
                ....*....|....*....|....*....
gi 15599592 133 LT-----GKEgENVLgEAfdrGVDDFVSK 156
Cdd:cd17548  79 LTayamkGDR-EKIL-EA---GCDGYISK 102
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
52-156 2.41e-07

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: 48.95  E-value: 2.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  52 SILVVDDAKFSSAMIGRALSQAGYQ-DIRFASSASEALQQLEQ--------RPVSVLLaDWLMPEMDGLELTARVRQlDE 122
Cdd:cd17557   1 TILLVEDNPGDAELIQEAFKEAGVPnELHVVRDGEEALDFLRGegeyadapRPDLILL-DLNMPRMDGFEVLREIKA-DP 78
                        90       100       110
                ....*....|....*....|....*....|....
gi 15599592 123 SINHYTYIVLLTGKEGENVLgEAFDRGVDDFVSK 156
Cdd:cd17557  79 DLRRIPVVVLTTSDAEEDIE-RAYELGANSYIVK 111
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
53-118 2.62e-07

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


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 48.78  E-value: 2.62e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQDIRFaSSASEALQQLEQRP--VSVLLADWLMPEMDGLELTARVR 118
Cdd:cd17584   1 VLVVDDDPTCLAILKRMLLRCGYQVTTC-TDAEEALSMLRENKdeFDLVITDVHMPDMDGFEFLELIR 67
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
53-121 3.59e-07

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: 48.73  E-value: 3.59e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599592  53 ILVVDDAKFSSAMIGRALSQA-GYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARV---RQLD 121
Cdd:COG2197   4 VLIVDDHPLVREGLRALLEAEpDIEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRLltpRERE 76
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
53-167 4.41e-07

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: 47.81  E-value: 4.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQ-DIrfASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESInhytYIV 131
Cdd:cd17573   1 ILLIEDDSTLGKEISKGLNEKGYQaDV--AESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSI----VVI 74
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15599592 132 LLTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRI 167
Cdd:cd17573  75 VLSDNPKTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
53-156 4.65e-07

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 47.44  E-value: 4.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQDIRFASSASeALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDEsinhyTYIVL 132
Cdd:cd19936   1 IALVDDDRNILTSVSMALEAEGFSVETYTDGAS-ALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKST-----LPVIF 74
                        90       100
                ....*....|....*....|....*.
gi 15599592 133 LTGKEGE--NVLGeaFDRGVDDFVSK 156
Cdd:cd19936  75 LTSKDDEidEVFG--LRMGADDYITK 98
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
53-156 5.41e-07

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: 47.93  E-value: 5.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINhyTYIVL 132
Cdd:cd17552   4 ILVIDDEEDIREVVQACLEKLAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQS--IPVIL 81
                        90       100
                ....*....|....*....|....
gi 15599592 133 LTGKEGENVLGEAFDRGVDDFVSK 156
Cdd:cd17552  82 LTAKAQPSDRQRFASLGVAGVIAK 105
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
53-149 6.36e-07

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: 47.55  E-value: 6.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQDIRfASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINhytyIVL 132
Cdd:cd17553   3 ILIVDDQYGIRILLNEVFNKEGYQTFQ-AANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIR----VII 77
                        90
                ....*....|....*..
gi 15599592 133 LTGKEGENVLGEAFDRG 149
Cdd:cd17553  78 MTAYGELDMIQESKELG 94
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
53-156 1.18e-06

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 50.23  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   53 ILVVDDAKFSSAMIGRALSQAGYQDIRfASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESinhyTYIVL 132
Cdd:PRK11361   7 ILIVDDEDNVRRMLSTAFALQGFETHC-ANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETR----TPVIL 81
                         90       100
                 ....*....|....*....|....
gi 15599592  133 LTGKEGENVLGEAFDRGVDDFVSK 156
Cdd:PRK11361  82 MTAYAEVETAVEALRCGAFDYVIK 105
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
53-185 1.72e-06

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: 46.38  E-value: 1.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQ-AGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESInhytYIV 131
Cdd:cd17532   1 ALIVDDEPLAREELRYLLEEhPDIEIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPP----LIV 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15599592 132 LLTGKEGENVlgEAFDRGVDDFVSKaamneqlvPriYAADRLCNTLQRLLVENR 185
Cdd:cd17532  77 FVTAYDEYAV--EAFELNAVDYLLK--------P--FSEERLAEALAKLRKRLS 118
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
53-156 2.53e-06

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: 45.45  E-value: 2.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINhyTYIVL 132
Cdd:cd19927   1 ILLVDDDPGIRLAVKDYLEDQGFT-VIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDT--IPVIF 77
                        90       100
                ....*....|....*....|....*.
gi 15599592 133 LT--GKEGENVLGeaFDRGVDDFVSK 156
Cdd:cd19927  78 LTakGMTSDRIKG--YNAGCDGYLSK 101
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
51-123 3.66e-06

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: 45.51  E-value: 3.66e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599592  51 LSILVVDDAKFSSAMIGRALSQAGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELtarVRQLDES 123
Cdd:cd17530   1 LRVLVLDDDPFQCMMAATILEDLGPGNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEF---LRHLAES 70
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
51-124 4.69e-06

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 48.58  E-value: 4.69e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599592    51 LSILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESI 124
Cdd:PRK09959  959 LSILIADDHPTNRLLLKRQLNLLGY-DVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSL 1031
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
51-106 6.02e-06

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 42.94  E-value: 6.02e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 15599592     51 LSILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMP 106
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYE-VDEATDGEEALELLKEEKPDLILLDIMMP 55
pleD PRK09581
response regulator PleD; Reviewed
53-173 6.35e-06

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 47.97  E-value: 6.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   53 ILVVDD---------AKFSsamigralsqAGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRqlDES 123
Cdd:PRK09581   5 ILVVDDipanvklleAKLL----------AEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLK--SDP 72
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15599592  124 INHYTYIVLLTGkegenvLGEAFDR------GVDDFVSKAAMNEQLVPRIYAADRL 173
Cdd:PRK09581  73 ATTHIPVVMVTA------LDDPEDRvrgleaGADDFLTKPINDVALFARVKSLTRL 122
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
51-163 7.39e-06

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: 44.70  E-value: 7.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  51 LSILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVS--VLLADWLMPEMDGLELTARVRQLDESiNHYT 128
Cdd:cd19933   1 LKVLLVDDNAVNRMVTKGLLEKLGCE-VTTVSSGEECLNLLASAEHSfqLVLLDLCMPEMDGFEVALRIRKLFGR-RERP 78
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15599592 129 YIVLLTGKEGENVLGEAFDRGVDDFVSK----AAMNEQL 163
Cdd:cd19933  79 LIVALTANTDDSTREKCLSLGMNGVITKpvslHALGDEL 117
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
201-356 9.87e-06

diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 45.41  E-value: 9.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   201 DTLTGLGNPRYLRQKLaDSLRQVETRGG-ALCYLLVGMPEAPVLRQRHGEAFHRELLLGVARRLQQLVRPLDVLVRLDEQ 279
Cdd:TIGR00254   5 DPLTGLYNRRYLEEML-DSELKRARRFQrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGE 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599592   280 HFALITLVEDLHECSSSSfKRLHDGLNLKAFKTSEG-FISLKAGIAMLGLDSGALPLGidELLQRTEALLPDAYASGR 356
Cdd:TIGR00254  84 EFVVILPGTPLEDALSKA-ERLRDAINSKPIEVAGSeTLTVTVSIGVACYPGHGLTLE--ELLKRADEALYQAKKAGR 158
orf27 CHL00148
Ycf27; Reviewed
46-167 1.01e-05

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 46.25  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   46 MPNPDLSILVVDDAKFSSAMIGRALSQAGYQDIRfASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQldESin 125
Cdd:CHL00148   2 MENSKEKILVVDDEAYIRKILETRLSIIGYEVIT-ASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRK--ES-- 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15599592  126 hYTYIVLLTGkegenvLGEAFDR------GVDDFVSKAAMNEQLVPRI 167
Cdd:CHL00148  77 -DVPIIMLTA------LGDVSDRitglelGADDYVVKPFSPKELEARI 117
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
51-170 1.05e-05

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: 44.33  E-value: 1.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  51 LSILVVDDAKFSSAMIGRALSQAGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQldesiNHYTYI 130
Cdd:cd19932   1 VRVLIAEDEALIRMDLREMLEEAGYEVVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITS-----ENIAPI 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15599592 131 VLLTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYAA 170
Cdd:cd19932  76 VLLTAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMA 115
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
52-119 1.64e-05

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: 43.55  E-value: 1.64e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599592  52 SILVVDDAKFSSAMIGRALSQAGYQDIRFASSASEALQQLEQRPVSVLLADWLMP-EMDGLELTARVRQ 119
Cdd:cd17534   2 KILIVEDEAIIALDLKEILESLGYEVVGIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIRE 70
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
46-185 1.84e-05

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 46.18  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   46 MPNPDLSILVVDDaKFSSAMIGRALSQA-GYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESI 124
Cdd:PRK10365   1 MTHDNIDILVVDD-DISHCTILQALLRGwGYN-VALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAI 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599592  125 NhytyIVLLTGKEGENVLGEAFDRGVDDFVSKaamneqlvPRIYaaDRLCNTLQRLLVENR 185
Cdd:PRK10365  79 P----VLIMTAYSSVETAVEALKTGALDYLIK--------PLDF--DNLQATLEKALAHTH 125
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
52-274 2.19e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 45.64  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   52 SILVVDDakfsSAMIGRALSQA-----GYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLdesinH 126
Cdd:PRK12555   2 RIGIVND----SPLAVEALRRAlardpDHEVVWVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAE-----R 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  127 YTYIVL---LTGKEGENVLgEAFDRGVDDFVSKAAMNEQLVPRIYAadrlcntlQRLLVENRllteNIARMEERNLVDTL 203
Cdd:PRK12555  73 PCPILIvtsLTERNASRVF-EAMGAGALDAVDTPTLGIGAGLEEYA--------AELLAKID----QIGRLLGRRLAPAA 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599592  204 TGLGNPRyLRQKLADSLRQVETRGG---ALCYLLVGMPE----APVLRQRHGEAFHRelllGVARRLQQLVrPLDVLV 274
Cdd:PRK12555 140 APAAASA-APFRTTPRLVAIGASAGgpaALAVLLGGLPAdfpaAIVIVQHVDAAFAA----GMAEWLDGQT-ALPVRE 211
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
53-138 3.50e-05

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: 42.36  E-value: 3.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQDIRFaSSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLdeSINHYTYIVL 132
Cdd:cd17602   1 VACVDDRPSIQKMIEYFLEKQGFRVVVI-DDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKS--SALKDTPIIM 77

                ....*.
gi 15599592 133 LTGKEG 138
Cdd:cd17602  78 LTGKDG 83
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
52-172 6.28e-05

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: 41.98  E-value: 6.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  52 SILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQldesinHYTY-I 130
Cdd:cd19939   1 RILIVEDELELARLTRDYLIKAGL-EVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVRE------HSHVpI 73
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15599592 131 VLLTGK--EGENVLGeaFDRGVDDFVSKAAMNEQLVPRIYAADR 172
Cdd:cd19939  74 LMLTARteEMDRVLG--LEMGADDYLCKPFSPRELLARVRALLR 115
PRK10816 PRK10816
two-component system response regulator PhoP;
53-172 6.40e-05

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 43.57  E-value: 6.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   53 ILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINhytyIVL 132
Cdd:PRK10816   3 VLVVEDNALLRHHLKVQLQDAGHQ-VDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLP----ILV 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 15599592  133 LTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYAADR 172
Cdd:PRK10816  78 LTARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALMR 117
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
53-119 6.71e-05

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


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 41.34  E-value: 6.71e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQ 119
Cdd:cd19928   1 ILVADDDRAIRTVLTQALGRAGYE-VRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKK 66
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
81-167 6.93e-05

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: 41.87  E-value: 6.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  81 ASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRqlDESINHYTYIVLLTGKEGenVLGEAFDRGVDDFVSKAAMN 160
Cdd:cd19930  30 ASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELR--EELPDTKVLIVTTFGRPG--YFRRALAAGVDGYVLKDRPI 105

                ....*..
gi 15599592 161 EQLVPRI 167
Cdd:cd19930 106 EELADAI 112
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
53-204 7.99e-05

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


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 43.17  E-value: 7.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQDIRFASsASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINhytyIVL 132
Cdd:COG4566   2 VYIVDDDEAVRDSLAFLLESAGLRVETFAS-AEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLP----VIF 76
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599592 133 LTGKegenvlG------EAFDRGVDDFVSKAAMNEQLVPRIYAAdrlcntlqrLLVENRLLTENIARMEERNLVDTLT 204
Cdd:COG4566  77 LTGH------GdvpmavRAMKAGAVDFLEKPFDDQALLDAVRRA---------LARDRARRAERARRAELRARLASLT 139
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
25-156 8.30e-05

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 44.45  E-value: 8.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   25 PATNRALAGSVPAPILFSSPFMPNPD------LSILVVDDAKFSSAMIGrALSQAGYQDIRFASSASEALQQLEQRPVSV 98
Cdd:PRK11107 636 PLSHTRLLPALLEPCHHKQPPLLPPTdesrlpLTVMAVDDNPANLKLIG-ALLEEQVEHVVLCDSGHQAVEQAKQRPFDL 714
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599592   99 LLADWLMPEMDGLELTARVRQLdeSINHYTYIVLLTG----KEGENVLGEafdrGVDDFVSK 156
Cdd:PRK11107 715 ILMDIQMPGMDGIRACELIRQL--PHNQNTPIIAVTAhamaGERERLLSA----GMDDYLAK 770
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
51-156 1.05e-04

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: 41.05  E-value: 1.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  51 LSILVVDDAK-FSSAMIGRALSQAGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESinHYTY 129
Cdd:cd17561   2 IKVLIADDNReFVQLLEEYLNSQPDMEVVGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLE--KRPK 79
                        90       100
                ....*....|....*....|....*..
gi 15599592 130 IVLLTGKEGENVLGEAFDRGVDDFVSK 156
Cdd:cd17561  80 IIMLTAFGQEDITQRAVELGASYYILK 106
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
53-119 1.06e-04

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 44.09  E-value: 1.06e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599592   53 ILVVDDAKFSSAMIGRALSQAGYQDIRFASsASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQ 119
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAGLTCTTFEN-GNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQ 71
PRK10766 PRK10766
two-component system response regulator TorR;
52-156 1.09e-04

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 43.10  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   52 SILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDEsinhyTYIV 131
Cdd:PRK10766   4 HILVVEDEPVTRARLQGYFEQEGYT-VSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRST-----VGII 77
                         90       100       110
                 ....*....|....*....|....*....|.
gi 15599592  132 LLTGKEgenvlgEAFDR------GVDDFVSK 156
Cdd:PRK10766  78 LVTGRT------DSIDRivglemGADDYVTK 102
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
53-120 1.17e-04

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: 41.55  E-value: 1.17e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599592  53 ILVVDDAKFSSAMIGRALS---QAGYQDIRfASSASEALQQLEQ-----RPVSVLLADWLMPEMDGLELTARVRQL 120
Cdd:cd17595   3 ILTVDDDPQVLRAVARDLRrqyGKDYRVLR-ADSGAEALDALKElklrgEAVALFLVDQRMPEMDGVEFLEKAMEL 77
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
53-167 1.95e-04

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 40.32  E-value: 1.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQDIRFASSASEALQQLEQRPVSVLLADW-LMPEMDGleltarvRQLDESINHYTYI- 130
Cdd:cd17589   1 FLIVDDQPTFRSMLKSMLRSLGVTRIDTASSGEEALRMCENKTYDIVLCDYnLGKGKNG-------QQLLEELRHKKLIs 73
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15599592 131 -----VLLTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRI 167
Cdd:cd17589  74 pstvfIMVTGESSRAMVLSALELEPDDYLLKPFTVSELRERL 115
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
53-156 2.53e-04

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: 40.43  E-value: 2.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQL-----------EQRPVSVLLADWLMPEMDGLELTARVRQLd 121
Cdd:cd17581   1 VLAVDDSLVDRKVIERLLRISSCR-VTAVDSGKRALEFLgledeedssnfNEPKVNMIITDYCMPGMTGYDLLKKVKES- 78
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15599592 122 ESINHYTYIVLltgkEGENV---LGEAFDRGVDDFVSK 156
Cdd:cd17581  79 SALKEIPVVIM----SSENIptrISRCLEEGAEDFLLK 112
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
53-170 3.51e-04

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 39.88  E-value: 3.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINhytyIVL 132
Cdd:cd17537   3 VYVVDDDEAVRDSLAFLLRSVGL-AVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIP----IIF 77
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15599592 133 LTGkEGENVLG-EAFDRGVDDFVSKAAMNEQLVPRIYAA 170
Cdd:cd17537  78 ITG-HGDVPMAvEAMKAGAVDFLEKPFRDQVLLDAIEQA 115
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
53-169 3.98e-04

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: 39.67  E-value: 3.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDEsinhyTYIVL 132
Cdd:cd19938   2 ILIVEDEPKLAQLLIDYLRAAGYA-PTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFSD-----VPIIM 75
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15599592 133 LTGK--EGENVLGeaFDRGVDDFVSKAAMNEQLVPRIYA 169
Cdd:cd19938  76 VTARveEIDRLLG--LELGADDYICKPYSPREVVARVKA 112
fixJ PRK09390
response regulator FixJ; Provisional
55-170 4.82e-04

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 40.76  E-value: 4.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   55 VVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINhytyIVLLT 134
Cdd:PRK09390   8 VVDDDEAMRDSLAFLLDSAGF-EVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLP----VIVMT 82
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 15599592  135 GKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYAA 170
Cdd:PRK09390  83 GHGDVPLAVEAMKLGAVDFIEKPFEDERLIGAIERA 118
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
53-156 5.68e-04

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: 38.72  E-value: 5.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDEsinhyTYIVL 132
Cdd:cd17621   1 VLVVEDEESFSDPLAYLLRKEGFE-VTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARSN-----VPVIM 74
                        90       100
                ....*....|....*....|....*.
gi 15599592 133 LTGKEGE--NVLGeaFDRGVDDFVSK 156
Cdd:cd17621  75 VTAKDSEidKVVG--LELGADDYVTK 98
PRK15479 PRK15479
transcriptional regulator TctD;
53-172 6.23e-04

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 40.86  E-value: 6.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   53 ILVVDDAKFSSAMIGRALSQAGYQ-DIRFASSASEALQQLEQRPVSVLlaDWLMPEMDGLELTARVRQLDESINhytyIV 131
Cdd:PRK15479   3 LLLAEDNRELAHWLEKALVQNGFAvDCVFDGLAADHLLQSEMYALAVL--DINMPGMDGLEVLQRLRKRGQTLP----VL 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 15599592  132 LLTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYAADR 172
Cdd:PRK15479  77 LLTARSAVADRVKGLNVGADDYLPKPFELEELDARLRALLR 117
PRK10693 PRK10693
two-component system response regulator RssB;
81-124 6.61e-04

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 41.13  E-value: 6.61e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 15599592   81 ASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESI 124
Cdd:PRK10693   3 AANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQT 46
PRK15115 PRK15115
response regulator GlrR; Provisional
52-120 9.21e-04

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 40.98  E-value: 9.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599592   52 SILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQL 120
Cdd:PRK15115   7 HLLLVDDDPGLLKLLGMRLTSEGYS-VVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKV 74
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
86-156 9.23e-04

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 40.24  E-value: 9.23e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599592   86 EALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESINhytyIVLLTGKEGENVLGEAFDRGVDDFVSK 156
Cdd:PRK09935  40 ITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQSTVK----VLFLSSKSECFYAGRAIQAGANGFVSK 106
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
46-170 1.03e-03

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 40.01  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   46 MPNPD-LSILVVDDakfsSAMIGRALSQ-----AGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQ 119
Cdd:PRK10651   1 MSNQEpATILLIDD----HPMLRTGVKQlismaPDITVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLRE 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15599592  120 LDESinhyTYIVLLTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYAA 170
Cdd:PRK10651  77 KSLS----GRIVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQA 123
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
53-171 1.30e-03

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 40.52  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   53 ILVVDDAKFSSAMIGRAL-SQAGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELtarVRQLdesINHYTYIV 131
Cdd:PRK00742   6 VLVVDDSAFMRRLISEILnSDPDIEVVGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDA---LEKI---MRLRPTPV 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15599592  132 L----LTGKEGENVLgEAFDRGVDDFVSKAAMNEQLVPRIYAAD 171
Cdd:PRK00742  80 VmvssLTERGAEITL-RALELGAVDFVTKPFLGISLGMDEYKEE 122
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
53-169 1.78e-03

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: 37.77  E-value: 1.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRqldeSINHYTYIVL 132
Cdd:cd17616   1 VLLIEDDSATAQSIELMLKSEGF-NVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLR----LAKVKTPILI 75
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15599592 133 LTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRIYA 169
Cdd:cd17616  76 LSGLADIEDKVKGLGFGADDYMTKPFHKDELVARIHA 112
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
46-156 1.88e-03

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 40.31  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   46 MPNPDLSILVVDDAKFsSAMIGRALSQAGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQlDESIN 125
Cdd:PRK11091 521 MPLPALNILLVEDIEL-NVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRE-RYPRE 598
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15599592  126 HYTYIVLLTGkegeNVLG---EAFDRGVDDFVSK 156
Cdd:PRK11091 599 DLPPLVALTA----NVLKdkkEYLDAGMDDVLSK 628
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
53-156 2.48e-03

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: 37.26  E-value: 2.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSQAGYqDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESInhytyIVL 132
Cdd:cd18159   1 ILIVEDDETIASLLKKHLEKWGY-EVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISNVP-----IIF 74
                        90       100
                ....*....|....*....|....
gi 15599592 133 LTGKEGENVLGEAFDRGVDDFVSK 156
Cdd:cd18159  75 ISSRDDNMDQVMAINMGGDDYITK 98
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
46-156 4.46e-03

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 38.02  E-value: 4.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   46 MPNPdlSILVVDDAKFSSAMIGRALSQAGYQdIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESIN 125
Cdd:PRK11083   1 MQQP--TILLVEDEQAIADTLVYALQSEGFT-VEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALP 77
                         90       100       110
                 ....*....|....*....|....*....|...
gi 15599592  126 hytyIVLLTGKEGE--NVLGeaFDRGVDDFVSK 156
Cdd:PRK11083  78 ----VIFLTARSDEvdRLVG--LEIGADDYVAK 104
PRK11697 PRK11697
two-component system response regulator BtsR;
51-180 4.52e-03

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 38.29  E-value: 4.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   51 LSILVVDDAKFSSAMIGRALSQAGyqDIRF---ASSASEALQQL-EQRPvSVLLADWLMPEMDGLELtarVRQLDEsiNH 126
Cdd:PRK11697   2 IKVLIVDDEPLAREELRELLQEEG--DIEIvgeCSNAIEAIGAIhRLKP-DVVFLDIQMPRISGLEL---VGMLDP--EH 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15599592  127 YTYIVLLTgkegenvlgeAFdrgvDDFVSKA----AMNEQLVPriYAADRLCNTLQRL 180
Cdd:PRK11697  74 MPYIVFVT----------AF----DEYAIKAfeehAFDYLLKP--IDPARLAKTLARL 115
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
54-170 5.28e-03

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 37.95  E-value: 5.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592   54 LVVDDAKFSSAMIGRALSQAGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQldesiNHYTYIVLL 133
Cdd:PRK09958   4 IIIDDHPLAIAAIRNLLIKNDIEILAELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRK-----RQYSGIIII 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 15599592  134 TGKEGENVLGE-AFDRGVDDFVSKAAMNEQLVPRIYAA 170
Cdd:PRK09958  79 VSAKNDHFYGKhCADAGANGFVSKKEGMNNIIAAIEAA 116
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
53-167 6.78e-03

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: 36.14  E-value: 6.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599592  53 ILVVDDAKFSSAMIGRALSqaGYQDIRFASSASEALQQLEQRPVSVLLADWLMPEMDGLELTARVRQLDESinHYTYIVL 132
Cdd:cd17539   1 VLLVDDRPSSAERIAAMLS--SEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERT--RQLPILA 76
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15599592 133 LTGKEGENVLGEAFDRGVDDFVSKAAMNEQLVPRI 167
Cdd:cd17539  77 VADPGDRGRLIRALEIGVNDYLVRPIDPNELLARV 111
 
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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