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Conserved domains on  [gi|1054616225|ref|WP_066384107|]
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ATP-binding protein [Anabaena sp. CA = ATCC 33047]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TMAO_torS super family cl37193
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
505-913 6.41e-89

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


The actual alignment was detected with superfamily member TIGR02956:

Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 305.93  E-value: 6.41e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  505 QEMR-NNLMLAALEFSHAAlkfAAEQAEIANRAKSQFLAKMSHELRTPLNAILGFTQLMtRNRSLSPEDQENLDIISRSG 583
Cdd:TIGR02956  434 QELAeTNERLNAEVKNHAK---ARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELL-GDTGLTSQQQQYLQVINRSG 509
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  584 EHLLALINDVLEMSKIEAGQLTLNESYFDLHRLIYSIREMFALKAADKGLEITINLGQEVNQYVFGDEGKLRQILINLIG 663
Cdd:TIGR02956  510 ESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVG 589
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  664 NAIKFTVVGHITLRVSyLNssstttpvDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKgGRQFMQGTGLGLPISRQFAK 743
Cdd:TIGR02956  590 NAIKFTDRGSVVLRVS-LN--------DDSSLLFEVEDTGCGIAEEEQATLFDAFTQAD-GRRRSGGTGLGLAISQRLVE 659
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  744 LMGGDVTVRSFPGQGTTFSCQVQLTLVDKIDvlpvTQVTRRVIGLepgqSPHRILIVEDIQENRQLMVKLLESVGFEVCA 823
Cdd:TIGR02956  660 AMDGELGVESELGVGSCFWFTLPLTRGKPAE----DSATLTVIDL----PPQRVLLVEDNEVNQMVAQGFLTRLGHKVTL 731
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  824 AENGLEAInLCVEWKP-HLIWMDIQMPVMDGYEATKEIRAMSEGKD-IKIIALTANAFQEDKQAVLNAGCDDFVAKPFEE 901
Cdd:TIGR02956  732 AESGQSAL-ECFHQHAfDLALLDINLPDGDGVTLLQQLRAIYGAKNeVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVE 810
                          410
                   ....*....|..
gi 1054616225  902 TVLFNKMAQYLN 913
Cdd:TIGR02956  811 EQLTAMIAVILA 822
PHY pfam00360
Phytochrome region; Phytochromes are red/far-red photochromic biliprotein photoreceptors which ...
335-512 2.33e-56

Phytochrome region; Phytochromes are red/far-red photochromic biliprotein photoreceptors which regulate plant development. They are widely represented in both photosynthetic and non-photosynthetic bacteria and are known in a variety of fungi. Although sequence similarities are low, this domain is structurally related to pfam01590, which is generally located immediately N-terminal to this domain. Compared with pfam01590, this domain carries an additional tongue-like hairpin loop between the fifth beta-sheet and the sixth alpha-helix which functions to seal the chromophore pocket and stabilize the photoactivated far-red-absorbing state (Pfr). The tongue carries a conserved PRxSF motif, from which an arginine finger points into the chromophore pocket close to ring D forming a salt bridge with a conserved aspartate residue.


:

Pssm-ID: 425635  Cd Length: 178  Bit Score: 192.48  E-value: 2.33e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  335 VKLIQEELRASLANQLDYIGnVFKRNETNLLDIVQAQGAVILLEEQLTVLGNTPSEAAIYELVNWLMNRNSQEIFYTDSL 414
Cdd:pfam00360    1 LRRIQDRLVEAMARADDLVD-GLVDQSPNLLDLVKADGAALCFGGNLLTLGETPPEEAIRDLAQWLGRNHDSEVFSTDSL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  415 PKIYPKAKNFQNIACGILAISIVLNQRSYhIIWFRPEQIQIVNWAGNPNQTLSVDPkNNLRLTPRTSFELWKETVKEKSL 494
Cdd:pfam00360   80 SQAYPEAAALADVASGLLAIPISRKPGNY-LLWFRPEVVRTVNWGGDPHKAVEIDP-GGVRLSPRKSFDAWKETVRGRSL 157
                          170
                   ....*....|....*...
gi 1054616225  495 PWQHFDLEVAQEMRNNLM 512
Cdd:pfam00360  158 PWSEVEIEAARELREALL 175
PAS_2 super family cl20158
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
15-129 1.79e-26

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


The actual alignment was detected with superfamily member pfam08446:

Pssm-ID: 400652  Cd Length: 107  Bit Score: 104.64  E-value: 1.79e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225   15 CEQDPINIPGSIQPHGMLIVLQEPELNILQVSENTRDYLGIDAKFLLGKNLSFLIPTATIRIIKQYLTQKNLSLIPLIEI 94
Cdd:pfam08446    1 CYLEPIQRPGLIQPHGCLLAVDEPSLRVLQYSENAAEMLGLPAEDLLGTDLRDLFGASSASLLRKALAAGEISLLNPILI 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1054616225   95 TLKCSSKcqpknqsnSFLGMLHRSENVLILELEPQ 129
Cdd:pfam08446   81 HSRTSGK--------PFYAILHRSDGGLVLELEPA 107
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
156-327 2.80e-11

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


:

Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 62.40  E-value: 2.80e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225   156 NLSELYQNLATSVRKVTQFDRIMIYKFETDNSGVIVAEDKQNHLETYLGLHYPATDIprIARQLYYEKWLRLIPDVNYQP 235
Cdd:smart00065    1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELVLVAADGLTLPTLGIRFPLDEG--LAGRVAETGRPLNIPDVEADP 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225   236 VKLIPtnnpitdtpldlsgaflrsvsplhiEYLQHMGVAASMSISLINQNRLWGLIACHH-YTPKKLDYE----IRKICE 310
Cdd:smart00065   79 LFAED-------------------------LLGRYQGVRSFLAVPLVADGELVGVLALHNkKSPRPFTEEdeelLQALAN 133
                           170
                    ....*....|....*..
gi 1054616225   311 FIGkfASIELVKQQEKH 327
Cdd:smart00065  134 QLA--IALANAQLYEEL 148
 
Name Accession Description Interval E-value
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
505-913 6.41e-89

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 305.93  E-value: 6.41e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  505 QEMR-NNLMLAALEFSHAAlkfAAEQAEIANRAKSQFLAKMSHELRTPLNAILGFTQLMtRNRSLSPEDQENLDIISRSG 583
Cdd:TIGR02956  434 QELAeTNERLNAEVKNHAK---ARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELL-GDTGLTSQQQQYLQVINRSG 509
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  584 EHLLALINDVLEMSKIEAGQLTLNESYFDLHRLIYSIREMFALKAADKGLEITINLGQEVNQYVFGDEGKLRQILINLIG 663
Cdd:TIGR02956  510 ESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVG 589
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  664 NAIKFTVVGHITLRVSyLNssstttpvDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKgGRQFMQGTGLGLPISRQFAK 743
Cdd:TIGR02956  590 NAIKFTDRGSVVLRVS-LN--------DDSSLLFEVEDTGCGIAEEEQATLFDAFTQAD-GRRRSGGTGLGLAISQRLVE 659
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  744 LMGGDVTVRSFPGQGTTFSCQVQLTLVDKIDvlpvTQVTRRVIGLepgqSPHRILIVEDIQENRQLMVKLLESVGFEVCA 823
Cdd:TIGR02956  660 AMDGELGVESELGVGSCFWFTLPLTRGKPAE----DSATLTVIDL----PPQRVLLVEDNEVNQMVAQGFLTRLGHKVTL 731
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  824 AENGLEAInLCVEWKP-HLIWMDIQMPVMDGYEATKEIRAMSEGKD-IKIIALTANAFQEDKQAVLNAGCDDFVAKPFEE 901
Cdd:TIGR02956  732 AESGQSAL-ECFHQHAfDLALLDINLPDGDGVTLLQQLRAIYGAKNeVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVE 810
                          410
                   ....*....|..
gi 1054616225  902 TVLFNKMAQYLN 913
Cdd:TIGR02956  811 EQLTAMIAVILA 822
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
431-762 3.67e-80

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 264.08  E-value: 3.67e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  431 ILAISIVLNQRSYHIIWFRPEQIQIVNWAGNPNQTLSVDPKNNLRLTPRTSFELWKETVKEKSLPWQHFDLEVAQEMRNN 510
Cdd:COG0642      4 LLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  511 LMLAALEFSHAALKFAAEQAEIANRAKSQFLAKMSHELRTPLNAILGFTQLMtrNRSLSPEDQENLDIISRSGEHLLALI 590
Cdd:COG0642     84 LLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELL--LEELDEEQREYLETILRSADRLLRLI 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  591 NDVLEMSKIEAGQLTLNESYFDLHRLIYSIREMFALKAADKGLEITINLGQEVnQYVFGDEGKLRQILINLIGNAIKFTV 670
Cdd:COG0642    162 NDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDL-PTVRGDPDRLRQVLLNLLSNAIKYTP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  671 VG-HITLRVSylnssstttpVDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGRQFmQGTGLGLPISRQFAKLMGGDV 749
Cdd:COG0642    241 EGgTVTVSVR----------REGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSRRG-GGTGLGLAIVKRIVELHGGTI 309
                          330
                   ....*....|...
gi 1054616225  750 TVRSFPGQGTTFS 762
Cdd:COG0642    310 EVESEPGKGTTFT 322
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
528-994 9.89e-76

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 267.87  E-value: 9.89e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  528 EQAEI--------------ANRAKSQFLAKMSHELRTPLNAILGFTQLMTRNrSLSPEDQENLDIISRSGEHLLALINDV 593
Cdd:PRK11107   270 EQMEIqnveldlakkraqeAARIKSEFLANMSHELRTPLNGVIGFTRQTLKT-PLTPTQRDYLQTIERSANNLLAIINDI 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  594 LEMSKIEAGQLTLNESYFDLHRLIYSIREMFALKAADKGLEITINLGQEVNQYVFGDEGKLRQILINLIGNAIKFTVVGH 673
Cdd:PRK11107   349 LDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGN 428
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  674 ITLRVSyLNSSSTttpvDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKGG--RQFmQGTGLGLPISRQFAKLMGGDVTV 751
Cdd:PRK11107   429 IDILVE-LRALSN----TKVQLEVQIRDTGIGISERQQSQLFQAFRQADASisRRH-GGTGLGLVITQKLVNEMGGDISF 502
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  752 RSFPGQGTTFSCQVQLTL-----VDKIDV--------------------------------------------------- 775
Cdd:PRK11107   503 HSQPNRGSTFWFHLPLDLnpnpiIDGLPTdclagkrllyvepnsaaaqatldilsetplevtysptlsqlpeahydilll 582
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  776 -LPVTQV----------------TRRVIGLEPGQSPH------------------------------------------- 795
Cdd:PRK11107   583 gLPVTFRepltmlherlakaksmTDFLILALPCHEQVlaeqlkqdgadaclskplshtrllpallepchhkqppllpptd 662
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 ------RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDI 869
Cdd:PRK11107   663 esrlplTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHNQNT 742
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  870 KIIALTANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKMAQYL-NLHYVYADNSLLIPPETPKKLQKLtaadlqvmsaNW 948
Cdd:PRK11107   743 PIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKpGPKFTSRVVAPEPPEPVHFPNATL----------DW 812
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*...
gi 1054616225  949 IAQVHEAALLIDDAK--LYNLFNQIPASEQQLAEALKDLVDNFHLETI 994
Cdd:PRK11107   813 QLALRQAAGKPDLARdmLQMLLDFLPEVRNKVEEALAGEDPEGLLDLI 860
PHY pfam00360
Phytochrome region; Phytochromes are red/far-red photochromic biliprotein photoreceptors which ...
335-512 2.33e-56

Phytochrome region; Phytochromes are red/far-red photochromic biliprotein photoreceptors which regulate plant development. They are widely represented in both photosynthetic and non-photosynthetic bacteria and are known in a variety of fungi. Although sequence similarities are low, this domain is structurally related to pfam01590, which is generally located immediately N-terminal to this domain. Compared with pfam01590, this domain carries an additional tongue-like hairpin loop between the fifth beta-sheet and the sixth alpha-helix which functions to seal the chromophore pocket and stabilize the photoactivated far-red-absorbing state (Pfr). The tongue carries a conserved PRxSF motif, from which an arginine finger points into the chromophore pocket close to ring D forming a salt bridge with a conserved aspartate residue.


Pssm-ID: 425635  Cd Length: 178  Bit Score: 192.48  E-value: 2.33e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  335 VKLIQEELRASLANQLDYIGnVFKRNETNLLDIVQAQGAVILLEEQLTVLGNTPSEAAIYELVNWLMNRNSQEIFYTDSL 414
Cdd:pfam00360    1 LRRIQDRLVEAMARADDLVD-GLVDQSPNLLDLVKADGAALCFGGNLLTLGETPPEEAIRDLAQWLGRNHDSEVFSTDSL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  415 PKIYPKAKNFQNIACGILAISIVLNQRSYhIIWFRPEQIQIVNWAGNPNQTLSVDPkNNLRLTPRTSFELWKETVKEKSL 494
Cdd:pfam00360   80 SQAYPEAAALADVASGLLAIPISRKPGNY-LLWFRPEVVRTVNWGGDPHKAVEIDP-GGVRLSPRKSFDAWKETVRGRSL 157
                          170
                   ....*....|....*...
gi 1054616225  495 PWQHFDLEVAQEMRNNLM 512
Cdd:pfam00360  158 PWSEVEIEAARELREALL 175
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
654-767 5.60e-47

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 163.05  E-value: 5.60e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  654 LRQILINLIGNAIKFTVVGHITLRVSYLNSSStttpvDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKGG--RQFmQGT 731
Cdd:cd16922      1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEE-----DGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSttRKY-GGT 74
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1054616225  732 GLGLPISRQFAKLMGGDVTVRSFPGQGTTFSCQVQL 767
Cdd:cd16922     75 GLGLAISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
649-762 1.63e-35

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 130.46  E-value: 1.63e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225   649 GDEGKLRQILINLIGNAIKFTV-VGHITLRVSylnssstttpVDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGRQF 727
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPeGGRITVTLE----------RDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRK 70
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 1054616225   728 MQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:smart00387   71 IGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFT 105
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
649-768 6.63e-31

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 117.08  E-value: 6.63e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  649 GDEGKLRQILINLIGNAIKFTVV-GHITLRVSylnssstttpvDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGRQF 727
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAAKaGEITVTLS-----------EGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGG 69
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1054616225  728 mqGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFSCQVQLT 768
Cdd:pfam02518   70 --GTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
PAS_2 pfam08446
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
15-129 1.79e-26

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 400652  Cd Length: 107  Bit Score: 104.64  E-value: 1.79e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225   15 CEQDPINIPGSIQPHGMLIVLQEPELNILQVSENTRDYLGIDAKFLLGKNLSFLIPTATIRIIKQYLTQKNLSLIPLIEI 94
Cdd:pfam08446    1 CYLEPIQRPGLIQPHGCLLAVDEPSLRVLQYSENAAEMLGLPAEDLLGTDLRDLFGASSASLLRKALAAGEISLLNPILI 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1054616225   95 TLKCSSKcqpknqsnSFLGMLHRSENVLILELEPQ 129
Cdd:pfam08446   81 HSRTSGK--------PFYAILHRSDGGLVLELEPA 107
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
527-767 6.09e-25

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 109.53  E-value: 6.09e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  527 AEQAEIANRAKSQFLAKMSHELRTPLNAILGftQLMTRNRSLSPEDQENLDIISRSGEHLLALINDVLEMSKIEAGQLTL 606
Cdd:NF012163   230 ASTLEKNEQMRRDFMADISHELRTPLAVLRA--ELEAIQDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEGALAY 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  607 NESYFDLHRLIYSIREMFALKAADKGLEITINLgqEVNQYVFGDEGKLRQILINLIGNAIKFTVVGHiTLRVSylnssst 686
Cdd:NF012163   308 QKASVDLVPLLEVEGGAFRERFASAGLELEVSL--PDSSLVFGDRDRLMQLFNNLLENSLRYTDSGG-SLHIS------- 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  687 TTPVDQVIIVFeVEDTGPGIPPEDMDLIFEAFIQAKGGRQFMQ-GTGLGLPISRQFAKLMGGDVTVRSFPGQGttFSCQV 765
Cdd:NF012163   378 ASQRPKEVTLT-VADSAPGVSDEQLARLFERFYRVEVSRNRASgGSGLGLAISLNIVQAHGGTLHAAHSPLGG--LRIVV 454

                   ..
gi 1054616225  766 QL 767
Cdd:NF012163   455 TL 456
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
535-769 8.06e-23

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 103.57  E-value: 8.06e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  535 RAKSQFLAKMSHELRTPLNAILGFTQLMTRNR-SLSPEdqenldiISRSGEhLL--------ALINDVLEMSKIEAGQLT 605
Cdd:NF040691   269 RLQQRFVSDVSHELRTPLTTIRMAADVIHDSRdDFDPA-------TARSAE-LLhteldrfeSLLSDLLEISRFDAGAAE 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  606 LNESYFDLHRLIYSIREMFALKAADKGLEITINL-GQEVNqyVFGDEGKLRQILINLIGNAIKFT----VVghITLRVSY 680
Cdd:NF040691   341 LDVEPVDLRPLVRRVVDALRQLAERAGVELRVDApGTPVV--AEVDPRRVERVLRNLVVNAIEHGegkpVV--VTVAQDD 416
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  681 lnssstttpvDQVIIVfeVEDTGPGIPPEDMDLIFEAFIQAKGGR-QFMQGTGLGLPISRQFAKLMGGDVTVRSFPGQGT 759
Cdd:NF040691   417 ----------TAVAVT--VRDHGVGLKPGEVALVFDRFWRADPARaRTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGS 484
                          250
                   ....*....|
gi 1054616225  760 TFscqvQLTL 769
Cdd:NF040691   485 QF----RLTL 490
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
156-327 2.80e-11

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 62.40  E-value: 2.80e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225   156 NLSELYQNLATSVRKVTQFDRIMIYKFETDNSGVIVAEDKQNHLETYLGLHYPATDIprIARQLYYEKWLRLIPDVNYQP 235
Cdd:smart00065    1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELVLVAADGLTLPTLGIRFPLDEG--LAGRVAETGRPLNIPDVEADP 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225   236 VKLIPtnnpitdtpldlsgaflrsvsplhiEYLQHMGVAASMSISLINQNRLWGLIACHH-YTPKKLDYE----IRKICE 310
Cdd:smart00065   79 LFAED-------------------------LLGRYQGVRSFLAVPLVADGELVGVLALHNkKSPRPFTEEdeelLQALAN 133
                           170
                    ....*....|....*..
gi 1054616225   311 FIGkfASIELVKQQEKH 327
Cdd:smart00065  134 QLA--IALANAQLYEEL 148
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
156-320 3.10e-11

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 61.73  E-value: 3.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  156 NLSELYQNLATSVRKVTQFDRIMIYKFEtdnsgvivaedkqnhletYLGLHYpatdIPRIARQLYyekwLRLIPDVNYQP 235
Cdd:pfam01590    1 DLEEILQTILEELRELLGADRCALYLPD------------------ADGLEY----LPPGARWLK----AAGLEIPPGTG 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  236 VKLIPTNNPITDTPLDLSGAFLRsvsplHIEYLQHMGVAASMSISLINQNRLWGLIACHHYTPKKLDYEIRKIcEFIGKF 315
Cdd:pfam01590   55 VTVLRTGRPLVVPDAAGDPRFLD-----PLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHPRPPFTEEELELL-EVLADQ 128

                   ....*
gi 1054616225  316 ASIEL 320
Cdd:pfam01590  129 VAIAL 133
AdeR_RR NF012227
efflux system response regulator transcription factor AdeR; This protein, the DNA-binding ...
797-899 6.26e-10

efflux system response regulator transcription factor AdeR; This protein, the DNA-binding regulator AdeR, works with its two-component system partner AdeS, to modulate expression of the AdeABC efflux pump.


Pssm-ID: 411091 [Multi-domain]  Cd Length: 239  Bit Score: 60.53  E-value: 6.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRamsEGKDIKIIALTA 876
Cdd:NF012227    14 ILVVEDEYDIGDIIEHYLKREGMRVIRAMNGKQAIEIHASQPIDLILLDIKLPELNGWEVLSKIR---QKAQTPVIMLTA 90
                           90       100
                   ....*....|....*....|...
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKPF 899
Cdd:NF012227    91 LDQDIDKVMALRIGADDFVVKPF 113
GAF COG2203
GAF domain [Signal transduction mechanisms];
138-384 4.37e-06

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 50.58  E-value: 4.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  138 LENYQILEKAIANINNSSNLSELYQNLATSVRKVTQFDRIMIYKFETDNSGVIVAEDKQNHLETYLGLHYPATdiprIAR 217
Cdd:COG2203    189 LERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPLGEG----LAG 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  218 QLYYEKWLRLIPDVNyqpvkliptnnpiTDTPLdlsgaflrsvSPLHIEYLQHMGVAASMSISLINQNRLWGLIACHHYT 297
Cdd:COG2203    265 RALRTGEPVVVNDAS-------------TDPRF----------APSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKE 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  298 PKKLDYEIRKICEFIGKFASIELVKQQEKHLGIYRQQVKLIQEELRASLANQLDYIGNVFKRNETNLLDIVQAQGAVILL 377
Cdd:COG2203    322 PRAFTEEDLELLEALADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAE 401

                   ....*..
gi 1054616225  378 EEQLTVL 384
Cdd:COG2203    402 LLLLLLD 408
 
Name Accession Description Interval E-value
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
505-913 6.41e-89

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 305.93  E-value: 6.41e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  505 QEMR-NNLMLAALEFSHAAlkfAAEQAEIANRAKSQFLAKMSHELRTPLNAILGFTQLMtRNRSLSPEDQENLDIISRSG 583
Cdd:TIGR02956  434 QELAeTNERLNAEVKNHAK---ARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELL-GDTGLTSQQQQYLQVINRSG 509
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  584 EHLLALINDVLEMSKIEAGQLTLNESYFDLHRLIYSIREMFALKAADKGLEITINLGQEVNQYVFGDEGKLRQILINLIG 663
Cdd:TIGR02956  510 ESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVG 589
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  664 NAIKFTVVGHITLRVSyLNssstttpvDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKgGRQFMQGTGLGLPISRQFAK 743
Cdd:TIGR02956  590 NAIKFTDRGSVVLRVS-LN--------DDSSLLFEVEDTGCGIAEEEQATLFDAFTQAD-GRRRSGGTGLGLAISQRLVE 659
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  744 LMGGDVTVRSFPGQGTTFSCQVQLTLVDKIDvlpvTQVTRRVIGLepgqSPHRILIVEDIQENRQLMVKLLESVGFEVCA 823
Cdd:TIGR02956  660 AMDGELGVESELGVGSCFWFTLPLTRGKPAE----DSATLTVIDL----PPQRVLLVEDNEVNQMVAQGFLTRLGHKVTL 731
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  824 AENGLEAInLCVEWKP-HLIWMDIQMPVMDGYEATKEIRAMSEGKD-IKIIALTANAFQEDKQAVLNAGCDDFVAKPFEE 901
Cdd:TIGR02956  732 AESGQSAL-ECFHQHAfDLALLDINLPDGDGVTLLQQLRAIYGAKNeVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVE 810
                          410
                   ....*....|..
gi 1054616225  902 TVLFNKMAQYLN 913
Cdd:TIGR02956  811 EQLTAMIAVILA 822
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
431-762 3.67e-80

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 264.08  E-value: 3.67e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  431 ILAISIVLNQRSYHIIWFRPEQIQIVNWAGNPNQTLSVDPKNNLRLTPRTSFELWKETVKEKSLPWQHFDLEVAQEMRNN 510
Cdd:COG0642      4 LLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  511 LMLAALEFSHAALKFAAEQAEIANRAKSQFLAKMSHELRTPLNAILGFTQLMtrNRSLSPEDQENLDIISRSGEHLLALI 590
Cdd:COG0642     84 LLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELL--LEELDEEQREYLETILRSADRLLRLI 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  591 NDVLEMSKIEAGQLTLNESYFDLHRLIYSIREMFALKAADKGLEITINLGQEVnQYVFGDEGKLRQILINLIGNAIKFTV 670
Cdd:COG0642    162 NDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDL-PTVRGDPDRLRQVLLNLLSNAIKYTP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  671 VG-HITLRVSylnssstttpVDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGRQFmQGTGLGLPISRQFAKLMGGDV 749
Cdd:COG0642    241 EGgTVTVSVR----------REGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSRRG-GGTGLGLAIVKRIVELHGGTI 309
                          330
                   ....*....|...
gi 1054616225  750 TVRSFPGQGTTFS 762
Cdd:COG0642    310 EVESEPGKGTTFT 322
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
528-994 9.89e-76

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 267.87  E-value: 9.89e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  528 EQAEI--------------ANRAKSQFLAKMSHELRTPLNAILGFTQLMTRNrSLSPEDQENLDIISRSGEHLLALINDV 593
Cdd:PRK11107   270 EQMEIqnveldlakkraqeAARIKSEFLANMSHELRTPLNGVIGFTRQTLKT-PLTPTQRDYLQTIERSANNLLAIINDI 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  594 LEMSKIEAGQLTLNESYFDLHRLIYSIREMFALKAADKGLEITINLGQEVNQYVFGDEGKLRQILINLIGNAIKFTVVGH 673
Cdd:PRK11107   349 LDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGN 428
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  674 ITLRVSyLNSSSTttpvDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKGG--RQFmQGTGLGLPISRQFAKLMGGDVTV 751
Cdd:PRK11107   429 IDILVE-LRALSN----TKVQLEVQIRDTGIGISERQQSQLFQAFRQADASisRRH-GGTGLGLVITQKLVNEMGGDISF 502
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  752 RSFPGQGTTFSCQVQLTL-----VDKIDV--------------------------------------------------- 775
Cdd:PRK11107   503 HSQPNRGSTFWFHLPLDLnpnpiIDGLPTdclagkrllyvepnsaaaqatldilsetplevtysptlsqlpeahydilll 582
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  776 -LPVTQV----------------TRRVIGLEPGQSPH------------------------------------------- 795
Cdd:PRK11107   583 gLPVTFRepltmlherlakaksmTDFLILALPCHEQVlaeqlkqdgadaclskplshtrllpallepchhkqppllpptd 662
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 ------RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDI 869
Cdd:PRK11107   663 esrlplTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHNQNT 742
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  870 KIIALTANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKMAQYL-NLHYVYADNSLLIPPETPKKLQKLtaadlqvmsaNW 948
Cdd:PRK11107   743 PIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKpGPKFTSRVVAPEPPEPVHFPNATL----------DW 812
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*...
gi 1054616225  949 IAQVHEAALLIDDAK--LYNLFNQIPASEQQLAEALKDLVDNFHLETI 994
Cdd:PRK11107   813 QLALRQAAGKPDLARdmLQMLLDFLPEVRNKVEEALAGEDPEGLLDLI 860
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
524-898 6.49e-72

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 254.48  E-value: 6.49e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  524 KFAAEQAEIANRAKSQFLAKMSHELRTPLNAILGFTQlMTRNRSLSPEDQENLDIISRSGEHLLALINDVLEMSKIEAGQ 603
Cdd:PRK11091   270 KRYQDALEKASRDKTTFISTISHELRTPLNGIVGLSR-ILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRK 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  604 LTLNESYFDLHRLIYSIREMFALKAADKGLEITINLGQEVNQYVFGDEGKLRQILINLIGNAIKFTVVGHITLRVSYLNS 683
Cdd:PRK11091   349 LQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRYEEG 428
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  684 SStttpvdqviIVFEVEDTGPGIPPEDMDLIFEAFIQAKG--GRQFMQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTF 761
Cdd:PRK11091   429 DM---------LTFEVEDSGIGIPEDELDKIFAMYYQVKDshGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCF 499
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  762 SCQVQLTLVDKIDVLPVTQVTRRVIGLepgqsphRILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHL 841
Cdd:PRK11091   500 TLTIHAPAVAEEVEDAFDEDDMPLPAL-------NILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDL 572
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1054616225  842 IWMDIQMPVMDGYEATKEIRAMSEGKDIK-IIALTANAFQeDKQAVLNAGCDDFVAKP 898
Cdd:PRK11091   573 VLLDIQLPDMTGLDIARELRERYPREDLPpLVALTANVLK-DKKEYLDAGMDDVLSKP 629
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
526-763 2.42e-71

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 236.73  E-value: 2.42e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  526 AAEQAEIANRAKSQFLAKMSHELRTPLNAILGFTQLMTRNRSLSPEDQ-ENLDIISRSGEHLLALINDVLEMSKIEAGQL 604
Cdd:COG2205      5 ALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEDLSPEERrELLEIIRESAERLLRLIEDLLDLSRLESGKL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  605 TLNESYFDLHRLIYSIREMFALKAADKGLEITINLGQEvNQYVFGDEGKLRQILINLIGNAIKFT-VVGHITLRVSYLNS 683
Cdd:COG2205     85 SLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPE-LPLVYADPELLEQVLANLLDNAIKYSpPGGTITISARREGD 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  684 SstttpvdqviIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGRQFmQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFSC 763
Cdd:COG2205    164 G----------VRISVSDNGPGIPEEELERIFERFYRGDNSRGE-GGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTV 232
PRK15347 PRK15347
two component system sensor kinase;
522-914 2.94e-71

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 254.95  E-value: 2.94e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  522 ALKFAAEQAEIANRAKSQFLAKMSHELRTPLNAILGFTQLMtRNRSLSPEDQENLDIISRSGEHLLALINDVLEMSKIEA 601
Cdd:PRK15347   383 ALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELL-QNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRIES 461
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  602 GQLTLNESYFDLHRLIYSIREMFALKAADKGLEITINLGQEVNQYVFGDEGKLRQILINLIGNAIKFTVVGHITLRVSYL 681
Cdd:PRK15347   462 GQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGGIRLRVKRH 541
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  682 NssstttpvDQVIivFEVEDTGPGIPPEDMDLIFEAFIQAKGGrqfMQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTF 761
Cdd:PRK15347   542 E--------QQLC--FTVEDTGCGIDIQQQQQIFTPFYQADTH---SQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCF 608
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  762 SCQVQLT-------------------------------------LVDK-IDVLPvTQVTRRVIGLEPGQsPH-------- 795
Cdd:PRK15347   609 SLVLPLNeyappeplkgelsaplalhrqlsawgitcqpghqnpaLLDPeLAYLP-GRLYDLLQQIIQGA-PNepvinlpl 686
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 -----RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKD-- 868
Cdd:PRK15347   687 qpwqlQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNLDpd 766
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1054616225  869 IKIIALTANAFQEDKQAVLNAGCDDFVAKPfeetVLFNKMAQYLNL 914
Cdd:PRK15347   767 CMIVALTANAAPEEIHRCKKAGMNHYLTKP----VTLAQLARALEL 808
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
431-763 1.27e-66

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 229.05  E-value: 1.27e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  431 ILAISIVLNQRSYHIIWFRPEQIQIVNWAGNPNQTLSVDPKNNLRLTPRTSFELWKETVKEKSLPWQHFDLEVAQEMRNN 510
Cdd:COG5002     59 LLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLALLILLAALLLLLSELLLLLLLLGRLSLRL 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  511 LMLAALEFSHAALKFAAEQAEIANRAKSQFLAKMSHELRTPLNAILGFTQLMTRNRSLSPEDQEN-LDIISRSGEHLLAL 589
Cdd:COG5002    139 SALLLGLLLLAAVERDITELERLEQMRREFVANVSHELRTPLTSIRGYLELLLDGAADDPEERREyLEIILEEAERLSRL 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  590 INDVLEMSKIEAGQLTLNESYFDLHRLIYSIREMFALKAADKGLEITINLGQEvNQYVFGDEGKLRQILINLIGNAIKFT 669
Cdd:COG5002    219 VNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPED-PLLVLGDPDRLEQVLTNLLDNAIKYT 297
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  670 VVG-HITLRVSYLNSSstttpvdqviIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGR-QFMQGTGLGLPISRQFAKLMGG 747
Cdd:COG5002    298 PEGgTITVSLREEDDQ----------VRISVRDTGIGIPEEDLPRIFERFYRVDKSRsRETGGTGLGLAIVKHIVEAHGG 367
                          330
                   ....*....|....*.
gi 1054616225  748 DVTVRSFPGQGTTFSC 763
Cdd:COG5002    368 RIWVESEPGKGTTFTI 383
PHY pfam00360
Phytochrome region; Phytochromes are red/far-red photochromic biliprotein photoreceptors which ...
335-512 2.33e-56

Phytochrome region; Phytochromes are red/far-red photochromic biliprotein photoreceptors which regulate plant development. They are widely represented in both photosynthetic and non-photosynthetic bacteria and are known in a variety of fungi. Although sequence similarities are low, this domain is structurally related to pfam01590, which is generally located immediately N-terminal to this domain. Compared with pfam01590, this domain carries an additional tongue-like hairpin loop between the fifth beta-sheet and the sixth alpha-helix which functions to seal the chromophore pocket and stabilize the photoactivated far-red-absorbing state (Pfr). The tongue carries a conserved PRxSF motif, from which an arginine finger points into the chromophore pocket close to ring D forming a salt bridge with a conserved aspartate residue.


Pssm-ID: 425635  Cd Length: 178  Bit Score: 192.48  E-value: 2.33e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  335 VKLIQEELRASLANQLDYIGnVFKRNETNLLDIVQAQGAVILLEEQLTVLGNTPSEAAIYELVNWLMNRNSQEIFYTDSL 414
Cdd:pfam00360    1 LRRIQDRLVEAMARADDLVD-GLVDQSPNLLDLVKADGAALCFGGNLLTLGETPPEEAIRDLAQWLGRNHDSEVFSTDSL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  415 PKIYPKAKNFQNIACGILAISIVLNQRSYhIIWFRPEQIQIVNWAGNPNQTLSVDPkNNLRLTPRTSFELWKETVKEKSL 494
Cdd:pfam00360   80 SQAYPEAAALADVASGLLAIPISRKPGNY-LLWFRPEVVRTVNWGGDPHKAVEIDP-GGVRLSPRKSFDAWKETVRGRSL 157
                          170
                   ....*....|....*...
gi 1054616225  495 PWQHFDLEVAQEMRNNLM 512
Cdd:pfam00360  158 PWSEVEIEAARELREALL 175
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
513-914 2.14e-53

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 202.06  E-value: 2.14e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  513 LAALEFSHaalKFAAEQAEIANRAKSQFLAKMSHELRTPLNAILGFTQLMTRNrSLSPEDQENLDIISRSGEHLLALIND 592
Cdd:PRK11466   423 LQELVIEH---RQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADN-PALNAQRDDLRAITDSGESLLTILND 498
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  593 VLEMSKIEAG--QLTLNESYFDLHRLIYSIREMFALKAADKGLEITINLGQEVNQYVFGDEGKLRQILINLIGNAIKFTV 670
Cdd:PRK11466   499 ILDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALRFTD 578
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  671 VGHITLRvsylnsssttTPVDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGRqfmQGTGLGLPISRQFAKLMGGDVT 750
Cdd:PRK11466   579 EGSIVLR----------SRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFVQVSGKR---GGTGLGLTISSRLAQAMGGELS 645
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  751 VRSFPGQGTTFSCQVQLtlvdKIDVLPVTQVTRRVIGLEpgqsPHRILIVEDIQENRQLMVKLLESVGFEVCAAENGLEA 830
Cdd:PRK11466   646 ATSTPEVGSCFCLRLPL----RVATAPVPKTVNQAVRLD----GLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQA 717
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  831 INLCVEWKP-HLIWMDIQMPVMDGYEATKEIraMSEGKDIKIIALTANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKMA 909
Cdd:PRK11466   718 LETLQNSEPfAAALVDFDLPDYDGITLARQL--AQQYPSLVLIGFSAHVIDETLRQRTSSLFRGIIPKPVPREVLGQLLA 795

                   ....*
gi 1054616225  910 QYLNL 914
Cdd:PRK11466   796 HYLQL 800
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
496-762 2.60e-50

Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms];


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 186.14  E-value: 2.60e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  496 WQHFDLEVAQEMRNNLMLAALEfshAALKFAAEQAEIANRAKSQFLAKMSHELRTPLNAILGFTQLMTR--NRSLSPEDQ 573
Cdd:COG4251    244 LLLLLILVLELLELRLELEELE---EELEERTAELERSNEELEQFAYVASHDLREPLRKISGFSQLLEEdyGDKLDEEGR 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  574 ENLDIISRSGEHLLALINDVLEMSKIEAGQLTLNEsyFDLHRLIYSIREMFALKAADKGLEITINLGQEVnqyvFGDEGK 653
Cdd:COG4251    321 EYLERIRDAAERMQALIDDLLAYSRVGRQELEFEP--VDLNELLEEVLEDLEPRIEERGAEIEVGPLPTV----RGDPTL 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  654 LRQILINLIGNAIKFT---VVGHITLRVSYLNSSstttpvdqviIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGRQFmQG 730
Cdd:COG4251    395 LRQVFQNLISNAIKYSrpgEPPRIEIGAEREGGE----------WVFSVRDNGIGIDPEYAEKIFEIFQRLHSRDEY-EG 463
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1054616225  731 TGLGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:COG4251    464 TGIGLAIVKKIVERHGGRIWVESEPGEGATFY 495
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
526-914 1.27e-49

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 190.57  E-value: 1.27e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  526 AAEQAeiaNRAKSQFLAKMSHELRTPLNAILGFTQLMtRNRSLSPEDQENLDIISRSGEHLLALINDVLEMSKIEAGQLT 605
Cdd:PRK10841   439 AAEQA---SQSKSMFLATVSHELRTPLYGIIGNLDLL-QTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQLK 514
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  606 LNESYFDLHRLIYSIREMFALKAADKGLEITINLGQEVNQYVFGDEGKLRQILINLIGNAIKFTVVGHITLRVSylnsss 685
Cdd:PRK10841   515 IEPREFSPREVINHITANYLPLVVKKRLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHVR------ 588
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  686 tttpVDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGRQ-FMQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFS-- 762
Cdd:PRK10841   589 ----VDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQrNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTir 664
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  763 ---------------------C----------------------QVQL---TLVDKIDVL-------------PVTQVTR 783
Cdd:PRK10841   665 iplygaqypqkkgveglqgkrCwlavrnasleqfletllqrsgiQVQRyegQEPTPEDVLitddpvqkkwqgrAVITFCR 744
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  784 RVIG----LEPGQ------SPH------------------------------------RILIVEDIQENRQLMVKLLESV 817
Cdd:PRK10841   745 RHIGipleIAPGEwvhstaTPHelpallariyrielesddsanalpstdkavsdnddmMILVVDDHPINRRLLADQLGSL 824
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  818 GFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMseGKDIKIIALTANAFQEDKQAVLNAGCDDFVAK 897
Cdd:PRK10841   825 GYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQL--GLTLPVIGVTANALAEEKQRCLEAGMDSCLSK 902
                          490
                   ....*....|....*..
gi 1054616225  898 PFEETVLFNKMAQYLNL 914
Cdd:PRK10841   903 PVTLDVLKQTLTVYAER 919
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
522-954 2.60e-48

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 187.63  E-value: 2.60e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  522 ALKFAAEQAEIANRAKSQFLAKMSHELRTPLNAILGFTQLMTrNRSLSPEDQ-ENLDIISRSGEHLLALINDVLEMSKIE 600
Cdd:PRK09959   697 ALEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLS-GSGLSKEQRvEAISLAYATGQSLLGLIGEILDVDKIE 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  601 AGQLTLNESYFDLHRLIYSIREMFALKAADKGLEITINLGQEVNQYVFGDEGKLRQILINLIGNAIKFTVVGHITLRVSY 680
Cdd:PRK09959   776 SGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSL 855
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  681 LNSSStttpvDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGRQfMQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTT 760
Cdd:PRK09959   856 GHIDD-----NHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQ-QTGSGLGLMICKELIKNMQGDLSLESHPGIGTT 929
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  761 FSCQVQLTLVDKIDVLPVTqvtrrviGLEPGQSPHR--ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWK 838
Cdd:PRK09959   930 FTITIPVEISQQVATVEAK-------AEQPITLPEKlsILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQH 1002
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  839 PHLIWMDIQMPVMDGYEATKEIRamSEGKDIKIIALTANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKMAQylnLHYVy 918
Cdd:PRK09959  1003 YDLLITDVNMPNMDGFELTRKLR--EQNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQ---LHQV- 1076
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1054616225  919 adnSLLIPPETPKKLQKL---TAADLQVMSANWIAQVHE 954
Cdd:PRK09959  1077 ---AHIAPQYRHLDIEALknnTANDLQLMQEILMTFQHE 1112
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
654-767 5.60e-47

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 163.05  E-value: 5.60e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  654 LRQILINLIGNAIKFTVVGHITLRVSYLNSSStttpvDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKGG--RQFmQGT 731
Cdd:cd16922      1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEE-----DGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSttRKY-GGT 74
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1054616225  732 GLGLPISRQFAKLMGGDVTVRSFPGQGTTFSCQVQL 767
Cdd:cd16922     75 GLGLAISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
790-915 1.56e-46

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: 162.71  E-value: 1.56e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  790 PGQSPHRILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDI 869
Cdd:COG0784      1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDI 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1054616225  870 KIIALTANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKMAQYLNLH 915
Cdd:COG0784     81 PIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARA 126
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
528-762 6.52e-43

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 160.40  E-value: 6.52e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  528 EQAEIANRAKS--QFLAKMSHELRTPLNAILGFTQLMTRNRSlSPEDQENLDIISRSGEHLLALINDVLEMSKIEAGQLT 605
Cdd:COG3852    124 RELRRAEKLAAvgELAAGLAHEIRNPLTGIRGAAQLLERELP-DDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPERE 202
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  606 LnesyFDLHRLIYSIREMfALKAADKGLEITINLGQEVNQyVFGDEGKLRQILINLIGNAIK-FTVVGHITLRVSYLNSS 684
Cdd:COG3852    203 P----VNLHEVLERVLEL-LRAEAPKNIRIVRDYDPSLPE-VLGDPDQLIQVLLNLVRNAAEaMPEGGTITIRTRVERQV 276
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054616225  685 STTTPVDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGrqfmqGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:COG3852    277 TLGGLRPRLYVRIEVIDNGPGIPEEILDRIFEPFFTTKEK-----GTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFR 349
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
797-908 3.88e-42

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: 149.54  E-value: 3.88e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAM-SEGKDIKIIALT 875
Cdd:cd17546      1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELeGGGRRTPIIALT 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1054616225  876 ANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKM 908
Cdd:cd17546     81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
499-762 9.00e-41

Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 154.19  E-value: 9.00e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  499 FDLEVAQEMRNNLMLAALEFSHAALKFAAEQAEianRAKSQFL--AKMS----------HELRTPLNAILGFTQLMTR-- 564
Cdd:COG4191     95 LLLLAALDAEENAELEELERDITELERAEEELR---ELQEQLVqsEKLAalgelaagiaHEINNPLAAILGNAELLRRrl 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  565 NRSLSPED-QENLDIISRSGEHLLALINDVLEMSKIEAGQLTLnesyFDLHRLIYSIREMFALKAADKGLEITINLGQEV 643
Cdd:COG4191    172 EDEPDPEElREALERILEGAERAAEIVRSLRAFSRRDEEEREP----VDLNELIDEALELLRPRLKARGIEVELDLPPDL 247
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  644 NQyVFGDEGKLRQILINLIGNAI---KFTVVGHITLRvsylnsssTTTPVDQVIIvfEVEDTGPGIPPEDMDLIFEAFIQ 720
Cdd:COG4191    248 PP-VLGDPGQLEQVLLNLLINAIdamEEGEGGRITIS--------TRREGDYVVI--SVRDNGPGIPPEVLERIFEPFFT 316
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1054616225  721 AKGGRQfmqGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:COG4191    317 TKPVGK---GTGLGLSISYGIVEKHGGRIEVESEPGGGTTFT 355
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
794-905 1.76e-39

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: 144.28  E-value: 1.76e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  794 PHRILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKIIA 873
Cdd:COG3706      1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIF 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1054616225  874 LTANAFQEDKQAVLNAGCDDFVAKPFEETVLF 905
Cdd:COG3706     81 LTALDDEEDRARALEAGADDYLTKPFDPEELL 112
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
796-900 2.54e-38

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: 138.44  E-value: 2.54e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKIIALT 875
Cdd:cd17548      1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALT 80
                           90       100
                   ....*....|....*....|....*
gi 1054616225  876 ANAFQEDKQAVLNAGCDDFVAKPFE 900
Cdd:cd17548     81 AYAMKGDREKILEAGCDGYISKPID 105
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
538-762 3.11e-37

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 147.04  E-value: 3.11e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  538 SQFLAKMSHELRTPLNAILGFTQLMtrNRSLSPEDQENLDIISRSGEHLLALINDVLEMSKIEAGQLTLnesyFDLHRLI 617
Cdd:COG5809    271 GELAAGIAHEIRNPLTSLKGFIQLL--KDTIDEEQKTYLDIMLSELDRIESIISEFLVLAKPQAIKYEP----KDLNTLI 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  618 YSIREMFALKAADKGLEITINLGQEVNqYVFGDEGKLRQILINLIGNAIKFTVV-GHITLRvsylnssstTTPVDQVIIV 696
Cdd:COG5809    345 EEVIPLLQPQALLKNVQIELELEDDIP-DILGDENQLKQVFINLLKNAIEAMPEgGNITIE---------TKAEDDDKVV 414
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054616225  697 FEVEDTGPGIPPEDMDLIFEAFIQAKGgrqfmQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:COG5809    415 ISVTDEGCGIPEERLKKLGEPFYTTKE-----KGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFS 475
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
535-763 1.37e-36

phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory histidine kinase PhoR associated with the phosphate ABC transporter in most Proteobacteria. Related proteins from Gram-positive organisms are not included in this model. The phoR gene usually is adjacent to the response regulator phoB gene (TIGR02154). [Signal transduction, Two-component systems]


Pssm-ID: 274368 [Multi-domain]  Cd Length: 333  Bit Score: 141.19  E-value: 1.37e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  535 RAKSQFLAKMSHELRTPLNAILGFTQLMTRNRSLSPEDQEN-LDIISRSGEHLLALINDVLEMSKIEAGQLTLNESYFDL 613
Cdd:TIGR02966  112 QMRRDFVANVSHELRTPLTVLRGYLETLADGPDEDPEEWNRaLEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDM 191
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  614 HRLIYSIREMFALKAADKGLEITINLgqEVNQYVFGDEGKLRQILINLIGNAIKFTVVG-HITLRVSylnssstttpVDQ 692
Cdd:TIGR02966  192 PALLDHLRDEAEALSQGKNHQITFEI--DGGVDVLGDEDELRSAFSNLVSNAIKYTPEGgTITVRWR----------RDG 259
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054616225  693 VIIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGR-QFMQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFSC 763
Cdd:TIGR02966  260 GGAEFSVTDTGIGIAPEHLPRLTERFYRVDKSRsRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFSF 331
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
649-762 1.63e-35

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 130.46  E-value: 1.63e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225   649 GDEGKLRQILINLIGNAIKFTV-VGHITLRVSylnssstttpVDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGRQF 727
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPeGGRITVTLE----------RDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRK 70
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 1054616225   728 MQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:smart00387   71 IGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFT 105
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
542-762 2.02e-35

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 140.10  E-value: 2.02e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  542 AKMSHELRTPLNAILGFTQLMTRNRSLSPED-----QENLDIISRSGEHLLALINDVLEMSKIEAGQLTLnesyFDLHRL 616
Cdd:COG5000    206 RRIAHEIKNPLTPIQLSAERLRRKLADKLEEdredlERALDTIIRQVDRLKRIVDEFLDFARLPEPQLEP----VDLNEL 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  617 IYSIREMFALKAADKGLEITINLGQEVNQyVFGDEGKLRQILINLIGNAIKFTV-VGHITLRVSYLNSSstttpvdqviI 695
Cdd:COG5000    282 LREVLALYEPALKEKDIRLELDLDPDLPE-VLADRDQLEQVLINLLKNAIEAIEeGGEIEVSTRREDGR----------V 350
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054616225  696 VFEVEDTGPGIPPEDMDLIFEAFIQAKGgrqfmQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:COG5000    351 RIEVSDNGPGIPEEVLERIFEPFFTTKP-----KGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFT 412
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
794-912 2.91e-35

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: 133.16  E-value: 2.91e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  794 PHRILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAmsEGKDIKIIA 873
Cdd:COG0745      1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRA--RPSDIPIIM 78
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1054616225  874 LTANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKMAQYL 912
Cdd:COG0745     79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALL 117
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
792-915 5.10e-35

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: 133.37  E-value: 5.10e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  792 QSPHRILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKI 871
Cdd:COG3437      4 GQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPV 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1054616225  872 IALTANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKMAQYLNLH 915
Cdd:COG3437     84 IFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELR 127
KinD COG5808
Sporulation sensor histidine kinase D [Cell cycle control, cell division, chromosome ...
330-762 1.29e-34

Sporulation sensor histidine kinase D [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444510 [Multi-domain]  Cd Length: 454  Bit Score: 138.34  E-value: 1.29e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  330 IYRQQVKLIQEELRASL---ANQLDYIGNVFKRNETnlLDIVQAQGAVILLEEqltVLGNTPSEAAIYELVNWLMNRNSQ 406
Cdd:COG5808     26 FYEDERDKMIEENLQELnlyRNKLDYFIETLARLDS--LATADIKVIKGILDE---TYDKDPRFSGLYILDESLMGAKAT 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  407 EIFYTDSLPKIYPKAKNFQNIACGILAISIVLNQRSYHIIWFRPEQ-IQIVNwagNPNQTLSVDPKNNLRLTPRTSF--E 483
Cdd:COG5808    101 KKTVISSDITSTISAPIMDKELTNFLLASIRMDYIRALINILDPDKyIEIVD---QNGQSVFTSGHREESKSVSNKLdkV 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  484 LWKETVKEKSLPWQHFDLEVAQEMRNNLMLAALEFSHAAL-----KFAAEQAEIANRAK-----SQFLAKMSHELRTPLN 553
Cdd:COG5808    178 PWEVEVYPNPVTNDELGQALAIRKLIILVLISIIFLLLQYnllkrKTLLERVIQEINTQkleliGTFAASTAHEIRNPLT 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  554 AILGFTQLMtRNRSLSPEDQENLDIISRSGEHLLALINDVLEMSKIEAGQLTLNesyfDLHRLIYSIREMFALKAADKGL 633
Cdd:COG5808    258 SIKGFIQLL-QEKYPELEDQKYFDIIQEEIQRINQIVSEFLVLGKPTAKKLELD----DLNELIEEILSIIDSEANLKNI 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  634 EITINLGQEvNQYVFGDEGKLRQILINLIGNAIKFTVVGHITLRVSYLNSSStttpvdqviIVFEVEDTGPGIPPEDMDL 713
Cdd:COG5808    333 RVEKQSLDE-PLHIKCDKDRIKQVLLNLIKNAIEAMKEGGKLTISIENDDEK---------AVIEVIDNGEGIPEDIIDE 402
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1054616225  714 IFEAFIQAKGGrqfmqGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:COG5808    403 IFEPFVTTKEG-----GTGLGLSVCKRIVEMHGGEIDIESEEGKGTTFT 446
KinC COG5807
Sporulation sensor histidine kinase C [Cell cycle control, cell division, chromosome ...
538-762 1.78e-32

Sporulation sensor histidine kinase C [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444509 [Multi-domain]  Cd Length: 358  Bit Score: 129.91  E-value: 1.78e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  538 SQFLAKMSHELRTPLNAILGFTQLMtRNRSLSPEDQENLDIISRSGEHLLALINDVLEMSKIEAgqltLNESYFDLHRLI 617
Cdd:COG5807    148 GELAAGIAHEIRNPLTSIKGFLQLL-QESREDSEREEYFNIIISEIDRINTIITELLVLSKPKK----FNFKKLNLNDVL 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  618 YSIREMFALKAADKGLEITINLGQEVNQyVFGDEGKLRQILINLIGNAIK-FTVVGHITLRVSYLNSSstttpvdqviIV 696
Cdd:COG5807    223 EDVIALLSTEAILKNISIKYDLADDEPV-INGDKNQLKQVFINLIKNAIEaMETGGNITIKTYVEGDF----------VV 291
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054616225  697 FEVEDTGPGIPPEDMDLIFEAFIQAKGgrqfmQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:COG5807    292 ISVKDEGIGIPEEVLEKIGEPFFTTKE-----EGTGLGLSICKKIIEEHNGTIEVESKPGKGTTFT 352
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
649-768 6.63e-31

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 117.08  E-value: 6.63e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  649 GDEGKLRQILINLIGNAIKFTVV-GHITLRVSylnssstttpvDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGRQF 727
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAAKaGEITVTLS-----------EGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGG 69
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1054616225  728 mqGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFSCQVQLT 768
Cdd:pfam02518   70 --GTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
797-900 4.08e-29

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: 112.17  E-value: 4.08e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKIIALTA 876
Cdd:cd17580      1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTG 80
                           90       100
                   ....*....|....*....|....
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKPFE 900
Cdd:cd17580     81 YGQPEDRERALEAGFDAHLVKPVD 104
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
797-907 6.65e-29

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: 111.47  E-value: 6.65e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAmsEGKDIKIIALTA 876
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRR--RDPTTPVIILTA 78
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKPFEETVLFNK 907
Cdd:pfam00072   79 HGDEDDAVEALEAGADDFLSKPFDPDELLAA 109
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
796-899 1.09e-28

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: 110.67  E-value: 1.09e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKIIALT 875
Cdd:cd17538      1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                           90       100
                   ....*....|....*....|....
gi 1054616225  876 ANAFQEDKQAVLNAGCDDFVAKPF 899
Cdd:cd17538     81 ALDDREDRIRGLEAGADDFLSKPI 104
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
502-761 1.82e-28

heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 120.18  E-value: 1.82e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  502 EVAQEMrnNLMLAALEFSHAALkfaaeqaeianrakSQFLAKMSHELRTPLNAILGFTQ-LMTRNRSLSP-ED--QENLD 577
Cdd:TIGR01386  222 ELAQSF--NAMLGRLEDAFQRL--------------SQFSADLAHELRTPLTNLLGQTQvALSQPRTGEEyREvlESNLE 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  578 IISRsgehLLALINDVLEMSKIEAGQLTLNESYFDLHRLIYSIREMFALKAADKGLEITInlgqEVNQYVFGDEGKLRQI 657
Cdd:TIGR01386  286 ELER----LSRMVSDMLFLARADNGQLALERVRLDLAAELAKVAEYFEPLAEERGVRIRV----EGEGLVRGDPQMFRRA 357
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  658 LINLIGNAIKFTVVGHiTLRVSYLNSSSTTTPVdqviivfeVEDTGPGIPPEDMDLIFEAFIQAKGGRQFMQ-GTGLGLP 736
Cdd:TIGR01386  358 ISNLLSNALRHTPDGG-TITVRIERRSDEVRVS--------VSNPGPGIPPEHLSRLFDRFYRVDPARSNSGeGTGLGLA 428
                          250       260
                   ....*....|....*....|....*
gi 1054616225  737 ISRQFAKLMGGDVTVRSfPGQGTTF 761
Cdd:TIGR01386  429 IVRSIMEAHGGRASAES-PDGKTRF 452
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
654-762 2.70e-28

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.


Pssm-ID: 340391 [Multi-domain]  Cd Length: 102  Bit Score: 109.61  E-value: 2.70e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  654 LRQILINLIGNAIKFTVV-GHITLRVSYLNSSstttpvdqviIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGRQfMQGTG 732
Cdd:cd00075      1 LEQVLSNLLDNALKYSPPgGTIEISLRQEGDG----------VVLEVEDNGPGIPEEDLERIFERFYRGDKSRE-GGGTG 69
                           90       100       110
                   ....*....|....*....|....*....|
gi 1054616225  733 LGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:cd00075     70 LGLAIVRRIVEAHGGRITVESEPGGGTTFT 99
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
798-898 5.92e-28

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: 108.26  E-value: 5.92e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  798 LIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAmsEGKDIKIIALTAN 877
Cdd:cd17574      1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLRE--KGSDIPIIMLTAK 78
                           90       100
                   ....*....|....*....|.
gi 1054616225  878 AFQEDKQAVLNAGCDDFVAKP 898
Cdd:cd17574     79 DEEEDKVLGLELGADDYITKP 99
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
796-898 1.74e-26

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: 104.47  E-value: 1.74e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLES-VGFEVCA-AENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMseGKDIKIIA 873
Cdd:COG4753      1 KVLIVDDEPLIREGLKRILEWeAGFEVVGeAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIREL--DPDTKIII 78
                           90       100
                   ....*....|....*....|....*
gi 1054616225  874 LTANAFQEDKQAVLNAGCDDFVAKP 898
Cdd:COG4753     79 LSGYSDFEYAQEAIKLGADDYLLKP 103
PAS_2 pfam08446
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
15-129 1.79e-26

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 400652  Cd Length: 107  Bit Score: 104.64  E-value: 1.79e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225   15 CEQDPINIPGSIQPHGMLIVLQEPELNILQVSENTRDYLGIDAKFLLGKNLSFLIPTATIRIIKQYLTQKNLSLIPLIEI 94
Cdd:pfam08446    1 CYLEPIQRPGLIQPHGCLLAVDEPSLRVLQYSENAAEMLGLPAEDLLGTDLRDLFGASSASLLRKALAAGEISLLNPILI 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1054616225   95 TLKCSSKcqpknqsnSFLGMLHRSENVLILELEPQ 129
Cdd:pfam08446   81 HSRTSGK--------PFYAILHRSDGGLVLELEPA 107
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
798-898 1.85e-26

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: 104.23  E-value: 1.85e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  798 LIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAmsEGKDIKIIALTAN 877
Cdd:cd00156      1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRE--LPPDIPVIVLTAK 78
                           90       100
                   ....*....|....*....|.
gi 1054616225  878 AFQEDKQAVLNAGCDDFVAKP 898
Cdd:cd00156     79 ADEEDAVRALELGADDYLVKP 99
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
527-767 6.09e-25

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 109.53  E-value: 6.09e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  527 AEQAEIANRAKSQFLAKMSHELRTPLNAILGftQLMTRNRSLSPEDQENLDIISRSGEHLLALINDVLEMSKIEAGQLTL 606
Cdd:NF012163   230 ASTLEKNEQMRRDFMADISHELRTPLAVLRA--ELEAIQDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEGALAY 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  607 NESYFDLHRLIYSIREMFALKAADKGLEITINLgqEVNQYVFGDEGKLRQILINLIGNAIKFTVVGHiTLRVSylnssst 686
Cdd:NF012163   308 QKASVDLVPLLEVEGGAFRERFASAGLELEVSL--PDSSLVFGDRDRLMQLFNNLLENSLRYTDSGG-SLHIS------- 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  687 TTPVDQVIIVFeVEDTGPGIPPEDMDLIFEAFIQAKGGRQFMQ-GTGLGLPISRQFAKLMGGDVTVRSFPGQGttFSCQV 765
Cdd:NF012163   378 ASQRPKEVTLT-VADSAPGVSDEQLARLFERFYRVEVSRNRASgGSGLGLAISLNIVQAHGGTLHAAHSPLGG--LRIVV 454

                   ..
gi 1054616225  766 QL 767
Cdd:NF012163   455 TL 456
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
545-904 2.83e-24

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 109.77  E-value: 2.83e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  545 SHELRTPLNAILGFTQlMTRNRSL-SPEDQENLDIISRSGEHLLALINDVLEMSKIEAGQLTlnesYFDLHRLIysiREM 623
Cdd:PRK13837   458 AHNFNNILGAILGYAE-MALNKLArHSRAARYIDEIISAGARARLIIDQILAFGRKGERNTK----PFDLSELV---TEI 529
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  624 FALKAADKGLEITINLGQEVNQ-YVFGDEGKLRQILINLIGNAIK-FTVVGHITLRVSYLN-------SSSTTTPVDqvI 694
Cdd:PRK13837   530 APLLRVSLPPGVELDFDQDQEPaVVEGNPAELQQVLMNLCSNAAQaMDGAGRVDISLSRAKlrapkvlSHGVLPPGR--Y 607
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  695 IVFEVEDTGPGIPPEDMDLIFEAFIQAKGGrqfmqGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFscQVQLTLVDKID 774
Cdd:PRK13837   608 VLLRVSDTGAGIDEAVLPHIFEPFFTTRAG-----GTGLGLATVHGIVSAHAGYIDVQSTVGRGTRF--DVYLPPSSKVP 680
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  775 VLPVTQVTRRVIGLEPGQSphrILIVEDIQENRQLMVKLL-----ESVGFEVCAaenglEAINLCVEWKPHLIWMDIQMP 849
Cdd:PRK13837   681 VAPQAFFGPGPLPRGRGET---VLLVEPDDATLERYEEKLaalgyEPVGFSTLA-----AAIAWISKGPERFDLVLVDDR 752
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1054616225  850 VMDGYEATKEIRAMSegKDIKIIALTANAFQEDKQAVLNAGCdDFVAKPFEETVL 904
Cdd:PRK13837   753 LLDEEQAAAALHAAA--PTLPIILGGNSKTMALSPDLLASVA-EILAKPISSRTL 804
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
796-902 4.43e-24

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: 97.90  E-value: 4.43e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGF-EVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKIIAL 874
Cdd:cd17551      2 RILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVMI 81
                           90       100
                   ....*....|....*....|....*...
gi 1054616225  875 TANAFQEDKQAVLNAGCDDFVAKPFEET 902
Cdd:cd17551     82 TADTDREVRLRALEAGATDFLTKPFDPV 109
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
793-915 1.12e-23

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: 105.05  E-value: 1.12e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  793 SPHRILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAmsEGKDIKII 872
Cdd:COG2204      1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRA--LDPDLPVI 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1054616225  873 ALTANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKMAQYLNLH 915
Cdd:COG2204     79 LLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERR 121
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
796-898 2.05e-23

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: 96.31  E-value: 2.05e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESV-GFEVCA-AENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIraMSEgKDIKIIA 873
Cdd:cd17541      2 RVLIVDDSAVMRKLLSRILESDpDIEVVGtARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRI--MAE-RPTPVVM 78
                           90       100
                   ....*....|....*....|....*...
gi 1054616225  874 LTANAfQEDKQAVLNA---GCDDFVAKP 898
Cdd:cd17541     79 VSSLT-EEGAEITLEAlelGAVDFIAKP 105
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
797-899 2.15e-23

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: 95.66  E-value: 2.15e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKIIALTA 876
Cdd:cd19920      1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTA 80
                           90       100
                   ....*....|....*....|...
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKPF 899
Cdd:cd19920     81 LTDTEDKVKGFELGAVDYITKPF 103
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
792-928 4.37e-23

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 95.81  E-value: 4.37e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  792 QSPHRILIVEDIQENRQLMVKLLESV-GFEVCA-AENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAmsEGKDI 869
Cdd:COG4565      1 MKMIRVLIVEDDPMVAELLRRYLERLpGFEVVGvASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRA--RGPDV 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1054616225  870 KIIALTANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKMAQYLNLHYVYADNSLLIPPE 928
Cdd:COG4565     79 DVIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQEEDLPE 137
PRK10490 PRK10490
sensor protein KdpD; Provisional
497-778 6.85e-23

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 105.50  E-value: 6.85e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  497 QHFDLEVAqemrNNLMLAALEFSHAALKFAAEQAEIANraksQFLAKMSHELRTPLNAILGFTQLMTRNrsLSPEDQENL 576
Cdd:PRK10490   632 ETFTLLIA----NALERLTLTASEEQARLASEREQLRN----ALLAALSHDLRTPLTVLFGQAEILTLD--LASEGSPHA 701
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  577 DIISRSGEHLLA---LINDVLEMSKIEAGQLTLNESYFDLHRLIYSiremfALKAADKGL---EITINLGQEVnQYVFGD 650
Cdd:PRK10490   702 RQASEIRQQVLNttrLVNNLLDMARIQSGGFNLRKEWLTLEEVVGS-----ALQMLEPGLsghPINLSLPEPL-TLIHVD 775
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  651 EGKLRQILINLIGNAIKFTvvGH---ITLRVsylnssstTTPVDQVIIvfEVEDTGPGIPPEDMDLIFEAFiqAKGGRQ- 726
Cdd:PRK10490   776 GPLFERVLINLLENAVKYA--GAqaeIGIDA--------HVEGERLQL--DVWDNGPGIPPGQEQLIFDKF--ARGNKEs 841
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1054616225  727 FMQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFSCQVQLTLVDKIDVLPV 778
Cdd:PRK10490   842 AIPGVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVTLPLETPPELEEFHE 893
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
535-769 8.06e-23

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 103.57  E-value: 8.06e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  535 RAKSQFLAKMSHELRTPLNAILGFTQLMTRNR-SLSPEdqenldiISRSGEhLL--------ALINDVLEMSKIEAGQLT 605
Cdd:NF040691   269 RLQQRFVSDVSHELRTPLTTIRMAADVIHDSRdDFDPA-------TARSAE-LLhteldrfeSLLSDLLEISRFDAGAAE 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  606 LNESYFDLHRLIYSIREMFALKAADKGLEITINL-GQEVNqyVFGDEGKLRQILINLIGNAIKFT----VVghITLRVSY 680
Cdd:NF040691   341 LDVEPVDLRPLVRRVVDALRQLAERAGVELRVDApGTPVV--AEVDPRRVERVLRNLVVNAIEHGegkpVV--VTVAQDD 416
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  681 lnssstttpvDQVIIVfeVEDTGPGIPPEDMDLIFEAFIQAKGGR-QFMQGTGLGLPISRQFAKLMGGDVTVRSFPGQGT 759
Cdd:NF040691   417 ----------TAVAVT--VRDHGVGLKPGEVALVFDRFWRADPARaRTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGS 484
                          250
                   ....*....|
gi 1054616225  760 TFscqvQLTL 769
Cdd:NF040691   485 QF----RLTL 490
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
544-769 8.89e-23

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 103.00  E-value: 8.89e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  544 MSHELRTPLNAILGFTQLMtrNRSLSPEDQEN-LDIISRSGEHLLALINDVLEMSKIEAGQLTLNESYFDLHRLIYSIRE 622
Cdd:PRK11100   263 LTHELKSPLAAIRGAAELL--QEDPPPEDRARfTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVE 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  623 MFALKAADKGLEITInlgQEVNQYVFGDEGKLRQILINLIGNAIKFTVVG-HITLRVSYLNssstttpvDQVIIVfeVED 701
Cdd:PRK11100   341 AREAQAAAKGITLRL---RPDDARVLGDPFLLRQALGNLLDNAIDFSPEGgTITLSAEVDG--------EQVALS--VED 407
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054616225  702 TGPGIPPEDMDLIFEAFI---QAKGGRQfmqGTGLGLPISRQFAKLMGGDVTVRSFPGQGTtfscQVQLTL 769
Cdd:PRK11100   408 QGPGIPDYALPRIFERFYslpRPANGRK---STGLGLAFVREVARLHGGEVTLRNRPEGGV----LATLTL 471
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
425-762 1.91e-22

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 103.12  E-value: 1.91e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  425 QNIACGILAISivlnqRSYHIIWFRPEQIQIV-----NWAGNP-NQTLSVDPK--NNLRLTPRTsfelwKETVKEKSLPW 496
Cdd:PRK11360   269 ESIADGVIAID-----RQGKITTMNPAAEVITglqrhELVGKPySELFPPNTPfaSPLLDTLEH-----GTEHVDLEISF 338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  497 QHFD----LEVAQEM----RNNLMLAALEFSH-AALKFAAEQAEIANR--AKSQFLAKMSHELRTPLNAILGFTQLMTRN 565
Cdd:PRK11360   339 PGRDrtieLSVSTSLlhntHGEMIGALVIFSDlTERKRLQRRVARQERlaALGELVAGVAHEIRNPLTAIRGYVQIWRQQ 418
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  566 RSLSPEdQENLDIISRSGEHLLALINDVLEMSKIeagqltlNESYF---DLHRLIYSIREMFALKAADKGLEITINLGQE 642
Cdd:PRK11360   419 TSDPPS-QEYLSVVLREVDRLNKVIDQLLEFSRP-------RESQWqpvSLNALVEEVLQLFQTAGVQARVDFETELDNE 490
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  643 VNQyVFGDEGKLRQILINLIGNAIK-FTVVGHITLRVSYLNSsstttpvDQVIIvfEVEDTGPGIPPEDMDLIFEAFIQA 721
Cdd:PRK11360   491 LPP-IWADPELLKQVLLNILINAVQaISARGKIRIRTWQYSD-------GQVAV--SIEDNGCGIDPELLKKIFDPFFTT 560
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1054616225  722 KGgrqfmQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:PRK11360   561 KA-----KGTGLGLALSQRIINAHGGDIEVESEPGVGTTFT 596
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
538-762 4.79e-22

Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444508 [Multi-domain]  Cd Length: 412  Bit Score: 99.94  E-value: 4.79e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  538 SQFLAKMSHELRTPLNAILGFTQLMTRNRSLSPEDQENLDIISRSGEHLLALINDVLEMSKIEAGQLTLnesyFDLHRLI 617
Cdd:COG5806    202 SELAASIAHEVRNPLTVVRGFIQLLQEPELSDEKRKQYIRIALEELDRAEAIITDYLTFAKPQPEKLEK----IDVSEEL 277
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  618 YSIREMFALKAADKGLEITINLgqEVNQYVFGDEGKLRQILINLIGNAIKFTVVGHiTLRVSYLNSSstttpvDQVIIvf 697
Cdd:COG5806    278 EHVIDVLSPYANMNNVEIQTEL--EPGLYIEGDRQKLQQCLINIIKNGIEAMPNGG-TLTIDVSIDK------NKVII-- 346
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054616225  698 EVEDTGPGIPPEDMDLIFEAFIQAKGgrqfmQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:COG5806    347 SIKDTGVGMTKEQLERLGEPYFSTKE-----KGTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFT 406
PRK09303 PRK09303
histidine kinase;
535-761 8.98e-22

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 98.48  E-value: 8.98e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  535 RAKSQFLAKMSHELRTPLNA--ILGFTQLMTRNRS---LSPEDQENL-DIISRSGEHLLALINDVLEMSKIEAGQLTLNE 608
Cdd:PRK09303   149 KFKDRVLAMLAHDLRTPLTAasLALETLELGQIDEdteLKPALIEQLqDQARRQLEEIERLITDLLEVGRTRWEALRFNP 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  609 SYFDLHRLIYSIREMFALKAADKGLEITINLGQEVnQYVFGDEGKLRQILINLIGNAIKFTVV-GHITLRVSYlnssSTT 687
Cdd:PRK09303   229 QKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSDL-PSVYADQERIRQVLLNLLDNAIKYTPEgGTITLSMLH----RTT 303
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054616225  688 TPVdQVIIVfeveDTGPGIPPEDMDLIFEAFIQAKGGRQfMQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTF 761
Cdd:PRK09303   304 QKV-QVSIC----DTGPGIPEEEQERIFEDRVRLPRDEG-TEGYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCF 371
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
539-762 1.27e-21

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 99.81  E-value: 1.27e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  539 QFLAKMSHELRTPLNAILGFTQLMtrnrSLSPEDQEN-LDIISRSGEHLLALINDVLEMSKIEAGQLTlnesYFDLHRLI 617
Cdd:COG5805    289 QLAAGIAHEIRNPLTSIKGFLQLL----QPGIEDKEEyFDIMLSELDRIESIISEFLALAKPQAVNKE----KENINELI 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  618 ysiREMFALKAADKGLE-ITINL-GQEVNQYVFGDEGKLRQILINLIGNAIK-FTVVGHITLRvsylnssstTTPVDQVI 694
Cdd:COG5805    361 ---QDVVTLLETEAILHnIQIRLeLLDEDPFIYCDENQIKQVFINLIKNAIEaMPNGGTITIH---------TEEEDNSV 428
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054616225  695 IVfEVEDTGPGIPPEDMDLIFEAFIQAKggrqfMQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:COG5805    429 II-RVIDEGIGIPEERLKKLGEPFFTTK-----EKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFT 490
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
797-912 1.82e-21

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: 90.46  E-value: 1.82e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKIIALTA 876
Cdd:cd17598      1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKPFEETVLFNKMAQYL 912
Cdd:cd17598     81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYIL 116
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
795-904 2.09e-21

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: 90.42  E-value: 2.09e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  795 HRILIVEDIQENRQLMVKLLESVGFEVCA-AENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSegKDIKIIA 873
Cdd:cd17542      1 KKVLIVDDAAFMRMMLKDILTKAGYEVVGeAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKID--PNAKVIM 78
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1054616225  874 LTANAFQEDKQAVLNAGCDDFVAKPFE-ETVL 904
Cdd:cd17542     79 CSAMGQEEMVKEAIKAGAKDFIVKPFQpERVL 110
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
797-908 6.36e-21

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: 88.98  E-value: 6.36e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMseGKDIKIIALTA 876
Cdd:cd17627      1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAA--GNDLPILVLTA 78
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKPFEETVLFNKM 908
Cdd:cd17627     79 RDSVSDRVAGLDAGADDYLVKPFALEELLARV 110
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
796-899 9.06e-21

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


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 88.46  E-value: 9.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKIIALT 875
Cdd:cd17618      2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIMLT 81
                           90       100
                   ....*....|....*....|....
gi 1054616225  876 ANAFQEDKQAVLNAGCDDFVAKPF 899
Cdd:cd17618     82 ARGEEEDKVRGLEAGADDYITKPF 105
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
797-901 2.51e-20

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: 87.39  E-value: 2.51e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLL--ESVGFEVCA-AENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAmsEGKDIKIIA 873
Cdd:cd17536      1 VLIVDDEPLIREGLKKLIdwEELGFEVVGeAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRE--LYPDIKIII 78
                           90       100
                   ....*....|....*....|....*....
gi 1054616225  874 LTANA-FQEDKQAvLNAGCDDFVAKPFEE 901
Cdd:cd17536     79 LSGYDdFEYAQKA-IRLGVVDYLLKPVDE 106
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
536-772 3.00e-20

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 94.69  E-value: 3.00e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  536 AKSQFLAKMSHELRTPLNAILGFTQLMTRNRSLSPEDQENLDIISRSGEHLLALINDVLEMSKIEAG-QLTLNESyFDLh 614
Cdd:PRK11006   203 ARRNFFANVSHELRTPLTVLQGYLEMMQDQPLEGALREKALHTMREQTQRMEGLVKQLLTLSKIEAApTIDLNEK-VDV- 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  615 RLIYSIREMFALKAADKGLEITINLGQEVNqyVFGDEGKLRQILINLIGNAIKFTVVG-HITlrVSYLNSSSTTtpvdqv 693
Cdd:PRK11006   281 PMMLRVLEREAQTLSQGKHTITFEVDNSLK--VFGNEDQLRSAISNLVYNAVNHTPEGtHIT--VRWQRVPQGA------ 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  694 iiVFEVEDTGPGIPPEDMDLIFEAFIQAKGGR-QFMQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFSCQVQLTLVDK 772
Cdd:PRK11006   351 --EFSVEDNGPGIAPEHIPRLTERFYRVDKARsRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLPERLIAK 428
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
536-602 8.71e-20

His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases.


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 83.80  E-value: 8.71e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054616225  536 AKSQFLAKMSHELRTPLNAILGFTQLMtRNRSLSPEDQENLDIISRSGEHLLALINDVLEMSKIEAG 602
Cdd:pfam00512    1 AKSEFLANLSHELRTPLTAIRGYLELL-RDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
536-602 1.04e-19

His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases.


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 83.77  E-value: 1.04e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054616225   536 AKSQFLAKMSHELRTPLNAILGFTQLMtRNRSLSPEDQENLDIISRSGEHLLALINDVLEMSKIEAG 602
Cdd:smart00388    1 AKREFLANLSHELRTPLTAIRGYLELL-LDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
pleD PRK09581
response regulator PleD; Reviewed
796-905 2.43e-19

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 92.27  E-value: 2.43e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENrqlmVKLLE----SVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKI 871
Cdd:PRK09581     4 RILVVDDIPAN----VKLLEakllAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPV 79
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1054616225  872 IALTANAFQEDKQAVLNAGCDDFVAKPFEETVLF 905
Cdd:PRK09581    80 VMVTALDDPEDRVRGLEAGADDFLTKPINDVALF 113
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
798-899 2.45e-19

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: 84.63  E-value: 2.45e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  798 LIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKIIALTAN 877
Cdd:cd19937      1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAK 80
                           90       100
                   ....*....|....*....|..
gi 1054616225  878 AFQEDKQAVLNAGCDDFVAKPF 899
Cdd:cd19937     81 GEEFDKVLGLELGADDYITKPF 102
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
534-598 3.03e-19

Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes.


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 82.26  E-value: 3.03e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054616225  534 NRAKSQFLAKMSHELRTPLNAILGFTQLMTRNRSLSPEDQENLDIISRSGEHLLALINDVLEMSK 598
Cdd:cd00082      1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
PRK10604 PRK10604
sensor protein RstB; Provisional
537-763 3.37e-19

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 91.59  E-value: 3.37e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  537 KSQFLAKMSHELRTPLnAILGFTQLMTRNrsLSPEDQENLDiisRSGEHLLALINDVLEMSKIEAGQLTLNESYFDLHRL 616
Cdd:PRK10604   212 KKQLIDGIAHELRTPL-VRLRYRLEMSDN--LSAAESQALN---RDIGQLEALIEELLTYARLDRPQNELHLSEPDLPAW 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  617 IYSIREMFALKAADKGLEITINlgqEVNQYVFGDEGKLRQILINLIGNAIKFTvvgHITLRVSYLnssstttpVDQVIIV 696
Cdd:PRK10604   286 LSTHLADIQAVTPEKTVRLDTP---HQGDYGALDMRLMERVLDNLLNNALRYA---HSRVRVSLL--------LDGNQAC 351
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054616225  697 FEVEDTGPGIPPEDMDLIFEAFIQAKGGR-QFMQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFSC 763
Cdd:PRK10604   352 LIVEDDGPGIPPEERERVFEPFVRLDPSRdRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSF 419
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
794-913 4.61e-19

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: 83.75  E-value: 4.61e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  794 PHRILIVEDiQENRQLMVKL-LESV-GFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKI 871
Cdd:cd17552      1 SKRILVIDD-EEDIREVVQAcLEKLaGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPV 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1054616225  872 IALTANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKMAQYLN 913
Cdd:cd17552     80 ILLTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLLG 121
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
797-898 4.86e-19

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: 82.98  E-value: 4.86e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSegkDIKIIALTA 876
Cdd:cd17620      1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWS---AVPVIVLSA 77
                           90       100
                   ....*....|....*....|..
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKP 898
Cdd:cd17620     78 RDEESDKIAALDAGADDYLTKP 99
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
499-761 7.98e-19

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 90.62  E-value: 7.98e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  499 FDLEVAQEMRNNLM----LAALEFSHAALKFAAE---------QAEIANRAK----SQFLAKMSHELRTPLNAILGFTQL 561
Cdd:PRK10364   182 LVSAQAREQRNTLIilfaLATVLLASLLAFFWYRrylrsrqllQDEMKRKEKlvalGHLAAGVAHEIRNPLSSIKGLAKY 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  562 MTRNRSLSPEDQENLDIISRSGEHLLALINDVLEMSKieAGQLTLNESyfDLHRLIYSIREMFALKAADKG--LEITINL 639
Cdd:PRK10364   262 FAERAPAGGEAHQLAQVMAKEADRLNRVVSELLELVK--PTHLALQAV--DLNDLINHSLQLVSQDANSREiqLRFTAND 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  640 GQEVNQyvfGDEGKLRQILINLIGNAIKfTVVGHITLRVSYLNSSstttpvDQVIIVfeVEDTGPGIPPEDMDLIFEAFI 719
Cdd:PRK10364   338 TLPEIQ---ADPDRLTQVLLNLYLNAIQ-AIGQHGVISVTASESG------AGVKIS--VTDSGKGIAADQLEAIFTPYF 405
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1054616225  720 QAKGgrqfmQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTF 761
Cdd:PRK10364   406 TTKA-----EGTGLGLAVVHNIVEQHGGTIQVASQEGKGATF 442
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
797-898 8.19e-19

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: 82.43  E-value: 8.19e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKIIALTA 876
Cdd:cd19927      1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80
                           90       100
                   ....*....|....*....|..
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKP 898
Cdd:cd19927     81 KGMTSDRIKGYNAGCDGYLSKP 102
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
797-898 1.18e-18

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


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 82.43  E-value: 1.18e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPH---------LIWMDIQMPVMDGYEATKEIRAMSEGK 867
Cdd:cd19924      1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKEgndlskeldLIITDIEMPKMDGYELTFELRDDPRLA 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1054616225  868 DIKIIALTANAFQEDKQAVLNAGCDDFVAKP 898
Cdd:cd19924     81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
654-761 2.86e-18

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 AtoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli AtoS, an HK of the AtoS-AtoC TCS. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have accessory domains such as HAMP or PAS sensor domains or CBS-pair domains.


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 80.93  E-value: 2.86e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  654 LRQILINLIGNAIK-FTVVGHITLRvsylnsssTTTPVDQVIIvfEVEDTGPGIPPEDMDLIFEAFIQAKggrQFMQGTG 732
Cdd:cd16943      4 LNQVLLNLLVNAAQaMEGRGRITIR--------TWAHVDQVLI--EVEDTGSGIDPEILGRIFDPFFTTK---PVGEGTG 70
                           90       100
                   ....*....|....*....|....*....
gi 1054616225  733 LGLPISRQFAKLMGGDVTVRSFPGQGTTF 761
Cdd:cd16943     71 LGLSLSYRIIQKHGGTIRVASVPGGGTRF 99
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
796-904 2.89e-18

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


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 81.63  E-value: 2.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAmsEGKDIKIIALT 875
Cdd:cd17615      1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRA--DGPDVPVLFLT 78
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1054616225  876 ANAFQEDKQAVLNAGCDDFVAKPF--EETVL 904
Cdd:cd17615     79 AKDSVEDRIAGLTAGGDDYVTKPFslEEVVA 109
orf27 CHL00148
Ycf27; Reviewed
793-899 3.56e-18

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 85.15  E-value: 3.56e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  793 SPHRILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSegkDIKII 872
Cdd:CHL00148     5 SKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKES---DVPII 81
                           90       100
                   ....*....|....*....|....*..
gi 1054616225  873 ALTANAFQEDKQAVLNAGCDDFVAKPF 899
Cdd:CHL00148    82 MLTALGDVSDRITGLELGADDYVVKPF 108
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
540-737 4.27e-18

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 88.54  E-value: 4.27e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  540 FLAKMSHELRTPLNAILG-FTQLMTRNRSLSPEDqenldIISRSGE--HLLALINDVLEMSKIEAGQLTLNESYFDLHRL 616
Cdd:PRK10549   243 FMADISHELRTPLAVLRGeLEAIQDGVRKFTPES-----VASLQAEvgTLTKLVDDLHQLSLSDEGALAYRKTPVDLVPL 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  617 IY----SIREMFAlkaaDKGLEITINLGQEVNqyVFGDEGKLRQILINLIGNAIKFTVVG---HITLRVSYlnssstttp 689
Cdd:PRK10549   318 LEvaggAFRERFA----SRGLTLQLSLPDSAT--VFGDPDRLMQLFNNLLENSLRYTDSGgslHISAEQRD--------- 382
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1054616225  690 vDQVIIVFEveDTGPGIPPEDMDLIFEAFIQAKGGRQFMQ-GTGLGLPI 737
Cdd:PRK10549   383 -KTLRLTFA--DSAPGVSDEQLQKLFERFYRTEGSRNRASgGSGLGLAI 428
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
650-767 8.30e-18

Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas putida TodS and Thauera aromatica TutC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) such Pseudomonas putida TodS HK of the TodS-TodT two-component regulatory system (TCS) which controls the expression of a toluene degradation pathway. Thauera aromatica TutC may be part of a TCS that is involved in anaerobic toluene metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), PAS sensor domain(s) and a REC domain.


Pssm-ID: 340402 [Multi-domain]  Cd Length: 110  Bit Score: 79.84  E-value: 8.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  650 DEGKLRQILINLIGNAIKFTVVG-HITLRVSylnssSTTTPVDQVIivfeVEDTGPGIPPEDMDLIFEAFIQA--KGGRQ 726
Cdd:cd16925      1 DAEKYERVVLNLLSNAFKFTPDGgRIRCILE-----KFRLNRFLLT----VSDSGPGIPPNLREEIFERFRQGdgSSTRA 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1054616225  727 FmQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFscQVQL 767
Cdd:cd16925     72 H-GGTGLGLSIVKEFVELHGGTVTVSDAPGGGALF--QVEL 109
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
796-912 8.72e-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: 8.72e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFE-VCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKIIAL 874
Cdd:cd19923      2 KVLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLMV 81
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1054616225  875 TANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKMAQYL 912
Cdd:cd19923     82 TAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
796-904 1.01e-17

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


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 80.04  E-value: 1.01e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKIIALT 875
Cdd:cd17562      2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILMLT 81
                           90       100
                   ....*....|....*....|....*....
gi 1054616225  876 ANAFQEDKQAVLNAGCDDFVAKPFEETVL 904
Cdd:cd17562     82 TESSDEKKQEGKAAGATGWLVKPFDPEQL 110
PRK13557 PRK13557
histidine kinase; Provisional
699-913 1.58e-17

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 87.03  E-value: 1.58e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  699 VEDTGPGIPPEDMDLIFEAFIQAKG-GrqfmQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTfscqVQLTL-VDKIDVL 776
Cdd:PRK13557   329 VTDTGSGMPPEILARVMDPFFTTKEeG----KGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTT----VRLYFpASDQAEN 400
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  777 PVTQVTRRVIGLepgQSPHRILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAIN-LCVEWKPHLIWMDIQMP-VMDGY 854
Cdd:PRK13557   401 PEQEPKARAIDR---GGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEiLDSHPEVDLLFTDLIMPgGMNGV 477
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054616225  855 EATKEIRAMSegKDIKIIALTANAfqEDKQAVLNAGCDDF--VAKPFEETVLFNKMAQYLN 913
Cdd:PRK13557   478 MLAREARRRQ--PKIKVLLTTGYA--EASIERTDAGGSEFdiLNKPYRRAELARRVRMVLD 534
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
536-772 1.60e-17

phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 88.07  E-value: 1.60e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  536 AKSQFLAKMSHELRTPLNAILGFTQLMTRNRSLSPEDQENLDIISRSgEHLLALINDVLEMSKIEAGQLTLNESYFDLHR 615
Cdd:PRK10618   449 ARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQS-DVLVRLVDNIQLLNMLETQDWKPEQELFSLQD 527
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  616 LIYSI-REMF-ALKAadKGLEITINLGQEVNQYVFGDEGKLRQILINLIGNAIKFTVVGHITLRVSYLNSSStttpvDQv 693
Cdd:PRK10618   528 LIDEVlPEVLpAIKR--KGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYGKITLEVDQDESSP-----DR- 599
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054616225  694 iIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGRQFMQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFSCQVQLTLVDK 772
Cdd:PRK10618   600 -LTIRILDTGAGVSIKELDNLHFPFLNQTQGDRYGKASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLKMLAADP 677
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
797-906 3.98e-17

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: 78.32  E-value: 3.98e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESV-GFEVCA-AENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRamSEGKDIKIIAL 874
Cdd:cd17535      1 VLIVDDHPLVREGLRRLLESEpDIEVVGeAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLR--RRYPDLKVIVL 78
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1054616225  875 TANAFQEDKQAVLNAGCDDFVAKPFEETVLFN 906
Cdd:cd17535     79 TAHDDPEYVLRALKAGAAGYLLKDSSPEELIE 110
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
797-901 5.42e-17

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: 77.71  E-value: 5.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQE-NRQLMVKLlESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRamSEGKDIKIIALT 875
Cdd:cd19934      1 LLLVEDDALlAAQLKEQL-SDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWR--SEGRATPVLILT 77
                           90       100
                   ....*....|....*....|....*...
gi 1054616225  876 ANAFQEDKQAVLNAGCDDFVAKPF--EE 901
Cdd:cd19934     78 ARDSWQDKVEGLDAGADDYLTKPFhiEE 105
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
796-905 5.72e-17

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: 77.84  E-value: 5.72e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCA-AENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGkdiKIIAL 874
Cdd:cd19932      2 RVLIAEDEALIRMDLREMLEEAGYEVVGeASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENIA---PIVLL 78
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1054616225  875 TANAFQEDKQAVLNAGCDDFVAKPFEETVLF 905
Cdd:cd19932     79 TAYSQQDLVERAKEAGAMAYLVKPFSESDLI 109
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
797-899 7.30e-17

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 77.35  E-value: 7.30e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSegkDIKIIALTA 876
Cdd:cd17623      1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTS---QVPVLMLTA 77
                           90       100
                   ....*....|....*....|...
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKPF 899
Cdd:cd17623     78 RGDDIDRILGLELGADDYLPKPF 100
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
797-899 7.86e-17

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: 77.46  E-value: 7.86e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSegkDIKIIALTA 876
Cdd:cd17614      1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTS---NVPIIMLTA 77
                           90       100
                   ....*....|....*....|...
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKPF 899
Cdd:cd17614     78 KDSEVDKVLGLELGADDYVTKPF 100
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
644-759 1.10e-16

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain.


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 76.68  E-value: 1.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  644 NQYVFGDEGKLRQILINLIGNAIKFTVVG-HITLRVSYLNSSstttpvdqviiVFEVEDTGPGIPPEDMDLIFEAFIQAK 722
Cdd:cd16940      4 DIQVQGDALLLFLLLRNLVDNAVRYSPQGsRVEIKLSADDGA-----------VIRVEDNGPGIDEEELEALFERFYRSD 72
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1054616225  723 GgrQFMQGTGLGLPISRQFAKLMGGDVTVRSFPGQGT 759
Cdd:cd16940     73 G--QNYGGSGLGLSIVKRIVELHGGQIFLGNAQGGGL 107
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
798-900 1.65e-16

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: 76.49  E-value: 1.65e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  798 LIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAmsEGKDIKIIALTAN 877
Cdd:cd17625      1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLRE--EGIETPVLLLTAL 78
                           90       100
                   ....*....|....*....|...
gi 1054616225  878 AFQEDKQAVLNAGCDDFVAKPFE 900
Cdd:cd17625     79 DAVEDRVKGLDLGADDYLPKPFS 101
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
797-907 1.68e-16

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: 76.17  E-value: 1.68e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEgkdIKIIALTA 876
Cdd:cd18159      1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISN---VPIIFISS 77
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKPFEETVLFNK 907
Cdd:cd18159     78 RDDNMDQVMAINMGGDDYITKPFDLDVLLAK 108
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
796-907 4.09e-16

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: 75.34  E-value: 4.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSegKDIKIIALT 875
Cdd:cd17554      2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKK--PDLPVIICT 79
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1054616225  876 ANAFQEDKQAVLNAgcDDFVAKPFEETVLFNK 907
Cdd:cd17554     80 AYSEYKSDFSSWAA--DAYVVKSSDLTELKET 109
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
796-904 4.76e-16

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: 75.10  E-value: 4.76e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSegkDIKIIALT 875
Cdd:cd19939      1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHS---HVPILMLT 77
                           90       100
                   ....*....|....*....|....*....
gi 1054616225  876 ANAFQEDKQAVLNAGCDDFVAKPFEETVL 904
Cdd:cd19939     78 ARTEEMDRVLGLEMGADDYLCKPFSPREL 106
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
795-900 5.08e-16

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 81.82  E-value: 5.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  795 HRILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGkdIKIIAL 874
Cdd:PRK11361     5 NRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETR--TPVILM 82
                           90       100
                   ....*....|....*....|....*.
gi 1054616225  875 TANAFQEDKQAVLNAGCDDFVAKPFE 900
Cdd:PRK11361    83 TAYAEVETAVEALRCGAFDYVIKPFD 108
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
634-762 9.98e-16

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis YcbM; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis YcbM, a HK of the two-component system YcbM-YcbL. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA).


Pssm-ID: 340423 [Multi-domain]  Cd Length: 125  Bit Score: 74.47  E-value: 9.98e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  634 EITINLgQEVNQYVFGDEGKLRQILINLIGNAIKFTVVGH---ITLRVsylnssstttpvDQVIIVFEVEDTGPGIPPED 710
Cdd:cd16947      2 QVEINI-PDRPIYANANTEALQRILKNLISNAIKYGSDGKflgMTLRE------------DEKHVYIDIWDKGKGISETE 68
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1054616225  711 MDLIFEAFIQAKGGR-QFMQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:cd16947     69 KDHVFERLYTLEDSRnSAKQGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFT 121
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
654-769 1.11e-15

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhizobium meliloti FixL, and Rhodobacter capsulatus DctS; includes hybrid sensor histidine kinase similar to Pseudomonas mendocina TmoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs), such as Pseudomonas mendocina TmoS HK of the TmoS-TmoT TCS, which controls the expression of the toluene-4-monooxygenase pathway, Rhizobium meliloti FixL HK of the FixL-FixJ TCS, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to O(2) levels, and Rhodobacter capsulatus DctS of the DctS-DctR TCS, which controls synthesis of the high-affinity C4-dicarboxylate transport system. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and PAS sensor domain(s); many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 73.58  E-value: 1.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  654 LRQILINLIGNAIKFTVVGHITLRVsyLNSSSTTTPVDQVIIvfEVEDTGPGIPPEDMDLIFEAFIQAKGgrqfmQGTGL 733
Cdd:cd16920      1 IQQVLINLVRNGIEAMSEGGCERRE--LTIRTSPADDRAVTI--SVKDTGPGIAEEVAGQLFDPFYTTKS-----EGLGM 71
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1054616225  734 GLPISRQFAKLMGGDVTVRSFPGQGTTFscqvQLTL 769
Cdd:cd16920     72 GLSICRSIIEAHGGRLSVESPAGGGATF----QFTL 103
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
654-758 1.23e-15

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli EnvZ and Pseudomonas aeruginosa BfmS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli EnvZ of the EnvZ-OmpR two-component regulatory system (TCS), which functions in osmoregulation. It also contains the HATPase domain of Pseudomonas aeruginosa BfmS, the HK of the BfmSR TCS, which functions in the regulation of the rhl quorum-sensing system and bacterial virulence in P. aeruginosa. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a periplasmic domain.


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 73.25  E-value: 1.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  654 LRQILINLIGNAIKFtvvGHITLRVSylnsssttTPVDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGRQfMQGTGL 733
Cdd:cd16950      1 LKRVLSNLVDNALRY---GGGWVEVS--------SDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNARG-TSGTGL 68
                           90       100
                   ....*....|....*....|....*
gi 1054616225  734 GLPISRQFAKLMGGDVTVRSFPGQG 758
Cdd:cd16950     69 GLAIVQRISDAHGGSLTLANRAGGG 93
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
795-901 1.50e-15

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: 73.71  E-value: 1.50e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  795 HRILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLcVEWKP--HLIWMDIQMPVMDGYEATKEIRAMSEGKDIKII 872
Cdd:cd17544      1 IKVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEV-LEQHPdiKLVITDYNMPEMDGFELVREIRKKYSRDQLAII 79
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1054616225  873 ALTANafqeDKQAV----LNAGCDDFVAKPF--EE 901
Cdd:cd17544     80 GISAS----GDNALsarfIKAGANDFLTKPFlpEE 110
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
796-904 2.48e-15

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: 73.21  E-value: 2.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCA-AENGLEAINLCVEWKPHLIWMDIQMP-VMDGYEATKEIRamsEGKDIKIIA 873
Cdd:cd17534      2 KILIVEDEAIIALDLKEILESLGYEVVGiADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIR---EKFDIPVIF 78
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1054616225  874 LTANAFQEDKQAVLNAGCDDFVAKPFEETVL 904
Cdd:cd17534     79 LTAYSDEETLERAKETNPYGYLVKPFNEREL 109
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
654-761 2.56e-15

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Methanosaeta harundinacea FilI and some hybrid sensor histidine kinases; This family includes FilI, the histidine kinase (HK) component of FilI-FilRs, a two-component signal transduction system (TCS) of the methanogenic archaeon, Methanosaeta harundinacea, which is involved in regulating methanogenesis. The cytoplasmic HK core consists of a C-terminal HK-like ATPase domain (represented here) and a histidine kinase dimerization and phosphoacceptor domain (HisKA) domain, which, in FilI, are coupled to CHASE, HAMP, PAS, and GAF sensor domains. FilI-FilRs catalyzes the phosphotransfer between FilI (HK) and FilRs (FilR1 and FilR2, response regulators) of the TCS. TCSs are predicted to be of bacterial origin, and acquired by archaea by horizontal gene transfer. This model also includes related HATPase domains such as that of Synechocystis sp. PCC6803 phytochrome-like protein Cph1. Proteins having this HATPase domain and HisKA domain also have accessory sensor domains such as CHASE, GAF, HAMP and PAS; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 72.74  E-value: 2.56e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  654 LRQILINLIGNAIKFTVVG-HITLRVSYLNSSSTTTpvdqviivFEVEDTGPGIPPEDMDLIFEAFiQAKGGRQFMQGTG 732
Cdd:cd16921      1 LGQVLTNLLGNAIKFRRPRrPPRIEVGAEDVGEEWT--------FYVRDNGIGIDPEYAEKVFGIF-QRLHSREEYEGTG 71
                           90       100
                   ....*....|....*....|....*....
gi 1054616225  733 LGLPISRQFAKLMGGDVTVRSFPGQGTTF 761
Cdd:cd16921     72 VGLAIVRKIIERHGGRIWLESEPGEGTTF 100
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
796-905 2.57e-15

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 75.38  E-value: 2.57e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCA-AENGLEAINLCVEWKPHLIWMDIQMPVMDGYEAtkeIRAMSEGKDIKIIAL 874
Cdd:COG3707      5 RVLVVDDEPLRRADLREGLREAGYEVVAeAADGEDAVELVRELKPDLVIVDIDMPDRDGLEA---ARQISEERPAPVILL 81
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1054616225  875 TANAFQEDKQAVLNAGCDDFVAKPFEETVLF 905
Cdd:COG3707     82 TAYSDPELIERALEAGVSAYLVKPLDPEDLL 112
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
796-901 3.09e-15

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 78.27  E-value: 3.09e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESV-GFEVCA-AENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRA-------M--- 863
Cdd:PRK00742     5 RVLVVDDSAFMRRLISEILNSDpDIEVVGtAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRlrptpvvMvss 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1054616225  864 --SEGKDIKIIALTANAFqedkqavlnagcdDFVAKPFEE 901
Cdd:PRK00742    85 ltERGAEITLRALELGAV-------------DFVTKPFLG 111
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
796-901 3.63e-15

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: 72.62  E-value: 3.63e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAmsEGKDIKIIALT 875
Cdd:cd17555      2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITK--ESPDTPVIVVS 79
                           90       100
                   ....*....|....*....|....*.
gi 1054616225  876 ANAFQEDKQAVLNAGCDDFVAKPFEE 901
Cdd:cd17555     80 GAGVMSDAVEALRLGAWDYLTKPIED 105
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
796-900 5.05e-15

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: 72.12  E-value: 5.05e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSegkDIKIIALT 875
Cdd:cd17626      2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAES---GVPIVMLT 78
                           90       100
                   ....*....|....*....|....*
gi 1054616225  876 ANAFQEDKQAVLNAGCDDFVAKPFE 900
Cdd:cd17626     79 AKSDTVDVVLGLESGADDYVAKPFK 103
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
541-765 8.04e-15

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 77.58  E-value: 8.04e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  541 LAKMSHELRTPLNAILGFTQLMtrnrslspEDQENLDIISRSGEHLLALINDVLEMSKIEAgqltLNEsyfdlhrLIYSi 620
Cdd:COG3290    193 LRAQRHDFRNHLHTISGLLQLG--------EYDEALEYIDEISEELQELIDSLLSRIGNPV----LAA-------LLLG- 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  621 remFALKAADKGLEITINLGQEVNQYVFGDEgKLRQILINLIGNAI-----KFTVVGHITLRVSYLNSSstttpvdqviI 695
Cdd:COG3290    253 ---KAARARERGIDLTIDIDSDLPDLPLSDT-DLVTILGNLLDNAIeavekLPEEERRVELSIRDDGDE----------L 318
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  696 VFEVEDTGPGIPPEDMDLIFEAFIQAKGGrqfmQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFSCQV 765
Cdd:COG3290    319 VIEVEDSGPGIPEELLEKIFERGFSTKLG----EGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRL 384
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
654-762 8.38e-15

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli GlnL (synonyms NtrB and NRII); This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs), similar to Escherichia coli GlnL/NtrB/NRII HK of the two-component regulatory system (TCS) GlnL/GlnG (NtrB-NtrC, or NRII-NRI), which regulates the transcription of genes encoding metabolic enzymes and permeases in response to carbon and nitrogen status in E. coli and related bacteria. Also included in this family are Rhodobacter capsulatus NtrB, Azospirillum brasilense NtrB, Vibrio alginolyticus NtrB, Rhizobium leguminosarum biovar phaseoli NtrB, and Herbaspirillum seropedicae NtrB. Escherichia coli GlnL/NtrB/NRII is both a kinase and a phosphatase, catalyzing the phosphorylation and dephosphorylation of GlnG/NtrC/NRI. The kinase and phosphatase activities of GlnL/NtrB/NRII are regulated by the PII signal transduction protein, which on binding to GlnL/NtrB/NRII, inhibits the kinase activity of GlnL/NtrB/NRII and activates the GlnL/NtrB/NRII phosphatase activity. Proteins having this HATPase domain also have a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also contain PAS sensor domain(s).


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 71.28  E-value: 8.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  654 LRQILINLIGNAIKFT--VVGHITLRVSYLNSSSTTTPVDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQakgGRQfmQGT 731
Cdd:cd16918      1 LIQVFLNLVRNAAQALagSGGEIILRTRTQRQVTLGHPRHRLALRVSVIDNGPGIPPDLQDTIFYPMVS---GRE--NGT 75
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1054616225  732 GLGLPISRQFAKLMGGDVTVRSFPGQgTTFS 762
Cdd:cd16918     76 GLGLAIAQNIVSQHGGVIECDSQPGH-TVFS 105
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
796-903 9.69e-15

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: 71.68  E-value: 9.69e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGF--EVCAAENGLEAIN-LCVEWK------PHLIWMDIQMPVMDGYEATKEIRAMSEG 866
Cdd:cd17557      1 TILLVEDNPGDAELIQEAFKEAGVpnELHVVRDGEEALDfLRGEGEyadaprPDLILLDLNMPRMDGFEVLREIKADPDL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1054616225  867 KDIKIIALTANAFQEDKQAVLNAGCDDFVAKP-----FEETV 903
Cdd:cd17557     81 RRIPVVVLTTSDAEEDIERAYELGANSYIVKPvdfeeFVEAI 122
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
797-900 1.25e-14

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


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 70.98  E-value: 1.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAmsEGKDIKIIALTA 876
Cdd:cd17624      1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRR--QGQSLPVLILTA 78
                           90       100
                   ....*....|....*....|....
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKPFE 900
Cdd:cd17624     79 RDGVDDRVAGLDAGADDYLVKPFA 102
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
654-765 2.21e-14

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Brucella abortus BvrS and Sinorhizobium meliloti ChvG; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Brucella abortus BvrS of the BvrR-BvrS two-component regulatory system (TCS), which controls cell invasion and intracellular survival, as well as Sinorhizobium meliloti and Agrobacterium tumefaciens ChvG of the ChvI-ChvG TCS necessary for endosymbiosis and pathogenicity in plants. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), an accessory HAMP sensor domain, a periplasmic stimulus-sensing domain, and some also have a sensor N-terminal transmembrane domain.


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 70.29  E-value: 2.21e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  654 LRQILINLIGNAIKFT--VVGHITLRVSYLNSSstttpvdqviIVFEVEDTGPGIPPEDMDLIFEAF-IQAKGGRQFMQG 730
Cdd:cd16953      1 LGQVLRNLIGNAISFSppDTGRITVSAMPTGKM----------VTISVEDEGPGIPQEKLESIFDRFyTERPANEAFGQH 70
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1054616225  731 TGLGLPISRQFAKLMGGDVTV--RSFPGQ--GTTFSCQV 765
Cdd:cd16953     71 SGLGLSISRQIIEAHGGISVAenHNQPGQviGARFTVQL 109
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
796-915 2.93e-14

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 73.31  E-value: 2.93e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESV-GFEVCA-AENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSegKDIKIIA 873
Cdd:COG3279      3 KILIVDDEPLARERLERLLEKYpDLEVVGeASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELD--PPPPIIF 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1054616225  874 LTA------NAFQEDkqAVlnagcdDFVAKPFEETVLFNKMAQYLNLH 915
Cdd:COG3279     81 TTAydeyalEAFEVN--AV------DYLLKPIDEERLAKALEKAKERL 120
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
797-898 2.97e-14

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: 69.39  E-value: 2.97e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAmsEGKDIKIIALTA 876
Cdd:cd19935      1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRA--AGKQTPVLMLTA 78
                           90       100
                   ....*....|....*....|..
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKP 898
Cdd:cd19935     79 RDSVEDRVKGLDLGADDYLVKP 100
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
796-911 3.53e-14

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


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 69.87  E-value: 3.53e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLL-ESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRamSEGKDIKIIAL 874
Cdd:cd17593      2 KVLICDDSSMARKQLARALpADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALP--VEQLETKVIVV 79
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1054616225  875 TANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKMAQY 911
Cdd:cd17593     80 SGDVQPEAKERVLELGALAFLKKPFDPEKLAQLLEEL 116
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
650-762 4.02e-14

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds.


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 69.24  E-value: 4.02e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  650 DEGKLRQILINLIGNAIKFT-VVGHITLRVSYLNSSstttpvdqviIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGRQFM 728
Cdd:cd16948      2 DAKWLSFIIGQIVSNALKYSkQGGKIEIYSETNEQG----------VVLSIKDFGIGIPEEDLPRVFDKGFTGENGRNFQ 71
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1054616225  729 QGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:cd16948     72 ESTGMGLYLVKKLCDKLGHKIDVESEVGEGTTFT 105
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
650-749 5.14e-14

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BaeS HK of the BaeS/BaeR two-component regulatory system (TCS), which responds to envelope stress. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensory domain.


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 69.03  E-value: 5.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  650 DEGKLRQILINLIGNAIKFTVVGHiTLRVSylnssstTTPVDQVIIVFeVEDTGPGIPPEDMDLIFEAFIQAKGGRQFMQ 729
Cdd:cd16946      1 DRDRLQQLFVNLLENSLRYTDTGG-KLRIR-------AAQTPQEVRLD-VEDSAPGVSDDQLARLFERFYRVESSRNRAS 71
                           90       100
                   ....*....|....*....|.
gi 1054616225  730 -GTGLGLPISRQFAKLMGGDV 749
Cdd:cd16946     72 gGSGLGLAICHNIALAHGGTI 92
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
796-899 6.12e-14

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: 68.94  E-value: 6.12e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSegkDIKIIALT 875
Cdd:cd19938      1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFS---DVPIIMVT 77
                           90       100
                   ....*....|....*....|....
gi 1054616225  876 ANAFQEDKQAVLNAGCDDFVAKPF 899
Cdd:cd19938     78 ARVEEIDRLLGLELGADDYICKPY 101
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
796-898 6.48e-14

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: 68.96  E-value: 6.48e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINL--CVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKD-IKII 872
Cdd:cd19933      2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLlaSAEHSFQLVLLDLCMPEMDGFEVALRIRKLFGRRErPLIV 81
                           90       100
                   ....*....|....*....|....*.
gi 1054616225  873 ALTANAFQEDKQAVLNAGCDDFVAKP 898
Cdd:cd19933     82 ALTANTDDSTREKCLSLGMNGVITKP 107
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
657-762 1.41e-13

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 67.70  E-value: 1.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  657 ILINLIGNAI-----KFTVVGHITLRVSYLNSsstttpvdqvIIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGRqfmqGT 731
Cdd:cd16915      4 IVGNLIDNALdalaaTGAPNKQVEVFLRDEGD----------DLVIEVRDTGPGIAPELRDKVFERGVSTKGQG----ER 69
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1054616225  732 GLGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:cd16915     70 GIGLALVRQSVERLGGSITVESEPGGGTTFS 100
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
654-762 1.66e-13

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Salmonella typhimurium RstB; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Salmonella typhimurium RstB HK of the RstA-RstB two-component regulatory system (TCS), which regulates expression of the constituents participating in pyrimidine metabolism and iron acquisition, and may be required for regulation of Salmonella motility and invasion. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensor domain.


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 67.46  E-value: 1.66e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  654 LRQILINLIGNAIKFTvvgHITLRVSYLNSSSTTTpvdqviivFEVEDTGPGIPPEDMDLIFEAFIQAKGGRQFMQ-GTG 732
Cdd:cd16939      1 MARALDNLLRNALRYA---HRTVRIALLVSGGRLT--------LIVEDDGPGIPAAARERVFEPFVRLDPSRDRATgGFG 69
                           90       100       110
                   ....*....|....*....|....*....|
gi 1054616225  733 LGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:cd16939     70 LGLAIVHRVALWHGGHVECDDSELGGACFR 99
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
795-904 2.11e-13

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 67.40  E-value: 2.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  795 HRILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGkdiKIIAL 874
Cdd:cd17622      1 TRILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQG---PILLL 77
                           90       100       110
                   ....*....|....*....|....*....|
gi 1054616225  875 TANAFQEDKQAVLNAGCDDFVAKPFEETVL 904
Cdd:cd17622     78 TALDSDIDHILGLELGADDYVVKPVEPAVL 107
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
537-753 2.20e-13

Cu(+)/Ag(+) sensor histidine kinase;


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 73.65  E-value: 2.20e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  537 KSQFLAKMSHELRTPLNAILGFTQL-MTRNRSlspeDQENLDIISRSGEH---LLALINDVLEMSKIEAGQLTLNESYFD 612
Cdd:PRK09835   262 QSNFSADIAHEIRTPITNLITQTEIaLSQSRS----QKELEDVLYSNLEEltrMAKMVSDMLFLAQADNNQLIPEKKMLD 337
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  613 LHRLIYSIREMFALKAADKGLEITINlGQEVnqYVFGDEGKLRQILINLIGNAIKFTVVGH-ITLRVSylnsssttTPVD 691
Cdd:PRK09835   338 LADEVGKVFDFFEAWAEERGVELRFV-GDPC--QVAGDPLMLRRAISNLLSNALRYTPAGEaITVRCQ--------EVDH 406
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054616225  692 QVIIVfeVEDTGPGIPPEDMDLIFEAFIQAKGGRQFM-QGTGLGLPISRQFAKLMGGDVTVRS 753
Cdd:PRK09835   407 QVQLV--VENPGTPIAPEHLPRLFDRFYRVDPSRQRKgEGSGIGLAIVKSIVVAHKGTVAVTS 467
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
794-873 3.03e-13

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: 67.61  E-value: 3.03e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  794 PHRILIVEDIQENRQLMVKLLESV-GFEVCA-AENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEI---------RA 862
Cdd:COG2197      1 MIRVLIVDDHPLVREGLRALLEAEpDIEVVGeAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRLltprerevlRL 80
                           90
                   ....*....|.
gi 1054616225  863 MSEGKDIKIIA 873
Cdd:COG2197     81 LAEGLSNKEIA 91
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
541-737 3.32e-13

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 73.04  E-value: 3.32e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  541 LAKMSHELRTPLNAILGFTQLMTRNRSLSPEdqenLDIISRSGEHLLALINDVLEMSKIEAGQlTLNESYFDLHRLIYSI 620
Cdd:PRK09470   247 LSDISHELRTPLTRLQLATALLRRRQGESKE----LERIETEAQRLDSMINDLLVLSRNQQKN-HLERETFKANSLWSEV 321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  621 RE--MFALKAADKGLEITINLGqevNQYVFGDEGKLRQILINLIGNAIKFtvvGHITLRVSYlnssstTTPVDQVIIVfe 698
Cdd:PRK09470   322 LEdaKFEAEQMGKSLTVSAPPG---PWPINGNPNALASALENIVRNALRY---SHTKIEVAF------SVDKDGLTIT-- 387
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1054616225  699 VEDTGPGIPPEDMDLIFEAFIQAKGGR-QFMQGTGLGLPI 737
Cdd:PRK09470   388 VDDDGPGVPEEEREQIFRPFYRVDEARdRESGGTGLGLAI 427
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
796-908 4.28e-13

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 69.75  E-value: 4.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKIIALT 875
Cdd:PRK10161     4 RILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLT 83
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1054616225  876 ANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKM 908
Cdd:PRK10161    84 ARGEEEDRVRGLETGADDYITKPFSPKELVARI 116
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
654-763 4.38e-13

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoR; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli or Vibrio cholera PhoR, the histidine kinase (HK) of PhoB-PhoR a two-component signal transduction system (TCS) involved in phosphate regulation. PhoR monitors extracellular inorganic phosphate (Pi) availability and PhoB, the response regulator, regulates transcription of genes of the phosphate regulon. PhoR is a bifunctional histidine autokinase/phospho-PhoB phosphatase; in phosphate deficiency, it autophosphorylates and Pi is transferred to PhoB, and when environmental Pi is abundant, it removes the phosphoryl group from phosphorylated PhoB. Other roles of PhoB-PhoR TCS have been described, including motility, biofilm formation, intestinal colonization, and virulence in V. cholera. E.coli PhoR and Bacillus subtilis PhoR (whose HATPase domain belongs to a different family) sense very different signals in each bacterium. In E. coli the PhoR signal comes from phosphate transport mediated by the PstSCAB2 phosphate transporter and the PhoU chaperone-like protein while in B. subtilis, the PhoR activation signal comes from wall teichoic acid (WTA) metabolism.


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 66.46  E-value: 4.38e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  654 LRQILINLIGNAIKFTV-VGHITLRVSYLNSSSTttpvdqviivFEVEDTGPGIPPEDMDLIFEAF--IQAKGGRQfMQG 730
Cdd:cd16952      1 LRSAFSNLVSNAVKYTPpSDTITVRWSQEESGAR----------LSVEDTGPGIPPEHIPRLTERFyrVDIERCRN-TGG 69
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1054616225  731 TGLGLPISRQFAKLMGGDVTVRSFPGQGTTFSC 763
Cdd:cd16952     70 TGLGLAIVKHVMSRHDARLLIASELGKGSRFTC 102
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
654-761 5.24e-13

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CreC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli CreC of the CreC-CreB two-component regulatory system (TCS) involved in catabolic regulation. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and accessory sensory domain(s) such as HAMP, CACHE or PAS.


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 65.94  E-value: 5.24e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  654 LRQILINLIGNAIKFTVV-GHITLRvsylnsssttTPVDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGRQFMQGTG 732
Cdd:cd16945      5 LRQAINNLLDNAIDFSPEgGLIALQ----------LEADTEGIELLVFDEGSGIPDYALNRVFERFYSLPRPHSGQKSTG 74
                           90       100
                   ....*....|....*....|....*....
gi 1054616225  733 LGLPISRQFAKLMGGDVTVRSFPGQGTTF 761
Cdd:cd16945     75 LGLAFVQEVAQLHGGRITLRNRPDGVLAF 103
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
796-849 7.92e-13

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: 63.74  E-value: 7.92e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1054616225   796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMP 849
Cdd:smart00448    2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
ompR PRK09468
osmolarity response regulator; Provisional
791-899 8.74e-13

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 69.23  E-value: 8.74e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  791 GQSPHRILIVEDIQENRQLMVKLLESVGFEVCAAENGlEAINLCVEWKP-HLIWMDIQMPVMDGYEATKEIRAmsEGKDI 869
Cdd:PRK09468     2 MQENYKILVVDDDMRLRALLERYLTEQGFQVRSAANA-EQMDRLLTRESfHLMVLDLMLPGEDGLSICRRLRS--QNNPT 78
                           90       100       110
                   ....*....|....*....|....*....|
gi 1054616225  870 KIIALTANAFQEDKQAVLNAGCDDFVAKPF 899
Cdd:PRK09468    79 PIIMLTAKGEEVDRIVGLEIGADDYLPKPF 108
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
797-899 1.02e-12

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 68.68  E-value: 1.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEgkdIKIIALTA 876
Cdd:PRK10529     4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQWSA---IPVIVLSA 80
                           90       100
                   ....*....|....*....|...
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKPF 899
Cdd:PRK10529    81 RSEESDKIAALDAGADDYLSKPF 103
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
795-900 1.86e-12

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: 64.72  E-value: 1.86e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  795 HRILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEgkdIKIIAL 874
Cdd:cd17619      1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSE---VGIILV 77
                           90       100
                   ....*....|....*....|....*.
gi 1054616225  875 TANAFQEDKQAVLNAGCDDFVAKPFE 900
Cdd:cd17619     78 TGRDDEVDRIVGLEIGADDYVTKPFN 103
PRK10610 PRK10610
chemotaxis protein CheY;
796-910 2.77e-12

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 65.00  E-value: 2.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFE-VCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKIIAL 874
Cdd:PRK10610     7 KFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMV 86
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1054616225  875 TANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKMAQ 910
Cdd:PRK10610    87 TAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNK 122
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
795-904 3.85e-12

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 67.14  E-value: 3.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  795 HRILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLcVEWKPHLIWMDIQMPVMDGYEATKEIRamsEGKDIKIIAL 874
Cdd:PRK10955     2 NKILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDL-LDDSIDLLLLDVMMPKKNGIDTLKELR---QTHQTPVIML 77
                           90       100       110
                   ....*....|....*....|....*....|
gi 1054616225  875 TANAFQEDKQAVLNAGCDDFVAKPFEETVL 904
Cdd:PRK10955    78 TARGSELDRVLGLELGADDYLPKPFNDREL 107
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
796-899 4.30e-12

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: 63.40  E-value: 4.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDiqeNRQlMVKLLESV-----GFEVCA-AENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDI 869
Cdd:cd17561      3 KVLIADD---NRE-FVQLLEEYlnsqpDMEVVGvAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRP 78
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1054616225  870 KIIALTANAfQED-KQAVLNAGCDDFVAKPF 899
Cdd:cd17561     79 KIIMLTAFG-QEDiTQRAVELGASYYILKPF 108
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
796-898 4.83e-12

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 68.37  E-value: 4.83e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESV-GFEVC-AAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKIIA 873
Cdd:PRK12555     2 RIGIVNDSPLAVEALRRALARDpDHEVVwVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAERPCPILIVTS 81
                           90       100
                   ....*....|....*....|....*
gi 1054616225  874 LTANAFQEDKQAvLNAGCDDFVAKP 898
Cdd:PRK12555    82 LTERNASRVFEA-MGAGALDAVDTP 105
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
646-762 7.59e-12

Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related domains; This family includes the histidine kinase-like ATPase domains (HATPase) of three out of the five receptors that recognize the plant hormone ethylene in Arabidopsis thaliana. These three proteins have been classified as belonging to subfamily 2: ETR2, ERS2, and EIN4. They lack most of the motifs characteristic of histidine kinases, and EIN4 is the only one in this group containing the conserved histidine that is phosphorylated in two-component and phosphorelay systems. This family also includes the HATPase domains of Escherichia coli RcsD phosphotransferase which is a component of the Rcs-signaling system, a complex multistep phosphorelay involving five proteins, and is involved in many transcriptional networks such as cell division, biofilm formation, and virulence, among others. Also included is Schizosaccharomyces pombe Mak3 (Phk1) which participates in a multi-step two-component related system which regulates H2O2-induced activation of the Sty1 stress-activated protein kinase pathway. Most proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a GAF sensor domain; most are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340415 [Multi-domain]  Cd Length: 133  Bit Score: 63.63  E-value: 7.59e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  646 YVFGDEGKLRQILINLIGNAIKFTV-VGHITLRVSYLNSSSTTTPV-----------DQVIIVFEVEDTGPGIPPEDMDL 713
Cdd:cd16938      4 VVVGDERRVFQVLLHMLGNLLKMRNgGGNITFRVFLEGGSEDRSDRdwgpwrpsmsdESVEIRFEVEINDSGSPSIESAS 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1054616225  714 IFEafIQAKGGRQFMQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:cd16938     84 MRN--SLNRRYNLSELGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMS 130
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
695-762 7.67e-12

Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar to Brucella abortus 2308 CckA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) similar to Brucella abortus 2308 CckA, which is a component of an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival; phosphoryl transfer initiates from the sensor kinase CckA and proceeds via the ChpT phosphotransferase to two regulatory substrates: the DNA-binding response regulator CtrA and the phospho-receiver protein CpdR. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), a REC signal receiver domain, and some contain PAS or PAS and GAF sensor domain(s).


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 63.17  E-value: 7.67e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054616225  695 IVFEVEDTGPGIPPEDMDLIFEAFIQAKG-GRqfmqGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:cd16919     48 VCLEVSDTGSGMPAEVLRRAFEPFFTTKEvGK----GTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVR 112
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
796-899 8.35e-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: 64.94  E-value: 8.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEgkDIKIIALT 875
Cdd:COG4567      6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDP--DARIVVLT 83
                           90       100
                   ....*....|....*....|....*....
gi 1054616225  876 -----ANAFqedkQAVlNAGCDDFVAKPF 899
Cdd:COG4567     84 gyasiATAV----EAI-KLGADDYLAKPA 107
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
788-899 1.11e-11

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 65.86  E-value: 1.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  788 LEPGQSPHRILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSegk 867
Cdd:PRK10710     4 LPIDENTPRILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRFS--- 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1054616225  868 DIKIIALTANAFQEDKQAVLNAGCDDFVAKPF 899
Cdd:PRK10710    81 DIPIVMVTAKIEEIDRLLGLEIGADDYICKPY 112
PRK15479 PRK15479
transcriptional regulator TctD;
796-900 1.56e-11

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 65.13  E-value: 1.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRamSEGKDIKIIALT 875
Cdd:PRK15479     2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLR--KRGQTLPVLLLT 79
                           90       100
                   ....*....|....*....|....*
gi 1054616225  876 ANAFQEDKQAVLNAGCDDFVAKPFE 900
Cdd:PRK15479    80 ARSAVADRVKGLNVGADDYLPKPFE 104
envZ PRK09467
osmolarity sensor protein; Provisional
541-771 1.59e-11

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 67.63  E-value: 1.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  541 LAKMSHELRTPLNAILGFTQLMtrnrslSPEDQENLDIIsrsgehllalINDVLEMSKIeAGQL-----TLNESYF---D 612
Cdd:PRK09467   233 MAGVSHDLRTPLTRIRLATEMM------SEEDGYLAESI----------NKDIEECNAI-IEQFidylrTGQEMPMemaD 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  613 LHRLIYSIremfALKAADKGLEITINLGQEVNQyVFGDEGKLRQILINLIGNAIKFtvvGHITLRVSylnsssttTPVDQ 692
Cdd:PRK09467   296 LNALLGEV----IAAESGYEREIETALQPGPIE-VPMNPIAIKRALANLVVNAARY---GNGWIKVS--------SGTEG 359
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  693 VIIVFEVEDTGPGIPPEDMDLIFEAFIQ---AKGGrqfmQGTGLGLPISRQFAKLMGGDVTVRSFPGQGttFSCQVQLTL 769
Cdd:PRK09467   360 KRAWFQVEDDGPGIPPEQLKHLFQPFTRgdsARGS----SGTGLGLAIVKRIVDQHNGKVELGNSEEGG--LSARAWLPL 433

                   ..
gi 1054616225  770 VD 771
Cdd:PRK09467   434 TT 435
PRK11517 PRK11517
DNA-binding response regulator HprR;
796-915 1.66e-11

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 64.92  E-value: 1.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEAtkeIRAMSEGKDIKIIALT 875
Cdd:PRK11517     2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQI---LQTLRTAKQTPVICLT 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1054616225  876 ANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKMAQYLNLH 915
Cdd:PRK11517    79 ARDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQLRQH 118
PRK11173 PRK11173
two-component response regulator; Provisional
792-899 2.72e-11

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 64.65  E-value: 2.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  792 QSPHrILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRamsEGKDIKI 871
Cdd:PRK11173     2 QTPH-ILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELR---EQANVAL 77
                           90       100
                   ....*....|....*....|....*...
gi 1054616225  872 IALTANAFQEDKQAVLNAGCDDFVAKPF 899
Cdd:PRK11173    78 MFLTGRDNEVDKILGLEIGADDYITKPF 105
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
156-327 2.80e-11

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 62.40  E-value: 2.80e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225   156 NLSELYQNLATSVRKVTQFDRIMIYKFETDNSGVIVAEDKQNHLETYLGLHYPATDIprIARQLYYEKWLRLIPDVNYQP 235
Cdd:smart00065    1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELVLVAADGLTLPTLGIRFPLDEG--LAGRVAETGRPLNIPDVEADP 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225   236 VKLIPtnnpitdtpldlsgaflrsvsplhiEYLQHMGVAASMSISLINQNRLWGLIACHH-YTPKKLDYE----IRKICE 310
Cdd:smart00065   79 LFAED-------------------------LLGRYQGVRSFLAVPLVADGELVGVLALHNkKSPRPFTEEdeelLQALAN 133
                           170
                    ....*....|....*..
gi 1054616225   311 FIGkfASIELVKQQEKH 327
Cdd:smart00065  134 QLA--IALANAQLYEEL 148
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
156-320 3.10e-11

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 61.73  E-value: 3.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  156 NLSELYQNLATSVRKVTQFDRIMIYKFEtdnsgvivaedkqnhletYLGLHYpatdIPRIARQLYyekwLRLIPDVNYQP 235
Cdd:pfam01590    1 DLEEILQTILEELRELLGADRCALYLPD------------------ADGLEY----LPPGARWLK----AAGLEIPPGTG 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  236 VKLIPTNNPITDTPLDLSGAFLRsvsplHIEYLQHMGVAASMSISLINQNRLWGLIACHHYTPKKLDYEIRKIcEFIGKF 315
Cdd:pfam01590   55 VTVLRTGRPLVVPDAAGDPRFLD-----PLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHPRPPFTEEELELL-EVLADQ 128

                   ....*
gi 1054616225  316 ASIEL 320
Cdd:pfam01590  129 VAIAL 133
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
797-899 3.23e-11

phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is part of the VirA/VirG two-component system that regulates the expression of virulence (vir) genes. The histidine kinase VirA senses a phenolic wound response signal, undergoes autophosphorylation, and phosphorelays to the VirG response regulator, which induces transcription of the vir regulon. VirG belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 61.31  E-value: 3.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSegkDIKIIALTA 876
Cdd:cd17594      2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARS---DVPIIIISG 78
                           90       100
                   ....*....|....*....|....
gi 1054616225  877 NAFQE-DKQAVLNAGCDDFVAKPF 899
Cdd:cd17594     79 DRRDEiDRVVGLELGADDYLAKPF 102
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
797-901 3.98e-11

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 61.01  E-value: 3.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVG-FEVCA-AENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSegKDIKIIAL 874
Cdd:cd17532      1 ALIVDDEPLAREELRYLLEEHPdIEIVGeAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLA--KPPLIVFV 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1054616225  875 TA------NAFQEDkqAVlnagcdDFVAKPFEE 901
Cdd:cd17532     79 TAydeyavEAFELN--AV------DYLLKPFSE 103
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
796-899 4.96e-11

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: 60.21  E-value: 4.96e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKP-HLIWMDIQMPVMDGYEATKEIRAMSegKDIKIIAL 874
Cdd:cd18160      1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELAREARKID--PDVKILFI 78
                           90       100
                   ....*....|....*....|....*...
gi 1054616225  875 T---ANAFQEDKQAVLNAGcddFVAKPF 899
Cdd:cd18160     79 SggaAAAPELLSDAVGDNA---TLKKPF 103
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
797-900 6.71e-11

phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins; NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 60.20  E-value: 6.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMseGKDIKIIALTA 876
Cdd:cd17550      1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEK--YPDLPVIMISG 78
                           90       100
                   ....*....|....*....|....*.
gi 1054616225  877 NAFQEDkqAV--LNAGCDDFVAKPFE 900
Cdd:cd17550     79 HGTIET--AVkaTKLGAYDFIEKPLS 102
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
797-898 6.86e-11

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 59.90  E-value: 6.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSegkDIKIIALTA 876
Cdd:cd17621      1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARS---NVPVIMVTA 77
                           90       100
                   ....*....|....*....|..
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKP 898
Cdd:cd17621     78 KDSEIDKVVGLELGADDYVTKP 99
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
794-910 9.86e-11

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 62.74  E-value: 9.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  794 PHRILIVEDIQENRQLMVKLLESV-GFEVCA-AENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAmsEGKDIKI 871
Cdd:PRK10651     6 PATILLIDDHPMLRTGVKQLISMApDITVVGeASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLRE--KSLSGRI 83
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1054616225  872 IALTANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKMAQ 910
Cdd:PRK10651    84 VVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQ 122
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
796-913 1.47e-10

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 59.49  E-value: 1.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEgkDIKIIALT 875
Cdd:cd17553      2 KILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDE--NIRVIIMT 79
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1054616225  876 ANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKMAQYLN 913
Cdd:cd17553     80 AYGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYLP 117
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
797-897 2.34e-10

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: 58.82  E-value: 2.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLL--ESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAmsEGKDIKIIAL 874
Cdd:cd19930      1 VLIAEDQEMVRGALAALLelEDDLEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELRE--ELPDTKVLIV 78
                           90       100
                   ....*....|....*....|...
gi 1054616225  875 TANAFQEDKQAVLNAGCDDFVAK 897
Cdd:cd19930     79 TTFGRPGYFRRALAAGVDGYVLK 101
PRK10766 PRK10766
two-component system response regulator TorR;
794-900 2.45e-10

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 61.59  E-value: 2.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  794 PHRILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSegkDIKIIA 873
Cdd:PRK10766     2 SYHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRS---TVGIIL 78
                           90       100
                   ....*....|....*....|....*..
gi 1054616225  874 LTANAFQEDKQAVLNAGCDDFVAKPFE 900
Cdd:PRK10766    79 VTGRTDSIDRIVGLEMGADDYVTKPLE 105
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
797-898 2.79e-10

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: 58.23  E-value: 2.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSegkDIKIIALTA 876
Cdd:cd19936      1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKS---TLPVIFLTS 77
                           90       100
                   ....*....|....*....|..
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKP 898
Cdd:cd19936     78 KDDEIDEVFGLRMGADDYITKP 99
PRK10816 PRK10816
two-component system response regulator PhoP;
796-903 3.96e-10

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 60.91  E-value: 3.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQ-LMVKLLEsVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRamSEGKDIKIIAL 874
Cdd:PRK10816     2 RVLVVEDNALLRHhLKVQLQD-AGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWR--SNDVSLPILVL 78
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1054616225  875 TANAFQEDKQAVLNAGCDDFVAKPF--EETV 903
Cdd:PRK10816    79 TARESWQDKVEVLSAGADDYVTKPFhiEEVM 109
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
526-753 4.74e-10

Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 63.55  E-value: 4.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  526 AAEQAEIANRAK----SQFLAKMSHELRTPLNAILgfTQLMTRNRSLSpedQENLDIISRSGEHLLALINdvlEMSKIEA 601
Cdd:COG4192    418 RQTQDELIQAAKmavvGQTMTSLAHELNQPLNAMS--MYLFSAKKALE---QENYAQLPTSLDKIEGLIE---RMDKIIK 489
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  602 G--QLT--LNESY--FDLHRLIYSIREMFALKAadKGLEITINLGQEVNqyVFGDEGKLRQILINLIGNAIKftvvghit 675
Cdd:COG4192    490 SlrQFSrkSDTPLqpVDLRQVIEQAWELVESRA--KPQQITLHIPDDLM--VQGDQVLLEQVLVNLLVNALD-------- 557
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  676 lrvsylnsSSTTTPVDQVIIVFE-------VEDTGPGIPpeDMDLIFEAFIQAKGgrqfmQGTGLGLPISRQFAKLMGGD 748
Cdd:COG4192    558 --------AVATQPQISVDLLSNaenlrvaISDNGNGWP--LVDKLFTPFTTTKE-----VGLGLGLSICRSIMQQFGGD 622

                   ....*
gi 1054616225  749 VTVRS 753
Cdd:COG4192    623 LYLAS 627
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
796-899 5.04e-10

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 60.71  E-value: 5.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRamSEGKDIKIIALT 875
Cdd:PRK09836     2 KLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLR--SANKGMPILLLT 79
                           90       100
                   ....*....|....*....|....
gi 1054616225  876 ANAFQEDKQAVLNAGCDDFVAKPF 899
Cdd:PRK09836    80 ALGTIEHRVKGLELGADDYLVKPF 103
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
545-765 5.75e-10

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 63.01  E-value: 5.75e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  545 SHELRTPLNAILGFTQLMtrnrslSPEDQEN--LDIISRSGEHLLALINDVleMSKIEAGQLTLNESYfdlhrliysire 622
Cdd:PRK11086   347 SHEFMNKLHVILGLLHLK------SYDQLEDyiLKTANNYQEEIGSLLGKI--KSPVIAGFLLGKISR------------ 406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  623 mfalkAADKGLEITINLGQEVNQYvfGDEG---KLRQILINLIGN---AIKFTVVGHITLRVSYLNssstttpvDQVIIv 696
Cdd:PRK11086   407 -----ARELGITLIISEDSQLPDS--GDEDqvhELITILGNLIENaleAVGGEEGGEISVSLHYRN--------GWLHC- 470
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054616225  697 fEVEDTGPGIPPEDMDLIFEAFIQAKGgrqfmQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFSCQV 765
Cdd:PRK11086   471 -EVSDDGPGIAPDEIDAIFDKGYSTKG-----SNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQI 533
AdeR_RR NF012227
efflux system response regulator transcription factor AdeR; This protein, the DNA-binding ...
797-899 6.26e-10

efflux system response regulator transcription factor AdeR; This protein, the DNA-binding regulator AdeR, works with its two-component system partner AdeS, to modulate expression of the AdeABC efflux pump.


Pssm-ID: 411091 [Multi-domain]  Cd Length: 239  Bit Score: 60.53  E-value: 6.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRamsEGKDIKIIALTA 876
Cdd:NF012227    14 ILVVEDEYDIGDIIEHYLKREGMRVIRAMNGKQAIEIHASQPIDLILLDIKLPELNGWEVLSKIR---QKAQTPVIMLTA 90
                           90       100
                   ....*....|....*....|...
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKPF 899
Cdd:NF012227    91 LDQDIDKVMALRIGADDFVVKPF 113
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
651-760 1.09e-09

Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain alpha-ketoacid dehydrogenase kinase and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of all four PDK isoforms (pyruvate dehydrogenase kinases 1-4) that have been described in mammals, and other PDKs including Saccharomyces Pkp1p and Pkp2p. PDKs and phosphatases tightly regulate the mitochondrial pyruvate dehydrogenase complex (PDC) by reversible phosphorylation. PDC catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA, connecting glycolysis and the TCA acid cycle. Also included in this family is mammalian branched-chain alpha-ketoacid dehydrogenase kinase (BDK), a mitochondrial protein kinase that phosphorylates a subunit of the branched-chain a-ketoacid dehydrogenase (BCKD) complex, which catalyzes the oxidative decarboxylation of branched-chain alpha-ketoacids derived from leucine, isoleucine, and valine, a rate-limiting step in the oxidative degradation of these branched-chain amino acids.


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 58.51  E-value: 1.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  651 EGKLRQILINLIGNAIKFTVVGHITlrvsylnSSSTTTPV------DQVIIVFEVEDTGPGIPPEDMDLIF--------- 715
Cdd:cd16929     41 PSHLYYILFELLKNAMRATVESHGD-------DSDDLPPIkvtvakGDEDLTIKISDRGGGIPREDLARLFsymystapq 113
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1054616225  716 -----EAFIQAKGGRQFMQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTT 760
Cdd:cd16929    114 pslddFSDLISGTQPSPLAGFGYGLPMSRLYAEYFGGDLDLQSMEGYGTD 163
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
797-910 1.17e-09

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 56.83  E-value: 1.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENG---LEAINLCVewkPHLIWMDIQMPVMDGYEATKEIRAMseGKDIKIIA 873
Cdd:cd17537      3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSAsafLAAAPPDQ---PGCLVLDVRMPGMSGLELQDELLAR--GSNIPIIF 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1054616225  874 LTANAfqeD-KQAV--LNAGCDDFVAKPFEETVLFNKMAQ 910
Cdd:cd17537     78 ITGHG---DvPMAVeaMKAGAVDFLEKPFRDQVLLDAIEQ 114
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
654-762 1.43e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain.


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 56.31  E-value: 1.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  654 LRQILINLIGNAI----KFTVvGHITLRVSYLNssstttpvDQVIIVfeVEDTGPGIPPEDMDLIFEAFIQAKG-GRqfm 728
Cdd:cd16976      1 IQQVLMNLLQNALdamgKVEN-PRIRIAARRLG--------GRLVLV--VRDNGPGIAEEHLSRVFDPFFTTKPvGK--- 66
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1054616225  729 qGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:cd16976     67 -GTGLGLSISYGIVEEHGGRLSVANEEGAGARFT 99
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
808-898 1.73e-09

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: 55.84  E-value: 1.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  808 QLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKIIALTANAFQEDKQAVL 887
Cdd:cd17602     12 KMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTGKDGLVDRIRAK 91
                           90
                   ....*....|.
gi 1054616225  888 NAGCDDFVAKP 898
Cdd:cd17602     92 MAGASGYLTKP 102
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
792-899 2.95e-09

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 58.43  E-value: 2.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  792 QSPHrILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEgkDIKI 871
Cdd:PRK11083     2 QQPT-ILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHP--ALPV 78
                           90       100
                   ....*....|....*....|....*...
gi 1054616225  872 IALTANAFQEDKQAVLNAGCDDFVAKPF 899
Cdd:PRK11083    79 IFLTARSDEVDRLVGLEIGADDYVAKPF 106
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
796-911 3.17e-09

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 55.71  E-value: 3.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESV-GFEVCA-AENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAmsEGKDIKIIA 873
Cdd:cd19925      2 NVLIVEDDPMVAEIHRAYVEQVpGFTVIGtAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRA--AGHDVDVIV 79
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1054616225  874 LTANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKMAQY 911
Cdd:cd19925     80 VTAANDVETVREALRLGVVDYLIKPFTFERLRQRLERY 117
glnL PRK11073
nitrogen regulation protein NR(II);
501-762 3.27e-09

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 59.71  E-value: 3.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  501 LEV-AQEMRNNLMLAALEFSHAALKFAAEQAEIANRAKSQFLAK-MSHELRTPLNAILGFTQLMTRnrSL-SPEDQENLD 577
Cdd:PRK11073    92 LSLtAQRLPEGMILLEMAPMDNQRRLSQEQLQHAQQVAARDLVRgLAHEIKNPLGGLRGAAQLLSK--ALpDPALTEYTK 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  578 IISRSGEHLLALINDVLEMSKieAGQLTLNesyfDLHRLIYSIREMFALKAADKgleITInlgqeVNQY------VFGDE 651
Cdd:PRK11073   170 VIIEQADRLRNLVDRLLGPQR--PGTHVTE----SIHKVAERVVQLVSLELPDN---VRL-----IRDYdpslpeLAHDP 235
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  652 GKLRQILINLIGNAIKFTVVGH--ITLRvsylnssstTTPVDQVII---------VFEVEDTGPGIPPEDMDLIFEAFIQ 720
Cdd:PRK11073   236 DQIEQVLLNIVRNALQALGPEGgtITLR---------TRTAFQLTLhgeryrlaaRIDIEDNGPGIPPHLQDTLFYPMVS 306
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1054616225  721 AKGGrqfmqGTGLGLPISRQFAKLMGGDVTVRSFPGQgTTFS 762
Cdd:PRK11073   307 GREG-----GTGLGLSIARNLIDQHSGKIEFTSWPGH-TEFS 342
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
540-761 3.43e-09

proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is paired with an adjacent response regulator (TIGR03787) gene. It co-occurs with a variant sortase enzyme (TIGR03784), usually in the same gene neighborhood, in proteobacterial species most of which are marine, and with an LPXTG motif-containing sortase target conserved protein (TIGR03788). Sortases and LPXTG proteins are far more common in Gram-positive bacteria, where sortase systems mediate attachment to the cell wall or cross-linking of pilin structures. We give this predicted sensor histidine kinase the gene symbol psdS, for Proteobacterial Dedicated Sortase system Sensor histidine kinase.


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 60.91  E-value: 3.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  540 FLAKMSHELRTPLnAILGFTQLMTRNRSLSPEDQENLDIISRSGEHLLALINDVLEMSKIEAGQLTLNESYFDLHRLIYS 619
Cdd:TIGR03785  488 MSSRLSHELRTPV-AVVRSSLENLELQALEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLSEVLSG 566
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  620 IreMFALKAADKGLEITINLGQEvNQYVFGDEGKLRQILINLIGNAIKFTVV-GHITLRVSYLNSSstttpvdqviIVFE 698
Cdd:TIGR03785  567 C--MQGYQMTYPPQRFELNIPET-PLVMRGSPELIAQMLDKLVDNAREFSPEdGLIEVGLSQNKSH----------ALLT 633
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054616225  699 VEDTGPGIPPEDMDLIFEAFIQAKG-GRQFMQGTGLGLPISRQFAKLMGGDVTVRSFP-GQGTTF 761
Cdd:TIGR03785  634 VSNEGPPLPEDMGEQLFDSMVSVRDqGAQDQPHLGLGLYIVRLIADFHQGRIQAENRQqNDGVVF 698
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
650-758 4.48e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Azorhizobium caulinodans NtrY; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Azorhizobium caulinodans ORS571 NtrY of the NtrY-NtrX TCS, which is involved in nitrogen fixation and metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also have PAS sensor domains.


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 54.85  E-value: 4.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  650 DEGKLRQILINLIGNAI-----KFTVVGHITLRVSylnssstttpVDQVI-IVFEVEDTGPGIPPEDMDLIFEAFIQAKG 723
Cdd:cd16944      1 DTTQISQVLTNILKNAAeaiegRPSDVGEVRIRVE----------ADQDGrIVLIVCDNGKGFPREMRHRATEPYVTTRP 70
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1054616225  724 grqfmQGTGLGLPISRQFAKLMGGDVTVRSFPGQG 758
Cdd:cd16944     71 -----KGTGLGLAIVKKIMEEHGGRISLSNREAGG 100
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
795-904 4.60e-09

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: 55.10  E-value: 4.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  795 HRILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSegKDIKIIAL 874
Cdd:cd17569      1 PTILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERY--PDTVRILL 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1054616225  875 TANAfqeDKQAVLNA----GCDDFVAKPFEETVL 904
Cdd:cd17569     79 TGYA---DLDAAIEAinegEIYRFLTKPWDDEEL 109
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
797-900 4.81e-09

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: 55.28  E-value: 4.81e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRamSEGKDIKIIALTA 876
Cdd:cd17572      1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQ--ERSLPTSVIVITA 78
                           90       100
                   ....*....|....*....|....
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKPFE 900
Cdd:cd17572     79 HGSVDIAVEAMRLGAYDFLEKPFD 102
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
797-904 6.74e-09

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


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 55.19  E-value: 6.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMseGKDIKIIALTA 876
Cdd:cd17549      1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIREL--DPDLPVILITG 78
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1054616225  877 NAfqeD-KQAV--LNAGCDDFVAKPFEETVL 904
Cdd:cd17549     79 HG---DvPMAVeaMRAGAYDFLEKPFDPERL 106
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
629-762 7.12e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG. PhoQ is the histidine kinase (HK) of the PhoP-PhoQ two-component regulatory system (TCS), which responds to the levels of Mg2+ and Ca2+, controls virulence, mediates the adaptation to Mg2+-limiting environments, and regulates numerous cellular activities. Providencia stuartii AarG is a putative sensor kinase which controls the expression of the 2'-N-acetyltransferase and an intrinsic multiple antibiotic resistance (Mar) response in Providencia stuartii. The AarG product is similar to PhoQ in that it is able to restore wild-type levels of resistance to a Salmonella typhimurium phoQ mutant. However, the expression of the 2'-N-acetyltransferase gene and of aarP (a gene encoding a transcriptional activator of 2'-N-acetyltransferase) are not significantly affected by the levels of Mg2+ or Ca2+. Most proteins in this group contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory HAMP sensor domain, and some have an intracellular membrane -interaction PhoQ sensor domain.


Pssm-ID: 340430 [Multi-domain]  Cd Length: 135  Bit Score: 55.33  E-value: 7.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  629 ADKGLEITINLGQEVNqyVFGDEGKLRQILINLIGNAIKFTVvGHITLRVSYlnsssttTPVDQVIIVfevEDTGPGIPP 708
Cdd:cd16954     15 QRKGVSISLDISPELR--FPGERNDLMELLGNLLDNACKWCL-EFVEVTARQ-------TDGGLHLIV---DDDGPGVPE 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1054616225  709 EDMDLIFEafiqaKGGR--QFMQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFS 762
Cdd:cd16954     82 SQRSKIFQ-----RGQRldEQRPGQGLGLAIAKEIVEQYGGELSLSDSPLGGARFE 132
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
647-758 1.06e-08

nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 58.76  E-value: 1.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  647 VFGDEGKLRQILINLIGNAIKFTVVGHITLRvsylnSSSTTTPVDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGRQ 726
Cdd:TIGR02938  381 ILGRELQLRSLFKALVDNAIEAMNIKGWKRR-----ELSITTALNGDLIVVSILDSGPGIPQDLRYKVFEPFFTTKGGSR 455
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1054616225  727 fmQGTGLGLPISRQFAKLMGGDVTVRSFPGQG 758
Cdd:TIGR02938  456 --KHIGMGLSVAQEIVADHGGIIDLDDDYSEG 485
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
797-899 1.22e-08

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: 53.95  E-value: 1.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSegKDIKIIALTA 876
Cdd:cd17616      1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAK--VKTPILILSG 78
                           90       100
                   ....*....|....*....|...
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKPF 899
Cdd:cd17616     79 LADIEDKVKGLGFGADDYMTKPF 101
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
796-900 1.40e-08

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: 53.82  E-value: 1.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAmsEGKDIKIIALT 875
Cdd:cd19919      2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQ--RHPDLPVIIMT 79
                           90       100
                   ....*....|....*....|....*
gi 1054616225  876 ANAFQEDKQAVLNAGCDDFVAKPFE 900
Cdd:cd19919     80 AHSDLDSAVSAYQGGAFEYLPKPFD 104
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
648-749 1.52e-08

Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana Phytochrome A, B, C, D and E; This family includes the histidine kinase-like ATPase (HATPase) domains of plant red/far-red photoreceptors, the phytochromes, and includes the Arabidopsis thaliana phytochrome family phyA-phyE. Following red light absorption, biologically inactive forms of phytochromes convert to active forms, which rapidly convert back to inactive forms upon far-red light irradiation. Phytochromes can be considered as having an N-terminal photosensory region to which a bilin chromophore is bound, and a C-terminal output region, which includes the HATPase domain represented here, and is involved in dimerization and presumably contributes to relaying the light signal to downstream signaling events.


Pssm-ID: 340409 [Multi-domain]  Cd Length: 113  Bit Score: 53.43  E-value: 1.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  648 FGDEGKLRQILINLIGNAIKFTVV--GHITLRVSylnssSTTTPVDQVIIV----FEVEDTGPGIPPEdmdLIFEAFiqa 721
Cdd:cd16932      1 YGDQIRLQQVLADFLLNAVRFTPSpgGWVEIKVS-----PTKKQIGDGVHVihleFRITHPGQGLPEE---LVQEMF--- 69
                           90       100
                   ....*....|....*....|....*...
gi 1054616225  722 kGGRQFMQGTGLGLPISRQFAKLMGGDV 749
Cdd:cd16932     70 -EENQWTTQEGLGLSISRKLVKLMNGDV 96
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
797-898 2.35e-08

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 53.14  E-value: 2.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINL-----------CVEWKPHLIWMDIQMPVMDGYEATKEIRAMSE 865
Cdd:cd17581      1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFlgledeedssnFNEPKVNMIITDYCMPGMTGYDLLKKVKESSA 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1054616225  866 GKDIKIIALTANAFQEDKQAVLNAGCDDFVAKP 898
Cdd:cd17581     81 LKEIPVVIMSSENIPTRISRCLEEGAEDFLLKP 113
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
797-910 4.53e-08

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 52.35  E-value: 4.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESV-GFEVCA-AENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAmsEGKDIKIIAL 874
Cdd:cd19931      1 VLLIDDHPLLRKGIKQLIELDpDFTVVGeASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALRE--EGVSARIVIL 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1054616225  875 TANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKMAQ 910
Cdd:cd19931     79 TVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQ 114
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
790-904 5.38e-08

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 54.47  E-value: 5.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  790 PGQSPHRILIVEDIQENRQLMVKLLES-VGFEVCA-AENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRamSEGK 867
Cdd:PRK10403     2 PEATPFQVLIVDDHPLMRRGVRQLLELdPGFEVVAeAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALR--RDGV 79
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1054616225  868 DIKIIALTANAFQEDKQAVLNAGCDDFVAKPFEETVL 904
Cdd:PRK10403    80 TAQIIILTVSDASSDVFALIDAGADGYLLKDSDPEVL 116
PRK15115 PRK15115
response regulator GlrR; Provisional
794-905 1.07e-07

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 55.61  E-value: 1.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  794 PHRILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGkdIKIIA 873
Cdd:PRK15115     5 PAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPG--MPVII 82
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1054616225  874 LTANAFQEDKQAVLNAGCDDFVAKPFEETVLF 905
Cdd:PRK15115    83 LTAHGSIPDAVAATQQGVFSFLTKPVDRDALY 114
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
797-912 1.22e-07

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 55.42  E-value: 1.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGkdIKIIALTA 876
Cdd:PRK10365     8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPA--IPVLIMTA 85
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKPFEetvlFNKMAQYL 912
Cdd:PRK10365    86 YSSVETAVEALKTGALDYLIKPLD----FDNLQATL 117
PRK10337 PRK10337
sensor protein QseC; Provisional
539-758 1.23e-07

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 55.43  E-value: 1.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  539 QFLAKMSHELRTPLNAIlgftQLMTRNRSLSPEDQE-------NLDI-ISRSGEhllaLINDVLEMSKIEAGQLTLNESY 610
Cdd:PRK10337   239 RFTSDAAHELRSPLAAL----KVQTEVAQLSDDDPQarkkallQLHAgIDRATR----LVDQLLTLSRLDSLDNLQDVAE 310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  611 FDLHRLIYS-IREMFAlKAADKGLEITINL--------GQEVnqyvfgdegkLRQILI-NLIGNAIKFTVVGH-ITLRvs 679
Cdd:PRK10337   311 IPLEDLLQSaVMDIYH-TAQQAGIDVRLTLnahpvirtGQPL----------LLSLLVrNLLDNAIRYSPQGSvVDVT-- 377
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054616225  680 yLNSSStttpvdqviivFEVEDTGPGIPPEDMDLIFEAFIQAKGgrQFMQGTGLGLPISRQFAKLMGGDVTVRSFPGQG 758
Cdd:PRK10337   378 -LNARN-----------FTVRDNGPGVTPEALARIGERFYRPPG--QEATGSGLGLSIVRRIAKLHGMNVSFGNAPEGG 442
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
797-898 1.33e-07

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 50.48  E-value: 1.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPH--LIWMDIQMPVMDGYEATKEIRAMSEGKDIKIIAL 874
Cdd:cd17582      1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNEidLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMM 80
                           90       100
                   ....*....|....*....|....*...
gi 1054616225  875 TANafqeDKQAV----LNAGCDDFVAKP 898
Cdd:cd17582     81 SSQ----DSVGVvfkcLSKGAADYLVKP 104
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
654-749 4.81e-07

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA; This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain.


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 48.86  E-value: 4.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  654 LRQILINLIGNAIKFTvvgHITLRVSYLNSSstttpvDQVIIVfeVEDTGPGIPPEDMDLIFEAFIQAKGGRQFMQ-GTG 732
Cdd:cd16949      1 LARALENVLRNALRYS---PSKILLDISQDG------DQWTIT--ITDDGPGVPEDQLEQIFLPFYRVDSARDRESgGTG 69
                           90
                   ....*....|....*..
gi 1054616225  733 LGLPISRQFAKLMGGDV 749
Cdd:cd16949     70 LGLAIAERAIEQHGGKI 86
PRK10643 PRK10643
two-component system response regulator PmrA;
796-899 5.35e-07

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 51.57  E-value: 5.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRamSEGKDIKIIALT 875
Cdd:PRK10643     2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWR--QKKYTLPVLILT 79
                           90       100
                   ....*....|....*....|....
gi 1054616225  876 ANAFQEDKQAVLNAGCDDFVAKPF 899
Cdd:PRK10643    80 ARDTLEDRVAGLDVGADDYLVKPF 103
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
796-898 6.83e-07

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: 48.98  E-value: 6.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEgkDIKIIALT 875
Cdd:cd17563      2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQP--DARIVVLT 79
                           90       100
                   ....*....|....*....|....*...
gi 1054616225  876 -----ANAFqedkQAVlNAGCDDFVAKP 898
Cdd:cd17563     80 gyasiATAV----EAI-KLGADDYLAKP 102
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
650-751 1.16e-06

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK. SpaK is the histidine kinase (HK) of the SpaK-SpaR two-component regulatory system (TCS), which is involved in the regulation of the biosynthesis of lantibiotic subtilin. NisK is the HK of the NisK-NisR TCS, which is involved in the regulation of the biosynthesis of lantibiotic nisin. SpaK and NisK may function as membrane-associated protein kinases that phosphorylate SpaR and NisR, respectively, in response to environmental signals.


Pssm-ID: 340434 [Multi-domain]  Cd Length: 107  Bit Score: 48.23  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  650 DEGKLRQILINLIGNAIKFTVVGhitlrvsylNSSSTTTPVDQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKGGRQFMQ 729
Cdd:cd16975      1 DTLLLSRALINIISNACQYAPEG---------GTVSISIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSGG 71
                           90       100
                   ....*....|....*....|..
gi 1054616225  730 GTGLGLPISRQFAKLMGGDVTV 751
Cdd:cd16975     72 HYGMGLYIAKNLVEKHGGSLII 93
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
541-764 1.19e-06

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 52.33  E-value: 1.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  541 LAKMSHELRTPLnAILGFTQLMTRN-RSLSPEDQEN--LDIISRSGEHllalINDVLEMSKIEAGQLTLNesyfdlhRLI 617
Cdd:PRK10815   270 LTDLTHSLKTPL-AVLQSTLRSLRSgKQMSVEQAEPimLEQISRISQQ----IGYYLHRASMRSEHNLLS-------REL 337
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  618 YSIREMF-ALKAA------DKGLEITINLGQEVNqyVFGDEGKLRQILINLIGNAIKFTV--VgHITLRVSYlnsssttt 688
Cdd:PRK10815   338 HSVAPLLdNLTSAlnkvyqRKGVNITLDISPEIT--FVGEKNDFMEVMGNVLDNACKYCLefV-EISARQTD-------- 406
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  689 pvDQVIIVfeVEDTGPGIPPEDMDLIFEafiqaKGGR--QFMQGTGLGLPISRQFAKLMGGDVTVRSFPGQGT----TFS 762
Cdd:PRK10815   407 --EHLHIV--VEDDGPGIPESKRELIFD-----RGQRadTLRPGQGLGLSVAREITEQYEGKISAGDSPLGGArmevIFG 477

                   ..
gi 1054616225  763 CQ 764
Cdd:PRK10815   478 RQ 479
PRK10693 PRK10693
two-component system response regulator RssB;
823-904 1.30e-06

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 51.53  E-value: 1.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  823 AAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRamSEGKDIKIIALTANAFQEDKQAVLNAGCDDFVAKP---- 898
Cdd:PRK10693     2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLR--NRGDQTPVLVISATENMADIAKALRLGVQDVLLKPvkdl 79

                   ....*...
gi 1054616225  899 --FEETVL 904
Cdd:PRK10693    80 nrLREMVF 87
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
797-904 1.44e-06

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: 49.71  E-value: 1.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMseGKDIKIIALTA 876
Cdd:COG4566      2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAAR--GSPLPVIFLTG 79
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1054616225  877 NAfqeD-KQAV--LNAGCDDFVAKPFEETVL 904
Cdd:COG4566     80 HG---DvPMAVraMKAGAVDFLEKPFDDQAL 107
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
797-940 1.91e-06

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


Pssm-ID: 274348 [Multi-domain]  Cd Length: 445  Bit Score: 51.67  E-value: 1.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVED---IQenRQLMVKLLEsvgFEVCAAENGLEAINLCVEWKPHLIWMDIQMP-----VMDGYEATKEIRAMSegKD 868
Cdd:TIGR02915    1 LLIVEDdlgLQ--KQLKWSFAD---YELAVAADRESAIALVRRHEPAVVTLDLGLPpdadgASEGLAALQQILAIA--PD 73
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054616225  869 IKIIALTANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKMAQYLNLHYVYADNSLLIPPETPKKLQKLTAAD 940
Cdd:TIGR02915   74 TKVIVITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHLYTLETENRRLQSALGGTALRGLITSS 145
PRK09483 PRK09483
response regulator; Provisional
797-897 2.00e-06

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 49.72  E-value: 2.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESV-GFEVCA-AENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEI-RAMSegkDIKIIA 873
Cdd:PRK09483     4 VLLVDDHELVRAGIRRILEDIkGIKVVGeACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKIlRYTP---DVKIIM 80
                           90       100
                   ....*....|....*....|....
gi 1054616225  874 LTANAFQEDKQAVLNAGCDDFVAK 897
Cdd:PRK09483    81 LTVHTENPLPAKVMQAGAAGYLSK 104
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
796-897 2.48e-06

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


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 47.79  E-value: 2.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVED---IQENRQLMVKLLESVGFEVCAAENglEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKII 872
Cdd:cd17575      2 MVLLVDDqaiIGEAVRRALADEEDIDFHYCSDPT--EAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPII 79
                           90       100
                   ....*....|....*....|....*
gi 1054616225  873 ALTANAFQEDKQAVLNAGCDDFVAK 897
Cdd:cd17575     80 VLSTKEEPEVKSEAFALGANDYLVK 104
PRK15369 PRK15369
two component system response regulator;
794-897 2.62e-06

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 49.31  E-value: 2.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  794 PHRILIVED----IQENRQLMVKL--LESVGFevcaAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRamSEGK 867
Cdd:PRK15369     3 NYKILLVDDheliINGIKNMLAPYprYKIVGQ----VDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLH--QRWP 76
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1054616225  868 DIKIIALTANafQEDKQA--VLNAGCDDFVAK 897
Cdd:PRK15369    77 AMNILVLTAR--QEEHMAsrTLAAGALGYVLK 106
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
539-747 2.97e-06

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 50.74  E-value: 2.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  539 QFLAKMSHELRTPLNAILGFTQLMtrnrslspEDQENLDI---ISRSgEHLLALINDVLEMSKieAGQLTLNESY--FDL 613
Cdd:PRK10755   139 LFTADVAHELRTPLAGIRLHLELL--------EKQHHIDVaplIARL-DQMMHTVEQLLQLAR--AGQSFSSGHYqtVKL 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  614 -HRLIYSIREMFALKAADKGLEITINLGqEVNQYVFGDEGKLRQILINLIGNAIKFTVVG-HITLRVSYLNSSStttpvd 691
Cdd:PRK10755   208 lEDVILPSQDELSEMLEQRQQTLLLPES-AADITVQGDATLLRLLLRNLVENAHRYSPEGsTITIKLSQEDGGA------ 280
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1054616225  692 qviiVFEVEDTGPGIPPEDMDLIFEAFiqakggRQFMQ---GTGLGLPISRQFAKLMGG 747
Cdd:PRK10755   281 ----VLAVEDEGPGIDESKCGELSKAF------VRMDSrygGIGLGLSIVSRITQLHHG 329
GAF COG2203
GAF domain [Signal transduction mechanisms];
138-384 4.37e-06

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 50.58  E-value: 4.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  138 LENYQILEKAIANINNSSNLSELYQNLATSVRKVTQFDRIMIYKFETDNSGVIVAEDKQNHLETYLGLHYPATdiprIAR 217
Cdd:COG2203    189 LERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRLPLGEG----LAG 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  218 QLYYEKWLRLIPDVNyqpvkliptnnpiTDTPLdlsgaflrsvSPLHIEYLQHMGVAASMSISLINQNRLWGLIACHHYT 297
Cdd:COG2203    265 RALRTGEPVVVNDAS-------------TDPRF----------APSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKE 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  298 PKKLDYEIRKICEFIGKFASIELVKQQEKHLGIYRQQVKLIQEELRASLANQLDYIGNVFKRNETNLLDIVQAQGAVILL 377
Cdd:COG2203    322 PRAFTEEDLELLEALADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAE 401

                   ....*..
gi 1054616225  378 EEQLTVL 384
Cdd:COG2203    402 LLLLLLD 408
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
797-906 4.94e-06

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: 46.47  E-value: 4.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKP--HLIWMDIQMPVMDGYEATKEIRamsEGKDIKIIAL 874
Cdd:cd17584      1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDefDLVITDVHMPDMDGFEFLELIR---LEMDLPVIMM 77
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1054616225  875 TAN-AFQEDKQAVLNAGCdDFVAKPFEETVLFN 906
Cdd:cd17584     78 SADgSTSTVMKGLAHGAC-DYLLKPVSIEDLKN 109
fixJ PRK09390
response regulator FixJ; Provisional
799-904 5.59e-06

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 48.07  E-value: 5.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  799 IVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAmsEGKDIKIIALTANA 878
Cdd:PRK09390     8 VVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKA--RGSPLPVIVMTGHG 85
                           90       100
                   ....*....|....*....|....*...
gi 1054616225  879 fqEDKQAV--LNAGCDDFVAKPFEETVL 904
Cdd:PRK09390    86 --DVPLAVeaMKLGAVDFIEKPFEDERL 111
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
654-762 5.80e-06

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Enterococcus faecium VanS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Enterococcus faecium VanS HK of the VanS-VanR two-component regulatory system (TCS) which activates the transcription of vanH, vanA and vanX vancomycin resistance genes. It also contains Ecoli YedV and PcoS, probable members of YedW-YedV TCS and PcoS-PcoR TCS, repectively. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); most also have a HAMP sensor domain.


Pssm-ID: 340400 [Multi-domain]  Cd Length: 102  Bit Score: 45.84  E-value: 5.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  654 LRQILINLIGNAIKF----TVVgHITlrvSYLNSsstttpvDQVIIvfEVEDTGPGIPPEDMDLIFEAFIQAKGGRQfMQ 729
Cdd:cd16923      1 LQRVFSNLLSNAIKYspenTRI-YIT---SFLTD-------DVVNI--MFKNPSSHPLDFKLEKLFERFYRGDNSRN-TE 66
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1054616225  730 GTGLGLPISRQFAKLMGGDVTVRSfPGQGTTFS 762
Cdd:cd16923     67 GAGLGLSIAKAIIELHGGSASAEY-DDNHDLFK 98
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
664-765 1.88e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains.


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 44.08  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  664 NAIKFTVVGHITLRVSYLNssstttpvDQVIIVfeVEDTGPGIPPEDMDlifeafiqakggrqfmQGTGLGLPISRQFAK 743
Cdd:cd16917     11 NALKHAGASRVRVTLSYTA--------DELTLT--VVDDGVGFDGPAPP----------------GGGGFGLLGMRERAE 64
                           90       100
                   ....*....|....*....|..
gi 1054616225  744 LMGGDVTVRSFPGQGTTFSCQV 765
Cdd:cd16917     65 LLGGTLTIGSRPGGGTRVTARL 86
PLN03029 PLN03029
type-a response regulator protein; Provisional
791-898 4.29e-05

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 45.79  E-value: 4.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  791 GQSPHRILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAI--------------------NLCVEWKPHLIWMDIQMPV 850
Cdd:PLN03029     5 TESQFHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALkflglheddrsnpdtpsvspNSHQEVEVNLIITDYCMPG 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1054616225  851 MDGYEATKEIRAMSEGKDIKIIALTANAFQEDKQAVLNAGCDDFVAKP 898
Cdd:PLN03029    85 MTGYDLLKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKP 132
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
532-762 9.68e-05

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 46.36  E-value: 9.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  532 IANRAksqflAKMSHElrTPLNAILGF---TQLMTRNRSLSPEDQ--ENLDIISRsgEHL--LALINDVLEMSKIE-AGQ 603
Cdd:PRK15053   300 IANRE-----AIRSGD--DLLGAIISFrskDEISTLNAQLTQIKQyvESLRTLRH--EHLnwMSTLNGLLQMKEYDrVLE 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  604 LTLNESYFDlHRLIYSIREMFA------------LKAADKGLEITINLGQEVNQYVFG-DEGKLRQILINLIGNAIKFTV 670
Cdd:PRK15053   371 MVQGESQAQ-QQLIDSLREAFAdrqvagllfgkvQRARELGLKMVIVPGSQLSQLPPGlDSTEFAAIVGNLLDNAFEASL 449
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  671 V---GHITLRVsYLNSSStttpvDQVIIvfEVEDTGPGIPPEDMDLIFEAFIQAKGGRQFMQGTGLGLPISrqFAKLMGG 747
Cdd:PRK15053   450 RsdeGNKIVEL-FLSDEG-----DDVVI--EVADQGCGVPESLRDKIFEQGVSTRADEPGEHGIGLYLIAS--YVTRCGG 519
                          250
                   ....*....|....*
gi 1054616225  748 DVTVRSFPGQGTTFS 762
Cdd:PRK15053   520 VITLEDNDPCGTLFS 534
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
797-904 1.35e-04

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: 42.42  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENgLEAINLCVEWKPH-LIWMDIQMPVMDGYEATKEIRAMSegKDIKIIALT 875
Cdd:cd17573      1 ILLIEDDSTLGKEISKGLNEKGYQADVAES-LKDGEYYIDIRNYdLVLVSDKLPDGNGLSIVSRIKEKH--PSIVVIVLS 77
                           90       100
                   ....*....|....*....|....*....
gi 1054616225  876 ANAFQEDKQAVLNAGCDDFVAKPFEETVL 904
Cdd:cd17573     78 DNPKTEQEIEAFKEGADDYIAKPFDFKVL 106
PRK13856 PRK13856
two-component response regulator VirG; Provisional
797-899 1.50e-04

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 44.42  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEAtkeIRAMSEGKDIKIIALTA 876
Cdd:PRK13856     4 VLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEI---VRSLATKSDVPIIIISG 80
                           90       100
                   ....*....|....*....|....
gi 1054616225  877 NAFQE-DKQAVLNAGCDDFVAKPF 899
Cdd:PRK13856    81 DRLEEaDKVVALELGATDFIAKPF 104
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
796-913 3.03e-04

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: 41.66  E-value: 3.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGF-EVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIR--------AMSEG 866
Cdd:cd17530      2 RVLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAeshsnaavILMSG 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1054616225  867 KDIKIIALTANAFQEDKQAVLNAgcddfVAKPFEETVLFNKMAQYLN 913
Cdd:cd17530     82 LDGGILESAETLAGANGLNLLGT-----LSKPFSPEELTELLTKYTA 123
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
797-899 3.26e-04

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 40.79  E-value: 3.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVE-WKPHLIWMDIQMP-VMDGYEATKEIRAMseGKDIKIIAL 874
Cdd:cd18161      1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESgPDIDLLVTDVIMPgGMNGSQLAEEARRR--RPDLKVLLT 78
                           90       100
                   ....*....|....*....|....*
gi 1054616225  875 TANAFQEDKQAVLNAGCdDFVAKPF 899
Cdd:cd18161     79 SGYAENAIEGGDLAPGV-DVLSKPF 102
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
796-898 3.83e-04

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: 41.58  E-value: 3.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESvGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKdIKIIaLT 875
Cdd:cd17596      2 TILVVDDEVRSLEALRRTLEE-DFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEV-VRII-IS 78
                           90       100
                   ....*....|....*....|....
gi 1054616225  876 ANAFQEDKQAVLN-AGCDDFVAKP 898
Cdd:cd17596     79 GYTDSEDIIAGINeAGIYQYLTKP 102
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
661-767 4.45e-04

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 41.05  E-value: 4.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  661 LIGNAIK----FTVVGHITLRVSYLNSSstttpvdqviIVFEVEDTGPGIPPEDMDLIFEAfiqakggrqfMQGTGLGLP 736
Cdd:COG2172     42 AVTNAVRhaygGDPDGPVEVELELDPDG----------LEIEVRDEGPGFDPEDLPDPYST----------LAEGGRGLF 101
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1054616225  737 ISRQFAKlmggDVTVRSFPGqGTTFSCQVQL 767
Cdd:COG2172    102 LIRRLMD----EVEYESDPG-GTTVRLVKRL 127
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
649-760 5.75e-04

Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine/threonine-protein kinase RsbT, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of Bacillus subtilis serine/threonine-protein kinase RsbT, a component of the stressosome signaling complex of Bacillus subtilis. The stressosome is formed from multiple copies of three proteins, a sensor protein RsbR, a scaffold protein RsbS, and RsbT, and responds to environmental changes by initiating a protein partner switching cascade. Stress perception increases the phosphorylation of RsbR and RsbS, by RsbT. Subsequent dissociation of RsbT from the stressosome activates the sigma-B cascade, leading to the release of the alternative sigma factor, sigma-B.


Pssm-ID: 340411 [Multi-domain]  Cd Length: 117  Bit Score: 40.43  E-value: 5.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  649 GDEGKLRQILINLIGNAIKFTVVGHITLRVsylnssstTTPVDQVIIVFEVEDTGPGIPpeDMDLIFEAFIQAKGgrqfm 728
Cdd:cd16934     21 VRQAEIATAVTELARNLLKHAGGGQVLLEV--------VAEGGRVALEILAVDQGPGIA--DVDEALRDGFSTGG----- 85
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1054616225  729 qGTGLGLPISRQFAklmgGDVTVRSFPGQGTT 760
Cdd:cd16934     86 -GLGLGLGGVRRLA----DEFDLHSAPGRGTV 112
PRK11697 PRK11697
two-component system response regulator BtsR;
796-855 1.01e-03

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 41.76  E-value: 1.01e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVG-FEVCA-AENGLEAINLCVEWKPHLIWMDIQMPVMDGYE 855
Cdd:PRK11697     3 KVLIVDDEPLAREELRELLQEEGdIEIVGeCSNAIEAIGAIHRLKPDVVFLDIQMPRISGLE 64
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
579-765 1.20e-03

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 41.91  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  579 ISRSGEHLLALINDVLEMSKIEAGQL--TLNESYFDLHRLIYSIR----EMFALKAA----------DKGLEITINlgqe 642
Cdd:COG4585     72 IKLQLEAARRLLDADPEAAREELEEIreLAREALAELRRLVRGLRppalDDLGLAAAleelaerllrAAGIRVELD---- 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  643 vnqyVFGDEGKL-RQILINL-------IGNAIKFTVVGHITLRVSYLNSSstttpvdqviIVFEVEDTGPGIPPEDMdli 714
Cdd:COG4585    148 ----VDGDPDRLpPEVELALyrivqeaLTNALKHAGATRVTVTLEVDDGE----------LTLTVRDDGVGFDPEAA--- 210
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1054616225  715 feafiqakggrqfmQGTGLGLPISRQFAKLMGGDVTVRSFPGQGTTFSCQV 765
Cdd:COG4585    211 --------------PGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATL 247
HATPase_LytS-like cd16957
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
691-765 1.20e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis LytS and Staphylococcus aureus LytS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), and a GAF sensor domain; most contain a DUF3816 domain.


Pssm-ID: 340433 [Multi-domain]  Cd Length: 106  Bit Score: 39.33  E-value: 1.20e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054616225  691 DQVIIVFEVEDTGPGIPPEDMDLIFEAFIQAKggrqfmQGTGLGLP-ISRQFAKLMG--GDVTVRSFPGQGTTFSCQV 765
Cdd:cd16957     34 DQHKVHVSVSDNGQGIPEERLDLLGKTTVTSE------KGTGTALEnLNRRLIGLFGseACLHIESEVHGGTEVWFVI 105
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
797-898 1.32e-03

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 39.06  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRAMSEGKDIKIIalTA 876
Cdd:cd19926      1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVI--TA 78
                           90       100
                   ....*....|....*....|..
gi 1054616225  877 NAFQEDKQAVLNAGCDDFVAKP 898
Cdd:cd19926     79 YGSLDTAIEALKAGAFDFLTKP 100
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
794-903 1.96e-03

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 41.78  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  794 PHRILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRamSEGKDIKIIA 873
Cdd:PRK10923     3 RGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIK--QRHPMLPVII 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1054616225  874 LTANAfqeDKQAVLNA---GCDDFVAKPF--EETV 903
Cdd:PRK10923    81 MTAHS---DLDAAVSAyqqGAFDYLPKPFdiDEAV 112
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
562-762 2.45e-03

Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 41.43  E-value: 2.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  562 MTRNRSLSPEDQENL-DIISR--SgehlLALINDVLEMSKieagqltlNESYFDLHRLIYSIREMFALKAADKGLEITIN 638
Cdd:COG3920    319 LQARRADDPEAREALeESQNRiqA----LALVHELLYQSE--------DWEGVDLRDYLRELLEPLRDSYGGRGIRIELD 386
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  639 lgqevnqyvfGDEGKLRQ-------ILIN-LIGNAIKF----TVVGHITLRVSylnssstttpVDQVIIVFEVEDTGPGI 706
Cdd:COG3920    387 ----------GPDVELPAdaavplgLILNeLVTNALKHaflsGEGGRIRVSWR----------REDGRLRLTVSDNGVGL 446
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1054616225  707 PPedmdlifeafiqakgGRQFMQGTGLGLPISRQFAKLMGGDVTVRSfpGQGTTFS 762
Cdd:COG3920    447 PE---------------DVDPPARKGLGLRLIRALVRQLGGTLELDR--PEGTRVR 485
PRK10336 PRK10336
two-component system response regulator QseB;
796-899 3.78e-03

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 39.88  E-value: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  796 RILIVEDIQENRQLMVKLLESVGFEVCAAENGLEAINLCVEWKPHLIWMDIQMPVMDGYEATKEIRamSEGKDIKIIALT 875
Cdd:PRK10336     2 RILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWR--EKGQREPVLILT 79
                           90       100
                   ....*....|....*....|....
gi 1054616225  876 ANAFQEDKQAVLNAGCDDFVAKPF 899
Cdd:PRK10336    80 ARDALAERVEGLRLGADDYLCKPF 103
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
671-769 4.29e-03

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 40.94  E-value: 4.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  671 VGHITLRVSYLNSSstttpvdqviIVFEVEDTGPGIPPE------------------DM------DLIFEAfiqakG--- 723
Cdd:COG0643    308 TGTITLSAYHEGGR----------VVIEVSDDGRGLDLEkirakaiekglitaeeaaALsdeellELIFAP-----Gfst 372
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1054616225  724 --------GRqfmqgtGLGLPISRQFAKLMGGDVTVRSFPGQGTTFSCQVQLTL 769
Cdd:COG0643    373 aeevtdlsGR------GVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTL 420
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
797-908 6.87e-03

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: 37.63  E-value: 6.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054616225  797 ILIVEDIQENRQLMVKLLESVGF-EVCAAENGLEAINLCVEWKPHLIWMDIQMPV-MDGYEATKEIRamsEGKDIK---- 870
Cdd:cd17589      1 FLIVDDQPTFRSMLKSMLRSLGVtRIDTASSGEEALRMCENKTYDIVLCDYNLGKgKNGQQLLEELR---HKKLISpstv 77
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1054616225  871 IIALTANAFQEDKQAVLNAGCDDFVAKPFEETVLFNKM 908
Cdd:cd17589     78 FIMVTGESSRAMVLSALELEPDDYLLKPFTVSELRERL 115
 
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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