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Conserved domains on  [gi|1228082595|ref|WP_094168523|]
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HAMP domain-containing protein [Prauserella marina]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11107 super family cl35992
hybrid sensory histidine kinase BarA; Provisional
828-1373 8.27e-86

hybrid sensory histidine kinase BarA; Provisional


The actual alignment was detected with superfamily member PRK11107:

Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 301.00  E-value: 8.27e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  828 IEVKNFEIEQARQeieeRAQQLAltsKYKSEFLANMSHELRTPL------TSLLIlagvlsqnSTQnLTPKQVEFAKVIE 901
Cdd:PRK11107   272 MEIQNVELDLAKK----RAQEAA---RIKSEFLANMSHELRTPLngvigfTRQTL--------KTP-LTPTQRDYLQTIE 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  902 SAGTDLLQLINDILDLSKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVPEQLSTDEQRLRQVLRN 981
Cdd:PRK11107   336 RSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITN 415
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  982 MLSNAVKFTEKGKVKLRV--RLVPADQVPgggaddpwLAFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGTGLGLS 1059
Cdd:PRK11107   416 LVGNAIKFTESGNIDILVelRALSNTKVQ--------LEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLV 487
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1060 ISRQVANLLGGELRAQSRLGAGSTFTLYVPVtpDFDTAVIDMGARPEPVLARRVLVVEAGEdqlltllvrgfatdlaDAR 1139
Cdd:PRK11107   488 ITQKLVNEMGGDISFHSQPNRGSTFWFHLPL--DLNPNPIIDGLPTDCLAGKRLLYVEPNS----------------AAA 549
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1140 EAVdvesvampdeaMERLAAGPVQcVVLDASLPgaaaltflqRLADGDYRVPVLAHP---TRRLSAAQERLIEA-HVRDH 1215
Cdd:PRK11107   550 QAT-----------LDILSETPLE-VTYSPTLS---------QLPEAHYDILLLGLPvtfREPLTMLHERLAKAkSMTDF 608
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1216 GVLLLSSLD-ELRERFLG-------------------LLPVTPEPEPEVVEPVASGLLGRRVLLIDDDARNVLAIAEMLK 1275
Cdd:PRK11107   609 LILALPCHEqVLAEQLKQdgadaclskplshtrllpaLLEPCHHKQPPLLPPTDESRLPLTVMAVDDNPANLKLIGALLE 688
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1276 LHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRFGSLPIIMVTAKAMAGDREKSLAAGASDY 1355
Cdd:PRK11107   689 EQVEHVVLCDSGHQAVEQAKQRP-FDLILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERLLSAGMDDY 767
                          570
                   ....*....|....*...
gi 1228082595 1356 VTKPVDAKELLTCIRRWI 1373
Cdd:PRK11107   768 LAKPIDEAMLKQVLLRYK 785
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
610-772 1.58e-25

GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, Signal transduction mechanisms];


:

Pssm-ID: 441559 [Multi-domain]  Cd Length: 156  Bit Score: 104.14  E-value: 1.58e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  610 ETTLANQDQDWLntnLARISGLLQGHRDLRAVTQLIMNELTPLV-GAQYGTFFLKEQGERLRLLASYGGAesgqGATEYE 688
Cdd:COG1956      1 EATSKEEDYDEL---LAQLSALLAGETDLIANLANISALLFEALpDYNWVGFYLVDGGGELVLGPFQGPP----ACTRIP 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  689 LGQSLLGQVASTRKAILVEQTP--PDYVRISSSlgsapPVNLIVLPIVFEEQVVGVIELASFT--RFSLVQRDFLEQLME 764
Cdd:COG1956     74 FGKGVCGTAAAEGETQLVPDVHafPGHIACDSA-----SRSEIVVPIFKDGEVIGVLDIDSPTpgRFDEEDQAGLEALAA 148

                   ....*...
gi 1228082595  765 SIGVNVNT 772
Cdd:COG1956    149 LLAEALDA 156
Tar super family cl43297
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
95-611 3.63e-11

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG0840:

Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 67.35  E-value: 3.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595   95 SVNAMAGNLTAQVRDIAGVATAVARGDLSQKITVQVRGELLELKNTINTMVDQLSSFADEVTRVAREVGSEGRLGGQAEV 174
Cdd:COG0840     12 LALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  175 PGVAGTWRDLTTSVNFMAGNLTAQVRSIAEVTTAVAKGDLSQKITVDARGEILELKSTINTMVDQLSSFADEVTRVAREV 254
Cdd:COG0840     92 LLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAA 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  255 GTEGILGGQAQVPGVAGTWRDLTTSV--NFMAGNLTAQVRSIAQVATAVARGDLSQKITVDARGEIFELKSTINTMVDQL 332
Cdd:COG0840    172 LALAAAALALALLAAALLALVALAIIlaLLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENL 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  333 SSFADEVTRVAREVGTEGRlggqadvkgvsgtwkGLTESVNVMADNLTDQVRSIAQVSAAVArgDLSQRITveakgEVAG 412
Cdd:COG0840    252 RELVGQVRESAEQVASASE---------------ELAASAEELAAGAEEQAASLEETAAAME--ELSATVQ-----EVAE 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  413 LAQTINTMVDTLSAFADEVTRVAREVgTEGILGGQARVANVAGTWKDLTDNVNSMaNNLTGQVRSIAQVTTAVA------ 486
Cdd:COG0840    310 NAQQAAELAEEASELAEEGGEVVEEA-VEGIEEIRESVEETAETIEELGESSQEI-GEIVDVIDDIAEQTNLLAlnaaie 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  487 --------RG---------NLSQKIDVDARgeilELKTTINTMVDTLSSFAAEVTRVAREVGKEGQLGGQAE--VEGVSG 547
Cdd:COG0840    388 aarageagRGfavvadevrKLAERSAEATK----EIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGeaLEEIVE 463
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1228082595  548 TWKRLTENVNELAGNLTRQVRAIAEVTSAVATGDLTRSITVEAKGEVSELKDNINAMVRSLRET 611
Cdd:COG0840    464 AVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQEL 527
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
828-1373 8.27e-86

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 301.00  E-value: 8.27e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  828 IEVKNFEIEQARQeieeRAQQLAltsKYKSEFLANMSHELRTPL------TSLLIlagvlsqnSTQnLTPKQVEFAKVIE 901
Cdd:PRK11107   272 MEIQNVELDLAKK----RAQEAA---RIKSEFLANMSHELRTPLngvigfTRQTL--------KTP-LTPTQRDYLQTIE 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  902 SAGTDLLQLINDILDLSKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVPEQLSTDEQRLRQVLRN 981
Cdd:PRK11107   336 RSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITN 415
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  982 MLSNAVKFTEKGKVKLRV--RLVPADQVPgggaddpwLAFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGTGLGLS 1059
Cdd:PRK11107   416 LVGNAIKFTESGNIDILVelRALSNTKVQ--------LEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLV 487
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1060 ISRQVANLLGGELRAQSRLGAGSTFTLYVPVtpDFDTAVIDMGARPEPVLARRVLVVEAGEdqlltllvrgfatdlaDAR 1139
Cdd:PRK11107   488 ITQKLVNEMGGDISFHSQPNRGSTFWFHLPL--DLNPNPIIDGLPTDCLAGKRLLYVEPNS----------------AAA 549
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1140 EAVdvesvampdeaMERLAAGPVQcVVLDASLPgaaaltflqRLADGDYRVPVLAHP---TRRLSAAQERLIEA-HVRDH 1215
Cdd:PRK11107   550 QAT-----------LDILSETPLE-VTYSPTLS---------QLPEAHYDILLLGLPvtfREPLTMLHERLAKAkSMTDF 608
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1216 GVLLLSSLD-ELRERFLG-------------------LLPVTPEPEPEVVEPVASGLLGRRVLLIDDDARNVLAIAEMLK 1275
Cdd:PRK11107   609 LILALPCHEqVLAEQLKQdgadaclskplshtrllpaLLEPCHHKQPPLLPPTDESRLPLTVMAVDDNPANLKLIGALLE 688
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1276 LHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRFGSLPIIMVTAKAMAGDREKSLAAGASDY 1355
Cdd:PRK11107   689 EQVEHVVLCDSGHQAVEQAKQRP-FDLILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERLLSAGMDDY 767
                          570
                   ....*....|....*...
gi 1228082595 1356 VTKPVDAKELLTCIRRWI 1373
Cdd:PRK11107   768 LAKPIDEAMLKQVLLRYK 785
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
748-1091 1.23e-69

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 237.11  E-value: 1.23e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  748 FTRFSLVQRDFLEQLMESIGVNVNTIVANARTDVLLEESQRLAAELSVRTEELQAQQAKLQQSNAELEEKAELLARQNRD 827
Cdd:COG0642      2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  828 IEVKNFEIEQARQEIEERAQQLALTSKYKSEFLANMSHELRTPLTSLLILAGVLSQNstqnLTPKQVEFAKVIESAGTDL 907
Cdd:COG0642     82 LLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE----LDEEQREYLETILRSADRL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  908 LQLINDILDLSKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVPeQLSTDEQRLRQVLRNMLSNAV 987
Cdd:COG0642    158 LRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLSNAI 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  988 KFTEKG-KVKLRVRlvpadqvpgggADDPWLAFSVIDTGIGIAEENLSTIFGAFQQADGttSRRYGGTGLGLSISRQVAN 1066
Cdd:COG0642    237 KYTPEGgTVTVSVR-----------REGDRVRISVEDTGPGIPPEDLERIFEPFFRTDP--SRRGGGTGLGLAIVKRIVE 303
                          330       340
                   ....*....|....*....|....*
gi 1228082595 1067 LLGGELRAQSRLGAGSTFTLYVPVT 1091
Cdd:COG0642    304 LHGGTIEVESEPGKGTTFTVTLPLA 328
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
775-1183 8.04e-61

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: 226.97  E-value: 8.04e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  775 ANARTDVLLEESQRLAA-ELsvrTEELQAQQAKLQQSNAELEEKAELLarqnrDIEVKNFEieQARQEIEEraqqlalTS 853
Cdd:TIGR02956  399 DTAAHNLKLQADERQVAqEL---QEHKESLEQLVAQRTQELAETNERL-----NAEVKNHA--KARAEAEE-------AN 461
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  854 KYKSEFLANMSHELRTPLTSLLILAGVLSQNStqnLTPKQVEFAKVIESAGTDLLQLINDILDLSKVEAGKMDIHPELVE 933
Cdd:TIGR02956  462 RAKSAFLATMSHEIRTPLNGILGTLELLGDTG---LTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFD 538
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  934 LRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVPEQLSTDEQRLRQVLRNMLSNAVKFTEKGKVKLRVRLvpadqvpgggAD 1013
Cdd:TIGR02956  539 LNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSL----------ND 608
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1014 DPWLAFSVIDTGIGIAEENLSTIFGAFQQADGttSRRYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPVtPD 1093
Cdd:TIGR02956  609 DSSLLFEVEDTGCGIAEEEQATLFDAFTQADG--RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPL-TR 685
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1094 FDTAVIDMGARPEPVLARRVLVVeagEDQLLTLLV-RGFATDLadareAVDVESVAMPDEAMERLAAGPVQCVVLDASLP 1172
Cdd:TIGR02956  686 GKPAEDSATLTVIDLPPQRVLLV---EDNEVNQMVaQGFLTRL-----GHKVTLAESGQSALECFHQHAFDLALLDINLP 757
                          410
                   ....*....|.
gi 1228082595 1173 GAAALTFLQRL 1183
Cdd:TIGR02956  758 DGDGVTLLQQL 768
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
975-1090 2.06e-50

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: 173.45  E-value: 2.06e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  975 LRQVLRNMLSNAVKFTEKGKVKLRVRLVPADQvpgggaDDPWLAFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGT 1054
Cdd:cd16922      1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEE------DGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGT 74
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1228082595 1055 GLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPV 1090
Cdd:cd16922     75 GLGLAISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
836-1089 5.54e-34

cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in Staphylococcus aureus (sp|Q2G2U4.1|WALK_STAA8). A shorter version, as found in Streptococcus pneumoniae, called WalK(Spn) or VicK, is not included. WalK is part of a two-component system and works with partner protein WalR.


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 139.50  E-value: 5.54e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  836 EQARQEIEERaqqlaltskyksEFLANMSHELRTPLTSLLILAGVLSQNSTQN--LTPKqveFAKVIESAGTDLLQLIND 913
Cdd:NF033092   364 EQEKIEQERR------------EFVANVSHELRTPLTTMRSYLEALADGAWKDpeLAPR---FLGVTQNETERMIRLVND 428
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  914 ILDLSKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEavvdPDVPEQLST---DEQRLRQVLRNMLSNAVKFT 990
Cdd:NF033092   429 LLQLSRMDSKDYKLNKEWVNFNEFFNYIIDRFEMILKNKNITFK----REFPKRDLWveiDTDKITQVLDNIISNAIKYS 504
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  991 -EKGKVKLRVRlvpadqvpgggADDPWLAFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGTGLGLSISRQVANLLG 1069
Cdd:NF033092   505 pEGGTITFRLL-----------ETHNRIIISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHG 573
                          250       260
                   ....*....|....*....|
gi 1228082595 1070 GELRAQSRLGAGSTFTLYVP 1089
Cdd:NF033092   574 GRIWAESEEGKGTTIYFTLP 593
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
970-1091 1.04e-33

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 125.84  E-value: 1.04e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595   970 TDEQRLRQVLRNMLSNAVKFT-EKGKVKLRVRlvpadqvpgggADDPWLAFSVIDTGIGIAEENLSTIFGAFQQADGTtS 1048
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTLE-----------RDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKR-S 68
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1228082595  1049 RRYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPVT 1091
Cdd:smart00387   69 RKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
842-1093 6.64e-32

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 132.07  E-value: 6.64e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  842 IEERAQQLALTSKYKSEFLANMSHELRTPLTSLLiLAGVLSQNSTQNLTPKQVEFAKVIESAGTDLLQLINDILDLSKVE 921
Cdd:NF040691   257 LQRQIRQLEELSRLQQRFVSDVSHELRTPLTTIR-MAADVIHDSRDDFDPATARSAELLHTELDRFESLLSDLLEISRFD 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  922 AGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAVVdPDVPEQLSTDEQRLRQVLRNMLSNAVKFTEKGKVKLRVrl 1001
Cdd:NF040691   336 AGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVDA-PGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTV-- 412
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1002 vpadqvpggGADDPWLAFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGTGLGLSISRQVANLLGGELRAQSRLGAG 1081
Cdd:NF040691   413 ---------AQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQG 483
                          250
                   ....*....|..
gi 1228082595 1082 STFTLYVPVTPD 1093
Cdd:NF040691   484 SQFRLTLPRVAG 495
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
970-1092 2.10e-28

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: 110.54  E-value: 2.10e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  970 TDEQRLRQVLRNMLSNAVKFTEKGKvKLRVRLVPADqvpgggaddpWLAFSVIDTGIGIAEENLSTIFGAFQQADgttSR 1049
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAAKAG-EITVTLSEGG----------ELTLTVEDNGIGIPPEDLPRIFEPFSTAD---KR 66
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1228082595 1050 RYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPVTP 1092
Cdd:pfam02518   67 GGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
610-772 1.58e-25

GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, Signal transduction mechanisms];


Pssm-ID: 441559 [Multi-domain]  Cd Length: 156  Bit Score: 104.14  E-value: 1.58e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  610 ETTLANQDQDWLntnLARISGLLQGHRDLRAVTQLIMNELTPLV-GAQYGTFFLKEQGERLRLLASYGGAesgqGATEYE 688
Cdd:COG1956      1 EATSKEEDYDEL---LAQLSALLAGETDLIANLANISALLFEALpDYNWVGFYLVDGGGELVLGPFQGPP----ACTRIP 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  689 LGQSLLGQVASTRKAILVEQTP--PDYVRISSSlgsapPVNLIVLPIVFEEQVVGVIELASFT--RFSLVQRDFLEQLME 764
Cdd:COG1956     74 FGKGVCGTAAAEGETQLVPDVHafPGHIACDSA-----SRSEIVVPIFKDGEVIGVLDIDSPTpgRFDEEDQAGLEALAA 148

                   ....*...
gi 1228082595  765 SIGVNVNT 772
Cdd:COG1956    149 LLAEALDA 156
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
824-1089 2.74e-22

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 101.83  E-value: 2.74e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  824 QNRDIEVKNFEIEQARQEIEERAQQLALTSKYKSEFLANMSHELRTPLTsllILAGVLS--QNSTQNLTPKQVefAKVIE 901
Cdd:NF012163   208 TTRVTPTSNDELGKLAQDFNQLASTLEKNEQMRRDFMADISHELRTPLA---VLRAELEaiQDGIRKFTPESL--DSLQA 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  902 SAGTdLLQLINDILDLSKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEaVVDPDVPEQLStDEQRLRQVLRN 981
Cdd:NF012163   283 EVGT-LTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELE-VSLPDSSLVFG-DRDRLMQLFNN 359
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  982 MLSNAVKFTEKGKvKLRVRlvpADQVPGGgaddpwLAFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGTGLGLSIS 1061
Cdd:NF012163   360 LLENSLRYTDSGG-SLHIS---ASQRPKE------VTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAIS 429
                          250       260
                   ....*....|....*....|....*...
gi 1228082595 1062 RQVANLLGGELRAQSRLGAGSTFTLYVP 1089
Cdd:NF012163   430 LNIVQAHGGTLHAAHSPLGGLRIVVTLP 457
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
834-1089 1.68e-17

two-component sensor histidine kinase AdeS; Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline.


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 85.82  E-value: 1.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  834 EIEQARQEIEERAQQLALTSKYKSEFLANMSHELRTPLTSLL-----ILAGVLSQNST--QNLTpKQVEfakviesagtD 906
Cdd:NF012226   116 EISELMHNFNDMAQKLESSVKNAQVWNAAIAHELRTPITILQgrlqgILDGVFEPDPAlfKSLL-NQVE----------G 184
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  907 LLQLINDILDLSKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAvvdpDVPEQL-STDEQRLRQVLRNMLSN 985
Cdd:NF012226   185 LSHLVEDLRTLSLVENQQLRLNYESVDLKDSIEKVLKMFEDRLEQAQLTIVL----NLTATPvFCDRRRIEQVLIALIDN 260
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  986 AVKFTEKGKVKLRVRLVpadqvpgggaDDPWLaFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGTGLGLSISRQVA 1065
Cdd:NF012226   261 AIRYANAGKLKISSSVI----------QDDWI-LQIEDEGPGIAEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIV 329
                          250       260
                   ....*....|....*....|....
gi 1228082595 1066 NLLGGELRAQSRLGaGSTFTLYVP 1089
Cdd:NF012226   330 IAHKGSIEYSNSQG-NSVFTIKLP 352
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
635-771 4.00e-16

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 76.35  E-value: 4.00e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  635 HRDLRAVTQLIMNELTPLVGAQYGTFFLKEQGERLrlLASYGGAESGQGATEYELGQSLLGQVASTRKAILVEQTPPDYV 714
Cdd:pfam13185    1 AADLEELLDAVLEAAVELGASAVGFILLVDDDGRL--AAWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPA 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1228082595  715 RISSSLGSAPPVNLIVLPIVFEEQVVGVIELASFT--RFSLVQRDFLEQLMESIGVNVN 771
Cdd:pfam13185   79 KKGLPAGHAGLRSFLSVPLVSGGRVVGVLALGSNRpgAFDEEDLELLELLAEQAAIAIE 137
resp_reg_YycF NF040534
response regulator YycF;
1255-1366 1.17e-11

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 66.28  E-value: 1.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1255 RRVLLIDDDArnvlAIAEMLKLH----GLSVEHAPNGRKGIE-ALRDSPDidLILMDVMMPEMDGYATTAAIRRMPRFgs 1329
Cdd:NF040534     1 KKILVVDDEK----PIADILEFNlkkeGYEVFCAYDGNEALElVEEEVPD--LVLLDIMLPGRDGMEVCREVRKKYDM-- 72
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1228082595 1330 lPIIMVTAKAMAGDREKSLAAGASDYVTKPVDAKELL 1366
Cdd:NF040534    73 -PIIMLTAKDSEIDKVLGLELGADDYVTKPFSTRELI 108
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
95-611 3.63e-11

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 67.35  E-value: 3.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595   95 SVNAMAGNLTAQVRDIAGVATAVARGDLSQKITVQVRGELLELKNTINTMVDQLSSFADEVTRVAREVGSEGRLGGQAEV 174
Cdd:COG0840     12 LALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  175 PGVAGTWRDLTTSVNFMAGNLTAQVRSIAEVTTAVAKGDLSQKITVDARGEILELKSTINTMVDQLSSFADEVTRVAREV 254
Cdd:COG0840     92 LLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAA 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  255 GTEGILGGQAQVPGVAGTWRDLTTSV--NFMAGNLTAQVRSIAQVATAVARGDLSQKITVDARGEIFELKSTINTMVDQL 332
Cdd:COG0840    172 LALAAAALALALLAAALLALVALAIIlaLLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENL 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  333 SSFADEVTRVAREVGTEGRlggqadvkgvsgtwkGLTESVNVMADNLTDQVRSIAQVSAAVArgDLSQRITveakgEVAG 412
Cdd:COG0840    252 RELVGQVRESAEQVASASE---------------ELAASAEELAAGAEEQAASLEETAAAME--ELSATVQ-----EVAE 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  413 LAQTINTMVDTLSAFADEVTRVAREVgTEGILGGQARVANVAGTWKDLTDNVNSMaNNLTGQVRSIAQVTTAVA------ 486
Cdd:COG0840    310 NAQQAAELAEEASELAEEGGEVVEEA-VEGIEEIRESVEETAETIEELGESSQEI-GEIVDVIDDIAEQTNLLAlnaaie 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  487 --------RG---------NLSQKIDVDARgeilELKTTINTMVDTLSSFAAEVTRVAREVGKEGQLGGQAE--VEGVSG 547
Cdd:COG0840    388 aarageagRGfavvadevrKLAERSAEATK----EIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGeaLEEIVE 463
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1228082595  548 TWKRLTENVNELAGNLTRQVRAIAEVTSAVATGDLTRSITVEAKGEVSELKDNINAMVRSLRET 611
Cdd:COG0840    464 AVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQEL 527
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
637-787 3.76e-10

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: 59.70  E-value: 3.76e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595   637 DLRAVTQLIMNELTPLVGAQYGTFFLKEQGER--LRLLASYGGAESGQGAtEYELGQSLLGQVASTRKAILVEQTPPDYV 714
Cdd:smart00065    1 DLEELLQTILEELRQLLGADRVLIYLVDENDRgeLVLVAADGLTLPTLGI-RFPLDEGLAGRVAETGRPLNIPDVEADPL 79
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1228082595   715 RISSSLGSAPPV-NLIVLPIVFEEQVVGVIELASFTRfslvQRDFL---EQLMESIGVNVNTIVANARtdvLLEESQ 787
Cdd:smart00065   80 FAEDLLGRYQGVrSFLAVPLVADGELVGVLALHNKKS----PRPFTeedEELLQALANQLAIALANAQ---LYEELR 149
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
383-424 1.27e-07

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 48.98  E-value: 1.27e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1228082595  383 VRSIAQVSAAVARGDLSQRITVEAKGEVAGLAQTINTMVDTL 424
Cdd:cd06225      4 LRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
286-332 3.58e-07

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 48.01  E-value: 3.58e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1228082595   286 NLTAQVRSIAQVATAVARGDLSQKITVDARGEIFELKSTINTMVDQL 332
Cdd:smart00304    2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRL 48
HAMP_2 pfam18947
HAMP domain;
455-518 4.10e-07

HAMP domain;


Pssm-ID: 465927 [Multi-domain]  Cd Length: 67  Bit Score: 48.25  E-value: 4.10e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1228082595  455 GTWKDLTDNVNSMANNLTGQVRSIAQVTTAVARGNLSQKIDVDARGEILELKTTINTMVDTLSS 518
Cdd:pfam18947    4 GDFRKIVEGVNNTLDAIITPLNEAADYVDRISKGDIPEKITDEYKGDFNEIKNNLNALIDAINA 67
PHA02515 PHA02515
hypothetical protein; Provisional
195-631 1.26e-04

hypothetical protein; Provisional


Pssm-ID: 107197 [Multi-domain]  Cd Length: 508  Bit Score: 46.31  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  195 LTAQVRSIAE----VTTAVAKGDLSQKITVDARGEILELKSTIN---TMVDQLSSFADEVTRVAREVGTEGILGGQAQVP 267
Cdd:PHA02515   114 LVIQIQQLADklsrTVQAPISGGLSSSEILEQLAEQLPLVSAVYghlANIDAVATNEADIDTVAASVGAVDTVAGDLGGT 193
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  268 GVAGTWRDLTTSVNFMAGNLTAQVRSIAQVATAVArgdlsqkiTVDARGEIFELKSTINTMVDQLSSFADEVTRVAREVG 347
Cdd:PHA02515   194 WAAGVSYDFGSIAVPPIGNTSPPGGNIVIVANSIG--------NVDTVAENIGDVSTVSTHLSSMLAVANDIDSVVSVAG 265
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  348 TEGRLGGQADVKGVSGTWKGLTESVNVMADNLTDqVRSIAqvsaavarGDLSQritVEAkgeVAGLAQTINTMVDTlsaf 427
Cdd:PHA02515   266 DLENIDAVADNAANINTVAGANANVNTVASNILD-VGTVA--------GNIDD---VQA---VAGNAANINVVADN---- 326
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  428 ADEVTRVArevgtegilGGQARVANVAGTwkdltdnvnsmANNLTGQVRSIAQVTTAVARGNlsqKIDVDARGEilelkT 507
Cdd:PHA02515   327 ADNINATA---------ANQANINAAVGN-----------ADNINAAVANQANINAVVGNAN---NINAVAANE-----G 378
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  508 TINTMVD------TLSSFAAEVTRVAREVGKEGQLGGQAEVEGVSGTWKRLTENVNELA-GNLTRQVRAIAEVTSAVATg 580
Cdd:PHA02515   379 NVNTVVDnladvqTVAGIAADVSTVAENEAAVAALGNDLTGQPMVIDYGDLSPASNPAApAGVLGAVWANAENIAAVAE- 457
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1228082595  581 dlTRSITVEAKGEVSELKDNIN-AMVRSLRETTLANQDQDWLNTNLARISGL 631
Cdd:PHA02515   458 --NIAVIIEAANNLPAILAALSgALVPANNLSDLADPAAARANIGLADLGGI 507
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
828-1373 8.27e-86

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 301.00  E-value: 8.27e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  828 IEVKNFEIEQARQeieeRAQQLAltsKYKSEFLANMSHELRTPL------TSLLIlagvlsqnSTQnLTPKQVEFAKVIE 901
Cdd:PRK11107   272 MEIQNVELDLAKK----RAQEAA---RIKSEFLANMSHELRTPLngvigfTRQTL--------KTP-LTPTQRDYLQTIE 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  902 SAGTDLLQLINDILDLSKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVPEQLSTDEQRLRQVLRN 981
Cdd:PRK11107   336 RSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITN 415
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  982 MLSNAVKFTEKGKVKLRV--RLVPADQVPgggaddpwLAFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGTGLGLS 1059
Cdd:PRK11107   416 LVGNAIKFTESGNIDILVelRALSNTKVQ--------LEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLV 487
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1060 ISRQVANLLGGELRAQSRLGAGSTFTLYVPVtpDFDTAVIDMGARPEPVLARRVLVVEAGEdqlltllvrgfatdlaDAR 1139
Cdd:PRK11107   488 ITQKLVNEMGGDISFHSQPNRGSTFWFHLPL--DLNPNPIIDGLPTDCLAGKRLLYVEPNS----------------AAA 549
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1140 EAVdvesvampdeaMERLAAGPVQcVVLDASLPgaaaltflqRLADGDYRVPVLAHP---TRRLSAAQERLIEA-HVRDH 1215
Cdd:PRK11107   550 QAT-----------LDILSETPLE-VTYSPTLS---------QLPEAHYDILLLGLPvtfREPLTMLHERLAKAkSMTDF 608
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1216 GVLLLSSLD-ELRERFLG-------------------LLPVTPEPEPEVVEPVASGLLGRRVLLIDDDARNVLAIAEMLK 1275
Cdd:PRK11107   609 LILALPCHEqVLAEQLKQdgadaclskplshtrllpaLLEPCHHKQPPLLPPTDESRLPLTVMAVDDNPANLKLIGALLE 688
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1276 LHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRFGSLPIIMVTAKAMAGDREKSLAAGASDY 1355
Cdd:PRK11107   689 EQVEHVVLCDSGHQAVEQAKQRP-FDLILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERLLSAGMDDY 767
                          570
                   ....*....|....*...
gi 1228082595 1356 VTKPVDAKELLTCIRRWI 1373
Cdd:PRK11107   768 LAKPIDEAMLKQVLLRYK 785
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
748-1091 1.23e-69

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 237.11  E-value: 1.23e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  748 FTRFSLVQRDFLEQLMESIGVNVNTIVANARTDVLLEESQRLAAELSVRTEELQAQQAKLQQSNAELEEKAELLARQNRD 827
Cdd:COG0642      2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  828 IEVKNFEIEQARQEIEERAQQLALTSKYKSEFLANMSHELRTPLTSLLILAGVLSQNstqnLTPKQVEFAKVIESAGTDL 907
Cdd:COG0642     82 LLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE----LDEEQREYLETILRSADRL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  908 LQLINDILDLSKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVPeQLSTDEQRLRQVLRNMLSNAV 987
Cdd:COG0642    158 LRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLSNAI 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  988 KFTEKG-KVKLRVRlvpadqvpgggADDPWLAFSVIDTGIGIAEENLSTIFGAFQQADGttSRRYGGTGLGLSISRQVAN 1066
Cdd:COG0642    237 KYTPEGgTVTVSVR-----------REGDRVRISVEDTGPGIPPEDLERIFEPFFRTDP--SRRGGGTGLGLAIVKRIVE 303
                          330       340
                   ....*....|....*....|....*
gi 1228082595 1067 LLGGELRAQSRLGAGSTFTLYVPVT 1091
Cdd:COG0642    304 LHGGTIEVESEPGKGTTFTVTLPLA 328
PRK15347 PRK15347
two component system sensor kinase;
840-1365 8.92e-67

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 244.55  E-value: 8.92e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  840 QEIEERAQQLALTSKYKSEFLANMSHELRTPLTSLLilaGVLS--QNSTqnLTPKQVEFAKVIESAGTDLLQLINDILDL 917
Cdd:PRK15347   382 QALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVL---GALEllQNTP--LTAEQMDLADTARQCTLSLLAIINNLLDF 456
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  918 SKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVPEQLSTDEQRLRQVLRNMLSNAVKFTEKGKVKL 997
Cdd:PRK15347   457 SRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGGIRL 536
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  998 RVRLVpADQvpgggaddpwLAFSVIDTGIGIAEENLSTIFGAFQQADGTTsrryGGTGLGLSISRQVANLLGGELRAQSR 1077
Cdd:PRK15347   537 RVKRH-EQQ----------LCFTVEDTGCGIDIQQQQQIFTPFYQADTHS----QGTGLGLTIASSLAKMMGGELTLFST 601
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1078 LGAGSTFTLYVPVTpDFdtavidmgARPEPVlarrvlvveagedqlltllvrgfatdladareavdvesvampdeamerl 1157
Cdd:PRK15347   602 PGVGSCFSLVLPLN-EY--------APPEPL------------------------------------------------- 623
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1158 aAGPVqcvvldaslpgAAALTFLQRLADGDYRvPVLAHPTRRLSAAQERLIEAHVRDHGVLLLSSLDELRERFLGLLPVT 1237
Cdd:PRK15347   624 -KGEL-----------SAPLALHRQLSAWGIT-CQPGHQNPALLDPELAYLPGRLYDLLQQIIQGAPNEPVINLPLQPWQ 690
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1238 PepepevvepvasgllgrRVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRkgiEALRDSPD--IDLILMDVMMPEMDGY 1315
Cdd:PRK15347   691 L-----------------QILLVDDVETNRDIIGMMLVELGQQVTTAASGT---EALELGRQhrFDLVLMDIRMPGLDGL 750
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1228082595 1316 ATTAAIRRMP--RFGSLPIIMVTAKAMAGDREKSLAAGASDYVTKPVDAKEL 1365
Cdd:PRK15347   751 ETTQLWRDDPnnLDPDCMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQL 802
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
841-1092 4.80e-66

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 223.25  E-value: 4.80e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  841 EIEERAQQLALTSKYKSEFLANMSHELRTPLTSLLILAGVLsQNSTQNLTPKQVEFAKVIESAGTDLLQLINDILDLSKV 920
Cdd:COG2205      1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELL-LDEEDLSPEERRELLEIIRESAERLLRLIEDLLDLSRL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  921 EAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVPEqLSTDEQRLRQVLRNMLSNAVKFT-EKGKVKLRV 999
Cdd:COG2205     80 ESGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPL-VYADPELLEQVLANLLDNAIKYSpPGGTITISA 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1000 RlvpadqvpgggADDPWLAFSVIDTGIGIAEENLSTIFGAFQQADGTtsRRYGGTGLGLSISRQVANLLGGELRAQSRLG 1079
Cdd:COG2205    159 R-----------REGDGVRISVSDNGPGIPEEELERIFERFYRGDNS--RGEGGTGLGLAIVKRIVEAHGGTIWVESEPG 225
                          250
                   ....*....|...
gi 1228082595 1080 AGSTFTLYVPVTP 1092
Cdd:COG2205    226 GGTTFTVTLPLAE 238
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
714-1093 1.90e-65

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 227.51  E-value: 1.90e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  714 VRISSSLGSAPPVNLIVLPIVFEEQVVGVIELASFTRFSLVQRDFLEQLMESIGVNVNTIVANARTDVLLEESQRLAAEL 793
Cdd:COG5002     29 LLLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLL 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  794 SVRTEELQAQQAKLQQSNAELEEKAELLARQNRDIEVKNFEIEQARQEIEERAQQLaltskyKSEFLANMSHELRTPLTS 873
Cdd:COG5002    109 ALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLEQM------RREFVANVSHELRTPLTS 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  874 LLILAGVLsQNSTQNLTPKQVEFAKVIESAGTDLLQLINDILDLSKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKG 953
Cdd:COG5002    183 IRGYLELL-LDGAADDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKG 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  954 LEFEAVVDPDVPeQLSTDEQRLRQVLRNMLSNAVKFT-EKGKVKLRVRlvpadqvpgggADDPWLAFSVIDTGIGIAEEN 1032
Cdd:COG5002    262 IELELDLPEDPL-LVLGDPDRLEQVLTNLLDNAIKYTpEGGTITVSLR-----------EEDDQVRISVRDTGIGIPEED 329
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1228082595 1033 LSTIFGAFQQADGTTSRRYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPVTPD 1093
Cdd:COG5002    330 LPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPLARE 390
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
775-1183 8.04e-61

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: 226.97  E-value: 8.04e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  775 ANARTDVLLEESQRLAA-ELsvrTEELQAQQAKLQQSNAELEEKAELLarqnrDIEVKNFEieQARQEIEEraqqlalTS 853
Cdd:TIGR02956  399 DTAAHNLKLQADERQVAqEL---QEHKESLEQLVAQRTQELAETNERL-----NAEVKNHA--KARAEAEE-------AN 461
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  854 KYKSEFLANMSHELRTPLTSLLILAGVLSQNStqnLTPKQVEFAKVIESAGTDLLQLINDILDLSKVEAGKMDIHPELVE 933
Cdd:TIGR02956  462 RAKSAFLATMSHEIRTPLNGILGTLELLGDTG---LTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFD 538
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  934 LRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVPEQLSTDEQRLRQVLRNMLSNAVKFTEKGKVKLRVRLvpadqvpgggAD 1013
Cdd:TIGR02956  539 LNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSL----------ND 608
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1014 DPWLAFSVIDTGIGIAEENLSTIFGAFQQADGttSRRYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPVtPD 1093
Cdd:TIGR02956  609 DSSLLFEVEDTGCGIAEEEQATLFDAFTQADG--RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPL-TR 685
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1094 FDTAVIDMGARPEPVLARRVLVVeagEDQLLTLLV-RGFATDLadareAVDVESVAMPDEAMERLAAGPVQCVVLDASLP 1172
Cdd:TIGR02956  686 GKPAEDSATLTVIDLPPQRVLLV---EDNEVNQMVaQGFLTRL-----GHKVTLAESGQSALECFHQHAFDLALLDINLP 757
                          410
                   ....*....|.
gi 1228082595 1173 GAAALTFLQRL 1183
Cdd:TIGR02956  758 DGDGVTLLQQL 768
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
836-1360 2.43e-55

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 209.44  E-value: 2.43e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  836 EQARQEIEERAQQlalTSKYKSEFLANMSHELRTPLTSLLilaGVLSQNSTQNLtPKQVE-FAKVIESAGTDLLQLINDI 914
Cdd:PRK10841   430 EESLQEMAQAAEQ---ASQSKSMFLATVSHELRTPLYGII---GNLDLLQTKEL-PKGVDrLVTAMNNSSSLLLKIISDI 502
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  915 LDLSKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVPEQLSTDEQRLRQVLRNMLSNAVKFTEKGK 994
Cdd:PRK10841   503 LDFSKIESEQLKIEPREFSPREVINHITANYLPLVVKKRLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGC 582
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  995 VKLRVRlvpadqvpgggADDPWLAFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGTGLGLSISRQVANLLGGELRA 1074
Cdd:PRK10841   583 IVLHVR-----------VDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISV 651
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1075 QSRLGAGSTFTLYVP-----VTPdfdTAVIDMGARPEPVLARRVLVVeagEDQLLTLLVRGFATDLADAREAVDVESVAM 1149
Cdd:PRK10841   652 DSEPGMGSQFTIRIPlygaqYPQ---KKGVEGLQGKRCWLAVRNASL---EQFLETLLQRSGIQVQRYEGQEPTPEDVLI 725
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1150 PDEAMERLAAGpVQCVVLDASLPGAAaltflQRLADGdYRVPVLAHPtRRLSAAQERL--IEAHVRDHGVLLLSSLDELr 1227
Cdd:PRK10841   726 TDDPVQKKWQG-RAVITFCRRHIGIP-----LEIAPG-EWVHSTATP-HELPALLARIyrIELESDDSANALPSTDKAV- 796
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1228 erflgllpvtpepepevvepVASGLLgrRVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDV 1307
Cdd:PRK10841   797 --------------------SDNDDM--MILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNH-IDIVLTDV 853
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1228082595 1308 MMPEMDGYATTAAIRRMPRfgSLPIIMVTAKAMAGDREKSLAAGASDYVTKPV 1360
Cdd:PRK10841   854 NMPNMDGYRLTQRLRQLGL--TLPVIGVTANALAEEKQRCLEAGMDSCLSKPV 904
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
975-1090 2.06e-50

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: 173.45  E-value: 2.06e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  975 LRQVLRNMLSNAVKFTEKGKVKLRVRLVPADQvpgggaDDPWLAFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGT 1054
Cdd:cd16922      1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEE------DGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGT 74
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1228082595 1055 GLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPV 1090
Cdd:cd16922     75 GLGLAISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
571-1092 1.25e-46

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 175.74  E-value: 1.25e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  571 AEVTSAVATGDLTRSITVEAKGEVSELKDNINAMVRSLRETTLANQDQDWLNTNLARISGLLQGHRDLRAVTQLIMNELT 650
Cdd:COG4251      1 LLLLALLLLLLLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALAL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  651 PLVGAQYGTFFLKEQGERLRLLASYGGAESGQGATEYELGQSLLGQVASTRKAILVEQTPPDYVRISSSLGSAPPVNLIV 730
Cdd:COG4251     81 LLLLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  731 LPIVFEEQVVGVIELASFTRFSLVQRDFLEQLMESIGVNVNTIVANARTDVLLEESQRLAAELSVRTEELQAQQAKLQQs 810
Cdd:COG4251    161 LLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLL- 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  811 naeLEEKAELLARQNRDIEVKNFEIEQARQEIEERAQQLALTSKYKSEFLANMSHELRTPLTSLLILAGVLSQNSTQNLT 890
Cdd:COG4251    240 ---LLILLLLLLILVLELLELRLELEELEEELEERTAELERSNEELEQFAYVASHDLREPLRKISGFSQLLEEDYGDKLD 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  891 PKQVEFAKVIESAGTDLLQLINDILDLSKVeaGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVpeqlST 970
Cdd:COG4251    317 EEGREYLERIRDAAERMQALIDDLLAYSRV--GRQELEFEPVDLNELLEEVLEDLEPRIEERGAEIEVGPLPTV----RG 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  971 DEQRLRQVLRNMLSNAVKFTEKGkVKLRVRLvpadqvpGGGADDPWLAFSVIDTGIGIAEENLSTIFGAFQQADGttSRR 1050
Cdd:COG4251    391 DPTLLRQVFQNLISNAIKYSRPG-EPPRIEI-------GAEREGGEWVFSVRDNGIGIDPEYAEKIFEIFQRLHS--RDE 460
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1228082595 1051 YGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPVTP 1092
Cdd:COG4251    461 YEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLPKAP 502
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1254-1376 2.42e-43

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: 153.85  E-value: 2.42e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1254 GRRVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRdSPDIDLILMDVMMPEMDGYATTAAIRRMPRFGSLPII 1333
Cdd:COG0784      5 GKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLR-AGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPII 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1228082595 1334 MVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRRWIAAA 1376
Cdd:COG0784     84 ALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARA 126
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
842-1172 2.55e-43

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 170.51  E-value: 2.55e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  842 IEERAQ-QLAL--TSKYKSEFLANMSHELRTPLTSLLILAGVLSQnsTQnLTPKQVEFAKVIESAGTDLLQLINDILDLS 918
Cdd:PRK11091   266 ITERKRyQDALekASRDKTTFISTISHELRTPLNGIVGLSRILLD--TE-LTAEQRKYLKTIHVSAITLGNIFNDIIDMD 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  919 KVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVPEQLSTDEQRLRQVLRNMLSNAVKFTEKGKVKLR 998
Cdd:PRK11091   343 KMERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVR 422
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  999 VRLVPADQvpgggaddpwLAFSVIDTGIGIAEENLSTIFGAFQQA-DGTTSRRYGGTGLGLSISRQVANLLGGELRAQSR 1077
Cdd:PRK11091   423 VRYEEGDM----------LTFEVEDSGIGIPEDELDKIFAMYYQVkDSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSE 492
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1078 LGAGSTFTL--YVPVTPDFDTAVIDMGARPEPVLarRVLVVeagEDQLLTLLVrgfATDLADAR-EAVDvesVAMP-DEA 1153
Cdd:PRK11091   493 EGKGSCFTLtiHAPAVAEEVEDAFDEDDMPLPAL--NILLV---EDIELNVIV---ARSVLEKLgNSVD---VAMTgKEA 561
                          330
                   ....*....|....*....
gi 1228082595 1154 MERLAAGPVQCVVLDASLP 1172
Cdd:PRK11091   562 LEMFDPDEYDLVLLDIQLP 580
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
857-1085 5.95e-41

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: 154.29  E-value: 5.95e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  857 SEFLANMSHELRTPLTSL-----LILAGVLSQNSTQNltpkqvEFAKVIESAGTDLLQLINDILDLSKVEAGKMDIHPEL 931
Cdd:TIGR02966  115 RDFVANVSHELRTPLTVLrgyleTLADGPDEDPEEWN------RALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEP 188
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  932 VELRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVPeqLSTDEQRLRQVLRNMLSNAVKFT-EKGKVKLRVRLVPadqvpgG 1010
Cdd:TIGR02966  189 VDMPALLDHLRDEAEALSQGKNHQITFEIDGGVD--VLGDEDELRSAFSNLVSNAIKYTpEGGTITVRWRRDG------G 260
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1228082595 1011 GAddpwlAFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFT 1085
Cdd:TIGR02966  261 GA-----EFSVTDTGIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFS 330
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
811-1185 1.01e-37

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 153.91  E-value: 1.01e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  811 NAELEEKAELLARQNRDIEVKNFEIEQARQEIEEraqqlalTSKYKSEFLANMSHELRTPLTSLLILAGVLSQnstQNLT 890
Cdd:PRK11466   406 NRHREQLAAQVKARTAELQELVIEHRQARAEAEK-------ASQAKSAFLAAMSHEIRTPLYGILGTAQLLAD---NPAL 475
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  891 PKQVEFAKVIESAGTDLLQLINDILDLSKVEAG--KMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVPEQL 968
Cdd:PRK11466   476 NAQRDDLRAITDSGESLLTILNDILDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTAL 555
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  969 STDEQRLRQVLRNMLSNAVKFTEKGKVKLRVrlvpadqvpggGADDPWLAFSVIDTGIGIAEENLSTIFGAFQQADGtts 1048
Cdd:PRK11466   556 MGDPRRIRQVITNLLSNALRFTDEGSIVLRS-----------RTDGEQWLVEVEDSGCGIDPAKLAEIFQPFVQVSG--- 621
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1049 rRYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPV---TPDFDTAVidmgARPEPVLARRVLVVeagEDQLLT 1125
Cdd:PRK11466   622 -KRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLrvaTAPVPKTV----NQAVRLDGLRLLLI---EDNPLT 693
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1228082595 1126 LlvRGFATDLADAreAVDVESVAMPDEAMERLAAG-PVQCVVLDASLPGAAALTFLQRLAD 1185
Cdd:PRK11466   694 Q--RITAEMLNTS--GAQVVAVGNAAQALETLQNSePFAAALVDFDLPDYDGITLARQLAQ 750
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
1255-1369 1.11e-37

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: 139.66  E-value: 1.11e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1255 RRVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRFGSLPIIM 1334
Cdd:COG3706      2 ARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHR-PDLILLDLEMPDMDGLELCRRLRADPRTADIPIIF 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1228082595 1335 VTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCI 1369
Cdd:COG3706     81 LTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
834-1093 3.19e-37

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 144.22  E-value: 3.19e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  834 EIEQAR--QEIEERAQQLALTSkyksEFLANMSHELRTPLTSLLILAGVLSQNSTQnltPKQVEFAKVIESAGTDLLQLI 911
Cdd:COG3852    115 DITERKrlERELRRAEKLAAVG----ELAAGLAHEIRNPLTGIRGAAQLLERELPD---DELREYTQLIIEEADRLNNLV 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  912 NDILDLSKveagKMDIHPELVELRQQVEYVRTTFQPlTAEKGLEFEAVVDPDVPEqLSTDEQRLRQVLRNMLSNAVK-FT 990
Cdd:COG3852    188 DRLLSFSR----PRPPEREPVNLHEVLERVLELLRA-EAPKNIRIVRDYDPSLPE-VLGDPDQLIQVLLNLVRNAAEaMP 261
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  991 EKGKVKLRVRLVPADQVPGGGADDpWLAFSVIDTGIGIAEENLSTIFGAFQqadgTTsrRYGGTGLGLSISRQVANLLGG 1070
Cdd:COG3852    262 EGGTITIRTRVERQVTLGGLRPRL-YVRIEVIDNGPGIPEEILDRIFEPFF----TT--KEKGTGLGLAIVQKIVEQHGG 334
                          250       260
                   ....*....|....*....|...
gi 1228082595 1071 ELRAQSRLGAGSTFTLYVPVTPD 1093
Cdd:COG3852    335 TIEVESEPGKGTTFRIYLPLEQA 357
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
727-1091 5.86e-37

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 143.79  E-value: 5.86e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  727 NLIVLPIVFEEQVVGVIELASFTRFSLVQRDFLEQLMESIGVNVNTIVANARTDVLLEESQRLAAELSVRTEELQAQQAK 806
Cdd:COG4191     11 LLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  807 LQQSNAELEEKAELLARQNRDIEVKNFEIEQARQEIEERAQQLALTSKYKS--EFLANMSHELRTPLTSLLILAGVLSQN 884
Cdd:COG4191     91 EALLLLLLAALDAEENAELEELERDITELERAEEELRELQEQLVQSEKLAAlgELAAGIAHEINNPLAAILGNAELLRRR 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  885 STQNLTPKQV-EFAKVIESAGTDLLQLINDILDLSKveagKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAVVDPD 963
Cdd:COG4191    171 LEDEPDPEELrEALERILEGAERAAEIVRSLRAFSR----RDEEEREPVDLNELIDEALELLRPRLKARGIEVELDLPPD 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  964 VPeQLSTDEQRLRQVLRNMLSN---AVKFTEKGKVKLRVRlvpadqvpgggADDPWLAFSVIDTGIGIAEENLSTIFGAF 1040
Cdd:COG4191    247 LP-PVLGDPGQLEQVLLNLLINaidAMEEGEGGRITISTR-----------REGDYVVISVRDNGPGIPPEVLERIFEPF 314
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1228082595 1041 QqadgTTSRRYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPVT 1091
Cdd:COG4191    315 F----TTKPVGKGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLPLA 361
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
1255-1374 4.92e-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: 133.75  E-value: 4.92e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1255 RRVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRFGSLPIIM 1334
Cdd:COG3437      7 PTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAP-PDLILLDVRMPGMDGFELLRLLRADPSTRDIPVIF 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1228082595 1335 VTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRRWIA 1374
Cdd:COG3437     86 LTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALE 125
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1255-1371 1.01e-34

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: 132.00  E-value: 1.01e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1255 RRVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRfgSLPIIM 1334
Cdd:COG0745      2 PRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEER-PDLILLDLMLPGMDGLEVCRRLRARPS--DIPIIM 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1228082595 1335 VTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRR 1371
Cdd:COG0745     79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRA 115
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
1257-1369 1.47e-34

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: 128.36  E-value: 1.47e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRFG-SLPIIMV 1335
Cdd:cd17546      1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEP-FDLVLMDLQMPVMDGLEATRRIRELEGGGrRTPIIAL 79
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1228082595 1336 TAKAMAGDREKSLAAGASDYVTKPVDAKELLTCI 1369
Cdd:cd17546     80 TANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
839-1090 3.67e-34

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: 138.57  E-value: 3.67e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  839 RQEIEE---RAQQLALTSkyksEFLANMSHELRTPLTSL-----LILAGVLSQNSTqnltpkqveFAKVIESAGTDLLQL 910
Cdd:COG5809    254 RKKLEEllrKSEKLSVVG----ELAAGIAHEIRNPLTSLkgfiqLLKDTIDEEQKT---------YLDIMLSELDRIESI 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  911 INDILDLSKVEAGKMdihpELVELRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVPeQLSTDEQRLRQVLRNMLSNAVKFT 990
Cdd:COG5809    321 ISEFLVLAKPQAIKY----EPKDLNTLIEEVIPLLQPQALLKNVQIELELEDDIP-DILGDENQLKQVFINLLKNAIEAM 395
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  991 EK-GKVKLRVRLVPADQVpgggaddpwlAFSVIDTGIGIAEENLSTIFGAFqqadgtTSRRYGGTGLGLSISRQVANLLG 1069
Cdd:COG5809    396 PEgGNITIETKAEDDDKV----------VISVTDEGCGIPEERLKKLGEPF------YTTKEKGTGLGLMVSYKIIEEHG 459
                          250       260
                   ....*....|....*....|.
gi 1228082595 1070 GELRAQSRLGAGSTFTLYVPV 1090
Cdd:COG5809    460 GKITVESEVGKGTTFSITLPI 480
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
836-1089 5.54e-34

cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in Staphylococcus aureus (sp|Q2G2U4.1|WALK_STAA8). A shorter version, as found in Streptococcus pneumoniae, called WalK(Spn) or VicK, is not included. WalK is part of a two-component system and works with partner protein WalR.


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 139.50  E-value: 5.54e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  836 EQARQEIEERaqqlaltskyksEFLANMSHELRTPLTSLLILAGVLSQNSTQN--LTPKqveFAKVIESAGTDLLQLIND 913
Cdd:NF033092   364 EQEKIEQERR------------EFVANVSHELRTPLTTMRSYLEALADGAWKDpeLAPR---FLGVTQNETERMIRLVND 428
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  914 ILDLSKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEavvdPDVPEQLST---DEQRLRQVLRNMLSNAVKFT 990
Cdd:NF033092   429 LLQLSRMDSKDYKLNKEWVNFNEFFNYIIDRFEMILKNKNITFK----REFPKRDLWveiDTDKITQVLDNIISNAIKYS 504
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  991 -EKGKVKLRVRlvpadqvpgggADDPWLAFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGTGLGLSISRQVANLLG 1069
Cdd:NF033092   505 pEGGTITFRLL-----------ETHNRIIISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHG 573
                          250       260
                   ....*....|....*....|
gi 1228082595 1070 GELRAQSRLGAGSTFTLYVP 1089
Cdd:NF033092   574 GRIWAESEEGKGTTIYFTLP 593
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
970-1091 1.04e-33

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 125.84  E-value: 1.04e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595   970 TDEQRLRQVLRNMLSNAVKFT-EKGKVKLRVRlvpadqvpgggADDPWLAFSVIDTGIGIAEENLSTIFGAFQQADGTtS 1048
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTLE-----------RDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKR-S 68
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1228082595  1049 RRYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPVT 1091
Cdd:smart00387   69 RKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
856-1192 1.63e-33

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 141.03  E-value: 1.63e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  856 KSEFLANMSHELRTPLTSLLilaGVLSQNSTQNLTPKQ-VEFAKVIESAGTDLLQLINDILDLSKVEAGKMDIHPELVEL 934
Cdd:PRK09959   712 KSQFLATMSHEIRTPISSIM---GFLELLSGSGLSKEQrVEAISLAYATGQSLLGLIGEILDVDKIESGNYQLQPQWVDI 788
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  935 RQQVEYVRTTFQPLTAEKGLEFEAvvDPDVPEQ--LSTDEQRLRQVLRNMLSNAVKFTEKGKVKLRVRLVPADQvpggga 1012
Cdd:PRK09959   789 PTLVQNTCHSFGAIAASKSIALSC--SSTFPDHylVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSLGHIDD------ 860
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1013 DDPWLAFSVIDTGIGIAEENLSTIFGAFQQAdgTTSRRYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPVTP 1092
Cdd:PRK09959   861 NHAVIKMTIMDSGSGLSQEEQQQLFKRYSQT--SAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEI 938
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1093 DFDTAVIDMGARPEPVLARRVLVVEAGEDQLLTLLVRGFATDLA-DAREAVDvesvamPDEAMERLAAGPVQCVVLDASL 1171
Cdd:PRK09959   939 SQQVATVEAKAEQPITLPEKLSILIADDHPTNRLLLKRQLNLLGyDVDEATD------GVQALHKVSMQHYDLLITDVNM 1012
                          330       340
                   ....*....|....*....|.
gi 1228082595 1172 PGAAALTFLQRLADGDYRVPV 1192
Cdd:PRK09959  1013 PNMDGFELTRKLREQNSSLPI 1033
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
755-1093 2.75e-32

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: 131.24  E-value: 2.75e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  755 QRDFLEQLMESIGVNVNTI-------VANARTDVLL--EESQRLAAELSVRTEELQAQQAKLQQSNAELEEKAELLARQN 825
Cdd:COG5000     88 RRRYLETILENLPAGVIVLdadgritLANPAAERLLgiPLEELIGKPLEELLPELDLAELLREALERGWQEEIELTRDGR 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  826 RDIEVKNFEIEQARQEI-------EERAQQLALTSkyksEFLANMSHELRTPLTSLLILAGVLSQNSTQNLTPKQVEFAK 898
Cdd:COG5000    168 RTLLVRASPLRDDGYVIvfdditeLLRAERLAAWG----ELARRIAHEIKNPLTPIQLSAERLRRKLADKLEEDREDLER 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  899 ---VIESAGTDLLQLINDILDLSKVEAgkmdIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVPEqLSTDEQRL 975
Cdd:COG5000    244 aldTIIRQVDRLKRIVDEFLDFARLPE----PQLEPVDLNELLREVLALYEPALKEKDIRLELDLDPDLPE-VLADRDQL 318
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  976 RQVLRNMLSNAVKFTE-KGKVKLRVRLvpadqvpgggaDDPWLAFSVIDTGIGIAEENLSTIFGAFQqadgTTSRRygGT 1054
Cdd:COG5000    319 EQVLINLLKNAIEAIEeGGEIEVSTRR-----------EDGRVRIEVSDNGPGIPEEVLERIFEPFF----TTKPK--GT 381
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1228082595 1055 GLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPVTPD 1093
Cdd:COG5000    382 GLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLAEE 420
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
842-1093 6.64e-32

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 132.07  E-value: 6.64e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  842 IEERAQQLALTSKYKSEFLANMSHELRTPLTSLLiLAGVLSQNSTQNLTPKQVEFAKVIESAGTDLLQLINDILDLSKVE 921
Cdd:NF040691   257 LQRQIRQLEELSRLQQRFVSDVSHELRTPLTTIR-MAADVIHDSRDDFDPATARSAELLHTELDRFESLLSDLLEISRFD 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  922 AGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAVVdPDVPEQLSTDEQRLRQVLRNMLSNAVKFTEKGKVKLRVrl 1001
Cdd:NF040691   336 AGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVDA-PGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTV-- 412
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1002 vpadqvpggGADDPWLAFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGTGLGLSISRQVANLLGGELRAQSRLGAG 1081
Cdd:NF040691   413 ---------AQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQG 483
                          250
                   ....*....|..
gi 1228082595 1082 STFTLYVPVTPD 1093
Cdd:NF040691   484 SQFRLTLPRVAG 495
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
1256-1371 1.77e-30

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: 116.49  E-value: 1.77e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIE-ALRDSPDidLILMDVMMPEMDGYATTAAIRRMPRFGSLPIIM 1334
Cdd:cd17548      1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEiARKEKPD--LILMDIQLPGMDGLEATRLLKEDPATRDIPVIA 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1228082595 1335 VTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRR 1371
Cdd:cd17548     79 LTAYAMKGDREKILEAGCDGYISKPIDTREFLETVAK 115
PRK09303 PRK09303
histidine kinase;
834-1090 2.28e-29

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 121.98  E-value: 2.28e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  834 EIEQARQEIEERAQQLaltsKYKSEFLANMSHELRTPLTSLLILAGVLSQNSTQNLTPKQVE----FAKVIESAGTDLLQ 909
Cdd:PRK09303   133 ELFVLRQENETLLEQL----KFKDRVLAMLAHDLRTPLTAASLALETLELGQIDEDTELKPAlieqLQDQARRQLEEIER 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  910 LINDILDLSKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVPEqLSTDEQRLRQVLRNMLSNAVKF 989
Cdd:PRK09303   209 LITDLLEVGRTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSDLPS-VYADQERIRQVLLNLLDNAIKY 287
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  990 TEK-GKVKLRVrLVPADQvpgggaddpWLAFSVIDTGIGIAEENLSTIF-GAF--QQADGTTsrrygGTGLGLSISRQVA 1065
Cdd:PRK09303   288 TPEgGTITLSM-LHRTTQ---------KVQVSICDTGPGIPEEEQERIFeDRVrlPRDEGTE-----GYGIGLSVCRRIV 352
                          250       260
                   ....*....|....*....|....*
gi 1228082595 1066 NLLGGELRAQSRLGAGSTFTLYVPV 1090
Cdd:PRK09303   353 RVHYGQIWVDSEPGQGSCFHFTLPV 377
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
1258-1359 7.19e-29

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: 111.35  E-value: 7.19e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1258 LLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRdSPDIDLILMDVMMPEMDGYATTAAIRRMPRfgSLPIIMVTA 1337
Cdd:cd17574      1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAR-EEQPDLIILDVMLPGMDGFEVCRRLREKGS--DIPIIMLTA 77
                           90       100
                   ....*....|....*....|..
gi 1228082595 1338 KAMAGDREKSLAAGASDYVTKP 1359
Cdd:cd17574     78 KDEEEDKVLGLELGADDYITKP 99
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
1257-1369 1.45e-28

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: 111.01  E-value: 1.45e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRFGSLPIIMVT 1336
Cdd:cd17580      1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFR-PDVILSDIGMPGMDGYELARRLRELPWLANTPAIALT 79
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1228082595 1337 AKAMAGDREKSLAAGASDYVTKPVDAKELLTCI 1369
Cdd:cd17580     80 GYGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
970-1092 2.10e-28

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: 110.54  E-value: 2.10e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  970 TDEQRLRQVLRNMLSNAVKFTEKGKvKLRVRLVPADqvpgggaddpWLAFSVIDTGIGIAEENLSTIFGAFQQADgttSR 1049
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAAKAG-EITVTLSEGG----------ELTLTVEDNGIGIPPEDLPRIFEPFSTAD---KR 66
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1228082595 1050 RYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPVTP 1092
Cdd:pfam02518   67 GGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
1257-1370 8.32e-27

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: 106.08  E-value: 8.32e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSpDIDLILMDVMMPEMDGYATTAAIRRMPRfgSLPIIMVT 1336
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEE-RPDLILLDINMPGMDGLELLKRIRRRDP--TTPVIILT 77
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1228082595 1337 AKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:pfam00072   78 AHGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
1257-1360 9.25e-27

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: 105.67  E-value: 9.25e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRFGSLPIIMVT 1336
Cdd:cd19920      1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEP-PDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLT 79
                           90       100
                   ....*....|....*....|....
gi 1228082595 1337 AKAMAGDREKSLAAGASDYVTKPV 1360
Cdd:cd19920     80 ALTDTEDKVKGFELGAVDYITKPF 103
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
1258-1359 1.37e-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: 105.00  E-value: 1.37e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1258 LLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDsPDIDLILMDVMMPEMDGYATTAAIRRMPRfgSLPIIMVTA 1337
Cdd:cd00156      1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLRE-ERPDLVLLDLMMPGMDGLELLRKLRELPP--DIPVIVLTA 77
                           90       100
                   ....*....|....*....|..
gi 1228082595 1338 KAMAGDREKSLAAGASDYVTKP 1359
Cdd:cd00156     78 KADEEDAVRALELGADDYLVKP 99
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
1256-1370 1.83e-26

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: 105.22  E-value: 1.83e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHG-LSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRFGSLPIIM 1334
Cdd:cd17551      2 RILIVDDNPTNLLLLEALLRSAGyLEVVSFTDPREALAWCRENP-PDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVM 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1228082595 1335 VTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:cd17551     81 ITADTDREVRLRALEAGATDFLTKPFDPVELLARVR 116
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
1256-1360 1.09e-25

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: 102.58  E-value: 1.09e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIE-ALRDSPDidLILMDVMMPEMDGYATTAAIRRMPRFGSLPIIM 1334
Cdd:cd17538      1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALAlAEEELPD--LILLDVMMPGMDGFEVCRRLKEDPETRHIPVIM 78
                           90       100
                   ....*....|....*....|....*.
gi 1228082595 1335 VTAKAMAGDREKSLAAGASDYVTKPV 1360
Cdd:cd17538     79 ITALDDREDRIRGLEAGADDFLSKPI 104
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1255-1371 1.44e-25

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: 111.21  E-value: 1.44e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1255 RRVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRfgSLPIIM 1334
Cdd:COG2204      3 ARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEP-PDLVLLDLRMPGMDGLELLRELRALDP--DLPVIL 79
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1228082595 1335 VTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRR 1371
Cdd:COG2204     80 LTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVER 116
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
610-772 1.58e-25

GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, Signal transduction mechanisms];


Pssm-ID: 441559 [Multi-domain]  Cd Length: 156  Bit Score: 104.14  E-value: 1.58e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  610 ETTLANQDQDWLntnLARISGLLQGHRDLRAVTQLIMNELTPLV-GAQYGTFFLKEQGERLRLLASYGGAesgqGATEYE 688
Cdd:COG1956      1 EATSKEEDYDEL---LAQLSALLAGETDLIANLANISALLFEALpDYNWVGFYLVDGGGELVLGPFQGPP----ACTRIP 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  689 LGQSLLGQVASTRKAILVEQTP--PDYVRISSSlgsapPVNLIVLPIVFEEQVVGVIELASFT--RFSLVQRDFLEQLME 764
Cdd:COG1956     74 FGKGVCGTAAAEGETQLVPDVHafPGHIACDSA-----SRSEIVVPIFKDGEVIGVLDIDSPTpgRFDEEDQAGLEALAA 148

                   ....*...
gi 1228082595  765 SIGVNVNT 772
Cdd:COG1956    149 LLAEALDA 156
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
838-1092 7.34e-25

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 111.21  E-value: 7.34e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  838 ARQEIEERAQQL----ALtskykSEFLANMSHELRTPLTSLLILAGVLSQNSTQNLTPKqveFAKVIESAGTDLLQLIND 913
Cdd:PRK11360   373 ERKRLQRRVARQerlaAL-----GELVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQE---YLSVVLREVDRLNKVIDQ 444
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  914 ILDLSKVEAGKMdihpELVELRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVPEQLSTDEQrLRQVLRNMLSNAVK-FTEK 992
Cdd:PRK11360   445 LLEFSRPRESQW----QPVSLNALVEEVLQLFQTAGVQARVDFETELDNELPPIWADPEL-LKQVLLNILINAVQaISAR 519
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  993 GKVKLRVRLVPADQVpgggaddpwlAFSVIDTGIGIAEENLSTIFGAFQqadgTTsrRYGGTGLGLSISRQVANLLGGEL 1072
Cdd:PRK11360   520 GKIRIRTWQYSDGQV----------AVSIEDNGCGIDPELLKKIFDPFF----TT--KAKGTGLGLALSQRIINAHGGDI 583
                          250       260
                   ....*....|....*....|
gi 1228082595 1073 RAQSRLGAGSTFTLYVPVTP 1092
Cdd:PRK11360   584 EVESEPGVGTTFTLYLPINP 603
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
840-1089 6.99e-24

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: 106.70  E-value: 6.99e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  840 QEIEERAQQLaltskykSEFLANMSHELRTPLTSLLILAGV-LSQNSTQNltpkqvEFAKVIESAGTDLLQL---INDIL 915
Cdd:TIGR01386  232 GRLEDAFQRL-------SQFSADLAHELRTPLTNLLGQTQVaLSQPRTGE------EYREVLESNLEELERLsrmVSDML 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  916 DLSKVEAGKmdIHPELVE--LRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVPeqlsTDEQRLRQVLRNMLSNAVKFTEKG 993
Cdd:TIGR01386  299 FLARADNGQ--LALERVRldLAAELAKVAEYFEPLAEERGVRIRVEGEGLVR----GDPQMFRRAISNLLSNALRHTPDG 372
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  994 KvKLRVRLvpadqvpggGADDPWLAFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGTGLGLSISRQVANLLGGELR 1073
Cdd:TIGR01386  373 G-TITVRI---------ERRSDEVRVSVSNPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRAS 442
                          250
                   ....*....|....*.
gi 1228082595 1074 AQSrLGAGSTFTLYVP 1089
Cdd:TIGR01386  443 AES-PDGKTRFILRFP 457
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
824-1089 2.74e-22

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 101.83  E-value: 2.74e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  824 QNRDIEVKNFEIEQARQEIEERAQQLALTSKYKSEFLANMSHELRTPLTsllILAGVLS--QNSTQNLTPKQVefAKVIE 901
Cdd:NF012163   208 TTRVTPTSNDELGKLAQDFNQLASTLEKNEQMRRDFMADISHELRTPLA---VLRAELEaiQDGIRKFTPESL--DSLQA 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  902 SAGTdLLQLINDILDLSKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEaVVDPDVPEQLStDEQRLRQVLRN 981
Cdd:NF012163   283 EVGT-LTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELE-VSLPDSSLVFG-DRDRLMQLFNN 359
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  982 MLSNAVKFTEKGKvKLRVRlvpADQVPGGgaddpwLAFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGTGLGLSIS 1061
Cdd:NF012163   360 LLENSLRYTDSGG-SLHIS---ASQRPKE------VTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAIS 429
                          250       260
                   ....*....|....*....|....*...
gi 1228082595 1062 RQVANLLGGELRAQSRLGAGSTFTLYVP 1089
Cdd:NF012163   430 LNIVQAHGGTLHAAHSPLGGLRIVVTLP 457
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
1257-1370 1.33e-21

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: 91.21  E-value: 1.33e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSpDIDLILMDVMMPEMDGYATTAAIRRMPrfgSLPIIMVT 1336
Cdd:cd17623      1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEG-SPDLVVLDVMLPKMNGLDVLKELRKTS---QVPVLMLT 76
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1228082595 1337 AKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:cd17623     77 ARGDDIDRILGLELGADDYLPKPFNPRELVARIR 110
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1256-1374 1.43e-21

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 91.95  E-value: 1.43e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGL--SVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRmpRFGSLPII 1333
Cdd:COG4565      5 RVLIVEDDPMVAELLRRYLERLPGfeVVGVASSGEEALALLAEHR-PDLILLDIYLPDGDGLELLRELRA--RGPDVDVI 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1228082595 1334 MVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRRWIA 1374
Cdd:COG4565     82 VITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLE 122
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
1255-1370 3.10e-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: 90.39  E-value: 3.10e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1255 RRVLLIDDDArnvlAIAEMLKLH----GLSVEHAPNGRKGIEALRDSPDiDLILMDVMMPEMDGYATTAAIRRMPRFGSL 1330
Cdd:cd17618      1 RTILIVEDEP----AIREMIAFNleraGFDVVEAEDAESAVNLIVEPRP-DLILLDWMLPGGSGIQFIRRLKRDEMTRDI 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1228082595 1331 PIIMVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:cd17618     76 PIIMLTARGEEEDKVRGLEAGADDYITKPFSPRELVARIK 115
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
859-1089 3.72e-21

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 98.16  E-value: 3.72e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  859 FLANMSHELRTPLTsllILAGVLSQNSTQNLTPKQVEFA-KVIESAGTDLLQLINDILDLSKVEAGKMDIHPELVELRQQ 937
Cdd:PRK11006   207 FFANVSHELRTPLT---VLQGYLEMMQDQPLEGALREKAlHTMREQTQRMEGLVKQLLTLSKIEAAPTIDLNEKVDVPMM 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  938 VEYVRTTFQPLTAEK-GLEFEavVDPDVpeQLSTDEQRLRQVLRNMLSNAVKFTEKG-KVKLRVRLVPAdqvpggGADdp 1015
Cdd:PRK11006   284 LRVLEREAQTLSQGKhTITFE--VDNSL--KVFGNEDQLRSAISNLVYNAVNHTPEGtHITVRWQRVPQ------GAE-- 351
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1228082595 1016 wlaFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVP 1089
Cdd:PRK11006   352 ---FSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLP 422
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
1258-1366 6.57e-21

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: 89.25  E-value: 6.57e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1258 LLIDDDArnvlAIAEMLKLH----GLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRFGSLPII 1333
Cdd:cd19937      1 LVVDDEE----DIVELLKYNlekeGYEVVTAYDGEEALKRAKDEK-PDLIILDLMLPGIDGLEVCRILRSDPKTSSIPII 75
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1228082595 1334 MVTAKAMAGDREKSLAAGASDYVTKPVDAKELL 1366
Cdd:cd19937     76 MLTAKGEEFDKVLGLELGADDYITKPFSPRELL 108
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
1255-1371 2.02e-20

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: 87.99  E-value: 2.02e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1255 RRVLLIDDDA--RNVLAIA-EMLKlhGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRFGSLP 1331
Cdd:cd17552      2 KRILVIDDEEdiREVVQAClEKLA--GWEVLTASSGQEGLEKAATEQ-PDAILLDVMMPDMDGLATLKKLQANPETQSIP 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1228082595 1332 IIMVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRR 1371
Cdd:cd17552     79 VILLTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAK 118
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
1257-1371 4.64e-20

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: 87.00  E-value: 4.64e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDS-PDIdlILMDVMMPEMDGYATTAAIRRMPRFGSLPIIMV 1335
Cdd:cd17598      1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHrPTL--VISDIVMPEMDGYELCRKIKSDPDLKDIPVILL 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1228082595 1336 TAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRR 1371
Cdd:cd17598     79 TTLSDPRDVIRGLECGADNFITKPYDEKYLLSRIKY 114
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
1258-1370 5.44e-20

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: 86.89  E-value: 5.44e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1258 LLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRfgSLPIIMVTA 1337
Cdd:cd17625      1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGI-YDLIILDIMLPGMDGLEVLKSLREEGI--ETPVLLLTA 77
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1228082595 1338 KAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:cd17625     78 LDAVEDRVKGLDLGADDYLPKPFSLAELLARIR 110
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
1256-1359 1.48e-19

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: 84.83  E-value: 1.48e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEML-KLHGLS-VEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRfgSLPII 1333
Cdd:COG4753      1 KVLIVDDEPLIREGLKRILeWEAGFEvVGEAENGEEALELLEEHK-PDLVITDINMPGMDGLELLEAIRELDP--DTKII 77
                           90       100
                   ....*....|....*....|....*.
gi 1228082595 1334 MVTAKAMAGDREKSLAAGASDYVTKP 1359
Cdd:COG4753     78 ILSGYSDFEYAQEAIKLGADDYLLKP 103
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
975-1089 2.01e-19

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: 84.69  E-value: 2.01e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  975 LRQVLRNMLSNAVKFTEKGKVKlRVRlVPADQVPgggadDPWLaFSVIDTGIGIAEENLSTIFGAFQQADGTTSrrYGGT 1054
Cdd:cd16921      1 LGQVLTNLLGNAIKFRRPRRPP-RIE-VGAEDVG-----EEWT-FYVRDNGIGIDPEYAEKVFGIFQRLHSREE--YEGT 70
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1228082595 1055 GLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVP 1089
Cdd:cd16921     71 GVGLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
1257-1359 3.29e-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: 83.97  E-value: 3.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGrkgIEALR--DSPDIDLILMDVMMPEMDGYATTAAIRRMPRFGSLPIIM 1334
Cdd:cd19927      1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNG---LEALDllNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIF 77
                           90       100
                   ....*....|....*....|....*
gi 1228082595 1335 VTAKAMAGDREKSLAAGASDYVTKP 1359
Cdd:cd19927     78 LTAKGMTSDRIKGYNAGCDGYLSKP 102
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
1256-1371 9.60e-19

phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains; This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 83.62  E-value: 9.60e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVE--HAPNGRKGIEALR------DSPDIDLILMDVMMPEMDGYATTAAIRRMPRF 1327
Cdd:cd17557      1 TILLVEDNPGDAELIQEAFKEAGVPNElhVVRDGEEALDFLRgegeyaDAPRPDLILLDLNMPRMDGFEVLREIKADPDL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1228082595 1328 GSLPIIMVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRR 1371
Cdd:cd17557     81 RRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRS 124
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
1257-1370 1.68e-18

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: 82.43  E-value: 1.68e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPDiDLILMDVMMPEMDGYATTAAIRRMPRfgSLPIIMVT 1336
Cdd:cd17627      1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRP-DAVVLDVMMPRLDGLEVCRRLRAAGN--DLPILVLT 77
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1228082595 1337 AKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:cd17627     78 ARDSVSDRVAGLDAGADDYLVKPFALEELLARVR 111
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
834-1090 2.90e-18

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: 88.77  E-value: 2.90e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  834 EIEQARQEIEeRAQQLALTSkyksEFLANMSHELRTPLTS------LLilagvlsqNSTQNLTPKQVEFAK-VIESagtd 906
Cdd:COG5806    184 ENILLRKELQ-RAEKLEVVS----ELAASIAHEVRNPLTVvrgfiqLL--------QEPELSDEKRKQYIRiALEE---- 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  907 lLQ----LINDILDLSKVEAGKMDIhpelVELRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVpeQLSTDEQRLRQVLRNM 982
Cdd:COG5806    247 -LDraeaIITDYLTFAKPQPEKLEK----IDVSEELEHVIDVLSPYANMNNVEIQTELEPGL--YIEGDRQKLQQCLINI 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  983 LSNAVKFTEK-GKVKLRVRLVPADQVpgggaddpwlaFSVIDTGIGIAEENLSTIfgafqqadGTT--SRRYGGTGLGLS 1059
Cdd:COG5806    320 IKNGIEAMPNgGTLTIDVSIDKNKVI-----------ISIKDTGVGMTKEQLERL--------GEPyfSTKEKGTGLGTM 380
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1228082595 1060 ISRQVANLLGGELRAQSRLGAGSTFTLYVPV 1090
Cdd:COG5806    381 VSYRIIEAMNGTIRVESEVGKGTTFTITLPL 411
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
1257-1359 7.99e-18

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: 79.79  E-value: 7.99e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRdSPDIDLILMDVMMPEMDGYATTAAIRRMPRfgSLPIIMVT 1336
Cdd:cd19935      1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLAL-TNEYDLIILDVMLPGLDGLEVLRRLRAAGK--QTPVLMLT 77
                           90       100
                   ....*....|....*....|...
gi 1228082595 1337 AKAMAGDREKSLAAGASDYVTKP 1359
Cdd:cd19935     78 ARDSVEDRVKGLDLGADDYLVKP 100
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
1255-1371 1.06e-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: 80.42  E-value: 1.06e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1255 RRVLLIDDDA--RNVLAIAemLKLHGLSVEHAPNGRKGIEALRdSPDIDLILMDVMMPEMDGYATTAAIRRMPRFGSLPI 1332
Cdd:cd17562      1 KKILAVDDSAsiRQMVSFT--LRGAGYEVVEAADGRDALSKAQ-SKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPI 77
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1228082595 1333 IMVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRR 1371
Cdd:cd17562     78 LMLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKK 116
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
1256-1370 1.15e-17

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: 80.11  E-value: 1.15e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPDiDLILMDVMMPEMDGYATTAAIRRmprFGSLPIIMV 1335
Cdd:cd19938      1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPP-DLILLDLMLPGTDGLTLCREIRR---FSDVPIIMV 76
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1228082595 1336 TAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:cd19938     77 TARVEEIDRLLGLELGADDYICKPYSPREVVARVK 111
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
1256-1368 1.26e-17

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: 80.26  E-value: 1.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDD--ARNVlaIAEMLKLHGLSVEHAPNGRKGIEALRDSPDIDLILMDVMMPEMDGYATTAAIRRmpRFGS--LP 1331
Cdd:cd17544      2 KVLVVDDSatSRNH--LRALLRRHNFQVLEAANGQEALEVLEQHPDIKLVITDYNMPEMDGFELVREIRK--KYSRdqLA 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1228082595 1332 IIMVTAkamAGDREKS---LAAGASDYVTKPVdAKELLTC 1368
Cdd:cd17544     78 IIGISA---SGDNALSarfIKAGANDFLTKPF-LPEEFYC 113
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
1257-1371 1.32e-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: 79.86  E-value: 1.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDA------RNVLAIAemlklHGLS-VEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRmpRFGS 1329
Cdd:cd17535      1 VLIVDDHPlvreglRRLLESE-----PDIEvVGEAADGEEALALLRELR-PDVVLMDLSMPGMDGIEALRRLRR--RYPD 72
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1228082595 1330 LPIIMVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRR 1371
Cdd:cd17535     73 LKVIVLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRA 114
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
1257-1359 1.36e-17

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: 79.73  E-value: 1.36e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRD--------SPDIDLILMDVMMPEMDGYATTAAIRRMPRFG 1328
Cdd:cd19924      1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENlakegndlSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1228082595 1329 SLPIIMVTAKAMAGDREKSLAAGASDYVTKP 1359
Cdd:cd19924     81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
834-1089 1.68e-17

two-component sensor histidine kinase AdeS; Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline.


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 85.82  E-value: 1.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  834 EIEQARQEIEERAQQLALTSKYKSEFLANMSHELRTPLTSLL-----ILAGVLSQNST--QNLTpKQVEfakviesagtD 906
Cdd:NF012226   116 EISELMHNFNDMAQKLESSVKNAQVWNAAIAHELRTPITILQgrlqgILDGVFEPDPAlfKSLL-NQVE----------G 184
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  907 LLQLINDILDLSKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAvvdpDVPEQL-STDEQRLRQVLRNMLSN 985
Cdd:NF012226   185 LSHLVEDLRTLSLVENQQLRLNYESVDLKDSIEKVLKMFEDRLEQAQLTIVL----NLTATPvFCDRRRIEQVLIALIDN 260
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  986 AVKFTEKGKVKLRVRLVpadqvpgggaDDPWLaFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGTGLGLSISRQVA 1065
Cdd:NF012226   261 AIRYANAGKLKISSSVI----------QDDWI-LQIEDEGPGIAEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIV 329
                          250       260
                   ....*....|....*....|....
gi 1228082595 1066 NLLGGELRAQSRLGaGSTFTLYVP 1089
Cdd:NF012226   330 IAHKGSIEYSNSQG-NSVFTIKLP 352
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
1256-1370 1.91e-17

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 82.93  E-value: 1.91e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSpdIDLILMDVMMPEMDGYATTAAIRRMPRfgsLPIIMV 1335
Cdd:PRK10955     3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDS--IDLLLLDVMMPKKNGIDTLKELRQTHQ---TPVIML 77
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1228082595 1336 TAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:PRK10955    78 TARGSELDRVLGLELGADDYLPKPFNDRELVARIR 112
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
1257-1370 2.19e-17

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: 79.07  E-value: 2.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRmpRFGSLPIIMVT 1336
Cdd:cd17624      1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGP-YDLVILDLGLPDGDGLDLLRRWRR--QGQSLPVLILT 77
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1228082595 1337 AKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:cd17624     78 ARDGVDDRVAGLDAGADDYLVKPFALEELLARLR 111
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
839-1095 2.41e-17

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 86.61  E-value: 2.41e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  839 RQEIEERAQ---QLALTSKyKSE-----FLANMSHELRTPLTsllILAGVLS--QNSTQNLTPKQVE--FAKViesagTD 906
Cdd:PRK10549   216 RDELGRLAQdfnQLASTLE-KNEqmrrdFMADISHELRTPLA---VLRGELEaiQDGVRKFTPESVAslQAEV-----GT 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  907 LLQLINDILDLSKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEfeavVDPDVPEQ--LSTDEQRLRQVLRNMLS 984
Cdd:PRK10549   287 LTKLVDDLHQLSLSDEGALAYRKTPVDLVPLLEVAGGAFRERFASRGLT----LQLSLPDSatVFGDPDRLMQLFNNLLE 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  985 NAVKFTEKGKvKLRVRLVpadqvpgggADDPWLAFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGTGLGLSISRQV 1064
Cdd:PRK10549   363 NSLRYTDSGG-SLHISAE---------QRDKTLRLTFADSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNI 432
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1228082595 1065 ANLLGGELRAQ-SRLGaGSTFTLYVPVTPDFD 1095
Cdd:PRK10549   433 VEAHNGRIIAAhSPFG-GVSITVELPLERDLQ 463
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
1257-1371 2.41e-17

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: 79.84  E-value: 2.41e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEAL-RDSPDIdlILMDVMMPEMDGYATTAAIRRMPRfgSLPIIMV 1335
Cdd:cd17549      1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALsPDFPGV--VISDIRMPGMDGLELLAQIRELDP--DLPVILI 76
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1228082595 1336 TAK---AMAgdrEKSLAAGASDYVTKPVDAKELLTCIRR 1371
Cdd:cd17549     77 TGHgdvPMA---VEAMRAGAYDFLEKPFDPERLLDVVRR 112
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
1257-1365 2.46e-17

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: 79.21  E-value: 2.46e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPD-IDLILMDVMMPEMDGYATTAAIRRMPrfgSLPIIMV 1335
Cdd:cd17584      1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDeFDLVITDVHMPDMDGFEFLELIRLEM---DLPVIMM 77
                           90       100       110
                   ....*....|....*....|....*....|
gi 1228082595 1336 TAKAMAGDREKSLAAGASDYVTKPVDAKEL 1365
Cdd:cd17584     78 SADGSTSTVMKGLAHGACDYLLKPVSIEDL 107
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
1256-1365 4.75e-17

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: 78.53  E-value: 4.75e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDD--DARNVlaIAEMLKLHGLS-VEHAPNGRKGIEALRdSPDIDLILMDVMMPEMDGYATTAAIRRMPRFGSLPI 1332
Cdd:cd19923      2 KVLVVDDfsTMRRI--IKNLLKELGFNnVEEAEDGVDALEKLK-AGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPV 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1228082595 1333 IMVTAKAMAGDREKSLAAGASDYVTKPVDAKEL 1365
Cdd:cd19923     79 LMVTAEAKKENVIAAAQAGVNNYIVKPFTAATL 111
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
1256-1370 4.77e-17

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: 78.19  E-value: 4.77e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSpDIDLILMDVMMPEMDGYATTaaiRRMPRFGSLPIIMV 1335
Cdd:cd17622      2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIARE-KPDAVLLDIMLPGIDGLTLC---RDLRPKYQGPILLL 77
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1228082595 1336 TAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:cd17622     78 TALDSDIDHILGLELGADDYVVKPVEPAVLLARLR 112
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
1256-1370 7.41e-17

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: 77.80  E-value: 7.41e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPDiDLILMDVMMPEMDGYATTAAIRRmprFGSLPIIMV 1335
Cdd:cd19939      1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQP-SLVVLDIMLPGMDGLTVCREVRE---HSHVPILML 76
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1228082595 1336 TAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:cd19939     77 TARTEEMDRVLGLEMGADDYLCKPFSPRELLARVR 111
orf27 CHL00148
Ycf27; Reviewed
1256-1370 1.23e-16

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 80.92  E-value: 1.23e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDArNVLAIAEM-LKLHGLSVEHAPNGRKGIEALR-DSPDidLILMDVMMPEMDGYATTAAIRRMprfGSLPII 1333
Cdd:CHL00148     8 KILVVDDEA-YIRKILETrLSIIGYEVITASDGEEALKLFRkEQPD--LVILDVMMPKLDGYGVCQEIRKE---SDVPII 81
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1228082595 1334 MVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:CHL00148    82 MLTALGDVSDRITGLELGADDYVVKPFSPKELEARIR 118
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
821-1089 1.32e-16

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 84.44  E-value: 1.32e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  821 LARQNRDIEVKNFEIEQARQEIEERAQQLALTSKY-----------KSEFLANMSHELRTPLTSLLILAG-VLSQNSTQN 888
Cdd:PRK09835   216 VSRQIQNITSKDLDVRLDPQTVPIELEQLVLSFNHmieriedvftrQSNFSADIAHEIRTPITNLITQTEiALSQSRSQK 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  889 ltpkqvEFAKVIESA---GTDLLQLINDILDLSkvEAGKMDIHPELV--ELRQQVEYVRTTFQPLTAEKGLEFEAVVDPd 963
Cdd:PRK09835   296 ------ELEDVLYSNleeLTRMAKMVSDMLFLA--QADNNQLIPEKKmlDLADEVGKVFDFFEAWAEERGVELRFVGDP- 366
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  964 vpEQLSTDEQRLRQVLRNMLSNAVKFTEKGK-VKLRVRLVpADQVpgggaddpwlAFSVIDTGIGIAEENLSTIFGAFQQ 1042
Cdd:PRK09835   367 --CQVAGDPLMLRRAISNLLSNALRYTPAGEaITVRCQEV-DHQV----------QLVVENPGTPIAPEHLPRLFDRFYR 433
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1228082595 1043 ADGTTSRRYGGTGLGLSISRQVANLLGGELRAQSRLGAgSTFTLYVP 1089
Cdd:PRK09835   434 VDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDARG-TRFVISLP 479
pleD PRK09581
response regulator PleD; Reviewed
1256-1370 1.33e-16

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 84.18  E-value: 1.33e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRFGSLPIIMV 1335
Cdd:PRK09581     4 RILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQ-PDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMV 82
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1228082595 1336 TAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:PRK09581    83 TALDDPEDRVRGLEAGADDFLTKPINDVALFARVK 117
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
971-1089 1.50e-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 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: 76.73  E-value: 1.50e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  971 DEQRLRQVLRNMLSNAVKFTEKGKvKLRVRlvpADQVPGGgaddpwLAFSVIDTGIGIAEENLSTIFGAFQQADGTTSRR 1050
Cdd:cd16946      1 DRDRLQQLFVNLLENSLRYTDTGG-KLRIR---AAQTPQE------VRLDVEDSAPGVSDDQLARLFERFYRVESSRNRA 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1228082595 1051 YGGTGLGLSISRQVANLLGGELRAQ-SRLGaGSTFTLYVP 1089
Cdd:cd16946     71 SGGSGLGLAICHNIALAHGGTISAEhSPLG-GLRLVLTLP 109
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
1255-1371 1.60e-16

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 76.76  E-value: 1.60e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1255 RRVLLIDDDA--RNVLAiaEMLKLHGLSVEHAPNGRKGIEALRDSpDIDLILMDVMMPEMDGYATTAAIRRMPRfgSLPI 1332
Cdd:COG5803      3 KKILIVDDQAgiRMLLK--EVLKKEGYEVFQAANGKEALEKVKEL-KPDLVLLDMKMPGMDGIEILKEIKEIDP--DIPV 77
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1228082595 1333 IMVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRR 1371
Cdd:COG5803     78 IMMTAYGELDMVEEAKELGAKGYFTKPFDIDELREAVNK 116
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
971-1089 2.10e-16

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: 76.38  E-value: 2.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  971 DEQRLRQVLRNMLSNAVKFT-EKGKVKLRVRLvpadqvpgggADDPWLAFSVIDTGIGIAEENLSTIFGAFQQADGTTSR 1049
Cdd:cd16925      1 DAEKYERVVLNLLSNAFKFTpDGGRIRCILEK----------FRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTR 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1228082595 1050 RYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVP 1089
Cdd:cd16925     71 AHGGTGLGLSIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
1256-1370 3.54e-16

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: 76.28  E-value: 3.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLS--VEHAPNGRKGIE-ALRDSPDIdlILMDVMMPEMDGYATTAAI-RRMPrfgsLP 1331
Cdd:cd17541      2 RVLIVDDSAVMRKLLSRILESDPDIevVGTARDGEEALEkIKELKPDV--ITLDIEMPVMDGLEALRRImAERP----TP 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1332 IIMVTAKAMAGDRE--KSLAAGASDYVTKPV---------DAKELLTCIR 1370
Cdd:cd17541     76 VVMVSSLTEEGAEItlEALELGAVDFIAKPSggisldleeIAEELIEKIK 125
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
635-771 4.00e-16

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 76.35  E-value: 4.00e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  635 HRDLRAVTQLIMNELTPLVGAQYGTFFLKEQGERLrlLASYGGAESGQGATEYELGQSLLGQVASTRKAILVEQTPPDYV 714
Cdd:pfam13185    1 AADLEELLDAVLEAAVELGASAVGFILLVDDDGRL--AAWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPA 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1228082595  715 RISSSLGSAPPVNLIVLPIVFEEQVVGVIELASFT--RFSLVQRDFLEQLMESIGVNVN 771
Cdd:pfam13185   79 KKGLPAGHAGLRSFLSVPLVSGGRVVGVLALGSNRpgAFDEEDLELLELLAEQAAIAIE 137
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
1255-1371 4.07e-16

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 82.97  E-value: 4.07e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1255 RRVLLIDDD--ARNVLAIAemLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRfgSLPI 1332
Cdd:PRK11361     5 NRILIVDDEdnVRRMLSTA--FALQGFETHCANNGRTALHLFADIH-PDVVLMDIRMPEMDGIKALKEMRSHET--RTPV 79
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1228082595 1333 IMVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRR 1371
Cdd:PRK11361    80 ILMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQR 118
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
1257-1359 4.67e-16

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: 74.89  E-value: 4.67e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDA--RNVLAIAemLKLHGLSVEHAPNGRKGI-EALRDSPDidLILMDVMMPEMDGyatTAAIRRMPRFGSLPII 1333
Cdd:cd17620      1 ILVIEDEPqiRRFLRTA--LEAHGYRVFEAETGQEGLlEAATRKPD--LIILDLGLPDMDG---LEVIRRLREWSAVPVI 73
                           90       100
                   ....*....|....*....|....*.
gi 1228082595 1334 MVTAKAMAGDREKSLAAGASDYVTKP 1359
Cdd:cd17620     74 VLSARDEESDKIAALDAGADDYLTKP 99
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
856-923 4.72e-16

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 73.75  E-value: 4.72e-16
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1228082595   856 KSEFLANMSHELRTPLTSLLILAGVLsqnSTQNLTPKQVEFAKVIESAGTDLLQLINDILDLSKVEAG 923
Cdd:smart00388    2 KREFLANLSHELRTPLTAIRGYLELL---LDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
862-1090 5.17e-16

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 82.58  E-value: 5.17e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  862 NMSHELRTPLTSLLILAGVLSQNstqnLTPKQVE-FAKVIESAGTDLLQLINDILDLSKVEAGKMDIHPELVELRQQVEY 940
Cdd:PRK11100   262 TLTHELKSPLAAIRGAAELLQED----PPPEDRArFTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEE 337
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  941 VRTTFQPLTAEKGLEFEavVDPDvPEQLSTDEQRLRQVLRNMLSNAVKFT-EKGKVKLRVRLVpADQVpgggaddpwlAF 1019
Cdd:PRK11100   338 LVEAREAQAAAKGITLR--LRPD-DARVLGDPFLLRQALGNLLDNAIDFSpEGGTITLSAEVD-GEQV----------AL 403
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1228082595 1020 SVIDTGIGIAEENLSTIFGAFQqadgTTSRRYGG---TGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPV 1090
Cdd:PRK11100   404 SVEDQGPGIPDYALPRIFERFY----SLPRPANGrksTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLPR 473
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
1256-1371 6.36e-16

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: 75.32  E-value: 6.36e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRmpRFGSLPIIMV 1335
Cdd:cd17555      2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQ-PDLVLCDLRMPEMDGLEVLKQITK--ESPDTPVIVV 78
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1228082595 1336 TAKAMAGDREKSLAAGASDYVTKPV-DAKELLTCIRR 1371
Cdd:cd17555     79 SGAGVMSDAVEALRLGAWDYLTKPIeDLAVLEHAVRR 115
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
826-1091 8.85e-16

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: 82.09  E-value: 8.85e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  826 RDI-EVKNFEIEQARQEIEERAQQLAltskykseflANMSHELRTPLTSLlilAGVLsqnstQNLTPKQV---EFAKVIE 901
Cdd:COG5805    266 RDItEKKEAEELMARSEKLSIAGQLA----------AGIAHEIRNPLTSI---KGFL-----QLLQPGIEdkeEYFDIML 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  902 SAGTDLLQLINDILDLSKVEAgkmdIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVPEqLSTDEQRLRQVLRN 981
Cdd:COG5805    328 SELDRIESIISEFLALAKPQA----VNKEKENINELIQDVVTLLETEAILHNIQIRLELLDEDPF-IYCDENQIKQVFIN 402
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  982 MLSNAVKFTEK-GKVKLRVRlvpadqvpgggADDPWLAFSVIDTGIGIAEENLSTIFGAFQqadgTTSRRygGTGLGLSI 1060
Cdd:COG5805    403 LIKNAIEAMPNgGTITIHTE-----------EEDNSVIIRVIDEGIGIPEERLKKLGEPFF----TTKEK--GTGLGLMV 465
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1228082595 1061 SRQVANLLGGELRAQSRLGAGSTFTLYVPVT 1091
Cdd:COG5805    466 SYKIIENHNGTIDIDSKVGKGTTFTITLPLS 496
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
975-1090 8.89e-16

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: 74.38  E-value: 8.89e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  975 LRQVLRNMLSNAVK-FTEKGKVKLRVrlvpadqvpggGADDPWLAFSVIDTGIGIAEENLSTIFGAFQqadgTTSRRYGG 1053
Cdd:cd16943      4 LNQVLLNLLVNAAQaMEGRGRITIRT-----------WAHVDQVLIEVEDTGSGIDPEILGRIFDPFF----TTKPVGEG 68
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1228082595 1054 TGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPV 1090
Cdd:cd16943     69 TGLGLSLSYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
1256-1370 1.15e-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: 74.43  E-value: 1.15e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDArnvlAIAEM----LKLHGLSVEHAPNGRKGIEALRDSPDiDLILMDVMMPEMDGYATTAAIRRMprfGSLP 1331
Cdd:cd17626      2 RILVVDDDA----ALAEMigivLRGEGFDPAFCGDGTQALAAFREVRP-DLVLLDLMLPGIDGIEVCRQIRAE---SGVP 73
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1228082595 1332 IIMVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:cd17626     74 IVMLTAKSDTVDVVLGLESGADDYVAKPFKPKELVARIR 112
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
824-1093 1.24e-15

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 82.67  E-value: 1.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  824 QNRDIEVK-NFEIEQARQEIEERAQQlaltskyKSEFLANMSHELRTPLTSLLILAGVLSQnsTQNLTPKQVEFAKVIES 902
Cdd:PRK10618   424 RDQDREVLvNKKLQQAQREYEKNQQA-------RKAFLQNIGDELKQPLQSLAQLAAQLRQ--TSDEEQQQPELDQLAEQ 494
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  903 AGTdLLQLINDILDLSKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAVVDPDVPEQLSTDEQRLRQVLRNM 982
Cdd:PRK10618   495 SDV-LVRLVDNIQLLNMLETQDWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLL 573
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  983 LSNAVKFTEKGKVKLRVRlvpadqvPGGGADDPwLAFSVIDTGIGIAEENLSTIFGAFqqADGTTSRRYG-GTGLGLSIS 1061
Cdd:PRK10618   574 LNYAITTTAYGKITLEVD-------QDESSPDR-LTIRILDTGAGVSIKELDNLHFPF--LNQTQGDRYGkASGLTFFLC 643
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1228082595 1062 RQVANLLGGELRAQSRLGAGSTFTLYVPVTPD 1093
Cdd:PRK10618   644 NQLCRKLGGHLTIKSREGLGTRYSIHLKMLAA 675
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
1257-1366 1.54e-15

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: 74.00  E-value: 1.54e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDArnvlAIAEMLKLH----GLSVEHAPNGRKGIEaLRDSPDIDLILMDVMMPEMDGYATTAAIRRMprfGSLPI 1332
Cdd:cd17614      1 ILVVDDEK----PISDILKFNltkeGYEVVTAYDGREALE-KVEEEQPDLILLDLMLPEKDGLEVCREVRKT---SNVPI 72
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1228082595 1333 IMVTAKAMAGDREKSLAAGASDYVTKPVDAKELL 1366
Cdd:cd17614     73 IMLTAKDSEVDKVLGLELGADDYVTKPFSNRELL 106
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
1255-1371 1.57e-15

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: 73.79  E-value: 1.57e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1255 RRVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALrDSPDIDLILMDVMMPEMDGYATTAAIRRmpRFGSLPIIM 1334
Cdd:cd17554      1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKL-ESEDPDLVILDIKMPGMDGLETLRKIRE--KKPDLPVII 77
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1228082595 1335 VTAKAMAGDREKSLAAGAsdYVTKPVDAKELLTCIRR 1371
Cdd:cd17554     78 CTAYSEYKSDFSSWAADA--YVVKSSDLTELKETIKR 112
PRK10490 PRK10490
sensor protein KdpD; Provisional
836-1101 1.59e-15

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 82.01  E-value: 1.59e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  836 EQARQEIEEraQQLaltskyKSEFLANMSHELRTPLTSLLILAGVLsqnsTQNLTPKQVEFAKVIESAGTDLL---QLIN 912
Cdd:PRK10490   652 EQARLASER--EQL------RNALLAALSHDLRTPLTVLFGQAEIL----TLDLASEGSPHARQASEIRQQVLnttRLVN 719
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  913 DILDLSKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFeavvdpDVPEQLS---TDEQRLRQVLRNMLSNAVKF 989
Cdd:PRK10490   720 NLLDMARIQSGGFNLRKEWLTLEEVVGSALQMLEPGLSGHPINL------SLPEPLTlihVDGPLFERVLINLLENAVKY 793
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  990 T-EKGKVKLRVRlvpadqvpgggADDPWLAFSVIDTGIGIAEENLSTIFGAFQQADGTTSrrYGGTGLGLSISRQVANLL 1068
Cdd:PRK10490   794 AgAQAEIGIDAH-----------VEGERLQLDVWDNGPGIPPGQEQLIFDKFARGNKESA--IPGVGLGLAICRAIVEVH 860
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1228082595 1069 GGELRAQSRLGAGSTFTLYVPVT--PDFDTAVIDM 1101
Cdd:PRK10490   861 GGTIWAENRPEGGACFRVTLPLEtpPELEEFHEDM 895
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
856-923 1.60e-15

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 72.24  E-value: 1.60e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1228082595  856 KSEFLANMSHELRTPLTSLLILAGVLsqnSTQNLTPKQVEFAKVIESAGTDLLQLINDILDLSKVEAG 923
Cdd:pfam00512    2 KSEFLANLSHELRTPLTAIRGYLELL---RDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1254-1370 3.36e-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: 3.36e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1254 GRRVLLIDDDARNVLAIAEMLKLHGLSV-EHAPNGRKGIEALRDsPDIDLILMDVMMPEMDGyatTAAIRRMPRFGSLPI 1332
Cdd:COG3707      3 GLRVLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRE-LKPDLVIVDIDMPDRDG---LEAARQISEERPAPV 78
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1228082595 1333 IMVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:COG3707     79 ILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALE 116
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
1257-1374 5.59e-15

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: 72.76  E-value: 5.59e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEH---APNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRmpRFGSLPII 1333
Cdd:cd17536      1 VLIVDDEPLIREGLKKLIDWEELGFEVvgeAENGEEALELIEEHK-PDIVITDIRMPGMDGLELIEKIRE--LYPDIKII 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1228082595 1334 MVT-------AKamagdreKSLAAGASDYVTKPVDAKELLTCIRRWIA 1374
Cdd:cd17536     78 ILSgyddfeyAQ-------KAIRLGVVDYLLKPVDEEELEEALEKAKE 118
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
975-1089 1.05e-14

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: 71.46  E-value: 1.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  975 LRQVLRNMLSNAVKFT-EKGKVKLRVRLVPAdqvpggGADdpwlaFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGG 1053
Cdd:cd16952      1 LRSAFSNLVSNAVKYTpPSDTITVRWSQEES------GAR-----LSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGG 69
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1228082595 1054 TGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVP 1089
Cdd:cd16952     70 TGLGLAIVKHVMSRHDARLLIASELGKGSRFTCLFP 105
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
970-1089 1.07e-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: 71.55  E-value: 1.07e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  970 TDEQRLRQVLRNMLSNAVKFT-EKGKVKLRVRlvpadqvpgggADDPWLAFSVIDTGIGIAEENLSTIFGAFqqADGTTS 1048
Cdd:cd16948      1 TDAKWLSFIIGQIVSNALKYSkQGGKIEIYSE-----------TNEQGVVLSIKDFGIGIPEEDLPRVFDKG--FTGENG 67
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1228082595 1049 RRYG-GTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVP 1089
Cdd:cd16948     68 RNFQeSTGMGLYLVKKLCDKLGHKIDVESEVGEGTTFTITFP 109
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
1256-1374 2.36e-14

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 74.08  E-value: 2.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEML-KLHGLS-VEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRfgSLPII 1333
Cdd:COG3279      3 KILIVDDEPLARERLERLLeKYPDLEvVGEASNGEEALELLEEHK-PDLVFLDIQMPGLDGFELARQLRELDP--PPPII 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1228082595 1334 MVTAkamagDREKSLAA---GASDYVTKPVDAKELLTCIRRWIA 1374
Cdd:COG3279     80 FTTA-----YDEYALEAfevNAVDYLLKPIDEERLAKALEKAKE 118
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
1256-1370 3.68e-14

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


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 70.07  E-value: 3.68e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDA--RNVLAIAemLKLHGLSVEHAPNGRKGIEALRD-SPDidLILMDVMMPEMDGYATTAAIRRMPrfGSLPI 1332
Cdd:cd17615      1 RVLVVDDEPniTELLSMA--LRYEGWDVETAADGAEALAAAREfRPD--AVVLDIMLPDMDGLEVLRRLRADG--PDVPV 74
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1228082595 1333 IMVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:cd17615     75 LFLTAKDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLR 112
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
1255-1369 3.85e-14

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: 70.13  E-value: 3.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1255 RRVLLIDDDARNVLAIAEMLKLHGLSV-EHAPNGRKGIEALRDSPdIDLILMDVMMP-EMDGYATTAAIRrmpRFGSLPI 1332
Cdd:cd17534      1 KKILIVEDEAIIALDLKEILESLGYEVvGIADSGEEAIELAEENK-PDLILMDINLKgDMDGIEAAREIR---EKFDIPV 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1228082595 1333 IMVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCI 1369
Cdd:cd17534     77 IFLTAYSDEETLERAKETNPYGYLVKPFNERELKAAI 113
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
950-1089 8.83e-14

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 74.88  E-value: 8.83e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  950 AEKGLEFEAVVDPDVPEQLSTDEQrLRQVLRNMLSNAV-----KFTEKGKVKLRVRlvpadqvpgggADDPWLAFSVIDT 1024
Cdd:COG3290    258 RERGIDLTIDIDSDLPDLPLSDTD-LVTILGNLLDNAIeavekLPEEERRVELSIR-----------DDGDELVIEVEDS 325
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1228082595 1025 GIGIAEENLSTIFgafqqADGTTSRRYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVP 1089
Cdd:COG3290    326 GPGIPEELLEKIF-----ERGFSTKLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLP 385
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
1257-1370 1.47e-13

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: 68.20  E-value: 1.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEaLRDSPDIDLILMDVMMPEMDGYATTAAIR--RMPRfgslPIIM 1334
Cdd:cd17616      1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLD-LGKLYDYDIILLDLNLPDMSGYEVLRTLRlaKVKT----PILI 75
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1228082595 1335 VTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:cd17616     76 LSGLADIEDKVKGLGFGADDYMTKPFHKDELVARIH 111
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
1256-1371 2.05e-13

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 71.64  E-value: 2.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPDiDLILMDVMMPEMDGYATTAAIRRmprFGSLPIIMV 1335
Cdd:PRK10710    12 RILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPP-DLILLDLMLPGTDGLTLCREIRR---FSDIPIVMV 87
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1228082595 1336 TAKAMAGDREKSLAAGASDYVTKPVDAKELL----TCIRR 1371
Cdd:PRK10710    88 TAKIEEIDRLLGLEIGADDYICKPYSPREVVarvkTILRR 127
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
956-1086 2.17e-13

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: 68.31  E-value: 2.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  956 FEAVVD-PDVPEQLSTDEQRLRQVLRNMLSNAVKFTEKGK---VKLRvrlvpadqvpgggADDPWLAFSVIDTGIGIAEE 1031
Cdd:cd16947      1 FQVEINiPDRPIYANANTEALQRILKNLISNAIKYGSDGKflgMTLR-------------EDEKHVYIDIWDKGKGISET 67
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1228082595 1032 NLSTIFGAFQQADGTTSRRYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTL 1086
Cdd:cd16947     68 EKDHVFERLYTLEDSRNSAKQGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTV 122
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
625-799 2.50e-13

Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 69.92  E-value: 2.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  625 LARISGLLQGHRDLRAVTQLIMNELTPLVGAQYGTFFL-KEQGERLRLLASYGGAESGQGATEYELGQSLLGQVASTRKA 703
Cdd:COG3605      6 LRRISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLlDPDGGRLELRATEGLNPEAVGKVRLPLGEGLVGLVAERGEP 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  704 ILVE--QTPPDYVRIsSSLGSAPPVNLIVLPIVFEEQVVGVIELASFTRFSLVQRDflEQLMESIGVNVNTIVANARtdv 781
Cdd:COG3605     86 LNLAdaASHPRFKYF-PETGEEGFRSFLGVPIIRRGRVLGVLVVQSREPREFTEEE--VEFLVTLAAQLAEAIANAE--- 159
                          170
                   ....*....|....*...
gi 1228082595  782 LLEESQRLAAELSVRTEE 799
Cdd:COG3605    160 LLGELRAALAELSLAREE 177
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
1255-1371 2.50e-13

phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response regulator CheY contains a stand-alone REC domain. Chemotaxis is a behavior known for motile bacteria that directs their movement in response to chemical gradients. CheY is involved in transmitting sensory signals from chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 67.69  E-value: 2.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1255 RRVLLIDDDARNVLAIAEMLKLHGLS-VEHAPNGRKGIEALRDSpDIDLILMDVMMPEMDGYATTAAIRRMPRfgSLPII 1333
Cdd:cd17542      1 KKVLIVDDAAFMRMMLKDILTKAGYEvVGEAANGEEAVEKYKEL-KPDLVTMDITMPEMDGIEALKEIKKIDP--NAKVI 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1228082595 1334 MVTAkamAGDRE---KSLAAGASDYVTKPVDAKELLTCIRR 1371
Cdd:cd17542     78 MCSA---MGQEEmvkEAIKAGAKDFIVKPFQPERVLEAVEK 115
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
847-1083 3.11e-13

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 72.69  E-value: 3.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  847 QQLALTSKYKSEFLANMSHELRTPLTSLLILAGVLSQNSTQNLTP--KQVE-FAKVIES------AGTDL-------LQL 910
Cdd:PRK10755   128 SRLTSTLDQERLFTADVAHELRTPLAGIRLHLELLEKQHHIDVAPliARLDqMMHTVEQllqlarAGQSFssghyqtVKL 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  911 INDILDLSKVEAGkmdihpELVELRQQveyvRTTFQPLTAEKGLEFEAVVdpdvpeqlstdeqrLRQVLRNMLSNAVKFT 990
Cdd:PRK10755   208 LEDVILPSQDELS------EMLEQRQQ----TLLLPESAADITVQGDATL--------------LRLLLRNLVENAHRYS 263
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  991 EKGKvKLRVRLVpadqvpgggADDPWLAFSVIDTGIGIAEENLSTIFGAFQQADgttsRRYGGTGLGLSISRQVANLLGG 1070
Cdd:PRK10755   264 PEGS-TITIKLS---------QEDGGAVLAVEDEGPGIDESKCGELSKAFVRMD----SRYGGIGLGLSIVSRITQLHHG 329
                          250
                   ....*....|...
gi 1228082595 1071 ELRAQSRLGAGST 1083
Cdd:PRK10755   330 QFFLQNRQERSGT 342
PRK11517 PRK11517
DNA-binding response regulator HprR;
1256-1370 4.17e-13

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 70.31  E-value: 4.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIE-ALRDspDIDLILMDVMMPEMDGYATTAAIRRMPRfgsLPIIM 1334
Cdd:PRK11517     2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYlALKD--DYALIILDIMLPGMDGWQILQTLRTAKQ---TPVIC 76
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1228082595 1335 VTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:PRK11517    77 LTARDSVDDRVRGLDSGANDYLVKPFSFSELLARVR 112
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
1257-1376 4.55e-13

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: 69.36  E-value: 4.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGrkgiEALRDSPDIDL---ILMDVMMPEMDGYATTAAIRRMPRfgSLPII 1333
Cdd:COG4566      2 VYIVDDDEAVRDSLAFLLESAGLRVETFASA----EAFLAALDPDRpgcLLLDVRMPGMSGLELQEELAARGS--PLPVI 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1228082595 1334 MVTAkamAGDRE---KSLAAGASDYVTKPVDAKELLTCIRRWIAAA 1376
Cdd:COG4566     76 FLTG---HGDVPmavRAMKAGAVDFLEKPFDDQALLDAVRRALARD 118
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
856-919 5.57e-13

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: 64.93  E-value: 5.57e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1228082595  856 KSEFLANMSHELRTPLTSLLILAGVLSQNSTQNltPKQVEFAKVIESAGTDLLQLINDILDLSK 919
Cdd:cd00082      4 KGEFLANVSHELRTPLTAIRGALELLEEELLDD--EEQREYLERIREEAERLLRLINDLLDLSR 65
ompR PRK09468
osmolarity response regulator; Provisional
1254-1370 6.54e-13

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 70.00  E-value: 6.54e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1254 GRRVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGrKGIEALRDSPDIDLILMDVMMPEMDGYAttaAIRRMPRFGS-LPI 1332
Cdd:PRK09468     5 NYKILVVDDDMRLRALLERYLTEQGFQVRSAANA-EQMDRLLTRESFHLMVLDLMLPGEDGLS---ICRRLRSQNNpTPI 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1228082595 1333 IMVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:PRK09468    81 IMLTAKGEEVDRIVGLEIGADDYLPKPFNPRELLARIR 118
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
1257-1370 1.06e-12

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: 66.07  E-value: 1.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPDiDLILMDVMMPEMDGYATTAAIRRmpRFGSLPIIMVT 1336
Cdd:cd17572      1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPP-DVVLLDLKLPDMSGMEILKWIQE--RSLPTSVIVIT 77
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1228082595 1337 AKA---MAGDrekSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:cd17572     78 AHGsvdIAVE---AMRLGAYDFLEKPFDADRLRVTVR 111
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
861-1090 1.12e-12

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 72.13  E-value: 1.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  861 ANMSHELRTPLTSLLILAGVLSQNSTQNLTPKQVefAKVIESAGTDLLQLINDILDLSKveagKMDIHPELVELRQQVEY 940
Cdd:PRK10364   242 AGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQL--AQVMAKEADRLNRVVSELLELVK----PTHLALQAVDLNDLINH 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  941 VRTTFQPLTAEKGLEFEAVVDPDVPEqLSTDEQRLRQVLRNMLSNAVKFTEKGKVKLrvrlVPADQVPGGgaddpwLAFS 1020
Cdd:PRK10364   316 SLQLVSQDANSREIQLRFTANDTLPE-IQADPDRLTQVLLNLYLNAIQAIGQHGVIS----VTASESGAG------VKIS 384
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1021 VIDTGIGIAEENLSTIFGAFqqadGTTSRRygGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPV 1090
Cdd:PRK10364   385 VTDSGKGIAADQLEAIFTPY----FTTKAE--GTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLPV 448
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
1255-1366 1.29e-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: 67.63  E-value: 1.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1255 RRVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRmpRFGSLPIIM 1334
Cdd:COG4567      5 RSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAP-PDYAVLDLRLGDGSGLDLIEALRE--RDPDARIVV 81
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1228082595 1335 VTAKAMAGDREKSLAAGASDYVTKPVDAKELL 1366
Cdd:COG4567     82 LTGYASIATAVEAIKLGADDYLAKPADADDLL 113
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
1257-1359 1.43e-12

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: 65.11  E-value: 1.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRD-SPDIDLILMDVMMPEMDGYATTAAIRRMPRFGSLPIIMV 1335
Cdd:cd17582      1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDeQNEIDLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMM 80
                           90       100
                   ....*....|....*....|....
gi 1228082595 1336 TAKAMAGDREKSLAAGASDYVTKP 1359
Cdd:cd17582     81 SSQDSVGVVFKCLSKGAADYLVKP 104
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
964-1086 1.94e-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: 65.94  E-value: 1.94e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  964 VPEQLSTDEQRLRQVLRNMLSNAVKFTEK-GKVKLRVRLVPADQVPGGGADDPWLAFS-----VIDTGIGIAEENLSTIF 1037
Cdd:cd16938      1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGgGNITFRVFLEGGSEDRSDRDWGPWRPSMsdesvEIRFEVEINDSGSPSIE 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1228082595 1038 GAFQQAdgTTSRRYG----GTGLGLSISRQVANLLGGELRAQSRLGAGSTFTL 1086
Cdd:cd16938     81 SASMRN--SLNRRYNlselGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSL 131
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
975-1089 1.97e-12

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: 64.65  E-value: 1.97e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  975 LRQVLRNMLSNAVKFTeKGKVKLrvrlvpadqvpGGGADDPWLAFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGT 1054
Cdd:cd16949      1 LARALENVLRNALRYS-PSKILL-----------DISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGT 68
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1228082595 1055 GLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVP 1089
Cdd:cd16949     69 GLGLAIAERAIEQHGGKIKASNRKPGGLRVRIWLP 103
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
1257-1370 2.28e-12

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 65.00  E-value: 2.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRfgSLPIIMVT 1336
Cdd:cd19934      1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEP-YDLVVLDLGLPGMDGLSVLRRWRSEGR--ATPVLILT 77
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1228082595 1337 AKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:cd19934     78 ARDSWQDKVEGLDAGADDYLTKPFHIEELLARLR 111
PRK10604 PRK10604
sensor protein RstB; Provisional
862-1094 2.36e-12

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 70.79  E-value: 2.36e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  862 NMSHELRTPLTSL---LILAGVLSQNSTQNLTpkqvefakviesagTDLLQL---INDILDLSKVEAGKMDIHPELVELR 935
Cdd:PRK10604   218 GIAHELRTPLVRLryrLEMSDNLSAAESQALN--------------RDIGQLealIEELLTYARLDRPQNELHLSEPDLP 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  936 QQVEYVRTTFQPLTAEKGLEFEAVVDPDVpeqLSTDEQRLRQVLRNMLSNAVKFTEKgkvKLRVRL-VPADQVpgggadd 1014
Cdd:PRK10604   284 AWLSTHLADIQAVTPEKTVRLDTPHQGDY---GALDMRLMERVLDNLLNNALRYAHS---RVRVSLlLDGNQA------- 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1015 pwlAFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGTGLGLSISRQVANLLGGELRA-QSRLGaGSTFTLYVPVTPD 1093
Cdd:PRK10604   351 ---CLIVEDDGPGIPPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCdESELG-GARFSFSWPVWHN 426

                   .
gi 1228082595 1094 F 1094
Cdd:PRK10604   427 L 427
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
1257-1359 3.38e-12

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 64.00  E-value: 3.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDaRNVLAIAEM-LKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMprfGSLPIIMV 1335
Cdd:cd19936      1 IALVDDD-RNILTSVSMaLEAEGFSVETYTDGASALDGLNARP-PDLAILDIKMPRMDGMELLQRLRQK---STLPVIFL 75
                           90       100
                   ....*....|....*....|....
gi 1228082595 1336 TAKAMAGDREKSLAAGASDYVTKP 1359
Cdd:cd19936     76 TSKDDEIDEVFGLRMGADDYITKP 99
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
1256-1359 3.39e-12

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: 64.06  E-value: 3.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPDIDLILMDVMMPEMDGYATTAAIRRM-PrfgSLPIIM 1334
Cdd:cd18160      1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDIDIVVTDIVMPEMDGIELAREARKIdP---DVKILF 77
                           90       100
                   ....*....|....*....|....*
gi 1228082595 1335 VTAKAMAGDREKSLAAGASDYVTKP 1359
Cdd:cd18160     78 ISGGAAAAPELLSDAVGDNATLKKP 102
glnL PRK11073
nitrogen regulation protein NR(II);
835-1090 3.63e-12

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 69.34  E-value: 3.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  835 IEQAR---QEIEERAQQLAltskyKSEFLANMSHELRTPLTSLLILAGVLSQNSTQnltPKQVEFAKVIESAGTDLLQLI 911
Cdd:PRK11073   111 MDNQRrlsQEQLQHAQQVA-----ARDLVRGLAHEIKNPLGGLRGAAQLLSKALPD---PALTEYTKVIIEQADRLRNLV 182
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  912 NDILDLSKVEAGKMD-IHPELVELRQQVEyvrttfqpLTAEKGLEFEAVVDPDVPEqLSTDEQRLRQVLRNMLSNAVKFT 990
Cdd:PRK11073   183 DRLLGPQRPGTHVTEsIHKVAERVVQLVS--------LELPDNVRLIRDYDPSLPE-LAHDPDQIEQVLLNIVRNALQAL 253
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  991 EK--GKVKLRVRlvPADQVPGGGADDPWLA-FSVIDTGIGIAEENLSTIFGAFqqadgtTSRRYGGTGLGLSISRQVANL 1067
Cdd:PRK11073   254 GPegGTITLRTR--TAFQLTLHGERYRLAArIDIEDNGPGIPPHLQDTLFYPM------VSGREGGTGLGLSIARNLIDQ 325
                          250       260
                   ....*....|....*....|...
gi 1228082595 1068 LGGELRAQSRLGAgSTFTLYVPV 1090
Cdd:PRK11073   326 HSGKIEFTSWPGH-TEFSVYLPI 347
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
1256-1365 4.33e-12

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 67.29  E-value: 4.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDArnvlAIAE----MLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTaaiRRMPRFGS-L 1330
Cdd:PRK11083     5 TILLVEDEQ----AIADtlvyALQSEGFTVEWFERGLPALDKLRQQP-PDLVILDVGLPDISGFELC---RQLLAFHPaL 76
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1228082595 1331 PIIMVTAKAMAGDREKSLAAGASDYVTKPVDAKEL 1365
Cdd:PRK11083    77 PVIFLTARSDEVDRLVGLEIGADDYVAKPFSPREV 111
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
1301-1359 7.65e-12

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: 63.16  E-value: 7.65e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1228082595 1301 DLILMDVMMPEMDGYATTAAIRRMPRFGSLPIIMVTAKAMAGDREKSLAAGASDYVTKP 1359
Cdd:cd17602     44 DLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTGKDGLVDRIRAKMAGASGYLTKP 102
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
975-1081 8.91e-12

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: 63.19  E-value: 8.91e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  975 LRQVLRNMLSNAVKFT-EKGKVKLRVRLVPADQvpgggaddpwlaFSVIDTGIGIAEENLSTIFGAFQQADGTTsrrYGG 1053
Cdd:cd16940     14 LFLLLRNLVDNAVRYSpQGSRVEIKLSADDGAV------------IRVEDNGPGIDEEELEALFERFYRSDGQN---YGG 78
                           90       100
                   ....*....|....*....|....*...
gi 1228082595 1054 TGLGLSISRQVANLLGGELRAQSRLGAG 1081
Cdd:cd16940     79 SGLGLSIVKRIVELHGGQIFLGNAQGGG 106
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
1253-1370 1.10e-11

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 66.28  E-value: 1.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1253 LGRRVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALrDSPDIDLILMDVMMPEMDGYATTAAIRRMPRFGSLPI 1332
Cdd:PRK10161     1 MARRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQL-NEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPV 79
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1228082595 1333 IMVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:PRK10161    80 VMLTARGEEEDRVRGLETGADDYITKPFSPKELVARIK 117
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
975-1081 1.11e-11

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: 62.47  E-value: 1.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  975 LRQVLRNMLSNAVKFtekGKVKLRVRlvpadqvpgGGADDPWLAFSVIDTGIGIAEENLSTIFGAFQQADgtTSRRYGGT 1054
Cdd:cd16950      1 LKRVLSNLVDNALRY---GGGWVEVS---------SDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGD--NARGTSGT 66
                           90       100
                   ....*....|....*....|....*..
gi 1228082595 1055 GLGLSISRQVANLLGGELRAQSRLGAG 1081
Cdd:cd16950     67 GLGLAIVQRISDAHGGSLTLANRAGGG 93
resp_reg_YycF NF040534
response regulator YycF;
1255-1366 1.17e-11

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 66.28  E-value: 1.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1255 RRVLLIDDDArnvlAIAEMLKLH----GLSVEHAPNGRKGIE-ALRDSPDidLILMDVMMPEMDGYATTAAIRRMPRFgs 1329
Cdd:NF040534     1 KKILVVDDEK----PIADILEFNlkkeGYEVFCAYDGNEALElVEEEVPD--LVLLDIMLPGRDGMEVCREVRKKYDM-- 72
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1228082595 1330 lPIIMVTAKAMAGDREKSLAAGASDYVTKPVDAKELL 1366
Cdd:NF040534    73 -PIIMLTAKDSEIDKVLGLELGADDYVTKPFSTRELI 108
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
975-1089 1.69e-11

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: 62.03  E-value: 1.69e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  975 LRQVLRNMLSNAVKFTEKGKVKLRVRLVPADQvpgggADDPWLAFSVIDTGIGIAEENLSTIFGAFqqadgtTSRRYGGT 1054
Cdd:cd16920      1 IQQVLINLVRNGIEAMSEGGCERRELTIRTSP-----ADDRAVTISVKDTGPGIAEEVAGQLFDPF------YTTKSEGL 69
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1228082595 1055 GLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVP 1089
Cdd:cd16920     70 GMGLSICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
975-1086 1.73e-11

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: 62.09  E-value: 1.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  975 LRQVLRNMLSNAVKFTEKgkvklrvRLVPADQVPGGGADDPWLaFSVIDTGIGIAEENLSTIFGAFqqadgTTSRRYG-G 1053
Cdd:cd16976      1 IQQVLMNLLQNALDAMGK-------VENPRIRIAARRLGGRLV-LVVRDNGPGIAEEHLSRVFDPF-----FTTKPVGkG 67
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1228082595 1054 TGLGLSISRQVANLLGGELRAQSRLGAGSTFTL 1086
Cdd:cd16976     68 TGLGLSISYGIVEEHGGRLSVANEEGAGARFTF 100
PRK15479 PRK15479
transcriptional regulator TctD;
1256-1370 2.08e-11

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 65.13  E-value: 2.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGiEALRDSPDIDLILMDVMMPEMDGYATTAAIRRmpRFGSLPIIMV 1335
Cdd:PRK15479     2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAA-DHLLQSEMYALAVLDINMPGMDGLEVLQRLRK--RGQTLPVLLL 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1228082595 1336 TAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:PRK15479    79 TARSAVADRVKGLNVGADDYLPKPFELEELDARLR 113
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
813-1079 2.21e-11

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 68.04  E-value: 2.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  813 ELEEKAELLA----RQNRDIEVKNFEIEQARQEIEERAQQLALTSKYKSEFLANMSHELRTPLTSLlilagvlsQNSTQN 888
Cdd:PRK09470   196 KLKNAADEVAqgnlRQHPELETGPQEFRQAGASFNQMVTALERMMTSQQRLLSDISHELRTPLTRL--------QLATAL 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  889 LTPKQVEFAKV--IESAGTDLLQLINDILDLSkveagkmdihpelvelRQQV--EYVRTTFqPLT-------------AE 951
Cdd:PRK09470   268 LRRRQGESKELerIETEAQRLDSMINDLLVLS----------------RNQQknHLERETF-KANslwsevledakfeAE 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  952 K-GLEFEAVVDPDvPEQLSTDEQRLRQVLRNMLSNAVKFtekGKVKLRVRLVpadqvpgggADDPWLAFSVIDTGIGIAE 1030
Cdd:PRK09470   331 QmGKSLTVSAPPG-PWPINGNPNALASALENIVRNALRY---SHTKIEVAFS---------VDKDGLTITVDDDGPGVPE 397
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1031 ENLSTIFGAFQQADGTTSRRYGGTGLGLSISRQVANLLGGELRA-QSRLG 1079
Cdd:PRK09470   398 EEREQIFRPFYRVDEARDRESGGTGLGLAIVENAIQQHRGWVKAeDSPLG 447
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
1256-1360 2.38e-11

phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and similar proteins; Plant ethylene receptors contain N-terminal transmembrane domains that contain an ethylene binding site and also serve in localization of the receptor to the endoplasmic reticulum or the Golgi apparatus and a C-terminal histidine kinase (HK)-like domain. There are five ethylene receptors (ETR1, ERS1, ETR2, ERS2, and EIN4) in Arabidopsis thaliana. ETR1, ETR2, and EIN4 also contain REC domains C-terminal to the HK domain. ETR1 and ERS1 belong to subfamily 1, and have functional HK domains while ETR2, ERS2, and EIN4 belong to subfamily 2, and lack the necessary residues for HK activity and may function as serine/threonine kinases. The plant hormone ethylene plays an important role in plant growth and development. It regulates seed germination, seedling growth, leaf and petal abscission, fruit ripening, organ senescence, and pathogen responses. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 62.03  E-value: 2.38e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEAL-RDSPDIDLILMDVMMPEMDGYATTAAIR-RMPRFGSLPII 1333
Cdd:cd19933      2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLaSAEHSFQLVLLDLCMPEMDGFEVALRIRkLFGRRERPLIV 81
                           90       100
                   ....*....|....*....|....*..
gi 1228082595 1334 MVTAKAMAGDREKSLAAGASDYVTKPV 1360
Cdd:cd19933     82 ALTANTDDSTREKCLSLGMNGVITKPV 108
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
1256-1366 2.53e-11

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: 62.02  E-value: 2.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGrKGIEALRDSPDIDLILMDVMMPEMDGYATTAAIRRMPRFGslpIIMV 1335
Cdd:cd17619      2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDG-EEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSEVG---IILV 77
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1228082595 1336 TAKAMAGDREKSLAAGASDYVTKPVDAKELL 1366
Cdd:cd17619     78 TGRDDEVDRIVGLEIGADDYVTKPFNPRELL 108
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
900-1092 3.06e-11

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 68.17  E-value: 3.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  900 IESAGTDLLQLINDILDLSKVEAGKmdIHP-ELVELRQQVEYVRTTFQPLTAEKGLEFE---AVVDPDvPEQLstdeqrl 975
Cdd:PRK13837   492 IISAGARARLIIDQILAFGRKGERN--TKPfDLSELVTEIAPLLRVSLPPGVELDFDQDqepAVVEGN-PAEL------- 561
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  976 RQVLRNMLSNAVK-FTEKGKVKLRVR--LVPADQVPGGGADDP--WLAFSVIDTGIGIAEENLSTIFGAFqqadGTTsrR 1050
Cdd:PRK13837   562 QQVLMNLCSNAAQaMDGAGRVDISLSraKLRAPKVLSHGVLPPgrYVLLRVSDTGAGIDEAVLPHIFEPF----FTT--R 635
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1228082595 1051 YGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPVTP 1092
Cdd:PRK13837   636 AGGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLPPSS 677
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
95-611 3.63e-11

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 67.35  E-value: 3.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595   95 SVNAMAGNLTAQVRDIAGVATAVARGDLSQKITVQVRGELLELKNTINTMVDQLSSFADEVTRVAREVGSEGRLGGQAEV 174
Cdd:COG0840     12 LALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  175 PGVAGTWRDLTTSVNFMAGNLTAQVRSIAEVTTAVAKGDLSQKITVDARGEILELKSTINTMVDQLSSFADEVTRVAREV 254
Cdd:COG0840     92 LLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAA 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  255 GTEGILGGQAQVPGVAGTWRDLTTSV--NFMAGNLTAQVRSIAQVATAVARGDLSQKITVDARGEIFELKSTINTMVDQL 332
Cdd:COG0840    172 LALAAAALALALLAAALLALVALAIIlaLLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENL 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  333 SSFADEVTRVAREVGTEGRlggqadvkgvsgtwkGLTESVNVMADNLTDQVRSIAQVSAAVArgDLSQRITveakgEVAG 412
Cdd:COG0840    252 RELVGQVRESAEQVASASE---------------ELAASAEELAAGAEEQAASLEETAAAME--ELSATVQ-----EVAE 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  413 LAQTINTMVDTLSAFADEVTRVAREVgTEGILGGQARVANVAGTWKDLTDNVNSMaNNLTGQVRSIAQVTTAVA------ 486
Cdd:COG0840    310 NAQQAAELAEEASELAEEGGEVVEEA-VEGIEEIRESVEETAETIEELGESSQEI-GEIVDVIDDIAEQTNLLAlnaaie 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  487 --------RG---------NLSQKIDVDARgeilELKTTINTMVDTLSSFAAEVTRVAREVGKEGQLGGQAE--VEGVSG 547
Cdd:COG0840    388 aarageagRGfavvadevrKLAERSAEATK----EIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGeaLEEIVE 463
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1228082595  548 TWKRLTENVNELAGNLTRQVRAIAEVTSAVATGDLTRSITVEAKGEVSELKDNINAMVRSLRET 611
Cdd:COG0840    464 AVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQEL 527
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
1257-1359 3.90e-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: 61.06  E-value: 3.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALrDSPDIDLILMDVMMPEMDGyatTAAIRRMPRFGSLPIIMVT 1336
Cdd:cd17621      1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEF-DRAGADIVLLDLMLPGLSG---TEVCRQLRARSNVPVIMVT 76
                           90       100
                   ....*....|....*....|...
gi 1228082595 1337 AKAMAGDREKSLAAGASDYVTKP 1359
Cdd:cd17621     77 AKDSEIDKVVGLELGADDYVTKP 99
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
1257-1370 5.03e-11

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 60.92  E-value: 5.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMprfGSLPIIMVT 1336
Cdd:cd17594      2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRR-VDLVLLDLRLGQESGLDLLRTIRAR---SDVPIIIIS 77
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1228082595 1337 A-KAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:cd17594     78 GdRRDEIDRVVGLELGADDYLAKPFGLRELLARVR 112
PRK10610 PRK10610
chemotaxis protein CheY;
1256-1365 7.73e-11

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 61.14  E-value: 7.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGL-SVEHAPNGRKGIEALRDSpDIDLILMDVMMPEMDGYATTAAIRRMPRFGSLPIIM 1334
Cdd:PRK10610     7 KFLVVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALNKLQAG-GFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLM 85
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1228082595 1335 VTAKAMAGDREKSLAAGASDYVTKPVDAKEL 1365
Cdd:PRK10610    86 VTAEAKKENIIAAAQAGASGYVVKPFTAATL 116
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
1257-1374 8.36e-11

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 65.82  E-value: 8.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRfgSLPIIMVT 1336
Cdd:PRK10365     8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQV-FDLVLCDVRMAEMDGIATLKEIKALNP--AIPVLIMT 84
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1228082595 1337 AKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRRWIA 1374
Cdd:PRK10365    85 AYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALA 122
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
1258-1367 8.81e-11

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: 60.63  E-value: 8.81e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1258 LLIDDDARnvLAIAEMLKL----HGLSVEHAPNGRKGIEALRDSpDIDLILMDVMMPEMDGYATTAAIRRMPRfgSLPII 1333
Cdd:cd17593      3 VLICDDSS--MARKQLARAlpadWDVEITFAENGEEALEILREG-RIDVLFLDLTMPVMDGYEVLEALPVEQL--ETKVI 77
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1228082595 1334 MVTAKAMAGDREKSLAAGASDYVTKPVDAKELLT 1367
Cdd:cd17593     78 VVSGDVQPEAKERVLELGALAFLKKPFDPEKLAQ 111
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
1256-1310 1.14e-10

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: 57.96  E-value: 1.14e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1228082595  1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRdSPDIDLILMDVMMP 1310
Cdd:smart00448    2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLK-EEKPDLILLDIMMP 55
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
1257-1371 1.26e-10

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: 59.82  E-value: 1.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMprFGSLPIIMVT 1336
Cdd:cd17550      1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERR-PDLVLLDIWLPDMDGLELLKEIKEK--YPDLPVIMIS 77
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1228082595 1337 AKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRR 1371
Cdd:cd17550     78 GHGTIETAVKATKLGAYDFIEKPLSLDRLLLTIER 112
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
975-1090 1.96e-10

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: 58.98  E-value: 1.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  975 LRQVLRNMLSNAVKFTEKgkvklRVRLVPADQvpgggadDPWLAFSVIDTGIGIAEENLSTIFGAFQQADGTTSRRYGGT 1054
Cdd:cd16939      1 MARALDNLLRNALRYAHR-----TVRIALLVS-------GGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGF 68
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1228082595 1055 GLGLSISRQVANLLGGELRA-QSRLGaGSTFTLYVPV 1090
Cdd:cd16939     69 GLGLAIVHRVALWHGGHVECdDSELG-GACFRLTWPR 104
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
975-1089 1.98e-10

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: 59.12  E-value: 1.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  975 LRQVLRNMLSNAVKFTEKGKVKLRVRLvpadqvpGGGADDpwLAFSVIDTGIGIAEENLSTIFGAFQqADGTTSRRYG-G 1053
Cdd:cd16953      1 LGQVLRNLIGNAISFSPPDTGRITVSA-------MPTGKM--VTISVEDEGPGIPQEKLESIFDRFY-TERPANEAFGqH 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1228082595 1054 TGLGLSISRQVANLLGG----ELRAQSRLGAGSTFTLYVP 1089
Cdd:cd16953     71 SGLGLSISRQIIEAHGGisvaENHNQPGQVIGARFTVQLP 110
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
1255-1369 2.46e-10

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: 59.35  E-value: 2.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1255 RRVLLIDDDARNVLAIAEMLKLHGLSV-EHAPNGRKGIE-ALRDSPDidLILMDVMMPEMDGyATTAAIRRMPRFGslPI 1332
Cdd:cd19932      1 VRVLIAEDEALIRMDLREMLEEAGYEVvGEASDGEEAVElAKKHKPD--LVIMDVKMPRLDG-IEAAKIITSENIA--PI 75
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1228082595 1333 IMVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCI 1369
Cdd:cd19932     76 VLLTAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAI 112
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
88-485 3.05e-10

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 64.66  E-value: 3.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595   88 TWKDLTESVNAMAGNLTAQVRDIAGVATAVARGDLSQKITVQVRGELLELKNTINTMVDQLSSFADEVTRVAREVGSEGR 167
Cdd:COG0840     99 ALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAA 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  168 LGGQAEVPGVAGTWRDLTTSVNFMAGNLTAQVRSIAEVTTAVAKGDLSQKITVDARGEILELKSTINTMVDQLSSFADEV 247
Cdd:COG0840    179 LALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQV 258
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  248 TRVAREvgtegilggqaqvpgVAGTWRDLTTSVNFMAGNLTAQVRSIAQVATAVArgdlsqkitvdargeifELKSTINT 327
Cdd:COG0840    259 RESAEQ---------------VASASEELAASAEELAAGAEEQAASLEETAAAME-----------------ELSATVQE 306
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  328 MVDQlssfADEVTRVAREVGTEGRLGGQAdVKGVSGTWKGLTESVNVMAD---NLTDQVRSIAQVS-------------- 390
Cdd:COG0840    307 VAEN----AQQAAELAEEASELAEEGGEV-VEEAVEGIEEIRESVEETAEtieELGESSQEIGEIVdviddiaeqtnlla 381
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  391 --AAV--AR-GD--------------LSQRiTVEAKGEVAGLAQTINTMVDTLSAFADEVTRVAREvGTEGILGGQARVA 451
Cdd:COG0840    382 lnAAIeaARaGEagrgfavvadevrkLAER-SAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEE-GVELVEEAGEALE 459
                          410       420       430
                   ....*....|....*....|....*....|....
gi 1228082595  452 NVAGTWKDLTDNVNSMANNLTGQVRSIAQVTTAV 485
Cdd:COG0840    460 EIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAI 493
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
637-787 3.76e-10

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: 59.70  E-value: 3.76e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595   637 DLRAVTQLIMNELTPLVGAQYGTFFLKEQGER--LRLLASYGGAESGQGAtEYELGQSLLGQVASTRKAILVEQTPPDYV 714
Cdd:smart00065    1 DLEELLQTILEELRQLLGADRVLIYLVDENDRgeLVLVAADGLTLPTLGI-RFPLDEGLAGRVAETGRPLNIPDVEADPL 79
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1228082595   715 RISSSLGSAPPV-NLIVLPIVFEEQVVGVIELASFTRfslvQRDFL---EQLMESIGVNVNTIVANARtdvLLEESQ 787
Cdd:smart00065   80 FAEDLLGRYQGVrSFLAVPLVADGELVGVLALHNKKS----PRPFTeedEELLQALANQLAIALANAQ---LYEELR 149
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
971-1072 3.83e-10

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: 58.24  E-value: 3.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  971 DEQRLRQVLRNMLSNAVKFT-EKGKVKLRVRLvpadqvpgggaDDPWLAFSVIDTGIGIAEENLSTIFGAFQQADgtTSR 1049
Cdd:cd16975      1 DTLLLSRALINIISNACQYApEGGTVSISIYD-----------EEEYLYFEIWDNGHGFSEQDLKKALELFYRDD--TSR 67
                           90       100
                   ....*....|....*....|....
gi 1228082595 1050 RYGG-TGLGLSISRQVANLLGGEL 1072
Cdd:cd16975     68 RSGGhYGMGLYIAKNLVEKHGGSL 91
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
1256-1371 3.88e-10

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


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 58.44  E-value: 3.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDA--RNVLAIAemLKLHGLSVEHAPNGRKGIEAL-RDSPDidLILMDVMMPEMDGYATTAAIRRmpRFGSLPI 1332
Cdd:cd19919      2 TVWIVDDDSsiRWVLERA--LAGAGLTVTSFENAQEALAALaSSQPD--VLISDIRMPGMDGLALLAQIKQ--RHPDLPV 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1228082595 1333 IMVTAKAmagDREKSLAA---GASDYVTKPVDAKELLTCIRR 1371
Cdd:cd19919     76 IIMTAHS---DLDSAVSAyqgGAFEYLPKPFDIDEAVALVER 114
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
975-1089 9.63e-10

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: 57.01  E-value: 9.63e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  975 LRQVLRNMLSNAVKFTEKgkvKLRVRLVPADqvpgggaDDPWLAFSVIDTGIGIAEENLSTIFGAFQQADgtTSRRYGGT 1054
Cdd:cd16923      1 LQRVFSNLLSNAIKYSPE---NTRIYITSFL-------TDDVVNIMFKNPSSHPLDFKLEKLFERFYRGD--NSRNTEGA 68
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1228082595 1055 GLGLSISRQVANLLGGELRAQSrLGAGSTFTLYVP 1089
Cdd:cd16923     69 GLGLSIAKAIIELHGGSASAEY-DDNHDLFKVRLP 102
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
1256-1370 9.95e-10

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 60.32  E-value: 9.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEaLRDSPDIDLILMDVMMPEMDGYAttaaIRRMPRFGS--LPII 1333
Cdd:PRK09836     2 KLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYH-LAMTGDYDLIILDIMLPDVNGWD----IVRMLRSANkgMPIL 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1228082595 1334 MVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:PRK09836    77 LLTALGTIEHRVKGLELGADDYLVKPFAFAELLARVR 113
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
1257-1371 1.16e-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: 57.22  E-value: 1.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRkgieALRDSPDIDL---ILMDVMMPEMDGYATTAAIRRMPRfgSLPII 1333
Cdd:cd17537      3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSAS----AFLAAAPPDQpgcLVLDVRMPGMSGLELQDELLARGS--NIPII 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1228082595 1334 MVTAKA---MAgdrEKSLAAGASDYVTKPVDAKELLTCIRR 1371
Cdd:cd17537     77 FITGHGdvpMA---VEAMKAGAVDFLEKPFRDQVLLDAIEQ 114
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
185-575 1.20e-09

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 62.73  E-value: 1.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  185 TTSVNFMAGNLTAQVRSIAEVTTAVAKGDLSQKITVDARGEILELKSTINTMVDQLSSFADEVTRVAREVGTEGILGGQA 264
Cdd:COG0840     10 LLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  265 QVPGVAGTWRDLTTSVNFMAGNLTAQVRSIAQVATAVARGDLSQKITVDARGEIFELKSTINTMVDQLSSFADEVTRVAR 344
Cdd:COG0840     90 LLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEA 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  345 EVGTEGRLGGQADVKGVSGTWKGLTESV--NVMADNLTDQVRSIAQVSAAVARGDLSQRITVEAKGEVAGLAQTINTMVD 422
Cdd:COG0840    170 AALALAAAALALALLAAALLALVALAIIlaLLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIE 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  423 TLSAFADEVTRVAREvgtegilggqarvanVAGTWKDLTDNVNSMANNLTGQVRSIAQVTTAVArgnlsqkidvdargei 502
Cdd:COG0840    250 NLRELVGQVRESAEQ---------------VASASEELAASAEELAAGAEEQAASLEETAAAME---------------- 298
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1228082595  503 lELKTTINTMVDTlssfAAEVTRVAREVGKEGQLGGQAeVEGVSGTWKRLTENVNELAG---NLTRQVRAIAEVTS 575
Cdd:COG0840    299 -ELSATVQEVAEN----AQQAAELAEEASELAEEGGEV-VEEAVEGIEEIRESVEETAEtieELGESSQEIGEIVD 368
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
1257-1371 1.23e-09

phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family response regulators; Streptococcus agalactiae NsrR is a lantibiotic resistance-associated response regulator and is part of the nisin resistance operon. It is a member of the NsrRK two-component system (TCS) that is involved in the regulation of lantibiotic resistance genes such as a membrane-associated lipoprotein of LanI, and the nsr gene cluster which encodes for the resistance protein NSR and the ABC transporter NsrFP, both conferring resistance against nisin. This subfamily also includes Staphylococcus epidermidis GraR, part of the GraR/GraS TCS involved in resistance against cationic antimicrobial peptides, and Bacillus subtilis BceR, part of the BceS/BceR TCS involved in the regulation of bacitracin resistance. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 57.29  E-value: 1.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRD-SPDidLILMDVMMPEMDGYATTAAIRRmprFGSLPIIMV 1335
Cdd:cd18159      1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQfKPD--LVLLDINLPYFDGFYWCREIRQ---ISNVPIIFI 75
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1228082595 1336 TAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRR 1371
Cdd:cd18159     76 SSRDDNMDQVMAINMGGDDYITKPFDLDVLLAKIKA 111
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
1256-1370 1.48e-09

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 61.44  E-value: 1.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGlsvEH-----APNGRKGIE-ALRDSPDidLILMDVMMPEMDGYATTAAI-RRMPrfg 1328
Cdd:PRK12555     2 RIGIVNDSPLAVEALRRALARDP---DHevvwvATDGAQAVErCAAQPPD--VILMDLEMPRMDGVEATRRImAERP--- 73
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1228082595 1329 sLPIIMVTAKAMAGDRE--KSLAAGASDYVTKPV---------DAKELLTCIR 1370
Cdd:PRK12555    74 -CPILIVTSLTERNASRvfEAMGAGALDAVDTPTlgigagleeYAAELLAKID 125
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
975-1089 1.49e-09

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: 57.00  E-value: 1.49e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  975 LRQVLRNMLSNAVK-FTEKGKVKLRVRLVPADQVPGGGADD----PWLAFSVIDTGIGIAEENLSTIFGAFQqadgTTSR 1049
Cdd:cd16919      1 LELAILNLAVNARDaMPEGGRLTIETSNQRVDADYALNYRDlipgNYVCLEVSDTGSGMPAEVLRRAFEPFF----TTKE 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1228082595 1050 RYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVP 1089
Cdd:cd16919     77 VGKGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
Spo0A COG5801
Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell ...
1256-1370 2.07e-09

Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444503 [Multi-domain]  Cd Length: 264  Bit Score: 59.81  E-value: 2.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARnvlaIAEMLKlHGLS-------VEHAPNGRKGIEALRD-SPDIdlILMDVMMPEMDGYATTAAIRRMPRF 1327
Cdd:COG5801      6 KVLIADDNRE----FCELLE-EYLSsqpdmevVGVAYNGLEALELIEEkKPDV--VILDIIMPHLDGLGVLEKLREMNLE 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1228082595 1328 GSLPIIMVTA----KAMagdrEKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:COG5801     79 KRPKVIMLTAfgqeDIT----QRAVELGADYYILKPFDLDVLAERIR 121
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1256-1376 2.37e-09

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 60.93  E-value: 2.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLH-GLSV-EHAPNGRKGIE-ALRDSPDIdlILMDVMMPEMDGYATTAAI-RRMPrfgsLP 1331
Cdd:PRK00742     5 RVLVVDDSAFMRRLISEILNSDpDIEVvGTAPDGLEAREkIKKLNPDV--ITLDVEMPVMDGLDALEKImRLRP----TP 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1228082595 1332 IIMVTAKAMAGDRE--KSLAAGASDYVTKPV--------DAKELLtcIRRWIAAA 1376
Cdd:PRK00742    79 VVMVSSLTERGAEItlRALELGAVDFVTKPFlgislgmdEYKEEL--AEKVRAAA 131
PRK10766 PRK10766
two-component system response regulator TorR;
1253-1366 2.69e-09

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 58.90  E-value: 2.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1253 LGRRVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSpDIDLILMDVMMPEMDGYATTAAIRRMPRFGslpI 1332
Cdd:PRK10766     1 MSYHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQ-HVDLILLDINLPGEDGLMLTRELRSRSTVG---I 76
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1228082595 1333 IMVTAKAMAGDREKSLAAGASDYVTKPVDAKELL 1366
Cdd:PRK10766    77 ILVTGRTDSIDRIVGLEMGADDYVTKPLELRELL 110
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
1257-1360 3.00e-09

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 56.22  E-value: 3.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEAL----------RDSPDIDLILMDVMMPEMDGYATTAAIRRMPR 1326
Cdd:cd17581      1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLgledeedssnFNEPKVNMIITDYCMPGMTGYDLLKKVKESSA 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1228082595 1327 FGSLPIIMVTAKAMAGDREKSLAAGASDYVTKPV 1360
Cdd:cd17581     81 LKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPV 114
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
1256-1372 3.22e-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: 56.10  E-value: 3.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARnVLAIAEML--KLHGLSV-EHAPNGRKGIEALRDsPDIDLILMDVMMPEMDGYATTAAIRRmpRFGSLPI 1332
Cdd:cd19925      2 NVLIVEDDPM-VAEIHRAYveQVPGFTViGTAGTGEEALKLLKE-RQPDLILLDIYLPDGNGLDLLRELRA--AGHDVDV 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1228082595 1333 IMVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRRW 1372
Cdd:cd19925     78 IVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRLERY 117
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
275-610 3.37e-09

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 61.19  E-value: 3.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  275 DLTTSVNFMAGNLTAQVRSIAQVATAVARGDLSQKITVDARGEIFELKSTINTMVDQLSSFADEVTRVAREVGTEGRLGG 354
Cdd:COG0840     10 LLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  355 QADVKGVSGTWKGLTESVNVMADNLTDQVRSIAQVSAAVARGDLSQRITVEAKGEVAGLAQTINTMVDTLSAFADEVTRV 434
Cdd:COG0840     90 LLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEA 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  435 AREVGTEGILGGQARVANVAGTWKDLTDNVNSMANNLTGQVRSIAQVTTAVARGNLSQKIDVDARGEILELKTTINTMVD 514
Cdd:COG0840    170 AALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIE 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  515 TLSSFAAEVTRVAREVGKE--------GQLGGQAE-----VEGVSGTWKRLTENVNELAGNlTRQVRAIAEVTSAVA-TG 580
Cdd:COG0840    250 NLRELVGQVRESAEQVASAseelaasaEELAAGAEeqaasLEETAAAMEELSATVQEVAEN-AQQAAELAEEASELAeEG 328
                          330       340       350
                   ....*....|....*....|....*....|
gi 1228082595  581 DLTRSITVEAKGEVSELKDNINAMVRSLRE 610
Cdd:COG0840    329 GEVVEEAVEGIEEIRESVEETAETIEELGE 358
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
975-1086 5.11e-09

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: 55.16  E-value: 5.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  975 LRQVLRNMLSNAVKFT-EKGKVKLRVRlvpadqvpgggADDPWLAFSVIDTGIGIAEENLSTIFGAFQQ-ADGTTSRRyg 1052
Cdd:cd16945      5 LRQAINNLLDNAIDFSpEGGLIALQLE-----------ADTEGIELLVFDEGSGIPDYALNRVFERFYSlPRPHSGQK-- 71
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1228082595 1053 GTGLGLSISRQVANLLGGELRAQSRL-GAGSTFTL 1086
Cdd:cd16945     72 STGLGLAFVQEVAQLHGGRITLRNRPdGVLAFLTL 106
PRK10336 PRK10336
two-component system response regulator QseB;
1256-1359 5.68e-09

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 57.98  E-value: 5.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRfgSLPIIMV 1335
Cdd:PRK10336     2 RILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAP-YDAVILDLTLPGMDGRDILREWREKGQ--REPVLIL 78
                           90       100
                   ....*....|....*....|....
gi 1228082595 1336 TAKAMAGDREKSLAAGASDYVTKP 1359
Cdd:PRK10336    79 TARDALAERVEGLRLGADDYLCKP 102
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
320-955 6.48e-09

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 60.51  E-value: 6.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  320 ELKSTINTMVDQLSSFADEVTRVAREVGTEGRLGGQADVKGVSGTWKGLTESVNVMADNLTDQVRSIAQVSAAVARGDLS 399
Cdd:COG2770      1 LLLLLLALLLLLLLLLLLLLLAGALLVLALISLRLLLALLLLLLLLLALLLLLLLLLLLLLAALVLLALLLAAALLLLLL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  400 QRITVEAKGEVAGLAQTINTMVDTLSAFADEVTRVAREVGTEGILGGQARVANVAGTWKDLTDNVNSMANNLTGQVRSIA 479
Cdd:COG2770     81 LLSLVALAALLLALLLLLLLALLLLLAALLLLLLLAALALLLLLLLLLAALLALLLALALLALLLGLAAARLLLAALLAL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  480 QVTTAVARGNLSQKIDVDARGEILELKTTINTMVDTLSSFAAEVTRVAREVGKEGQLGGQAEVEGVSGTWKrltenvneL 559
Cdd:COG2770    161 AAALALALGAGELLLLADLAAAIAALLAALLLLLLGGLLLVVLLEAALAALLLLLLLALLALLLALLLALL--------L 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  560 AGNLTRQVRAIAEVTSAVATGDLTRSITVEAKGEVSELKDNINAMVRSLRETTlaNQDQDWLNTNLARISGLLQGHRDLR 639
Cdd:COG2770    233 ARRITRPLRRLAEAARRIAAGDLDVRIPVSRKDEIGELARAFNRMADSLRESI--EEAEEEEELAEAELARLLEALLELL 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  640 AVTQLIMNELTPLVGAQYGTFFLKEQGERLRLLASYGGAESGQGATEYELGQSLLGQVASTRKAILVEQTPPDYVRISSS 719
Cdd:COG2770    311 LALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAA 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  720 LGSAPPVNLIVLPIVFEEQVVGVIELASFTRFSLVQRDFLEQLMESIGVNVNTIVANARTDVLLEESQRLAAELSVRTEE 799
Cdd:COG2770    391 VLALLAALAAALLLLELALEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAE 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  800 LQAQQAKLQQSNAELEEKAELLARQNRDIEVKNFEIEQARQEIEERAQQLALTSKYKSEFLANMSHELRTPLTSLLILAG 879
Cdd:COG2770    471 ALLLLAALLLLAALGALELLLLEEEEEAGAAAEELAEELLLLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAA 550
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1228082595  880 VLSQNSTQNLTPKQVEFAKVIESAGTDLLQLINDILDLSKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLE 955
Cdd:COG2770    551 LLALLLALAAVEAAALLLAALLLAAVAALLELAALLLLLLAAAEALAALELELAAAAEAALAEAELLEVAAAAEAG 626
GAF COG2203
GAF domain [Signal transduction mechanisms];
558-1078 1.23e-08

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 59.44  E-value: 1.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  558 ELAGNLTRQVRAIAEVTSAVATGDLTRSITVEAKGEVSELKDNINAMVRSLRETTLANQDQDWLNTNLARISGLLQGHRD 637
Cdd:COG2203    128 RLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALRSALD 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  638 LRAVTQLIMNELTPLVGAQYGTFFLK-EQGERLRLLASYGGAESgqGATEYELGQSLLGQVASTRKAILVEQTPPDYV-- 714
Cdd:COG2203    208 LEELLQRILELAGELLGADRGAILLVdEDGGELELVAAPGLPEE--ELGRLPLGEGLAGRALRTGEPVVVNDASTDPRfa 285
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  715 -RISSSLGSAPPVNLIVLPIVFEEQVVGVIELASFT--RFSLVQRDFLEQLMESIGVNVNTivANARTDVLLEESQRLAA 791
Cdd:COG2203    286 pSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEprAFTEEDLELLEALADQAAIAIER--ARLYEALEAALAALLQE 363
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  792 ELSVRTEELQAQQAKLQQSNAELEEKAELLARQNRDIEVKNFEIEQARQEIEERAQQLALTSKYKSEFLANMSHELRTPL 871
Cdd:COG2203    364 LALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLR 443
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  872 TSLLILAGVLSQNSTQNLTPKQVEFAKVIESAGTDLLQLINDILDLSKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAE 951
Cdd:COG2203    444 RLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVLASLLLALLLLLLLLLLL 523
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  952 KGLEFEAVVDPDVPEQLSTDEQRLRQVLRNMLSNAVKFTEKGKVKLRVRLVPADQVPGGGADDPWLAFSVIDTGIGIAEE 1031
Cdd:COG2203    524 LLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIELALALILALALLELLLVAVGDLLLL 603
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1228082595 1032 NLSTIFGAFQQADGTTSRRYGGTGLGLSISRQVANLLGGELRAQSRL 1078
Cdd:COG2203    604 ERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALAL 650
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
1256-1370 1.36e-08

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: 54.72  E-value: 1.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLH-GLSVEHAPNGRKGIE-ALRDSPDIdlILMDVMMPEMDGYATTAAIRRMPRFGSLPII 1333
Cdd:cd17575      2 MVLLVDDQAIIGEAVRRALADEeDIDFHYCSDPTEAIEvASQIKPTV--ILQDLVMPGVDGLTLVRFFRANPATRDIPII 79
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1228082595 1334 MVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:cd17575     80 VLSTKEEPEVKSEAFALGANDYLVKLPDKIELVARIR 116
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
1257-1360 1.44e-08

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: 53.89  E-value: 1.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPDIDLILMDVMMP-EMDGyaTTAAIRRMPRFGSLPIIMV 1335
Cdd:cd18161      1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPDIDLLVTDVIMPgGMNG--SQLAEEARRRRPDLKVLLT 78
                           90       100
                   ....*....|....*....|....*
gi 1228082595 1336 TAKAMAGDREKSLAAGAsDYVTKPV 1360
Cdd:cd18161     79 SGYAENAIEGGDLAPGV-DVLSKPF 102
PRK15115 PRK15115
response regulator GlrR; Provisional
1256-1369 1.65e-08

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 58.70  E-value: 1.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRmpRFGSLPIIMV 1335
Cdd:PRK15115     7 HLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREK-VDLVISDLRMDEMDGMQLFAEIQK--VQPGMPVIIL 83
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1228082595 1336 TAKAMAGDREKSLAAGASDYVTKPVDAKELLTCI 1369
Cdd:PRK15115    84 TAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAI 117
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
1257-1369 1.77e-08

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 53.59  E-value: 1.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGiEALRDSPDIDLILMDVMMPEMDGYATTAAIRRmpRFGSLPIIMVT 1336
Cdd:cd17573      1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDG-EYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKE--KHPSIVVIVLS 77
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1228082595 1337 AKAMAGDREKSLAAGASDYVTKPVDAKELLTCI 1369
Cdd:cd17573     78 DNPKTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
1256-1359 1.83e-08

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


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 53.77  E-value: 1.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHG--LSVEHAPNGRKGIEALRDSpDIDLILMDVMMPEMDGYATTAAIRRMPRFGSLPII 1333
Cdd:cd17561      3 KVLIADDNREFVQLLEEYLNSQPdmEVVGVAHNGQEALELIEEK-EPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPKII 81
                           90       100
                   ....*....|....*....|....*.
gi 1228082595 1334 MVTAKAMAGDREKSLAAGASDYVTKP 1359
Cdd:cd17561     82 MLTAFGQEDITQRAVELGASYYILKP 107
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
1255-1366 2.73e-08

phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; Rhodobacter sphaeroides RegA, also called response regulator PrrA, is the DNA binding regulatory protein of a redox-responsive two-component regulatory system RegB/RegA that is involved in transactivating anaerobic expression of the photosynthetic apparatus. It contains a REC domain and a DNA-binding helix-turn-helix output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 53.22  E-value: 2.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1255 RRVLLIDDDA--RNVLAIAemLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRmpRFGSLPI 1332
Cdd:cd17563      1 KSLLLVDDDEvfAERLARA--LERRGFEVETAHSVEEALALAREEK-PDYAVLDLRLGGDSGLDLIPPLRA--LQPDARI 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1228082595 1333 IMVTAKAmagdrekSLAA-------GASDYVTKPVDAKELL 1366
Cdd:cd17563     76 VVLTGYA-------SIATaveaiklGADDYLAKPADADEIL 109
PRK10643 PRK10643
two-component system response regulator PmrA;
1256-1373 3.50e-08

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 55.43  E-value: 3.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGiEALRDSPDIDLILMDVMMPEMDGYATTAAIRRmpRFGSLPIIMV 1335
Cdd:PRK10643     2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREA-EALLESGHYSLVVLDLGLPDEDGLHLLRRWRQ--KKYTLPVLIL 78
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1228082595 1336 TAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRRWI 1373
Cdd:PRK10643    79 TARDTLEDRVAGLDVGADDYLVKPFALEELHARIRALI 116
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
44-682 3.52e-08

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 58.20  E-value: 3.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595   44 EISTVFNGMVDQLSVFTSEVTRVAREVGTDGKLGGQATVPGVSGTWKDLTESVNAMAGNLTAQVRDIAGVATAVARGDLS 123
Cdd:COG2770      1 LLLLLLALLLLLLLLLLLLLLAGALLVLALISLRLLLALLLLLLLLLALLLLLLLLLLLLLAALVLLALLLAAALLLLLL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  124 QKITVQVRGELLELKNTINTMVDQLSSFADEVTRVAREVGSEGRLGGQAEVPGVAGTWRDLTTSVNFMAGNLTAQVRSIA 203
Cdd:COG2770     81 LLSLVALAALLLALLLLLLLALLLLLAALLLLLLLAALALLLLLLLLLAALLALLLALALLALLLGLAAARLLLAALLAL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  204 EVTTAVAKGDLSQKITVDARGEILELKSTINTMVDQLSSFADEVTRVAREVGTEGILGGQAQVPGVAGTWrdlttsvnFM 283
Cdd:COG2770    161 AAALALALGAGELLLLADLAAAIAALLAALLLLLLGGLLLVVLLEAALAALLLLLLLALLALLLALLLAL--------LL 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  284 AGNLTAQVRSIAQVATAVARGDLSQKITVDARGEIFELKSTINTMVDQLSSFADEVTRVAREVGTEGRLGGQADVKGVSG 363
Cdd:COG2770    233 ARRITRPLRRLAEAARRIAAGDLDVRIPVSRKDEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLA 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  364 TWKGLTESVNVMADNLTDQVRSIAQVSAAVARGDLSQRITVEAKGEVAGLAQTINTMVDTLSAFADEVTRVAREVGTEGI 443
Cdd:COG2770    313 LLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVL 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  444 LGGQARVANVAGTWKDLTDNVNSMANNLTGQVRSIAQVTTAVARGNLSQKIDVDARGEILELKTTINTMVDTLSSFAAEV 523
Cdd:COG2770    393 ALLAALAAALLLLELALEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEAL 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  524 TRVAREVGKEGQLGGQAEVEGVSGTWKRLTENVNELAGNLTRQVRAIAEVTSAVATGDLTRSITVEAKGEVSELKDNINA 603
Cdd:COG2770    473 LLLAALLLLAALGALELLLLEEEEEAGAAAEELAEELLLLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAALL 552
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1228082595  604 MVRSLRETTLANQDQDWLNTNLARISGLLQGHRDLRAVTQLIMNELTPLVGAQYGTFFLKEQGERLRLLASYGGAESGQ 682
Cdd:COG2770    553 ALLLALAAVEAAALLLAALLLAAVAALLELAALLLLLLAAAEALAALELELAAAAEAALAEAELLEVAAAAEAGAALLA 631
PRK13557 PRK13557
histidine kinase; Provisional
953-1161 5.37e-08

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 57.37  E-value: 5.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  953 GLEFEAVVDPDVPeQLSTDEQRLRQVLRNMLSNAVK-FTEKGKVKLRVR--------LVPADQVPGGGaddpWLAFSVID 1023
Cdd:PRK13557   257 AVTIETDLAPDLW-NCRIDPTQAEVALLNVLINARDaMPEGGRVTIRTRnveiededLAMYHGLPPGR----YVSIAVTD 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1024 TGIGIAEENLSTIFGAFqqadGTTSRRYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPVTPDFDTAVIDMGA 1103
Cdd:PRK13557   332 TGSGMPPEILARVMDPF----FTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFPASDQAENPEQEPKA 407
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1228082595 1104 RPEpvlAR----RVLVVEAGEDqlLTLLVRGFATDLadareAVDVESVAMPDEAMERLAAGP 1161
Cdd:PRK13557   408 RAI---DRggteTILIVDDRPD--VAELARMILEDF-----GYRTLVASNGREALEILDSHP 459
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
1257-1370 7.86e-08

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 54.81  E-value: 7.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDA--RNVLAIAemLKLHGLSVEHAPNGRKG-IEALRDSPDidLILMDVMMPEMDGyatTAAIRRMPRFGSLPII 1333
Cdd:PRK10529     4 VLIVEDEQaiRRFLRTA--LEGDGMRVFEAETLQRGlLEAATRKPD--LIILDLGLPDGDG---IEFIRDLRQWSAIPVI 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1228082595 1334 MVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:PRK10529    77 VLSARSEESDKIAALDAGADDYLSKPFGIGELQARLR 113
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
637-768 8.92e-08

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: 52.48  E-value: 8.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  637 DLRAVTQLIMNELTPLVGAQYGTFFLKEQGERLRLLASYGGAESGQGATEYELGqsllGQVASTRKAILVEQTPPD--YV 714
Cdd:pfam01590    1 DLEEILQTILEELRELLGADRCALYLPDADGLEYLPPGARWLKAAGLEIPPGTG----VTVLRTGRPLVVPDAAGDprFL 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1228082595  715 RISSSLGSAPPVNLIVLPIVFEEQVVGVIELASFTR-FSLVQRDFLEQLMESIGV 768
Cdd:pfam01590   77 DPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHPRPpFTEEELELLEVLADQVAI 131
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
383-424 1.27e-07

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 48.98  E-value: 1.27e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1228082595  383 VRSIAQVSAAVARGDLSQRITVEAKGEVAGLAQTINTMVDTL 424
Cdd:cd06225      4 LRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
196-240 1.62e-07

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 48.98  E-value: 1.62e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1228082595  196 TAQVRSIAEVTTAVAKGDLSQKITVDARGEILELKSTINTMVDQL 240
Cdd:cd06225      1 TRPLRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
975-1089 2.00e-07

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: 50.86  E-value: 2.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  975 LRQVLRNMLSNAVKFTEKGKVKLRVRLVPADQVPGGGADDPW-LAFSVIDTGIGIAEENLSTIFGAFqqadgtTSRRYGG 1053
Cdd:cd16918      1 LIQVFLNLVRNAAQALAGSGGEIILRTRTQRQVTLGHPRHRLaLRVSVIDNGPGIPPDLQDTIFYPM------VSGRENG 74
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1228082595 1054 TGLGLSISRQVANLLGGELRAQSRLGAgSTFTLYVP 1089
Cdd:cd16918     75 TGLGLAIAQNIVSQHGGVIECDSQPGH-TVFSVSLP 109
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
1256-1370 2.33e-07

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: 50.86  E-value: 2.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRmpRFGSLPIIMV 1335
Cdd:cd17569      2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEP-VDVVISDQRMPGMDGAELLKRVRE--RYPDTVRILL 78
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1228082595 1336 TAKAmagDREKSLAA----GASDYVTKPVDAKELLTCIR 1370
Cdd:cd17569     79 TGYA---DLDAAIEAinegEIYRFLTKPWDDEELKETIR 114
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
1256-1376 3.03e-07

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 52.72  E-value: 3.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDA--RN----VLAIAEMLKLhglsVEHAPNGRKGIEaLRDSPDIDLILMDVMMPEMDGYATTAAIRRMPRFGS 1329
Cdd:PRK10651     8 TILLIDDHPmlRTgvkqLISMAPDITV----VGEASNGEQGIE-LAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGR 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1228082595 1330 lpIIMVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRRwiAAA 1376
Cdd:PRK10651    83 --IVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQ--AAA 125
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
1257-1371 3.51e-07

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


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 50.39  E-value: 3.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEML-KLHGLSVEhaPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRFGSLPIIMV 1335
Cdd:cd17539      1 VLLVDDRPSSAERIAAMLsSEHEVVVE--ADPDEALFRAAEGP-FDLVIVSLALEDFDGLRLCSQLRSLERTRQLPILAV 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1228082595 1336 takAMAGDRE---KSLAAGASDYVTKPVDAKELL----TCIRR 1371
Cdd:cd17539     78 ---ADPGDRGrliRALEIGVNDYLVRPIDPNELLarvrTQIRR 117
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
286-332 3.58e-07

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 48.01  E-value: 3.58e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1228082595   286 NLTAQVRSIAQVATAVARGDLSQKITVDARGEIFELKSTINTMVDQL 332
Cdd:smart00304    2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRL 48
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
821-1093 3.64e-07

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 54.25  E-value: 3.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  821 LARQNRDIEVKNFEIEQARQEIEERAQQLALtskyKSEFLANMshelrtpLTSLLILAgvLSQNstqnltPKQVEfaKVI 900
Cdd:COG2972    221 MVERIKELIEEVYELELEKKEAELKALQAQI----NPHFLFNT-------LNSIRWLA--ELED------PEEAE--EML 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  901 EsagtDLLQLINDILDLSKveagkmdihpELVELRQQVEYVRT--TFQPLTAEKGLEFEAVVDPDVPEQLstdeqrlrqV 978
Cdd:COG2972    280 E----ALSKLLRYSLSKGD----------ELVTLEEELELIKSylEIQKLRFGDRLEVEIEIDEELLDLL---------I 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  979 LRNMLS----NAVKF-----TEKGKVKLRVRLvpadqvpgggaDDPWLAFSVIDTGIGIAEENLSTIFGAFqqadgttSR 1049
Cdd:COG2972    337 PKLILQplveNAIEHgiepkEGGGTIRISIRK-----------EGDRLVITVEDNGVGMPEEKLEKLLEEL-------SS 398
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1228082595 1050 RYGGTGLGLSISRQVANLLGGE---LRAQSRLGAGSTFTLYVPVTPD 1093
Cdd:COG2972    399 KGEGRGIGLRNVRERLKLYYGEeygLEIESEPGEGTTVTIRIPLEEE 445
HAMP_2 pfam18947
HAMP domain;
455-518 4.10e-07

HAMP domain;


Pssm-ID: 465927 [Multi-domain]  Cd Length: 67  Bit Score: 48.25  E-value: 4.10e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1228082595  455 GTWKDLTDNVNSMANNLTGQVRSIAQVTTAVARGNLSQKIDVDARGEILELKTTINTMVDTLSS 518
Cdd:pfam18947    4 GDFRKIVEGVNNTLDAIITPLNEAADYVDRISKGDIPEKITDEYKGDFNEIKNNLNALIDAINA 67
HAMP pfam00672
HAMP domain;
282-332 4.43e-07

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 48.00  E-value: 4.43e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1228082595  282 FMAGNLTAQVRSIAQVATAVARGDLSQKITVDARGEIFELKSTINTMVDQL 332
Cdd:pfam00672    1 LLARRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERL 51
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
288-332 4.91e-07

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 47.44  E-value: 4.91e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1228082595  288 TAQVRSIAQVATAVARGDLSQKITVDARGEIFELKSTINTMVDQL 332
Cdd:cd06225      1 TRPLRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
1258-1371 6.10e-07

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: 49.58  E-value: 6.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1258 LLIDDDARNVL-AIAEMLKLHG--LSVEHAPNGRKGIEALRD-SPDIdlILMDVMMPEMDGYATTAAIRRmprfgSLP-- 1331
Cdd:cd19930      1 VLIAEDQEMVRgALAALLELEDdlEVVAQASNGQEALRLVLKhSPDV--AILDIEMPGRTGLEVAAELRE-----ELPdt 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1228082595 1332 -IIMVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRR 1371
Cdd:cd19930     74 kVLIVTTFGRPGYFRRALAAGVDGYVLKDRPIEELADAIRT 114
HAMP pfam00672
HAMP domain;
190-240 7.44e-07

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 47.23  E-value: 7.44e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1228082595  190 FMAGNLTAQVRSIAEVTTAVAKGDLSQKITVDARGEILELKSTINTMVDQL 240
Cdd:pfam00672    1 LLARRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERL 51
PRK10337 PRK10337
sensor protein QseC; Provisional
859-1069 7.89e-07

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 53.11  E-value: 7.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  859 FLANMSHELRTPLTSLLILAGV--LSQNSTQNLTPKQVEFAKVIESAGtdllQLINDILDLSKVEAGKmdihpelvelrq 936
Cdd:PRK10337   240 FTSDAAHELRSPLAALKVQTEVaqLSDDDPQARKKALLQLHAGIDRAT----RLVDQLLTLSRLDSLD------------ 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  937 qveyVRTTFQPLTAEKGLEfEAVVDPDVPEQLSTDEQRL--------RQ--------VLRNMLSNAVKFTEKGKVkLRVR 1000
Cdd:PRK10337   304 ----NLQDVAEIPLEDLLQ-SAVMDIYHTAQQAGIDVRLtlnahpviRTgqplllslLVRNLLDNAIRYSPQGSV-VDVT 377
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1228082595 1001 LVPAdqvpgggaddpwlAFSVIDTGIGIAEENLSTIFGAFQQADGTTSRrygGTGLGLSISRQVANLLG 1069
Cdd:PRK10337   378 LNAR-------------NFTVRDNGPGVTPEALARIGERFYRPPGQEAT---GSGLGLSIVRRIAKLHG 430
pleD PRK09581
response regulator PleD; Reviewed
1224-1371 8.14e-07

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 53.37  E-value: 8.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1224 DELRERflGLLPVTPEPEPEVVEPVASGLLGRRVLLIDDDARNVLAIAEMLK-LHGLSVE-HAPNGRkgIEALRDSPDid 1301
Cdd:PRK09581   127 DELRLR--ASTNAEIGVTALMIMAYANKDEDGRILLVDDDVSQAERIANILKeEFRVVVVsDPSEAL--FNAAETNYD-- 200
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1228082595 1302 LILMDVMMPEMDGYATTAAIRRMPRFGSLPIIMVTAkamAGDREKSLAA---GASDYVTKPVDAKELL----TCIRR 1371
Cdd:PRK09581   201 LVIVSANFENYDPLRLCSQLRSKERTRYVPILLLVD---EDDDPRLVKAlelGVNDYLMRPIDKNELLarvrTQIRR 274
HAMP_2 pfam18947
HAMP domain;
86-146 8.22e-07

HAMP domain;


Pssm-ID: 465927 [Multi-domain]  Cd Length: 67  Bit Score: 47.48  E-value: 8.22e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1228082595   86 SGTWKDLTESVNAMAGNLTAQVRDIAGVATAVARGDLSQKITVQVRGELLELKNTINTMVD 146
Cdd:pfam18947    3 QGDFRKIVEGVNNTLDAIITPLNEAADYVDRISKGDIPEKITDEYKGDFNEIKNNLNALID 63
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
194-240 8.66e-07

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 47.24  E-value: 8.66e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1228082595   194 NLTAQVRSIAEVTTAVAKGDLSQKITVDARGEILELKSTINTMVDQL 240
Cdd:smart00304    2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRL 48
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
1257-1371 9.34e-07

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: 49.07  E-value: 9.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDD--ARNVLAIaeMLKLHG--LSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRMPRfgsLP- 1331
Cdd:cd17532      1 ALIVDDEplAREELRY--LLEEHPdiEIVGEAENGEEALEAIEELK-PDVVFLDIQMPGLDGLELAKKLSKLAK---PPl 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1228082595 1332 IIMVTAKamagdREKSLAA---GASDYVTKPVDAKELLTCIRR 1371
Cdd:cd17532     75 IVFVTAY-----DEYAVEAfelNAVDYLLKPFSEERLAEALAK 112
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
475-516 9.38e-07

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 46.67  E-value: 9.38e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1228082595  475 VRSIAQVTTAVARGNLSQKIDVDARGEILELKTTINTMVDTL 516
Cdd:cd06225      4 LRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
562-611 1.17e-06

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 46.86  E-value: 1.17e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1228082595   562 NLTRQVRAIAEVTSAVATGDLTRSITVEAKGEVSELKDNINAMVRSLRET 611
Cdd:smart00304    2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEET 51
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
1257-1371 1.17e-06

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 48.88  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHG--LSVEHAPNGRKGIE-ALRDSPDIdlILMDVMMPEMDGYATTAAIRRmpRFGSLPII 1333
Cdd:cd19931      1 VLLIDDHPLLRKGIKQLIELDPdfTVVGEASSGEEGIElAERLDPDL--ILLDLNMKGMSGLDTLKALRE--EGVSARIV 76
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1228082595 1334 MVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRR 1371
Cdd:cd19931     77 ILTVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQ 114
HAMP pfam00672
HAMP domain;
559-610 1.38e-06

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 46.46  E-value: 1.38e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1228082595  559 LAGNLTRQVRAIAEVTSAVATGDLTRSITVEAKGEVSELKDNINAMVRSLRE 610
Cdd:pfam00672    2 LARRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERLRE 53
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
951-1097 1.43e-06

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 52.61  E-value: 1.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  951 EKGLEFEAVVDPDVPEqlSTDEQR---LRQVLRNMLSN---AVKFTEKGKVKLRVRLVpadqvpgggadDPWLAFSVIDT 1024
Cdd:PRK11086   409 ELGITLIISEDSQLPD--SGDEDQvheLITILGNLIENaleAVGGEEGGEISVSLHYR-----------NGWLHCEVSDD 475
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1228082595 1025 GIGIAEENLSTIFgafqqaDGTTSRRYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPVTPDFDTA 1097
Cdd:PRK11086   476 GPGIAPDEIDAIF------DKGYSTKGSNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIPWDGERSNR 542
HAMP pfam00672
HAMP domain;
374-426 1.45e-06

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 46.46  E-value: 1.45e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1228082595  374 VMADNLTDQVRSIAQVSAAVARGDLSQRITVEAKGEVAGLAQTINTMVDTLSA 426
Cdd:pfam00672    1 LLARRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERLRE 53
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
1016-1089 1.61e-06

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: 48.05  E-value: 1.61e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1228082595 1016 WLAFSVIDTGIGIAEENLSTIFgafqqADGTTSRRYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVP 1089
Cdd:cd16915     36 DLVIEVRDTGPGIAPELRDKVF-----ERGVSTKGQGERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
378-426 1.94e-06

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 46.09  E-value: 1.94e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1228082595   378 NLTDQVRSIAQVSAAVARGDLSQRITVEAKGEVAGLAQTINTMVDTLSA 426
Cdd:smart00304    2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEE 50
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
846-1089 1.97e-06

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: 52.44  E-value: 1.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  846 AQQLALTSKYkSEFLANMS----HELRTPL----TSLLILAGVLSQNSTQnltpKQVEFAkvieSAGTDLLQLI-NDILD 916
Cdd:TIGR03785  472 AQMVARLRQY-THYLENMSsrlsHELRTPVavvrSSLENLELQALEQEKQ----KYLERA----REGTERLSMIlNNMSE 542
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  917 LSKVEAGKMDIHPELVELRQQVEYVRTTFQPLTAEKGLEFEAVVDPDV----PEQLStdeqrlrQVLRNMLSNAVKFTEK 992
Cdd:TIGR03785  543 ATRLEQAIQSAEVEDFDLSEVLSGCMQGYQMTYPPQRFELNIPETPLVmrgsPELIA-------QMLDKLVDNAREFSPE 615
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  993 GKVkLRVRLVPADQvpgggadDPWLafSVIDTGIGIAEENLSTIFGAF--QQADGTTSRRYggTGLGLSISRQVANLLGG 1070
Cdd:TIGR03785  616 DGL-IEVGLSQNKS-------HALL--TVSNEGPPLPEDMGEQLFDSMvsVRDQGAQDQPH--LGLGLYIVRLIADFHQG 683
                          250       260
                   ....*....|....*....|
gi 1228082595 1071 ELRAQSRL-GAGSTFTLYVP 1089
Cdd:TIGR03785  684 RIQAENRQqNDGVVFRISLP 703
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
469-521 2.03e-06

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 46.09  E-value: 2.03e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1228082595   469 NNLTGQVRSIAQVTTAVARGNLSQKIDVDARGEILELKTTINTMVDTLSSFAA 521
Cdd:smart00304    1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
104-148 2.08e-06

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 45.90  E-value: 2.08e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1228082595  104 TAQVRDIAGVATAVARGDLSQKITVQVRGELLELKNTINTMVDQL 148
Cdd:cd06225      1 TRPLRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
HAMP_2 pfam18947
HAMP domain;
546-610 2.35e-06

HAMP domain;


Pssm-ID: 465927 [Multi-domain]  Cd Length: 67  Bit Score: 46.33  E-value: 2.35e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1228082595  546 SGTWKRLTENVNELAGNLTRQVRAIAEVTSAVATGDLTRSITVEAKGEVSELKDNINAMVRSLRE 610
Cdd:pfam18947    3 QGDFRKIVEGVNNTLDAIITPLNEAADYVDRISKGDIPEKITDEYKGDFNEIKNNLNALIDAINA 67
envZ PRK09467
osmolarity sensor protein; Provisional
860-1092 3.42e-06

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 51.06  E-value: 3.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  860 LANMSHELRTPLTSLLiLAgvlsqnsTQNLTPKQVEFAKVIESAGTDLLQLINDILD-LSKVEAGKMdihpELVELRQQV 938
Cdd:PRK09467   233 MAGVSHDLRTPLTRIR-LA-------TEMMSEEDGYLAESINKDIEECNAIIEQFIDyLRTGQEMPM----EMADLNALL 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  939 EYVrttfqpLTAEKGLEFEAVVD-PDVPEQLSTDEQRLRQVLRNMLSNAVKFTeKGKVKLRvrlvpadqvpgGGADDPWL 1017
Cdd:PRK09467   301 GEV------IAAESGYEREIETAlQPGPIEVPMNPIAIKRALANLVVNAARYG-NGWIKVS-----------SGTEGKRA 362
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1228082595 1018 AFSVIDTGIGIAEENLSTIFGAFQQADgtTSRRYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPVTP 1092
Cdd:PRK09467   363 WFQVEDDGPGIPPEQLKHLFQPFTRGD--SARGSSGTGLGLAIVKRIVDQHNGKVELGNSEEGGLSARAWLPLTT 435
HAMP_2 pfam18947
HAMP domain;
362-426 5.78e-06

HAMP domain;


Pssm-ID: 465927 [Multi-domain]  Cd Length: 67  Bit Score: 45.17  E-value: 5.78e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1228082595  362 SGTWKGLTESVNVMADNLTDQVRSIAQVSAAVARGDLSQRITVEAKGEVAGLAQTINTMVDTLSA 426
Cdd:pfam18947    3 QGDFRKIVEGVNNTLDAIITPLNEAADYVDRISKGDIPEKITDEYKGDFNEIKNNLNALIDAINA 67
HAMP_2 pfam18947
HAMP domain;
179-238 6.83e-06

HAMP domain;


Pssm-ID: 465927 [Multi-domain]  Cd Length: 67  Bit Score: 44.78  E-value: 6.83e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  179 GTWRDLTTSVNFMAGNLTAQVRSIAEVTTAVAKGDLSQKITVDARGEILELKSTINTMVD 238
Cdd:pfam18947    4 GDFRKIVEGVNNTLDAIITPLNEAADYVDRISKGDIPEKITDEYKGDFNEIKNNLNALID 63
HAMP pfam00672
HAMP domain;
99-148 7.47e-06

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 44.54  E-value: 7.47e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1228082595   99 MAGNLTAQVRDIAGVATAVARGDLSQKITVQVRGELLELKNTINTMVDQL 148
Cdd:pfam00672    2 LARRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERL 51
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
1256-1321 7.65e-06

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: 46.81  E-value: 7.65e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHG--LSVEHAPNGRKGIEALRDsPDIDLILMDVMMPEMDGYATTAAI 1321
Cdd:COG2197      3 RVLIVDDHPLVREGLRALLEAEPdiEVVGEAADGEEALELLEE-LRPDVVLLDIRMPGMDGLEALRRL 69
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
190-252 8.32e-06

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: 49.96  E-value: 8.32e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1228082595  190 FMAGNLTAQVRSIAEVTTAVAKGDLSQKITVDARGEILELKSTINTMVDQLSSFADEVTRVAR 252
Cdd:COG5000     28 LLARRLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARAFNRMTDQLKEQREELEERRR 90
PRK13856 PRK13856
two-component response regulator VirG; Provisional
1255-1370 8.38e-06

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 48.66  E-value: 8.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1255 RRVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATtaaIRRMPRFGSLPIIM 1334
Cdd:PRK13856     2 KHVLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASET-VDVVVVDLNLGREDGLEI---VRSLATKSDVPIII 77
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1228082595 1335 VTAKAM-AGDREKSLAAGASDYVTKPVDAKELLTCIR 1370
Cdd:PRK13856    78 ISGDRLeEADKVVALELGATDFIAKPFGTREFLARIR 114
HAMP pfam00672
HAMP domain;
467-516 8.57e-06

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 44.15  E-value: 8.57e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1228082595  467 MANNLTGQVRSIAQVTTAVARGNLSQKIDVDARGEILELKTTINTMVDTL 516
Cdd:pfam00672    2 LARRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERL 51
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
102-148 8.60e-06

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 44.16  E-value: 8.60e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1228082595   102 NLTAQVRDIAGVATAVARGDLSQKITVQVRGELLELKNTINTMVDQL 148
Cdd:smart00304    2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRL 48
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
564-608 1.10e-05

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 43.59  E-value: 1.10e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1228082595  564 TRQVRAIAEVTSAVATGDLTRSITVEAKGEVSELKDNINAMVRSL 608
Cdd:cd06225      1 TRPLRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
374-436 1.32e-05

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: 49.19  E-value: 1.32e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1228082595  374 VMADNLTDQVRSIAQVSAAVARGDLSQRITVEAKGEVAGLAQTINTMVDTLSAFADEVTRVAR 436
Cdd:COG5000     28 LLARRLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARAFNRMTDQLKEQREELEERRR 90
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
1255-1373 1.38e-05

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: 45.62  E-value: 1.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1255 RRVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEALRDSPDiDLILMDVMMPEMDGYATTAAIRRMPRfgSLPIIM 1334
Cdd:cd17553      1 EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERP-DLVLLDMKIPGMDGIEILKRMKVIDE--NIRVII 77
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1228082595 1335 VTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRRWI 1373
Cdd:cd17553     78 MTAYGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1111-1193 1.65e-05

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: 48.81  E-value: 1.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1111 RRVLVVEaGEDQLLTLLVRGFAtdladaREAVDVESVAMPDEAMERLAAGPVQCVVLDASLPGAAALTFLQRLADGDYRV 1190
Cdd:COG2204      3 ARILVVD-DDPDIRRLLKELLE------RAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDL 75

                   ...
gi 1228082595 1191 PVL 1193
Cdd:COG2204     76 PVI 78
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
971-1073 1.71e-05

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: 45.34  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  971 DEQRLRQVLRNMLSNAVKFT--EKGKVKLRVrlVPADQVPGGGADDPWLAFSVIDTGIGIAEENLSTIFgafqQADGTTS 1048
Cdd:cd16932      3 DQIRLQQVLADFLLNAVRFTpsPGGWVEIKV--SPTKKQIGDGVHVIHLEFRITHPGQGLPEELVQEMF----EENQWTT 76
                           90       100
                   ....*....|....*....|....*
gi 1228082595 1049 RRyggtGLGLSISRQVANLLGGELR 1073
Cdd:cd16932     77 QE----GLGLSISRKLVKLMNGDVR 97
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
282-344 1.88e-05

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: 48.80  E-value: 1.88e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1228082595  282 FMAGNLTAQVRSIAQVATAVARGDLSQKITVDARGEIFELKSTINTMVDQLSSFADEVTRVAR 344
Cdd:COG5000     28 LLARRLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARAFNRMTDQLKEQREELEERRR 90
PRK13557 PRK13557
histidine kinase; Provisional
1254-1371 2.15e-05

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 48.90  E-value: 2.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1254 GRRVLLIDDDARNVLAIAEM-LKLHGLSVEHAPNGRKGIEALRDSPDIDLILMDVMMP-EMDGYATTAAIRRM-PRfgsL 1330
Cdd:PRK13557   414 GTETILIVDDRPDVAELARMiLEDFGYRTLVASNGREALEILDSHPEVDLLFTDLIMPgGMNGVMLAREARRRqPK---I 490
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1228082595 1331 PIIMVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRR 1371
Cdd:PRK13557   491 KVLLTTGYAEASIERTDAGGSEFDILNKPYRRAELARRVRM 531
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1112-1217 2.21e-05

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 45.73  E-value: 2.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1112 RVLVVEAgeDQLLTLLVRGFATDLADAREAVDVESVAmpdEAMERLAAGPVQCVVLDASLPGAAALTFLQRLADGDYRVP 1191
Cdd:COG4565      5 RVLIVED--DPMVAELLRRYLERLPGFEVVGVASSGE---EALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVD 79
                           90       100
                   ....*....|....*....|....*.
gi 1228082595 1192 VLAhptrrLSAAQERLIEAHVRDHGV 1217
Cdd:COG4565     80 VIV-----ITAARDPETVREALRAGV 100
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
1257-1374 2.85e-05

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 48.33  E-value: 2.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEAL-RDSPDIdlILMDVMMPEMDGYATTAAIRRmpRFGSLPIIMV 1335
Cdd:PRK10923     6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALaSKTPDV--LLSDIRMPGMDGLALLKQIKQ--RHPMLPVIIM 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1228082595 1336 TAKAmagDREKSLAA---GASDYVTKPVDAKELLTCIRRWIA 1374
Cdd:PRK10923    82 TAHS---DLDAAVSAyqqGAFDYLPKPFDIDEAVALVERAIS 120
PRK15369 PRK15369
two component system response regulator;
1256-1358 2.90e-05

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 46.61  E-value: 2.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDA------RNVLAIAEMLKLhglsVEHAPNGRKGIEALRD-SPDIdlILMDVMMPEMDGYATTAAIRRmpRFG 1328
Cdd:PRK15369     5 KILLVDDHEliingiKNMLAPYPRYKI----VGQVDNGLEVYNACRQlEPDI--VILDLGLPGMNGLDVIPQLHQ--RWP 76
                           90       100       110
                   ....*....|....*....|....*....|
gi 1228082595 1329 SLPIIMVTAKAMAGDREKSLAAGASDYVTK 1358
Cdd:PRK15369    77 AMNILVLTARQEEHMASRTLAAGALGYVLK 106
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
1259-1359 3.39e-05

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: 44.07  E-value: 3.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1259 LIDDDARNVLAIAEM-LKLHGLSVEHAPNGRKGIEALrDSPDIDLILMDVMMPEMDGYATTAAIRRmpRFGSLPIIMVTA 1337
Cdd:cd19926      2 LVVDDEPDIRELLEItLGRMGLDVRSARNVKEARELL-ASEPYDLCLTDMRLPDGSGLELVQHIQQ--RLPQTPVAVITA 78
                           90       100
                   ....*....|....*....|..
gi 1228082595 1338 KAMAGDREKSLAAGASDYVTKP 1359
Cdd:cd19926     79 YGSLDTAIEALKAGAFDFLTKP 100
PLN03029 PLN03029
type-a response regulator protein; Provisional
1257-1365 5.33e-05

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 46.18  E-value: 5.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEAL------RDSPD-------------IDLILMDVMMPEMDGYAT 1317
Cdd:PLN03029    11 VLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLglheddRSNPDtpsvspnshqeveVNLIITDYCMPGMTGYDL 90
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1228082595 1318 TAAIRRMPRFGSLPIIMVTAKAMAGDREKSLAAGASDYVTKPVDAKEL 1365
Cdd:PLN03029    91 LKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDL 138
HAMP_2 pfam18947
HAMP domain;
271-330 6.52e-05

HAMP domain;


Pssm-ID: 465927 [Multi-domain]  Cd Length: 67  Bit Score: 42.09  E-value: 6.52e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  271 GTWRDLTTSVNFMAGNLTAQVRSIAQVATAVARGDLSQKITVDARGEIFELKSTINTMVD 330
Cdd:pfam18947    4 GDFRKIVEGVNNTLDAIITPLNEAADYVDRISKGDIPEKITDEYKGDFNEIKNNLNALID 63
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
1255-1314 7.39e-05

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: 43.58  E-value: 7.39e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1228082595 1255 RRVLLIDDDARNVLAIAEML-KLHGLSVEHAPNGRKGIEALRDSpDIDLILMDVMMPEMDG 1314
Cdd:cd17530      1 LRVLVLDDDPFQCMMAATILeDLGPGNVDEADDGREALVILLCN-APDIIICDLKMPDMDG 60
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
950-1079 7.85e-05

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: 43.77  E-value: 7.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  950 AEKGLEFEAVVDPDVpeQLSTDEQRLRQVLRNMLSNAVKFTEKgkvklRVRlVPADQVPGGgaddpwLAFSVIDTGIGIA 1029
Cdd:cd16954     15 QRKGVSISLDISPEL--RFPGERNDLMELLGNLLDNACKWCLE-----FVE-VTARQTDGG------LHLIVDDDGPGVP 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1228082595 1030 EENLSTIFGAFQQADgtTSRRygGTGLGLSISRQVANLLGGELRA-QSRLG 1079
Cdd:cd16954     81 ESQRSKIFQRGQRLD--EQRP--GQGLGLAIAKEIVEQYGGELSLsDSPLG 127
PHA02515 PHA02515
hypothetical protein; Provisional
195-631 1.26e-04

hypothetical protein; Provisional


Pssm-ID: 107197 [Multi-domain]  Cd Length: 508  Bit Score: 46.31  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  195 LTAQVRSIAE----VTTAVAKGDLSQKITVDARGEILELKSTIN---TMVDQLSSFADEVTRVAREVGTEGILGGQAQVP 267
Cdd:PHA02515   114 LVIQIQQLADklsrTVQAPISGGLSSSEILEQLAEQLPLVSAVYghlANIDAVATNEADIDTVAASVGAVDTVAGDLGGT 193
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  268 GVAGTWRDLTTSVNFMAGNLTAQVRSIAQVATAVArgdlsqkiTVDARGEIFELKSTINTMVDQLSSFADEVTRVAREVG 347
Cdd:PHA02515   194 WAAGVSYDFGSIAVPPIGNTSPPGGNIVIVANSIG--------NVDTVAENIGDVSTVSTHLSSMLAVANDIDSVVSVAG 265
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  348 TEGRLGGQADVKGVSGTWKGLTESVNVMADNLTDqVRSIAqvsaavarGDLSQritVEAkgeVAGLAQTINTMVDTlsaf 427
Cdd:PHA02515   266 DLENIDAVADNAANINTVAGANANVNTVASNILD-VGTVA--------GNIDD---VQA---VAGNAANINVVADN---- 326
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  428 ADEVTRVArevgtegilGGQARVANVAGTwkdltdnvnsmANNLTGQVRSIAQVTTAVARGNlsqKIDVDARGEilelkT 507
Cdd:PHA02515   327 ADNINATA---------ANQANINAAVGN-----------ADNINAAVANQANINAVVGNAN---NINAVAANE-----G 378
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  508 TINTMVD------TLSSFAAEVTRVAREVGKEGQLGGQAEVEGVSGTWKRLTENVNELA-GNLTRQVRAIAEVTSAVATg 580
Cdd:PHA02515   379 NVNTVVDnladvqTVAGIAADVSTVAENEAAVAALGNDLTGQPMVIDYGDLSPASNPAApAGVLGAVWANAENIAAVAE- 457
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1228082595  581 dlTRSITVEAKGEVSELKDNIN-AMVRSLRETTLANQDQDWLNTNLARISGL 631
Cdd:PHA02515   458 --NIAVIIEAANNLPAILAALSgALVPANNLSDLADPAAARANIGLADLGGI 507
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
98-160 1.36e-04

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: 46.11  E-value: 1.36e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1228082595   98 AMAGNLTAQVRDIAGVATAVARGDLSQKITVQVRGELLELKNTINTMVDQLSSFADEVTRVAR 160
Cdd:COG5000     28 LLARRLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARAFNRMTDQLKEQREELEERRR 90
PRK10816 PRK10816
two-component system response regulator PhoP;
1256-1366 1.70e-04

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 44.73  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDA--RNVLAIaeMLKLHGLSVEHAPNGRKGIEALRDS-PDIDLIlmDVMMPEMDGyatTAAIRR-MPRFGSLP 1331
Cdd:PRK10816     2 RVLVVEDNAllRHHLKV--QLQDAGHQVDAAEDAKEADYYLNEHlPDIAIV--DLGLPDEDG---LSLIRRwRSNDVSLP 74
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1228082595 1332 IIMVTAKAMAGDREKSLAAGASDYVTKPVDAKELL 1366
Cdd:PRK10816    75 ILVLTARESWQDKVEVLSAGADDYVTKPFHIEEVM 109
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
1256-1358 3.03e-04

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 43.86  E-value: 3.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLSVEHAPNGRKGIEA-LRDSPDidLILMDVMMPEMDGYATTAAIRrmPRFGSlPIIM 1334
Cdd:PRK10701     3 KIVFVEDDAEVGSLIAAYLAKHDIDVTVEPRGDRAEATiLREQPD--LVLLDIMLPGKDGMTICRDLR--PKWQG-PIVL 77
                           90       100
                   ....*....|....*....|....
gi 1228082595 1335 VTAKAMAGDREKSLAAGASDYVTK 1358
Cdd:PRK10701    78 LTSLDSDMNHILALEMGACDYILK 101
PRK09483 PRK09483
response regulator; Provisional
1257-1374 3.57e-04

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 43.56  E-value: 3.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLK-LHGLSVE-HAPNGRKGIEALRDSpDIDLILMDVMMPEMDGYATTaaiRRMPRFGS-LPII 1333
Cdd:PRK09483     4 VLLVDDHELVRAGIRRILEdIKGIKVVgEACCGEDAVKWCRTN-AVDVVLMDMNMPGIGGLEAT---RKILRYTPdVKII 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1228082595 1334 MVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIR------RWIA 1374
Cdd:PRK09483    80 MLTVHTENPLPAKVMQAGAAGYLSKGAAPQEVVSAIRsvhsgqRYIA 126
PRK10693 PRK10693
two-component system response regulator RssB;
1284-1360 4.86e-04

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 43.83  E-value: 4.86e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1228082595 1284 APNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRmpRFGSLPIIMVTAKAMAGDREKSLAAGASDYVTKPV 1360
Cdd:PRK10693     3 AANGVDALELLGGFT-PDLIICDLAMPRMNGIEFVEHLRN--RGDQTPVLVISATENMADIAKALRLGVQDVLLKPV 76
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
1113-1193 6.02e-04

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: 40.93  E-value: 6.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1113 VLVVEageDQllTLLVRGFATDLADAREAVDVESVAMpdEAMERLAAGPVQCVVLDASLPGAAALTFLQRLADGDYRVPV 1192
Cdd:cd17624      1 ILLVE---DD--ALLGDGLKTGLRKAGYAVDWVRTGA--EAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPV 73

                   .
gi 1228082595 1193 L 1193
Cdd:cd17624     74 L 74
fixJ PRK09390
response regulator FixJ; Provisional
1257-1376 7.47e-04

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 42.30  E-value: 7.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDARNVLAIAEMLKLHGLSV---EHAPNGRKGIEALRDSpdidLILMDVMMPEMDGyatTAAIRRMPRFGS-LPI 1332
Cdd:PRK09390     6 VHVVDDDEAMRDSLAFLLDSAGFEVrlfESAQAFLDALPGLRFG----CVVTDVRMPGIDG---IELLRRLKARGSpLPV 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1228082595 1333 IMVTAKA---MAGDREKslaAGASDYVTKPVDAKELLTCIRRWIAAA 1376
Cdd:PRK09390    79 IVMTGHGdvpLAVEAMK---LGAVDFIEKPFEDERLIGAIERALAQA 122
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
971-1089 1.22e-03

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: 39.83  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  971 DEQRLRQVLRNMLSNAVKFTE---KGKVKLRVRlVPADQvpgggadDPWLAFSVIDTGIGIAEENLSTIFGAFqqadgtT 1047
Cdd:cd16944      1 DTTQISQVLTNILKNAAEAIEgrpSDVGEVRIR-VEADQ-------DGRIVLIVCDNGKGFPREMRHRATEPY------V 66
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1228082595 1048 SRRYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVP 1089
Cdd:cd16944     67 TTRPKGTGLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
PRK10600 PRK10600
nitrate/nitrite two-component system sensor histidine kinase NarX;
382-435 1.36e-03

nitrate/nitrite two-component system sensor histidine kinase NarX;


Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 43.12  E-value: 1.36e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1228082595  382 QVRSIAQvsaAVARGDLSQRITVEAKGEVAGLAQTINTMVDTLSA-FADEVTRVA 435
Cdd:PRK10600   155 QLLSMAN---AVSHRDFTQRANISGRDEMAMLGTALNNMSAELAEsYAVLEQRVQ 206
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
1113-1194 1.90e-03

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: 39.44  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1113 VLVVEagEDQLLTLLVRGFATDladarEAVDVESVAMPDEAMERLAAGPVQCVVLDASLPGAAALTFLQRLADGDYRVPV 1192
Cdd:pfam00072    1 VLIVD--DDPLIRELLRQLLEK-----EGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPV 73

                   ..
gi 1228082595 1193 LA 1194
Cdd:pfam00072   74 II 75
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
975-1089 2.16e-03

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: 38.69  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  975 LRQVLRNMLSNAVKFTEKGKVklRVRLVpadqvpgggADDPWLAFSVIDTGIGIAEENlstifgafqqadgttsrRYGGT 1054
Cdd:cd16917      1 LYRIVQEALTNALKHAGASRV--RVTLS---------YTADELTLTVVDDGVGFDGPA-----------------PPGGG 52
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1228082595 1055 GLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVP 1089
Cdd:cd16917     53 GFGLLGMRERAELLGGTLTIGSRPGGGTRVTARLP 87
PRK11173 PRK11173
two-component response regulator; Provisional
1256-1365 2.51e-03

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 41.15  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDA--RNVL-AIAEMlklHGLSVEHAPNGRKGIEALRDSpDIDLILMDVMMPEMDGYATTAAIRRMprfGSLPI 1332
Cdd:PRK11173     5 HILIVEDELvtRNTLkSIFEA---EGYDVFEATDGAEMHQILSEN-DINLVIMDINLPGKNGLLLARELREQ---ANVAL 77
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1228082595 1333 IMVTAKAMAGDREKSLAAGASDYVTKPVDAKEL 1365
Cdd:PRK11173    78 MFLTGRDNEVDKILGLEIGADDYITKPFNPREL 110
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
1256-1376 2.66e-03

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 40.99  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHGLS--VEHAPNGRKGIeALRDSPDIDLILMDVMMPEMDGYATTAAIRRMPRfgSLPII 1333
Cdd:PRK10403     8 QVLIVDDHPLMRRGVRQLLELDPGFevVAEAGDGASAI-DLANRLDPDVILLDLNMKGMSGLDTLNALRRDGV--TAQII 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1228082595 1334 MVTAKAMAGDREKSLAAGASDYVTKPVDAKELLTCIRRWIAAA 1376
Cdd:PRK10403    85 ILTVSDASSDVFALIDAGADGYLLKDSDPEVLLEAIRAGAKGS 127
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
871-1093 2.68e-03

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 41.14  E-value: 2.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  871 LTSLLILAGVLSQNSTQNLTPKQVEFAKVIESAgTDLLQLINDILDlskveagkmDIHPELVELRQQVEYVRTTFQPLTA 950
Cdd:COG4585     69 LSAIKLQLEAARRLLDADPEAAREELEEIRELA-REALAELRRLVR---------GLRPPALDDLGLAAALEELAERLLR 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  951 EKGLEFEAVVDPDVPEQLSTDEQRLRQVLRNMLSNAVKFTEKGKVKLRVRlvpadqvpgggADDPWLAFSVIDTGIGIAE 1030
Cdd:COG4585    139 AAGIRVELDVDGDPDRLPPEVELALYRIVQEALTNALKHAGATRVTVTLE-----------VDDGELTLTVRDDGVGFDP 207
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1228082595 1031 EnlstifgafqqadgttsrRYGGTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVPVTPD 1093
Cdd:COG4585    208 E------------------AAPGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPLAAA 252
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
1110-1193 3.89e-03

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: 39.90  E-value: 3.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1110 ARRVLVVEaGEDQLLTLLVRGFAtdladaREAVDVESVAMPDEAMERLAAGPVQCVVLDASLPGAAALTFLQRL--ADGD 1187
Cdd:COG4567      4 DRSLLLVD-DDEAFARVLARALE------RRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALreRDPD 76

                   ....*.
gi 1228082595 1188 YRVPVL 1193
Cdd:COG4567     77 ARIVVL 82
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
975-1089 6.07e-03

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: 39.25  E-value: 6.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595  975 LRQVLRNMLSNAVKFTEKGK-----VKLRVRLvpadqvpgggaDDPWLAFSVIDTGIGIAEENLSTIF------------ 1037
Cdd:cd16929     48 LFELLKNAMRATVESHGDDSddlppIKVTVAK-----------GDEDLTIKISDRGGGIPREDLARLFsymystapqpsl 116
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1228082595 1038 --GAFQQADGTTSRRYGgTGLGLSISRQVANLLGGELRAQSRLGAGSTFTLYVP 1089
Cdd:cd16929    117 ddFSDLISGTQPSPLAG-FGYGLPMSRLYAEYFGGDLDLQSMEGYGTDVYIYLK 169
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
1260-1360 7.02e-03

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 37.64  E-value: 7.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1260 IDDDARNVLAIAEMLKLH---GLSVEHAPNGRKGI-EALRDSPDIDLIlmDVMMPEMDGYATTAAIRrmPRFGSLPIIM- 1334
Cdd:cd17565      3 IVDDDKNIIKILSDIIEDddlGEVVGEADNGAQAYdEILFLQPDIVLI--DLLMPGMDGIQLVRKLK--DTGSNGKFIMi 78
                           90       100
                   ....*....|....*....|....*...
gi 1228082595 1335 --VTAKAMagdREKSLAAGASDYVTKPV 1360
Cdd:cd17565     79 sqVSDKEM---IGKAYQAGIEFFINKPI 103
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
1256-1371 7.70e-03

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: 38.12  E-value: 7.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1256 RVLLIDDDARNVLAIAEMLKLHgLSVEHAPNGRKGIEALRDSPdIDLILMDVMMPEMDGYATTAAIRRmpRFGSLPIIMV 1335
Cdd:cd17596      2 TILVVDDEVRSLEALRRTLEED-FDVLTAASAEEALAILEEEW-VQVILCDQRMPGTTGVEFLKEVRE--RWPEVVRIII 77
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1228082595 1336 TAKAMAGDREKSL-AAGASDYVTKPVDAKELLTCIRR 1371
Cdd:cd17596     78 SGYTDSEDIIAGInEAGIYQYLTKPWHPDQLLLTVRN 114
PRK10430 PRK10430
two-component system response regulator DcuR;
1257-1371 7.74e-03

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 39.71  E-value: 7.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228082595 1257 VLLIDDDArnvlAIAEMLKLHGLSVE------HAPNGRKGIEALRDSP-DIDLILMDVMMPEMDGYATTAAIRRMPRfgS 1329
Cdd:PRK10430     4 VLIVDDDA----MVAELNRRYVAQIPgfqccgTASTLEQAKEIIFNSDtPIDLILLDIYMQQENGLDLLPVLHEAGC--K 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1228082595 1330 LPIIMVTAKAMAGDREKSLAAGASDYVTKPVDA---KELLTCIRR 1371
Cdd:PRK10430    78 SDVIVISSAADAATIKDSLHYGVVDYLIKPFQAsrfEEALTGWRQ 122
 
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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