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Conserved domains on  [gi|1190634387|gb|OSZ91472|]
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hybrid sensor histidine kinase/response regulator [Yersinia pestis subsp. microtus bv. Caucasica]

Protein Classification

hybrid sensor histidine kinase/response regulator( domain architecture ID 11487749)

hybrid sensor histidine kinase/response regulator, part of a two-component regulatory system, receives the signal from the sensor partner in a two-component system through its receiver (REC) domain and functions as a protein kinase that phosphorylates a target protein in response to various signals; may contain a HAMP domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK15347 PRK15347
two component system sensor kinase;
1-924 0e+00

two component system sensor kinase;


:

Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 1558.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387   1 MGKASSLVTRLTLLMGVTLTVIWLILIATTAFFSYENTRQILINELTHMASMRADLSNHQFEGAERDAASLISRReslQS 80
Cdd:PRK15347    3 MTWQTSLVIRLTLLLGLTLIIIWLLSVATTAYFSFEQTRQHIIEELSHLSSMRADLSNQRFEGAERDAKNLMYRC---QS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387  81 TSPLPEISIKHYDSYYIPFNLDSCNINQH-KNDLWIIQAYGTAGQTYYLDSFIIKQKEGIVLFPPQKSSSDYLNQRRKDL 159
Cdd:PRK15347   80 ATEIDHNDIKPEVSRYIPFNPKNCDPTLNgKKDRWFIQAYGIAGQSYYLDSFILKPKEGISLFSPDKSSSDYLTLRPLEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 160 LLLPKFPTHNNIYWGAPTYTPQGGWHVSVAVCDKVGTLAGFALKLNDLIAYNHPVEQRDINLLLDKNGELLPISQQATSS 239
Cdd:PRK15347  160 KQLPLQPTHNGIYWGKPEYIPGGGWHVSVAVADKQGVLVGFTVKLNDLISYNHPVLDDDINLWLDQNGELLPFSTIPLSS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 240 NQLHEILNQLKNSKLHDGWQQTPDYLVLRTQLKGPGWQQLVIYPRMGFAWEALKPALYQLPFALAILLLLTSVLSLLLRY 319
Cdd:PRK15347  240 NQLQKILNQLENVKLHDGWQQIPDYLVLRTQLKGPGWQQVTLYPRRNLANEALKPALQQLPFALLILVLLTSVLFLLLRR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 320 YLAIPLWNFINIIGATGPQAMEPRLPINRIDELGHIARAYNNLLDTLNEQYDTLEMKVKERTLALAEAKRAAEQANRRKS 399
Cdd:PRK15347  320 YLAKPLWRFVDIINKTGPAALEPRLPENRLDELGSIAKAYNQLLDTLNEQYDTLENKVAERTQALAEAKQRAEQANKRKS 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 400 DHLTTISHEIRTPLNGALGAVELLQNTPLDAGQMRLAETAHQCSLSLLAIINNLLDFSRIESGQMTLSLEKTALLPLLDQ 479
Cdd:PRK15347  400 EHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPLLDQ 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 480 AMLTIHSQALSKSLALSTFISANIPLELELDTLRLRQILVNLLGNAVKFTPQGRIQLRVRRQNQTLCFTVEDTGCGIDVQ 559
Cdd:PRK15347  480 AMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGGIRLRVKRHEQQLCFTVEDTGCGIDIQ 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 560 HQQTIFQPFMQTSDHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLPFNAITPPMPFHGELFAPQRLHAQLSA 639
Cdd:PRK15347  560 QQQQIFTPFYQADTHSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPLNEYAPPEPLKGELSAPLALHRQLSA 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 640 WGMTCQPelaNQPSRHFVDNALCYLPGRLYAKLKQYLQGAETEALKSLPLQPWQMHILLVDDSETNRDITGMMLQQLGHQ 719
Cdd:PRK15347  640 WGITCQP---GHQNPALLDPELAYLPGRLYDLLQQIIQGAPNEPVINLPLQPWQLQILLVDDVETNRDIIGMMLVELGQQ 716
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 720 VTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANIDSHCMITALSANASPDEQIKTSQAGMNHYLSKP 799
Cdd:PRK15347  717 VTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNLDPDCMIVALTANAAPEEIHRCKKAGMNHYLTKP 796
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 800 VTLGQLAEMLDLTAQFQLERGVDLSPQLSEPQPLLDLADSALSLKLYQSLQVLIQQAKDAIENLPVLSHTLHTIKGCAGQ 879
Cdd:PRK15347  797 VTLAQLARALELAAEYQLLRGIELSPQDSSCSPLLDTDDMALNSKLYQSLLLLLAQIEQAVENQEVLSQLLHTLKGCAGQ 876
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....*
gi 1190634387 880 AGLIELQDAVIQLEHALDTHETLTQQEIIQLDEIIHVLLQPPTTC 924
Cdd:PRK15347  877 AGLTELQCAVIDLENALETGEILSLEELTDLRELIHALFKNPTTC 921
 
Name Accession Description Interval E-value
PRK15347 PRK15347
two component system sensor kinase;
1-924 0e+00

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 1558.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387   1 MGKASSLVTRLTLLMGVTLTVIWLILIATTAFFSYENTRQILINELTHMASMRADLSNHQFEGAERDAASLISRReslQS 80
Cdd:PRK15347    3 MTWQTSLVIRLTLLLGLTLIIIWLLSVATTAYFSFEQTRQHIIEELSHLSSMRADLSNQRFEGAERDAKNLMYRC---QS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387  81 TSPLPEISIKHYDSYYIPFNLDSCNINQH-KNDLWIIQAYGTAGQTYYLDSFIIKQKEGIVLFPPQKSSSDYLNQRRKDL 159
Cdd:PRK15347   80 ATEIDHNDIKPEVSRYIPFNPKNCDPTLNgKKDRWFIQAYGIAGQSYYLDSFILKPKEGISLFSPDKSSSDYLTLRPLEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 160 LLLPKFPTHNNIYWGAPTYTPQGGWHVSVAVCDKVGTLAGFALKLNDLIAYNHPVEQRDINLLLDKNGELLPISQQATSS 239
Cdd:PRK15347  160 KQLPLQPTHNGIYWGKPEYIPGGGWHVSVAVADKQGVLVGFTVKLNDLISYNHPVLDDDINLWLDQNGELLPFSTIPLSS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 240 NQLHEILNQLKNSKLHDGWQQTPDYLVLRTQLKGPGWQQLVIYPRMGFAWEALKPALYQLPFALAILLLLTSVLSLLLRY 319
Cdd:PRK15347  240 NQLQKILNQLENVKLHDGWQQIPDYLVLRTQLKGPGWQQVTLYPRRNLANEALKPALQQLPFALLILVLLTSVLFLLLRR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 320 YLAIPLWNFINIIGATGPQAMEPRLPINRIDELGHIARAYNNLLDTLNEQYDTLEMKVKERTLALAEAKRAAEQANRRKS 399
Cdd:PRK15347  320 YLAKPLWRFVDIINKTGPAALEPRLPENRLDELGSIAKAYNQLLDTLNEQYDTLENKVAERTQALAEAKQRAEQANKRKS 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 400 DHLTTISHEIRTPLNGALGAVELLQNTPLDAGQMRLAETAHQCSLSLLAIINNLLDFSRIESGQMTLSLEKTALLPLLDQ 479
Cdd:PRK15347  400 EHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPLLDQ 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 480 AMLTIHSQALSKSLALSTFISANIPLELELDTLRLRQILVNLLGNAVKFTPQGRIQLRVRRQNQTLCFTVEDTGCGIDVQ 559
Cdd:PRK15347  480 AMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGGIRLRVKRHEQQLCFTVEDTGCGIDIQ 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 560 HQQTIFQPFMQTSDHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLPFNAITPPMPFHGELFAPQRLHAQLSA 639
Cdd:PRK15347  560 QQQQIFTPFYQADTHSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPLNEYAPPEPLKGELSAPLALHRQLSA 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 640 WGMTCQPelaNQPSRHFVDNALCYLPGRLYAKLKQYLQGAETEALKSLPLQPWQMHILLVDDSETNRDITGMMLQQLGHQ 719
Cdd:PRK15347  640 WGITCQP---GHQNPALLDPELAYLPGRLYDLLQQIIQGAPNEPVINLPLQPWQLQILLVDDVETNRDIIGMMLVELGQQ 716
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 720 VTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANIDSHCMITALSANASPDEQIKTSQAGMNHYLSKP 799
Cdd:PRK15347  717 VTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNLDPDCMIVALTANAAPEEIHRCKKAGMNHYLTKP 796
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 800 VTLGQLAEMLDLTAQFQLERGVDLSPQLSEPQPLLDLADSALSLKLYQSLQVLIQQAKDAIENLPVLSHTLHTIKGCAGQ 879
Cdd:PRK15347  797 VTLAQLARALELAAEYQLLRGIELSPQDSSCSPLLDTDDMALNSKLYQSLLLLLAQIEQAVENQEVLSQLLHTLKGCAGQ 876
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....*
gi 1190634387 880 AGLIELQDAVIQLEHALDTHETLTQQEIIQLDEIIHVLLQPPTTC 924
Cdd:PRK15347  877 AGLTELQCAVIDLENALETGEILSLEELTDLRELIHALFKNPTTC 921
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
350-927 4.22e-91

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: 310.94  E-value: 4.22e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 350 DELGHIARAYNNLLDT-----------------LNEQYDTLEMKVKERTLALAE--------------AKRAAEQANRRK 398
Cdd:TIGR02956 385 DELAHMGRAIEAFRDTaahnlklqaderqvaqeLQEHKESLEQLVAQRTQELAEtnerlnaevknhakARAEAEEANRAK 464
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 399 SDHLTTISHEIRTPLNGALGAVELLQNTPLDAGQMRLAETAHQCSLSLLAIINNLLDFSRIESGQMTLSLEKTALLPLLD 478
Cdd:TIGR02956 465 SAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLD 544
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 479 QAMLTIHSQALSKSLALSTFISANIPLELELDTLRLRQILVNLLGNAVKFTPQGRIQLRVRRQNQ-TLCFTVEDTGCGID 557
Cdd:TIGR02956 545 DVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDsSLLFEVEDTGCGIA 624
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 558 VQHQQTIFQPFMQTSDHEQ--GTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLPFNaitppmpfhgelfapqrlha 635
Cdd:TIGR02956 625 EEEQATLFDAFTQADGRRRsgGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLT-------------------- 684
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 636 qlsawgmTCQPElanqpsrhfvdnalcylpgrlyaklkqylQGAETEALKSLPLQpwqmHILLVDDSETNRDITGMMLQQ 715
Cdd:TIGR02956 685 -------RGKPA-----------------------------EDSATLTVIDLPPQ----RVLLVEDNEVNQMVAQGFLTR 724
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 716 LGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANIDSHCMItALSANASPDEQIKTSQAGMNHY 795
Cdd:TIGR02956 725 LGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIYGAKNEVKFI-AFSAHVFNEDVAQYLAAGFDGF 803
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 796 LSKPVTLGQL----------------AEMLDLTAQFQLERGVDLSPQLSEPQP------LLD---LADSALSL---KLYQ 847
Cdd:TIGR02956 804 LAKPVVEEQLtamiavilaggksnteAPVLSASPSFDSASVIENAQADDIPESnqasefLLDeeqLQQDIEVLgveKVRQ 883
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 848 SLQVLIQQAKDAIENLPV---------LSHTLHTIKGCAGQAGLIELQdaviQLEHALDTHETLTQQEIIQLDEIIHVLL 918
Cdd:TIGR02956 884 LVALFKTSSAEQLEELSAaravdddaqIKKLAHKLKGSAGSLGLTQLT----QLCQQLEKQGKTGALELSDIDEIKQAWQ 959

                  ....*....
gi 1190634387 919 QPPTTCEST 927
Cdd:TIGR02956 960 ASKTALDQW 968
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
291-615 1.98e-75

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 250.21  E-value: 1.98e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 291 ALKPALYQLPFALAILLLLTSVLSLLLRYYLAIPLWNFINIIGATGPQAMEPRLPINRIDELGHIARAYN-NLLDTLNEQ 369
Cdd:COG0642     2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLlLLLLLLLLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 370 YDTLEMKVKERTLALAEAKRAAEQANRRKSDHLTTISHEIRTPLNGALGAVELLQNTPlDAGQMRLAETAHQCSLSLLAI 449
Cdd:COG0642    82 LLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEEL-DEEQREYLETILRSADRLLRL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 450 INNLLDFSRIESGQMTLSLEKTALLPLLDQAMLTIHSQALSKSLALSTFISANIPLeLELDTLRLRQILVNLLGNAVKFT 529
Cdd:COG0642   161 INDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPT-VRGDPDRLRQVLLNLLSNAIKYT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 530 PQG-RIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQT--SDHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGS 606
Cdd:COG0642   240 PEGgTVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTdpSRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGT 319

                  ....*....
gi 1190634387 607 CFSLCLPFN 615
Cdd:COG0642   320 TFTVTLPLA 328
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
514-614 4.69e-45

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: 157.65  E-value: 4.69e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 514 LRQILVNLLGNAVKFTPQGRIQLRVRRQNQT-----LCFTVEDTGCGIDVQHQQTIFQPFMQTSDH----EQGTGLGLAI 584
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEedgvqLRFSVEDTGIGIPEEQQARLFEPFSQADSSttrkYGGTGLGLAI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1190634387 585 ADNLAKMMGGHLTVFSEPGQGSCFSLCLPF 614
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
510-614 2.77e-37

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 135.47  E-value: 2.77e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387  510 DTLRLRQILVNLLGNAVKFTP-QGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQ---GTGLGLAIA 585
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTPeGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRkigGTGLGLSIV 81
                           90       100
                   ....*....|....*....|....*....
gi 1190634387  586 DNLAKMMGGHLTVFSEPGQGSCFSLCLPF 614
Cdd:smart00387  82 KKLVELHGGEISVESEPGGGTTFTITLPL 110
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
510-614 3.98e-33

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: 123.63  E-value: 3.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 510 DTLRLRQILVNLLGNAVKFTPQ-GRIQLRVRRQNQtLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQ-GTGLGLAIADN 587
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAAKaGEITVTLSEGGE-LTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGgGTGLGLSIVRK 80
                          90       100
                  ....*....|....*....|....*..
gi 1190634387 588 LAKMMGGHLTVFSEPGQGSCFSLCLPF 614
Cdd:pfam02518  81 LVELLGGTITVESEPGGGTTVTLTLPL 107
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
343-622 1.25e-29

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 124.37  E-value: 1.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 343 RLPINRIDELGHIARAYNNLLDTLNEQYDTLEmkvkertlALAEAKRaaeqanRRKSDhlttISHEIRTPLNGALGAVEL 422
Cdd:NF040691  234 RMPVKGEDDLARLARSFNQMADSLQRQIRQLE--------ELSRLQQ------RFVSD----VSHELRTPLTTIRMAADV 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 423 LQNT--PLDAGQMRLAETAHQCSLSLLAIINNLLDFSRIESGQMTLSLEKTALLPLLDQAMLTiHSQalsksLA--LSTF 498
Cdd:NF040691  296 IHDSrdDFDPATARSAELLHTELDRFESLLSDLLEISRFDAGAAELDVEPVDLRPLVRRVVDA-LRQ-----LAerAGVE 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 499 ISANIPLE---LELDTLRLRQILVNLLGNAVKFTPQGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQT---- 571
Cdd:NF040691  370 LRVDAPGTpvvAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTVAQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRAdpar 449
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1190634387 572 SDHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLPFNA----ITPPMP 622
Cdd:NF040691  450 ARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTLPRVAgdrlTTSPLP 504
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
343-613 5.44e-21

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 97.20  E-value: 5.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 343 RLPINRIDELGHIARAYNNLLDTLNEQydtlemkvkertlalaeakraaeQANRRksDHLTTISHEIRTPLNGALGAVEL 422
Cdd:NF012163  210 RVTPTSNDELGKLAQDFNQLASTLEKN-----------------------EQMRR--DFMADISHELRTPLAVLRAELEA 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 423 LQNTpldagqMRLAETAHQCSL-----SLLAIINNLLDFSRIESGQMTLSLEKTALLPLLDQAMLTIHSQALSKSLALST 497
Cdd:NF012163  265 IQDG------IRKFTPESLDSLqaevgTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEV 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 498 FISANIPLELELDtlRLRQILVNLLGNAVKFTPQ-GRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQ 576
Cdd:NF012163  339 SLPDSSLVFGDRD--RLMQLFNNLLENSLRYTDSgGSLHISASQRPKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRN 416
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1190634387 577 ----GTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:NF012163  417 rasgGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVTLP 457
 
Name Accession Description Interval E-value
PRK15347 PRK15347
two component system sensor kinase;
1-924 0e+00

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 1558.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387   1 MGKASSLVTRLTLLMGVTLTVIWLILIATTAFFSYENTRQILINELTHMASMRADLSNHQFEGAERDAASLISRReslQS 80
Cdd:PRK15347    3 MTWQTSLVIRLTLLLGLTLIIIWLLSVATTAYFSFEQTRQHIIEELSHLSSMRADLSNQRFEGAERDAKNLMYRC---QS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387  81 TSPLPEISIKHYDSYYIPFNLDSCNINQH-KNDLWIIQAYGTAGQTYYLDSFIIKQKEGIVLFPPQKSSSDYLNQRRKDL 159
Cdd:PRK15347   80 ATEIDHNDIKPEVSRYIPFNPKNCDPTLNgKKDRWFIQAYGIAGQSYYLDSFILKPKEGISLFSPDKSSSDYLTLRPLEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 160 LLLPKFPTHNNIYWGAPTYTPQGGWHVSVAVCDKVGTLAGFALKLNDLIAYNHPVEQRDINLLLDKNGELLPISQQATSS 239
Cdd:PRK15347  160 KQLPLQPTHNGIYWGKPEYIPGGGWHVSVAVADKQGVLVGFTVKLNDLISYNHPVLDDDINLWLDQNGELLPFSTIPLSS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 240 NQLHEILNQLKNSKLHDGWQQTPDYLVLRTQLKGPGWQQLVIYPRMGFAWEALKPALYQLPFALAILLLLTSVLSLLLRY 319
Cdd:PRK15347  240 NQLQKILNQLENVKLHDGWQQIPDYLVLRTQLKGPGWQQVTLYPRRNLANEALKPALQQLPFALLILVLLTSVLFLLLRR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 320 YLAIPLWNFINIIGATGPQAMEPRLPINRIDELGHIARAYNNLLDTLNEQYDTLEMKVKERTLALAEAKRAAEQANRRKS 399
Cdd:PRK15347  320 YLAKPLWRFVDIINKTGPAALEPRLPENRLDELGSIAKAYNQLLDTLNEQYDTLENKVAERTQALAEAKQRAEQANKRKS 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 400 DHLTTISHEIRTPLNGALGAVELLQNTPLDAGQMRLAETAHQCSLSLLAIINNLLDFSRIESGQMTLSLEKTALLPLLDQ 479
Cdd:PRK15347  400 EHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPLLDQ 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 480 AMLTIHSQALSKSLALSTFISANIPLELELDTLRLRQILVNLLGNAVKFTPQGRIQLRVRRQNQTLCFTVEDTGCGIDVQ 559
Cdd:PRK15347  480 AMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGGIRLRVKRHEQQLCFTVEDTGCGIDIQ 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 560 HQQTIFQPFMQTSDHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLPFNAITPPMPFHGELFAPQRLHAQLSA 639
Cdd:PRK15347  560 QQQQIFTPFYQADTHSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPLNEYAPPEPLKGELSAPLALHRQLSA 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 640 WGMTCQPelaNQPSRHFVDNALCYLPGRLYAKLKQYLQGAETEALKSLPLQPWQMHILLVDDSETNRDITGMMLQQLGHQ 719
Cdd:PRK15347  640 WGITCQP---GHQNPALLDPELAYLPGRLYDLLQQIIQGAPNEPVINLPLQPWQLQILLVDDVETNRDIIGMMLVELGQQ 716
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 720 VTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANIDSHCMITALSANASPDEQIKTSQAGMNHYLSKP 799
Cdd:PRK15347  717 VTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNLDPDCMIVALTANAAPEEIHRCKKAGMNHYLTKP 796
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 800 VTLGQLAEMLDLTAQFQLERGVDLSPQLSEPQPLLDLADSALSLKLYQSLQVLIQQAKDAIENLPVLSHTLHTIKGCAGQ 879
Cdd:PRK15347  797 VTLAQLARALELAAEYQLLRGIELSPQDSSCSPLLDTDDMALNSKLYQSLLLLLAQIEQAVENQEVLSQLLHTLKGCAGQ 876
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....*
gi 1190634387 880 AGLIELQDAVIQLEHALDTHETLTQQEIIQLDEIIHVLLQPPTTC 924
Cdd:PRK15347  877 AGLTELQCAVIDLENALETGEILSLEELTDLRELIHALFKNPTTC 921
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
350-927 4.22e-91

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: 310.94  E-value: 4.22e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 350 DELGHIARAYNNLLDT-----------------LNEQYDTLEMKVKERTLALAE--------------AKRAAEQANRRK 398
Cdd:TIGR02956 385 DELAHMGRAIEAFRDTaahnlklqaderqvaqeLQEHKESLEQLVAQRTQELAEtnerlnaevknhakARAEAEEANRAK 464
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 399 SDHLTTISHEIRTPLNGALGAVELLQNTPLDAGQMRLAETAHQCSLSLLAIINNLLDFSRIESGQMTLSLEKTALLPLLD 478
Cdd:TIGR02956 465 SAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLD 544
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 479 QAMLTIHSQALSKSLALSTFISANIPLELELDTLRLRQILVNLLGNAVKFTPQGRIQLRVRRQNQ-TLCFTVEDTGCGID 557
Cdd:TIGR02956 545 DVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDsSLLFEVEDTGCGIA 624
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 558 VQHQQTIFQPFMQTSDHEQ--GTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLPFNaitppmpfhgelfapqrlha 635
Cdd:TIGR02956 625 EEEQATLFDAFTQADGRRRsgGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLT-------------------- 684
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 636 qlsawgmTCQPElanqpsrhfvdnalcylpgrlyaklkqylQGAETEALKSLPLQpwqmHILLVDDSETNRDITGMMLQQ 715
Cdd:TIGR02956 685 -------RGKPA-----------------------------EDSATLTVIDLPPQ----RVLLVEDNEVNQMVAQGFLTR 724
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 716 LGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANIDSHCMItALSANASPDEQIKTSQAGMNHY 795
Cdd:TIGR02956 725 LGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIYGAKNEVKFI-AFSAHVFNEDVAQYLAAGFDGF 803
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 796 LSKPVTLGQL----------------AEMLDLTAQFQLERGVDLSPQLSEPQP------LLD---LADSALSL---KLYQ 847
Cdd:TIGR02956 804 LAKPVVEEQLtamiavilaggksnteAPVLSASPSFDSASVIENAQADDIPESnqasefLLDeeqLQQDIEVLgveKVRQ 883
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 848 SLQVLIQQAKDAIENLPV---------LSHTLHTIKGCAGQAGLIELQdaviQLEHALDTHETLTQQEIIQLDEIIHVLL 918
Cdd:TIGR02956 884 LVALFKTSSAEQLEELSAaravdddaqIKKLAHKLKGSAGSLGLTQLT----QLCQQLEKQGKTGALELSDIDEIKQAWQ 959

                  ....*....
gi 1190634387 919 QPPTTCEST 927
Cdd:TIGR02956 960 ASKTALDQW 968
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
291-615 1.98e-75

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 250.21  E-value: 1.98e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 291 ALKPALYQLPFALAILLLLTSVLSLLLRYYLAIPLWNFINIIGATGPQAMEPRLPINRIDELGHIARAYN-NLLDTLNEQ 369
Cdd:COG0642     2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLlLLLLLLLLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 370 YDTLEMKVKERTLALAEAKRAAEQANRRKSDHLTTISHEIRTPLNGALGAVELLQNTPlDAGQMRLAETAHQCSLSLLAI 449
Cdd:COG0642    82 LLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEEL-DEEQREYLETILRSADRLLRL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 450 INNLLDFSRIESGQMTLSLEKTALLPLLDQAMLTIHSQALSKSLALSTFISANIPLeLELDTLRLRQILVNLLGNAVKFT 529
Cdd:COG0642   161 INDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPT-VRGDPDRLRQVLLNLLSNAIKYT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 530 PQG-RIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQT--SDHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGS 606
Cdd:COG0642   240 PEGgTVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTdpSRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGT 319

                  ....*....
gi 1190634387 607 CFSLCLPFN 615
Cdd:COG0642   320 TFTVTLPLA 328
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
387-917 8.41e-70

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 249.77  E-value: 8.41e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 387 AKRAAEQANRRKSDHLTTISHEIRTPLNGALGAVELLQNTPLDAGQMRLAETAHQCSLSLLAIINNLLDFSRIESGQMTL 466
Cdd:PRK11107  282 AKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVL 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 467 -----SLEKTallplLDQAMLTIHSQALSKSLALSTFISANIPLELELDTLRLRQILVNLLGNAVKFTPQGRIQLRVRRQ 541
Cdd:PRK11107  362 enipfSLRET-----LDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELR 436
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 542 NQ-----TLCFTVEDTGCGIDVQHQQTIFQPFMQ----TSDHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCL 612
Cdd:PRK11107  437 ALsntkvQLEVQIRDTGIGISERQQSQLFQAFRQadasISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHL 516
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 613 PFNaiTPPMPFHGEL-----------------FAPQRLHAQLSAWGM--TCQPELANQPSRHFvDNALCYLP-------G 666
Cdd:PRK11107  517 PLD--LNPNPIIDGLptdclagkrllyvepnsAAAQATLDILSETPLevTYSPTLSQLPEAHY-DILLLGLPvtfreplT 593
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 667 RLYAKLKQYLQGA-------------ETEALK--------SLP---------LQPWQMH-----------------ILLV 699
Cdd:PRK11107  594 MLHERLAKAKSMTdflilalpcheqvLAEQLKqdgadaclSKPlshtrllpaLLEPCHHkqppllpptdesrlpltVMAV 673
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 700 DDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANidSHCMITALSANA 779
Cdd:PRK11107  674 DDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHN--QNTPIIAVTAHA 751
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 780 SPDEQIKTSQAGMNHYLSKPVTLGQLAEML----DLTAQFQLERGVDLSPQLSEPQPLLD--LA------DSALSLKLYQ 847
Cdd:PRK11107  752 MAGERERLLSAGMDDYLAKPIDEAMLKQVLlrykPGPKFTSRVVAPEPPEPVHFPNATLDwqLAlrqaagKPDLARDMLQ 831
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 848 SL-------QVLIQQAKDAiENLPVLSHTLHTIKGCAGQAGLIELQDAVIQLEHAL--DTHETLTQQEIIQL-DEIIHVL 917
Cdd:PRK11107  832 MLldflpevRNKVEEALAG-EDPEGLLDLIHKLHGSCSYSGVPRLKKLCQLIEQQLrsGTSVEDLEPELLELlDEMENVA 910
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
383-613 2.47e-69

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 230.18  E-value: 2.47e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 383 ALAEAKRAAEQANRRKSDHLTTISHEIRTPLNGALGAVELLQN--TPLDAGQMRLAETAHQCSLSLLAIINNLLDFSRIE 460
Cdd:COG2205     1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDeeDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 461 SGQMTLSLEKTALLPLLDQAMLTIHSQALSKSLALSTFISANiPLELELDTLRLRQILVNLLGNAVKFTPQG-RIQLRVR 539
Cdd:COG2205    81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPE-LPLVYADPELLEQVLANLLDNAIKYSPPGgTITISAR 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1190634387 540 RQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQ--TSDHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:COG2205   160 REGDGVRISVSDNGPGIPEEELERIFERFYRgdNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLP 235
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
386-886 2.48e-68

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 243.31  E-value: 2.48e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 386 EAKR---AAEQANRRKSDHLTTISHEIRTPLNGALGAVELLQNTPLDAGQMRLAETAHQCSLSLLAIINNLLDFSRIESG 462
Cdd:PRK11091  268 ERKRyqdALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERR 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 463 QMTLSLEKTALLPLLDQAMLTIHSQALSKSLALSTFISANIPLELELDTLRLRQILVNLLGNAVKFTPQGRIQLRVRR-Q 541
Cdd:PRK11091  348 KLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRYeE 427
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 542 NQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSD-----HEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLclpfna 616
Cdd:PRK11091  428 GDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDshggkPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTL------ 501
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 617 itppmpfhgelfapqRLHAQLSAWGMTCQPELANQPsrhfvdnalcyLPGrlyaklkqylqgaetealkslplqpwqMHI 696
Cdd:PRK11091  502 ---------------TIHAPAVAEEVEDAFDEDDMP-----------LPA---------------------------LNI 528
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 697 LLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGL--ATTARWRHDPANIDShcmITA 774
Cdd:PRK11091  529 LLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLdiARELRERYPREDLPP---LVA 605
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 775 LSANASPDEQiKTSQAGMNHYLSKPVTLGQLAEMLDLTAQFQLERGVDLSPQLS--EPQPLLDLA------DSALSLKLY 846
Cdd:PRK11091  606 LTANVLKDKK-EYLDAGMDDVLSKPLSVPALTAMIKKFWDTQDDEESTVTTEESskANEALLDIPmleqyvELVGPKLIT 684
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1190634387 847 QSLQVLIQQAKDAIEnlpVLSHTL------------HTIKGCAGQAGLIELQ 886
Cdd:PRK11091  685 DSLAVFEKMMPGYLS---VLDSNLtardqkgiveeaHKIKGAAGSVGLRHLQ 733
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
384-809 5.16e-68

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 244.88  E-value: 5.16e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 384 LAEAKRAAEQANRRKSDHLTTISHEIRTPLNGALGAVELLQNTPLDAGQMRLAETAHQCSLSLLAIINNLLDFSRIESGQ 463
Cdd:PRK10841  433 LQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQ 512
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 464 mtLSLEKTALLPLldQAMLTIHSQALS----KSLALSTFISANIPLELELDTLRLRQILVNLLGNAVKFTPQGRIQLRVR 539
Cdd:PRK10841  513 --LKIEPREFSPR--EVINHITANYLPlvvkKRLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHVR 588
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 540 RQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQ----TSDHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLP-F 614
Cdd:PRK10841  589 VDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQvgtgVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIPlY 668
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 615 NAITPPMPFHGEL------------FAPQRLHAQLSAWGMTCQ-----------------PELANQPSRHFVD------- 658
Cdd:PRK10841  669 GAQYPQKKGVEGLqgkrcwlavrnaSLEQFLETLLQRSGIQVQryegqeptpedvlitddPVQKKWQGRAVITfcrrhig 748
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 659 -----------------NALCYLPGRLYAKlkqylQGAETEALKSLPLQPWQ------MHILLVDDSETNRDITGMMLQQ 715
Cdd:PRK10841  749 ipleiapgewvhstatpHELPALLARIYRI-----ELESDDSANALPSTDKAvsdnddMMILVVDDHPINRRLLADQLGS 823
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 716 LGHQVTRADSGTTALA-IGRQHrFDLVLMDIRMPVLDGLATTARWRHDPANIDshcmITALSANASPDEQIKTSQAGMNH 794
Cdd:PRK10841  824 LGYQCKTANDGVDALNvLSKNH-IDIVLTDVNMPNMDGYRLTQRLRQLGLTLP----VIGVTANALAEEKQRCLEAGMDS 898
                         490
                  ....*....|....*
gi 1190634387 795 YLSKPVTLGQLAEML 809
Cdd:PRK10841  899 CLSKPVTLDVLKQTL 913
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
276-613 8.34e-61

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 212.11  E-value: 8.34e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 276 WQQLVIYPRMGFAWEALKPALYQLPFALAILLLLTSVLSLLLRYYLAIPLWNFINIIGATGPQAMEPRLPINRIDELGHI 355
Cdd:COG5002    41 LLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLALLILLAALLLL 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 356 ARAYNNLLDTLNEQYDTLEMKVKERTLALAEAK--RAAEQANRRKSDHLTTISHEIRTPLNGALGAVELLQNTPLDAGQM 433
Cdd:COG5002   121 LSELLLLLLLLGRLSLRLSALLLGLLLLAAVERdiTELERLEQMRREFVANVSHELRTPLTSIRGYLELLLDGAADDPEE 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 434 --RLAETAHQCSLSLLAIINNLLDFSRIESGQMTLSLEKTALLPLLDQAMLTIHSQALSKSLALSTFISANiPLELELDT 511
Cdd:COG5002   201 rrEYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPED-PLLVLGDP 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 512 LRLRQILVNLLGNAVKFTPQG-RIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQT----SDHEQGTGLGLAIAD 586
Cdd:COG5002   280 DRLEQVLTNLLDNAIKYTPEGgTITVSLREEDDQVRISVRDTGIGIPEEDLPRIFERFYRVdksrSRETGGTGLGLAIVK 359
                         330       340
                  ....*....|....*....|....*..
gi 1190634387 587 NLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:COG5002   360 HIVEAHGGRIWVESEPGKGTTFTITLP 386
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
346-904 1.78e-58

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 216.70  E-value: 1.78e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 346 INRIDELGHIARAYNNLLDTLNEQYDTLEMKVKERTLALAE-------AKRAAEQANRRKSDHLTTISHEIRTPLNGALG 418
Cdd:PRK11466  385 VRELDTIGRLMDAFRSNVHALNRHREQLAAQVKARTAELQElviehrqARAEAEKASQAKSAFLAAMSHEIRTPLYGILG 464
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 419 AVELLQNTPLDAGQMRLAETAHQCSLSLLAIINNLLDFSRIESGQMTLSL--EKTALLPLLDQAMLTIHSQALSKSLALS 496
Cdd:PRK11466  465 TAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAGGKNVSVsdEPFEPRPLLESTLQLMSGRVKGRPIRLA 544
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 497 TFISANIPLELELDTLRLRQILVNLLGNAVKFTPQGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQ 576
Cdd:PRK11466  545 TDIADDLPTALMGDPRRIRQVITNLLSNALRFTDEGSIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFVQVSGKRG 624
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 577 GTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLPFNAITPPMpfhgelfapqrlhaqlsawgmtcqPELANQPSRhf 656
Cdd:PRK11466  625 GTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLRVATAPV------------------------PKTVNQAVR-- 678
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 657 vdnalcyLPGRlyaklkqylqgaetealkslplqpwqmHILLVDDSETNRDITGMMLQQLGHQVTRADSGTTAL-AIGRQ 735
Cdd:PRK11466  679 -------LDGL---------------------------RLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALeTLQNS 724
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 736 HRFDLVLMDIRMPVLDGLaTTARwrhDPANIDSHCMITALSANASPDEQIKTSQAGMNHYLSKPVTLGQLAEMLD--LTA 813
Cdd:PRK11466  725 EPFAAALVDFDLPDYDGI-TLAR---QLAQQYPSLVLIGFSAHVIDETLRQRTSSLFRGIIPKPVPREVLGQLLAhyLQL 800
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 814 QFQLERGVDLSpQLSEP----------QPLLDLADSALSLklyqSLQVLIQQAKDAIENLPVLSHTLhtiKGCAGQAGLI 883
Cdd:PRK11466  801 QVNNDQPLDVS-QLNEDaalmgtekihEWLALFKQHALPL----LDEIDIARASQDSEKIKRAAHQL---KSSCSSLGMR 872
                         570       580
                  ....*....|....*....|....*
gi 1190634387 884 ELQDAVIQLEH----ALDTHETLTQ 904
Cdd:PRK11466  873 QASQACAQLEQqplsAPLPHEEITR 897
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
286-613 1.79e-45

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 167.67  E-value: 1.79e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 286 GFAWEALKPALYQLPFALAILLLLTSVLSLLLRYYLAIPLWNFINIIGATGPQAMEPRLPINRIDELGHIARAYNNLLDT 365
Cdd:COG4191    25 LLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLLEALLLLLLAALDAE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 366 LNEQYDTLEMKVKERTLALAEAKRAAEQAnrRKSDHLTT-------ISHEIRTPLNGALGAVELLQN----TPLDAGQMR 434
Cdd:COG4191   105 ENAELEELERDITELERAEEELRELQEQL--VQSEKLAAlgelaagIAHEINNPLAAILGNAELLRRrledEPDPEELRE 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 435 LAETAHQCSLSLLAIINNLLDFSRiesgQMTLSLEKTALLPLLDQAMLTIHSQALSKSLALSTFISANIPLeLELDTLRL 514
Cdd:COG4191   183 ALERILEGAERAAEIVRSLRAFSR----RDEEEREPVDLNELIDEALELLRPRLKARGIEVELDLPPDLPP-VLGDPGQL 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 515 RQILVNLLGN---AVKFTPQGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQGTGLGLAIADNLAKM 591
Cdd:COG4191   258 EQVLLNLLINaidAMEEGEGGRITISTRREGDYVVISVRDNGPGIPPEVLERIFEPFFTTKPVGKGTGLGLSISYGIVEK 337
                         330       340
                  ....*....|....*....|..
gi 1190634387 592 MGGHLTVFSEPGQGSCFSLCLP 613
Cdd:COG4191   338 HGGRIEVESEPGGGTTFTITLP 359
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
514-614 4.69e-45

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: 157.65  E-value: 4.69e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 514 LRQILVNLLGNAVKFTPQGRIQLRVRRQNQT-----LCFTVEDTGCGIDVQHQQTIFQPFMQTSDH----EQGTGLGLAI 584
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEedgvqLRFSVEDTGIGIPEEQQARLFEPFSQADSSttrkYGGTGLGLAI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1190634387 585 ADNLAKMMGGHLTVFSEPGQGSCFSLCLPF 614
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
383-910 4.07e-43

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 170.69  E-value: 4.07e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387  383 ALAEAKRAAEQANRRKSDHLTTISHEIRTPLNGALGAVELLQNTPLDAGQ-MRLAETAHQCSLSLLAIINNLLDFSRIES 461
Cdd:PRK09959   697 ALEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQrVEAISLAYATGQSLLGLIGEILDVDKIES 776
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387  462 GQMTLSLEKTALLPLLDQAMLTIHSQALSKSLALSTfiSANIPLE--LELDTLRLRQILVNLLGNAVKFTPQGRIQL--- 536
Cdd:PRK09959   777 GNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSC--SSTFPDHylVKIDPQAFKQVLSNLLSNALKFTTEGAVKItts 854
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387  537 --RVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQ--GTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCL 612
Cdd:PRK09959   855 lgHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQqtGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITI 934
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387  613 PFNAItppmpfhgelfapqrlhaqlsawgmtcqpelanqpsrhfvdnalcylpgrlyaklkQYLQGAETEALKSLPLqPW 692
Cdd:PRK09959   935 PVEIS--------------------------------------------------------QQVATVEAKAEQPITL-PE 957
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387  693 QMHILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDpaniDSHCMI 772
Cdd:PRK09959   958 KLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQ----NSSLPI 1033
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387  773 TALSANASPDEQIKTSQAGMNHYLSKPVTLGQLAEMLDltaqfQLERGVDLSPQLSEPQPLLDLADSALSLKLYQSLQVL 852
Cdd:PRK09959  1034 WGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLS-----QLHQVAHIAPQYRHLDIEALKNNTANDLQLMQEILMT 1108
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1190634387  853 IQQakDAIENLPVLSHTLH-----TIKGCA----GQAGLIELQDaVIQLEHALDTHETL--TQQEIIQL 910
Cdd:PRK09959  1109 FQH--ETHKDLPAAFHALEagdnrTFHQCIhrihGAANILNLQK-LINISHQLEITPVSddSKPEILQL 1174
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
275-613 2.21e-41

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 159.57  E-value: 2.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 275 GWQQLVIYPRMGFAWEALKPALYQLPFALAILLLLTSVLSLLLRYYLAIPLWNFINIIGATGPQAMEPRLPINRIDELGH 354
Cdd:COG4251   159 LLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLL 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 355 IARAYNNLLDTLNEQYDTLEMKVKERTLALAEAKRAAEQANRRKSDHLTTISHEIRTPLNGALGAVELLQ---NTPLDAG 431
Cdd:COG4251   239 LLLILLLLLLILVLELLELRLELEELEEELEERTAELERSNEELEQFAYVASHDLREPLRKISGFSQLLEedyGDKLDEE 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 432 QMRLAETAHQCSLSLLAIINNLLDFSRIesGQMTLSLEKTALLPLLDQAMLTIHSQALSKSLalsTFISANIPlELELDT 511
Cdd:COG4251   319 GREYLERIRDAAERMQALIDDLLAYSRV--GRQELEFEPVDLNELLEEVLEDLEPRIEERGA---EIEVGPLP-TVRGDP 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 512 LRLRQILVNLLGNAVKFT---PQGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPF--MQTSDHEQGTGLGLAIAD 586
Cdd:COG4251   393 TLLRQVFQNLISNAIKYSrpgEPPRIEIGAEREGGEWVFSVRDNGIGIDPEYAEKIFEIFqrLHSRDEYEGTGIGLAIVK 472
                         330       340
                  ....*....|....*....|....*..
gi 1190634387 587 NLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:COG4251   473 KIVERHGGRIWVESEPGEGATFYFTLP 499
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
405-613 2.70e-38

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: 148.57  E-value: 2.70e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 405 ISHEIRTPLNGALGAVELLQ-----NTPLDAGQM-RLAETAHQCSLSLLAIINNLLDFSRIESGQMtlslEKTALLPLLD 478
Cdd:COG5000   208 IAHEIKNPLTPIQLSAERLRrkladKLEEDREDLeRALDTIIRQVDRLKRIVDEFLDFARLPEPQL----EPVDLNELLR 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 479 QAMLTIHSQALSKSLALSTFISANIPlELELDTLRLRQILVNLLGNAVKFTPQ-GRIQLRVRRQNQTLCFTVEDTGCGID 557
Cdd:COG5000   284 EVLALYEPALKEKDIRLELDLDPDLP-EVLADRDQLEQVLINLLKNAIEAIEEgGEIEVSTRREDGRVRIEVSDNGPGIP 362
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1190634387 558 VQHQQTIFQPFMQTsdHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:COG5000   363 EEVLERIFEPFFTT--KPKGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLP 416
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
397-613 3.72e-38

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: 149.74  E-value: 3.72e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 397 RKSDHLT-------TISHEIRTPLNGALGAVELLQNTPLDAGQMRLaETAHQCSLSLLAIINNLLDFSRIESGQMtlslE 469
Cdd:COG5809   262 RKSEKLSvvgelaaGIAHEIRNPLTSLKGFIQLLKDTIDEEQKTYL-DIMLSELDRIESIISEFLVLAKPQAIKY----E 336
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 470 KTALLPLLDQAMLTIHSQALSKSLALSTFISANIPLeLELDTLRLRQILVNLLGNAVKFTP-QGRIQLRVRRQNQT-LCF 547
Cdd:COG5809   337 PKDLNTLIEEVIPLLQPQALLKNVQIELELEDDIPD-ILGDENQLKQVFINLLKNAIEAMPeGGNITIETKAEDDDkVVI 415
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1190634387 548 TVEDTGCGIDVQHQQTIFQPFMQTSdhEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:COG5809   416 SVTDEGCGIPEERLKKLGEPFYTTK--EKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLP 479
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
696-809 2.06e-37

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: 135.67  E-value: 2.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANiDSHCMITAL 775
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGG-GRRTPIIAL 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKPVTLGQLAEML 809
Cdd:cd17546    80 TANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
510-614 2.77e-37

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 135.47  E-value: 2.77e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387  510 DTLRLRQILVNLLGNAVKFTP-QGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQ---GTGLGLAIA 585
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTPeGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRkigGTGLGLSIV 81
                           90       100
                   ....*....|....*....|....*....
gi 1190634387  586 DNLAKMMGGHLTVFSEPGQGSCFSLCLPF 614
Cdd:smart00387  82 KKLVELHGGEISVESEPGGGTTFTITLPL 110
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
694-809 5.29e-37

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: 135.36  E-value: 5.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 694 MHILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANidSHCMIT 773
Cdd:COG0784     6 KRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRL--PDIPII 83
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1190634387 774 ALSANASPDEQIKTSQAGMNHYLSKPVTLGQLAEML 809
Cdd:COG0784    84 ALTAYADEEDRERALEAGADDYLTKPVDPEELLEAL 119
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
405-620 5.88e-34

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 134.20  E-value: 5.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 405 ISHEIRTPLNGALGAVELLQNTPLDAGQMRLAETAHQCSLSLLAIINNLLDFSRIESGQMtlslEKTALLPLLDQAMLTI 484
Cdd:COG3852   142 LAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPER----EPVNLHEVLERVLELL 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 485 HSQALsKSLALSTFISANIPlELELDTLRLRQILVNLLGNAVKFTP-QGRIQLRVRRQNQT----------LCFTVEDTG 553
Cdd:COG3852   218 RAEAP-KNIRIVRDYDPSLP-EVLGDPDQLIQVLLNLVRNAAEAMPeGGTITIRTRVERQVtlgglrprlyVRIEVIDNG 295
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1190634387 554 CGIDVQHQQTIFQPFMQTsdHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLPFNAITPP 620
Cdd:COG3852   296 PGIPEEILDRIFEPFFTT--KEKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQAEEE 360
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
510-614 3.98e-33

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: 123.63  E-value: 3.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 510 DTLRLRQILVNLLGNAVKFTPQ-GRIQLRVRRQNQtLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQ-GTGLGLAIADN 587
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAAKaGEITVTLSEGGE-LTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGgGTGLGLSIVRK 80
                          90       100
                  ....*....|....*....|....*..
gi 1190634387 588 LAKMMGGHLTVFSEPGQGSCFSLCLPF 614
Cdd:pfam02518  81 LVELLGGTITVESEPGGGTTVTLTLPL 107
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
392-609 1.47e-31

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: 126.55  E-value: 1.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 392 EQANRRKSDHLTTISHEIRTPLNGALGAVELLQNTPLDAGQM--RLAETAHQCSLSLLAIINNLLDFSRIESGQMTLSLE 469
Cdd:TIGR02966 108 RRLEQMRRDFVANVSHELRTPLTVLRGYLETLADGPDEDPEEwnRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDE 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 470 KTALLPLLDqamlTIHSQALSKSLALSTFISANI--PLELELDTLRLRQILVNLLGNAVKFTP-QGRIQLRVRRQNQTLC 546
Cdd:TIGR02966 188 PVDMPALLD----HLRDEAEALSQGKNHQITFEIdgGVDVLGDEDELRSAFSNLVSNAIKYTPeGGTITVRWRRDGGGAE 263
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1190634387 547 FTVEDTGCGIDVQHQQTIFQPFMQT----SDHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFS 609
Cdd:TIGR02966 264 FSVTDTGIGIAPEHLPRLTERFYRVdksrSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFS 330
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
693-831 5.98e-31

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: 120.01  E-value: 5.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 693 QMHILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANIDSHcmI 772
Cdd:COG3706     1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIP--I 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1190634387 773 TALSANASPDEQIKTSQAGMNHYLSKPVTLGQLAEMLDLTAQFQLERGVDLSPQLSEPQ 831
Cdd:COG3706    79 IFLTALDDEEDRARALEAGADDYLTKPFDPEELLARVDLVARYGGEEFAILLPGTDLEG 137
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
342-613 6.10e-30

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 124.57  E-value: 6.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 342 PRLPINRIDELGHIARAYNNLLDTLneqydtlemkvkertlalaEAKRAAEQanrrksdHLTTISHEIRTPLNGALGAVE 421
Cdd:PRK11100  226 VPLPKLGSSELRELAQALESMRVKL-------------------EGKAYVEQ-------YVQTLTHELKSPLAAIRGAAE 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 422 LLQNTPLDAGQMRLAETAHQCSLSLLAIINNLLDFSRIESGQMTLSLEKTALLPLLDQAMLTIHSQALSKSLALSTFISa 501
Cdd:PRK11100  280 LLQEDPPPEDRARFTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEAREAQAAAKGITLRLRPD- 358
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 502 niPLELELDTLRLRQILVNLLGNAVKFTPQG-RIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTS---DHEQG 577
Cdd:PRK11100  359 --DARVLGDPFLLRQALGNLLDNAIDFSPEGgTITLSAEVDGEQVALSVEDQGPGIPDYALPRIFERFYSLPrpaNGRKS 436
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1190634387 578 TGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:PRK11100  437 TGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLP 472
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
343-622 1.25e-29

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 124.37  E-value: 1.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 343 RLPINRIDELGHIARAYNNLLDTLNEQYDTLEmkvkertlALAEAKRaaeqanRRKSDhlttISHEIRTPLNGALGAVEL 422
Cdd:NF040691  234 RMPVKGEDDLARLARSFNQMADSLQRQIRQLE--------ELSRLQQ------RFVSD----VSHELRTPLTTIRMAADV 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 423 LQNT--PLDAGQMRLAETAHQCSLSLLAIINNLLDFSRIESGQMTLSLEKTALLPLLDQAMLTiHSQalsksLA--LSTF 498
Cdd:NF040691  296 IHDSrdDFDPATARSAELLHTELDRFESLLSDLLEISRFDAGAAELDVEPVDLRPLVRRVVDA-LRQ-----LAerAGVE 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 499 ISANIPLE---LELDTLRLRQILVNLLGNAVKFTPQGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQT---- 571
Cdd:NF040691  370 LRVDAPGTpvvAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTVAQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRAdpar 449
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1190634387 572 SDHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLPFNA----ITPPMP 622
Cdd:NF040691  450 ARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTLPRVAgdrlTTSPLP 504
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
384-617 5.54e-29

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 123.54  E-value: 5.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 384 LAEAKRAAEQANRrkSDHLTT-------ISHEIRTPLNGALGAVELLQNTPLDAGQMRLAETAHQCSLSLLAIINNLLDF 456
Cdd:PRK11360  371 LTERKRLQRRVAR--QERLAAlgelvagVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEF 448
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 457 SRIESGQMtlslEKTALLPLLDQA---MLTIHSQAlskSLALSTFISANIPLeLELDTLRLRQILVNLLGNAVKFTPQ-G 532
Cdd:PRK11360  449 SRPRESQW----QPVSLNALVEEVlqlFQTAGVQA---RVDFETELDNELPP-IWADPELLKQVLLNILINAVQAISArG 520
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 533 RIQLRVRRQNQT-LCFTVEDTGCGIDVQHQQTIFQPFMQTSDheQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLC 611
Cdd:PRK11360  521 KIRIRTWQYSDGqVAVSIEDNGCGIDPELLKKIFDPFFTTKA--KGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLY 598

                  ....*.
gi 1190634387 612 LPFNAI 617
Cdd:PRK11360  599 LPINPQ 604
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
693-856 5.32e-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: 112.36  E-value: 5.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 693 QMHILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANIDshcmI 772
Cdd:COG0745     1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIP----I 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 773 TALSANASPDEQIKTSQAGMNHYLSKPVTLGQLAE----MLDLTAQFQLERGVDLSPqlSEPQPLLDLADSALSLKLYQS 848
Cdd:COG0745    77 IMLTARDDEEDRVRGLEAGADDYLTKPFDPEELLAriraLLRRRAAEVLRVGDLLDL--AAREVTRDGEPVELTPKEFRL 154

                  ....*...
gi 1190634387 849 LQVLIQQA 856
Cdd:COG0745   155 LELLMRNP 162
PRK09303 PRK09303
histidine kinase;
366-613 7.79e-28

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 116.59  E-value: 7.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 366 LNEQYDTL--EMKVKERTLALaeakraaeqanrrksdhlttISHEIRTPLNGALGAVE---LLQNTPLDAGQMRLAETAH 440
Cdd:PRK09303  137 LRQENETLleQLKFKDRVLAM--------------------LAHDLRTPLTAASLALEtleLGQIDEDTELKPALIEQLQ 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 441 QCSLSLLAIIN----NLLDFSRIESGQMTLSLEKTALLPLLDQAMLTIHSQALSKSLALSTFISANIPLeLELDTLRLRQ 516
Cdd:PRK09303  197 DQARRQLEEIErlitDLLEVGRTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSDLPS-VYADQERIRQ 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 517 ILVNLLGNAVKFTP-QGRIQLRV-RRQNQTLCFTVEDTGCGIDVQHQQTIFQPF--MQTSDHEQGTGLGLAIADNLAKMM 592
Cdd:PRK09303  276 VLLNLLDNAIKYTPeGGTITLSMlHRTTQKVQVSICDTGPGIPEEEQERIFEDRvrLPRDEGTEGYGIGLSVCRRIVRVH 355
                         250       260
                  ....*....|....*....|.
gi 1190634387 593 GGHLTVFSEPGQGSCFSLCLP 613
Cdd:PRK09303  356 YGQIWVDSEPGQGSCFHFTLP 376
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
696-809 1.48e-27

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: 107.54  E-value: 1.48e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANidSHCMITAL 775
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWL--ANTPAIAL 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKPVTLGQLAEML 809
Cdd:cd17580    79 TGYGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
PRK10490 PRK10490
sensor protein KdpD; Provisional
379-627 1.37e-26

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 117.06  E-value: 1.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 379 ERtLALAE----AKRAAEQANRRKSdHLTTISHEIRTPLNGALGAVELL------QNTP--LDAGQMRlaetahQCSLSL 446
Cdd:PRK10490  643 ER-LTLTAseeqARLASEREQLRNA-LLAALSHDLRTPLTVLFGQAEILtldlasEGSPhaRQASEIR------QQVLNT 714
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 447 LAIINNLLDFSRIESGQMTLSLEKTALLPLLDQAMltihsQALSKSLALSTfISANIPLELEL---DTLRLRQILVNLLG 523
Cdd:PRK10490  715 TRLVNNLLDMARIQSGGFNLRKEWLTLEEVVGSAL-----QMLEPGLSGHP-INLSLPEPLTLihvDGPLFERVLINLLE 788
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 524 NAVKFT-PQGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQtSDHEQ---GTGLGLAIADNLAKMMGGHLTVF 599
Cdd:PRK10490  789 NAVKYAgAQAEIGIDAHVEGERLQLDVWDNGPGIPPGQEQLIFDKFAR-GNKESaipGVGLGLAICRAIVEVHGGTIWAE 867
                         250       260       270
                  ....*....|....*....|....*....|
gi 1190634387 600 SEPGQGSCFSLCLPFNaiTPPM--PFHGEL 627
Cdd:PRK10490  868 NRPEGGACFRVTLPLE--TPPEleEFHEDM 895
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
694-836 5.32e-25

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: 104.09  E-value: 5.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 694 MHILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANidSHCMIT 773
Cdd:COG3437     7 PTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPST--RDIPVI 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1190634387 774 ALSANASPDEQIKTSQAGMNHYLSKPVTLGQLAEMLD--LTAQFQLERGVDLSPQLSEPQPLLDL 836
Cdd:COG3437    85 FLTALADPEDRERALEAGADDYLTKPFDPEELLARVRnaLELRRLQRELDDLVLYLKLAAPLHDI 149
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
697-799 3.92e-24

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: 97.30  E-value: 3.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 697 LLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANIDshcmITALS 776
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIP----VIVLT 76
                          90       100
                  ....*....|....*....|...
gi 1190634387 777 ANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd00156    77 AKADEEDAVRALELGADDYLVKP 99
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
374-616 9.79e-24

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 105.64  E-value: 9.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 374 EMKVKERTLALAeakraaeqanrrksdHLTT-ISHEIRTPLNGALG-AVELLQNTPLDAGQMRLAETAHQCSLSLLAIIN 451
Cdd:PRK10364  227 EMKRKEKLVALG---------------HLAAgVAHEIRNPLSSIKGlAKYFAERAPAGGEAHQLAQVMAKEADRLNRVVS 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 452 NLLDFSRiesgQMTLSLEKTALLPLLDQAMLTIHSQALSKSLALSTFISANIPLeLELDTLRLRQILVNLLGNAVKFTPQ 531
Cdd:PRK10364  292 ELLELVK----PTHLALQAVDLNDLINHSLQLVSQDANSREIQLRFTANDTLPE-IQADPDRLTQVLLNLYLNAIQAIGQ 366
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 532 -GRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDheQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSL 610
Cdd:PRK10364  367 hGVISVTASESGAGVKISVTDSGKGIAADQLEAIFTPYFTTKA--EGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTL 444

                  ....*.
gi 1190634387 611 CLPFNA 616
Cdd:PRK10364  445 WLPVNI 450
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
696-810 2.62e-23

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: 95.68  E-value: 2.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRhdpaNIDSHCMITAL 775
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIR----RRDPTTPVIIL 76
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKPVTLGQLAEMLD 810
Cdd:pfam00072  77 TAHGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
693-827 3.91e-23

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


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 103.12  E-value: 3.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 693 QMHILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRhdpaNIDSHCMI 772
Cdd:COG2204     2 MARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELR----ALDPDLPV 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1190634387 773 TALSANASPDEQIKTSQAGMNHYLSKPVTLGQLAEMLD-LTAQFQLERGVDLSPQL 827
Cdd:COG2204    78 ILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVErALERRRLRRENAEDSGL 133
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
405-613 9.21e-23

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


Pssm-ID: 444508 [Multi-domain]  Cd Length: 412  Bit Score: 101.87  E-value: 9.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 405 ISHEIRTPLNGALGAVELLQNTPL-DAGQMRLAETAhqcsLSLL----AIINNLLDFSRIESGQM-TLSLEKTallplLD 478
Cdd:COG5806   208 IAHEVRNPLTVVRGFIQLLQEPELsDEKRKQYIRIA----LEELdraeAIITDYLTFAKPQPEKLeKIDVSEE-----LE 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 479 QAMLTIHSQALSKSLALSTFISAniPLELELDTLRLRQILVNLLGNAVKFTPQ-GRIQLRVRRQNQTLCFTVEDTGCGID 557
Cdd:COG5806   279 HVIDVLSPYANMNNVEIQTELEP--GLYIEGDRQKLQQCLINIIKNGIEAMPNgGTLTIDVSIDKNKVIISIKDTGVGMT 356
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1190634387 558 VQHQQTIFQPFMQTSdhEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:COG5806   357 KEQLERLGEPYFSTK--EKGTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFTITLP 410
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
405-613 1.26e-22

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 102.01  E-value: 1.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 405 ISHEIRTPLNGALGAVELLQNTPLDaGQMRlaETAHQCSLSLL----AIINNLLDFSRIESGQMtLSLEKTALLPlldqA 480
Cdd:PRK11006  211 VSHELRTPLTVLQGYLEMMQDQPLE-GALR--EKALHTMREQTqrmeGLVKQLLTLSKIEAAPT-IDLNEKVDVP----M 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 481 MLTI---HSQALSKSLALSTF-ISANipLELELDTLRLRQILVNLLGNAVKFTPQG-RIQLRVRRQNQTLCFTVEDTGCG 555
Cdd:PRK11006  283 MLRVlerEAQTLSQGKHTITFeVDNS--LKVFGNEDQLRSAISNLVYNAVNHTPEGtHITVRWQRVPQGAEFSVEDNGPG 360
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1190634387 556 IDVQHQQTIFQPFMQT----SDHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:PRK11006  361 IAPEHIPRLTERFYRVdkarSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLP 422
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
696-800 1.45e-22

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: 93.37  E-value: 1.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANidSHCMITAL 775
Cdd:cd17548     2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPAT--RDIPVIAL 79
                          90       100
                  ....*....|....*....|....*
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKPV 800
Cdd:cd17548    80 TAYAMKGDREKILEAGCDGYISKPI 104
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
514-613 2.26e-21

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: 89.79  E-value: 2.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 514 LRQILVNLLGNAVK-FTPQGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQGTGLGLAIADNLAKMM 592
Cdd:cd16943     4 LNQVLLNLLVNAAQaMEGRGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPFFTTKPVGEGTGLGLSLSYRIIQKH 83
                          90       100
                  ....*....|....*....|.
gi 1190634387 593 GGHLTVFSEPGQGSCFSLCLP 613
Cdd:cd16943    84 GGTIRVASVPGGGTRFTIILP 104
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
343-613 5.44e-21

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 97.20  E-value: 5.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 343 RLPINRIDELGHIARAYNNLLDTLNEQydtlemkvkertlalaeakraaeQANRRksDHLTTISHEIRTPLNGALGAVEL 422
Cdd:NF012163  210 RVTPTSNDELGKLAQDFNQLASTLEKN-----------------------EQMRR--DFMADISHELRTPLAVLRAELEA 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 423 LQNTpldagqMRLAETAHQCSL-----SLLAIINNLLDFSRIESGQMTLSLEKTALLPLLDQAMLTIHSQALSKSLALST 497
Cdd:NF012163  265 IQDG------IRKFTPESLDSLqaevgTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEV 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 498 FISANIPLELELDtlRLRQILVNLLGNAVKFTPQ-GRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQ 576
Cdd:NF012163  339 SLPDSSLVFGDRD--RLMQLFNNLLENSLRYTDSgGSLHISASQRPKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRN 416
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1190634387 577 ----GTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:NF012163  417 rasgGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVTLP 457
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
324-603 7.81e-21

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: 96.69  E-value: 7.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 324 PLWNFINIIGATGPQAMEPRLPINRI-DELGHIARAYNNLLDTLneqydtlemkvkertlalaeakraaEQANRRKSDHL 402
Cdd:TIGR01386 191 PLRRLSAVAARISPESLDQRLDPSRApAELRELAQSFNAMLGRL-------------------------EDAFQRLSQFS 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 403 TTISHEIRTPLNGALGAVELLQNTPLDAGQMRLAETAHQCSLS-LLAIINNLLDFSRIESGQMTLSLEKTALLPLLDQam 481
Cdd:TIGR01386 246 ADLAHELRTPLTNLLGQTQVALSQPRTGEEYREVLESNLEELErLSRMVSDMLFLARADNGQLALERVRLDLAAELAK-- 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 482 LTIHSQALSKSLALSTFISANipLELELDTLRLRQILVNLLGNAVKFTPQG-RIQLRVRRQNQTLCFTVEDTGCGIDVQH 560
Cdd:TIGR01386 324 VAEYFEPLAEERGVRIRVEGE--GLVRGDPQMFRRAISNLLSNALRHTPDGgTITVRIERRSDEVRVSVSNPGPGIPPEH 401
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1190634387 561 QQTIFQPFMQT----SDHEQGTGLGLAIADNLAKMMGGHLTVFSEPG 603
Cdd:TIGR01386 402 LSRLFDRFYRVdparSNSGEGTGLGLAIVRSIMEAHGGRASAESPDG 448
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
386-613 1.50e-20

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: 96.34  E-value: 1.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 386 EAKRAAEQAnrRKSDHLT-------TISHEIRTPLNGALGAVELLQNTPLDA---GQMRLAEtahqcsLS-LLAIINNLL 454
Cdd:COG5805   270 EKKEAEELM--ARSEKLSiagqlaaGIAHEIRNPLTSIKGFLQLLQPGIEDKeeyFDIMLSE------LDrIESIISEFL 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 455 DFSRiesgQMTLSLEKTALLPLLDQAMLTIHSQALSKSLALSTFISANIPlELELDTLRLRQILVNLLGNAVKFTPQ-GR 533
Cdd:COG5805   342 ALAK----PQAVNKEKENINELIQDVVTLLETEAILHNIQIRLELLDEDP-FIYCDENQIKQVFINLIKNAIEAMPNgGT 416
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 534 IQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSdhEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:COG5805   417 ITIHTEEEDNSVIIRVIDEGIGIPEERLKKLGEPFFTTK--EKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLP 494
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
514-613 1.91e-20

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: 87.00  E-value: 1.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 514 LRQILVNLLGNAVKFT---PQGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPF--MQTSDHEQGTGLGLAIADNL 588
Cdd:cd16921     1 LGQVLTNLLGNAIKFRrprRPPRIEVGAEDVGEEWTFYVRDNGIGIDPEYAEKVFGIFqrLHSREEYEGTGVGLAIVRKI 80
                          90       100
                  ....*....|....*....|....*
gi 1190634387 589 AKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:cd16921    81 IERHGGRIWLESEPGEGTTFYFTLP 105
PRK10604 PRK10604
sensor protein RstB; Provisional
405-622 1.95e-20

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 95.06  E-value: 1.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 405 ISHEIRTPLNGALGAVELLQNtPLDAGQMRLAETAHQcslsLLAIINNLLDFSRIESGQMTLSLEKTALLPLLDQAMLTI 484
Cdd:PRK10604  219 IAHELRTPLVRLRYRLEMSDN-LSAAESQALNRDIGQ----LEALIEELLTYARLDRPQNELHLSEPDLPAWLSTHLADI 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 485 HSQALSKSLALSTfisANIPLELELDTLRLRQILVNLLGNAVKFTpQGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTI 564
Cdd:PRK10604  294 QAVTPEKTVRLDT---PHQGDYGALDMRLMERVLDNLLNNALRYA-HSRVRVSLLLDGNQACLIVEDDGPGIPPEERERV 369
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1190634387 565 FQPFM---QTSDHEQG-TGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLPFNAITPPMP 622
Cdd:PRK10604  370 FEPFVrldPSRDRATGgCGLGLAIVHSIALAMGGSVNCDESELGGARFSFSWPVWHNLPQFT 431
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
694-816 2.99e-20

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 87.72  E-value: 2.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 694 MHILLVDDSETNRDITGMMLQQLG--HQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANIDshcm 771
Cdd:COG4565     4 IRVLIVEDDPMVAELLRRYLERLPgfEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVD---- 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1190634387 772 ITALSANASPDEQIKTSQAGMNHYLSKPVTLGQLAEMLDLTAQFQ 816
Cdd:COG4565    80 VIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYR 124
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
695-800 4.22e-20

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


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 86.01  E-value: 4.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 695 HILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPAN-----Idsh 769
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETrhipvI--- 77
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1190634387 770 cMITALSanaSPDEQIKTSQAGMNHYLSKPV 800
Cdd:cd17538    78 -MITALD---DREDRIRGLEAGADDFLSKPI 104
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
344-613 6.17e-20

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 95.14  E-value: 6.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 344 LPINRIDELGHIARAYNNLLDTLNEQYDTLEMKVKERtlALAEAKRAAEQANRRKSDHL-------TTISHEIRTPLNgA 416
Cdd:COG4192   374 IPVDGNDEIGRIARLLRVFRDQAIEKTQELETEIEER--KRIEKNLRQTQDELIQAAKMavvgqtmTSLAHELNQPLN-A 450
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 417 LGAVELLQNTPLDAGQMRLAETAHQCSLSLLA----IINNLLDFSRIESGqmtlSLEKTALLPLLDQAMLTIHSQALSKS 492
Cdd:COG4192   451 MSMYLFSAKKALEQENYAQLPTSLDKIEGLIErmdkIIKSLRQFSRKSDT----PLQPVDLRQVIEQAWELVESRAKPQQ 526
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 493 lalstfISANIPLELE--LDTLRLRQILVNLLGNAVKFTP-QGRIQLRVRRQNQTLCFTVEDTGCGIDVQhqQTIFQPFm 569
Cdd:COG4192   527 ------ITLHIPDDLMvqGDQVLLEQVLVNLLVNALDAVAtQPQISVDLLSNAENLRVAISDNGNGWPLV--DKLFTPF- 597
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1190634387 570 qTSDHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:COG4192   598 -TTTKEVGLGLGLSICRSIMQQFGGDLYLASTLERGAMVILEFN 640
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
514-612 1.35e-19

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: 84.82  E-value: 1.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 514 LRQILVNLLGNA---VKFTPQGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQGTGLGLAIADNLAK 590
Cdd:cd16976     1 IQQVLMNLLQNAldaMGKVENPRIRIAARRLGGRLVLVVRDNGPGIAEEHLSRVFDPFFTTKPVGKGTGLGLSISYGIVE 80
                          90       100
                  ....*....|....*....|..
gi 1190634387 591 MMGGHLTVFSEPGQGSCFSLCL 612
Cdd:cd16976    81 EHGGRLSVANEEGAGARFTFDL 102
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
696-799 6.63e-19

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 82.51  E-value: 6.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLG--HQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTAR-WRHDPanidsHCMI 772
Cdd:COG4753     2 VLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAiRELDP-----DTKI 76
                          90       100
                  ....*....|....*....|....*..
gi 1190634387 773 TALSANASPDEQIKTSQAGMNHYLSKP 799
Cdd:COG4753    77 IILSGYSDFEYAQEAIKLGADDYLLKP 103
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
694-800 7.56e-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: 82.87  E-value: 7.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 694 MHILLVDDSETNRDITGMMLQQLG-HQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPAniDSHC-- 770
Cdd:cd17551     1 MRILIVDDNPTNLLLLEALLRSAGyLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPG--LEDVpi 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1190634387 771 -MITalsanASPDEQIKTS--QAGMNHYLSKPV 800
Cdd:cd17551    79 vMIT-----ADTDREVRLRalEAGATDFLTKPF 106
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
694-810 6.97e-18

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 80.46  E-value: 6.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 694 MHILLVDDSETNRDITGMMLQQLGHQ-VTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANidSHCMI 772
Cdd:cd19923     1 MKVLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGAL--SHLPV 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1190634387 773 TALSANASPDEQIKTSQAGMNHYLSKPVTLGQLAEMLD 810
Cdd:cd19923    79 LMVTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLE 116
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
514-613 9.46e-18

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: 79.73  E-value: 9.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 514 LRQILVNLLGNAVKFTPQ-GRIQLRVRRQ---------------NQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQG 577
Cdd:cd16919     1 LELAILNLAVNARDAMPEgGRLTIETSNQrvdadyalnyrdlipGNYVCLEVSDTGSGMPAEVLRRAFEPFFTTKEVGKG 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1190634387 578 TGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:cd16919    81 TGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
696-800 1.08e-17

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: 79.09  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANidSHCMITAL 775
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPAT--RHIPVIFL 78
                          90       100
                  ....*....|....*....|....*
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKPV 800
Cdd:cd19920    79 TALTDTEDKVKGFELGAVDYITKPF 103
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
350-597 1.08e-17

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 87.00  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 350 DELGHIARAYNNLLDTL--NEQYdtlemkvkertlalaeakraaeqanRRksDHLTTISHEIRTPLNGALGAVELLQN-- 425
Cdd:PRK10549  217 DELGRLAQDFNQLASTLekNEQM-------------------------RR--DFMADISHELRTPLAVLRGELEAIQDgv 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 426 ---TPlDAGQMRLAETAhqcslSLLAIINNLLDFSRIESGQMTLSLEKTALLPLLDQAMLTIHSQALSKSLALSTFISAN 502
Cdd:PRK10549  270 rkfTP-ESVASLQAEVG-----TLTKLVDDLHQLSLSDEGALAYRKTPVDLVPLLEVAGGAFRERFASRGLTLQLSLPDS 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 503 IPLELELDtlRLRQILVNLLGNAVKFT-PQGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQ----G 577
Cdd:PRK10549  344 ATVFGDPD--RLMQLFNNLLENSLRYTdSGGSLHISAEQRDKTLRLTFADSAPGVSDEQLQKLFERFYRTEGSRNrasgG 421
                         250       260
                  ....*....|....*....|
gi 1190634387 578 TGLGLAIADNLAKMMGGHLT 597
Cdd:PRK10549  422 SGLGLAICLNIVEAHNGRII 441
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
397-462 2.26e-17

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 76.87  E-value: 2.26e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1190634387 397 RKSDHLTTISHEIRTPLNGALGAVELLQNTPLDAGQMRLAETAHQCSLSLLAIINNLLDFSRIESG 462
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
397-462 3.09e-17

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 76.45  E-value: 3.09e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1190634387  397 RKSDHLTTISHEIRTPLNGALGAVELLQNTPLDAGQMRLAETAHQCSLSLLAIINNLLDFSRIESG 462
Cdd:smart00388   1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
697-799 4.19e-17

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: 77.45  E-value: 4.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 697 LLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPAN---IdshcMIT 773
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDipiI----MLT 76
                          90       100
                  ....*....|....*....|....*.
gi 1190634387 774 ALSanaSPDEQIKTSQAGMNHYLSKP 799
Cdd:cd17574    77 AKD---EEEDKVLGLELGADDYITKP 99
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
510-613 5.53e-17

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: 77.53  E-value: 5.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 510 DTLRLRQILVNLLGNAVKFTPQG---RIQLRVRRQNQTLcFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQ----GTGLGL 582
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTPDGgriRCILEKFRLNRFL-LTVSDSGPGIPPNLREEIFERFRQGDGSSTrahgGTGLGL 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1190634387 583 AIADNLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:cd16925    80 SIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
475-613 5.54e-17

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 84.13  E-value: 5.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 475 PLLDQAMLTIHSQALSKSLALSTFISANIPlELELDTLRLRQILVNLLGNAV-----KFTPQGRIQLRVRRQNQTLCFTV 549
Cdd:COG3290   244 PVLAALLLGKAARARERGIDLTIDIDSDLP-DLPLSDTDLVTILGNLLDNAIeavekLPEEERRVELSIRDDGDELVIEV 322
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1190634387 550 EDTGCGIDVQHQQTIFQP-FmqTSDHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:COG3290   323 EDSGPGIPEELLEKIFERgF--STKLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLP 385
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
510-613 1.37e-16

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


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 76.35  E-value: 1.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 510 DTLRLRQILVNLLGNAVKFT-PQGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQ----GTGLGLAI 584
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTdTGGKLRIRAAQTPQEVRLDVEDSAPGVSDDQLARLFERFYRVESSRNrasgGSGLGLAI 80
                          90       100
                  ....*....|....*....|....*....
gi 1190634387 585 ADNLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:cd16946    81 CHNIALAHGGTISAEHSPLGGLRLVLTLP 109
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
693-819 3.91e-16

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: 77.69  E-value: 3.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 693 QMHILLVDDSETNRDITGMMLQQLGHQV-TRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPAnidshCM 771
Cdd:COG3707     3 GLRVLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP-----AP 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1190634387 772 ITALSANASPDEQIKTSQAGMNHYLSKPVTLGQLAEMLDLT-AQFQLER 819
Cdd:COG3707    78 VILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELAlARFRELR 126
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
405-806 5.24e-16

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 82.80  E-value: 5.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 405 ISHEIRTPLNGALGAVELLQNTpLDAGQMR---LAETAHQCSLSLLaIINNLLDFSRI-ESGQMTLSLEK--TALLPLLd 478
Cdd:PRK13837  457 IAHNFNNILGAILGYAEMALNK-LARHSRAaryIDEIISAGARARL-IIDQILAFGRKgERNTKPFDLSElvTEIAPLL- 533
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 479 qamltihSQALSKSLALStFISANIPLELELDTLRLRQILVNLLGNAVK-FTPQGRIQLRVRRQNQT------------- 544
Cdd:PRK13837  534 -------RVSLPPGVELD-FDQDQEPAVVEGNPAELQQVLMNLCSNAAQaMDGAGRVDISLSRAKLRapkvlshgvlppg 605
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 545 ----LCftVEDTGCGIDVQHQQTIFQPFMQTsdHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLPfnAITPP 620
Cdd:PRK13837  606 ryvlLR--VSDTGAGIDEAVLPHIFEPFFTT--RAGGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLP--PSSKV 679
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 621 MPfhgelfapqrlhaqlsawgmtcQPELANQPSRHFVDNalcylpgrlyaklkqylqgAETealkslplqpwqmhILLVD 700
Cdd:PRK13837  680 PV----------------------APQAFFGPGPLPRGR-------------------GET--------------VLLVE 704
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 701 DSETNRDITGMMLQQLGHQ---VTRADSGTTALAIGRQhRFDLVLMDIRMPVLDGLATTarwrHDPANIDSHCMITALSA 777
Cdd:PRK13837  705 PDDATLERYEEKLAALGYEpvgFSTLAAAIAWISKGPE-RFDLVLVDDRLLDEEQAAAA----LHAAAPTLPIILGGNSK 779
                         410       420
                  ....*....|....*....|....*....
gi 1190634387 778 NASPDEQIKTSQAgmnHYLSKPVTLGQLA 806
Cdd:PRK13837  780 TMALSPDLLASVA---EILAKPISSRTLA 805
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
510-605 5.41e-16

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


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 74.75  E-value: 5.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 510 DTLRLRQILVNLLGNAVKFTPQG-RIQLRVRRQNQTLcFTVEDTGCGIDVQHQQTIFQPFMQT-SDHEQGTGLGLAIADN 587
Cdd:cd16940    10 DALLLFLLLRNLVDNAVRYSPQGsRVEIKLSADDGAV-IRVEDNGPGIDEEELEALFERFYRSdGQNYGGSGLGLSIVKR 88
                          90
                  ....*....|....*...
gi 1190634387 588 LAKMMGGHLTVFSEPGQG 605
Cdd:cd16940    89 IVELHGGQIFLGNAQGGG 106
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
694-748 1.14e-15

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: 71.83  E-value: 1.14e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1190634387  694 MHILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMP 748
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
514-613 4.36e-15

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


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 71.71  E-value: 4.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 514 LRQILVNLLGNAVKFtpqGRIQLRVRRQ--NQTLCFTVEDTGCGIDVQHQQTIFQPFMQ--TSDHEQGTGLGLAIADNLA 589
Cdd:cd16950     1 LKRVLSNLVDNALRY---GGGWVEVSSDgeGNRTRIQVLDNGPGIAPEEVDELFQPFYRgdNARGTSGTGLGLAIVQRIS 77
                          90       100
                  ....*....|....*....|....
gi 1190634387 590 KMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:cd16950    78 DAHGGSLTLANRAGGGLCARIELP 101
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
696-809 4.89e-15

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: 72.05  E-value: 4.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAI--GRQHRFDLVLMDIRMPVLDGLATTARWRhdpANIDSHC--M 771
Cdd:cd19933     3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLlaSAEHSFQLVLLDLCMPEMDGFEVALRIR---KLFGRRErpL 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1190634387 772 ITALSANASPDEQIKTSQAGMNHYLSKPVTLGQLAEML 809
Cdd:cd19933    80 IVALTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
402-644 5.93e-15

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 79.59  E-value: 5.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 402 LTTISHEIRTPLNGALGAVELLQNTPLDAGQMRLAETAHQCSLSLLAIINNLLDFSRIESGQMTLSLEKTALLPLLDQAM 481
Cdd:PRK10618  454 LQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNMLETQDWKPEQELFSLQDLIDEVL 533
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 482 LTIHSQALSKSLALstFISANIPLELEL--DTLRLRQILVNLLGNAVKFTPQGRIQLRVRRQNQ---TLCFTVEDTGCGI 556
Cdd:PRK10618  534 PEVLPAIKRKGLQL--LIHNHLKAEQLRigDRDALRKILLLLLNYAITTTAYGKITLEVDQDESspdRLTIRILDTGAGV 611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 557 DVQHQQTIFQPFM---QTSDHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLPFNAITPPMPFHGElfapqRL 633
Cdd:PRK10618  612 SIKELDNLHFPFLnqtQGDRYGKASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLKMLAADPEVEEEEE-----KL 686
                         250       260       270
                  ....*....|....*....|....*....|
gi 1190634387 634 -------------------HAQLSAWGMTC 644
Cdd:PRK10618  687 ldgvtvllditseevrkivTRQLENWGATC 716
PRK13557 PRK13557
histidine kinase; Provisional
353-761 1.43e-14

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 77.79  E-value: 1.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 353 GHIARAYNNLLDTLNEQYDTLEMKVKERTLALAEAKRAAEQAnRRKSDHLTTISHEirtplngalgavellqntpldagq 432
Cdd:PRK13557  168 GGIAHDFNNLLQVMSGYLDVIQAALSHPDADRGRMARSVENI-RAAAERAATLTQQ------------------------ 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 433 mrlaetahqcslsllaiinnLLDFSRIESGQ-MTLSLEKtallplLDQAMLTIHSQALSKSLALSTFISANIPlELELDT 511
Cdd:PRK13557  223 --------------------LLAFARKQRLEgRVLNLNG------LVSGMGELAERTLGDAVTIETDLAPDLW-NCRIDP 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 512 LRLRQILVNLLGNAVKFTPQGRiQLRVRRQNQTL-----------------CFTVEDTGCGIDVQHQQTIFQPFMQTSDH 574
Cdd:PRK13557  276 TQAEVALLNVLINARDAMPEGG-RVTIRTRNVEIededlamyhglppgryvSIAVTDTGSGMPPEILARVMDPFFTTKEE 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 575 EQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLPF--NAITPPMPfhgelfAPQRLHAQlsawgmtcqpelanqp 652
Cdd:PRK13557  355 GKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFPAsdQAENPEQE------PKARAIDR---------------- 412
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 653 srhfvdnalcylpgrlyaklkqylQGAETealkslplqpwqmhILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAI 732
Cdd:PRK13557  413 ------------------------GGTET--------------ILIVDDRPDVAELARMILEDFGYRTLVASNGREALEI 454
                         410       420       430
                  ....*....|....*....|....*....|...
gi 1190634387 733 GRQH-RFDLVLMDIRMP-VLDG--LATTARWRH 761
Cdd:PRK13557  455 LDSHpEVDLLFTDLIMPgGMNGvmLAREARRRQ 487
envZ PRK09467
osmolarity sensor protein; Provisional
405-613 1.77e-14

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 76.87  E-value: 1.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 405 ISHEIRTPLNGALGAVELLQntpldAGQMRLAET----AHQCSlsllAIINNLLDFSRieSGQmTLSLEKTALLPLLDQA 480
Cdd:PRK09467  236 VSHDLRTPLTRIRLATEMMS-----EEDGYLAESinkdIEECN----AIIEQFIDYLR--TGQ-EMPMEMADLNALLGEV 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 481 MLTIHSQALSKSLALSTfisanIPLELELDTLRLRQILVNLLGNAVKFTpQGRIQLRVRRQNQTLCFTVEDTGCGIDVQH 560
Cdd:PRK09467  304 IAAESGYEREIETALQP-----GPIEVPMNPIAIKRALANLVVNAARYG-NGWIKVSSGTEGKRAWFQVEDDGPGIPPEQ 377
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1190634387 561 QQTIFQPFMQ--TSDHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:PRK09467  378 LKHLFQPFTRgdSARGSSGTGLGLAIVKRIVDQHNGKVELGNSEEGGLSARAWLP 432
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
514-613 1.97e-14

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: 70.15  E-value: 1.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 514 LRQILVNLLGNAVKFTpQGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQ----GTGLGLAIADNLA 589
Cdd:cd16939     1 MARALDNLLRNALRYA-HRTVRIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDratgGFGLGLAIVHRVA 79
                          90       100
                  ....*....|....*....|....
gi 1190634387 590 KMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:cd16939    80 LWHGGHVECDDSELGGACFRLTWP 103
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
504-612 2.57e-14

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: 70.23  E-value: 2.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 504 PLELELDTLRLRQILVNLLGNAVKFTPQGR-IQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHE----QGT 578
Cdd:cd16947    11 PIYANANTEALQRILKNLISNAIKYGSDGKfLGMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRnsakQGN 90
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1190634387 579 GLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCL 612
Cdd:cd16947    91 GLGLTITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
695-807 2.64e-14

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: 70.02  E-value: 2.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 695 HILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANIDSHcmITA 774
Cdd:cd17562     2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTP--ILM 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1190634387 775 LSANASPDEQIKTSQAGMNHYLSKPVTLGQLAE 807
Cdd:cd17562    80 LTTESSDEKKQEGKAAGATGWLVKPFDPEQLLE 112
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
514-613 3.50e-14

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: 69.35  E-value: 3.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 514 LRQILVNLLGNAVKFTP--QGRIQLRVRRQNQ----------TLCFTVEDTGCGIDVQHQQTIFQPFMqtSDHEQGTGLG 581
Cdd:cd16918     1 LIQVFLNLVRNAAQALAgsGGEIILRTRTQRQvtlghprhrlALRVSVIDNGPGIPPDLQDTIFYPMV--SGRENGTGLG 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1190634387 582 LAIADNLAKMMGGHLTVFSEPGQgSCFSLCLP 613
Cdd:cd16918    79 LAIAQNIVSQHGGVIECDSQPGH-TVFSVSLP 109
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
696-808 9.70e-14

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


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 68.42  E-value: 9.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHR--FDLVLMDIRMPVLDGLATTARwrhdpANIDSHCMIT 773
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKdeFDLVITDVHMPDMDGFEFLEL-----IRLEMDLPVI 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1190634387 774 ALSANASPDEQIKTSQAGMNHYLSKPVTLGQLAEM 808
Cdd:cd17584    76 MMSADGSTSTVMKGLAHGACDYLLKPVSIEDLKNI 110
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
696-807 3.07e-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: 67.15  E-value: 3.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQ-QLGHQVTR-ADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRhdpaNIDSHCMIT 773
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLEsEPDIEVVGeAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLR----RRYPDLKVI 76
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1190634387 774 ALSANASpDEQIKTS-QAGMNHYLSKPVTLGQLAE 807
Cdd:cd17535    77 VLTAHDD-PEYVLRAlKAGAAGYLLKDSSPEELIE 110
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
395-458 3.33e-13

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


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 65.31  E-value: 3.33e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1190634387 395 NRRKSDHLTTISHEIRTPLNGALGAVELLQNTPL-DAGQMRLAETAHQCSLSLLAIINNLLDFSR 458
Cdd:cd00082     1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLdDEEQREYLERIREEAERLLRLINDLLDLSR 65
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
514-613 3.50e-13

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


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 66.46  E-value: 3.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 514 LRQILVNLLGNAVKFTPQG-RIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQT----SDHEQGTGLGLAIADNL 588
Cdd:cd16952     1 LRSAFSNLVSNAVKYTPPSdTITVRWSQEESGARLSVEDTGPGIPPEHIPRLTERFYRVdierCRNTGGTGLGLAIVKHV 80
                          90       100
                  ....*....|....*....|....*
gi 1190634387 589 AKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:cd16952    81 MSRHDARLLIASELGKGSRFTCLFP 105
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
696-805 4.71e-13

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: 66.64  E-value: 4.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDsetNRDITGMM---LQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDpaniDSHCMI 772
Cdd:cd17627     1 ILVVDD---DRAVRESLrrsLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAA----GNDLPI 73
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1190634387 773 TALSANASPDEQIKTSQAGMNHYLSKPVTLGQL 805
Cdd:cd17627    74 LVLTARDSVSDRVAGLDAGADDYLVKPFALEEL 106
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
695-799 5.95e-13

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: 66.12  E-value: 5.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 695 HILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANidSHCMITA 774
Cdd:cd17618     2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMT--RDIPIIM 79
                          90       100
                  ....*....|....*....|....*
gi 1190634387 775 LSANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd17618    80 LTARGEEEDKVRGLEAGADDYITKP 104
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
696-799 8.58e-13

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: 65.48  E-value: 8.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIG---------RQHRFDLVLMDIRMPVLDGLATTARWRHDPANI 766
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLenlakegndLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1190634387 767 DSHCMItaLSANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd19924    81 NIPVIL--NSSLSGEFSRARGKKVGADAYLAKF 111
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
695-815 8.68e-13

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: 65.90  E-value: 8.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 695 HILLVDDSETNRDITGMMLQQLG--HQVTRADSGTTALAIGRQH-------RFDLVLMDIRMPVLDGLATTARWRHDPan 765
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGvpNELHVVRDGEEALDFLRGEgeyadapRPDLILLDLNMPRMDGFEVLREIKADP-- 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1190634387 766 idSHCMITA--LSANASPDEQIKTSQAGMNHYLSKPVTLGQLAEMLDLTAQF 815
Cdd:cd17557    79 --DLRRIPVvvLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSLGEY 128
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
694-760 1.20e-12

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: 65.32  E-value: 1.20e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1190634387 694 MHILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWR 760
Cdd:cd17554     1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIR 67
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
514-613 1.62e-12

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: 64.61  E-value: 1.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 514 LRQILVNllgnAVKFTPQ-GRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQP-FMQTSDHEQG--TGLGLAIADNLA 589
Cdd:cd16948    10 IGQIVSN----ALKYSKQgGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKgFTGENGRNFQesTGMGLYLVKKLC 85
                          90       100
                  ....*....|....*....|....
gi 1190634387 590 KMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:cd16948    86 DKLGHKIDVESEVGEGTTFTITFP 109
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
510-613 1.97e-12

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: 64.48  E-value: 1.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 510 DTLRLRQILVNLLGNA---VKFTPQGRIQLRVR---RQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSdhEQGTGLGLA 583
Cdd:cd16944     1 DTTQISQVLTNILKNAaeaIEGRPSDVGEVRIRveaDQDGRIVLIVCDNGKGFPREMRHRATEPYVTTR--PKGTGLGLA 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1190634387 584 IADNLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:cd16944    79 IVKKIMEEHGGRISLSNREAGGACIRIILP 108
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
695-809 2.13e-12

DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 66.48  E-value: 2.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 695 HILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLA--TTARWRHDPANIdshCMI 772
Cdd:COG4567     6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDliEALRERDPDARI---VVL 82
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1190634387 773 TALSANASPDEQIKtsqAGMNHYLSKPVTLGQLAEML 809
Cdd:COG4567    83 TGYASIATAVEAIK---LGADDYLAKPADADDLLAAL 116
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
517-613 2.58e-12

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: 63.85  E-value: 2.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 517 ILVNLLGNAV-----KFTPQGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHeQGTGLGLAIADNLAKM 591
Cdd:cd16915     4 IVGNLIDNALdalaaTGAPNKQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVFERGVSTKGQ-GERGIGLALVRQSVER 82
                          90       100
                  ....*....|....*....|..
gi 1190634387 592 MGGHLTVFSEPGQGSCFSLCLP 613
Cdd:cd16915    83 LGGSITVESEPGGGTTFSIRIP 104
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
343-615 2.97e-12

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 70.05  E-value: 2.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 343 RLPINRIDELGHIARAYNNLLDTLNEqydtLEMKVKERTLALAEAKRAAEQA--NRrksdH-----LTTISHEIRTplNG 415
Cdd:COG2972   202 RLEVSGNDEIGILARSFNEMVERIKE----LIEEVYELELEKKEAELKALQAqiNP----HflfntLNSIRWLAEL--ED 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 416 ALGAVEllqntpldagqmrlaetahqcslsllaIINNLLDFSR--IESGQMTLSL-EKTALLplldQAMLTIHSQALSKS 492
Cdd:COG2972   272 PEEAEE---------------------------MLEALSKLLRysLSKGDELVTLeEELELI----KSYLEIQKLRFGDR 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 493 LALSTFISANIpLELELDTLRLrQILVNllgNAVKF-----TPQGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQP 567
Cdd:COG2972   321 LEVEIEIDEEL-LDLLIPKLIL-QPLVE---NAIEHgiepkEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLLEE 395
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1190634387 568 FmqtSDHEQGTGLGLAIADNLAKMM---GGHLTVFSEPGQGSCFSLCLPFN 615
Cdd:COG2972   396 L---SSKGEGRGIGLRNVRERLKLYygeEYGLEIESEPGEGTTVTIRIPLE 443
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
696-801 4.57e-12

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: 63.76  E-value: 4.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANIDshcmITAL 775
Cdd:cd17555     3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTP----VIVV 78
                          90       100
                  ....*....|....*....|....*.
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKPVT 801
Cdd:cd17555    79 SGAGVMSDAVEALRLGAWDYLTKPIE 104
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
695-810 7.78e-12

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: 62.95  E-value: 7.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 695 HILLVDDSETNRDITGMMLQQL-GHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPA--NIDshcm 771
Cdd:cd17552     3 RILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPEtqSIP---- 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1190634387 772 ITALSANASPDEQIKTSQAGMNHYLSKP---VTL-GQLAEMLD 810
Cdd:cd17552    79 VILLTAKAQPSDRQRFASLGVAGVIAKPfdpLTLaEQIAKLLG 121
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
694-811 8.27e-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: 62.82  E-value: 8.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 694 MHILLVDDSETNRDITGMMLQQLGHQVT-RADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDpaNIDSHCMI 772
Cdd:cd19932     1 VRVLIAEDEALIRMDLREMLEEAGYEVVgEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSE--NIAPIVLL 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1190634387 773 TALSANaspDEQIKTSQAGMNHYLSKPVTLGQLAEMLDL 811
Cdd:cd19932    79 TAYSQQ---DLVERAKEAGAMAYLVKPFSESDLIPAIEM 114
PRK10610 PRK10610
chemotaxis protein CheY;
693-810 8.58e-12

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 63.45  E-value: 8.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 693 QMHILLVDDSETNRDITGMMLQQLG-HQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANidSHCM 771
Cdd:PRK10610    5 ELKFLVVDDFSTMRRIVRNLLKELGfNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAM--SALP 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1190634387 772 ITALSANASPDEQIKTSQAGMNHYLSKPVTLGQLAEMLD 810
Cdd:PRK10610   83 VLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLN 121
pleD PRK09581
response regulator PleD; Reviewed
696-800 1.03e-11

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 68.39  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANidSH---CMI 772
Cdd:PRK09581    5 ILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPAT--THipvVMV 82
                          90       100
                  ....*....|....*....|....*...
gi 1190634387 773 TALSanaSPDEQIKTSQAGMNHYLSKPV 800
Cdd:PRK09581   83 TALD---DPEDRVRGLEAGADDFLTKPI 107
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
696-799 1.09e-11

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: 62.01  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANIdsHCMITAL 775
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFD--TIPVIFL 78
                          90       100
                  ....*....|....*....|....
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd19927    79 TAKGMTSDRIKGYNAGCDGYLSKP 102
PRK10337 PRK10337
sensor protein QseC; Provisional
362-611 1.25e-11

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 67.75  E-value: 1.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 362 LLDTLNEQYD-TLEMKVKERtlalaeakraaeqanRRKSDhlttISHEIRTPLNGALGAVELLQnTPLDAGQMRlaetah 440
Cdd:PRK10337  219 LVEALNQLFArTHAMMVRER---------------RFTSD----AAHELRSPLAALKVQTEVAQ-LSDDDPQAR------ 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 441 QCSLSLLA--------IINNLLDFSRIESGQMTLSLEKTALLPLLDQAMLTIHSQALSkslalstfisANIPLELELDT- 511
Cdd:PRK10337  273 KKALLQLHagidratrLVDQLLTLSRLDSLDNLQDVAEIPLEDLLQSAVMDIYHTAQQ----------AGIDVRLTLNAh 342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 512 --------LRLRQILVNLLGNAVKFTPQG-RIQLRVRRQnqtlCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQ-GTGLG 581
Cdd:PRK10337  343 pvirtgqpLLLSLLVRNLLDNAIRYSPQGsVVDVTLNAR----NFTVRDNGPGVTPEALARIGERFYRPPGQEAtGSGLG 418
                         250       260       270
                  ....*....|....*....|....*....|
gi 1190634387 582 LAIADNLAKMMGGHLTVFSEPGQGSCFSLC 611
Cdd:PRK10337  419 LSIVRRIAKLHGMNVSFGNAPEGGFEAKVS 448
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
514-613 1.74e-11

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: 61.57  E-value: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 514 LRQILVNLLGNAVKFTPQgRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQ----GTGLGLAIADNLA 589
Cdd:cd16949     1 LARALENVLRNALRYSPS-KILLDISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDresgGTGLGLAIAERAI 79
                          90       100
                  ....*....|....*....|....
gi 1190634387 590 KMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:cd16949    80 EQHGGKIKASNRKPGGLRVRIWLP 103
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
696-805 2.66e-11

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: 61.60  E-value: 2.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDpaNIDSHCMItaL 775
Cdd:cd17615     2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRAD--GPDVPVLF--L 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKPVTLGQL 805
Cdd:cd17615    78 TAKDSVEDRIAGLTAGGDDYVTKPFSLEEV 107
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
514-613 2.78e-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: 60.87  E-value: 2.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 514 LRQILVNLLGNAVKFTPQG---RIQLRVRRQNQTLCF---TVEDTGCGIDVQHQQTIFQPFMQTSdhEQGTGLGLAIADN 587
Cdd:cd16920     1 IQQVLINLVRNGIEAMSEGgceRRELTIRTSPADDRAvtiSVKDTGPGIAEEVAGQLFDPFYTTK--SEGLGMGLSICRS 78
                          90       100
                  ....*....|....*....|....*.
gi 1190634387 588 LAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:cd16920    79 IIEAHGGRLSVESPAGGGATFQFTLP 104
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
694-799 3.08e-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: 3.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 694 MHILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHR-FDLVLMDIRMPVLDGLATTARWRHdpaNIDSHCM- 771
Cdd:cd17544     1 IKVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPdIKLVITDYNMPEMDGFELVREIRK---KYSRDQLa 77
                          90       100
                  ....*....|....*....|....*...
gi 1190634387 772 ITALSANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd17544    78 IIGISASGDNALSARFIKAGANDFLTKP 105
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
693-831 3.47e-11

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 66.59  E-value: 3.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 693 QMHILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWR-HDPAnIDSHCM 771
Cdd:PRK10365    5 NIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKaLNPA-IPVLIM 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 772 iTALSANASPDEQIKTsqaGMNHYLSKPVTLGQLAEMLDLTAQFQLERGVDLsPQLSEPQ 831
Cdd:PRK10365   84 -TAYSSVETAVEALKT---GALDYLIKPLDFDNLQATLEKALAHTHSIDAET-PAVTASQ 138
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
405-597 4.59e-11

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 65.37  E-value: 4.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 405 ISHEIRTPLNGALGAVELLQNTPLDAGQMRLAETAHqcslsLLAIINNLLDFSRIE----SG-QMTLSLEKTALLPLLDQ 479
Cdd:PRK10755  144 VAHELRTPLAGIRLHLELLEKQHHIDVAPLIARLDQ-----MMHTVEQLLQLARAGqsfsSGhYQTVKLLEDVILPSQDE 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 480 --AMLTIHSQALSKSLALSTFIsanipleLELDTLRLRQILVNLLGNAVKFTPQG-RIQLRVRRQNQTLCFTVEDTGCGI 556
Cdd:PRK10755  219 lsEMLEQRQQTLLLPESAADIT-------VQGDATLLRLLLRNLVENAHRYSPEGsTITIKLSQEDGGAVLAVEDEGPGI 291
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1190634387 557 DVQHQQTIFQPFMQTSDHEQGTGLGLAIADNLAKMMGGHLT 597
Cdd:PRK10755  292 DESKCGELSKAFVRMDSRYGGIGLGLSIVSRITQLHHGQFF 332
glnL PRK11073
nitrogen regulation protein NR(II);
366-613 5.86e-11

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 65.10  E-value: 5.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 366 LNEQYDTLEMKV--KERTLALAEAKRAAEQANRrksDHLTTISHEIRTPLNGALGAVELLQNTPLDAGQMRLAETAHQCS 443
Cdd:PRK11073   99 LPEGMILLEMAPmdNQRRLSQEQLQHAQQVAAR---DLVRGLAHEIKNPLGGLRGAAQLLSKALPDPALTEYTKVIIEQA 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 444 LSLLAIINNLLDFSRIESGQMT---LSLEKTALLPLLDqamltihsqaLSKSLALSTFISANIPlELELDTLRLRQILVN 520
Cdd:PRK11073  176 DRLRNLVDRLLGPQRPGTHVTEsihKVAERVVQLVSLE----------LPDNVRLIRDYDPSLP-ELAHDPDQIEQVLLN 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 521 LLGNAVKFTPQ--GRIQLRVRRQNQTLC----------FTVEDTGCGIDVQHQQTIFQPFMqtSDHEQGTGLGLAIADNL 588
Cdd:PRK11073  245 IVRNALQALGPegGTITLRTRTAFQLTLhgeryrlaarIDIEDNGPGIPPHLQDTLFYPMV--SGREGGTGLGLSIARNL 322
                         250       260
                  ....*....|....*....|....*
gi 1190634387 589 AKMMGGHLTVFSEPGQgSCFSLCLP 613
Cdd:PRK11073  323 IDQHSGKIEFTSWPGH-TEFSVYLP 346
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
694-805 6.77e-11

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: 60.15  E-value: 6.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 694 MHILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRhdpaNIDSHCMIT 773
Cdd:cd17563     1 KSLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLR----ALQPDARIV 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1190634387 774 ALSANASpdeqIKTS-QA---GMNHYLSKPVTLGQL 805
Cdd:cd17563    77 VLTGYAS----IATAvEAiklGADDYLAKPADADEI 108
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
343-613 9.49e-11

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: 65.53  E-value: 9.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 343 RLPINRI-DELGHIARAYNNLLDTLNEQYDTLE-MKVKertlalaeakraaeqanrrksdhlttISHEIRTPLNGALGAV 420
Cdd:TIGR03785 454 AIPASRSrDEIGDLSRSFAQMVARLRQYTHYLEnMSSR--------------------------LSHELRTPVAVVRSSL 507
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 421 ELLQNTPLDAGQMRLAETAHQCSLSLLAIINNLLDFSRIEsgQMTLSLEKTAlLPLldqamltihSQALSKSLALSTFIS 500
Cdd:TIGR03785 508 ENLELQALEQEKQKYLERAREGTERLSMILNNMSEATRLE--QAIQSAEVED-FDL---------SEVLSGCMQGYQMTY 575
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 501 ANIPLELELD----TLR-----LRQILVNLLGNAVKFTPQ-GRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFM- 569
Cdd:TIGR03785 576 PPQRFELNIPetplVMRgspelIAQMLDKLVDNAREFSPEdGLIEVGLSQNKSHALLTVSNEGPPLPEDMGEQLFDSMVs 655
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1190634387 570 --QTSDHEQG-TGLGLAIADNLAKMMGGHLTVFSEP-GQGSCFSLCLP 613
Cdd:TIGR03785 656 vrDQGAQDQPhLGLGLYIVRLIADFHQGRIQAENRQqNDGVVFRISLP 703
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
694-758 1.02e-10

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: 60.29  E-value: 1.02e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1190634387 694 MHILLVDDSETNRDITGMMLQQLG--HQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTAR 758
Cdd:COG2197     2 IRVLIVDDHPLVREGLRALLEAEPdiEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRR 68
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
696-760 1.76e-10

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


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 59.05  E-value: 1.76e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWR 760
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIK 65
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
514-613 2.09e-10

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


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 58.74  E-value: 2.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 514 LRQILVNLLGNAVKFTP--QGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFM----QTSDHEQGTGLGLAIADN 587
Cdd:cd16953     1 LGQVLRNLIGNAISFSPpdTGRITVSAMPTGKMVTISVEDEGPGIPQEKLESIFDRFYterpANEAFGQHSGLGLSISRQ 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1190634387 588 LAKMMGGHLTV--FSEPGQ--GSCFSLCLP 613
Cdd:cd16953    81 IIEAHGGISVAenHNQPGQviGARFTVQLP 110
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
510-603 2.57e-10

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: 58.24  E-value: 2.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 510 DTLRLRQILVNLLGNAVKFTPQ-GRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFM---QTSDHEQGTGLGLAIA 585
Cdd:cd16945     1 DPFLLRQAINNLLDNAIDFSPEgGLIALQLEADTEGIELLVFDEGSGIPDYALNRVFERFYslpRPHSGQKSTGLGLAFV 80
                          90
                  ....*....|....*...
gi 1190634387 586 DNLAKMMGGHLTVFSEPG 603
Cdd:cd16945    81 QEVAQLHGGRITLRNRPD 98
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
510-612 3.59e-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: 58.62  E-value: 3.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 510 DTLRLRQILVNLLGNAVKFT-PQGRIQLRVR---------------------RQNQTLCFTVEDTGCGidvqhQQTIFQP 567
Cdd:cd16938     8 DERRVFQVLLHMLGNLLKMRnGGGNITFRVFleggsedrsdrdwgpwrpsmsDESVEIRFEVEINDSG-----SPSIESA 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1190634387 568 FMQTS------DHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCL 612
Cdd:cd16938    83 SMRNSlnrrynLSELGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
697-805 6.85e-10

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: 57.23  E-value: 6.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 697 LLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHdpANIDSHC-MITAL 775
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLRE--EGIETPVlLLTAL 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1190634387 776 SANAspdEQIKTSQAGMNHYLSKPVTLGQL 805
Cdd:cd17625    79 DAVE---DRVKGLDLGADDYLPKPFSLAEL 105
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
696-799 7.14e-10

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 57.34  E-value: 7.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDP--ANIDShCMIT 773
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPdlKDIPV-ILLT 79
                          90       100
                  ....*....|....*....|....*.
gi 1190634387 774 ALSanaSPDEQIKTSQAGMNHYLSKP 799
Cdd:cd17598    80 TLS---DPRDVIRGLECGADNFITKP 102
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
694-810 8.65e-10

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 60.22  E-value: 8.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 694 MHILLVDDSETNRDITGMMLQQLG--HQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDG--LATTARWRHDPANI--- 766
Cdd:COG3279     2 MKILIVDDEPLARERLERLLEKYPdlEVVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGfeLARQLRELDPPPPIift 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1190634387 767 ---DSHcMITALSANASpdeqiktsqagmnHYLSKPVTLGQLAEMLD 810
Cdd:COG3279    82 tayDEY-ALEAFEVNAV-------------DYLLKPIDEERLAKALE 114
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
696-809 9.13e-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: 57.35  E-value: 9.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDitGM--MLQQLGHQVTR---ADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDpaNIDSHC 770
Cdd:cd17536     1 VLIVDDEPLIRE--GLkkLIDWEELGFEVvgeAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIREL--YPDIKI 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1190634387 771 MI-----------TALSANASpdeqiktsqagmnHYLSKPVTLGQLAEML 809
Cdd:cd17536    77 IIlsgyddfeyaqKAIRLGVV-------------DYLLKPVDEEELEEAL 113
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
696-800 1.06e-09

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: 56.90  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLG-HQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGL-ATTARWRHDP-ANIdshCMI 772
Cdd:cd17542     3 VLIVDDAAFMRMMLKDILTKAGyEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIeALKEIKKIDPnAKV---IMC 79
                          90       100
                  ....*....|....*....|....*...
gi 1190634387 773 TALSANASPDEQIKtsqAGMNHYLSKPV 800
Cdd:cd17542    80 SAMGQEEMVKEAIK---AGAKDFIVKPF 104
PRK15115 PRK15115
response regulator GlrR; Provisional
695-810 1.53e-09

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 61.39  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 695 HILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANIDshcmITA 774
Cdd:PRK15115    7 HLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMP----VII 82
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1190634387 775 LSANASPDEQIKTSQAGMNHYLSKPVTLGQLAEMLD 810
Cdd:PRK15115   83 LTAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAID 118
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
495-619 1.96e-09

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 61.07  E-value: 1.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 495 LSTFISANIPLELELDTLRLRQ-------ILVN-LLGNAVKF----TPQGRIQLRVRRQNQTLCFTVEDTGCGIDvqhqq 562
Cdd:COG3920   373 RDSYGGRGIRIELDGPDVELPAdaavplgLILNeLVTNALKHaflsGEGGRIRVSWRREDGRLRLTVSDNGVGLP----- 447
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1190634387 563 tifqpfmQTSDHEQGTGLGLAIADNLAKMMGGHLTVfsEPGQGSCFSLCLPFNAITP 619
Cdd:COG3920   448 -------EDVDPPARKGLGLRLIRALVRQLGGTLEL--DRPEGTRVRITFPLAELAA 495
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
517-614 2.10e-09

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 61.08  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 517 ILVNLLGN---AVKFTPQGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDheQGTGLGLAIADNLAKMMG 593
Cdd:PRK11086  437 ILGNLIENaleAVGGEEGGEISVSLHYRNGWLHCEVSDDGPGIAPDEIDAIFDKGYSTKG--SNRGVGLYLVKQSVENLG 514
                          90       100
                  ....*....|....*....|.
gi 1190634387 594 GHLTVFSEPGQGSCFSLCLPF 614
Cdd:PRK11086  515 GSIAVESEPGVGTQFFVQIPW 535
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
696-816 2.23e-09

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 60.63  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWR-HDPANidshcMITA 774
Cdd:PRK11361    7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRsHETRT-----PVIL 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1190634387 775 LSANASPDEQIKTSQAGMNHYLSKPVTLGQLAEMLDLTAQFQ 816
Cdd:PRK11361   82 MTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQ 123
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
696-799 2.30e-09

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


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 55.52  E-value: 2.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHdpANIDSHCMItaL 775
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRA--AGKQTPVLM--L 76
                          90       100
                  ....*....|....*....|....
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd19935    77 TARDSVEDRVKGLDLGADDYLVKP 100
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
696-820 2.54e-09

phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex aeolicus and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include Aquifex aeolicus NtrC1 and Vibrio quorum-sensing signal integrator LuxO. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 56.05  E-value: 2.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLA--TTARWRHDPANIdshCMIT 773
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEilKWIQERSLPTSV---IVIT 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1190634387 774 alsANASPDEQIKTSQAGMNHYLSKPVTlgqlAEMLDLTAQFQLERG 820
Cdd:cd17572    78 ---AHGSVDIAVEAMRLGAYDFLEKPFD----ADRLRVTVRNALKHR 117
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
696-753 3.79e-09

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


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 55.49  E-value: 3.79e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGL 753
Cdd:cd17569     3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGA 60
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
696-805 4.74e-09

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: 55.11  E-value: 4.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLV-DDSETNRDITgMMLQQLGHQVTR-ADSGTTALAIGRQHRFDLVLMDIRMP-VLDGLATTARWRHdpaniDSHCMI 772
Cdd:cd17534     3 ILIVeDEAIIALDLK-EILESLGYEVVGiADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIRE-----KFDIPV 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1190634387 773 TALSANASPD--EQIK-TSQAGmnhYLSKPVTLGQL 805
Cdd:cd17534    77 IFLTAYSDEEtlERAKeTNPYG---YLVKPFNEREL 109
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
696-799 4.95e-09

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: 54.98  E-value: 4.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLV-DDSETNRDITGMMLQQlGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANIDshcmITA 774
Cdd:cd19934     1 LLLVeDDALLAAQLKEQLSDA-GYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATP----VLI 75
                          90       100
                  ....*....|....*....|....*
gi 1190634387 775 LSANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd19934    76 LTARDSWQDKVEGLDAGADDYLTKP 100
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
696-806 5.00e-09

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: 54.80  E-value: 5.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHdpANIDSHCMItaL 775
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRR--QGQSLPVLI--L 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKPVTLGQLA 806
Cdd:cd17624    77 TARDGVDDRVAGLDAGADDYLVKPFALEELL 107
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
696-799 6.36e-09

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: 54.09  E-value: 6.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTAR---WRHDPanidshcmI 772
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRlreWSAVP--------V 72
                          90       100
                  ....*....|....*....|....*..
gi 1190634387 773 TALSANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd17620    73 IVLSARDEESDKIAALDAGADDYLTKP 99
orf27 CHL00148
Ycf27; Reviewed
693-799 8.73e-09

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 57.03  E-value: 8.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 693 QMHILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHdpaniDSHCMI 772
Cdd:CHL00148    6 KEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRK-----ESDVPI 80
                          90       100
                  ....*....|....*....|....*..
gi 1190634387 773 TALSANASPDEQIKTSQAGMNHYLSKP 799
Cdd:CHL00148   81 IMLTALGDVSDRITGLELGADDYVVKP 107
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
506-613 9.12e-09

Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some hybrid sensor histidine kinases; This family includes the cytoplasmic histidine kinase (HK) CheA, a transmembrane receptor which, together with cytoplasmic adaptor protein (CheW), forms the lattice at the core of the chemosensory array that controls the cellular chemotaxis of motile bacteria and archaea. CheA forms a two-component signal transduction system (TCS) with the response regulator CheY. Proteins having this CheA-like HATPase domain generally also have a histidine-phosphotransfer domain, a histidine kinase homodimeric domain, and a regulatory domain; some are hybrid sensor histidine kinases as they contain a REC signal receiver domain.


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 56.05  E-value: 9.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 506 ELELDTLRLRQI---LVNLLGNAV--------------KfTPQGRIQLRVRRQNQTLCFTVEDTGCGI------------ 556
Cdd:cd16916    28 DTELDKSVLEKLadpLTHLLRNAVdhgieapeerlaagK-PPEGTITLRAEHQGNQVVIEVSDDGRGIdrekirekaier 106
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1190634387 557 ------------DVQHQQTIFQPFMQTSDHE---QGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:cd16916   107 glitadeaatlsDDEVLNLIFAPGFSTAEQVtdvSGRGVGMDVVKRSIESLGGTIEVESEPGQGTTFTIRLP 178
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
695-805 1.24e-08

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 53.93  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 695 HILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHdpaniDSHCMITA 774
Cdd:cd17619     2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELRE-----QSEVGIIL 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1190634387 775 LSANASPDEQIKTSQAGMNHYLSKPVTLGQL 805
Cdd:cd17619    77 VTGRDDEVDRIVGLEIGADDYVTKPFNPREL 107
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
694-758 1.46e-08

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: 53.93  E-value: 1.46e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1190634387 694 MHILLVDDSETNRDITGMMLQQL-GHQV-TRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTAR 758
Cdd:cd17541     1 IRVLIVDDSAVMRKLLSRILESDpDIEVvGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRR 67
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
473-609 1.71e-08

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: 53.79  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 473 LLPLLDQAMLTIHSqalSKSLALSTFISANIPLELELDTLRlrQILVNLLGNAVKFTpQGRIQLRVRRQNQTLCFTVEDT 552
Cdd:cd16954     2 LLDSLCSALNKVYQ---RKGVSISLDISPELRFPGERNDLM--ELLGNLLDNACKWC-LEFVEVTARQTDGGLHLIVDDD 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1190634387 553 GCGIDVQHQQTIFQPFMQTSDHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFS 609
Cdd:cd16954    76 GPGVPESQRSKIFQRGQRLDEQRPGQGLGLAIAKEIVEQYGGELSLSDSPLGGARFE 132
PRK10816 PRK10816
two-component system response regulator PhoP;
694-843 1.90e-08

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 55.90  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 694 MHILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANIDshcmIT 773
Cdd:PRK10816    1 MRVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLP----IL 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1190634387 774 ALSANASPDEQIKTSQAGMNHYLSKPVTLGQLAEMLdltaQFQLERGVDLSPQLSEPQP-LLDLADSALSL 843
Cdd:PRK10816   77 VLTARESWQDKVEVLSAGADDYVTKPFHIEEVMARM----QALMRRNSGLASQVISLPPfQVDLSRRELSI 143
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
402-613 1.94e-08

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 57.63  E-value: 1.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 402 LTTISHEIRTPLNGALGAVELLQNTPLDAGQMRLAETAHQcslSLLAIINNLLDFSRIesgQMTLSLEKTAL-LPLLDQA 480
Cdd:PRK09470  247 LSDISHELRTPLTRLQLATALLRRRQGESKELERIETEAQ---RLDSMINDLLVLSRN---QQKNHLERETFkANSLWSE 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 481 ML---TIHSQALSKSLALST-----FISANIPLeleldtlrLRQILVNLLGNAVKFTpQGRIQLRVRRQNQTLCFTVEDT 552
Cdd:PRK09470  321 VLedaKFEAEQMGKSLTVSAppgpwPINGNPNA--------LASALENIVRNALRYS-HTKIEVAFSVDKDGLTITVDDD 391
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1190634387 553 GCGIDVQHQQTIFQPFMQTSD----HEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:PRK09470  392 GPGVPEEEREQIFRPFYRVDEardrESGGTGLGLAIVENAIQQHRGWVKAEDSPLGGLRLTIWLP 456
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
697-799 2.00e-08

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: 53.05  E-value: 2.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 697 LLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANidSHCMITALS 776
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKT--SSIPIIMLT 78
                          90       100
                  ....*....|....*....|...
gi 1190634387 777 ANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd19937    79 AKGEEFDKVLGLELGADDYITKP 101
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
694-809 2.51e-08

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: 52.92  E-value: 2.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 694 MHILLVDDSETNRDITGMMLQQ-LGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRhdpaNIDSHCMI 772
Cdd:cd17593     1 MKVLICDDSSMARKQLARALPAdWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALP----VEQLETKV 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1190634387 773 TALSANASPDEQIKTSQAGMNHYLSKPVTLGQLAEML 809
Cdd:cd17593    77 IVVSGDVQPEAKERVLELGALAFLKKPFDPEKLAQLL 113
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
695-810 2.68e-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: 53.02  E-value: 2.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 695 HILLVDDSETNRDITGMMLQQLG--HQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLA--TTARWRHDPANIdshC 770
Cdd:cd19925     2 NVLIVEDDPMVAEIHRAYVEQVPgfTVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDllRELRAAGHDVDV---I 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1190634387 771 MITAlsanASPDEQIKTS-QAGMNHYLSKPVTLGQLAEMLD 810
Cdd:cd19925    79 VVTA----ANDVETVREAlRLGVVDYLIKPFTFERLRQRLE 115
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
696-799 4.91e-08

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 52.03  E-value: 4.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLV-DDSETNRDITgMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRhdPANIDSHCMIta 774
Cdd:cd17616     1 VLLIeDDSATAQSIE-LMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLR--LAKVKTPILI-- 75
                          90       100
                  ....*....|....*....|....*
gi 1190634387 775 LSANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd17616    76 LSGLADIEDKVKGLGFGADDYMTKP 100
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
696-799 9.65e-08

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


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 51.12  E-value: 9.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANIDshcmITAL 775
Cdd:cd19919     3 VWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLP----VIIM 78
                          90       100
                  ....*....|....*....|....
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd19919    79 TAHSDLDSAVSAYQGGAFEYLPKP 102
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
397-613 1.49e-07

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 55.16  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 397 RKSDHLTTISHEIRTPLNGALGAVELLqntpldagqmrLAETAHQCSLSLLaIINNLLDFSRIE---SGQMTLSLEKTAL 473
Cdd:PRK09835  261 RQSNFSADIAHEIRTPITNLITQTEIA-----------LSQSRSQKELEDV-LYSNLEELTRMAkmvSDMLFLAQADNNQ 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 474 LpLLDQAMLTIHSQALSkslaLSTFISA-----NIPLELEL-------DTLRLRQILVNLLGNAVKFTPQG-RIQLRVRR 540
Cdd:PRK09835  329 L-IPEKKMLDLADEVGK----VFDFFEAwaeerGVELRFVGdpcqvagDPLMLRRAISNLLSNALRYTPAGeAITVRCQE 403
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1190634387 541 QNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQ----GTGLGLAIADNLAKMMGGHLTVFSEPgQGSCFSLCLP 613
Cdd:PRK09835  404 VDHQVQLVVENPGTPIAPEHLPRLFDRFYRVDPSRQrkgeGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRFVISLP 479
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
696-799 1.57e-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: 50.19  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHR-FDLVLMDIRMPVLDGLATTARWRhdpaNIDSHCMITA 774
Cdd:cd18160     2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKdIDIVVTDIVMPEMDGIELAREAR----KIDPDVKILF 77
                          90       100
                  ....*....|....*....|....*
gi 1190634387 775 LSANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd18160    78 ISGGAAAAPELLSDAVGDNATLKKP 102
PRK11517 PRK11517
DNA-binding response regulator HprR;
694-805 2.11e-07

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 52.59  E-value: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 694 MHILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDG---LATTARWRHDPanidshc 770
Cdd:PRK11517    1 MKILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGwqiLQTLRTAKQTP------- 73
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1190634387 771 mITALSANASPDEQIKTSQAGMNHYLSKPVTLGQL 805
Cdd:PRK11517   74 -VICLTARDSVDDRVRGLDSGANDYLVKPFSFSEL 107
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
696-800 2.14e-07

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 50.04  E-value: 2.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQH-RFDLVLMDIRMP-VLDG--LATTARWRHDPANIdshCM 771
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGpDIDLLVTDVIMPgGMNGsqLAEEARRRRPDLKV---LL 77
                          90       100
                  ....*....|....*....|....*....
gi 1190634387 772 ITALSANASPDEQIktsQAGMNhYLSKPV 800
Cdd:cd18161    78 TSGYAENAIEGGDL---APGVD-VLSKPF 102
PRK09483 PRK09483
response regulator; Provisional
696-798 2.43e-07

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 52.42  E-value: 2.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNR--------DITGMMLqqlghqVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATT---ARWRHDPA 764
Cdd:PRK09483    4 VLLVDDHELVRagirrileDIKGIKV------VGEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATrkiLRYTPDVK 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1190634387 765 NIdshcMITALSANASPdeqIKTSQAGMNHYLSK 798
Cdd:PRK09483   78 II----MLTVHTENPLP---AKVMQAGAAGYLSK 104
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
510-598 2.93e-07

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: 49.77  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 510 DTLRLRQILVNLLGNAVKFTPQGR-IQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQ--TSDHEQG-TGLGLAIA 585
Cdd:cd16975     1 DTLLLSRALINIISNACQYAPEGGtVSISIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRddTSRRSGGhYGMGLYIA 80
                          90
                  ....*....|...
gi 1190634387 586 DNLAKMMGGHLTV 598
Cdd:cd16975    81 KNLVEKHGGSLII 93
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
376-616 3.34e-07

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 52.70  E-value: 3.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 376 KVKERTLALAEAKRAAEQANRRK--SD-------HLTTISHEIRtplngalGAVELLQNTPLDAGQM--RLAETAHQCSL 444
Cdd:COG4585    34 RAAELERELAARAEEAREEERRRiaRElhdgvgqSLSAIKLQLE-------AARRLLDADPEAAREEleEIRELAREALA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 445 SLLAIINNLldfsriesgqMTLSLEKTALLPLLDQAMLTIHSQAlskSLALSTFISAN---IPLELELDTLRlrqILVNL 521
Cdd:COG4585   107 ELRRLVRGL----------RPPALDDLGLAAALEELAERLLRAA---GIRVELDVDGDpdrLPPEVELALYR---IVQEA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 522 LGNAVKFTPQGRIQLRVRRQNQTLCFTVEDTGCGIDVqhqqtifqpfmqtsDHEQGTGLGLAIADNLAKMMGGHLTVFSE 601
Cdd:COG4585   171 LTNALKHAGATRVTVTLEVDDGELTLTVRDDGVGFDP--------------EAAPGGGLGLRGMRERAEALGGTLTIGSA 236
                         250
                  ....*....|....*
gi 1190634387 602 PGQGSCFSLCLPFNA 616
Cdd:COG4585   237 PGGGTRVRATLPLAA 251
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
696-805 4.33e-07

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: 49.34  E-value: 4.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHdpaniDSHCMITAL 775
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRK-----TSNVPIIML 75
                          90       100       110
                  ....*....|....*....|....*....|
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKPVTLGQL 805
Cdd:cd17614    76 TAKDSEVDKVLGLELGADDYVTKPFSNREL 105
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
696-805 6.23e-07

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 49.09  E-value: 6.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRhdpaNIDSHCMITAL 775
Cdd:cd17553     3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMK----VIDENIRVIIM 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKPVTLGQL 805
Cdd:cd17553    79 TAYGELDMIQESKELGALTHFAKPFDIDEI 108
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
514-613 6.30e-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: 6.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 514 LRQILVNLLGNAVKFTPQ-GRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQ--TSDHEQGTGLGLAIADNLAK 590
Cdd:cd16923     1 LQRVFSNLLSNAIKYSPEnTRIYITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRgdNSRNTEGAGLGLSIAKAIIE 80
                          90       100
                  ....*....|....*....|...
gi 1190634387 591 MMGGHLTVFSEpGQGSCFSLCLP 613
Cdd:cd16923    81 LHGGSASAEYD-DNHDLFKVRLP 102
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
696-763 6.95e-07

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: 49.03  E-value: 6.95e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRH-DP 763
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRElDP 69
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
696-799 1.47e-06

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: 47.85  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHdpaniDSHCMITAL 775
Cdd:cd17626     3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRA-----ESGVPIVML 77
                          90       100
                  ....*....|....*....|....
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd17626    78 TAKSDTVDVVLGLESGADDYVAKP 101
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
694-780 1.48e-06

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 51.42  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 694 MHILLVDDSETNRDI-TGMMLQQLGHQV--TRADsGTTALAIGRQHRFDLVLMDIRMPVLDGLATTAR-WRHDPANIdsh 769
Cdd:PRK12555    1 MRIGIVNDSPLAVEAlRRALARDPDHEVvwVATD-GAQAVERCAAQPPDVILMDLEMPRMDGVEATRRiMAERPCPI--- 76
                          90
                  ....*....|..
gi 1190634387 770 CMITAL-SANAS 780
Cdd:PRK12555   77 LIVTSLtERNAS 88
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
514-613 1.66e-06

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


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 46.78  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 514 LRQILVNLLGNAVKFTPQGRIQLRVRRQNQTLCFTVEDTGCGIDVqhqqtifqpfmqtSDHEQGTGLGLAIADNLAKMMG 593
Cdd:cd16917     1 LYRIVQEALTNALKHAGASRVRVTLSYTADELTLTVVDDGVGFDG-------------PAPPGGGGFGLLGMRERAELLG 67
                          90       100
                  ....*....|....*....|
gi 1190634387 594 GHLTVFSEPGQGSCFSLCLP 613
Cdd:cd16917    68 GTLTIGSRPGGGTRVTARLP 87
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
696-799 1.76e-06

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: 47.19  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHdpaniDSHCMITAL 775
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRA-----RSNVPVIMV 75
                          90       100
                  ....*....|....*....|....
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd17621    76 TAKDSEIDKVVGLELGADDYVTKP 99
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
696-799 2.31e-06

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: 47.30  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHdpaniDSHCMITAL 775
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRK-----TSQVPVLML 75
                          90       100
                  ....*....|....*....|....
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd17623    76 TARGDDIDRILGLELGADDYLPKP 99
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
530-619 3.50e-06

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 50.95  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 530 PQGRIQLRVRRQNQTLCFTVEDTGCGIDVQH------------------------QQTIFQP-FmqtSDHEQ-----GTG 579
Cdd:COG0643   307 ETGTITLSAYHEGGRVVIEVSDDGRGLDLEKirakaiekglitaeeaaalsdeelLELIFAPgF---STAEEvtdlsGRG 383
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1190634387 580 LGLAI-ADNLAKMmGGHLTVFSEPGQGSCFSLCLPFN-AITP 619
Cdd:COG0643   384 VGMDVvKTNIEAL-GGTIEIESEPGKGTTFTLRLPLTlAIID 424
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
695-754 4.82e-06

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


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 48.17  E-value: 4.82e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 695 HILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLA 754
Cdd:COG4566     1 TVYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLE 60
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
696-799 6.86e-06

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: 45.68  E-value: 6.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDsetNRDITGMMLQQLGHQ-----VTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDpaNIDSHC 770
Cdd:cd17561     4 VLIADD---NREFVQLLEEYLNSQpdmevVGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRM--RLEKRP 78
                          90       100
                  ....*....|....*....|....*....
gi 1190634387 771 MITALSANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd17561    79 KIIMLTAFGQEDITQRAVELGASYYILKP 107
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
847-919 9.10e-06

Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072).


Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 44.65  E-value: 9.10e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1190634387 847 QSLQVLIQQAKDAI--ENLPVLSHTLHTIKGCAGQAGLIELQDAVIQLEHALDTHE-TLTQQEIIQLDEIIHVLLQ 919
Cdd:pfam01627   8 EEAPELLEQLEQALdaEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLLREGElPLDPELLEALRDLLEALRA 83
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
693-760 9.59e-06

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 47.65  E-value: 9.59e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1190634387 693 QMHILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWR 760
Cdd:PRK11083    3 QPTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLL 70
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
510-614 1.04e-05

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 45.67  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 510 DTLRLRQILVNLLGNAVK----FTPQGRIQLRVRRQNQTLCFTVEDTGCGIDVQHqqtIFQPFmqtsDHEQGTGLGLAIA 585
Cdd:COG2172    31 DADDLVLAVSEAVTNAVRhaygGDPDGPVEVELELDPDGLEIEVRDEGPGFDPED---LPDPY----STLAEGGRGLFLI 103
                          90       100
                  ....*....|....*....|....*....
gi 1190634387 586 DNLAKmmggHLTVFSEPGqGSCFSLCLPF 614
Cdd:COG2172   104 RRLMD----EVEYESDPG-GTTVRLVKRL 127
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
696-800 1.13e-05

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: 45.45  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLaTTARWRHDPANIDshcmITAL 775
Cdd:cd17622     3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGL-TLCRDLRPKYQGP----ILLL 77
                          90       100
                  ....*....|....*....|....*
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKPV 800
Cdd:cd17622    78 TALDSDIDHILGLELGADDYVVKPV 102
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
695-753 1.35e-05

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 45.28  E-value: 1.35e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1190634387 695 HILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGL 753
Cdd:cd17537     2 TVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGL 60
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
696-799 1.67e-05

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: 44.97  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHdpaniDSHCMITAL 775
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQ-----ISNVPIIFI 75
                          90       100
                  ....*....|....*....|....
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd18159    76 SSRDDNMDQVMAINMGGDDYITKP 99
PRK10766 PRK10766
two-component system response regulator TorR;
695-805 2.62e-05

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 46.57  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 695 HILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHdpaniDSHCMITA 774
Cdd:PRK10766    4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRS-----RSTVGIIL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1190634387 775 LSANASPDEQIKTSQAGMNHYLSKPVTLGQL 805
Cdd:PRK10766   79 VTGRTDSIDRIVGLEMGADDYVTKPLELREL 109
PRK15479 PRK15479
transcriptional regulator TctD;
694-805 2.95e-05

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 46.25  E-value: 2.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 694 MHILLVDDsetNRDITGMM---LQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANIDshc 770
Cdd:PRK15479    1 MRLLLAED---NRELAHWLekaLVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLP--- 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1190634387 771 mITALSANASPDEQIKTSQAGMNHYLSKPVTLGQL 805
Cdd:PRK15479   75 -VLLLTARSAVADRVKGLNVGADDYLPKPFELEEL 108
ompR PRK09468
osmolarity response regulator; Provisional
695-799 3.05e-05

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 46.51  E-value: 3.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 695 HILLVDDSETNRDITGMMLQQLGHQV-TRADSGTTALAIGRQHrFDLVLMDIRMPVLDGLATTARWRHDPANIDshcmIT 773
Cdd:PRK09468    7 KILVVDDDMRLRALLERYLTEQGFQVrSAANAEQMDRLLTRES-FHLMVLDLMLPGEDGLSICRRLRSQNNPTP----II 81
                          90       100
                  ....*....|....*....|....*.
gi 1190634387 774 ALSANASPDEQIKTSQAGMNHYLSKP 799
Cdd:PRK09468   82 MLTAKGEEVDRIVGLEIGADDYLPKP 107
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
696-800 3.33e-05

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 43.80  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQ--LGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRhdpaNIDSHCMIT 773
Cdd:cd17565     1 FYIVDDDKNIIKILSDIIEDddLGEVVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLK----DTGSNGKFI 76
                          90       100
                  ....*....|....*....|....*..
gi 1190634387 774 ALSANASPDEQIKTSQAGMNHYLSKPV 800
Cdd:cd17565    77 MISQVSDKEMIGKAYQAGIEFFINKPI 103
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
720-807 3.83e-05

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 43.80  E-value: 3.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 720 VTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANidshCMITALSANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd19930    27 VAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPD----TKVLIVTTFGRPGYFRRALAAGVDGYVLKD 102

                  ....*...
gi 1190634387 800 VTLGQLAE 807
Cdd:cd19930   103 RPIEELAD 110
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
696-799 4.48e-05

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


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 43.26  E-value: 4.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANIDshcmITAL 775
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLP----IIVM 76
                          90       100
                  ....*....|....*....|....
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd19928    77 SAQNTLMTAVKAAERGAFEYLPKP 100
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
696-753 4.73e-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: 43.68  E-value: 4.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGH--QVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGL 753
Cdd:cd17532     1 ALIVDDEPLAREELRYLLEEHPDieIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGL 60
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
696-799 5.51e-05

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 43.13  E-value: 5.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHdpANIDSHCMITAL 775
Cdd:cd17602     1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRK--SSALKDTPIIML 78
                          90       100
                  ....*....|....*....|....
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd17602    79 TGKDGLVDRIRAKMAGASGYLTKP 102
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
695-800 6.50e-05

phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; Acinetobacter baumannii BfmR is part of the BfmR/S two-component system that functions as the master regulator of biofilm initiation. BfmR confers resistance to complement-mediated bactericidal activity, independent of capsular polysaccharide, and also increases resistance to the clinically important antimicrobials meropenem and colistin, making it a potential antimicrobial target. Its inhibition would have the dual benefit of significantly decreasing in vivo survival and increasing sensitivity to selected antimicrobials. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 43.13  E-value: 6.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 695 HILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHdpaniDSHCMITA 774
Cdd:cd19939     1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVRE-----HSHVPILM 75
                          90       100
                  ....*....|....*....|....*.
gi 1190634387 775 LSANASPDEQIKTSQAGMNHYLSKPV 800
Cdd:cd19939    76 LTARTEEMDRVLGLEMGADDYLCKPF 101
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
343-542 6.53e-05

Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 46.42  E-value: 6.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 343 RLPINRIDELGHIARAYNNLLDTLNEQYDTLEmkvkertlaLAEAKRAAEQANRRKSDHLTTISHEIRTPLNGALGAVEL 422
Cdd:COG3850   164 RVPVSGRDELGTLARAFNRMADELQELYAELE---------EEEELEAELELLALLDELLLLAALLLLLALLLALLLAAL 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 423 LQNTPLDAGQMRLAETAHQCSLSLLAIINNLLDFSRIESGQMTLSLEKTALLPLLDQAMLTIHSQALSKSLALSTFISAN 502
Cdd:COG3850   235 LAALLLLLLLQDALAESELLALNILAGLLELLLALLLLLLASALLLLELELLALLLELVELLALAAAEEALLLLVELAAL 314
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1190634387 503 IPLELELDTLRLRQILVNLLGNAVKFTPQGRIQLRVRRQN 542
Cdd:COG3850   315 LLLLLLQAIANASLLLIALASVVAALLELASILALQAALE 354
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
696-809 7.79e-05

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 43.02  E-value: 7.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLG-HQVTRADSGTTALAIGRQHRFDLVLMDIRM-------PVLDGLattarwRHDPAnID 767
Cdd:cd17589     1 FLIVDDQPTFRSMLKSMLRSLGvTRIDTASSGEEALRMCENKTYDIVLCDYNLgkgkngqQLLEEL------RHKKL-IS 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1190634387 768 SHC---MITA-------LSA-NASPDEqiktsqagmnhYLSKPVTLGQLAEML 809
Cdd:cd17589    74 PSTvfiMVTGessramvLSAlELEPDD-----------YLLKPFTVSELRERL 115
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
510-608 8.91e-05

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


Pssm-ID: 340409 [Multi-domain]  Cd Length: 113  Bit Score: 42.64  E-value: 8.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 510 DTLRLRQILVNLLGNAVKFTP--QGRIQLRV-RRQNQT--------LCFTVEDTGCGIDVQHQQTIFqpfmqtsDHEQGT 578
Cdd:cd16932     3 DQIRLQQVLADFLLNAVRFTPspGGWVEIKVsPTKKQIgdgvhvihLEFRITHPGQGLPEELVQEMF-------EENQWT 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1190634387 579 ---GLGLAIADNLAKMMGGHLTVFSEPGQgSCF 608
Cdd:cd16932    76 tqeGLGLSISRKLVKLMNGDVRYLREAGR-SYF 107
HATPase_c_5 pfam14501
GHKL domain; This family represents the structurally related ATPase domains of histidine ...
517-610 8.96e-05

GHKL domain; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 433996 [Multi-domain]  Cd Length: 102  Bit Score: 42.59  E-value: 8.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 517 ILVNLLGNA---VKFTPQGR-IQLRVRRQNQTLCFTVEDTgcgidVQHQQTIFQPFMQTSDHEQGTGLGLAIADNLAKMM 592
Cdd:pfam14501   9 IFGNLLDNAieaCSKIDDNRfIRLKIREKQNFLIIRIENT-----YEGELKFEGKLPSTKTKGDGHGIGLKSIRRIVKKY 83
                          90
                  ....*....|....*...
gi 1190634387 593 GGHLTVFSEPGqgsCFSL 610
Cdd:pfam14501  84 GGNLSTEIENG---IFTL 98
PRK13435 PRK13435
response regulator; Provisional
693-841 9.65e-05

response regulator; Provisional


Pssm-ID: 184052 [Multi-domain]  Cd Length: 145  Bit Score: 43.50  E-value: 9.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 693 QMHILLVDDsetnRDITGMML----QQLGHQVT-RADSGTTALAIGRQHRFDLVLMDIRMpvLDGLATTARWRHdpanID 767
Cdd:PRK13435    5 QLKVLIVED----EALIALELeklvEEAGHEVVgIAMSSEQAIALGRRRQPDVALVDVHL--ADGPTGVEVARR----LS 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1190634387 768 SHCMITALSANASPdEQIKTSQAGMNHYLSKPVTLGQLAEMLDLTAQFQleRGVDLSPqlsEPQPLLDLADSAL 841
Cdd:PRK13435   75 ADGGVEVVFMTGNP-ERVPHDFAGALGVIAKPYSPRGVARALSYLSARR--VGDRASG---PTPMGVFLAPATL 142
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
694-843 1.32e-04

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 44.53  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 694 MHILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRhdpaNIDSHCMIT 773
Cdd:PRK09836    1 MKLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLR----SANKGMPIL 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1190634387 774 ALSANASPDEQIKTSQAGMNHYLSKPVTLGQ-LAEMLDLtaqfqLERGvdlSPQLSEPQplLDLADSALSL 843
Cdd:PRK09836   77 LLTALGTIEHRVKGLELGADDYLVKPFAFAElLARVRTL-----LRRG---AAVIIESQ--FQVADLMVDL 137
PRK10336 PRK10336
two-component system response regulator QseB;
694-810 1.48e-04

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 44.12  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 694 MHILLVDDSETNRDITGMMLQQLGHQV---TRADSGTTALAigrQHRFDLVLMDIRMPVLDGLATTARWR----HDPANI 766
Cdd:PRK10336    1 MRILLIEDDMLIGDGIKTGLSKMGFSVdwfTQGRQGKEALY---SAPYDAVILDLTLPGMDGRDILREWRekgqREPVLI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1190634387 767 dshcmitaLSANASPDEQIKTSQAGMNHYLSKPVTLGQLAEMLD 810
Cdd:PRK10336   78 --------LTARDALAERVEGLRLGADDYLCKPFALIEVAARLE 113
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
696-799 1.55e-04

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: 41.62  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAI--GRQHRFDLVLMDIRMPVLDGLATTAR-WRHDpanIDSHCMI 772
Cdd:cd17582     1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVleDEQNEIDLILTEVDLPVSSGFKLLSYiMRHK---ICKNIPV 77
                          90       100
                  ....*....|....*....|....*..
gi 1190634387 773 TALSANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd17582    78 IMMSSQDSVGVVFKCLSKGAADYLVKP 104
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
509-613 1.86e-04

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 45.21  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 509 LDTLRLRQILVNLLGNAVKF---TPQG--RIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQGT-GLGL 582
Cdd:PRK15053  428 LDSTEFAAIVGNLLDNAFEAslrSDEGnkIVELFLSDEGDDVVIEVADQGCGVPESLRDKIFEQGVSTRADEPGEhGIGL 507
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1190634387 583 AIADNLAKMMGGHLTVFSEPGQGSCFSLCLP 613
Cdd:PRK15053  508 YLIASYVTRCGGVITLEDNDPCGTLFSIFIP 538
HPtr COG2198
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
302-909 2.28e-04

HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];


Pssm-ID: 441800 [Multi-domain]  Cd Length: 871  Bit Score: 45.04  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 302 ALAILLLLTSVLSLLLRYYLAIPLWNFINIIGATGPQAMEPRLPINRIDELGHIARAYNNLLDTLNEQYDTLEMKVKERT 381
Cdd:COG2198   228 AAAALAAELALAELAALLLLLLLLLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLELLLLLLL 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 382 LALAEAKRAAEQANRRKSDHLTTISHEIRTPLNGALGAVELLQNTPLDAGQMRLAETAHQCSLSLLAIINNLLDFSRIES 461
Cdd:COG2198   308 ALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLALLLALLLAAAAALAAALEALLTELALILLLLL 387
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 462 GQMTLSLEKTALLPLLDQAMLTIHSQALSKSLALSTFISANIPLELELDTLRLRQILVNLLGNAVKFTPQGRIQLRVRRQ 541
Cdd:COG2198   388 LLLLLLILLGLLLLLLLSLLLSLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLGLLLLLLLLLGLLLLLLLGLLLLALLL 467
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 542 NQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQGTGLGLAIADNLAKMMGGHLTVFSEPGQGSCFSLCLPFNAITPPM 621
Cdd:COG2198   468 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVAAALAALALLLLLALLLLLLLDLLILGLLLILLLLLLGLL 547
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 622 PFHGELFAPQRLHAQLSAWGMTCQPELANQPSRHFVDNALCYLPGRLYAKLKQYLQGAETEALKSLPLQPWQMHI---LL 698
Cdd:COG2198   548 ALGLAALLLLLALLLGLGLLLGLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLALLLALLAAAAALLLLLLLLALlllLL 627
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 699 VDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANIDSHCMITALSAN 778
Cdd:COG2198   628 LLLLLLLLLLLLLLLLLLLLLLLLLAVLLAAAAAAAALAALDLLLDLDDMMMMLDDMMAEAARARALAARAAAIAAAAAA 707
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 779 ASPDEQIKTSQAGMNHYLSKPVTLGQLAEMLDLTAQFQLERGVDLSPQLSEPQPLLDLA-------DSALSLKLYQ---- 847
Cdd:COG2198   708 AAAAAAAAAAAAAALLAALLLLLLLLLLLLLLLLLLLLAAAAAAAASPAAPALPVLDLEalrrlggDPELLRELLElfle 787
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1190634387 848 SLQVLIQQAKDAIE--NLPVLSHTLHTIKGCAGQAGLIELQDAVIQLEHALDTHETLTQQEIIQ 909
Cdd:COG2198   788 ELPELLAELRQALAagDLEALARLAHKLKGSAGNLGAPRLAELAAELEQAARAGDLEEAEELLA 851
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
696-805 2.35e-04

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 41.65  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLV-DDSETNRDITGMmLQQLGHQVTRADS---GTTALAIgrqHRFDLVLMDIRMPVLDGLATTARWRHDPANIdshcM 771
Cdd:cd17573     1 ILLIeDDSTLGKEISKG-LNEKGYQADVAESlkdGEYYIDI---RNYDLVLVSDKLPDGNGLSIVSRIKEKHPSI----V 72
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1190634387 772 ITALSANASPDEQIKTSQAGMNHYLSKPVTLGQL 805
Cdd:cd17573    73 VIVLSDNPKTEQEIEAFKEGADDYIAKPFDFKVL 106
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
695-807 2.48e-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: 41.66  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 695 HILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHdpaniDSHCMITA 774
Cdd:cd17594     1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRA-----RSDVPIII 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1190634387 775 LSANASPDEQIKTS-QAGMNHYLSKPVTLGQLAE 807
Cdd:cd17594    76 ISGDRRDEIDRVVGlELGADDYLAKPFGLRELLA 109
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
696-819 2.58e-04

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


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 41.97  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQlGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLA--TTARWRH-DPANI------ 766
Cdd:cd17596     3 ILVVDDEVRSLEALRRTLEE-DFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEflKEVRERWpEVVRIiisgyt 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1190634387 767 DSHCMITALsanaspdeqiktSQAGMNHYLSKPVTLGQLAEMLDLTAQ-FQLER 819
Cdd:cd17596    82 DSEDIIAGI------------NEAGIYQYLTKPWHPDQLLLTVRNAARlFELQR 123
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
696-799 3.52e-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: 40.51  E-value: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHdpaniDSHCMITAL 775
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQ-----KSTLPVIFL 75
                          90       100
                  ....*....|....*....|....
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd19936    76 TSKDDEIDEVFGLRMGADDYITKP 99
PRK10643 PRK10643
two-component system response regulator PmrA;
694-805 4.26e-04

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 42.72  E-value: 4.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 694 MHILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDpaNIDSHCMIt 773
Cdd:PRK10643    1 MKILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQK--KYTLPVLI- 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1190634387 774 aLSANASPDEQIKTSQAGMNHYLSKPVTLGQL 805
Cdd:PRK10643   78 -LTARDTLEDRVAGLDVGADDYLVKPFALEEL 108
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
696-799 8.04e-04

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 39.83  E-value: 8.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTarwrhdpANIDSHCM---I 772
Cdd:cd19926     1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELV-------QHIQQRLPqtpV 73
                          90       100
                  ....*....|....*....|....*..
gi 1190634387 773 TALSANASPDEQIKTSQAGMNHYLSKP 799
Cdd:cd19926    74 AVITAYGSLDTAIEALKAGAFDFLTKP 100
PRK10935 PRK10935
nitrate/nitrite two-component system sensor histidine kinase NarQ;
342-389 1.32e-03

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


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 42.53  E-value: 1.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1190634387 342 PRLPINRIDELGHIARAYNNLLDTLNEQYDTLEMKVKERTLALAEAKR 389
Cdd:PRK10935  198 IPLDTTLPNELGLLAKAFNQMSSELHKLYRSLEASVEEKTRKLTQANR 245
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
696-809 1.82e-03

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


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 39.35  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGH-QVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTarwRHDPaniDSHCMItA 774
Cdd:cd17530     3 VLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFL---RHLA---ESHSNA-A 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1190634387 775 LSANASPDEQIKTSQAGMNH--------YLSKPVTLGQLAEML 809
Cdd:cd17530    76 VILMSGLDGGILESAETLAGanglnllgTLSKPFSPEELTELL 118
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
343-585 2.19e-03

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 41.64  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 343 RLPINRIDELGHIARAYNNLLDTLNEQYDTLEMKVKERTLALAEAKRAAEQANRRKSDHLTTISHEIRTPLNGALGAVEL 422
Cdd:COG2770   258 RIPVSRKDEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLL 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 423 LQNTPLDA----GQMRLAETAHQCSLSLLAIINNLLDFSRIESGQMTLSLEKTALLPLLDQAMLTIHSQALSKSLALSTF 498
Cdd:COG2770   338 LALLLLLLlaadLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALL 417
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 499 ISANIPLELELDTLRLRQILVNLLGNAVKFTPQGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQGT 578
Cdd:COG2770   418 ALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEEEEE 497

                  ....*..
gi 1190634387 579 GLGLAIA 585
Cdd:COG2770   498 AGAAAEE 504
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
696-799 2.62e-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: 38.86  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDS-ETNRDITGMMLQQLG--HQVTRADSGTTALAIGRQHRFD-----LVLMDIRMPVLDGLATTARWRHdpanID 767
Cdd:cd17595     3 ILTVDDDpQVLRAVARDLRRQYGkdYRVLRADSGAEALDALKELKLRgeavaLFLVDQRMPEMDGVEFLEKAME----LF 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1190634387 768 SHCMITALSANASPDEQIKT-SQAGMNHYLSKP 799
Cdd:cd17595    79 PEAKRVLLTAYADTDAAIRAiNDVQLDYYLLKP 111
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
694-799 2.69e-03

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 40.56  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 694 MH-ILLVDDsetNRDITGMM---LQQLGHQVTRADSGTTALAIgRQHRFDLVLMDIRMPVLDGLATTARWRHdpaniDSH 769
Cdd:PRK10955    1 MNkILLVDD---DRELTSLLkelLEMEGFNVIVAHDGEQALDL-LDDSIDLLLLDVMMPKKNGIDTLKELRQ-----THQ 71
                          90       100       110
                  ....*....|....*....|....*....|
gi 1190634387 770 CMITALSANASPDEQIKTSQAGMNHYLSKP 799
Cdd:PRK10955   72 TPVIMLTARGSELDRVLGLELGADDYLPKP 101
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
521-589 2.78e-03

Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.


Pssm-ID: 340413 [Multi-domain]  Cd Length: 91  Bit Score: 38.02  E-value: 2.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1190634387 521 LLGNAVK----FTPQGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQtifqpfmQTSDHEQGTGLGLAIADNLA 589
Cdd:cd16936     8 AVTNAVRhayrHDGPGPVRLELDLDPDRLRVEVTDSGPGFDPLRPA-------DPDAGLREGGRGLALIRALM 73
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
696-829 3.00e-03

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 40.01  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRdiTGmmLQQLGHQ------VTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHdpANIDSH 769
Cdd:PRK10651    9 ILLIDDHPMLR--TG--VKQLISMapditvVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLRE--KSLSGR 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 770 cmITALSANASPDEQIKTSQAGMNHYLSKPVTLGQLAEMLDLTAQFQlergVDLSPQLSE 829
Cdd:PRK10651   83 --IVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQAAAGE----MVLSEALTP 136
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
696-805 3.45e-03

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 40.09  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHDPANIDshCMITAL 775
Cdd:PRK10161    5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRD--IPVVML 82
                          90       100       110
                  ....*....|....*....|....*....|
gi 1190634387 776 SANASPDEQIKTSQAGMNHYLSKPVTLGQL 805
Cdd:PRK10161   83 TARGEEEDRVRGLETGADDYITKPFSPKEL 112
fixJ PRK09390
response regulator FixJ; Provisional
699-753 3.95e-03

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 39.60  E-value: 3.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1190634387 699 VDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGL 753
Cdd:PRK09390    9 VDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGI 63
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
695-753 4.74e-03

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: 37.74  E-value: 4.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1190634387 695 HILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGL 753
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGL 59
HATPase_AgrC-ComD-like cd16935
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
499-603 4.82e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Staphylococcus aureus AgrC and Streptococcus pneumoniae ComD which are involved in quorum sensing; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) including Staphylococcus aureus AgrC which is an HK of the accessory gene regulator (agr) quorum sensing two-component regulatory system (TCS) AgrC-AgrA. The agr system plays a part in the transition from persistent to virulent phenotype. This family also includes Streptococcus pneumoniae ComD HK of the ComD-ComE TCS, involved in quorum sensing and genetic competence.


Pssm-ID: 340412 [Multi-domain]  Cd Length: 134  Bit Score: 38.33  E-value: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 499 ISANIPLELELDTLRLRQILVNLLGNAV----KFTPQGR-IQLRVRRQNQTLCFTVEDTGCGidvqHQQTIFQPFmQTSD 573
Cdd:cd16935    22 IEIDIPILLPISPLDLCIIFGNLLDNAIeacaKIDKENRfIHLKIRQKKGFLIISIENSYEG----ELKKKNGLF-LSTK 96
                          90       100       110
                  ....*....|....*....|....*....|
gi 1190634387 574 HEQGTGLGLAIADNLAKMMGGHLTVFSEPG 603
Cdd:cd16935    97 KDKNHGIGLKSIREIVKKYNGNLSIEYENG 126
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
696-752 4.96e-03

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: 38.12  E-value: 4.96e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTAL-----------AIGRQHRFDLVLMDIRMPVLDG 752
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALeflgledeedsSNFNEPKVNMIITDYCMPGMTG 68
HATPase_YpdA-YehU-LytS-like cd16924
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
516-613 5.07e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YpdA, YehU, Bacillus subtilis LytS, and some hybrid sensor histidine kinases; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. It also includes the HATPase domains of Escherichia coli YpdA and YehU, HKs of YpdA-YpdB and YehU-YehTCSs, which are involved together in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), some having accessory sensor domain(s) such as Cache, HAMP or GAF; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340401 [Multi-domain]  Cd Length: 103  Bit Score: 37.43  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 516 QILV-NLLGNAV-KFTPQGRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMqtsdheQGTGLGLAIADNLAKMMG 593
Cdd:cd16924     7 QPLVeNAIQHGLsPLTDKGVVTISALKEDNHVMIEVEDNGRGIDPKVLNILGKKPK------EGNGIGLYNVHQRLILLF 80
                          90       100
                  ....*....|....*....|...
gi 1190634387 594 G---HLTVFSEPGQGSCFSLCLP 613
Cdd:cd16924    81 GedyGIHIASEPDKGTRITFTIP 103
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
696-830 5.33e-03

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 40.24  E-value: 5.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 696 ILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGLATTARWRHdpanidSHCM--IT 773
Cdd:PRK10923    6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQ------RHPMlpVI 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1190634387 774 ALSANASPDEQIKTSQAGMNHYLSKPVTLGQLAEMLDLTAQFQLERGVDLSPQLSEP 830
Cdd:PRK10923   80 IMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNIQVNGP 136
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
693-805 5.52e-03

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 39.40  E-value: 5.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 693 QMHILLVDDSETNRDITGMMLQQLGHQVTRADSGTTALAIGRQHRFDLVLMDIRMPVLDGL---ATTARWRHDPanidsh 769
Cdd:PRK10529    1 MTNVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIefiRDLRQWSAIP------ 74
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1190634387 770 cmITALSANASPDEQIKTSQAGMNHYLSKPVTLGQL 805
Cdd:PRK10529   75 --VIVLSARSEESDKIAALDAGADDYLSKPFGIGEL 108
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
512-606 7.01e-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: 37.78  E-value: 7.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 512 LRLRQILVNLLGNAVKFTPQGRIQLRVRRQNQTLCFTVEDTGCGIDVqhqqtifqpfmQTSDHEQGTgLGLAIADNLAKM 591
Cdd:cd16951    42 LVVNELLQNALKHAFSDREGGTITIRSVVDGDYLRITVIDDGVGLPQ-----------DEDWPNKGS-LGLQIVRSLVEG 109
                          90
                  ....*....|....*
gi 1190634387 592 MGGHLTVFSEPGQGS 606
Cdd:cd16951   110 ELKAFLEVQSAENGT 124
PRK09191 PRK09191
two-component response regulator; Provisional
712-746 7.04e-03

two-component response regulator; Provisional


Pssm-ID: 236402 [Multi-domain]  Cd Length: 261  Bit Score: 39.45  E-value: 7.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1190634387 712 MLQQLGHQV-----TRADsgttALAIGRQHRFDLVLMDIR 746
Cdd:PRK09191  156 LVESLGHRVtgiarTRAE----AVALAKKTRPGLILADIQ 191
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
351-602 7.38e-03

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 40.00  E-value: 7.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 351 ELGHIARAYNNLLDTLNEQYDtlemkvKERTLalaeakraaeqanrrksdhLTTISHEIRTPLngalgAVelLQNT--PL 428
Cdd:PRK10815  244 ELTSLVRNLNRLLKNERERYT------KYRTT-------------------LTDLTHSLKTPL-----AV--LQSTlrSL 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 429 DAGQMRLAETAHQCSLSLLAIINNLLDF----SRIESGQMTLSLEKTALLPLLDQAMLTIHSQALSKSLALSTFISANIP 504
Cdd:PRK10815  292 RSGKQMSVEQAEPIMLEQISRISQQIGYylhrASMRSEHNLLSRELHSVAPLLDNLTSALNKVYQRKGVNITLDISPEIT 371
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190634387 505 LELELDTLRlrQILVNLLGNAVKFTPQgRIQLRVRRQNQTLCFTVEDTGCGIDVQHQQTIFQPFMQTSDHEQGTGLGLAI 584
Cdd:PRK10815  372 FVGEKNDFM--EVMGNVLDNACKYCLE-FVEISARQTDEHLHIVVEDDGPGIPESKRELIFDRGQRADTLRPGQGLGLSV 448
                         250
                  ....*....|....*...
gi 1190634387 585 ADNLAKMMGGHLTVFSEP 602
Cdd:PRK10815  449 AREITEQYEGKISAGDSP 466
 
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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