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Conserved domains on  [gi|739103821|ref|WP_036974399|]
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MULTISPECIES: response regulator [Pseudoalteromonas]

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
597-1116 1.02e-107

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: 359.16  E-value: 1.02e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  597 AKEAAEQAVKAKSEFLASMSHEIRTPMNGVIG----MLniikQTKLDSQQNHHIQLAQSSAESLLHIINDILDFSKIEAG 672
Cdd:PRK11107  282 AKKRAQEAARIKSEFLANMSHELRTPLNGVIGftrqTL----KTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAG 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  673 KLDIENISFNVSKLLGDTVESFAIKAEQNNTKLVLDatqINH---EFIVSDPNRIRQIINNLLGNAIKFTKDGEIIVLAT 749
Cdd:PRK11107  358 KLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLN---IDPdvpDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVE 434
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  750 VKPI-DDAMYLDCSVVDSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTFNF 828
Cdd:PRK11107  435 LRALsNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWF 514
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  829 SIkvKLDYKKQSLEPSHIIDK---KQILIADSCTLSSNIAKKQLQLWGAEVEEINDMASLLNRAkqqngqrcdaifVDYq 905
Cdd:PRK11107  515 HL--PLDLNPNPIIDGLPTDClagKRLLYVEPNSAAAQATLDILSETPLEVTYSPTLSQLPEAH------------YDI- 579
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  906 LYMQASAAEKQAFKTHFN-----ATRCKRILMAPMSlTEKQTRQTLK---VESIIFKPLTPSDLFNSLANDKY------I 971
Cdd:PRK11107  580 LLLGLPVTFREPLTMLHErlakaKSMTDFLILALPC-HEQVLAEQLKqdgADACLSKPLSHTRLLPALLEPCHhkqpplL 658
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  972 EQQQINKETLvkkvatyTVnsasqiLLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMP 1051
Cdd:PRK11107  659 PPTDESRLPL-------TV------MAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQR---PFDLILMDIQMP 722
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739103821 1052 EMDGYQATRAIRngdAGTAHREVSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKLSVW 1116
Cdd:PRK11107  723 GMDGIRACELIR---QLPHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRY 784
CHASE COG3452
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction ...
10-727 1.54e-83

Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction mechanisms];


:

Pssm-ID: 442675 [Multi-domain]  Cd Length: 785  Bit Score: 289.13  E-value: 1.54e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   10 KKLRKLRLAFWFSLALIVLIGFVLDHINYNRGKDAFRSQELAKLSAYRAELESILISNIQLVRGLAVAVAAEPNLDQTRF 89
Cdd:COG3452     8 LLRRRPLLLALLAFLLLLAVGAVLERLLREQEEQQLRAEVLQELSAIRARLEGELNARLSLLRGLAALVEANPGISQEEF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   90 AQIAAPLFETSSELRNIGGAPDMVIRMAYPLEGNEKSIGLNFLENAAQRDDAIKARDENTIVMAGPLELVQGGHALVARM 169
Cdd:COG3452    88 ERLARNLLEDYPGIRNIALAPDGVIRYVYPLAGNEAALGLDLRTDPEQRAAALRARESGQLVLAGPVNLVQGGRGLIGRL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  170 PVFMPPDH-KFWGLLSVVLDINKIYTNSGLVSLGNHYDVALQGRNGKGQHGEFFYGQKHILENTPLSFSITFPGGEWRMY 248
Cdd:COG3452   168 PVFLDGGDdRFWGFVSAVIDLDRLLDSAGLDDAQDGYQIALRGRDGDGAEGEVFYGDAALFDQDPVTLEVNLPGGSWQLA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  249 VAPKAGWSPPSSTIWPLRIAIILVCALFASASLFFLKMLERQYKSERMLETMSSLAKIgAWSFNLETKSMYWSDMTKQIF 328
Cdd:COG3452   248 AAPKGGWLASPRNALPLRLAGLLISLLLALLVYLLRQLLLLRLLLLLLRLELIAAALL-LLLLALDLLLELLLLLRLAEA 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  329 NYPINKQPEWPTNFNGFKAGFSRDKIRHLYEQALKHGKSFETQIQIINAKGDAVWVLVHCEAEHKNGRCIKLFgSIQDID 408
Cdd:COG3452   327 LLQERLRALALLAALEDLLLLKFDRDLLDLLLLLELEAILALLLLLRRLLRSREARGGLGGDLVRVGGVIDGR-VAVILI 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  409 ARKLIELENQKIALHNEILASLTVNDAVLTGNLNLskhVIVQAICHALNVDRASIWLFSDDRQSLNTFAIHDQSNPQFSD 488
Cdd:COG3452   406 IEALELAEARLAALDQERDASDVALGAALVVLEAL---LIIALLRELALLAGALLARKSLLLALDLAAESERLRYLELLL 482
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  489 -PISLQQIEVQNYFDAINNNAVINASDAQQHPFTKDLYTDYLDKFDIRSLLTVIIPTGSKTMGVVCAEKCHSRQQWSKNE 567
Cdd:COG3452   483 gDALRERIRRALLRLQLLSLDLSALAAVLGAESLAGLLISVFIDARILEAERLELALVAGEVALEELLLRLLGEILLLRA 562
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  568 ESFLIAVAALIGSLHASQRRIETEQQLVKAKEAAEQAVKAKSEFLASMSHEIRtpMNGVIGMLNIIKQTKLDSQQNHHIQ 647
Cdd:COG3452   563 ELILALLDAKSGLSALELSGLLAGRAALDSLLLLLALALRQLDESALFILEEL--LLRLIIDLRIERLLLLLLGGEILLG 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  648 LAQSSAESLLHIINDILDFSKIEAGkLDIENISFNVSKLLGDTVESFAIKAEQNNTKLVLDATQINHEFIVSDPNRIRQI 727
Cdd:COG3452   641 ELALLLLLLVLIILILLSVEEAGLI-LALSLLLALLLLAILDAAVSLLATLLLLFQLLLLLLIILEGLLAELVAEALRLA 719
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
597-1116 1.02e-107

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 359.16  E-value: 1.02e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  597 AKEAAEQAVKAKSEFLASMSHEIRTPMNGVIG----MLniikQTKLDSQQNHHIQLAQSSAESLLHIINDILDFSKIEAG 672
Cdd:PRK11107  282 AKKRAQEAARIKSEFLANMSHELRTPLNGVIGftrqTL----KTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAG 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  673 KLDIENISFNVSKLLGDTVESFAIKAEQNNTKLVLDatqINH---EFIVSDPNRIRQIINNLLGNAIKFTKDGEIIVLAT 749
Cdd:PRK11107  358 KLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLN---IDPdvpDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVE 434
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  750 VKPI-DDAMYLDCSVVDSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTFNF 828
Cdd:PRK11107  435 LRALsNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWF 514
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  829 SIkvKLDYKKQSLEPSHIIDK---KQILIADSCTLSSNIAKKQLQLWGAEVEEINDMASLLNRAkqqngqrcdaifVDYq 905
Cdd:PRK11107  515 HL--PLDLNPNPIIDGLPTDClagKRLLYVEPNSAAAQATLDILSETPLEVTYSPTLSQLPEAH------------YDI- 579
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  906 LYMQASAAEKQAFKTHFN-----ATRCKRILMAPMSlTEKQTRQTLK---VESIIFKPLTPSDLFNSLANDKY------I 971
Cdd:PRK11107  580 LLLGLPVTFREPLTMLHErlakaKSMTDFLILALPC-HEQVLAEQLKqdgADACLSKPLSHTRLLPALLEPCHhkqpplL 658
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  972 EQQQINKETLvkkvatyTVnsasqiLLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMP 1051
Cdd:PRK11107  659 PPTDESRLPL-------TV------MAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQR---PFDLILMDIQMP 722
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739103821 1052 EMDGYQATRAIRngdAGTAHREVSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKLSVW 1116
Cdd:PRK11107  723 GMDGIRACELIR---QLPHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRY 784
CHASE COG3452
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction ...
10-727 1.54e-83

Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 442675 [Multi-domain]  Cd Length: 785  Bit Score: 289.13  E-value: 1.54e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   10 KKLRKLRLAFWFSLALIVLIGFVLDHINYNRGKDAFRSQELAKLSAYRAELESILISNIQLVRGLAVAVAAEPNLDQTRF 89
Cdd:COG3452     8 LLRRRPLLLALLAFLLLLAVGAVLERLLREQEEQQLRAEVLQELSAIRARLEGELNARLSLLRGLAALVEANPGISQEEF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   90 AQIAAPLFETSSELRNIGGAPDMVIRMAYPLEGNEKSIGLNFLENAAQRDDAIKARDENTIVMAGPLELVQGGHALVARM 169
Cdd:COG3452    88 ERLARNLLEDYPGIRNIALAPDGVIRYVYPLAGNEAALGLDLRTDPEQRAAALRARESGQLVLAGPVNLVQGGRGLIGRL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  170 PVFMPPDH-KFWGLLSVVLDINKIYTNSGLVSLGNHYDVALQGRNGKGQHGEFFYGQKHILENTPLSFSITFPGGEWRMY 248
Cdd:COG3452   168 PVFLDGGDdRFWGFVSAVIDLDRLLDSAGLDDAQDGYQIALRGRDGDGAEGEVFYGDAALFDQDPVTLEVNLPGGSWQLA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  249 VAPKAGWSPPSSTIWPLRIAIILVCALFASASLFFLKMLERQYKSERMLETMSSLAKIgAWSFNLETKSMYWSDMTKQIF 328
Cdd:COG3452   248 AAPKGGWLASPRNALPLRLAGLLISLLLALLVYLLRQLLLLRLLLLLLRLELIAAALL-LLLLALDLLLELLLLLRLAEA 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  329 NYPINKQPEWPTNFNGFKAGFSRDKIRHLYEQALKHGKSFETQIQIINAKGDAVWVLVHCEAEHKNGRCIKLFgSIQDID 408
Cdd:COG3452   327 LLQERLRALALLAALEDLLLLKFDRDLLDLLLLLELEAILALLLLLRRLLRSREARGGLGGDLVRVGGVIDGR-VAVILI 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  409 ARKLIELENQKIALHNEILASLTVNDAVLTGNLNLskhVIVQAICHALNVDRASIWLFSDDRQSLNTFAIHDQSNPQFSD 488
Cdd:COG3452   406 IEALELAEARLAALDQERDASDVALGAALVVLEAL---LIIALLRELALLAGALLARKSLLLALDLAAESERLRYLELLL 482
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  489 -PISLQQIEVQNYFDAINNNAVINASDAQQHPFTKDLYTDYLDKFDIRSLLTVIIPTGSKTMGVVCAEKCHSRQQWSKNE 567
Cdd:COG3452   483 gDALRERIRRALLRLQLLSLDLSALAAVLGAESLAGLLISVFIDARILEAERLELALVAGEVALEELLLRLLGEILLLRA 562
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  568 ESFLIAVAALIGSLHASQRRIETEQQLVKAKEAAEQAVKAKSEFLASMSHEIRtpMNGVIGMLNIIKQTKLDSQQNHHIQ 647
Cdd:COG3452   563 ELILALLDAKSGLSALELSGLLAGRAALDSLLLLLALALRQLDESALFILEEL--LLRLIIDLRIERLLLLLLGGEILLG 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  648 LAQSSAESLLHIINDILDFSKIEAGkLDIENISFNVSKLLGDTVESFAIKAEQNNTKLVLDATQINHEFIVSDPNRIRQI 727
Cdd:COG3452   641 ELALLLLLLVLIILILLSVEEAGLI-LALSLLLALLLLAILDAAVSLLATLLLLFQLLLLLLIILEGLLAELVAEALRLA 719
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
551-1124 1.20e-74

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: 267.41  E-value: 1.20e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   551 VVCAEKCHSRQQWSKNEESFLIAVAALIGSLHASQRRIETE-QQLVKAKEAAEQAVKAKSEFLASMSHEIRTPMNGVIGM 629
Cdd:TIGR02956  406 KLQADERQVAQELQEHKESLEQLVAQRTQELAETNERLNAEvKNHAKARAEAEEANRAKSAFLATMSHEIRTPLNGILGT 485
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   630 LNIIKQTKLDSQQNHHIQLAQSSAESLLHIINDILDFSKIEAGKLDIENISFNVSKLLGDTVESFAIKAEQNNTKLVLDA 709
Cdd:TIGR02956  486 LELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNI 565
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   710 TQINHEFIVSDPNRIRQIINNLLGNAIKFTKDGEiIVLATvkPIDDAMYLDCSVVDSGVGIKPEKQATLFDSFTQADAst 789
Cdd:TIGR02956  566 PEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGS-VVLRV--SLNDDSSLLFEVEDTGCGIAEEEQATLFDAFTQADG-- 640
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   790 TRRYGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTFNFSIKVKldykkqslepshiidkkqiliadsctlssniakkql 869
Cdd:TIGR02956  641 RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLT------------------------------------ 684
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   870 qlwgaeveeindmasllnrakqqngqrcdaifvdyqlymQASAAEKQAFKTHFNatrckrilmapmsltekqtrqtlkve 949
Cdd:TIGR02956  685 ---------------------------------------RGKPAEDSATLTVID-------------------------- 699
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   950 siifkpltpsdlfnslandkyieqqqinketlvkkvatytVNSAsQILLVEDNKVNQMVAGALLKQAGISFDIAENGLEA 1029
Cdd:TIGR02956  700 ----------------------------------------LPPQ-RVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSA 738
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  1030 IAKIANREhmpYELILMDCQMPEMDGYQATRAIRNGDAgtAHREVSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSL 1109
Cdd:TIGR02956  739 LECFHQHA---FDLALLDINLPDGDGVTLLQQLRAIYG--AKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQL 813
                          570
                   ....*....|....*..
gi 739103821  1110 NKKLSVWL--DTHQERE 1124
Cdd:TIGR02956  814 TAMIAVILagGKSNTEA 830
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
567-830 1.91e-74

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 249.83  E-value: 1.91e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  567 EESFLIAVAALIGSLHASQRRIETEQQLVKAKEAAEQAVKAKSEFLASMSHEIRTPMNGVIGMLNIIKQTkLDSQQNHHI 646
Cdd:COG0642    69 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE-LDEEQREYL 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  647 QLAQSSAESLLHIINDILDFSKIEAGKLDIENISFNVSKLLGDTVESFAIKAEQNNTKLVLDATQiNHEFIVSDPNRIRQ 726
Cdd:COG0642   148 ETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPD-DLPTVRGDPDRLRQ 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  727 IINNLLGNAIKFTKDGEIIVLaTVKPIDDAMYLdcSVVDSGVGIKPEKQATLFDSFTQADASttRRYGGTGLGLAIVKQL 806
Cdd:COG0642   227 VLLNLLSNAIKYTPEGGTVTV-SVRREGDRVRI--SVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRI 301
                         250       260
                  ....*....|....*....|....
gi 739103821  807 CKLMQGDVNVVSSYGEGSTFNFSI 830
Cdd:COG0642   302 VELHGGTIEVESEPGKGTTFTVTL 325
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
724-832 3.33e-49

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: 169.60  E-value: 3.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  724 IRQIINNLLGNAIKFTKDGEIIVLATVKPIDDAMY-LDCSVVDSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLGLAI 802
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVqLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 739103821  803 VKQLCKLMQGDVNVVSSYGEGSTFNFSIKV 832
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
720-833 8.27e-33

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 122.76  E-value: 8.27e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821    720 DPNRIRQIINNLLGNAIKFTKDGEIIVLaTVKPIDDAMYLdcSVVDSGVGIKPEKQATLFDSFTQADaSTTRRYGGTGLG 799
Cdd:smart00387    2 DPDRLRQVLSNLLDNAIKYTPEGGRITV-TLERDGDHVEI--TVEDNGPGIPPEDLEKIFEPFFRTD-KRSRKIGGTGLG 77
                            90       100       110
                    ....*....|....*....|....*....|....
gi 739103821    800 LAIVKQLCKLMQGDVNVVSSYGEGSTFNFSIKVK 833
Cdd:smart00387   78 LSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
CHASE smart01079
This domain is found in the extracellular portion of receptor-like proteins - such as serine ...
60-209 1.66e-28

This domain is found in the extracellular portion of receptor-like proteins - such as serine/threonine kinases and adenylyl cyclases; Predicted to be a ligand binding domain.


Pssm-ID: 215015  Cd Length: 176  Bit Score: 112.81  E-value: 1.66e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821     60 LESILISNIQLVRGLAVAvaaePNLDQTRFAQIAAPLFETSSELRNIGGAPDM------VIRMAYPLEGNEKSIGLNFLE 133
Cdd:smart01079   14 LELQLNRRLPGIQGLGWA----PRVPPAERAAFEAALRAGGPGLFNIRLAPDGerdeyfVITYIEPLAGNEAALGLDLLS 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821    134 NAAQRDDAIKARDENTIVMAGPLELVQGGH---ALVARMPVFMPPD------HKFWGLLSVVLDINKIYTNSGLVSLGNH 204
Cdd:smart01079   90 EPVRRAALERARDSGRPVLSGPVTLVQGTGdgrGFLLRLPVYRGGPptstrrEALWGFVSAVFRLDDLLEGLLGALDLPG 169

                    ....*
gi 739103821    205 YDVAL 209
Cdd:smart01079  170 LDLAL 174
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
720-833 7.10e-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: 108.61  E-value: 7.10e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   720 DPNRIRQIINNLLGNAIKFTKDGEIIvlaTVKpIDDAMYLDCSVVDSGVGIKPEKQATLFDSFTQADastTRRYGGTGLG 799
Cdd:pfam02518    2 DELRLRQVLSNLLDNALKHAAKAGEI---TVT-LSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGGTGLG 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 739103821   800 LAIVKQLCKLMQGDVNVVSSYGEGSTFNFSIKVK 833
Cdd:pfam02518   75 LSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
611-826 3.26e-26

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 114.35  E-value: 3.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  611 FLASMSHEIRTPMNGVIGMLNII--KQTKLDSQQNHHIQLAQSSAESLLHIINDILDFSKIEAG--KLDIENIsfNVSKL 686
Cdd:NF040691  274 FVSDVSHELRTPLTTIRMAADVIhdSRDDFDPATARSAELLHTELDRFESLLSDLLEISRFDAGaaELDVEPV--DLRPL 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  687 LGDTVESFAIKAEQNNTKLVLDA--TQINHEFivsDPNRIRQIINNLLGNAIKFTKDGEIIVlaTVKPIDDAMYLdcSVV 764
Cdd:NF040691  352 VRRVVDALRQLAERAGVELRVDApgTPVVAEV---DPRRVERVLRNLVVNAIEHGEGKPVVV--TVAQDDTAVAV--TVR 424
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739103821  765 DSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTF 826
Cdd:NF040691  425 DHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQF 486
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
592-802 1.47e-22

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 102.21  E-value: 1.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  592 QQLVKAKEAAEQAVKAKSEFLASMSHEIRTPMNGVIGMLNIIkQTKLDSQQNHHIQLAQSSAESLLHIINDILDFSKIEA 671
Cdd:NF012163  224 QDFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRAELEAI-QDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDE 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  672 GKLDIENISFNVSKLLGDTVESFAIKAEQNNTKLVLDATqiNHEFIVSDPNRIRQIINNLLGNAIKFTKD-GEIIVLATV 750
Cdd:NF012163  303 GALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLP--DSSLVFGDRDRLMQLFNNLLENSLRYTDSgGSLHISASQ 380
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 739103821  751 KPIDDAMYLDcsvvDSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLGLAI 802
Cdd:NF012163  381 RPKEVTLTVA----DSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAI 428
CHASE pfam03924
CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - ...
82-223 1.20e-13

CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - such as serine/threonine kinases and adenylyl cyclases. This is a ligand-binding domain that binds cytokinin (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 427591  Cd Length: 184  Bit Score: 70.40  E-value: 1.20e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821    82 PNLDQTRFAQIAAPLFETSSELRNIG--------------------GAPDMVIR------------MAYPLEGNEKSIGL 129
Cdd:pfam03924    1 DSVDREEFRRYAASLLLRRPGIQGLGwaprvpaaeraafeaavraeGFPDFTIRpagdrdeyfpiiYIEPLAGNNRALGF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   130 NFLENAAQRDDAIKARDENTIVMAGPLELVQGGH---ALVARMPVFMPPDH--------KFWGLLSVVLDINKIYtnSGL 198
Cdd:pfam03924   81 DMASEPVRREAIERARDTGEPVLSGPVTLVQDGDgqpGFLLYLPVYRGGPPdtvaerraALLGFVYAPFRIDDLL--EAA 158
                          170       180
                   ....*....|....*....|....*.
gi 739103821   199 VSLGNHYDVALQGRNG-KGQHGEFFY 223
Cdd:pfam03924  159 LLRLGEDGLDLALYDGtSASAPELLY 184
PRK11061 PRK11061
phosphoenolpyruvate--protein phosphotransferase;
440-576 7.66e-06

phosphoenolpyruvate--protein phosphotransferase;


Pssm-ID: 182937 [Multi-domain]  Cd Length: 748  Bit Score: 49.99  E-value: 7.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  440 NLNLSKHVIVQAICHALNVDRASIWLFSDDRQSLNTFAIHDQSNPQfSDPISLqqievqnyfdAINNNAV---------I 510
Cdd:PRK11061   17 RLNEALDILVTETCLAMDTEVCSVYLADHDRRCYYLMATRGLKKPR-GRTVTL----------AFDEGIVglvgrlaepI 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739103821  511 NASDAQQHPFTKdlYTDYLDKFDIRSLLTVIIPTGSKTMGVVCAEKcHSRQQWSKNEESFLIAVAA 576
Cdd:PRK11061   86 NLADAQKHPSFK--YIPSVKEERFRAFLGVPIIYRRQLLGVLVVQQ-RELRQFDESEESFLVTLAT 148
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
597-1116 1.02e-107

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 359.16  E-value: 1.02e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  597 AKEAAEQAVKAKSEFLASMSHEIRTPMNGVIG----MLniikQTKLDSQQNHHIQLAQSSAESLLHIINDILDFSKIEAG 672
Cdd:PRK11107  282 AKKRAQEAARIKSEFLANMSHELRTPLNGVIGftrqTL----KTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAG 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  673 KLDIENISFNVSKLLGDTVESFAIKAEQNNTKLVLDatqINH---EFIVSDPNRIRQIINNLLGNAIKFTKDGEIIVLAT 749
Cdd:PRK11107  358 KLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLN---IDPdvpDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVE 434
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  750 VKPI-DDAMYLDCSVVDSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTFNF 828
Cdd:PRK11107  435 LRALsNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWF 514
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  829 SIkvKLDYKKQSLEPSHIIDK---KQILIADSCTLSSNIAKKQLQLWGAEVEEINDMASLLNRAkqqngqrcdaifVDYq 905
Cdd:PRK11107  515 HL--PLDLNPNPIIDGLPTDClagKRLLYVEPNSAAAQATLDILSETPLEVTYSPTLSQLPEAH------------YDI- 579
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  906 LYMQASAAEKQAFKTHFN-----ATRCKRILMAPMSlTEKQTRQTLK---VESIIFKPLTPSDLFNSLANDKY------I 971
Cdd:PRK11107  580 LLLGLPVTFREPLTMLHErlakaKSMTDFLILALPC-HEQVLAEQLKqdgADACLSKPLSHTRLLPALLEPCHhkqpplL 658
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  972 EQQQINKETLvkkvatyTVnsasqiLLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMP 1051
Cdd:PRK11107  659 PPTDESRLPL-------TV------MAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQR---PFDLILMDIQMP 722
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739103821 1052 EMDGYQATRAIRngdAGTAHREVSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKLSVW 1116
Cdd:PRK11107  723 GMDGIRACELIR---QLPHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRY 784
CHASE COG3452
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction ...
10-727 1.54e-83

Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 442675 [Multi-domain]  Cd Length: 785  Bit Score: 289.13  E-value: 1.54e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   10 KKLRKLRLAFWFSLALIVLIGFVLDHINYNRGKDAFRSQELAKLSAYRAELESILISNIQLVRGLAVAVAAEPNLDQTRF 89
Cdd:COG3452     8 LLRRRPLLLALLAFLLLLAVGAVLERLLREQEEQQLRAEVLQELSAIRARLEGELNARLSLLRGLAALVEANPGISQEEF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   90 AQIAAPLFETSSELRNIGGAPDMVIRMAYPLEGNEKSIGLNFLENAAQRDDAIKARDENTIVMAGPLELVQGGHALVARM 169
Cdd:COG3452    88 ERLARNLLEDYPGIRNIALAPDGVIRYVYPLAGNEAALGLDLRTDPEQRAAALRARESGQLVLAGPVNLVQGGRGLIGRL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  170 PVFMPPDH-KFWGLLSVVLDINKIYTNSGLVSLGNHYDVALQGRNGKGQHGEFFYGQKHILENTPLSFSITFPGGEWRMY 248
Cdd:COG3452   168 PVFLDGGDdRFWGFVSAVIDLDRLLDSAGLDDAQDGYQIALRGRDGDGAEGEVFYGDAALFDQDPVTLEVNLPGGSWQLA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  249 VAPKAGWSPPSSTIWPLRIAIILVCALFASASLFFLKMLERQYKSERMLETMSSLAKIgAWSFNLETKSMYWSDMTKQIF 328
Cdd:COG3452   248 AAPKGGWLASPRNALPLRLAGLLISLLLALLVYLLRQLLLLRLLLLLLRLELIAAALL-LLLLALDLLLELLLLLRLAEA 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  329 NYPINKQPEWPTNFNGFKAGFSRDKIRHLYEQALKHGKSFETQIQIINAKGDAVWVLVHCEAEHKNGRCIKLFgSIQDID 408
Cdd:COG3452   327 LLQERLRALALLAALEDLLLLKFDRDLLDLLLLLELEAILALLLLLRRLLRSREARGGLGGDLVRVGGVIDGR-VAVILI 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  409 ARKLIELENQKIALHNEILASLTVNDAVLTGNLNLskhVIVQAICHALNVDRASIWLFSDDRQSLNTFAIHDQSNPQFSD 488
Cdd:COG3452   406 IEALELAEARLAALDQERDASDVALGAALVVLEAL---LIIALLRELALLAGALLARKSLLLALDLAAESERLRYLELLL 482
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  489 -PISLQQIEVQNYFDAINNNAVINASDAQQHPFTKDLYTDYLDKFDIRSLLTVIIPTGSKTMGVVCAEKCHSRQQWSKNE 567
Cdd:COG3452   483 gDALRERIRRALLRLQLLSLDLSALAAVLGAESLAGLLISVFIDARILEAERLELALVAGEVALEELLLRLLGEILLLRA 562
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  568 ESFLIAVAALIGSLHASQRRIETEQQLVKAKEAAEQAVKAKSEFLASMSHEIRtpMNGVIGMLNIIKQTKLDSQQNHHIQ 647
Cdd:COG3452   563 ELILALLDAKSGLSALELSGLLAGRAALDSLLLLLALALRQLDESALFILEEL--LLRLIIDLRIERLLLLLLGGEILLG 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  648 LAQSSAESLLHIINDILDFSKIEAGkLDIENISFNVSKLLGDTVESFAIKAEQNNTKLVLDATQINHEFIVSDPNRIRQI 727
Cdd:COG3452   641 ELALLLLLLVLIILILLSVEEAGLI-LALSLLLALLLLAILDAAVSLLATLLLLFQLLLLLLIILEGLLAELVAEALRLA 719
PRK15347 PRK15347
two component system sensor kinase;
589-1114 7.48e-79

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 278.45  E-value: 7.48e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  589 ETEQQLVKAKEAAEQAVKAKSEFLASMSHEIRTPMNGVIGMLNIIKQTKLDSQQNHHIQLAQSSAESLLHIINDILDFSK 668
Cdd:PRK15347  379 ERTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSR 458
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  669 IEAGKLDIENISFNVSKLLGD---TVESFAIkaeqnNTKLVLDaTQINHEF---IVSDPNRIRQIINNLLGNAIKFTKDG 742
Cdd:PRK15347  459 IESGQMTLSLEETALLPLLDQamlTIQGPAQ-----SKSLTLR-TFVGAHVplyLHLDSLRLRQILVNLLGNAVKFTETG 532
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  743 EIIVlaTVKPIDDAMYLdcSVVDSGVGIKPEKQATLFDSFTQADASTtrryGGTGLGLAIVKQLCKLMQGDVNVVSSYGE 822
Cdd:PRK15347  533 GIRL--RVKRHEQQLCF--TVEDTGCGIDIQQQQQIFTPFYQADTHS----QGTGLGLTIASSLAKMMGGELTLFSTPGV 604
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  823 GSTFNFSIKVkldykkQSLEPSHIIdkKQILIADSCTlssniaKKQLQLWGAEVEEINDMASLLNRakqqngqrcDAIFV 902
Cdd:PRK15347  605 GSCFSLVLPL------NEYAPPEPL--KGELSAPLAL------HRQLSAWGITCQPGHQNPALLDP---------ELAYL 661
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  903 DYQLYmqasaaekqafkthfnatrckRILmapmslteKQTRQTLKVESIIFKPLTPSDLfnslandkyieqqqinketlv 982
Cdd:PRK15347  662 PGRLY---------------------DLL--------QQIIQGAPNEPVINLPLQPWQL--------------------- 691
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  983 kkvatytvnsasQILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKiaNREHMpYELILMDCQMPEMDGYQATRAI 1062
Cdd:PRK15347  692 ------------QILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALEL--GRQHR-FDLVLMDIRMPGLDGLETTQLW 756
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 739103821 1063 RNGDAGTaHREVSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKLS 1114
Cdd:PRK15347  757 RDDPNNL-DPDCMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARALE 807
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
551-1124 1.20e-74

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: 267.41  E-value: 1.20e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   551 VVCAEKCHSRQQWSKNEESFLIAVAALIGSLHASQRRIETE-QQLVKAKEAAEQAVKAKSEFLASMSHEIRTPMNGVIGM 629
Cdd:TIGR02956  406 KLQADERQVAQELQEHKESLEQLVAQRTQELAETNERLNAEvKNHAKARAEAEEANRAKSAFLATMSHEIRTPLNGILGT 485
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   630 LNIIKQTKLDSQQNHHIQLAQSSAESLLHIINDILDFSKIEAGKLDIENISFNVSKLLGDTVESFAIKAEQNNTKLVLDA 709
Cdd:TIGR02956  486 LELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNI 565
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   710 TQINHEFIVSDPNRIRQIINNLLGNAIKFTKDGEiIVLATvkPIDDAMYLDCSVVDSGVGIKPEKQATLFDSFTQADAst 789
Cdd:TIGR02956  566 PEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGS-VVLRV--SLNDDSSLLFEVEDTGCGIAEEEQATLFDAFTQADG-- 640
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   790 TRRYGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTFNFSIKVKldykkqslepshiidkkqiliadsctlssniakkql 869
Cdd:TIGR02956  641 RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLT------------------------------------ 684
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   870 qlwgaeveeindmasllnrakqqngqrcdaifvdyqlymQASAAEKQAFKTHFNatrckrilmapmsltekqtrqtlkve 949
Cdd:TIGR02956  685 ---------------------------------------RGKPAEDSATLTVID-------------------------- 699
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   950 siifkpltpsdlfnslandkyieqqqinketlvkkvatytVNSAsQILLVEDNKVNQMVAGALLKQAGISFDIAENGLEA 1029
Cdd:TIGR02956  700 ----------------------------------------LPPQ-RVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSA 738
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  1030 IAKIANREhmpYELILMDCQMPEMDGYQATRAIRNGDAgtAHREVSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSL 1109
Cdd:TIGR02956  739 LECFHQHA---FDLALLDINLPDGDGVTLLQQLRAIYG--AKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQL 813
                          570
                   ....*....|....*..
gi 739103821  1110 NKKLSVWL--DTHQERE 1124
Cdd:TIGR02956  814 TAMIAVILagGKSNTEA 830
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
567-830 1.91e-74

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 249.83  E-value: 1.91e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  567 EESFLIAVAALIGSLHASQRRIETEQQLVKAKEAAEQAVKAKSEFLASMSHEIRTPMNGVIGMLNIIKQTkLDSQQNHHI 646
Cdd:COG0642    69 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE-LDEEQREYL 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  647 QLAQSSAESLLHIINDILDFSKIEAGKLDIENISFNVSKLLGDTVESFAIKAEQNNTKLVLDATQiNHEFIVSDPNRIRQ 726
Cdd:COG0642   148 ETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPD-DLPTVRGDPDRLRQ 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  727 IINNLLGNAIKFTKDGEIIVLaTVKPIDDAMYLdcSVVDSGVGIKPEKQATLFDSFTQADASttRRYGGTGLGLAIVKQL 806
Cdd:COG0642   227 VLLNLLSNAIKYTPEGGTVTV-SVRREGDRVRI--SVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRI 301
                         250       260
                  ....*....|....*....|....
gi 739103821  807 CKLMQGDVNVVSSYGEGSTFNFSI 830
Cdd:COG0642   302 VELHGGTIEVESEPGKGTTFTVTL 325
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
593-830 7.11e-65

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 219.39  E-value: 7.11e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  593 QLVKAKEAAEQAVKAKSEFLASMSHEIRTPMNGVIGMLNIIKQ--TKLDSQQNHHIQLAQSSAESLLHIINDILDFSKIE 670
Cdd:COG2205     1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDeeDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  671 AGKLDIENISFNVSKLLGDTVESFAIKAEQNNTKLVLDaTQINHEFIVSDPNRIRQIINNLLGNAIKFTKDGEIIVLaTV 750
Cdd:COG2205    81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELD-LPPELPLVYADPELLEQVLANLLDNAIKYSPPGGTITI-SA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  751 KPIDDAMYLdcSVVDSGVGIKPEKQATLFDSFTQADasTTRRYGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTFNFSI 830
Cdd:COG2205   159 RREGDGVRI--SVSDNGPGIPEEELERIFERFYRGD--NSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTL 234
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
558-1118 6.69e-64

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 234.87  E-value: 6.69e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  558 HSRQQwskNEE---SFLIAVAAligslhasqrRIETEQQLVKAKEAAEQAVKAKSEFLASMSHEIRTPMNGVIGMLNIIK 634
Cdd:PRK10841  407 HSRYR---NENvaiCVLVDVSA----------RVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQ 473
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  635 QTKLDSQQNHHIQLAQSSAESLLHIINDILDFSKIEAGKLDIENISFNVSKllgdtVESFAIKaeqNNTKLVLDATQINH 714
Cdd:PRK10841  474 TKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEPREFSPRE-----VINHITA---NYLPLVVKKRLGLY 545
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  715 EFIVS--------DPNRIRQIINNLLGNAIKFTKDGEIIVLATVKpiDDamYLDCSVVDSGVGIKPEKQATLFDSFTQAD 786
Cdd:PRK10841  546 CFIEPdvpvalngDPMRLQQVISNLLSNAIKFTDTGCIVLHVRVD--GD--YLSFRVRDTGVGIPAKEVVRLFDPFFQVG 621
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  787 ASTTRRYGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTfnFSIKVKLdYKKQSLEPshiidkkqiliadscTLSSNIAK 866
Cdd:PRK10841  622 TGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQ--FTIRIPL-YGAQYPQK---------------KGVEGLQG 683
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  867 KQLQLWgaeveeI-ND-MASLLNRAKQQNGQRC-----------DAIFVDYQLymqasaAEKQAFKTHFnaTRCKRILMA 933
Cdd:PRK10841  684 KRCWLA------VrNAsLEQFLETLLQRSGIQVqryegqeptpeDVLITDDPV------QKKWQGRAVI--TFCRRHIGI 749
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  934 PmslteKQTRQTLKVESiifkPLTPSDLFNSLANDKYIEQQ-QINKETLVKKVATYTVNSASQILLVEDNKVNQMVAGAL 1012
Cdd:PRK10841  750 P-----LEIAPGEWVHS----TATPHELPALLARIYRIELEsDDSANALPSTDKAVSDNDDMMILVVDDHPINRRLLADQ 820
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821 1013 LKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNgdagtAHREVSIVALTANAMQGDKERCL 1092
Cdd:PRK10841  821 LGSLGYQCKTANDGVDALNVLSKN---HIDIVLTDVNMPNMDGYRLTQRLRQ-----LGLTLPVIGVTANALAEEKQRCL 892
                         570       580
                  ....*....|....*....|....*.
gi 739103821 1093 NAGMNDYLTKPLNFDSLNKKLSVWLD 1118
Cdd:PRK10841  893 EAGMDSCLSKPVTLDVLKQTLTVYAE 918
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
599-835 1.50e-62

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 218.27  E-value: 1.50e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  599 EAAEQAVKAKSEFLASMSHEIRTPMNGVIGMLNIIKQTKLDS--QQNHHIQLAQSSAESLLHIINDILDFSKIEAGKLDI 676
Cdd:COG5002   156 TELERLEQMRREFVANVSHELRTPLTSIRGYLELLLDGAADDpeERREYLEIILEEAERLSRLVNDLLDLSRLESGELKL 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  677 ENISFNVSKLLGDTVESFAIKAEQNNTKLVLDATQiNHEFIVSDPNRIRQIINNLLGNAIKFTKDGEIIVLaTVKPIDDA 756
Cdd:COG5002   236 EKEPVDLAELLEEVVEELRPLAEEKGIELELDLPE-DPLLVLGDPDRLEQVLTNLLDNAIKYTPEGGTITV-SLREEDDQ 313
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739103821  757 MYLdcSVVDSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTFNFSIKVKLD 835
Cdd:COG5002   314 VRI--SVRDTGIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPLARE 390
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
596-1124 2.16e-61

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 225.20  E-value: 2.16e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  596 KAKEAAEQAVKAKSEFLASMSHEIRTPMNGVIGMLNIIKQTKLDSQQNHHIQLAQSSAESLLHIINDILDFSKIEAGKLD 675
Cdd:PRK11091  271 RYQDALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQ 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  676 IENISFNVSKLLGDtVESFA-IKAEQNNTKLVLDATQINHEFIVSDPNRIRQIINNLLGNAIKFTKDGEIIVLATVKPID 754
Cdd:PRK11091  351 LDNQPIDFTDFLAD-LENLSgLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRYEEGD 429
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  755 DAMYldcSVVDSGVGIKPEKQATLFDSFTQA-DASTTRRYGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTFNFSIKVk 833
Cdd:PRK11091  430 MLTF---EVEDSGIGIPEDELDKIFAMYYQVkDSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHA- 505
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  834 ldykkqslepshiidkkqILIADSctlssniakkqlqlwGAEVEEINDMasllnrakqqngqrcdaifvdyqlymqasaa 913
Cdd:PRK11091  506 ------------------PAVAEE---------------VEDAFDEDDM------------------------------- 521
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  914 ekqafkthfnatrckrilmapmsltekqtrqtlkvesiifkPLTpsdlfnslandkyieqqqinketlvkkvatytvnsA 993
Cdd:PRK11091  522 -----------------------------------------PLP-----------------------------------A 525
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  994 SQILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANREhmpYELILMDCQMPEMDGYQATRAIRNGDAGtaHRE 1073
Cdd:PRK11091  526 LNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDE---YDLVLLDIQLPDMTGLDIARELRERYPR--EDL 600
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 739103821 1074 VSIVALTANAMqGDKERCLNAGMNDYLTKPLNFDSLNKKLSVWLDTHQERE 1124
Cdd:PRK11091  601 PPLVALTANVL-KDKKEYLDAGMDDVLSKPLSVPALTAMIKKFWDTQDDEE 650
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
724-832 3.33e-49

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: 169.60  E-value: 3.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  724 IRQIINNLLGNAIKFTKDGEIIVLATVKPIDDAMY-LDCSVVDSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLGLAI 802
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVqLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 739103821  803 VKQLCKLMQGDVNVVSSYGEGSTFNFSIKV 832
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
996-1109 8.57e-49

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: 168.80  E-value: 8.57e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNGDAGTAHreVS 1075
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEE---PFDLVLMDLQMPVMDGLEATRRIRELEGGGRR--TP 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKPLNFDSL 1109
Cdd:cd17546    76 IIALTANALEEDREKCLEAGMDDYLSKPVKLDQL 109
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
583-988 9.90e-48

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 185.11  E-value: 9.90e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  583 ASQRRIETE--QQLV----KAKEAAEQAVKAKSEFLASMSHEIRTPMNGVIGMLNIIKQTKLDSQQNHHIQLAQSSAESL 656
Cdd:PRK11466  413 AAQVKARTAelQELViehrQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESL 492
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  657 LHIINDILDFSKIEAG--KLDIENISFNVSKLLGDTVESFAIKAEQNNTKLVLDATQINHEFIVSDPNRIRQIINNLLGN 734
Cdd:PRK11466  493 LTILNDILDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSN 572
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  735 AIKFTKDGEIIVLATVkpiDDAMYLdCSVVDSGVGIKPEKQATLFDSFTQADAsttrRYGGTGLGLAIVKQLCKLMQGDV 814
Cdd:PRK11466  573 ALRFTDEGSIVLRSRT---DGEQWL-VEVEDSGCGIDPAKLAEIFQPFVQVSG----KRGGTGLGLTISSRLAQAMGGEL 644
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  815 NVVSSYGEGSTFNFSIKVK---LDYKKQSLEPSHIIDKKQILIADScTLSSNIAKKQLQLWGAEVEEINDMASLLnrAKQ 891
Cdd:PRK11466  645 SATSTPEVGSCFCLRLPLRvatAPVPKTVNQAVRLDGLRLLLIEDN-PLTQRITAEMLNTSGAQVVAVGNAAQAL--ETL 721
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  892 QNGQRCDAIFVDYQLYMQASAAEKQAFKTHFNATrcKRILMAPMSLTEKQTRQTLKV-ESIIFKPLTPSDLFNSLANDKY 970
Cdd:PRK11466  722 QNSEPFAAALVDFDLPDYDGITLARQLAQQYPSL--VLIGFSAHVIDETLRQRTSSLfRGIIPKPVPREVLGQLLAHYLQ 799
                         410       420
                  ....*....|....*....|.
gi 739103821  971 IEQQQ---INKETLVKKVATY 988
Cdd:PRK11466  800 LQVNNdqpLDVSQLNEDAALM 820
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
598-893 1.76e-45

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 179.16  E-value: 1.76e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  598 KEAAEQAVKAKSEFLASMSHEIRTPMNGVIGMLNIIKQTKLDSQQN-HHIQLAQSSAESLLHIINDILDFSKIEAGKLDI 676
Cdd:PRK09959  702 RNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRvEAISLAYATGQSLLGLIGEILDVDKIESGNYQL 781
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  677 ENISFNVSKLLGDTVESFAIKAEQNNTKLVLDATQINHEFIVSDPNRIRQIINNLLGNAIKFTKDGEIIVLATVKPIDDA 756
Cdd:PRK09959  782 QPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSLGHIDDN 861
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  757 -MYLDCSVVDSGVGIKPEKQATLFDSFTQADASttRRYGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTFNFSIKVKLD 835
Cdd:PRK09959  862 hAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAG--RQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEIS 939
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739103821  836 YKKQSLE-----PSHIIDKKQILIADSCTLSSNIAKKQLQLWGAEVEEINDMASLLNRAKQQN 893
Cdd:PRK09959  940 QQVATVEakaeqPITLPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQH 1002
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
404-833 1.68e-44

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 169.20  E-value: 1.68e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  404 IQDIDARKLIELENQKIALHNEILASLTVNDAVLTGNLNLSKHVIVQAICHALNVDRASIWLFSDDRQSLNTFAIHDQSN 483
Cdd:COG4251    78 LALLLLLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLL 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  484 PQFSDPISLQQIEVQNYFDAINNNAVINASDAQQHPFTKDLYTDYLDKFDIRSLLTVIIPTGSKTMGVVCAEKCHSRQQW 563
Cdd:COG4251   158 LLLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVL 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  564 SKNEESFLIAVAALIGSLHASQRRIETEQQLVKAKEAAEQAVKAKSEFLASMSHEIRTPMNGVIGMLNIIKQ---TKLDS 640
Cdd:COG4251   238 LLLLILLLLLLILVLELLELRLELEELEEELEERTAELERSNEELEQFAYVASHDLREPLRKISGFSQLLEEdygDKLDE 317
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  641 QQNHHIQLAQSSAESLLHIINDILDFSKIEAGKLDIENIsfNVSKLLGDTVESFAIKAEQNNTKLVLDATQInhefIVSD 720
Cdd:COG4251   318 EGREYLERIRDAAERMQALIDDLLAYSRVGRQELEFEPV--DLNELLEEVLEDLEPRIEERGAEIEVGPLPT----VRGD 391
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  721 PNRIRQIINNLLGNAIKFTKDGE--IIVLATVKpiDDAMYLdCSVVDSGVGIKPEKQATLFDSFTQADasTTRRYGGTGL 798
Cdd:COG4251   392 PTLLRQVFQNLISNAIKYSRPGEppRIEIGAER--EGGEWV-FSVRDNGIGIDPEYAEKIFEIFQRLH--SRDEYEGTGI 466
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 739103821  799 GLAIVKQLCKLMQGDVNVVSSYGEGSTFNFSIKVK 833
Cdd:COG4251   467 GLAIVKKIVERHGGRIWVESEPGEGATFYFTLPKA 501
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
996-1122 2.40e-42

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: 150.77  E-value: 2.40e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRngdAGTAHREVS 1075
Cdd:COG0784     8 ILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAG---PPDLILLDINMPGMDGLELLRRIR---ALPRLPDIP 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKLSVWLDTHQE 1122
Cdd:COG0784    82 IIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
587-835 2.17e-39

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: 153.59  E-value: 2.17e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  587 RIETEQQLvkakEAAEQAVKAkSEFLASMSHEIRTPMNGVIGMLNIIKQTKlDSQQNHHIQLAQSSAESLLHIINDILDF 666
Cdd:COG5809   254 RKKLEELL----RKSEKLSVV-GELAAGIAHEIRNPLTSLKGFIQLLKDTI-DEEQKTYLDIMLSELDRIESIISEFLVL 327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  667 SKIEAGKLDieniSFNVSKLLGDTVESFAIKAEQNNTKLVLDATQiNHEFIVSDPNRIRQIINNLLGNAIKFTKDGEIIV 746
Cdd:COG5809   328 AKPQAIKYE----PKDLNTLIEEVIPLLQPQALLKNVQIELELED-DIPDILGDENQLKQVFINLLKNAIEAMPEGGNIT 402
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  747 LATVKPIDDAMYLdcSVVDSGVGIKPEKQATLFDSFTqadastTRRYGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTF 826
Cdd:COG5809   403 IETKAEDDDKVVI--SVTDEGCGIPEERLKKLGEPFY------TTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTF 474

                  ....*....
gi 739103821  827 NFSIKVKLD 835
Cdd:COG5809   475 SITLPIKLS 483
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
996-1113 1.37e-33

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: 127.72  E-value: 1.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNgDAGTAHreVS 1075
Cdd:COG3706     4 ILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEH---RPDLILLDLEMPDMDGLELCRRLRA-DPRTAD--IP 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKL 1113
Cdd:COG3706    78 IIFLTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
996-1109 2.67e-33

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: 124.57  E-value: 2.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIanREHMPyELILMDCQMPEMDGYQATRAIRnGDAGTAHreVS 1075
Cdd:cd17548     2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIA--RKEKP-DLILMDIQLPGMDGLEATRLLK-EDPATRD--IP 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKPLNFDSL 1109
Cdd:cd17548    76 VIALTAYAMKGDREKILEAGCDGYISKPIDTREF 109
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
609-830 2.70e-33

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: 131.95  E-value: 2.70e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   609 SEFLASMSHEIRTPMNGVIGMLNIIKQTKL--DSQQNHHIQLAQSSAESLLHIINDILDFSKIEAGKLDIENISFNVSKL 686
Cdd:TIGR02966  115 RDFVANVSHELRTPLTVLRGYLETLADGPDedPEEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPAL 194
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   687 LGDTVESFAIKAEQNNTKLVLDA-TQInheFIVSDPNRIRQIINNLLGNAIKFTKDG-EIIVLATVKPiDDAMYldcSVV 764
Cdd:TIGR02966  195 LDHLRDEAEALSQGKNHQITFEIdGGV---DVLGDEDELRSAFSNLVSNAIKYTPEGgTITVRWRRDG-GGAEF---SVT 267
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739103821   765 DSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTFNFSI 830
Cdd:TIGR02966  268 DTGIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFSFIF 333
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
720-833 8.27e-33

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 122.76  E-value: 8.27e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821    720 DPNRIRQIINNLLGNAIKFTKDGEIIVLaTVKPIDDAMYLdcSVVDSGVGIKPEKQATLFDSFTQADaSTTRRYGGTGLG 799
Cdd:smart00387    2 DPDRLRQVLSNLLDNAIKYTPEGGRITV-TLERDGDHVEI--TVEDNGPGIPPEDLEKIFEPFFRTD-KRSRKIGGTGLG 77
                            90       100       110
                    ....*....|....*....|....*....|....
gi 739103821    800 LAIVKQLCKLMQGDVNVVSSYGEGSTFNFSIKVK 833
Cdd:smart00387   78 LSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
571-830 2.76e-31

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 126.84  E-value: 2.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  571 LIAVAALIGSLHASQRRIETEQQLVKAKEAAEQAVKAKS--EFLASMSHEIRTPMNGVIG----MLNIIKQTKLDSQQNH 644
Cdd:COG4191   103 AEENAELEELERDITELERAEEELRELQEQLVQSEKLAAlgELAAGIAHEINNPLAAILGnaelLRRRLEDEPDPEELRE 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  645 HIQLAQSSAESLLHIINDILDFSKieAGKLDIEniSFNVSKLLGDTVESFAIKAEQNNTKLVLDATQiNHEFIVSDPNRI 724
Cdd:COG4191   183 ALERILEGAERAAEIVRSLRAFSR--RDEEERE--PVDLNELIDEALELLRPRLKARGIEVELDLPP-DLPPVLGDPGQL 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  725 RQIINNLLGNAI---KFTKDGEIIVlaTVKPIDDAMYLdcSVVDSGVGIKPEKQATLFDSFTqadasTTRRYG-GTGLGL 800
Cdd:COG4191   258 EQVLLNLLINAIdamEEGEGGRITI--STRREGDYVVI--SVRDNGPGIPPEVLERIFEPFF-----TTKPVGkGTGLGL 328
                         250       260       270
                  ....*....|....*....|....*....|
gi 739103821  801 AIVKQLCKLMQGDVNVVSSYGEGSTFNFSI 830
Cdd:COG4191   329 SISYGIVEKHGGRIEVESEPGGGTTFTITL 358
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
585-833 7.99e-29

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 119.57  E-value: 7.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  585 QRRIETEQQLVKAKEAAeqavkakSEFLASMSHEIRTPMNGVIGMLNIIKQTKLDSQQNHHIQLAQSSAESLLHIINDIL 664
Cdd:COG3852   119 RKRLERELRRAEKLAAV-------GELAAGLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLL 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  665 DFSKIEAGKLDieniSFNVSKLLGDTVESfaIKAE-QNNTKLVLDATQINHEFIVsDPNRIRQIINNLLGNAIKFTKDGE 743
Cdd:COG3852   192 SFSRPRPPERE----PVNLHEVLERVLEL--LRAEaPKNIRIVRDYDPSLPEVLG-DPDQLIQVLLNLVRNAAEAMPEGG 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  744 IIVLAT-------VKPIDDAMYLDCSVVDSGVGIKPEKQATLFDSFTqadasTTRRyGGTGLGLAIVKQLCKLMQGDVNV 816
Cdd:COG3852   265 TITIRTrverqvtLGGLRPRLYVRIEVIDNGPGIPEEILDRIFEPFF-----TTKE-KGTGLGLAIVQKIVEQHGGTIEV 338
                         250
                  ....*....|....*..
gi 739103821  817 VSSYGEGSTFNFSIKVK 833
Cdd:COG3852   339 ESEPGKGTTFRIYLPLE 355
CHASE smart01079
This domain is found in the extracellular portion of receptor-like proteins - such as serine ...
60-209 1.66e-28

This domain is found in the extracellular portion of receptor-like proteins - such as serine/threonine kinases and adenylyl cyclases; Predicted to be a ligand binding domain.


Pssm-ID: 215015  Cd Length: 176  Bit Score: 112.81  E-value: 1.66e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821     60 LESILISNIQLVRGLAVAvaaePNLDQTRFAQIAAPLFETSSELRNIGGAPDM------VIRMAYPLEGNEKSIGLNFLE 133
Cdd:smart01079   14 LELQLNRRLPGIQGLGWA----PRVPPAERAAFEAALRAGGPGLFNIRLAPDGerdeyfVITYIEPLAGNEAALGLDLLS 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821    134 NAAQRDDAIKARDENTIVMAGPLELVQGGH---ALVARMPVFMPPD------HKFWGLLSVVLDINKIYTNSGLVSLGNH 204
Cdd:smart01079   90 EPVRRAALERARDSGRPVLSGPVTLVQGTGdgrGFLLRLPVYRGGPptstrrEALWGFVSAVFRLDDLLEGLLGALDLPG 169

                    ....*
gi 739103821    205 YDVAL 209
Cdd:smart01079  170 LDLAL 174
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
592-826 3.13e-28

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: 118.91  E-value: 3.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  592 QQLVKAKEAAeqavkAKSEFLASMSHEIRTPMNGVIGMLNIIKQTKLDSQQNHHIQLAQSS------AESLLHIINDILD 665
Cdd:COG5000   190 TELLRAERLA-----AWGELARRIAHEIKNPLTPIQLSAERLRRKLADKLEEDREDLERALdtiirqVDRLKRIVDEFLD 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  666 FSKIEAGKLDIenisFNVSKLLGDTVESFAIKAEQNNTKLVLDATQiNHEFIVSDPNRIRQIINNLLGNAIKFTKDGEII 745
Cdd:COG5000   265 FARLPEPQLEP----VDLNELLREVLALYEPALKEKDIRLELDLDP-DLPEVLADRDQLEQVLINLLKNAIEAIEEGGEI 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  746 VLaTVKPIDDAMYLdcSVVDSGVGIKPEKQATLFDSFTqadasTTRRyGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGST 825
Cdd:COG5000   340 EV-STRREDGRVRI--EVSDNGPGIPEEVLERIFEPFF-----TTKP-KGTGLGLAIVKKIVEEHGGTIELESRPGGGTT 410

                  .
gi 739103821  826 F 826
Cdd:COG5000   411 F 411
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
995-1109 4.54e-28

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 112.74  E-value: 4.54e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  995 QILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNgdagtAHREV 1074
Cdd:COG0745     3 RILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEE---RPDLILLDLMLPGMDGLEVCRRLRA-----RPSDI 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 739103821 1075 SIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSL 1109
Cdd:COG0745    75 PIIMLTARDDEEDRVRGLEAGADDYLTKPFDPEEL 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
720-833 7.10e-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: 108.61  E-value: 7.10e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   720 DPNRIRQIINNLLGNAIKFTKDGEIIvlaTVKpIDDAMYLDCSVVDSGVGIKPEKQATLFDSFTQADastTRRYGGTGLG 799
Cdd:pfam02518    2 DELRLRQVLSNLLDNALKHAAKAGEI---TVT-LSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGGTGLG 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 739103821   800 LAIVKQLCKLMQGDVNVVSSYGEGSTFNFSIKVK 833
Cdd:pfam02518   75 LSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
996-1124 1.52e-26

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: 109.10  E-value: 1.52e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRnGDAGTAHreVS 1075
Cdd:COG3437     9 VLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEA---PPDLILLDVRMPGMDGFELLRLLR-ADPSTRD--IP 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKLSVWLDTHQERE 1124
Cdd:COG3437    83 VIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQR 131
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
611-826 3.26e-26

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 114.35  E-value: 3.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  611 FLASMSHEIRTPMNGVIGMLNII--KQTKLDSQQNHHIQLAQSSAESLLHIINDILDFSKIEAG--KLDIENIsfNVSKL 686
Cdd:NF040691  274 FVSDVSHELRTPLTTIRMAADVIhdSRDDFDPATARSAELLHTELDRFESLLSDLLEISRFDAGaaELDVEPV--DLRPL 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  687 LGDTVESFAIKAEQNNTKLVLDA--TQINHEFivsDPNRIRQIINNLLGNAIKFTKDGEIIVlaTVKPIDDAMYLdcSVV 764
Cdd:NF040691  352 VRRVVDALRQLAERAGVELRVDApgTPVVAEV---DPRRVERVLRNLVVNAIEHGEGKPVVV--TVAQDDTAVAV--TVR 424
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739103821  765 DSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTF 826
Cdd:NF040691  425 DHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQF 486
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
995-1113 8.22e-26

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: 103.25  E-value: 8.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  995 QILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANREHmPYELILMDCQMPEMDGYQATRAIRngDAGTAHREV 1074
Cdd:cd19933     2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEH-SFQLVLLDLCMPEMDGFEVALRIR--KLFGRRERP 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 739103821 1075 SIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKL 1113
Cdd:cd19933    79 LIVALTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
996-1113 1.06e-25

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: 102.61  E-value: 1.06e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIanrEHMPYELILMDCQMPEMDGYQATRAIRNGDAGTAhrevs 1075
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELL---KEERPDLILLDINMPGMDGLELLKRIRRRDPTTP----- 72
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 739103821  1076 IVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKL 1113
Cdd:pfam00072   73 VIILTAHGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
571-829 1.98e-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: 108.24  E-value: 1.98e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   571 LIAVAALIGSLHASQR----RIETE-QQLVKAKEAA----EQAVKAKSEFLASMSHEIRTPMNgvigmlNIIKQTKL--- 638
Cdd:TIGR01386  195 LSAVAARISPESLDQRldpsRAPAElRELAQSFNAMlgrlEDAFQRLSQFSADLAHELRTPLT------NLLGQTQVals 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   639 -DSQQNHHIQLAQSSAES---LLHIINDILDFSKIEAGKLDIENISFNVSKLLGDTVESFAIKAEQNNTKLVLDATQinh 714
Cdd:TIGR01386  269 qPRTGEEYREVLESNLEElerLSRMVSDMLFLARADNGQLALERVRLDLAAELAKVAEYFEPLAEERGVRIRVEGEG--- 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   715 eFIVSDPNRIRQIINNLLGNAIKFTKDGEIIvlaTVKPIDDAMYLDCSVVDSGVGIKPEKQATLFDSFTQADASTTRRYG 794
Cdd:TIGR01386  346 -LVRGDPQMFRRAISNLLSNALRHTPDGGTI---TVRIERRSDEVRVSVSNPGPGIPPEHLSRLFDRFYRVDPARSNSGE 421
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 739103821   795 GTGLGLAIVKQLCKLMQGDVNVVSSYGEgSTFNFS 829
Cdd:TIGR01386  422 GTGLGLAIVRSIMEAHGGRASAESPDGK-TRFILR 455
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
997-1103 1.11e-22

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: 93.45  E-value: 1.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  997 LLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNGdagtaHREVSI 1076
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREE---RPDLVLLDLMMPGMDGLELLRKLREL-----PPDIPV 72
                          90       100
                  ....*....|....*....|....*..
gi 739103821 1077 VALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:cd00156    73 IVLTAKADEEDAVRALELGADDYLVKP 99
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
592-802 1.47e-22

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 102.21  E-value: 1.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  592 QQLVKAKEAAEQAVKAKSEFLASMSHEIRTPMNGVIGMLNIIkQTKLDSQQNHHIQLAQSSAESLLHIINDILDFSKIEA 671
Cdd:NF012163  224 QDFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRAELEAI-QDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDE 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  672 GKLDIENISFNVSKLLGDTVESFAIKAEQNNTKLVLDATqiNHEFIVSDPNRIRQIINNLLGNAIKFTKD-GEIIVLATV 750
Cdd:NF012163  303 GALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLP--DSSLVFGDRDRLMQLFNNLLENSLRYTDSgGSLHISASQ 380
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 739103821  751 KPIDDAMYLDcsvvDSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLGLAI 802
Cdd:NF012163  381 RPKEVTLTVA----DSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAI 428
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
607-834 3.21e-22

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 100.86  E-value: 3.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  607 AKSEFLASMSHEIRTPMNGVIGMLNIIKQTKLDSQQN---HHIQLAQSS-AESLlhiINDILDFSKIEAG-KLDIENIsF 681
Cdd:PRK11006  203 ARRNFFANVSHELRTPLTVLQGYLEMMQDQPLEGALRekaLHTMREQTQrMEGL---VKQLLTLSKIEAApTIDLNEK-V 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  682 NVSKLLgDTVESFAIKAEQNNTKLVLDatqINHEFIV-SDPNRIRQIINNLLGNAIKFTKDGEIIVLATVKPIDDAMYld 760
Cdd:PRK11006  279 DVPMML-RVLEREAQTLSQGKHTITFE---VDNSLKVfGNEDQLRSAISNLVYNAVNHTPEGTHITVRWQRVPQGAEF-- 352
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739103821  761 cSVVDSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTFNFSIKVKL 834
Cdd:PRK11006  353 -SVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLPERL 425
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
997-1103 2.07e-21

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: 89.77  E-value: 2.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  997 LLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNgdagtAHREVSI 1076
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREE---QPDLIILDVMLPGMDGFEVCRRLRE-----KGSDIPI 72
                          90       100
                  ....*....|....*....|....*..
gi 739103821 1077 VALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:cd17574    73 IMLTAKDEEEDKVLGLELGADDYITKP 99
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
996-1103 2.27e-21

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: 89.86  E-value: 2.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIAnrEHMPyELILMDCQMPEMDGYQATRAIRNgDAGTAHreVS 1075
Cdd:cd17538     2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAE--EELP-DLILLDVMMPGMDGFEVCRRLKE-DPETRH--IP 75
                          90       100
                  ....*....|....*....|....*...
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:cd17538    76 VIMITALDDREDRIRGLEAGADDFLSKP 103
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
587-833 2.50e-21

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 99.66  E-value: 2.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  587 RIETEQQLVKAKEAAeqavkAKSEFLASMSHEIRTPMNGVIGMLNIIKQTKLDSQQNHHIQLAQSSAESLLHIINDILDF 666
Cdd:PRK11360  374 RKRLQRRVARQERLA-----ALGELVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEF 448
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  667 SKIEAGKldieNISFNVSKLLGDTVESFAIKAEQNNTKLVLDaTQINHEFIVSDPNRIRQIINNLLGNAIK-FTKDGEII 745
Cdd:PRK11360  449 SRPRESQ----WQPVSLNALVEEVLQLFQTAGVQARVDFETE-LDNELPPIWADPELLKQVLLNILINAVQaISARGKIR 523
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  746 VlATVKPIDDAMYLdcSVVDSGVGIKPEKQATLFDSFTqadasTTRRyGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGST 825
Cdd:PRK11360  524 I-RTWQYSDGQVAV--SIEDNGCGIDPELLKKIFDPFF-----TTKA-KGTGLGLALSQRIINAHGGDIEVESEPGVGTT 594

                  ....*...
gi 739103821  826 FNFSIKVK 833
Cdd:PRK11360  595 FTLYLPIN 602
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
996-1109 8.93e-21

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: 88.67  E-value: 8.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNGDAGtahREVS 1075
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRF---RPDVILSDIGMPGMDGYELARRLRELPWL---ANTP 74
                          90       100       110
                  ....*....|....*....|....*....|....
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKPLNFDSL 1109
Cdd:cd17580    75 AIALTGYGQPEDRERALEAGFDAHLVKPVDPDEL 108
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
720-830 4.03e-20

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: 86.78  E-value: 4.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  720 DPNRIRQIINNLLGNAIKFTKDGEIIvlATVKPIDDAMYLDCSVVDSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLG 799
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTPDGGRI--RCILEKFRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGLG 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 739103821  800 LAIVKQLCKLMQGDVNVVSSYGEGSTFNFSI 830
Cdd:cd16925    79 LSIVKEFVELHGGTVTVSDAPGGGALFQVEL 109
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
608-830 4.95e-20

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 94.84  E-value: 4.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  608 KSEFLASMSHEIRTPMNgvigmlNIIKQTKLDSQQNHhiqlAQSSAESLLH-----------IINDILDFSKIEAGKLDI 676
Cdd:PRK09835  262 QSNFSADIAHEIRTPIT------NLITQTEIALSQSR----SQKELEDVLYsnleeltrmakMVSDMLFLAQADNNQLIP 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  677 ENISFNVSKLLGDTVESFAIKAEQNNTKLVLDATqinHEFIVSDPNRIRQIINNLLGNAIKFTKDGEIIVLaTVKPIDDA 756
Cdd:PRK09835  332 EKKMLDLADEVGKVFDFFEAWAEERGVELRFVGD---PCQVAGDPLMLRRAISNLLSNALRYTPAGEAITV-RCQEVDHQ 407
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739103821  757 MYLdcSVVDSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLGLAIVKQLCKLMQGDVNvVSSYGEGSTFNFSI 830
Cdd:PRK09835  408 VQL--VVENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVA-VTSDARGTRFVISL 478
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
607-672 6.57e-20

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 84.57  E-value: 6.57e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739103821   607 AKSEFLASMSHEIRTPMNGVIGMLNIIKQTKLDSQQNHHIQLAQSSAESLLHIINDILDFSKIEAG 672
Cdd:pfam00512    1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
996-1103 1.04e-19

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: 85.26  E-value: 1.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRngdAGTAHREVS 1075
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAE---PPDLILLDVMMPGMDGFEVCRRLK---ADPATRHIP 74
                          90       100
                  ....*....|....*....|....*...
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:cd19920    75 VIFLTALTDTEDKVKGFELGAVDYITKP 102
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
996-1121 2.70e-19

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 85.41  E-value: 2.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNK-VNQMVAGALLKQAGIS-FDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNgdagtAHRE 1073
Cdd:COG4565     6 VLIVEDDPmVAELLRRYLERLPGFEvVGVASSGEEALALLAEH---RPDLILLDIYLPDGDGLELLRELRA-----RGPD 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 739103821 1074 VSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKLSVWLDTHQ 1121
Cdd:COG4565    78 VDVIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRR 125
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
607-672 2.76e-19

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 82.61  E-value: 2.76e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739103821    607 AKSEFLASMSHEIRTPMNGVIGMLNIIKQTKLDSQQNHHIQLAQSSAESLLHIINDILDFSKIEAG 672
Cdd:smart00388    1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
994-1105 4.09e-19

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: 84.03  E-value: 4.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  994 SQILLVEDNKVNQMVAGALLKQAG-ISFDIAENGLEAIAKIanREHmPYELILMDCQMPEMDGYQATRAIRngdAGTAHR 1072
Cdd:cd17551     1 MRILIVDDNPTNLLLLEALLRSAGyLEVVSFTDPREALAWC--REN-PPDLILLDYMMPGMDGLEFIRRLR---ALPGLE 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 739103821 1073 EVSIVALTANAMQGDKERCLNAGMNDYLTKPLN 1105
Cdd:cd17551    75 DVPIVMITADTDREVRLRALEAGATDFLTKPFD 107
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
996-1124 1.19e-18

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: 90.02  E-value: 1.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRngdagTAHREVS 1075
Cdd:COG2204     5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREE---PPDLVLLDLRMPGMDGLELLRELR-----ALDPDLP 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKLSVWLDTHQERE 1124
Cdd:COG2204    77 VILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRR 125
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
996-1103 3.18e-18

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: 80.97  E-value: 3.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNK-VNQMVAGALLKQAGIS-FDIAENGLEAIAKIanREHMPyELILMDCQMPEMDGYQATRAIRNgdagtAHRE 1073
Cdd:COG4753     2 VLIVDDEPlIREGLKRILEWEAGFEvVGEAENGEEALELL--EEHKP-DLVITDINMPGMDGLELLEAIRE-----LDPD 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 739103821 1074 VSIVALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:COG4753    74 TKIIILSGYSDFEYAQEAIKLGADDYLLKP 103
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
720-814 3.52e-18

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: 80.97  E-value: 3.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  720 DPNRIRQIINNLLGNAIKFTKDGEIIVLATVKpIDDAMYLDcsVVDSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLG 799
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTGGKLRIRAAQ-TPQEVRLD--VEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGLG 77
                          90
                  ....*....|....*
gi 739103821  800 LAIVKQLCKLMQGDV 814
Cdd:cd16946    78 LAICHNIALAHGGTI 92
PRK09303 PRK09303
histidine kinase;
593-832 1.31e-17

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 86.16  E-value: 1.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  593 QLVKAKEAAEQAVKAKSEFLASMSHEIRTPMNGvigmLNIIKQTKLDSQQNHHIQLAQSSAESLLH-----------IIN 661
Cdd:PRK09303  136 VLRQENETLLEQLKFKDRVLAMLAHDLRTPLTA----ASLALETLELGQIDEDTELKPALIEQLQDqarrqleeierLIT 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  662 DILDFSK-------IEAGKLDIENISFNVSKLLGDTVESfaiKAEQNNTKLVLDATQInhefiVSDPNRIRQIINNLLGN 734
Cdd:PRK09303  212 DLLEVGRtrwealrFNPQKLDLGSLCQEVILELEKRWLA---KSLEIQTDIPSDLPSV-----YADQERIRQVLLNLLDN 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  735 AIKFTKDGEIIVLA-----TVKpiddamyLDCSVVDSGVGIKPEKQATLF-DSFT-QADASTTrrygGTGLGLAIVKQLC 807
Cdd:PRK09303  284 AIKYTPEGGTITLSmlhrtTQK-------VQVSICDTGPGIPEEEQERIFeDRVRlPRDEGTE----GYGIGLSVCRRIV 352
                         250       260
                  ....*....|....*....|....*
gi 739103821  808 KLMQGDVNVVSSYGEGSTFNFSIKV 832
Cdd:PRK09303  353 RVHYGQIWVDSEPGQGSCFHFTLPV 377
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
995-1109 1.46e-17

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: 80.15  E-value: 1.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  995 QILLVEDNKVNQMVAGALLKQAGISFDI--AENGLEAIAKIanREHMPYE------LILMDCQMPEMDGYQATRAIRNgD 1066
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGVPNELhvVRDGEEALDFL--RGEGEYAdaprpdLILLDLNMPRMDGFEVLREIKA-D 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 739103821 1067 AGTahREVSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSL 1109
Cdd:cd17557    78 PDL--RRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEF 118
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
598-833 2.35e-17

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: 86.71  E-value: 2.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  598 KEAAEQAvkAKSEFL-------ASMSHEIRTPMNGVIGMLNIIKQTKLDsqQNHHIQLAQSSAESLLHIINDILDFSKIE 670
Cdd:COG5805   272 KEAEELM--ARSEKLsiagqlaAGIAHEIRNPLTSIKGFLQLLQPGIED--KEEYFDIMLSELDRIESIISEFLALAKPQ 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  671 AGKLDIENISfnvsKLLGDTV---ESFAIKaeqNNTKLVLDATQINhEFIVSDPNRIRQIINNLLGNAIKFTKDGEIIVL 747
Cdd:COG5805   348 AVNKEKENIN----ELIQDVVtllETEAIL---HNIQIRLELLDED-PFIYCDENQIKQVFINLIKNAIEAMPNGGTITI 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  748 ATvKPIDDAMYLDcsVVDSGVGIKPEKQATLFDSFTqadasTTRRyGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTFN 827
Cdd:COG5805   420 HT-EEEDNSVIIR--VIDEGIGIPEERLKKLGEPFF-----TTKE-KGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFT 490

                  ....*.
gi 739103821  828 FSIKVK 833
Cdd:COG5805   491 ITLPLS 496
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
724-830 5.25e-17

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: 77.75  E-value: 5.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  724 IRQIINNLLGNAIKFTKDGEIIVLaTVKPIDDAMYLDCSVVDSGVGIKPEKQATLFDSFTQADasTTRRYGGTGLGLAIV 803
Cdd:cd16921     1 LGQVLTNLLGNAIKFRRPRRPPRI-EVGAEDVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRLH--SREEYEGTGVGLAIV 77
                          90       100
                  ....*....|....*....|....*..
gi 739103821  804 KQLCKLMQGDVNVVSSYGEGSTFNFSI 830
Cdd:cd16921    78 RKIIERHGGRIWLESEPGEGTTFYFTL 104
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
593-802 1.32e-16

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 83.91  E-value: 1.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  593 QLVKAKEAAEQAVKAkseFLASMSHEIRTPMNGVIGMLNIIKQ--TKLDSQQNHHIQlaqSSAESLLHIINDILDFSKIE 670
Cdd:PRK10549  228 QLASTLEKNEQMRRD---FMADISHELRTPLAVLRGELEAIQDgvRKFTPESVASLQ---AEVGTLTKLVDDLHQLSLSD 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  671 AGKLDIENISFNVSKLLGDTVESFAIKAEQNNTKLVLDATQINHEFivSDPNRIRQIINNLLGNAIKFTKDGEIIVLATV 750
Cdd:PRK10549  302 EGALAYRKTPVDLVPLLEVAGGAFRERFASRGLTLQLSLPDSATVF--GDPDRLMQLFNNLLENSLRYTDSGGSLHISAE 379
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 739103821  751 KpidDAMYLDCSVVDSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLGLAI 802
Cdd:PRK10549  380 Q---RDKTLRLTFADSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAI 428
PRK10604 PRK10604
sensor protein RstB; Provisional
616-836 1.57e-16

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 83.50  E-value: 1.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  616 SHEIRTPMNGVIGMLNIIKQTKLDSQQ--NHHI-QLaqssaESLlhiINDILDFSKIEAGKLDIENISFNVSKLLGDTVE 692
Cdd:PRK10604  220 AHELRTPLVRLRYRLEMSDNLSAAESQalNRDIgQL-----EAL---IEELLTYARLDRPQNELHLSEPDLPAWLSTHLA 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  693 SFAIKAEQNNTKLVLDATQinhEFIVSDPNRIRQIINNLLGNAIKFTKDgeiiVLATVKPIDDAMYLdCSVVDSGVGIKP 772
Cdd:PRK10604  292 DIQAVTPEKTVRLDTPHQG---DYGALDMRLMERVLDNLLNNALRYAHS----RVRVSLLLDGNQAC-LIVEDDGPGIPP 363
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739103821  773 EKQATLFDSFTQADASTTRRYGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTFNFSIKVKLDY 836
Cdd:PRK10604  364 EERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSFSWPVWHNL 427
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
996-1103 2.93e-16

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: 75.17  E-value: 2.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVnqmVAGAL---LKQAGISFDIAENGLEAIAKIanrEHMPYELILMDCQMPEMDGYQATRAIRNgdagtAHR 1072
Cdd:cd19935     1 ILVVEDEKK---LAEYLkkgLTEEGYAVDVAYDGEDGLHLA---LTNEYDLIILDVMLPGLDGLEVLRRLRA-----AGK 69
                          90       100       110
                  ....*....|....*....|....*....|.
gi 739103821 1073 EVSIVALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:cd19935    70 QTPVLMLTARDSVEDRVKGLDLGADDYLVKP 100
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
997-1109 3.19e-16

phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 75.72  E-value: 3.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  997 LLVEDNK-VNQMVAgALLKQAGISFDIAENGLEAIAKIANREhmpYELILMDCQMPEMDGYQATRAIRNgdagtAHREVS 1075
Cdd:cd17625     1 LVVEDEKdLSEAIT-KHLKKEGYTVDVCFDGEEGLEYALSGI---YDLIILDIMLPGMDGLEVLKSLRE-----EGIETP 71
                          90       100       110
                  ....*....|....*....|....*....|....
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKPLNFDSL 1109
Cdd:cd17625    72 VLLLTALDAVEDRVKGLDLGADDYLPKPFSLAEL 105
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
996-1109 3.89e-16

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: 75.60  E-value: 3.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKvnqMVAGAL---LKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNgdagtAHR 1072
Cdd:cd17624     1 ILLVEDDA---LLGDGLktgLRKAGYAVDWVRTGAEAEAALASG---PYDLVILDLGLPDGDGLDLLRRWRR-----QGQ 69
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 739103821 1073 EVSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSL 1109
Cdd:cd17624    70 SLPVLILTARDGVDDRVAGLDAGADDYLVKPFALEEL 106
PRK10490 PRK10490
sensor protein KdpD; Provisional
542-846 1.06e-15

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 82.39  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  542 IPTGSKTMGVVCAEKCHSRQ----QWSKNEESFLIAVAALIGSLHASQRrieTEQqlvkAKEAAEQAvKAKSEFLASMSH 617
Cdd:PRK10490  602 LKSAQKTYGLLAVEPGNLRQlmipEQQRLLETFTLLIANALERLTLTAS---EEQ----ARLASERE-QLRNALLAALSH 673
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  618 EIRTPMNGVIGMLNIIKQtKLDSQQNHHIQLAQSSAESLLH---IINDILDFSKIEAGKLDIENISFNVSKLLGDTVESF 694
Cdd:PRK10490  674 DLRTPLTVLFGQAEILTL-DLASEGSPHARQASEIRQQVLNttrLVNNLLDMARIQSGGFNLRKEWLTLEEVVGSALQML 752
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  695 AIKAEQNNTKLVLDATQInheFIVSDPNRIRQIINNLLGNAIKFTKDG-EIIVLATVkpidDAMYLDCSVVDSGVGIKPE 773
Cdd:PRK10490  753 EPGLSGHPINLSLPEPLT---LIHVDGPLFERVLINLLENAVKYAGAQaEIGIDAHV----EGERLQLDVWDNGPGIPPG 825
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739103821  774 KQATLFDSFTQADASTTrrYGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTFNFSIKVKldyKKQSLEPSHI 846
Cdd:PRK10490  826 QEQLIFDKFARGNKESA--IPGVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVTLPLE---TPPELEEFHE 893
CHASE1 COG3614
Extracytoplasmic sensor domain CHASE1 (specificity unknown) [Signal transduction mechanisms];
17-284 1.60e-15

Extracytoplasmic sensor domain CHASE1 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 442832 [Multi-domain]  Cd Length: 588  Bit Score: 81.27  E-value: 1.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   17 LAFWFSLALIVLIGFVLDHINYNRGKDAF--RSQELAklsayrAELESILISNIQLVRGLAVAVAAEPNLDQTRFAQIAA 94
Cdd:COG3614    16 LVLLLGLLLTALAWWAVRRAEEQRARARFerLADELA------SALEERLDAYEQVLRGLAGLFAASDDVTRAEFRRYVA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   95 P--LFETSSELRNIG--------------------GAPDMVIRMA------------YPL-EGNEKSIGLNFLENAAQRD 139
Cdd:COG3614    90 SldLLRRYPGIQGLGwaprvpaaeraafeaaaraeGFPDFRIRPAgerdeyfpityiEPLdARNRRALGFDMASEPVRRA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  140 DAIKARDENTIVMAGPLELVQGG---HALVARMPVF---MPPD------HKFWGLLSVVLDINKIYTNSGLVSLGNHYDV 207
Cdd:COG3614   170 AMERARDTGRPAASGPVTLVQETdgqPGFLLYLPVYrggAPPDtvaerrAALRGFVYAPFRMDDLLAGVLGRLADRDLDL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  208 AL-QGRNgkGQHGEFFY---GQKHILENTPLSFS--ITFPGGEWRMYVAPKAGWSPPSSTIWPLriaIILVCALFASASL 281
Cdd:COG3614   250 RLyDGTD--PGPPQLLYdssPAAPAAAAPALSATrtLEVAGRTWTLEFRPTPAFEAALRSWLPW---LVLLGGLLLSLLL 324

                  ...
gi 739103821  282 FFL 284
Cdd:COG3614   325 ALL 327
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
724-830 1.83e-15

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: 73.39  E-value: 1.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  724 IRQIINNLLGNAIKFTKDGEIIvlaTVKPIDDAMYLDCSVVDSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLGLAIV 803
Cdd:cd16952     1 LRSAFSNLVSNAVKYTPPSDTI---TVRWSQEESGARLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAIV 77
                          90       100
                  ....*....|....*....|....*..
gi 739103821  804 KQLCKLMQGDVNVVSSYGEGSTFNFSI 830
Cdd:cd16952    78 KHVMSRHDARLLIASELGKGSRFTCLF 104
GAF COG2203
GAF domain [Signal transduction mechanisms];
404-736 1.88e-15

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 81.39  E-value: 1.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  404 IQDIDARKLIELENQKI--ALHNEILASLTVNDAVLTgnlnlskhvIVQAICHALNVDRASIWLFSDDRQSLNTFAIHDQ 481
Cdd:COG2203   178 ARLLTQRARLELERLALlnEISQALRSALDLEELLQR---------ILELAGELLGADRGAILLVDEDGGELELVAAPGL 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  482 SNPQfsdpisLQQIEVQNYF--DAINNNAVINASDAQQHPFTKDLYTDYLDKFDIRSLLTVIIPTGSKTMGVVCAEKCHS 559
Cdd:COG2203   249 PEEE------LGRLPLGEGLagRALRTGEPVVVNDASTDPRFAPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEP 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  560 RqQWSKNEESFLIAVAALIGSLHASQRRIETEQQLVKAKEAAEQAVKAKSEFLASMSHEIRTPMNGVIGMLNIIKQTKLD 639
Cdd:COG2203   323 R-AFTEEDLELLEALADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAE 401
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  640 SQQNHHIQLAQSSAESLLHIINDILDFSKIEAGKLDIENISFNVSKLLGDTVESFAIKAEQNNTKLVLDATQINHEFIVS 719
Cdd:COG2203   402 LLLLLLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLAL 481
                         330
                  ....*....|....*..
gi 739103821  720 DPNRIRQIINNLLGNAI 736
Cdd:COG2203   482 ALLAALLLLLLLLLALL 498
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
606-668 5.68e-15

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: 70.32  E-value: 5.68e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739103821  606 KAKSEFLASMSHEIRTPMNGVIGMLNIIKQTKLDS-QQNHHIQLAQSSAESLLHIINDILDFSK 668
Cdd:cd00082     2 QAKGEFLANVSHELRTPLTAIRGALELLEEELLDDeEQREYLERIREEAERLLRLINDLLDLSR 65
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
446-594 5.88e-15

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: 73.18  E-value: 5.88e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821    446 HVIVQAICHALNVDRASIWLFS-DDRQSLNTFAIHDQSNPQFSDPISLQQIEVQnyfDAINNNAVINASDAQQHP-FTKD 523
Cdd:smart00065    7 QTILEELRQLLGADRVLIYLVDeNDRGELVLVAADGLTLPTLGIRFPLDEGLAG---RVAETGRPLNIPDVEADPlFAED 83
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739103821    524 LYTDYLDkfdIRSLLTVIIPTGSKTMGVVCAEKCHSRQQWSKNEESFLIAVAALIGslhASQRRIETEQQL 594
Cdd:smart00065   84 LLGRYQG---VRSFLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLA---IALANAQLYEEL 148
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
996-1103 7.23e-15

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: 71.64  E-value: 7.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEA------IAKIANREHMPYELILMDCQMPEMDGYQATRAIRNgdaGT 1069
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEAlnklenLAKEGNDLSKELDLIITDIEMPKMDGYELTFELRD---DP 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 739103821 1070 AHREVSIVALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:cd19924    78 RLANIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
994-1103 2.46e-14

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


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 70.36  E-value: 2.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  994 SQILLVEDN-KVNQMVAgALLKQAGISFDIAENGLEAIAKIAnrEHMPyELILMDCQMPEMDGYQATRAIRNgDAGTahR 1072
Cdd:cd17618     1 RTILIVEDEpAIREMIA-FNLERAGFDVVEAEDAESAVNLIV--EPRP-DLILLDWMLPGGSGIQFIRRLKR-DEMT--R 73
                          90       100       110
                  ....*....|....*....|....*....|.
gi 739103821 1073 EVSIVALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:cd17618    74 DIPIIMLTARGEEEDKVRGLEAGADDYITKP 104
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
996-1103 3.82e-14

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: 69.12  E-value: 3.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNGDAgtahreVS 1075
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATR---KPDLIILDLGLPDMDGLEVIRRLREWSA------VP 71
                          90       100
                  ....*....|....*....|....*...
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:cd17620    72 VIVLSARDEESDKIAALDAGADDYLTKP 99
PRK11517 PRK11517
DNA-binding response regulator HprR;
995-1120 3.91e-14

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 73.01  E-value: 3.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  995 QILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIaKIANREHmpYELILMDCQMPEMDGYQATRAIRngdagTAHrEV 1074
Cdd:PRK11517    2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGL-YLALKDD--YALIILDIMLPGMDGWQILQTLR-----TAK-QT 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 739103821 1075 SIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKLSVWLDTH 1120
Cdd:PRK11517   73 PVICLTARDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQLRQH 118
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
603-830 7.98e-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: 7.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  603 QAVKAKSEFLASMSHEIRTPMNGVIGMLniikqtkldsqQNHHIQLAQSSAESLLHIINDILDFSKIEagkldIENISfn 682
Cdd:COG3290   184 EGVKELAEALRAQRHDFRNHLHTISGLL-----------QLGEYDEALEYIDEISEELQELIDSLLSR-----IGNPV-- 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  683 VSKLLgdtvESFAIKAEQNNTKLVLDATQINHEFIVSDPNrIRQIINNLLGNAI-----KFTKDGEIIVLATvkpiDDAM 757
Cdd:COG3290   246 LAALL----LGKAARARERGIDLTIDIDSDLPDLPLSDTD-LVTILGNLLDNAIeavekLPEEERRVELSIR----DDGD 316
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739103821  758 YLDCSVVDSGVGIKPEKQATLFDsftqaDASTTRRYGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTFNFSI 830
Cdd:COG3290   317 ELVIEVEDSGPGIPEELLEKIFE-----RGFSTKLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRL 384
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
599-803 8.12e-14

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 75.35  E-value: 8.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  599 EAAEQAVKAKSEFLASMSHEIRTPMNGVIGMLNIIKQTKLDSQQNHHIQlaqSSAESLLHIINDILDFSKIEAgKLDIEN 678
Cdd:PRK09470  234 TALERMMTSQQRLLSDISHELRTPLTRLQLATALLRRRQGESKELERIE---TEAQRLDSMINDLLVLSRNQQ-KNHLER 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  679 ISFNVSKLLGDTVESFAIKAEQNNTKLVLDAtQINHEFIVSDPNRIRQIINNLLGNAIKFTKDgEIIVLATVkpidDAMY 758
Cdd:PRK09470  310 ETFKANSLWSEVLEDAKFEAEQMGKSLTVSA-PPGPWPINGNPNALASALENIVRNALRYSHT-KIEVAFSV----DKDG 383
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 739103821  759 LDCSVVDSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLGLAIV 803
Cdd:PRK09470  384 LTITVDDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAIV 428
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
564-838 9.78e-14

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 74.82  E-value: 9.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  564 SKNEESFLIAVAALIGSLHAS-------QRRIETEQQLVKAKEAAEQAVkAKSEFLASMSHEIRTPMNGVIGMLNIIKQT 636
Cdd:PRK10364  187 AREQRNTLIILFALATVLLASllaffwyRRYLRSRQLLQDEMKRKEKLV-ALGHLAAGVAHEIRNPLSSIKGLAKYFAER 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  637 KLDSQQNHhiQLAQ---SSAESLLHIINDILDFSK---IEAGKLDIENISFNVSKLLGDTVESFAIKAEQNNTKLVldat 710
Cdd:PRK10364  266 APAGGEAH--QLAQvmaKEADRLNRVVSELLELVKpthLALQAVDLNDLINHSLQLVSQDANSREIQLRFTANDTL---- 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  711 qinhEFIVSDPNRIRQIINNLLGNAIK-FTKDGEIIVlaTVKPIDDAMYLdcSVVDSGVGIKPEKQATLFDSF--TQADa 787
Cdd:PRK10364  340 ----PEIQADPDRLTQVLLNLYLNAIQaIGQHGVISV--TASESGAGVKI--SVTDSGKGIAADQLEAIFTPYftTKAE- 410
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 739103821  788 sttrrygGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTFNFSIKVKLDYKK 838
Cdd:PRK10364  411 -------GTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLPVNITRRD 454
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
996-1110 1.08e-13

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: 68.96  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVN-QMVAGALLKQAGISF-DIAENGLEAIAKIanREHMPyELILMDCQMPEMDGYQATRAIRngdagtAHRE 1073
Cdd:cd17541     3 VLIVDDSAVMrKLLSRILESDPDIEVvGTARDGEEALEKI--KELKP-DVITLDIEMPVMDGLEALRRIM------AERP 73
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 739103821 1074 VSIVALTANAMQGDKE--RCLNAGMNDYLTKPLNFDSLN 1110
Cdd:cd17541    74 TPVVMVSSLTEEGAEItlEALELGAVDFIAKPSGGISLD 112
CHASE pfam03924
CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - ...
82-223 1.20e-13

CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - such as serine/threonine kinases and adenylyl cyclases. This is a ligand-binding domain that binds cytokinin (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 427591  Cd Length: 184  Bit Score: 70.40  E-value: 1.20e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821    82 PNLDQTRFAQIAAPLFETSSELRNIG--------------------GAPDMVIR------------MAYPLEGNEKSIGL 129
Cdd:pfam03924    1 DSVDREEFRRYAASLLLRRPGIQGLGwaprvpaaeraafeaavraeGFPDFTIRpagdrdeyfpiiYIEPLAGNNRALGF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   130 NFLENAAQRDDAIKARDENTIVMAGPLELVQGGH---ALVARMPVFMPPDH--------KFWGLLSVVLDINKIYtnSGL 198
Cdd:pfam03924   81 DMASEPVRREAIERARDTGEPVLSGPVTLVQDGDgqpGFLLYLPVYRGGPPdtvaerraALLGFVYAPFRIDDLL--EAA 158
                          170       180
                   ....*....|....*....|....*.
gi 739103821   199 VSLGNHYDVALQGRNG-KGQHGEFFY 223
Cdd:pfam03924  159 LLRLGEDGLDLALYDGtSASAPELLY 184
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
724-831 2.12e-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: 67.92  E-value: 2.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  724 IRQIINNLLGNAIKFTKDGEIIVLaTVKPIDDAMYLDcsVVDSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLGLAIV 803
Cdd:cd16947    21 LQRILKNLISNAIKYGSDGKFLGM-TLREDEKHVYID--IWDKGKGISETEKDHVFERLYTLEDSRNSAKQGNGLGLTIT 97
                          90       100
                  ....*....|....*....|....*...
gi 739103821  804 KQLCKLMQGDVNVVSSYGEGSTFNFSIK 831
Cdd:cd16947    98 KRLAESMGGSIYVNSKPYEKTVFTVTLK 125
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
614-816 2.66e-13

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 73.73  E-value: 2.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  614 SMSHEIRTPMNGVIGMLNIIkQTKLDSQQNHHIqLAQSSAES--LLHIINDILDFSKIEAGK--LDIENIsfNVSKLLGD 689
Cdd:PRK11100  262 TLTHELKSPLAAIRGAAELL-QEDPPPEDRARF-TGNILTQSarLQQLIDRLLELARLEQRQelEVLEPV--ALAALLEE 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  690 TVESFAIKAEQNNTKLVLDATQINhefIVSDPNRIRQIINNLLGNAIKFT-KDGEIIVLATVkpidDAMYLDCSVVDSGV 768
Cdd:PRK11100  338 LVEAREAQAAAKGITLRLRPDDAR---VLGDPFLLRQALGNLLDNAIDFSpEGGTITLSAEV----DGEQVALSVEDQGP 410
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 739103821  769 GIkPE-KQATLFDSFTqadaSTTRRYGG---TGLGLAIVKQLCKLMQGDVNV 816
Cdd:PRK11100  411 GI-PDyALPRIFERFY----SLPRPANGrksTGLGLAFVREVARLHGGEVTL 457
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
592-876 2.84e-13

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 74.58  E-value: 2.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  592 QQLVKAKEAAEQAVKAKSEFLASMSHEIRTPMNGVIGMLNIIKQTKLDSQQNHHIQLAQSSAESLLHIINDILDFSKIEA 671
Cdd:PRK10618  434 KKLQQAQREYEKNQQARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNMLET 513
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  672 GKLDIENISFNVSKLLGDTVESFAIKAEQNNTKLV----LDATQINHefivSDPNRIRQIINNLLGNAIKFTKDGEIIVl 747
Cdd:PRK10618  514 QDWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLLihnhLKAEQLRI----GDRDALRKILLLLLNYAITTTAYGKITL- 588
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  748 aTVKPidDAMYLDC---SVVDSGVGIKPEKQATL---FDSFTQADasttrRYG-GTGLGLAIVKQLCKLMQGDVNVVSSY 820
Cdd:PRK10618  589 -EVDQ--DESSPDRltiRILDTGAGVSIKELDNLhfpFLNQTQGD-----RYGkASGLTFFLCNQLCRKLGGHLTIKSRE 660
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 739103821  821 GEGSTFNFSIKVKLDYKKQSLEPSHIIDKKQILIADSCTLSSNIAKKQLQLWGAEV 876
Cdd:PRK10618  661 GLGTRYSIHLKMLAADPEVEEEEEKLLDGVTVLLDITSEEVRKIVTRQLENWGATC 716
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
992-1110 3.41e-13

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 73.34  E-value: 3.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  992 SASQILLVEDNK-VNQMVAGALLKQaGISFDIAENGLEAIAKIANrehMPYELILMDCQMPEMDGYQATRAIRNGDAGTA 1070
Cdd:PRK11361    3 AINRILIVDDEDnVRRMLSTAFALQ-GFETHCANNGRTALHLFAD---IHPDVVLMDIRMPEMDGIKALKEMRSHETRTP 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 739103821 1071 hrevsIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLN 1110
Cdd:PRK11361   79 -----VILMTAYAEVETAVEALRCGAFDYVIKPFDLDELN 113
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
996-1102 4.98e-13

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: 66.77  E-value: 4.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQM-VAGALLKQAGIS-FDIAENGLEAIAKIanREHMPyELILMDCQMPEMDGYQATRAIRNgdagtAHRE 1073
Cdd:cd17535     1 VLIVDDHPLVREgLRRLLESEPDIEvVGEAADGEEALALL--RELRP-DVVLMDLSMPGMDGIEALRRLRR-----RYPD 72
                          90       100
                  ....*....|....*....|....*....
gi 739103821 1074 VSIVALTANAMQGDKERCLNAGMNDYLTK 1102
Cdd:cd17535    73 LKVIVLTAHDDPEYVLRALKAGAAGYLLK 101
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
996-1103 9.60e-13

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: 65.48  E-value: 9.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIaKIANREHmpYELILMDCQMPEMDGYQATRAIRNgdaGTAHREVS 1075
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEAL-DLLNQYI--PDLIISDIIMPGVDGYSLLGKLRK---NADFDTIP 74
                          90       100
                  ....*....|....*....|....*...
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:cd19927    75 VIFLTAKGMTSDRIKGYNAGCDGYLSKP 102
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
724-835 1.01e-12

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: 65.16  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  724 IRQIINNLLGNAIKFTKdGEIIVLATVKPiddaMYLDCSVVDSGVGIKPEKQATLFDSFTQADASttRRYGGTGLGLAIV 803
Cdd:cd16950     1 LKRVLSNLVDNALRYGG-GWVEVSSDGEG----NRTRIQVLDNGPGIAPEEVDELFQPFYRGDNA--RGTSGTGLGLAIV 73
                          90       100       110
                  ....*....|....*....|....*....|..
gi 739103821  804 KQLCKLMQGDVNVVSSYGEGstfnFSIKVKLD 835
Cdd:cd16950    74 QRISDAHGGSLTLANRAGGG----LCARIELP 101
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
995-1104 1.17e-12

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: 65.76  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  995 QILLVEDNKVNQMVAGALLKQAGisFDI---AENGLEAIAKIanREHMPyELILMDCQMPEMDGYQATRAIRNGDAGtah 1071
Cdd:cd17542     2 KVLIVDDAAFMRMMLKDILTKAG--YEVvgeAANGEEAVEKY--KELKP-DLVTMDITMPEMDGIEALKEIKKIDPN--- 73
                          90       100       110
                  ....*....|....*....|....*....|...
gi 739103821 1072 reVSIVALTANAMQGDKERCLNAGMNDYLTKPL 1104
Cdd:cd17542    74 --AKVIMCSAMGQEEMVKEAIKAGAKDFIVKPF 104
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
996-1109 1.63e-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: 1.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNK-VNQMVAGALLKQaGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNGDagtahREV 1074
Cdd:cd19934     1 LLLVEDDAlLAAQLKEQLSDA-GYVVDVAEDGEEALFQGEEE---PYDLVVLDLGLPGMDGLSVLRRWRSEG-----RAT 71
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 739103821 1075 SIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSL 1109
Cdd:cd19934    72 PVLILTARDSWQDKVEGLDAGADDYLTKPFHIEEL 106
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
609-830 1.80e-12

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: 71.70  E-value: 1.80e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   609 SEFLASMS----HEIRTPMNGVIGMLNIIKQTKLDSQQNHHIQLAQSSAESLLHIINDILDFSKIEAGKLDIENISFNVS 684
Cdd:TIGR03785  482 THYLENMSsrlsHELRTPVAVVRSSLENLELQALEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLS 561
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   685 KLLGDTVESFAIKAEQNNTKLVLDAT----QINHEFIVsdpnrirQIINNLLGNAIKFTKDGEIIVLaTVKPIDDAMYLd 760
Cdd:TIGR03785  562 EVLSGCMQGYQMTYPPQRFELNIPETplvmRGSPELIA-------QMLDKLVDNAREFSPEDGLIEV-GLSQNKSHALL- 632
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739103821   761 cSVVDSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLGLAIVKQLCKLMQGDVNVVSSY-GEGSTFNFSI 830
Cdd:TIGR03785  633 -TVSNEGPPLPEDMGEQLFDSMVSVRDQGAQDQPHLGLGLYIVRLIADFHQGRIQAENRQqNDGVVFRISL 702
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
995-1109 1.94e-12

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: 65.13  E-value: 1.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  995 QILLVEDNKVNQMVAGALLKQAGisFDI---AENGLEAIAKIanREHMPyELILMDCQMPEMDGYQATRAIrngdagTAH 1071
Cdd:cd19932     2 RVLIAEDEALIRMDLREMLEEAG--YEVvgeASDGEEAVELA--KKHKP-DLVIMDVKMPRLDGIEAAKII------TSE 70
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 739103821 1072 REVSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSL 1109
Cdd:cd19932    71 NIAPIVLLTAYSQQDLVERAKEAGAMAYLVKPFSESDL 108
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
996-1109 2.09e-12

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: 64.71  E-value: 2.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDN-KVNQMVAGALlKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNGDagtahREV 1074
Cdd:cd17627     1 ILVVDDDrAVRESLRRSL-RFEGYEVETAVDGAEALRVISGN---RPDAVVLDVMMPRLDGLEVCRRLRAAG-----NDL 71
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 739103821 1075 SIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSL 1109
Cdd:cd17627    72 PILVLTARDSVSDRVAGLDAGADDYLVKPFALEEL 106
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
572-826 2.26e-12

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 71.63  E-value: 2.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  572 IAVAALIGslHASQRRIETEQQLVKAK-EAAE--QAVKAksefLAS-MSHEIRTPMNGVIGMLNIiKQTKLD--SQQNHH 645
Cdd:PRK13837  416 LALDCLAH--AIERRRLETERDALERRlEHARrlEAVGT----LASgIAHNFNNILGAILGYAEM-ALNKLArhSRAARY 488
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  646 IQLAQSSAESLLHIINDILDFSKieagKLDIENISFNVSKLLGDTVESFAIkAEQNNTKLVLDATQINHEfIVSDPNRIR 725
Cdd:PRK13837  489 IDEIISAGARARLIIDQILAFGR----KGERNTKPFDLSELVTEIAPLLRV-SLPPGVELDFDQDQEPAV-VEGNPAELQ 562
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  726 QIINNLLGNAIKFTKDG---EIIVLATVKPIDDAM---------YLDCSVVDSGVGIKPEKQATLFDSFTqadastTRRY 793
Cdd:PRK13837  563 QVLMNLCSNAAQAMDGAgrvDISLSRAKLRAPKVLshgvlppgrYVLLRVSDTGAGIDEAVLPHIFEPFF------TTRA 636
                         250       260       270
                  ....*....|....*....|....*....|...
gi 739103821  794 GGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTF 826
Cdd:PRK13837  637 GGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRF 669
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
720-834 2.31e-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: 64.73  E-value: 2.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  720 DPNRIRQIINNLLGNAIKFTKDGEIIVLATVKPIDDAMyldcSVVDSGVGIKPEKQATLFDSFTQADASTtrrYGGTGLG 799
Cdd:cd16940    10 DALLLFLLLRNLVDNAVRYSPQGSRVEIKLSADDGAVI----RVEDNGPGIDEEELEALFERFYRSDGQN---YGGSGLG 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 739103821  800 LAIVKQLCKLMQGDVNVVSSYGEGstfnFSIKVKL 834
Cdd:cd16940    83 LSIVKRIVELHGGQIFLGNAQGGG----LEAWVRL 113
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
996-1113 2.50e-12

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: 64.67  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGIS-FDIAENGLEAIAKIanrEHMPYELILMDCQMPEMDGYQATRAIRngdAGTAHREV 1074
Cdd:cd19923     3 VLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKL---KAGGFDFVITDWNMPNMDGLELLKTIR---ADGALSHL 76
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 739103821 1075 SIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKL 1113
Cdd:cd19923    77 PVLMVTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKL 115
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
995-1109 5.76e-12

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: 63.66  E-value: 5.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  995 QILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIanREHMPyELILMDCQMPEMDGYQATRAIRNgdagtAHREV 1074
Cdd:COG5803     4 KILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKV--KELKP-DLVLLDMKMPGMDGIEILKEIKE-----IDPDI 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 739103821 1075 SIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSL 1109
Cdd:COG5803    76 PVIMMTAYGELDMVEEAKELGAKGYFTKPFDIDEL 110
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
446-579 6.72e-12

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: 64.04  E-value: 6.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   446 HVIVQAICHALNVDRASIWLFSDDRQSLNTfaihdqSNPQFSDPISLQQIEVQNYfDAINNNAVINASDAQQHPFTKDLY 525
Cdd:pfam01590    7 QTILEELRELLGADRCALYLPDADGLEYLP------PGARWLKAAGLEIPPGTGV-TVLRTGRPLVVPDAAGDPRFLDPL 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 739103821   526 tDYLDKFDIRSLLTVIIPTGSKTMGVVCAEkcHSRQQWSKNEESFLIAVAALIG 579
Cdd:pfam01590   80 -LLLRNFGIRSLLAVPIIDDGELLGVLVLH--HPRPPFTEEELELLEVLADQVA 130
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
721-826 7.86e-12

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: 62.82  E-value: 7.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  721 PNRIRQIINNLLGNAIK-FTKDGEIivlaTVKPIDDAMYLDCSVVDSGVGIKPEKQATLFDSFTqadasTTRRYG-GTGL 798
Cdd:cd16943     1 PSQLNQVLLNLLVNAAQaMEGRGRI----TIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPFF-----TTKPVGeGTGL 71
                          90       100
                  ....*....|....*....|....*...
gi 739103821  799 GLAIVKQLCKLMQGDVNVVSSYGEGSTF 826
Cdd:cd16943    72 GLSLSYRIIQKHGGTIRVASVPGGGTRF 99
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
996-1105 9.89e-12

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: 62.71  E-value: 9.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANREhmpYELILMDCQMPEMDGYQATRAIRngdagtAHREVS 1075
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGS---PDLVVLDVMLPKMNGLDVLKELR------KTSQVP 71
                          90       100       110
                  ....*....|....*....|....*....|
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKPLN 1105
Cdd:cd17623    72 VLMLTARGDDIDRILGLELGADDYLPKPFN 101
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
995-1122 1.03e-11

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 68.52  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  995 QILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIanREHMpYELILMDCQMPEMDGYQATRAIRngdagTAHREV 1074
Cdd:PRK10365    7 DILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQV--REQV-FDLVLCDVRMAEMDGIATLKEIK-----ALNPAI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 739103821 1075 SIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKLSVWLDTHQE 1122
Cdd:PRK10365   79 PVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHS 126
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
996-1105 1.66e-11

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: 62.34  E-value: 1.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIanREHMPyELILMDCQMPEMDGYQATRAIRnGDAGTAHreVS 1075
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAML--AEHRP-TLVISDIVMPEMDGYELCRKIK-SDPDLKD--IP 74
                          90       100       110
                  ....*....|....*....|....*....|
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKPLN 1105
Cdd:cd17598    75 VILLTTLSDPRDVIRGLECGADNFITKPYD 104
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
727-829 1.74e-11

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: 61.92  E-value: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  727 IINNLLGNAIKFTKDGEIIvlaTVKPIDDAMYLDCSVVDSGVGIKPEKQATLFDS-FTQADASTTRRygGTGLGLAIVKQ 805
Cdd:cd16948     9 IIGQIVSNALKYSKQGGKI---EIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKgFTGENGRNFQE--STGMGLYLVKK 83
                          90       100
                  ....*....|....*....|....
gi 739103821  806 LCKLMQGDVNVVSSYGEGSTFNFS 829
Cdd:cd16948    84 LCDKLGHKIDVESEVGEGTTFTIT 107
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
730-829 2.72e-11

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: 61.29  E-value: 2.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  730 NLLGNAIKFTkDGEIIVLATVKpiDDAMYLDcsVVDSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLGLAIVKQLCKL 809
Cdd:cd16939     7 NLLRNALRYA-HRTVRIALLVS--GGRLTLI--VEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAIVHRVALW 81
                          90       100
                  ....*....|....*....|
gi 739103821  810 MQGDVNVVSSYGEGSTFNFS 829
Cdd:cd16939    82 HGGHVECDDSELGGACFRLT 101
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
724-830 2.90e-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: 61.26  E-value: 2.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  724 IRQIINNLLGNAIKFTKDGEI---IVLATVKPIDDAMyLDCSVVDSGVGIKPEKQATLFDSFTQADASttrrygGTGLGL 800
Cdd:cd16920     1 IQQVLINLVRNGIEAMSEGGCerrELTIRTSPADDRA-VTISVKDTGPGIAEEVAGQLFDPFYTTKSE------GLGMGL 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 739103821  801 AIVKQLCKLMQGDVNVVSSYGEGSTFNFSI 830
Cdd:cd16920    74 SICRSIIEAHGGRLSVESPAGGGATFQFTL 103
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
720-816 3.32e-11

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: 60.94  E-value: 3.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  720 DPNRIRQIINNLLGNAIKFTKDGEIIVLATVKPIDDAMYLdcsVVDSGVGIKPEKQATLFDSF-TQADASTTRRygGTGL 798
Cdd:cd16945     1 DPFLLRQAINNLLDNAIDFSPEGGLIALQLEADTEGIELL---VFDEGSGIPDYALNRVFERFySLPRPHSGQK--STGL 75
                          90
                  ....*....|....*...
gi 739103821  799 GLAIVKQLCKLMQGDVNV 816
Cdd:cd16945    76 GLAFVQEVAQLHGGRITL 93
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
996-1051 3.37e-11

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: 59.50  E-value: 3.37e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 739103821    996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANrehMPYELILMDCQMP 1051
Cdd:smart00448    3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKE---EKPDLILLDIMMP 55
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
996-1103 3.42e-11

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: 61.38  E-value: 3.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIAnrEHMPYELILMDCQMPEMDGYQATRAIRNgdaGTAHREVS 1075
Cdd:cd17544     3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLE--QHPDIKLVITDYNMPEMDGFELVREIRK---KYSRDQLA 77
                          90       100
                  ....*....|....*....|....*...
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:cd17544    78 IIGISASGDNALSARFIKAGANDFLTKP 105
envZ PRK09467
osmolarity sensor protein; Provisional
612-816 3.83e-11

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 66.47  E-value: 3.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  612 LASMSHEIRTPMngvigmlniikqTKldsqqnhhIQLAQ---SSAESLLH--IINDILDFSKI---------EAGKLDIE 677
Cdd:PRK09467  233 MAGVSHDLRTPL------------TR--------IRLATemmSEEDGYLAesINKDIEECNAIieqfidylrTGQEMPME 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  678 NISFNvsKLLGDTVESFAIKAEQNNTKLVLDATQINhefivSDPNRIRQIINNLLGNAIKFTKdGEIIVLATVkpidDAM 757
Cdd:PRK09467  293 MADLN--ALLGEVIAAESGYEREIETALQPGPIEVP-----MNPIAIKRALANLVVNAARYGN-GWIKVSSGT----EGK 360
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 739103821  758 YLDCSVVDSGVGIKPEKQATLFDSFTQADasTTRRYGGTGLGLAIVKQLCKLMQGDVNV 816
Cdd:PRK09467  361 RAWFQVEDDGPGIPPEQLKHLFQPFTRGD--SARGSSGTGLGLAIVKRIVDQHNGKVEL 417
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
996-1105 4.36e-11

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


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 63.44  E-value: 4.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGIS-FDIAENGLEAIAKIanREHMPyELILMDCQMPEMDGYQATRAIrngdagTAHREV 1074
Cdd:COG3707     6 VLVVDDEPLRRADLREGLREAGYEvVAEAADGEDAVELV--RELKP-DLVIVDIDMPDRDGLEAARQI------SEERPA 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 739103821 1075 SIVALTANAMQGDKERCLNAGMNDYLTKPLN 1105
Cdd:COG3707    77 PVILLTAYSDPELIERALEAGVSAYLVKPLD 107
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
422-607 5.65e-11

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 62.61  E-value: 5.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  422 LHNEILASLTVNDAVltgnlnlskHVIVQAICHALNVDRASIWLFSDDRQSLNTFAiHDQSNPQfsdpiSLQQIEVQnyF 501
Cdd:COG3605     9 ISEAVASALDLDEAL---------DRIVRRIAEALGVDVCSIYLLDPDGGRLELRA-TEGLNPE-----AVGKVRLP--L 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  502 D------AINNNAVINASDAQQHP-FtkdLYTDYLDKFDIRSLLTVIIPTGSKTMGVVCAEKCHSRqQWSKNEESFLIAV 574
Cdd:COG3605    72 GeglvglVAERGEPLNLADAASHPrF---KYFPETGEEGFRSFLGVPIIRRGRVLGVLVVQSREPR-EFTEEEVEFLVTL 147
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 739103821  575 AALIGSL--HA---SQRRIETEQQLVKAKEAAEQAVKA 607
Cdd:COG3605   148 AAQLAEAiaNAellGELRAALAELSLAREEEREAAVEA 185
pleD PRK09581
response regulator PleD; Reviewed
1023-1105 5.76e-11

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 66.08  E-value: 5.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821 1023 AENGLEAIAkIANREHMpyELILMDCQMPEMDGYQATRAIRNgDAGTAHreVSIVALTANAMQGDKERCLNAGMNDYLTK 1102
Cdd:PRK09581   32 ASSGAEAIA-ICEREQP--DIILLDVMMPGMDGFEVCRRLKS-DPATTH--IPVVMVTALDDPEDRVRGLEAGADDFLTK 105

                  ...
gi 739103821 1103 PLN 1105
Cdd:PRK09581  106 PIN 108
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
996-1105 1.10e-10

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: 59.71  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRngdagtAHREVS 1075
Cdd:cd17619     3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQ---DIDLVLLDINLPGKDGLSLTRELR------EQSEVG 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKPLN 1105
Cdd:cd17619    74 IILVTGRDDEVDRIVGLEIGADDYVTKPFN 103
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
996-1103 1.29e-10

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: 59.74  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKiaNREHMPyELILMDCQMPEMDGYQATRAIRNgdagtaHREVS 1075
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEK--VEEEQP-DLILLDLMLPEKDGLEVCREVRK------TSNVP 71
                          90       100
                  ....*....|....*....|....*...
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:cd17614    72 IIMLTAKDSEVDKVLGLELGADDYVTKP 99
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
996-1109 1.36e-10

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 59.73  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGI---SFDIAENGLEaIAKIANrehmpYELILMDCQMPEMDGYQATRAIRngdagTAHR 1072
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFnvyTTDLGEEGLD-LGKLYD-----YDIILLDLNLPDMSGYEVLRTLR-----LAKV 69
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 739103821 1073 EVSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSL 1109
Cdd:cd17616    70 KTPILILSGLADIEDKVKGLGFGADDYMTKPFHKDEL 106
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
996-1109 1.38e-10

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: 59.73  E-value: 1.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGIS-FDIAENGLEAIAKIanREHMPyELILMDCQMP-EMDGYQATRAIRNgdagtaHRE 1073
Cdd:cd17534     3 ILIVEDEAIIALDLKEILESLGYEvVGIADSGEEAIELA--EENKP-DLILMDINLKgDMDGIEAAREIRE------KFD 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 739103821 1074 VSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSL 1109
Cdd:cd17534    74 IPVIFLTAYSDEETLERAKETNPYGYLVKPFNEREL 109
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
996-1110 1.49e-10

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: 59.52  E-value: 1.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNgdagtAHREVS 1075
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQ---PPDVVLLDLKLPDMSGMEILKWIQE-----RSLPTS 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 739103821 1076 IVALTA--------NAMQgdkerclnAGMNDYLTKPLNFDSLN 1110
Cdd:cd17572    73 VIVITAhgsvdiavEAMR--------LGAYDFLEKPFDADRLR 107
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
1013-1109 1.59e-10

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: 59.59  E-value: 1.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821 1013 LKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNGDagtAHREVSIVALTANAMQGDKERCL 1092
Cdd:cd19937    17 LEKEGYEVVTAYDGEEALKRAKDE---KPDLIILDLMLPGIDGLEVCRILRSDP---KTSSIPIIMLTAKGEEFDKVLGL 90
                          90
                  ....*....|....*..
gi 739103821 1093 NAGMNDYLTKPLNFDSL 1109
Cdd:cd19937    91 ELGADDYITKPFSPREL 107
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
996-1113 2.79e-10

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: 58.89  E-value: 2.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVnqMVAG--ALLKQAGISFDI---AENGLEAIAKIanREHMPyELILMDCQMPEMDGYQATRAIRNgdagtA 1070
Cdd:cd17536     1 VLIVDDEPL--IREGlkKLIDWEELGFEVvgeAENGEEALELI--EEHKP-DIVITDIRMPGMDGLELIEKIRE-----L 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 739103821 1071 HREVSIVALTANAmqgDKE---RCLNAGMNDYLTKPLNFDSLNKKL 1113
Cdd:cd17536    71 YPDIKIIILSGYD---DFEyaqKAIRLGVVDYLLKPVDEEELEEAL 113
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
996-1109 3.05e-10

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: 58.85  E-value: 3.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDN-KVNQMVAGALlKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRngdAGTAHREV 1074
Cdd:cd17562     3 ILAVDDSaSIRQMVSFTL-RGAGYEVVEAADGRDALSKAQSK---KFDLIITDQNMPNMDGIELIKELR---KLPAYKFT 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 739103821 1075 SIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSL 1109
Cdd:cd17562    76 PILMLTTESSDEKKQEGKAAGATGWLVKPFDPEQL 110
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
995-1103 3.21e-10

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: 58.54  E-value: 3.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  995 QILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIAnreHMPYELILMDCQMPEMDGYQATRAIRngdagtAHREV 1074
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVR---HTPPDLILLDLMLPGTDGLTLCREIR------RFSDV 71
                          90       100
                  ....*....|....*....|....*....
gi 739103821 1075 SIVALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:cd19938    72 PIIMVTARVEEIDRLLGLELGADDYICKP 100
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
715-830 3.53e-10

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: 59.01  E-value: 3.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  715 EFIVSDPNRIRQIINNLLGNAIKFTKDGEIIVL--------ATVKPIDDAMYLDCSVvDSGVGIKPEKQATLFDSFTQAD 786
Cdd:cd16938     3 DVVVGDERRVFQVLLHMLGNLLKMRNGGGNITFrvfleggsEDRSDRDWGPWRPSMS-DESVEIRFEVEINDSGSPSIES 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 739103821  787 ASTT----RRYG----GTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTFNFSI 830
Cdd:cd16938    82 ASMRnslnRRYNlselGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
611-812 4.11e-10

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 62.68  E-value: 4.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  611 FLASMSHEIRTPMNGVIGMLNIIkqtkldsQQNHHIQLAQSSA--ESLLHIINDILDFSKIE----AGkldieniSFNVS 684
Cdd:PRK10755  140 FTADVAHELRTPLAGIRLHLELL-------EKQHHIDVAPLIArlDQMMHTVEQLLQLARAGqsfsSG-------HYQTV 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  685 KLLGDTV----ESFAIKAEQNNTKLVL--DATQINhefIVSDPNRIRQIINNLLGNAIKFTKDGEIIvlaTVKPIDDAMY 758
Cdd:PRK10755  206 KLLEDVIlpsqDELSEMLEQRQQTLLLpeSAADIT---VQGDATLLRLLLRNLVENAHRYSPEGSTI---TIKLSQEDGG 279
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 739103821  759 LDCSVVDSGVGIKPEKQATLFDSFTQADasttRRYGGTGLGLAIVKQLCKLMQG 812
Cdd:PRK10755  280 AVLAVEDEGPGIDESKCGELSKAFVRMD----SRYGGIGLGLSIVSRITQLHHG 329
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
726-822 9.54e-10

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: 57.03  E-value: 9.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  726 QIINNLLGNAIKFTK--DGEIIVLA------TVKPIDDAMYLDCSVVDSGVGIKPEKQATLFDSFTqadastTRRYGGTG 797
Cdd:cd16918     3 QVFLNLVRNAAQALAgsGGEIILRTrtqrqvTLGHPRHRLALRVSVIDNGPGIPPDLQDTIFYPMV------SGRENGTG 76
                          90       100
                  ....*....|....*....|....*
gi 739103821  798 LGLAIVKQLCKLMQGDVNVVSSYGE 822
Cdd:cd16918    77 LGLAIAQNIVSQHGGVIECDSQPGH 101
PRK15479 PRK15479
transcriptional regulator TctD;
995-1113 1.56e-09

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 59.35  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  995 QILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAiakianrEHM----PYELILMDCQMPEMDGYQA-TRAIRNGdagt 1069
Cdd:PRK15479    2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAA-------DHLlqseMYALAVLDINMPGMDGLEVlQRLRKRG---- 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 739103821 1070 ahREVSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKL 1113
Cdd:PRK15479   71 --QTLPVLLLTARSAVADRVKGLNVGADDYLPKPFELEELDARL 112
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
995-1114 1.77e-09

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


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 56.39  E-value: 1.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  995 QILLVEDNKV--NQMvAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNGDagtahR 1072
Cdd:cd17593     2 KVLICDDSSMarKQL-ARALPADWDVEITFAENGEEALEILREG---RIDVLFLDLTMPVMDGYEVLEALPVEQ-----L 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 739103821 1073 EVSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKLS 1114
Cdd:cd17593    73 ETKVIVVSGDVQPEAKERVLELGALAFLKKPFDPEKLAQLLE 114
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
994-1105 2.51e-09

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 55.94  E-value: 2.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  994 SQILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAkiANREHMPyELILMDCQMPEMDGYQATRAIRngdagtAHRE 1073
Cdd:cd17626     1 ARILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALA--AFREVRP-DLVLLDLMLPGIDGIEVCRQIR------AESG 71
                          90       100       110
                  ....*....|....*....|....*....|..
gi 739103821 1074 VSIVALTANAMQGDKERCLNAGMNDYLTKPLN 1105
Cdd:cd17626    72 VPIVMLTAKSDTVDVVLGLESGADDYVAKPFK 103
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
996-1103 4.74e-09

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 54.68  E-value: 4.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNgdaGTAHREVS 1075
Cdd:cd17602     1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNS---KPDLILIDIDMPDLDGYELCSLLRK---SSALKDTP 74
                          90       100
                  ....*....|....*....|....*...
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:cd17602    75 IIMLTGKDGLVDRIRAKMAGASGYLTKP 102
glnL PRK11073
nitrogen regulation protein NR(II);
584-818 6.15e-09

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 59.32  E-value: 6.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  584 SQRRIETEQQlvkaKEAAEQAVKaksEFLASMSHEIRTPMNGVIGMLNIIKQTKLDSQQNHHIQLAQSSAESLLHIINDI 663
Cdd:PRK11073  113 NQRRLSQEQL----QHAQQVAAR---DLVRGLAHEIKNPLGGLRGAAQLLSKALPDPALTEYTKVIIEQADRLRNLVDRL 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  664 LDFSKieAGKLDIENISF---NVSKLLgdTVESfaikaeQNNTKLVLDATQINHEFIVsDPNRIRQIINNLLGNAIK-FT 739
Cdd:PRK11073  186 LGPQR--PGTHVTESIHKvaeRVVQLV--SLEL------PDNVRLIRDYDPSLPELAH-DPDQIEQVLLNIVRNALQaLG 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  740 KDGEIIVLAT---------------VKPIDdamyldcsVVDSGVGIKPEKQATLFDSFTQAdasttrRYGGTGLGLAIVK 804
Cdd:PRK11073  255 PEGGTITLRTrtafqltlhgeryrlAARID--------IEDNGPGIPPHLQDTLFYPMVSG------REGGTGLGLSIAR 320
                         250
                  ....*....|....
gi 739103821  805 QLCKLMQGDVNVVS 818
Cdd:PRK11073  321 NLIDQHSGKIEFTS 334
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
727-826 6.54e-09

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: 54.60  E-value: 6.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  727 IINNLLGNAIKFTKD-----GEIIVLATvkpiDDAMYLDCSVVDSGVGIKPEKQATLFDSftqadASTTRRYGGTGLGLA 801
Cdd:cd16915     4 IVGNLIDNALDALAAtgapnKQVEVFLR----DEGDDLVIEVRDTGPGIAPELRDKVFER-----GVSTKGQGERGIGLA 74
                          90       100
                  ....*....|....*....|....*
gi 739103821  802 IVKQLCKLMQGDVNVVSSYGEGSTF 826
Cdd:cd16915    75 LVRQSVERLGGSITVESEPGGGTTF 99
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
996-1109 7.39e-09

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: 54.56  E-value: 7.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANREHMpYELILMDCQMPEMDGYQATRAIRNgdagtaHREVS 1075
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDE-FDLVITDVHMPDMDGFEFLELIRL------EMDLP 73
                          90       100       110
                  ....*....|....*....|....*....|....
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKPLNFDSL 1109
Cdd:cd17584    74 VIMMSADGSTSTVMKGLAHGACDYLLKPVSIEDL 107
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
996-1113 8.42e-09

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 57.52  E-value: 8.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQ-AGISF-DIAENGLEAIAKIanREHMPyELILMDCQMPEMDGYQATRAIRNGDAG----- 1068
Cdd:COG3279     4 ILIVDDEPLARERLERLLEKyPDLEVvGEASNGEEALELL--EEHKP-DLVFLDIQMPGLDGFELARQLRELDPPppiif 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 739103821 1069 -TAHREVSIVALTANAMqgdkerclnagmnDYLTKPLNFDSLNKKL 1113
Cdd:COG3279    81 tTAYDEYALEAFEVNAV-------------DYLLKPIDEERLAKAL 113
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
996-1103 9.36e-09

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: 54.30  E-value: 9.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNgdagtaHREVS 1075
Cdd:cd19939     2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDE---QPSLVVLDIMLPGMDGLTVCREVRE------HSHVP 72
                          90       100
                  ....*....|....*....|....*...
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:cd19939    73 ILMLTARTEEMDRVLGLEMGADDYLCKP 100
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
996-1117 1.14e-08

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: 54.28  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDN-KVNQMVAGALlKQAGISFDIAENGLEAIAkiANREHMPyELILMDCQMPEMDGYQATRAIRNGDAgtahrEV 1074
Cdd:cd17615     2 VLVVDDEpNITELLSMAL-RYEGWDVETAADGAEALA--AAREFRP-DAVVLDIMLPDMDGLEVLRRLRADGP-----DV 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 739103821 1075 SIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKLSVWL 1117
Cdd:cd17615    73 PVLFLTAKDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALL 115
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
995-1109 1.52e-08

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 56.47  E-value: 1.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  995 QILLVEDNKVNQMVAGALLKQAGISFDIAENGLEA--IAKIANrehmpYELILMDCQMPEMDGYQATRAIRNGDAGtahr 1072
Cdd:PRK09836    2 KLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGyhLAMTGD-----YDLIILDIMLPDVNGWDIVRMLRSANKG---- 72
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 739103821 1073 eVSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSL 1109
Cdd:PRK09836   73 -MPILLLTALGTIEHRVKGLELGADDYLVKPFAFAEL 108
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
995-1109 1.78e-08

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: 53.71  E-value: 1.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  995 QILLVEDNKVNQMVAGALL-KQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNgDAGTahRE 1073
Cdd:cd17552     3 RILVIDDEEDIREVVQACLeKLAGWEVLTASSGQEGLEKAATE---QPDAILLDVMMPDMDGLATLKKLQA-NPET--QS 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 739103821 1074 VSIVALTANAMQGDKERCLNAGMNDYLTKPlnFDSL 1109
Cdd:cd17552    77 IPVILLTAKAQPSDRQRFASLGVAGVIAKP--FDPL 110
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
996-1116 2.00e-08

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: 53.40  E-value: 2.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGiSFDI---AENGLEAIAKIanREHMPyELILMDCQMPEMDGYQATRAIRNgdagtAHR 1072
Cdd:cd19925     3 VLIVEDDPMVAEIHRAYVEQVP-GFTVigtAGTGEEALKLL--KERQP-DLILLDIYLPDGNGLDLLRELRA-----AGH 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 739103821 1073 EVSIVALT-ANAMQGDKErCLNAGMNDYLTKPLNFDSLNKKLSVW 1116
Cdd:cd19925    74 DVDVIVVTaANDVETVRE-ALRLGVVDYLIKPFTFERLRQRLERY 117
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
996-1081 2.18e-08

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: 53.38  E-value: 2.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNgdagtAHREVS 1075
Cdd:cd17554     3 ILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESE---DPDLVILDIKMPGMDGLETLRKIRE-----KKPDLP 74

                  ....*.
gi 739103821 1076 IVALTA 1081
Cdd:cd17554    75 VIICTA 80
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
726-814 2.46e-08

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: 52.71  E-value: 2.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  726 QIINNLLGNAIKFTkDGEIIVLATVKpiDDAMYLDcsVVDSGVGIKPEKQATLFDSFTQADASTTRRYGGTGLGLAIVKQ 805
Cdd:cd16949     3 RALENVLRNALRYS-PSKILLDISQD--GDQWTIT--ITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAIAER 77

                  ....*....
gi 739103821  806 LCKLMQGDV 814
Cdd:cd16949    78 AIEQHGGKI 86
PRK10766 PRK10766
two-component system response regulator TorR;
996-1104 4.06e-08

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 55.04  E-value: 4.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGlEAIAKIANREHMpyELILMDCQMPEMDGYQATRAIRNgdagtaHREVS 1075
Cdd:PRK10766    5 ILVVEDEPVTRARLQGYFEQEGYTVSEAASG-AGMREIMQNQHV--DLILLDINLPGEDGLMLTRELRS------RSTVG 75
                          90       100
                  ....*....|....*....|....*....
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKPL 1104
Cdd:PRK10766   76 IILVTGRTDSIDRIVGLEMGADDYVTKPL 104
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
585-819 4.68e-08

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 57.39  E-value: 4.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  585 QRRIETEQQLVKAKE----AAEQAVKAKSefLASMSHEIRTPMNGVIGMLNIIK---QTKLDSQQNHHIQLAQSSAESLL 657
Cdd:COG4192   408 EERKRIEKNLRQTQDeliqAAKMAVVGQT--MTSLAHELNQPLNAMSMYLFSAKkalEQENYAQLPTSLDKIEGLIERMD 485
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  658 HIINDILDFSKieagKLDIENISFNVSKLLGDTVESFAIKAEQNNTKLVLDatqiNHEFIVSDPNRIRQIINNLLGNAIK 737
Cdd:COG4192   486 KIIKSLRQFSR----KSDTPLQPVDLRQVIEQAWELVESRAKPQQITLHIP----DDLMVQGDQVLLEQVLVNLLVNALD 557
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  738 FTKDGEIIvlaTVKPIDDAMYLDCSVVDSGVGIKPEKQatLFDSFTqadastTRRYGGTGLGLAIVKQLCKLMQGDVNVV 817
Cdd:COG4192   558 AVATQPQI---SVDLLSNAENLRVAISDNGNGWPLVDK--LFTPFT------TTKEVGLGLGLSICRSIMQQFGGDLYLA 626

                  ..
gi 739103821  818 SS 819
Cdd:COG4192   627 ST 628
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
996-1103 4.94e-08

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: 51.82  E-value: 4.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIanrEHMPYELILMDCQMPEMDGYQATRAIRngdagtAHREVS 1075
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEF---DRAGADIVLLDLMLPGLSGTEVCRQLR------ARSNVP 71
                          90       100
                  ....*....|....*....|....*...
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:cd17621    72 VIMVTAKDSEIDKVVGLELGADDYVTKP 99
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
995-1105 8.72e-08

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 54.42  E-value: 8.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  995 QILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmpYELILMDCQMPEMDGYQATRAIRNgdagtaHREV 1074
Cdd:PRK10955    3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDS----IDLLLLDVMMPKKNGIDTLKELRQ------THQT 72
                          90       100       110
                  ....*....|....*....|....*....|.
gi 739103821 1075 SIVALTANAMQGDKERCLNAGMNDYLTKPLN 1105
Cdd:PRK10955   73 PVIMLTARGSELDRVLGLELGADDYLPKPFN 103
PRK10643 PRK10643
two-component system response regulator PmrA;
995-1123 1.27e-07

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 53.50  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  995 QILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANREhmpYELILMDCQMPEMDGYQATRAIRNgdagtAHREV 1074
Cdd:PRK10643    2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGH---YSLVVLDLGLPDEDGLHLLRRWRQ-----KKYTL 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 739103821 1075 SIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKLSVWLDTHQER 1123
Cdd:PRK10643   74 PVLILTARDTLEDRVAGLDVGADDYLVKPFALEELHARIRALIRRHQGQ 122
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
996-1104 2.30e-07

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: 50.44  E-value: 2.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAI--------AKIANREHMPYELILMDCQMPEMDGYQATRAIRngdA 1067
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALeflgledeEDSSNFNEPKVNMIITDYCMPGMTGYDLLKKVK---E 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 739103821 1068 GTAHREVSIVALTANAMQGDKERCLNAGMNDYLTKPL 1104
Cdd:cd17581    78 SSALKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPV 114
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
996-1104 3.75e-07

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: 49.89  E-value: 3.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAkiANREHMPyELILMDCQMPEMDGYQATRAIRngdagTAHREVS 1075
Cdd:cd17555     3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLE--LFRSEQP-DLVLCDLRMPEMDGLEVLKQIT-----KESPDTP 74
                          90       100
                  ....*....|....*....|....*....
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKPL 1104
Cdd:cd17555    75 VIVVSGAGVMSDAVEALRLGAWDYLTKPI 103
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
994-1120 4.69e-07

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 52.11  E-value: 4.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  994 SQILLVEDNK-VNQMVAGALLKQAGISFDiAENGLEAIAKIANREhmPyELILMDCQMPEMDGYQATRAIRNGDAgtahr 1072
Cdd:PRK10529    2 TNVLIVEDEQaIRRFLRTALEGDGMRVFE-AETLQRGLLEAATRK--P-DLIILDLGLPDGDGIEFIRDLRQWSA----- 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 739103821 1073 eVSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKLSVWLDTH 1120
Cdd:PRK10529   73 -IPVIVLSARSEESDKIAALDAGADDYLSKPFGIGELQARLRVALRRH 119
ompR PRK09468
osmolarity response regulator; Provisional
989-1105 5.26e-07

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 51.90  E-value: 5.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  989 TVNSASQILLVEDNkvnqMVAGALLK----QAGISFDIAENGlEAIAKIANREHmpYELILMDCQMPEMDGYQATRAIRN 1064
Cdd:PRK09468    1 MMQENYKILVVDDD----MRLRALLEryltEQGFQVRSAANA-EQMDRLLTRES--FHLMVLDLMLPGEDGLSICRRLRS 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 739103821 1065 gdagtAHREVSIVALTANAMQGDKERCLNAGMNDYLTKPLN 1105
Cdd:PRK09468   74 -----QNNPTPIIMLTAKGEEVDRIVGLEIGADDYLPKPFN 109
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
725-834 6.64e-07

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: 48.54  E-value: 6.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  725 RQIINNLLGNAIKFTKDGEIIVLATVkpiDDAMYLDCSVVDSGVGIKPEKQATLFDSFTQADASttRRYGGTGLGLAIVK 804
Cdd:cd16923     2 QRVFSNLLSNAIKYSPENTRIYITSF---LTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNS--RNTEGAGLGLSIAK 76
                          90       100       110
                  ....*....|....*....|....*....|
gi 739103821  805 QLCKLMQGDVNvVSSYGEGSTFnfsiKVKL 834
Cdd:cd16923    77 AIIELHGGSAS-AEYDDNHDLF----KVRL 101
PRK10610 PRK10610
chemotaxis protein CheY;
995-1114 6.91e-07

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 49.59  E-value: 6.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  995 QILLVEDNKVNQMVAGALLKQAGI-SFDIAENGLEAIAKIANREhmpYELILMDCQMPEMDGYQATRAIRnGDAGTAhrE 1073
Cdd:PRK10610    7 KFLVVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALNKLQAGG---FGFVISDWNMPNMDGLELLKTIR-ADGAMS--A 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 739103821 1074 VSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKLS 1114
Cdd:PRK10610   81 LPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLN 121
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
996-1103 8.42e-07

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: 48.65  E-value: 8.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANREhmPYELILMDCQMPEMDGYQATRAIRNgdagtAHREVS 1075
Cdd:cd18160     2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGK--DIDIVVTDIVMPEMDGIELAREARK-----IDPDVK 74
                          90       100
                  ....*....|....*....|....*....
gi 739103821 1076 IVALTANAMQGdKERCLNA-GMNDYLTKP 1103
Cdd:cd18160    75 ILFISGGAAAA-PELLSDAvGDNATLKKP 102
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
1004-1062 9.55e-07

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 52.19  E-value: 9.55e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739103821 1004 VNQM-VAGALLKQAgISFD-------IAENGLEAIAKIAnrEHMPyELILMDCQMPEMDGYQATRAI 1062
Cdd:PRK12555    6 VNDSpLAVEALRRA-LARDpdhevvwVATDGAQAVERCA--AQPP-DVILMDLEMPRMDGVEATRRI 68
PRK10816 PRK10816
two-component system response regulator PhoP;
995-1113 1.49e-06

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 50.51  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  995 QILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIAnrEHMPyELILMDCQMPEMDGYQATRAIRNGDAgtahrEV 1074
Cdd:PRK10816    2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLN--EHLP-DIAIVDLGLPDEDGLSLIRRWRSNDV-----SL 73
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 739103821 1075 SIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKL 1113
Cdd:PRK10816   74 PILVLTARESWQDKVEVLSAGADDYVTKPFHIEEVMARM 112
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
996-1109 1.59e-06

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 47.81  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKV-NQMVAGALlKQAGISFDIAEN---GlEAIAKIANrehmpYELILMDCQMPEMDGYQATrairnGDAGTAH 1071
Cdd:cd17573     1 ILLIEDDSTlGKEISKGL-NEKGYQADVAESlkdG-EYYIDIRN-----YDLVLVSDKLPDGNGLSIV-----SRIKEKH 68
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 739103821 1072 REVSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSL 1109
Cdd:cd17573    69 PSIVVIVLSDNPKTEQEIEAFKEGADDYIAKPFDFKVL 106
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
996-1062 1.76e-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: 48.35  E-value: 1.76e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739103821  996 ILLVEDNK-VNQMVAGALLKQAGISF-DIAENGLEAIAKIanREHMPyELILMDCQMPEMDGYQATRAI 1062
Cdd:COG2197     4 VLIVDDHPlVREGLRALLEAEPDIEVvGEAADGEEALELL--EELRP-DVVLLDIRMPGMDGLEALRRL 69
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1021-1103 1.97e-06

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 51.30  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821 1021 DIAENGLEAIAKIAnrEHMPyELILMDCQMPEMDGYQATRAIrngdagTAHREVSIV---ALTAnamQGDKE--RCLNAG 1095
Cdd:PRK00742   33 GTAPDGLEAREKIK--KLNP-DVITLDVEMPVMDGLDALEKI------MRLRPTPVVmvsSLTE---RGAEItlRALELG 100

                  ....*...
gi 739103821 1096 MNDYLTKP 1103
Cdd:PRK00742  101 AVDFVTKP 108
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
996-1113 2.01e-06

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: 47.66  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANREhmPyELILMDCQMPEMDGYQATRAIRNgdagtaHREVS 1075
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFK--P-DLVLLDINLPYFDGFYWCREIRQ------ISNVP 71
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKL 1113
Cdd:cd18159    72 IIFISSRDDNMDQVMAINMGGDDYITKPFDLDVLLAKI 109
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
993-1105 2.43e-06

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 50.10  E-value: 2.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  993 ASQILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIakiaNREHMPY-ELILMDCQMPEMDGYQATRAIRNgDAGTah 1071
Cdd:PRK10161    2 ARRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAV----NQLNEPWpDLILLDWMLPGGSGIQFIKHLKR-ESMT-- 74
                          90       100       110
                  ....*....|....*....|....*....|....
gi 739103821 1072 REVSIVALTANAMQGDKERCLNAGMNDYLTKPLN 1105
Cdd:PRK10161   75 RDIPVVMLTARGEEEDRVRGLETGADDYITKPFS 108
orf27 CHL00148
Ycf27; Reviewed
991-1113 2.49e-06

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 50.10  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  991 NSASQILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIanREHMPyELILMDCQMPEMDGYQATRAIRNgdagta 1070
Cdd:CHL00148    4 NSKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLF--RKEQP-DLVILDVMMPKLDGYGVCQEIRK------ 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 739103821 1071 HREVSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKL 1113
Cdd:CHL00148   75 ESDVPIIMLTALGDVSDRITGLELGADDYVVKPFSPKELEARI 117
PRK15115 PRK15115
response regulator GlrR; Provisional
989-1111 2.60e-06

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 51.38  E-value: 2.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  989 TVNSASQILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIaKIANREhmPYELILMDCQMPEMDGYQATRAIRNGDAG 1068
Cdd:PRK15115    1 MSRKPAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEAL-RVLNRE--KVDLVISDLRMDEMDGMQLFAEIQKVQPG 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 739103821 1069 tahreVSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNK 1111
Cdd:PRK15115   78 -----MPVIILTAHGSIPDAVAATQQGVFSFLTKPVDRDALYK 115
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
723-814 2.76e-06

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: 47.27  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  723 RIRQIINNLLGNAIKFT--KDG--EIIVLATVKPIDD---AMYLDCSVVDSGVGIKPEkqatLFDSFTQADASTTRRygg 795
Cdd:cd16932     6 RLQQVLADFLLNAVRFTpsPGGwvEIKVSPTKKQIGDgvhVIHLEFRITHPGQGLPEE----LVQEMFEENQWTTQE--- 78
                          90
                  ....*....|....*....
gi 739103821  796 tGLGLAIVKQLCKLMQGDV 814
Cdd:cd16932    79 -GLGLSISRKLVKLMNGDV 96
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
720-830 2.83e-06

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


Pssm-ID: 340434 [Multi-domain]  Cd Length: 107  Bit Score: 47.07  E-value: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  720 DPNRIRQIINNLLGNAIKFTKDGEIIVLaTVKpiDDAMYLDCSVVDSGVGIKPEKQATLFDSFTQADasTTRRYGG-TGL 798
Cdd:cd16975     1 DTLLLSRALINIISNACQYAPEGGTVSI-SIY--DEEEYLYFEIWDNGHGFSEQDLKKALELFYRDD--TSRRSGGhYGM 75
                          90       100       110
                  ....*....|....*....|....*....|..
gi 739103821  799 GLAIVKQLCKLMQGDVNVVSSYGEGSTFNFSI 830
Cdd:cd16975    76 GLYIAKNLVEKHGGSLIIENSQKGGAEVTVKI 107
PAS COG2202
PAS domain [Signal transduction mechanisms];
285-416 3.26e-06

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 50.02  E-value: 3.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  285 KMLERQ-YKSERMLETMSSLAKIGAWSFNLETKSMYWSDMTKQIFNYPinKQPEWPTNFNGFKAGFSRDKIRHLYEQALK 363
Cdd:COG2202   126 KRAEEAlRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYS--PEELLGKSLLDLLHPEDRERLLELLRRLLE 203
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 739103821  364 HG-KSFETQIQIINAKGDAVWVLVHCEAEHKNGRCIKLFGSIQDIDARKLIELE 416
Cdd:COG2202   204 GGrESYELELRLKDGDGRWVWVEASAVPLRDGGEVIGVLGIVRDITERKRAEEA 257
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
995-1107 3.41e-06

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


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 47.27  E-value: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  995 QILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANreHMPyELILMDCQMPEMDGYQATRAIRNgdagtAHREV 1074
Cdd:cd19919     2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALAS--SQP-DVLISDIRMPGMDGLALLAQIKQ-----RHPDL 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 739103821 1075 SIVALTANAmqgDKERCLNA---GMNDYLTKPlnFD 1107
Cdd:cd19919    74 PVIIMTAHS---DLDSAVSAyqgGAFEYLPKP--FD 104
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
989-1113 3.54e-06

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 49.26  E-value: 3.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  989 TVNSASQILLVED-----NKVNQMVAGAllkqAGISFdIAE--NGLEAIAKIanREHMPyELILMDCQMPEMDGYQATRA 1061
Cdd:PRK10651    2 SNQEPATILLIDDhpmlrTGVKQLISMA----PDITV-VGEasNGEQGIELA--ESLDP-DLILLDLNMPGMNGLETLDK 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 739103821 1062 IRngDAGTAHRevsIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNKKL 1113
Cdd:PRK10651   74 LR--EKSLSGR---IVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKAL 120
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
726-812 3.96e-06

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: 46.80  E-value: 3.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  726 QIINNLLGNAIKFTKDGEIIVLATVKPIDDAMYLdcSVVDSGVGIKPEKQATLFDSF-TQADASTTrrYG-GTGLGLAIV 803
Cdd:cd16953     3 QVLRNLIGNAISFSPPDTGRITVSAMPTGKMVTI--SVEDEGPGIPQEKLESIFDRFyTERPANEA--FGqHSGLGLSIS 78

                  ....*....
gi 739103821  804 KQLCKLMQG 812
Cdd:cd16953    79 RQIIEAHGG 87
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
994-1103 4.24e-06

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: 46.99  E-value: 4.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  994 SQILLVEDN-KVNQMVAgALLKQAGISFDIAENGLEAIAKIANreHMPyELILMDCQMPEMDGYQATRAIRNGDAGtahr 1072
Cdd:cd17622     1 TRILLVEDDpKLARLIA-DFLESHGFNVVVEHRGDRALEVIAR--EKP-DAVLLDIMLPGIDGLTLCRDLRPKYQG---- 72
                          90       100       110
                  ....*....|....*....|....*....|.
gi 739103821 1073 evSIVALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:cd17622    73 --PILLLTALDSDIDHILGLELGADDYVVKP 101
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
996-1102 6.37e-06

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 46.50  E-value: 6.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNkvnQMVAGALLKQAGISFDI-----AENGLEAIAKIanREHMPyELILMDCQMPEMDGYQATRAIRNgdagtA 1070
Cdd:cd19930     1 VLIAEDQ---EMVRGALAALLELEDDLevvaqASNGQEALRLV--LKHSP-DVAILDIEMPGRTGLEVAAELRE-----E 69
                          90       100       110
                  ....*....|....*....|....*....|..
gi 739103821 1071 HREVSIVALTANAMQGDKERCLNAGMNDYLTK 1102
Cdd:cd19930    70 LPDTKVLIVTTFGRPGYFRRALAAGVDGYVLK 101
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
996-1109 7.42e-06

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: 45.95  E-value: 7.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNK-VNQMVAGaLLKQAGISFDIAENGLEAIAKIANREhmpYELILMDCQMPEMDGYQATRAIRngdagTAHREV 1074
Cdd:cd17550     1 ILIVDDEEdIRESLSG-ILEDEGYEVDTAADGEEALKLIKERR---PDLVLLDIWLPDMDGLELLKEIK-----EKYPDL 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 739103821 1075 SIVALT-----ANAMQGDKErclnaGMNDYLTKPLNFDSL 1109
Cdd:cd17550    72 PVIMISghgtiETAVKATKL-----GAYDFIEKPLSLDRL 106
PRK11061 PRK11061
phosphoenolpyruvate--protein phosphotransferase;
440-576 7.66e-06

phosphoenolpyruvate--protein phosphotransferase;


Pssm-ID: 182937 [Multi-domain]  Cd Length: 748  Bit Score: 49.99  E-value: 7.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  440 NLNLSKHVIVQAICHALNVDRASIWLFSDDRQSLNTFAIHDQSNPQfSDPISLqqievqnyfdAINNNAV---------I 510
Cdd:PRK11061   17 RLNEALDILVTETCLAMDTEVCSVYLADHDRRCYYLMATRGLKKPR-GRTVTL----------AFDEGIVglvgrlaepI 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739103821  511 NASDAQQHPFTKdlYTDYLDKFDIRSLLTVIIPTGSKTMGVVCAEKcHSRQQWSKNEESFLIAVAA 576
Cdd:PRK11061   86 NLADAQKHPSFK--YIPSVKEERFRAFLGVPIIYRRQLLGVLVVQQ-RELRQFDESEESFLVTLAT 148
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
991-1103 9.59e-06

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 48.14  E-value: 9.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  991 NSASQILLVEDN-KVNQMVAGaLLKQAGISFDIAENGLEAIAKIanREHmPYELILMDCQMPEMDGYQATRAIRNgdagt 1069
Cdd:PRK10710    8 ENTPRILIVEDEpKLGQLLID-YLQAASYATTLLSHGDEVLPYV--RQT-PPDLILLDLMLPGTDGLTLCREIRR----- 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 739103821 1070 aHREVSIVALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:PRK10710   79 -FSDIPIVMVTAKIEEIDRLLGLEIGADDYICKP 111
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
720-826 1.10e-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: 46.09  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  720 DPNRIRQIINNLLGNAIKFTkDGEIIVlaTVKPIDDAMYLdcSVVDSGVGIKPEKQATLFDSFTQADASTTrrygGTGLG 799
Cdd:cd16954    34 ERNDLMELLGNLLDNACKWC-LEFVEV--TARQTDGGLHL--IVDDDGPGVPESQRSKIFQRGQRLDEQRP----GQGLG 104
                          90       100
                  ....*....|....*....|....*..
gi 739103821  800 LAIVKQLCKLMQGDVNVVSSYGEGSTF 826
Cdd:cd16954   105 LAIAKEIVEQYGGELSLSDSPLGGARF 131
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
720-831 1.19e-05

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: 45.22  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  720 DPNRIRQIINNLLGNA---IKFTKDGEIIVLATVKPiDDAMYLDCSVVDSGVGIKPEKQATLFDSFTqadastTRRYGGT 796
Cdd:cd16944     1 DTTQISQVLTNILKNAaeaIEGRPSDVGEVRIRVEA-DQDGRIVLIVCDNGKGFPREMRHRATEPYV------TTRPKGT 73
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 739103821  797 GLGLAIVKQLCKLMQGDVNVVSSYGEGSTFNFSIK 831
Cdd:cd16944    74 GLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
PRK10336 PRK10336
two-component system response regulator QseB;
995-1104 1.90e-05

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 47.20  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  995 QILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANrehMPYELILMDCQMPEMDGYQATRAIRngDAGtahREV 1074
Cdd:PRK10336    2 RILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYS---APYDAVILDLTLPGMDGRDILREWR--EKG---QRE 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 739103821 1075 SIVALTANAMQGDKERCLNAGMNDYLTKPL 1104
Cdd:PRK10336   74 PVLILTARDALAERVEGLRLGADDYLCKPF 103
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
616-826 2.19e-05

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 48.37  E-value: 2.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  616 SHEIRTPMNGVIGMLNIIKQTKLdsqQNHHIQLAQSSAESLLHIINDILdfSKIEAGkldienisFNVSKLlgdtveSFA 695
Cdd:PRK11086  347 SHEFMNKLHVILGLLHLKSYDQL---EDYILKTANNYQEEIGSLLGKIK--SPVIAG--------FLLGKI------SRA 407
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  696 ikAEQNNTKLVLDATQI--------NHEFIVsdpnrirqIINNLLGN---AIKFTKDGEIIVLATVKPIddamYLDCSVV 764
Cdd:PRK11086  408 --RELGITLIISEDSQLpdsgdedqVHELIT--------ILGNLIENaleAVGGEEGGEISVSLHYRNG----WLHCEVS 473
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739103821  765 DSGVGIKPEKQATLFDSftqaDASTtrRYGGTGLGLAIVKQLCKLMQGDVNVVSSYGEGSTF 826
Cdd:PRK11086  474 DDGPGIAPDEIDAIFDK----GYST--KGSNRGVGLYLVKQSVENLGGSIAVESEPGVGTQF 529
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
996-1109 2.24e-05

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: 46.06  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIanrEHMPYELILMDCQMPEMDGYQATRAIRNGDAGTAhrevs 1075
Cdd:COG4567     7 LLLVDDDEAFARVLARALERRGFEVTTAASVEEALALL---EQAPPDYAVLDLRLGDGSGLDLIEALRERDPDAR----- 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 739103821 1076 IVALT-----ANAMQGDKerclnAGMNDYLTKPLNFDSL 1109
Cdd:COG4567    79 IVVLTgyasiATAVEAIK-----LGADDYLAKPADADDL 112
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
1023-1114 2.74e-05

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: 44.45  E-value: 2.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821 1023 AENGLEAIAKIanREHMPyELILMDCQMPEMDGYQATRAIRNGDA------GTAHREVSIVALTANAMqgdkerclnagm 1096
Cdd:cd17532    30 AENGEEALEAI--EELKP-DVVFLDIQMPGLDGLELAKKLSKLAKpplivfVTAYDEYAVEAFELNAV------------ 94
                          90
                  ....*....|....*...
gi 739103821 1097 nDYLTKPLNFDSLNKKLS 1114
Cdd:cd17532    95 -DYLLKPFSEERLAEALA 111
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
996-1102 3.29e-05

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: 44.71  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNK-VNQMVAGALLKQAGISFDIAENGLEAIAkIANREHmPyELILMDCQMPEMDGYQATRAIRngdAGTAHREV 1074
Cdd:cd17575     3 VLLVDDQAiIGEAVRRALADEEDIDFHYCSDPTEAIE-VASQIK-P-TVILQDLVMPGVDGLTLVRFFR---ANPATRDI 76
                          90       100
                  ....*....|....*....|....*...
gi 739103821 1075 SIVALTANAMQGDKERCLNAGMNDYLTK 1102
Cdd:cd17575    77 PIIVLSTKEEPEVKSEAFALGANDYLVK 104
PRK10337 PRK10337
sensor protein QseC; Provisional
611-811 3.39e-05

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 47.72  E-value: 3.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  611 FLASMSHEIRTPMNGvigmLNI---IKQTKLDSQQNHHIQLAQssaeslLH--------IINDILDFSKIEAGKL--DIE 677
Cdd:PRK10337  240 FTSDAAHELRSPLAA----LKVqteVAQLSDDDPQARKKALLQ------LHagidratrLVDQLLTLSRLDSLDNlqDVA 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  678 NISFNvsKLLGDTVESFAIKAEQNNTKLVLDAtqinhefivSDPNRIRQ--------IINNLLGNAIKFTKDGeiivlAT 749
Cdd:PRK10337  310 EIPLE--DLLQSAVMDIYHTAQQAGIDVRLTL---------NAHPVIRTgqplllslLVRNLLDNAIRYSPQG-----SV 373
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739103821  750 VKPIDDAMYLdcSVVDSGVGIKPEKQATLFDSFTQ---ADASttrrygGTGLGLAIVKQLCKL--MQ 811
Cdd:PRK10337  374 VDVTLNARNF--TVRDNGPGVTPEALARIGERFYRppgQEAT------GSGLGLSIVRRIAKLhgMN 432
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
996-1103 4.63e-05

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: 43.54  E-value: 4.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIaKIANREHMPYELILMDCQMPEMDGYQATRAIRNGDagtAHREVS 1075
Cdd:cd17582     1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAW-DVLEDEQNEIDLILTEVDLPVSSGFKLLSYIMRHK---ICKNIP 76
                          90       100
                  ....*....|....*....|....*...
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:cd17582    77 VIMMSSQDSVGVVFKCLSKGAADYLVKP 104
PRK13557 PRK13557
histidine kinase; Provisional
730-825 4.99e-05

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 47.36  E-value: 4.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  730 NLLGNAIKFTKDGEIIVLAT----VKPIDDAMYLDC--------SVVDSGVGIKPEKQATLFDSFTqadasTTRRYG-GT 796
Cdd:PRK13557  284 NVLINARDAMPEGGRVTIRTrnveIEDEDLAMYHGLppgryvsiAVTDTGSGMPPEILARVMDPFF-----TTKEEGkGT 358
                          90       100
                  ....*....|....*....|....*....
gi 739103821  797 GLGLAIVKQLCKLMQGDVNVVSSYGEGST 825
Cdd:PRK13557  359 GLGLSMVYGFAKQSGGAVRIYSEVGEGTT 387
PAS COG2202
PAS domain [Signal transduction mechanisms];
285-456 5.43e-05

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 46.17  E-value: 5.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  285 KMLERQYKSERMLETMSSLAKIGAWSFNLETKSMYWSDMTKQIFNYP----INKqpewptNFNGFKAGFSRDKIRHLYEQ 360
Cdd:COG2202     1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSaeelLGK------TLRDLLPPEDDDEFLELLRA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  361 ALKHGKSFETQIQIINAKGDAVWVLVHCEAEH-KNGRCIKLFGSIQDIDARKLIElenQKIALHNEILASL--TVNDAVL 437
Cdd:COG2202    75 ALAGGGVWRGELRNRRKDGSLFWVELSISPVRdEDGEITGFVGIARDITERKRAE---EALRESEERLRLLveNAPDGIF 151
                         170
                  ....*....|....*....
gi 739103821  438 TGNLNLSKHVIVQAICHAL 456
Cdd:COG2202   152 VLDLDGRILYVNPAAEELL 170
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
740-827 8.79e-05

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: 43.14  E-value: 8.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  740 KDGEIIVLATVKPIDDAM-----------YLDCSVVDSGVGIKPEKQATLFDSFTqadasTTRRYG-GTGLGLAIVKQLC 807
Cdd:cd16919    18 EGGRLTIETSNQRVDADYalnyrdlipgnYVCLEVSDTGSGMPAEVLRRAFEPFF-----TTKEVGkGTGLGLSMVYGFV 92
                          90       100
                  ....*....|....*....|
gi 739103821  808 KLMQGDVNVVSSYGEGSTFN 827
Cdd:cd16919    93 KQSGGHLRIYSEPGVGTTVR 112
PLN03029 PLN03029
type-a response regulator protein; Provisional
987-1111 2.47e-04

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 43.87  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  987 TYTVNSASQILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIA-----------------NREHMPYELILMDCQ 1049
Cdd:PLN03029    2 GITTESQFHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGlheddrsnpdtpsvspnSHQEVEVNLIITDYC 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739103821 1050 MPEMDGYQATRAIRNGdagTAHREVSIVALTANAMQGDKERCLNAGMNDYLTKPLNFDSLNK 1111
Cdd:PLN03029   82 MPGMTGYDLLKKIKES---SSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDLNR 140
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
318-404 3.58e-04

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


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 40.40  E-value: 3.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821   318 MYWSDMTKQIFNYPinkQPEWPTNFNGFKAGFS---RDKIRHLYEQALKHGKSFETQIQIINAKGDAVWVLVHCEAEH-K 393
Cdd:pfam08447    2 IYWSPRFEEILGYT---PEELLGKGESWLDLVHpddRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRdE 78
                           90
                   ....*....|.
gi 739103821   394 NGRCIKLFGSI 404
Cdd:pfam08447   79 NGKPVRVIGVA 89
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
724-828 4.34e-04

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: 40.90  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  724 IRQIINNLLGNAIKFTKDGEI--IVLATVKPIDDAMYldcSVVDSGVGIKPEKQATLFDSFTqadasTTRRYG-GTGLGL 800
Cdd:cd16976     1 IQQVLMNLLQNALDAMGKVENprIRIAARRLGGRLVL---VVRDNGPGIAEEHLSRVFDPFF-----TTKPVGkGTGLGL 72
                          90       100
                  ....*....|....*....|....*...
gi 739103821  801 AIVKQLCKLMQGDVNVVSSYGEGSTFNF 828
Cdd:cd16976    73 SISYGIVEEHGGRLSVANEEGAGARFTF 100
PRK11173 PRK11173
two-component response regulator; Provisional
995-1105 4.59e-04

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 43.08  E-value: 4.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  995 QILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANREhmpYELILMDCQMPEMDGYQATRAIRngdagtAHREV 1074
Cdd:PRK11173    5 HILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSEND---INLVIMDINLPGKNGLLLARELR------EQANV 75
                          90       100       110
                  ....*....|....*....|....*....|.
gi 739103821 1075 SIVALTANAMQGDKERCLNAGMNDYLTKPLN 1105
Cdd:PRK11173   76 ALMFLTGRDNEVDKILGLEIGADDYITKPFN 106
PRK10693 PRK10693
two-component system response regulator RssB;
1023-1113 6.23e-04

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 43.06  E-value: 6.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821 1023 AENGLEAIAKIanrEHMPYELILMDCQMPEMDGYQATRAIRNgdagtAHREVSIVALTANAMQGDKERCLNAGMNDYLTK 1102
Cdd:PRK10693    3 AANGVDALELL---GGFTPDLIICDLAMPRMNGIEFVEHLRN-----RGDQTPVLVISATENMADIAKALRLGVQDVLLK 74
                          90
                  ....*....|..
gi 739103821 1103 PL-NFDSLNKKL 1113
Cdd:PRK10693   75 PVkDLNRLREMV 86
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
996-1103 6.47e-04

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: 40.12  E-value: 6.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRngdagtAHREVS 1075
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNAR---PPDLAILDIKMPRMDGMELLQRLR------QKSTLP 71
                          90       100
                  ....*....|....*....|....*...
gi 739103821 1076 IVALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:cd19936    72 VIFLTSKDDEIDEVFGLRMGADDYITKP 99
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
996-1103 7.52e-04

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 40.51  E-value: 7.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANREHmpyELILMDCQMPEMDGYQATRAIRngdagtAHREVS 1075
Cdd:cd17594     2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRV---DLVLLDLRLGQESGLDLLRTIR------ARSDVP 72
                          90       100
                  ....*....|....*....|....*....
gi 739103821 1076 IVALTANAMQ-GDKERCLNAGMNDYLTKP 1103
Cdd:cd17594    73 IIIISGDRRDeIDRVVGLELGADDYLAKP 101
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
996-1109 8.02e-04

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


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 40.12  E-value: 8.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKV-NQMVAGALLKQaGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNGDAgtahrEV 1074
Cdd:cd17563     3 LLLVDDDEVfAERLARALERR-GFEVETAHSVEEALALAREE---KPDYAVLDLRLGGDSGLDLIPPLRALQP-----DA 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 739103821 1075 SIVALT-----ANAMQGDKerclnAGMNDYLTKPLNFDSL 1109
Cdd:cd17563    74 RIVVLTgyasiATAVEAIK-----LGADDYLAKPADADEI 108
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
996-1109 8.99e-04

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: 40.55  E-value: 8.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIanREHMPyELILMDCQMPEMDGYQATRAIRNGDAG------T 1069
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAAL--SPDFP-GVVISDIRMPGMDGLELLAQIRELDPDlpviliT 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 739103821 1070 AHREVSivaLTANAMQgdkerclnAGMNDYLTKPLNFDSL 1109
Cdd:cd17549    78 GHGDVP---MAVEAMR--------AGAYDFLEKPFDPERL 106
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
718-833 1.35e-03

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 42.70  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  718 VSDPNRIRQIinnLLGNAIKF-----TKDGEIIVLATVKpiDDAMYLdcSVVDSGVGIKPEKQATLFDSFTQADasttrr 792
Cdd:COG2972   334 LLIPKLILQP---LVENAIEHgiepkEGGGTIRISIRKE--GDRLVI--TVEDNGVGMPEEKLEKLLEELSSKG------ 400
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 739103821  793 yGGTGLGLAIVKQLCKLMQGD---VNVVSSYGEGSTFNFSIKVK 833
Cdd:COG2972   401 -EGRGIGLRNVRERLKLYYGEeygLEIESEPGEGTTVTIRIPLE 443
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
723-831 2.54e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Erythrobacter litoralis blue light-activated histidine kinase 2; This domain family includes the histidine kinase-like ATPase (HATPase) domain of blue light-activated histidine kinase 2 of Erythrobacter litoralis (EL346). Signaling commonly occurs within HK dimers, however EL346 functions as a monomer. Also included in this family are the HATPase domains of ethanolamine utilization sensory transduction histidine kinase (EutW), whereby regulation of ethanolamine, a carbon and nitrogen source for gut bacteria, results in autophosphorylation and subsequent phosphoryl transfer to a response regulator (EutV) containing an RNA-binding domain. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory PAS sensor domain, while some have an N-terminal histidine kinase domain.


Pssm-ID: 340427 [Multi-domain]  Cd Length: 131  Bit Score: 39.32  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  723 RIRQIINNLLGNAIKFT-KDGEIIVLaTVKPIDDAMYLDCSVVDSGVGIkPEKqatlFDSFTQADasttrryggtgLGLA 801
Cdd:cd16951    39 AIGLVVNELLQNALKHAfSDREGGTI-TIRSVVDGDYLRITVIDDGVGL-PQD----EDWPNKGS-----------LGLQ 101
                          90       100       110
                  ....*....|....*....|....*....|
gi 739103821  802 IVKQLCKLMQGDVNVVSSYGEGSTFNFSIK 831
Cdd:cd16951   102 IVRSLVEGELKAFLEVQSAENGTRVNIDIP 131
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
996-1121 3.06e-03

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


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 39.24  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDN-KVNQMVAGALLKQAGISFDI-----AENGLEAIAKIANReHMPYELILMDCQMPEMDGYQ-ATRAIrngdag 1068
Cdd:cd17595     3 ILTVDDDpQVLRAVARDLRRQYGKDYRVlradsGAEALDALKELKLR-GEAVALFLVDQRMPEMDGVEfLEKAM------ 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739103821 1069 TAHREVSIVALTANAmqgDKERCLNAgMND-----YLTKPLN------FDSLNKKLSVWLDTHQ 1121
Cdd:cd17595    76 ELFPEAKRVLLTAYA---DTDAAIRA-INDvqldyYLLKPWDppeeklYPVLDDLLDDWQASYR 135
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
996-1103 3.13e-03

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


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 38.36  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNK-VNQMVAGALLKQAGISF-DIAENGLEAIAKIANREhmPyELILMDCQMPEMDGYQATRAIRNGDAGTahrE 1073
Cdd:cd17561     4 VLIADDNReFVQLLEEYLNSQPDMEVvGVAHNGQEALELIEEKE--P-DVLLLDIIMPHLDGIGVLEKLRRMRLEK---R 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 739103821 1074 VSIVALTANAMQGDKERCLNAGMNDYLTKP 1103
Cdd:cd17561    78 PKIIMLTAFGQEDITQRAVELGASYYILKP 107
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
718-819 3.28e-03

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 41.54  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  718 VSDPNRIRQIINNLLGNAIKFTKDgeiIVLATVKPIDDAMYLdcSVVDSGVGIKPEKQATLFDSFTQADasTTRRygGTG 797
Cdd:PRK10815  373 VGEKNDFMEVMGNVLDNACKYCLE---FVEISARQTDEHLHI--VVEDDGPGIPESKRELIFDRGQRAD--TLRP--GQG 443
                          90       100
                  ....*....|....*....|..
gi 739103821  798 LGLAIVKQLCKLMQGDVNVVSS 819
Cdd:PRK10815  444 LGLSVAREITEQYEGKISAGDS 465
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
996-1104 4.00e-03

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


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 38.45  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQ-MVAGALLKQAGIsfDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNGDAGtahREV 1074
Cdd:cd17539     1 VLLVDDRPSSAeRIAAMLSSEHEV--VVEADPDEALFRAAEG---PFDLVIVSLALEDFDGLRLCSQLRSLERT---RQL 72
                          90       100       110
                  ....*....|....*....|....*....|...
gi 739103821 1075 SIVALtanAMQGDKERCLNA---GMNDYLTKPL 1104
Cdd:cd17539    73 PILAV---ADPGDRGRLIRAleiGVNDYLVRPI 102
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
996-1103 8.85e-03

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


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 37.38  E-value: 8.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821  996 ILLVEDNKVNQMVAGALLKQAGISFDIAENGLEAIAKIANRehmPYELILMDCQMPEMDGYQATRAIRNGDAGTahreVS 1075
Cdd:cd17569     3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQE---PVDVVISDQRMPGMDGAELLKRVRERYPDT----VR 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 739103821 1076 IVaLTANAmqgDKERCLNAgMND-----YLTKP 1103
Cdd:cd17569    76 IL-LTGYA---DLDAAIEA-INEgeiyrFLTKP 103
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
1023-1113 8.96e-03

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: 37.33  E-value: 8.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739103821 1023 AENGLEAIaKIANRehMPYELILMDCQMPEMDGYQATRAIRngDAGTAHRevsIVALTANAMQGDKERCLNAGMNDYLTK 1102
Cdd:cd19931    30 ASSGEEGI-ELAER--LDPDLILLDLNMKGMSGLDTLKALR--EEGVSAR---IVILTVSDAEDDVVTALRAGADGYLLK 101
                          90
                  ....*....|.
gi 739103821 1103 PLNFDSLNKKL 1113
Cdd:cd19931   102 DMEPEDLLEAL 112
 
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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