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Conserved domains on  [gi|2738934608|ref|WP_348535073|]
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response regulator [Pseudoalteromonas sp. bablab_jr010]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TMAO_torS super family cl37193
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
357-750 5.68e-82

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


The actual alignment was detected with superfamily member TIGR02956:

Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 281.28  E-value: 5.68e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 357 LKDFNAQLEKQVDDKTNELVE--------------AVRAANNANRTKSQFLANMSHEIRTPLNGILGMTQLLLDNKdLAE 422
Cdd:TIGR02956 418 LQEHKESLEQLVAQRTQELAEtnerlnaevknhakARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTG-LTS 496
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 423 EEHEELVMIHQSANNLLLILNDILDFSKIEAGALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNISDSVPSCISLD 502
Cdd:TIGR02956 497 QQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGD 576
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 503 PLRFSQVINNILSNAGKFTESGDITMSCTMVNDR-MQISIRDTGIGISSEQQAKLFTEFTQADisTTRKYGGTGLGLTIS 581
Cdd:TIGR02956 577 GPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDSsLLFEVEDTGCGIAEEEQATLFDAFTQAD--GRRRSGGTGLGLAIS 654
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 582 KRIIELMAGELKLTSQEGVGSEFTITMPVIISNSASVDNQSTATpQLAGLNILLVEDNPVNQIVLKKMLHSTECNLKQAN 661
Cdd:TIGR02956 655 QRLVEAMDGELGVESELGVGSCFWFTLPLTRGKPAEDSATLTVI-DLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAE 733
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 662 DGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQnphLYGQAIIIAITANA---FEEDQQRCLVAGMDDFISKPINK 738
Cdd:TIGR02956 734 SGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRA---IYGAKNEVKFIAFSahvFNEDVAQYLAAGFDGFLAKPVVE 810
                         410
                  ....*....|..
gi 2738934608 739 DQLYACLNKWLK 750
Cdd:TIGR02956 811 EQLTAMIAVILA 822
PDC1_DGC_like cd12914
first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this ...
72-167 1.97e-10

first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the first PDC domain of Diguanylate-cyclases (DGCs), Histidine kinases (HKs), and other similar domains. Many members of this subfamily contain a C-terminal DGC (also called GGDEF) domain. DGCs regulate the turnover of cyclic diguanosine monophosphate. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


:

Pssm-ID: 350339  Cd Length: 123  Bit Score: 58.93  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608  72 LENMANLYPDFRTQIITDAFADVthfypqsLAVSLQQSNIRANVADRDYFIHAPSNKQG-YISTIFKGRGFGSlPIVAVS 150
Cdd:cd12914    32 LRRLLARLPEVRSIFVVDADGRV-------VASSGPGPAPGLDVSDRDYFQAARAGGGGlFISEPVISRVTGK-PVIPLS 103
                          90
                  ....*....|....*...
gi 2738934608 151 APIYIED-TFTGVVEGSL 167
Cdd:cd12914   104 RPIRDADgRFAGVVVASI 121
 
Name Accession Description Interval E-value
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
357-750 5.68e-82

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: 281.28  E-value: 5.68e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 357 LKDFNAQLEKQVDDKTNELVE--------------AVRAANNANRTKSQFLANMSHEIRTPLNGILGMTQLLLDNKdLAE 422
Cdd:TIGR02956 418 LQEHKESLEQLVAQRTQELAEtnerlnaevknhakARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTG-LTS 496
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 423 EEHEELVMIHQSANNLLLILNDILDFSKIEAGALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNISDSVPSCISLD 502
Cdd:TIGR02956 497 QQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGD 576
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 503 PLRFSQVINNILSNAGKFTESGDITMSCTMVNDR-MQISIRDTGIGISSEQQAKLFTEFTQADisTTRKYGGTGLGLTIS 581
Cdd:TIGR02956 577 GPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDSsLLFEVEDTGCGIAEEEQATLFDAFTQAD--GRRRSGGTGLGLAIS 654
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 582 KRIIELMAGELKLTSQEGVGSEFTITMPVIISNSASVDNQSTATpQLAGLNILLVEDNPVNQIVLKKMLHSTECNLKQAN 661
Cdd:TIGR02956 655 QRLVEAMDGELGVESELGVGSCFWFTLPLTRGKPAEDSATLTVI-DLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAE 733
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 662 DGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQnphLYGQAIIIAITANA---FEEDQQRCLVAGMDDFISKPINK 738
Cdd:TIGR02956 734 SGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRA---IYGAKNEVKFIAFSahvFNEDVAQYLAAGFDGFLAKPVVE 810
                         410
                  ....*....|..
gi 2738934608 739 DQLYACLNKWLK 750
Cdd:TIGR02956 811 EQLTAMIAVILA 822
PRK15347 PRK15347
two component system sensor kinase;
272-741 3.07e-72

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 253.41  E-value: 3.07e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 272 IIFIILLTSVFITQLSRWLTTPIRKLAEQIDKFEPENADTDtyLPQtwlevsrlqsqfsslanklalsfNRLHQ----AN 347
Cdd:PRK15347  303 LLILVLLTSVLFLLLRRYLAKPLWRFVDIINKTGPAALEPR--LPE-----------------------NRLDElgsiAK 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 348 HENELLNVrLKDFNAQLEKQVDDKTNELVEAVRAANNANRTKSQFLANMSHEIRTPLNGILGMTQLLlDNKDLAEEEHEE 427
Cdd:PRK15347  358 AYNQLLDT-LNEQYDTLENKVAERTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELL-QNTPLTAEQMDL 435
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 428 LVMIHQSANNLLLILNDILDFSKIEAGALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNISDSVPSCISLDPLRFS 507
Cdd:PRK15347  436 ADTARQCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLR 515
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 508 QVINNILSNAGKFTESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADISTtrkyGGTGLGLTISKRIIEL 587
Cdd:PRK15347  516 QILVNLLGNAVKFTETGGIRLRVKRHEQQLCFTVEDTGCGIDIQQQQQIFTPFYQADTHS----QGTGLGLTIASSLAKM 591
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 588 MAGELKLTSQEGVGSEFTITMPVI--------------------------ISNSASVDNQSTATPQLA------------ 629
Cdd:PRK15347  592 MGGELTLFSTPGVGSCFSLVLPLNeyappeplkgelsaplalhrqlsawgITCQPGHQNPALLDPELAylpgrlydllqq 671
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 630 ------------------GLNILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQ 691
Cdd:PRK15347  672 iiqgapnepvinlplqpwQLQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLE 751
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2738934608 692 CTKEIKQNP-HLYGQAIIIAITANAFEEDQQRCLVAGMDDFISKPINKDQL 741
Cdd:PRK15347  752 TTQLWRDDPnNLDPDCMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQL 802
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
342-610 6.25e-71

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 235.19  E-value: 6.25e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 342 RLHQANHENELLNVRLKDFNAQLEKQVDDKTNELVEAVRAANNANRTKSQFLANMSHEIRTPLNGILGMTQLLLDNKDla 421
Cdd:COG0642    63 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELD-- 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 422 EEEHEELVMIHQSANNLLLILNDILDFSKIEAGALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNISDSVPScISL 501
Cdd:COG0642   141 EEQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPT-VRG 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 502 DPLRFSQVINNILSNAGKFTESG-DITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADisTTRKYGGTGLGLTI 580
Cdd:COG0642   220 DPDRLRQVLLNLLSNAIKYTPEGgTVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTD--PSRRGGGTGLGLAI 297
                         250       260       270
                  ....*....|....*....|....*....|
gi 2738934608 581 SKRIIELMAGELKLTSQEGVGSEFTITMPV 610
Cdd:COG0642   298 VKRIVELHGGTIEVESEPGKGTTFTVTLPL 327
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
508-610 1.43e-44

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: 155.34  E-value: 1.43e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 508 QVINNILSNAGKFTESGDITMSCTMVND-----RMQISIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTGLGLTISK 582
Cdd:cd16922     3 QILLNLLGNAIKFTEEGEVTLRVSLEEEeedgvQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAISK 82
                          90       100
                  ....*....|....*....|....*...
gi 2738934608 583 RIIELMAGELKLTSQEGVGSEFTITMPV 610
Cdd:cd16922    83 KLVELMGGDISVESEPGQGSTFTFTLPL 110
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
391-609 8.09e-35

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


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 140.66  E-value: 8.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 391 QFLANMSHEIRTPLNGILGMTQLLLD----NKDLA-------EEEHEElvMIH------QsannlllilndildFSKIEA 453
Cdd:NF033092  374 EFVANVSHELRTPLTTMRSYLEALADgawkDPELAprflgvtQNETER--MIRlvndllQ--------------LSRMDS 437
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 454 GALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNISDSVPScISLDPLRFSQVINNILSNAGKFT-ESGDITMSCTM 532
Cdd:NF033092  438 KDYKLNKEWVNFNEFFNYIIDRFEMILKNKNITFKREFPKRDLW-VEIDTDKITQVLDNIISNAIKYSpEGGTITFRLLE 516
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2738934608 533 VNDRMQISIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMP 609
Cdd:NF033092  517 THNRIIISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAESEEGKGTTIYFTLP 593
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
502-610 6.05e-32

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 120.06  E-value: 6.05e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608  502 DPLRFSQVINNILSNAGKFT-ESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADiSTTRKYGGTGLGLTI 580
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTD-KRSRKIGGTGLGLSI 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 2738934608  581 SKRIIELMAGELKLTSQEGVGSEFTITMPV 610
Cdd:smart00387  81 VKKLVELHGGEISVESEPGGGTTFTITLPL 110
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
502-610 9.84e-28

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


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 107.84  E-value: 9.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 502 DPLRFSQVINNILSNAGKFT-ESGDITMSCTmVNDRMQISIRDTGIGISSEQQAKLFTEFTQADistTRKYGGTGLGLTI 580
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAaKAGEITVTLS-EGGELTLTVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGGTGLGLSI 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 2738934608 581 SKRIIELMAGELKLTSQEGVGSEFTITMPV 610
Cdd:pfam02518  78 VRKLVELLGGTITVESEPGGGTTVTLTLPL 107
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
246-609 8.14e-26

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 111.46  E-value: 8.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 246 WMVMTMLNRKHANdVAVNAWGQ----SLVMIIFIILLTSVFITQLSRWLTTPIRKLAEQIDKFEPENADTdtylpqtwle 321
Cdd:NF012163  141 ALGASPVERLTRN-TDINFDSQqkraSWLIVALALLLAALAAFLLARGLLAPVKRLVEATHRLAAGDYTT---------- 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 322 vsRLQSQFSSLANKLALSFNRLHQANHENEllnvrlkdfnaqlekqvddktnelveavraannanRTKSQFLANMSHEIR 401
Cdd:NF012163  210 --RVTPTSNDELGKLAQDFNQLASTLEKNE-----------------------------------QMRRDFMADISHELR 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 402 TPLNGILGMTQLLLDNKDLAEEEHeeLVMIHQSANNLLLILNDILDFSKIEAGALKLEYRAVEITKLLEQIAKVFSSTSV 481
Cdd:NF012163  253 TPLAVLRAELEAIQDGIRKFTPES--LDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFA 330
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 482 KKGVTFKLNISDSvpSCISLDPLRFSQVINNILSNAGKFTES-GDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEF 560
Cdd:NF012163  331 SAGLELEVSLPDS--SLVFGDRDRLMQLFNNLLENSLRYTDSgGSLHISASQRPKEVTLTVADSAPGVSDEQLARLFERF 408
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2738934608 561 TQADISTTRKYGGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMP 609
Cdd:NF012163  409 YRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVTLP 457
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
346-609 5.04e-23

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 103.57  E-value: 5.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 346 ANHENELLNVRLKDFNAQLEKQVDDKTNELVEAVRAANNANRTKSQFLANMSHEIRTPLNGILGMTQLLLDNKD------ 419
Cdd:NF040691  228 AGDLSERMPVKGEDDLARLARSFNQMADSLQRQIRQLEELSRLQQRFVSDVSHELRTPLTTIRMAADVIHDSRDdfdpat 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 420 --LAEEEHEELVMIHQsannlllILNDILDFSKIEAGALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNIsDSVPS 497
Cdd:NF040691  308 arSAELLHTELDRFES-------LLSDLLEISRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVDA-PGTPV 379
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 498 CISLDPLRFSQVINNILSNAGKFTESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTGLG 577
Cdd:NF040691  380 VAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTVAQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLG 459
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2738934608 578 LTISKRIIELMAGELKLTSQEGVGSEFTITMP 609
Cdd:NF040691  460 LAIALEDARLHGGWLEAWGRPGQGSQFRLTLP 491
PDC1_DGC_like cd12914
first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this ...
72-167 1.97e-10

first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the first PDC domain of Diguanylate-cyclases (DGCs), Histidine kinases (HKs), and other similar domains. Many members of this subfamily contain a C-terminal DGC (also called GGDEF) domain. DGCs regulate the turnover of cyclic diguanosine monophosphate. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350339  Cd Length: 123  Bit Score: 58.93  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608  72 LENMANLYPDFRTQIITDAFADVthfypqsLAVSLQQSNIRANVADRDYFIHAPSNKQG-YISTIFKGRGFGSlPIVAVS 150
Cdd:cd12914    32 LRRLLARLPEVRSIFVVDADGRV-------VASSGPGPAPGLDVSDRDYFQAARAGGGGlFISEPVISRVTGK-PVIPLS 103
                          90
                  ....*....|....*...
gi 2738934608 151 APIYIED-TFTGVVEGSL 167
Cdd:cd12914   104 RPIRDADgRFAGVVVASI 121
 
Name Accession Description Interval E-value
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
357-750 5.68e-82

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: 281.28  E-value: 5.68e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 357 LKDFNAQLEKQVDDKTNELVE--------------AVRAANNANRTKSQFLANMSHEIRTPLNGILGMTQLLLDNKdLAE 422
Cdd:TIGR02956 418 LQEHKESLEQLVAQRTQELAEtnerlnaevknhakARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTG-LTS 496
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 423 EEHEELVMIHQSANNLLLILNDILDFSKIEAGALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNISDSVPSCISLD 502
Cdd:TIGR02956 497 QQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGD 576
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 503 PLRFSQVINNILSNAGKFTESGDITMSCTMVNDR-MQISIRDTGIGISSEQQAKLFTEFTQADisTTRKYGGTGLGLTIS 581
Cdd:TIGR02956 577 GPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDSsLLFEVEDTGCGIAEEEQATLFDAFTQAD--GRRRSGGTGLGLAIS 654
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 582 KRIIELMAGELKLTSQEGVGSEFTITMPVIISNSASVDNQSTATpQLAGLNILLVEDNPVNQIVLKKMLHSTECNLKQAN 661
Cdd:TIGR02956 655 QRLVEAMDGELGVESELGVGSCFWFTLPLTRGKPAEDSATLTVI-DLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAE 733
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 662 DGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQnphLYGQAIIIAITANA---FEEDQQRCLVAGMDDFISKPINK 738
Cdd:TIGR02956 734 SGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRA---IYGAKNEVKFIAFSahvFNEDVAQYLAAGFDGFLAKPVVE 810
                         410
                  ....*....|..
gi 2738934608 739 DQLYACLNKWLK 750
Cdd:TIGR02956 811 EQLTAMIAVILA 822
PRK15347 PRK15347
two component system sensor kinase;
272-741 3.07e-72

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 253.41  E-value: 3.07e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 272 IIFIILLTSVFITQLSRWLTTPIRKLAEQIDKFEPENADTDtyLPQtwlevsrlqsqfsslanklalsfNRLHQ----AN 347
Cdd:PRK15347  303 LLILVLLTSVLFLLLRRYLAKPLWRFVDIINKTGPAALEPR--LPE-----------------------NRLDElgsiAK 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 348 HENELLNVrLKDFNAQLEKQVDDKTNELVEAVRAANNANRTKSQFLANMSHEIRTPLNGILGMTQLLlDNKDLAEEEHEE 427
Cdd:PRK15347  358 AYNQLLDT-LNEQYDTLENKVAERTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELL-QNTPLTAEQMDL 435
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 428 LVMIHQSANNLLLILNDILDFSKIEAGALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNISDSVPSCISLDPLRFS 507
Cdd:PRK15347  436 ADTARQCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLR 515
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 508 QVINNILSNAGKFTESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADISTtrkyGGTGLGLTISKRIIEL 587
Cdd:PRK15347  516 QILVNLLGNAVKFTETGGIRLRVKRHEQQLCFTVEDTGCGIDIQQQQQIFTPFYQADTHS----QGTGLGLTIASSLAKM 591
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 588 MAGELKLTSQEGVGSEFTITMPVI--------------------------ISNSASVDNQSTATPQLA------------ 629
Cdd:PRK15347  592 MGGELTLFSTPGVGSCFSLVLPLNeyappeplkgelsaplalhrqlsawgITCQPGHQNPALLDPELAylpgrlydllqq 671
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 630 ------------------GLNILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQ 691
Cdd:PRK15347  672 iiqgapnepvinlplqpwQLQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLE 751
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2738934608 692 CTKEIKQNP-HLYGQAIIIAITANAFEEDQQRCLVAGMDDFISKPINKDQL 741
Cdd:PRK15347  752 TTQLWRDDPnNLDPDCMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQL 802
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
342-610 6.25e-71

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 235.19  E-value: 6.25e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 342 RLHQANHENELLNVRLKDFNAQLEKQVDDKTNELVEAVRAANNANRTKSQFLANMSHEIRTPLNGILGMTQLLLDNKDla 421
Cdd:COG0642    63 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELD-- 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 422 EEEHEELVMIHQSANNLLLILNDILDFSKIEAGALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNISDSVPScISL 501
Cdd:COG0642   141 EEQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPT-VRG 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 502 DPLRFSQVINNILSNAGKFTESG-DITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADisTTRKYGGTGLGLTI 580
Cdd:COG0642   220 DPDRLRQVLLNLLSNAIKYTPEGgTVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTD--PSRRGGGTGLGLAI 297
                         250       260       270
                  ....*....|....*....|....*....|
gi 2738934608 581 SKRIIELMAGELKLTSQEGVGSEFTITMPV 610
Cdd:COG0642   298 VKRIVELHGGTIEVESEPGKGTTFTVTLPL 327
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
363-748 2.35e-69

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 245.14  E-value: 2.35e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 363 QLEKQvddktN-ELVEAVRAANNANRTKSQFLANMSHEIRTPLNGILGMTQLLLDNkDLAEEEHEELVMIHQSANNLLLI 441
Cdd:PRK11107  271 QMEIQ-----NvELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKT-PLTPTQRDYLQTIERSANNLLAI 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 442 LNDILDFSKIEAGALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNISDSVPSCISLDPLRFSQVINNILSNAGKFT 521
Cdd:PRK11107  345 INDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFT 424
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 522 ESGDITMSCTMV---NDRMQI--SIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTGLGLTISKRIIELMAGELKLTS 596
Cdd:PRK11107  425 ESGNIDILVELRalsNTKVQLevQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHS 504
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 597 QEGVGSEFTITMPVIISNSASVDNQSTAtpQLAGLNILLVEDNP-----VNQIV-------------------------- 645
Cdd:PRK11107  505 QPNRGSTFWFHLPLDLNPNPIIDGLPTD--CLAGKRLLYVEPNSaaaqaTLDILsetplevtysptlsqlpeahydilll 582
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 646 ----------------LKKMLHSTEC------------------------------------------------------ 655
Cdd:PRK11107  583 glpvtfrepltmlherLAKAKSMTDFlilalpcheqvlaeqlkqdgadaclskplshtrllpallepchhkqppllpptd 662
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 656 ----------------NLK--------------QANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPH---- 701
Cdd:PRK11107  663 esrlpltvmavddnpaNLKligalleeqvehvvLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHnqnt 742
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2738934608 702 ---------LYGQaiiiaitanafeedQQRCLVAGMDDFISKPINKDQLYACLNKW 748
Cdd:PRK11107  743 piiavtahaMAGE--------------RERLLSAGMDDYLAKPIDEAMLKQVLLRY 784
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
374-610 1.03e-66

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 220.55  E-value: 1.03e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 374 ELVEAVRAANNANRTKSQFLANMSHEIRTPLNGILGMTQLLLDNKDLAEEEHEELV-MIHQSANNLLLILNDILDFSKIE 452
Cdd:COG2205     1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEDLSPEERRELLeIIRESAERLLRLIEDLLDLSRLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 453 AGALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNISDSVPScISLDPLRFSQVINNILSNAGKFT-ESGDITMSCT 531
Cdd:COG2205    81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPL-VYADPELLEQVLANLLDNAIKYSpPGGTITISAR 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2738934608 532 MVNDRMQISIRDTGIGISSEQQAKLFTEFTQADisTTRKYGGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMPV 610
Cdd:COG2205   160 REGDGVRISVSDNGPGIPEEELERIFERFYRGD--NSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPL 236
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
381-747 6.04e-66

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 233.68  E-value: 6.04e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 381 AANNANRTKSQFLANMSHEIRTPLNGILGMTQLLLDNkDLAEEEHEELVMIHQSANNLLLILNDILDFSKIEAGALKLEY 460
Cdd:PRK11091  275 ALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDT-ELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQLDN 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 461 RAVEITKLLEQIAKVFSSTSVKKGVTFKLNISDSVPSCISLDPLRFSQVINNILSNAGKFTESGDITMSCTM-VNDRMQI 539
Cdd:PRK11091  354 QPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRYeEGDMLTF 433
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 540 SIRDTGIGISSEQQAKLFTEFTQA-DISTTRKYGGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMPVIISNSASV 618
Cdd:PRK11091  434 EVEDSGIGIPEDELDKIFAMYYQVkDSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAPAVAEEVE 513
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 619 DNQSTATPQLAGLNILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQ 698
Cdd:PRK11091  514 DAFDEDDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRE 593
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2738934608 699 NpHLYGQAIIIAITANAFEEDQQRCLVAGMDDFISKPINKDQLYACLNK 747
Cdd:PRK11091  594 R-YPREDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIKK 641
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
268-610 3.95e-62

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 213.65  E-value: 3.95e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 268 SLVMIIFIILLTSVFITQLSRWLTTPIRKLAEQIDKFEPENADTDTYLPQTWLEVSRLQSQFSSLANKLALSFNRLHQAN 347
Cdd:COG5002    29 LLLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 348 HENELLNVRLKDFNAQLEKQVDDKTNELVEAVRAANN---------------ANRTKSQFLANMSHEIRTPLNGILGMTQ 412
Cdd:COG5002   109 ALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLlllaaverditelerLEQMRREFVANVSHELRTPLTSIRGYLE 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 413 LLLDNKDLAEEEHEELV-MIHQSANNLLLILNDILDFSKIEAGALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNI 491
Cdd:COG5002   189 LLLDGAADDPEERREYLeIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDL 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 492 SDSVPScISLDPLRFSQVINNILSNAGKFTESGD-ITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADISTTRK 570
Cdd:COG5002   269 PEDPLL-VLGDPDRLEQVLTNLLDNAIKYTPEGGtITVSLREEDDQVRISVRDTGIGIPEEDLPRIFERFYRVDKSRSRE 347
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2738934608 571 YGGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMPV 610
Cdd:COG5002   348 TGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPL 387
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
266-750 7.38e-57

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 209.38  E-value: 7.38e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 266 GQSLVMIIFIilLTSVFITQLSRWL---TTPIRKLAE-QIDKFEPENA---DTDTylpqtwleVSRLQSQFSSLANKLal 338
Cdd:PRK11466  338 MVSLCALILI--LWRVVYRSVTRPLaeqTQALQRLLDgDIDSPFPETAgvrELDT--------IGRLMDAFRSNVHAL-- 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 339 sfnrlhqaNHENEllnvrlkdfnaQLEKQVDDKTNELVEAV------RA-ANNANRTKSQFLANMSHEIRTPLNGILGMT 411
Cdd:PRK11466  406 --------NRHRE-----------QLAAQVKARTAELQELViehrqaRAeAEKASQAKSAFLAAMSHEIRTPLYGILGTA 466
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 412 QLLLDNKdLAEEEHEELVMIHQSANNLLLILNDILDFSKIEAGA--LKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKL 489
Cdd:PRK11466  467 QLLADNP-ALNAQRDDLRAITDSGESLLTILNDILDYSAIEAGGknVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLAT 545
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 490 NISDSVPSCISLDPLRFSQVINNILSNAGKFTESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQAdistTR 569
Cdd:PRK11466  546 DIADDLPTALMGDPRRIRQVITNLLSNALRFTDEGSIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFVQV----SG 621
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 570 KYGGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMPVIISnSASVDNQSTATPQLAGLNILLVEDNPVNQIVLKKM 649
Cdd:PRK11466  622 KRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLRVA-TAPVPKTVNQAVRLDGLRLLLIEDNPLTQRITAEM 700
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 650 LHSTECNLKQANDGLEALEILQSYQA-DIILMDCQMPNMDGYQCTKEIKQnphLYGQAIIIAITANAFEEDQQR---CLV 725
Cdd:PRK11466  701 LNTSGAQVVAVGNAAQALETLQNSEPfAAALVDFDLPDYDGITLARQLAQ---QYPSLVLIGFSAHVIDETLRQrtsSLF 777
                         490       500
                  ....*....|....*....|....*
gi 2738934608 726 AGMddfISKPINKDQLYACLNKWLK 750
Cdd:PRK11466  778 RGI---IPKPVPREVLGQLLAHYLQ 799
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
375-741 2.96e-55

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 204.82  E-value: 2.96e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 375 LVEAVRAANNANRTKSQFLANMSHEIRTPLNGILGMTQLLlDNKDLAEEEHEELVMIHQSANNLLLILNDILDFSKIEAG 454
Cdd:PRK10841  433 LQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLL-QTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESE 511
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 455 ALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNISDSVPSCISLDPLRFSQVINNILSNAGKFTESGDITMSCTMVN 534
Cdd:PRK10841  512 QLKIEPREFSPREVINHITANYLPLVVKKRLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHVRVDG 591
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 535 DRMQISIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMP----- 609
Cdd:PRK10841  592 DYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIPlygaq 671
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 610 ---------------------------------------------------VIISNSASVDNQ----------------- 621
Cdd:PRK10841  672 ypqkkgveglqgkrcwlavrnasleqfletllqrsgiqvqryegqeptpedVLITDDPVQKKWqgravitfcrrhigipl 751
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 622 ---------STATPQ--LAGLN------------------------------ILLVEDNPVNQIVLKKMLHSTECNLKQA 660
Cdd:PRK10841  752 eiapgewvhSTATPHelPALLAriyrielesddsanalpstdkavsdnddmmILVVDDHPINRRLLADQLGSLGYQCKTA 831
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 661 NDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHLY---GqaiiiaITANAFEEDQQRCLVAGMDDFISKPIN 737
Cdd:PRK10841  832 NDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLpviG------VTANALAEEKQRCLEAGMDSCLSKPVT 905

                  ....
gi 2738934608 738 KDQL 741
Cdd:PRK10841  906 LDVL 909
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
371-747 5.57e-51

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 193.03  E-value: 5.57e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608  371 KTNELVEAVRA----ANNANRTKSQFLANMSHEIRTPLNGILGMTQLLLDNKDLAEEEHEELVMIHQSANNLLLILNDIL 446
Cdd:PRK09959   690 ETRDLIHALEVernkAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEIL 769
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608  447 DFSKIEAGALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTfkLNISDSVPS--CISLDPLRFSQVINNILSNAGKFTESG 524
Cdd:PRK09959   770 DVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIA--LSCSSTFPDhyLVKIDPQAFKQVLSNLLSNALKFTTEG 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608  525 --DITMSCTMVNDR---MQISIRDTGIGISSEQQAKLFTEFTQAdiSTTRKYGGTGLGLTISKRIIELMAGELKLTSQEG 599
Cdd:PRK09959   848 avKITTSLGHIDDNhavIKMTIMDSGSGLSQEEQQQLFKRYSQT--SAGRQQTGSGLGLMICKELIKNMQGDLSLESHPG 925
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608  600 VGSEFTITMPV-IISNSASVDNQSTATPQLA-GLNILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADI 677
Cdd:PRK09959   926 IGTTFTITIPVeISQQVATVEAKAEQPITLPeKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDL 1005
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2738934608  678 ILMDCQMPNMDGYQCTKEIK-QNPHL--YGQAIIIAItanafeEDQQRCLVAGMDDFISKPINKDQLYACLNK 747
Cdd:PRK09959  1006 LITDVNMPNMDGFELTRKLReQNSSLpiWGLTANAQA------NEREKGLSCGMNLCLFKPLTLDVLKTHLSQ 1072
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
508-610 1.43e-44

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: 155.34  E-value: 1.43e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 508 QVINNILSNAGKFTESGDITMSCTMVND-----RMQISIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTGLGLTISK 582
Cdd:cd16922     3 QILLNLLGNAIKFTEEGEVTLRVSLEEEeedgvQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAISK 82
                          90       100
                  ....*....|....*....|....*...
gi 2738934608 583 RIIELMAGELKLTSQEGVGSEFTITMPV 610
Cdd:cd16922    83 KLVELMGGDISVESEPGQGSTFTFTLPL 110
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
131-610 6.23e-39

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 151.48  E-value: 6.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 131 YISTIFKGRGFGSLPIVAVSAPIYIEDTFTGVVEGSLMFDYFASLRPSLFSHQGDLLILDAANKVVFSTIDDFKEMQQLS 210
Cdd:COG4251    25 LLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLLLLLLLELALVLLALLLVLLLLL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 211 NEEIDSFANEERFIIFDAHNEQQYYAKQARL-ADHNWMVMTMLNRKHANDVAVNAWGQSLVMIIFIILLTSVFITQLSRW 289
Cdd:COG4251   105 ALLLLLALLLLLELLLLLLALLLLLLLLALLlLEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAELELLLLL 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 290 LTTPIRKLAEQIDKFEPENADTDTYLPQTWLEVSRLQSQFSSLANKLALSFNRLHQANHENELLNVRLKDFNAQLEkqVD 369
Cdd:COG4251   185 LLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRLE--LE 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 370 DKTNELVEAVRAANNANRTKSQFLANMSHEIRTPLNGILGMTQLLLD--NKDLAEEEHEELVMIHQSANNLLLILNDILD 447
Cdd:COG4251   263 ELEEELEERTAELERSNEELEQFAYVASHDLREPLRKISGFSQLLEEdyGDKLDEEGREYLERIRDAAERMQALIDDLLA 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 448 FSKIEAGALKLEyrAVEITKLLEQIAKVFSSTSVKKGVTFKLnisDSVPScISLDPLRFSQVINNILSNAGKFTESGD-- 525
Cdd:COG4251   343 YSRVGRQELEFE--PVDLNELLEEVLEDLEPRIEERGAEIEV---GPLPT-VRGDPTLLRQVFQNLISNAIKYSRPGEpp 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 526 -ITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADisTTRKYGGTGLGLTISKRIIELMAGELKLTSQEGVGSEF 604
Cdd:COG4251   417 rIEIGAEREGGEWVFSVRDNGIGIDPEYAEKIFEIFQRLH--SRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATF 494

                  ....*.
gi 2738934608 605 TITMPV 610
Cdd:COG4251   495 YFTLPK 500
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
633-745 4.26e-38

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: 137.22  E-value: 4.26e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHLYGQAIIIAIT 712
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGRRTPIIALT 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2738934608 713 ANAFEEDQQRCLVAGMDDFISKPINKDQLYACL 745
Cdd:cd17546    81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
626-751 8.20e-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: 134.21  E-value: 8.20e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 626 PQLAGLNILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHL--- 702
Cdd:COG0784     1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLpdi 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2738934608 703 -------YGqaiiiaitanaFEEDQQRCLVAGMDDFISKPINKDQLYACLNKWLKA 751
Cdd:COG0784    81 piialtaYA-----------DEEDRERALEAGADDYLTKPVDPEELLEALRRLLAR 125
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
269-610 1.43e-35

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


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 139.71  E-value: 1.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 269 LVMIIFIILLTSVFIT-QLSRWLTTPIRKLAEQIDKFEpeNADTDTYLPQT-WLEVSRLQSQFSSLANKLALSFNRLHQA 346
Cdd:COG5000    11 LLLIALLLLLLALWLAlLLARRLTRPLRRLAEATRAVA--AGDLSVRLPVTgDDEIGELARAFNRMTDQLKEQREELEER 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 347 NHENE----------------------------LLNVRLKD--------------FNAQLEKQVDDKTNELVE------- 377
Cdd:COG5000    89 RRYLEtilenlpagvivldadgritlanpaaerLLGIPLEEligkpleellpeldLAELLREALERGWQEEIEltrdgrr 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 378 --AVRAAN-----------------NANRTKS--QFLANMSHEIRTPLNGILGMTQLLLDN-KDLAEEEHEELV----MI 431
Cdd:COG5000   169 tlLVRASPlrddgyvivfdditellRAERLAAwgELARRIAHEIKNPLTPIQLSAERLRRKlADKLEEDREDLEraldTI 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 432 HQSANNLLLILNDILDFSKIEagalKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNISDSVPScISLDPLRFSQVIN 511
Cdd:COG5000   249 IRQVDRLKRIVDEFLDFARLP----EPQLEPVDLNELLREVLALYEPALKEKDIRLELDLDPDLPE-VLADRDQLEQVLI 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 512 NILSNAGKFTES-GDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTqadisTTRKyGGTGLGLTISKRIIELMAG 590
Cdd:COG5000   324 NLLKNAIEAIEEgGEIEVSTRREDGRVRIEVSDNGPGIPEEVLERIFEPFF-----TTKP-KGTGLGLAIVKKIVEEHGG 397
                         410       420
                  ....*....|....*....|
gi 2738934608 591 ELKLTSQEGVGSEFTITMPV 610
Cdd:COG5000   398 TIELESRPGGGTTFTIRLPL 417
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
391-609 8.09e-35

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


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 140.66  E-value: 8.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 391 QFLANMSHEIRTPLNGILGMTQLLLD----NKDLA-------EEEHEElvMIH------QsannlllilndildFSKIEA 453
Cdd:NF033092  374 EFVANVSHELRTPLTTMRSYLEALADgawkDPELAprflgvtQNETER--MIRlvndllQ--------------LSRMDS 437
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 454 GALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNISDSVPScISLDPLRFSQVINNILSNAGKFT-ESGDITMSCTM 532
Cdd:NF033092  438 KDYKLNKEWVNFNEFFNYIIDRFEMILKNKNITFKREFPKRDLW-VEIDTDKITQVLDNIISNAIKYSpEGGTITFRLLE 516
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2738934608 533 VNDRMQISIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMP 609
Cdd:NF033092  517 THNRIIISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAESEEGKGTTIYFTLP 593
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
256-610 9.39e-35

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 136.08  E-value: 9.39e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 256 HANDVAVNAWGQSLVMIIFIILLTSVFITQLSRWLTTPIRKLAEQIDKFEPENADTDTYLPQTWLEVSRLQSQFSSLANK 335
Cdd:COG4191    12 LALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLLE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 336 LALSFNRLHQANHENELLNvRLKDFNAQLEKQVDDKT---NELVEAVRAAnnanrtkS--QFLANMSHEIRTPLNGILGM 410
Cdd:COG4191    92 ALLLLLLAALDAEENAELE-ELERDITELERAEEELRelqEQLVQSEKLA-------AlgELAAGIAHEINNPLAAILGN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 411 TQLL---LDNKDLAEEEHEELVMIHQSANNLLLILNDILDFSKIEagalKLEYRAVEITKLLEQIAKVFSSTSVKKGVTF 487
Cdd:COG4191   164 AELLrrrLEDEPDPEELREALERILEGAERAAEIVRSLRAFSRRD----EEEREPVDLNELIDEALELLRPRLKARGIEV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 488 KLNISDSVPScISLDPLRFSQVINNILSNA-----GKftESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTq 562
Cdd:COG4191   240 ELDLPPDLPP-VLGDPGQLEQVLLNLLINAidameEG--EGGRITISTRREGDYVVISVRDNGPGIPPEVLERIFEPFF- 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2738934608 563 adisTTRKYG-GTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMPV 610
Cdd:COG4191   316 ----TTKPVGkGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLPL 360
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
390-617 2.53e-34

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


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 137.41  E-value: 2.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 390 SQFLANMSHEIRTPLNGILGMTQLLLDNKDLAEEEHEELvmIHQSANNLLLILNDILDFSKIEAGalklEYRAVEITKLL 469
Cdd:COG5809   271 GELAAGIAHEIRNPLTSLKGFIQLLKDTIDEEQKTYLDI--MLSELDRIESIISEFLVLAKPQAI----KYEPKDLNTLI 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 470 EQIAKVFSSTSVKKGVTFKLNISDSVPsCISLDPLRFSQVINNILSNAGKFTES-GDITMSCT-MVNDRMQISIRDTGIG 547
Cdd:COG5809   345 EEVIPLLQPQALLKNVQIELELEDDIP-DILGDENQLKQVFINLLKNAIEAMPEgGNITIETKaEDDDKVVISVTDEGCG 423
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 548 ISSEQQAKLFTEFTqadistTRKYGGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMPVIISNSAS 617
Cdd:COG5809   424 IPEERLKKLGEPFY------TTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKLSEQVS 487
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
391-610 9.26e-33

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 130.35  E-value: 9.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 391 QFLANMSHEIRTPLNGILGMTQLLLdnKDLAEEEHEELV-MIHQSANNLLLILNDILDFSKIEAgalkLEYRAVEITKLL 469
Cdd:COG3852   137 ELAAGLAHEIRNPLTGIRGAAQLLE--RELPDDELREYTqLIIEEADRLNNLVDRLLSFSRPRP----PEREPVNLHEVL 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 470 EQIAKVFSSTsVKKGVTFKLNISDSVPScISLDPLRFSQVINNILSNA-------GKFT----ESGDITMSCTMVNDRMQ 538
Cdd:COG3852   211 ERVLELLRAE-APKNIRIVRDYDPSLPE-VLGDPDQLIQVLLNLVRNAaeampegGTITirtrVERQVTLGGLRPRLYVR 288
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2738934608 539 ISIRDTGIGISSEQQAKLFTEFTqadisTTRKyGGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMPV 610
Cdd:COG3852   289 IEVIDNGPGIPEEILDRIFEPFF-----TTKE-KGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPL 354
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
502-610 6.05e-32

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 120.06  E-value: 6.05e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608  502 DPLRFSQVINNILSNAGKFT-ESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADiSTTRKYGGTGLGLTI 580
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTD-KRSRKIGGTGLGLSI 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 2738934608  581 SKRIIELMAGELKLTSQEGVGSEFTITMPV 610
Cdd:smart00387  81 VKKLVELHGGEISVESEPGGGTTFTITLPL 110
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
387-607 6.82e-32

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: 126.94  E-value: 6.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 387 RTKSQFLANMSHEIRTPLNGILGMTQLLLDNKDLAEEEHEELV-MIHQSANNLLLILNDILDFSKIEAGALKLEYRAVEI 465
Cdd:TIGR02966 112 QMRRDFVANVSHELRTPLTVLRGYLETLADGPDEDPEEWNRALeIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDM 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 466 TKLLEQIAKVFSSTSVKKGVTFKLNISDSVPSCISLDPLRfsQVINNILSNAGKFT-ESGDITMSCTMVNDRMQISIRDT 544
Cdd:TIGR02966 192 PALLDHLRDEAEALSQGKNHQITFEIDGGVDVLGDEDELR--SAFSNLVSNAIKYTpEGGTITVRWRRDGGGAEFSVTDT 269
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2738934608 545 GIGISSEQQAKLFTEFTQADISTTRKYGGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTIT 607
Cdd:TIGR02966 270 GIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFSFI 332
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
631-745 2.86e-29

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: 114.62  E-value: 2.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 631 LNILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNP---HLY---- 703
Cdd:COG3706     2 ARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPrtaDIPiifl 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2738934608 704 -GQAIiiaitanafEEDQQRCLVAGMDDFISKPINKDQLYACL 745
Cdd:COG3706    82 tALDD---------EEDRARALEAGADDYLTKPFDPEELLARV 115
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
502-610 9.84e-28

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


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 107.84  E-value: 9.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 502 DPLRFSQVINNILSNAGKFT-ESGDITMSCTmVNDRMQISIRDTGIGISSEQQAKLFTEFTQADistTRKYGGTGLGLTI 580
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAaKAGEITVTLS-EGGELTLTVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGGTGLGLSI 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 2738934608 581 SKRIIELMAGELKLTSQEGVGSEFTITMPV 610
Cdd:pfam02518  78 VRKLVELLGGTITVESEPGGGTTVTLTLPL 107
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
273-609 5.72e-27

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: 114.79  E-value: 5.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 273 IFIILLTSVFITQLSRWLTT-----PIRKLAEQIDKFEPENADTDtylpqtwLEVSRLQSQFSSLAnklalsfnrlhqan 347
Cdd:TIGR01386 166 LILIAVLLVLLTALLGWWITrlglePLRRLSAVAARISPESLDQR-------LDPSRAPAELRELA-------------- 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 348 henellnvrlKDFNAQLEKqvddktneLVEAVRAAnnanrtkSQFLANMSHEIRTPLNGILGMTQLLLdNKDLAEEEHEE 427
Cdd:TIGR01386 225 ----------QSFNAMLGR--------LEDAFQRL-------SQFSADLAHELRTPLTNLLGQTQVAL-SQPRTGEEYRE 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 428 LVMIHQSANNLLLILNDILDF-SKIEAGALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNISDSVPScislDPLRF 506
Cdd:TIGR01386 279 VLESNLEELERLSRMVSDMLFlARADNGQLALERVRLDLAAELAKVAEYFEPLAEERGVRIRVEGEGLVRG----DPQMF 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 507 SQVINNILSNAGKFT-ESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTGLGLTISKRII 585
Cdd:TIGR01386 355 RRAISNLLSNALRHTpDGGTITVRIERRSDEVRVSVSNPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIM 434
                         330       340
                  ....*....|....*....|....
gi 2738934608 586 ELMAGELKLTSQEGvGSEFTITMP 609
Cdd:TIGR01386 435 EAHGGRASAESPDG-KTRFILRFP 457
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
246-609 8.14e-26

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 111.46  E-value: 8.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 246 WMVMTMLNRKHANdVAVNAWGQ----SLVMIIFIILLTSVFITQLSRWLTTPIRKLAEQIDKFEPENADTdtylpqtwle 321
Cdd:NF012163  141 ALGASPVERLTRN-TDINFDSQqkraSWLIVALALLLAALAAFLLARGLLAPVKRLVEATHRLAAGDYTT---------- 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 322 vsRLQSQFSSLANKLALSFNRLHQANHENEllnvrlkdfnaqlekqvddktnelveavraannanRTKSQFLANMSHEIR 401
Cdd:NF012163  210 --RVTPTSNDELGKLAQDFNQLASTLEKNE-----------------------------------QMRRDFMADISHELR 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 402 TPLNGILGMTQLLLDNKDLAEEEHeeLVMIHQSANNLLLILNDILDFSKIEAGALKLEYRAVEITKLLEQIAKVFSSTSV 481
Cdd:NF012163  253 TPLAVLRAELEAIQDGIRKFTPES--LDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFA 330
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 482 KKGVTFKLNISDSvpSCISLDPLRFSQVINNILSNAGKFTES-GDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEF 560
Cdd:NF012163  331 SAGLELEVSLPDS--SLVFGDRDRLMQLFNNLLENSLRYTDSgGSLHISASQRPKEVTLTVADSAPGVSDEQLARLFERF 408
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2738934608 561 TQADISTTRKYGGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMP 609
Cdd:NF012163  409 YRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVTLP 457
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
631-749 2.86e-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: 104.86  E-value: 2.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 631 LNILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPH--------L 702
Cdd:COG3437     7 PTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPStrdipvifL 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2738934608 703 YGQAIiiaitanafEEDQQRCLVAGMDDFISKPINKDQLYACLNKWL 749
Cdd:COG3437    87 TALAD---------PEDRERALEAGADDYLTKPFDPEELLARVRNAL 124
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
632-747 1.26e-24

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: 99.15  E-value: 1.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 632 NILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHLyGQAIIIAI 711
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPAT-RDIPVIAL 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2738934608 712 TANAFEEDQQRCLVAGMDDFISKPINKDQLYACLNK 747
Cdd:cd17548    80 TAYAMKGDREKILEAGCDGYISKPIDTREFLETVAK 115
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
335-610 1.24e-23

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 106.21  E-value: 1.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 335 KLALSFNRLHqaNHENELLN--VRLKDFNAQLEKQVddktnELVEAVRAAnnanrTKSQFLANMSHEIRTPLNGILGMTQ 412
Cdd:PRK11360  346 ELSVSTSLLH--NTHGEMIGalVIFSDLTERKRLQR-----RVARQERLA-----ALGELVAGVAHEIRNPLTAIRGYVQ 413
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 413 LLLDNKDLAEEEHEeLVMIHQSANNLLLILNDILDFSKieagALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNIS 492
Cdd:PRK11360  414 IWRQQTSDPPSQEY-LSVVLREVDRLNKVIDQLLEFSR----PRESQWQPVSLNALVEEVLQLFQTAGVQARVDFETELD 488
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 493 DSVPScISLDPLRFSQVINNILSNAGK-FTESGDITMSCTMVNDRMQ-ISIRDTGIGISSEQQAKLFTEFTqadistTRK 570
Cdd:PRK11360  489 NELPP-IWADPELLKQVLLNILINAVQaISARGKIRIRTWQYSDGQVaVSIEDNGCGIDPELLKKIFDPFF------TTK 561
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2738934608 571 YGGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMPV 610
Cdd:PRK11360  562 AKGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPI 601
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
394-612 3.98e-23

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 103.33  E-value: 3.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 394 ANMSHEIRTPLNGILGMTQLLLDNKDLAEEEHE-ELVMIHQsANNLLLILNDILDFSKieagALKLEYRAVEITKLLEQI 472
Cdd:PRK10364  242 AGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQlAQVMAKE-ADRLNRVVSELLELVK----PTHLALQAVDLNDLINHS 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 473 AKVFSSTSVKKGVTFKLNISDSVPScISLDPLRFSQVINNILSNA-GKFTESGDITMSCTMVNDRMQISIRDTGIGISSE 551
Cdd:PRK10364  317 LQLVSQDANSREIQLRFTANDTLPE-IQADPDRLTQVLLNLYLNAiQAIGQHGVISVTASESGAGVKISVTDSGKGIAAD 395
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2738934608 552 QQAKLFTEFTqadistTRKYGGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMPVII 612
Cdd:PRK10364  396 QLEAIFTPYF------TTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLPVNI 450
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
346-609 5.04e-23

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 103.57  E-value: 5.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 346 ANHENELLNVRLKDFNAQLEKQVDDKTNELVEAVRAANNANRTKSQFLANMSHEIRTPLNGILGMTQLLLDNKD------ 419
Cdd:NF040691  228 AGDLSERMPVKGEDDLARLARSFNQMADSLQRQIRQLEELSRLQQRFVSDVSHELRTPLTTIRMAADVIHDSRDdfdpat 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 420 --LAEEEHEELVMIHQsannlllILNDILDFSKIEAGALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNIsDSVPS 497
Cdd:NF040691  308 arSAELLHTELDRFES-------LLSDLLEISRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVDA-PGTPV 379
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 498 CISLDPLRFSQVINNILSNAGKFTESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTGLG 577
Cdd:NF040691  380 VAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTVAQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLG 459
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2738934608 578 LTISKRIIELMAGELKLTSQEGVGSEFTITMP 609
Cdd:NF040691  460 LAIALEDARLHGGWLEAWGRPGQGSQFRLTLP 491
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
633-743 5.19e-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: 94.53  E-value: 5.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPH--------LYG 704
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPttpviiltAHG 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2738934608 705 QaiiiaitanafEEDQQRCLVAGMDDFISKPINKDQLYA 743
Cdd:pfam00072  81 D-----------EDDAVEALEAGADDFLSKPFDPDELLA 108
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
633-736 1.73e-21

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


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 89.86  E-value: 1.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPH----------- 701
Cdd:cd17538     2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPEtrhipvimita 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2738934608 702 LYGQaiiiaitanafeEDQQRCLVAGMDDFISKPI 736
Cdd:cd17538    82 LDDR------------EDRIRGLEAGADDFLSKPI 104
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
502-609 2.04e-21

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: 89.86  E-value: 2.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 502 DPLRFSQVINNILSNAGKFTESGDITMSCTMVND--RMQISIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTGLGLT 579
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTPDGGRIRCILEKFRlnRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGLGLS 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 2738934608 580 ISKRIIELMAGELKLTSQEGVGSEFTITMP 609
Cdd:cd16925    81 IVKEFVELHGGTVTVSDAPGGGALFQVELP 110
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
633-743 5.16e-21

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: 91.94  E-value: 5.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHL--------YG 704
Cdd:COG0745     4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDipiimltaRD 83
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2738934608 705 QaiiiaitanafEEDQQRCLVAGMDDFISKPINKDQLYA 743
Cdd:COG0745    84 D-----------EEDRVRGLEAGADDYLTKPFDPEELLA 111
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
508-609 1.90e-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: 1.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 508 QVINNILSNAGKFTESGD---ITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQadISTTRKYGGTGLGLTISKRI 584
Cdd:cd16921     3 QVLTNLLGNAIKFRRPRRpprIEVGAEDVGEEWTFYVRDNGIGIDPEYAEKVFGIFQR--LHSREEYEGTGVGLAIVRKI 80
                          90       100
                  ....*....|....*....|....*
gi 2738934608 585 IELMAGELKLTSQEGVGSEFTITMP 609
Cdd:cd16921    81 IERHGGRIWLESEPGEGTTFYFTLP 105
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
502-609 3.07e-20

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: 86.36  E-value: 3.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 502 DPLRFSQVINNILSNAGKFTESG-DITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTGLGLTI 580
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTGgKLRIRAAQTPQEVRLDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGLGLAI 80
                          90       100
                  ....*....|....*....|....*....
gi 2738934608 581 SKRIIELMAGELKLTSQEGVGSEFTITMP 609
Cdd:cd16946    81 CHNIALAHGGTISAEHSPLGGLRLVLTLP 109
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
503-610 3.22e-20

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: 86.32  E-value: 3.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 503 PLRFSQVINNILSNAGK-FTESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTqadisTTRKYG-GTGLGLTI 580
Cdd:cd16943     1 PSQLNQVLLNLLVNAAQaMEGRGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPFF-----TTKPVGeGTGLGLSL 75
                          90       100       110
                  ....*....|....*....|....*....|
gi 2738934608 581 SKRIIELMAGELKLTSQEGVGSEFTITMPV 610
Cdd:cd16943    76 SYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
PRK09303 PRK09303
histidine kinase;
349-610 5.33e-19

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 89.63  E-value: 5.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 349 ENELLnvRLKDFNAQLEKQVDdktnelveavraannanrTKSQFLANMSHEIRTPLN--GILGMTQLLLDNKDLAEEEHE 426
Cdd:PRK09303  131 SDELF--VLRQENETLLEQLK------------------FKDRVLAMLAHDLRTPLTaaSLALETLELGQIDEDTELKPA 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 427 ELVMIHQSANNLllilndildFSKIE-------------AGALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNISD 493
Cdd:PRK09303  191 LIEQLQDQARRQ---------LEEIErlitdllevgrtrWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDIPS 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 494 SVPsCISLDPLRFSQVINNILSNAGKFTESGDiTMSCTMV---NDRMQISIRDTGIGISSEQQAKLFTEFT--QADISTT 568
Cdd:PRK09303  262 DLP-SVYADQERIRQVLLNLLDNAIKYTPEGG-TITLSMLhrtTQKVQVSICDTGPGIPEEEQERIFEDRVrlPRDEGTE 339
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2738934608 569 rkygGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMPV 610
Cdd:PRK09303  340 ----GYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFTLPV 377
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
391-610 5.74e-19

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: 90.95  E-value: 5.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 391 QFLANMSHEIRTPLNGILGMTQLLLDNKdlaeEEHEEL--VMIHQsannlllilndildFSKIE---------AGALKLE 459
Cdd:COG5805   289 QLAAGIAHEIRNPLTSIKGFLQLLQPGI----EDKEEYfdIMLSE--------------LDRIEsiiseflalAKPQAVN 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 460 YRAVEITKLLEQIAKVFSSTSVKKGVTFKLNISDSVPsCISLDPLRFSQVINNILSNAGKFTES-GDITMSCTMVNDRMQ 538
Cdd:COG5805   351 KEKENINELIQDVVTLLETEAILHNIQIRLELLDEDP-FIYCDENQIKQVFINLIKNAIEAMPNgGTITIHTEEEDNSVI 429
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2738934608 539 ISIRDTGIGISSEQQAKLFTEFTqadistTRKYGGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMPV 610
Cdd:COG5805   430 IRVIDEGIGIPEERLKKLGEPFF------TTKEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLPL 495
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
270-609 6.39e-19

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 90.60  E-value: 6.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 270 VMIIFIILLtSVFITQLsrwlttPIRKLAEQIDKFEPENADTdtylpqtwlevsRLQSQFSSLA-NKLALSFNRLhqanh 348
Cdd:PRK09835  196 LLIVFIVLL-AVHKGHA------PIRSVSRQIQNITSKDLDV------------RLDPQTVPIElEQLVLSFNHM----- 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 349 enellnvrlkdfnaqLEKQVDDKTnelveavRAANnanrtksqFLANMSHEIRTPLNGILGMTQLLLdNKDLAEEEHEEL 428
Cdd:PRK09835  252 ---------------IERIEDVFT-------RQSN--------FSADIAHEIRTPITNLITQTEIAL-SQSRSQKELEDV 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 429 VMIHQSANNLLLILNDILDF-SKIEAGALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNisdSVPSCISLDPLRFS 507
Cdd:PRK09835  301 LYSNLEELTRMAKMVSDMLFlAQADNNQLIPEKKMLDLADEVGKVFDFFEAWAEERGVELRFV---GDPCQVAGDPLMLR 377
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 508 QVINNILSNAGKFTESGD-ITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTGLGLTISKRIIE 586
Cdd:PRK09835  378 RAISNLLSNALRYTPAGEaITVRCQEVDHQVQLVVENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVV 457
                         330       340
                  ....*....|....*....|...
gi 2738934608 587 LMAGELKLTSqEGVGSEFTITMP 609
Cdd:PRK09835  458 AHKGTVAVTS-DARGTRFVISLP 479
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
633-745 1.72e-18

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: 81.35  E-value: 1.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHL---------- 702
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLantpaialtg 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2738934608 703 YGQaiiiaitanafEEDQQRCLVAGMDDFISKPINKDQLYACL 745
Cdd:cd17580    81 YGQ-----------PEDRERALEAGFDAHLVKPVDPDELIELI 112
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
634-735 2.06e-18

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 80.73  E-value: 2.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 634 LLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQN-PHL-------YGQ 705
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELpPDIpvivltaKAD 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 2738934608 706 aiiiaitanafEEDQQRCLVAGMDDFISKP 735
Cdd:cd00156    81 -----------EEDAVRALELGADDYLVKP 99
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
392-610 6.27e-18

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 87.38  E-value: 6.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 392 FLANMSHEIRTPLNGILGMTQLLLD--NKDLAEEEHE---------ELVM-IHQsannlllilndildFSKIEAGALKLE 459
Cdd:PRK10549  243 FMADISHELRTPLAVLRGELEAIQDgvRKFTPESVASlqaevgtltKLVDdLHQ--------------LSLSDEGALAYR 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 460 YRAVEITKLLEQIAKVFSSTSVKKGVTFKLNISDSVPscISLDPLRFSQVINNILSNAGKFTES-GDITMSCTMVNDRMQ 538
Cdd:PRK10549  309 KTPVDLVPLLEVAGGAFRERFASRGLTLQLSLPDSAT--VFGDPDRLMQLFNNLLENSLRYTDSgGSLHISAEQRDKTLR 386
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2738934608 539 ISIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMPV 610
Cdd:PRK10549  387 LTFADSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRIIAAHSPFGGVSITVELPL 458
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
632-735 1.44e-17

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: 78.66  E-value: 1.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 632 NILLVEDNPVNQIVLKKMLHSTE--CNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQ-NPHL------ 702
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRElDPDTkiiils 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2738934608 703 -YGQaiiiaitanafEEDQQRCLVAGMDDFISKP 735
Cdd:COG4753    81 gYSD-----------FEYAQEAIKLGADDYLLKP 103
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
506-609 4.25e-17

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: 77.37  E-value: 4.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 506 FSQVINNILSNAGKFTESgDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTGLGLTISKRII 585
Cdd:cd16949     1 LARALENVLRNALRYSPS-KILLDISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAIAERAI 79
                          90       100
                  ....*....|....*....|....
gi 2738934608 586 ELMAGELKLTSQEGVGSEFTITMP 609
Cdd:cd16949    80 EQHGGKIKASNRKPGGLRVRIWLP 103
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
633-736 2.36e-16

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: 75.24  E-value: 2.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPH--------LYG 704
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPAtrhipvifLTA 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2738934608 705 QAIIiaitanafeEDQQRCLVAGMDDFISKPI 736
Cdd:cd19920    81 LTDT---------EDKVKGFELGAVDYITKPF 103
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
508-609 2.62e-16

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: 75.13  E-value: 2.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 508 QVINNILSNA-----GKFTESGDITMSCTMVNDR-MQISIRDTGIGISSEQQAKLFTEFTqadistTRKYGGTGLGLTIS 581
Cdd:cd16920     3 QVLINLVRNGieamsEGGCERRELTIRTSPADDRaVTISVKDTGPGIAEEVAGQLFDPFY------TTKSEGLGMGLSIC 76
                          90       100
                  ....*....|....*....|....*...
gi 2738934608 582 KRIIELMAGELKLTSQEGVGSEFTITMP 609
Cdd:cd16920    77 RSIIEAHGGRLSVESPAGGGATFQFTLP 104
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
632-757 8.19e-16

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: 80.39  E-value: 8.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 632 NILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQ-NPHL-------Y 703
Cdd:COG2204     4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRAlDPDLpvilltgY 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2738934608 704 GQaiiiaitanafEEDQQRCLVAGMDDFISKPINKDQLYACLNKWLKALLNEQQ 757
Cdd:COG2204    84 GD-----------VETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRE 126
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
395-610 1.23e-15

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 80.27  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 395 NMSHEIRTPLNGILGMTQLLLDNKDLAEEEH------------EELV--MIHQSannlllilndildfskieagalKLEY 460
Cdd:PRK11100  262 TLTHELKSPLAAIRGAAELLQEDPPPEDRARftgniltqsarlQQLIdrLLELA----------------------RLEQ 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 461 R-------AVEITKLLEQIAKVFSSTSVKKGVTFKLNISDSVPSCislDPLRFSQVINNILSNAGKFT-ESGDITMSCTM 532
Cdd:PRK11100  320 RqelevlePVALAALLEELVEAREAQAAAKGITLRLRPDDARVLG---DPFLLRQALGNLLDNAIDFSpEGGTITLSAEV 396
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 533 VNDRMQISIRDTGIGISSEQQAKLFTEFtqadISTTRKYGG---TGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMP 609
Cdd:PRK11100  397 DGEQVALSVEDQGPGIPDYALPRIFERF----YSLPRPANGrksTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLP 472

                  .
gi 2738934608 610 V 610
Cdd:PRK11100  473 R 473
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
632-741 1.64e-15

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: 73.24  E-value: 1.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 632 NILLVEDNPVNQIVLKKMLHST-ECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHL-------- 702
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRSAgYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLedvpivmi 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2738934608 703 --YGQaiiiaitanafEEDQQRCLVAGMDDFISKPINKDQL 741
Cdd:cd17551    82 taDTD-----------REVRLRALEAGATDFLTKPFDPVEL 111
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
634-735 1.97e-15

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: 72.44  E-value: 1.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 634 LLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPH------LYGQAI 707
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSdipiimLTAKDE 80
                          90       100
                  ....*....|....*....|....*...
gi 2738934608 708 iiaitanafEEDQQRCLVAGMDDFISKP 735
Cdd:cd17574    81 ---------EEDKVLGLELGADDYITKP 99
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
392-609 2.27e-15

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 79.28  E-value: 2.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 392 FLANMSHEIRTP---LNGILGMTQllldNKDL--AEEEHEELVMIHQsANNLLLILNDILDFSKIEAG-ALKLEYRaVEI 465
Cdd:PRK11006  207 FFANVSHELRTPltvLQGYLEMMQ----DQPLegALREKALHTMREQ-TQRMEGLVKQLLTLSKIEAApTIDLNEK-VDV 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 466 TKLLEQIAKVFSSTSVKKGvTFKLNISDSVPSCISLDPLRfsQVINNILSNAGKFTESG-DITMSCTMVNDRMQISIRDT 544
Cdd:PRK11006  281 PMMLRVLEREAQTLSQGKH-TITFEVDNSLKVFGNEDQLR--SAISNLVYNAVNHTPEGtHITVRWQRVPQGAEFSVEDN 357
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2738934608 545 GIGISSEQQAKLFTEFTQADISTTRKYGGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMP 609
Cdd:PRK11006  358 GPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLP 422
PRK10490 PRK10490
sensor protein KdpD; Provisional
377-610 4.55e-15

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 79.31  E-value: 4.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 377 EAVRAANNANRTKSQFLANMSHEIRTPLNGILGMTQLLLdnKDLAEE--EHEELV-MIHQSANNLLLILNDILDFSKIEA 453
Cdd:PRK10490  652 EQARLASEREQLRNALLAALSHDLRTPLTVLFGQAEILT--LDLASEgsPHARQAsEIRQQVLNTTRLVNNLLDMARIQS 729
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 454 GA--LKLEYRAVE--ITKLLEQIAKVFSstsvkkGVTFKLNISDSVPsCISLDPLRFSQVINNILSNAGKFT-ESGDITM 528
Cdd:PRK10490  730 GGfnLRKEWLTLEevVGSALQMLEPGLS------GHPINLSLPEPLT-LIHVDGPLFERVLINLLENAVKYAgAQAEIGI 802
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 529 SCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADISTTrkYGGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITM 608
Cdd:PRK10490  803 DAHVEGERLQLDVWDNGPGIPPGQEQLIFDKFARGNKESA--IPGVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVTL 880

                  ..
gi 2738934608 609 PV 610
Cdd:PRK10490  881 PL 882
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
502-606 5.01e-15

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: 71.67  E-value: 5.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 502 DPLRFSQVINNILSNAGKFTESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADistTRKYGGTGLGLTIS 581
Cdd:cd16940    10 DALLLFLLLRNLVDNAVRYSPQGSRVEIKLSADDGAVIRVEDNGPGIDEEELEALFERFYRSD---GQNYGGSGLGLSIV 86
                          90       100
                  ....*....|....*....|....*
gi 2738934608 582 KRIIELMAGELKLTSQEGVGSEFTI 606
Cdd:cd16940    87 KRIVELHGGQIFLGNAQGGGLEAWV 111
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
632-741 6.06e-15

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


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 72.06  E-value: 6.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 632 NILLVEDNPVNQIVLKKMLHST--ECNLKQANDGLEALEILQ---SYQA----DIILMDCQMPNMDGYQCTKEIKQNPHL 702
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAgvPNELHVVRDGEEALDFLRgegEYADaprpDLILLDLNMPRMDGFEVLREIKADPDL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2738934608 703 -----------YgqaiiiaitanaFEEDQQRCLVAGMDDFISKPINKDQL 741
Cdd:cd17557    81 rripvvvlttsD------------AEEDIERAYELGANSYIVKPVDFEEF 118
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
633-735 9.74e-15

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


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 70.87  E-value: 9.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQ---------SYQADIILMDCQMPNMDGYQCTKEIKQNPHLy 703
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLEnlakegndlSKELDLIITDIEMPKMDGYELTFELRDDPRL- 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2738934608 704 GQAIIIAITANAFEEDQQRCLVAGMDDFISKP 735
Cdd:cd19924    80 ANIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
510-609 1.03e-14

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


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 70.69  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 510 INNILSNAGKFT-ESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTGLGLTISKRIIELM 588
Cdd:cd16952     5 FSNLVSNAVKYTpPSDTITVRWSQEESGARLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAIVKHVMSRH 84
                          90       100
                  ....*....|....*....|.
gi 2738934608 589 AGELKLTSQEGVGSEFTITMP 609
Cdd:cd16952    85 DARLLIASELGKGSRFTCLFP 105
envZ PRK09467
osmolarity sensor protein; Provisional
372-599 1.19e-14

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 76.87  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 372 TNELVEAVRAANNANRTKSQF-------LANMSHEIRTPLNGILGMTQLLLDNKD-LAE------EEHEELvmIHQsann 437
Cdd:PRK09467  205 ASEVRSVTRAFNQMAAGIKQLeddrtllMAGVSHDLRTPLTRIRLATEMMSEEDGyLAEsinkdiEECNAI--IEQ---- 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 438 lllilndildF-SKIEAGAlKLEYRAVEITKLLEQIAKVFSstsvKKGVTFKLNISDSvPSCISLDPLRFSQVINNILSN 516
Cdd:PRK09467  279 ----------FiDYLRTGQ-EMPMEMADLNALLGEVIAAES----GYEREIETALQPG-PIEVPMNPIAIKRALANLVVN 342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 517 AGKFTeSGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADisTTRKYGGTGLGLTISKRIIELMAGELKLT- 595
Cdd:PRK09467  343 AARYG-NGWIKVSSGTEGKRAWFQVEDDGPGIPPEQLKHLFQPFTRGD--SARGSSGTGLGLAIVKRIVDQHNGKVELGn 419

                  ....
gi 2738934608 596 SQEG 599
Cdd:PRK09467  420 SEEG 423
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
633-752 2.22e-14

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: 70.06  E-value: 2.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLK---QANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIK-QNPHL------ 702
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIDWEELGFEvvgEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIReLYPDIkiiils 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2738934608 703 -YGQaiiiaitanaFEEDQQrCLVAGMDDFISKPINKDQLYACLNKWLKAL 752
Cdd:cd17536    81 gYDD----------FEYAQK-AIRLGVVDYLLKPVDEEELEEALEKAKEEL 120
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
633-741 3.16e-14

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: 69.66  E-value: 3.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHLyGQAIIIAIT 712
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDL-KDIPVILLT 79
                          90       100
                  ....*....|....*....|....*....
gi 2738934608 713 ANAFEEDQQRCLVAGMDDFISKPINKDQL 741
Cdd:cd17598    80 TLSDPRDVIRGLECGADNFITKPYDEKYL 108
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
508-606 3.36e-14

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: 69.02  E-value: 3.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 508 QVINNILSNA----GKFtESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTqadisTTRKYG-GTGLGLTISK 582
Cdd:cd16976     3 QVLMNLLQNAldamGKV-ENPRIRIAARRLGGRLVLVVRDNGPGIAEEHLSRVFDPFF-----TTKPVGkGTGLGLSISY 76
                          90       100
                  ....*....|....*....|....
gi 2738934608 583 RIIELMAGELKLTSQEGVGSEFTI 606
Cdd:cd16976    77 GIVEEHGGRLSVANEEGAGARFTF 100
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
628-757 4.10e-14

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 70.00  E-value: 4.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 628 LAGLNILLVEDNPVNQIVLKKMLHSTE--CNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPH---- 701
Cdd:COG4565     1 MKMIRVLIVEDDPMVAELLRRYLERLPgfEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPdvdv 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 702 --LYGQAIiiaitanafEEDQQRCLVAGMDDFISKPINKDQLYACLNKWL--KALLNEQQ 757
Cdd:COG4565    81 ivITAARD---------PETVREALRAGVVDYLIKPFTFERLREALERYLeyRRLLREDQ 131
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
632-747 5.74e-14

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: 68.84  E-value: 5.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 632 NILLVEDNPVNQIVLKKMLHST-ECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQ---NPHL----- 702
Cdd:cd17542     2 KVLIVDDAAFMRMMLKDILTKAgYEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKidpNAKVimcsa 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2738934608 703 YGQaiiiaitanafEEDQQRCLVAGMDDFISKPINKDQLYACLNK 747
Cdd:cd17542    82 MGQ-----------EEMVKEAIKAGAKDFIVKPFQPERVLEAVEK 115
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
363-609 8.15e-14

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 74.11  E-value: 8.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 363 QLEKQVDDkTNELVEAVRAannanrtksqflanMSHEIRTPLNGILGMTQLlldnkdlaeEEHEELV-MIHQSANNLLLI 441
Cdd:COG3290   178 RLEEELEG-VKELAEALRA--------------QRHDFRNHLHTISGLLQL---------GEYDEALeYIDEISEELQEL 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 442 LNDILDFSKIEAgalkleyraveITKLLeqIAKvfSSTSVKKGVTFKLNISDSVPsCISLDPLRFSQVINNILSNA---- 517
Cdd:COG3290   234 IDSLLSRIGNPV-----------LAALL--LGK--AARARERGIDLTIDIDSDLP-DLPLSDTDLVTILGNLLDNAieav 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 518 -GKFTESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTE-FTqadistTRKYGGTGLGLTISKRIIELMAGELKLT 595
Cdd:COG3290   298 eKLPEEERRVELSIRDDGDELVIEVEDSGPGIPEELLEKIFERgFS------TKLGEGRGLGLALVKQIVEKYGGTIEVE 371
                         250
                  ....*....|....
gi 2738934608 596 SQEGVGSEFTITMP 609
Cdd:COG3290   372 SEEGEGTVFTVRLP 385
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
508-608 8.29e-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: 68.69  E-value: 8.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 508 QVINNILSNAGKFTESGDIT-MSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTGLGLTISKRIIE 586
Cdd:cd16947    23 RILKNLISNAIKYGSDGKFLgMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRNSAKQGNGLGLTITKRLAE 102
                          90       100
                  ....*....|....*....|..
gi 2738934608 587 LMAGELKLTSQEGVGSEFTITM 608
Cdd:cd16947   103 SMGGSIYVNSKPYEKTVFTVTL 124
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
631-741 1.08e-13

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


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 68.19  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 631 LNILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQAD--IILMDCQMPNMDGYQCTKEIK------QNPHL 702
Cdd:cd19933     1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHSfqLVLLDLCMPEMDGFEVALRIRklfgrrERPLI 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2738934608 703 YGQAIIIAitanafEEDQQRCLVAGMDDFISKPINKDQL 741
Cdd:cd19933    81 VALTANTD------DSTREKCLSLGMNGVITKPVSLHAL 113
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
631-745 4.46e-13

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: 66.41  E-value: 4.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 631 LNILLVEDNPVNQIVLKKML-HSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPH------LY 703
Cdd:cd17593     1 MKVLICDDSSMARKQLARALpADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLetkvivVS 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2738934608 704 G--QaiiiaitanafEEDQQRCLVAGMDDFISKPINKDQLYACL 745
Cdd:cd17593    81 GdvQ-----------PEAKERVLELGALAFLKKPFDPEKLAQLL 113
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
311-650 6.63e-13

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 72.40  E-value: 6.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 311 TDTYLPQTWLEVSRLQSQFSSLANklALSFNRLHQanhENELLNVRLKdfNAQLekqvddktnelVEAVRAannanrtks 390
Cdd:PRK13837  400 QRYGLRPPAGELQLLELALDCLAH--AIERRRLET---ERDALERRLE--HARR-----------LEAVGT--------- 452
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 391 qFLANMSHEIRTPLNGILGMTQLLLDNKDLAEEEHEELVMIHQSANNLLLILNDILDFSKIEAGALKleyrAVEITKLLE 470
Cdd:PRK13837  453 -LASGIAHNFNNILGAILGYAEMALNKLARHSRAARYIDEIISAGARARLIIDQILAFGRKGERNTK----PFDLSELVT 527
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 471 QIAKVFSsTSVKKGVTFKLNiSDSVPSCISLDPLRFSQVINNILSNAGK-FTESGDITMSCTMVNDR------------- 536
Cdd:PRK13837  528 EIAPLLR-VSLPPGVELDFD-QDQEPAVVEGNPAELQQVLMNLCSNAAQaMDGAGRVDISLSRAKLRapkvlshgvlppg 605
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 537 --MQISIRDTGIGISSEQQAKLFTEFTqadisTTRKyGGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMPVI--I 612
Cdd:PRK13837  606 ryVLLRVSDTGAGIDEAVLPHIFEPFF-----TTRA-GGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLPPSskV 679
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2738934608 613 SNSASVDNQSTATPQLAGLNILLVEDNPVNQIVLKKML 650
Cdd:PRK13837  680 PVAPQAFFGPGPLPRGRGETVLLVEPDDATLERYEEKL 717
pleD PRK09581
response regulator PleD; Reviewed
633-743 8.11e-13

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 71.09  E-value: 8.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNP---H-------- 701
Cdd:PRK09581    5 ILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPattHipvvmvta 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2738934608 702 LYGQaiiiaitanafeEDQQRCLVAGMDDFISKPINKDQLYA 743
Cdd:PRK09581   85 LDDP------------EDRVRGLEAGADDFLTKPINDVALFA 114
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
508-609 9.53e-13

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: 64.78  E-value: 9.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 508 QVINNILSNAGKFTeSGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADISttRKYGGTGLGLTISKRIIEL 587
Cdd:cd16950     3 RVLSNLVDNALRYG-GGWVEVSSDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNA--RGTSGTGLGLAIVQRISDA 79
                          90       100
                  ....*....|....*....|..
gi 2738934608 588 MAGELKLTSQEGVGSEFTITMP 609
Cdd:cd16950    80 HGGSLTLANRAGGGLCARIELP 101
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
504-609 1.30e-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: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 504 LRFsqVINNILSNAGKFT-ESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTE-FTQADISTTRKygGTGLGLTIS 581
Cdd:cd16948     6 LSF--IIGQIVSNALKYSkQGGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKgFTGENGRNFQE--STGMGLYLV 81
                          90       100
                  ....*....|....*....|....*...
gi 2738934608 582 KRIIELMAGELKLTSQEGVGSEFTITMP 609
Cdd:cd16948    82 KKLCDKLGHKIDVESEVGEGTTFTITFP 109
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
631-685 1.67e-12

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: 62.59  E-value: 1.67e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2738934608  631 LNILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMP 685
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
632-700 3.79e-12

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: 63.95  E-value: 3.79e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2738934608 632 NILLVEDNPVNQIVLKKMLHSTEcNLK---QANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEI-KQNP 700
Cdd:cd17541     2 RVLIVDDSAVMRKLLSRILESDP-DIEvvgTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRImAERP 73
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
386-435 3.88e-12

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: 61.84  E-value: 3.88e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2738934608 386 NRTKSQFLANMSHEIRTPLNGILGMTQLLLDNKDLAEEEHEELVMIHQSA 435
Cdd:cd00082     1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLERIREEA 50
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
633-741 6.12e-12

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: 62.91  E-value: 6.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLhSTECNLK---QANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQ-NPHLygqaii 708
Cdd:cd17535     1 VLIVDDHPLVREGLRRLL-ESEPDIEvvgEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRrYPDL------ 73
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2738934608 709 IAITANAFEEDQQ--RCLVAGMDDFISKPINKDQL 741
Cdd:cd17535    74 KVIVLTAHDDPEYvlRALKAGAAGYLLKDSSPEEL 108
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
633-702 1.14e-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: 61.62  E-value: 1.14e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHL 702
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADF 70
PRK13557 PRK13557
histidine kinase; Provisional
457-697 1.74e-11

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 67.39  E-value: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 457 KLEYRAVEITKLLEQIAKVFSSTsVKKGVTFKLNISDSVPSCiSLDPLRFSQVINNILSNA-GKFTESGDITMSCTMV-- 533
Cdd:PRK13557  231 RLEGRVLNLNGLVSGMGELAERT-LGDAVTIETDLAPDLWNC-RIDPTQAEVALLNVLINArDAMPEGGRVTIRTRNVei 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 534 --NDRMQ-----------ISIRDTGIGISSEQQAKLFTEFTqadisTTRKYG-GTGLGLTISKRIIELMAGELKLTSQEG 599
Cdd:PRK13557  309 edEDLAMyhglppgryvsIAVTDTGSGMPPEILARVMDPFF-----TTKEEGkGTGLGLSMVYGFAKQSGGAVRIYSEVG 383
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 600 VGSEFTITMPV--------IISNSASVDNQSTATpqlaglnILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQ 671
Cdd:PRK13557  384 EGTTVRLYFPAsdqaenpeQEPKARAIDRGGTET-------ILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILD 456
                         250       260
                  ....*....|....*....|....*...
gi 2738934608 672 SY-QADIILMDCQMP-NMDGYQCTKEIK 697
Cdd:PRK13557  457 SHpEVDLLFTDLIMPgGMNGVMLAREAR 484
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
509-609 2.87e-11

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: 60.76  E-value: 2.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 509 VINNILSNA-----GKFTESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTqadisTTRKYGGTGLGLTISKR 583
Cdd:cd16915     4 IVGNLIDNAldalaATGAPNKQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVFERGV-----STKGQGERGIGLALVRQ 78
                          90       100
                  ....*....|....*....|....*.
gi 2738934608 584 IIELMAGELKLTSQEGVGSEFTITMP 609
Cdd:cd16915    79 SVERLGGSITVESEPGGGTTFSIRIP 104
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
389-454 3.05e-11

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 59.53  E-value: 3.05e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2738934608 389 KSQFLANMSHEIRTPLNGILGMTQLLLDNKdLAEEEHEELVMIHQSANNLLLILNDILDFSKIEAG 454
Cdd:pfam00512   2 KSEFLANLSHELRTPLTAIRGYLELLRDEK-LDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
110-611 3.20e-11

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 66.19  E-value: 3.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 110 NIRANVADRDYFIHAPSNKQGYISTIFKGRGFGSLPIVAVSAPIYIEDTFTGVVEGSLMFDYFASLRPSLFSHQGDLLIL 189
Cdd:COG2972     1 LSKSLSLLSIVLLLLILLLLVLLILLLSLLLIILLLLLLLILLLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 190 DAANKVVFSTIDDFKEMQQLSNEEIDSFANEERFIIFDAHNEQQYYAKQARLADHNWMVMTMLNRKHANDVAVNAWGQSL 269
Cdd:COG2972    81 LILLLLLLLLLLLILLLSLLLLLALILLLALLLLLSILLLILGLLLIILLLLSLLGWTLVSLIPKSELFRGLFSLRRLIL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 270 VMIIFIILLTSVFITQLSRWLTTPIRKLAEQIDKFEPENadtdtylpqtwleVSRLQSQFSSLANKLALSFNRLHQanhe 349
Cdd:COG2972   161 LIILLLLLLALLLSYLLSRSITRPIKRLKKAMKKVEKGD-------------LVRLEVSGNDEIGILARSFNEMVE---- 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 350 nellnvRLKdfnaQLEKQVDDKTNELVEAVRAANnanrtKSQ----FLANMsheirtpLNGILGMtqLLLDNKDLAEEeh 425
Cdd:COG2972   224 ------RIK----ELIEEVYELELEKKEAELKAL-----QAQinphFLFNT-------LNSIRWL--AELEDPEEAEE-- 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 426 eelvMIHQsannlllilndildFSKI---------EAGALKLEyraVEITKLLEQIAKV-FsstsvKKGVTFKLNISDSV 495
Cdd:COG2972   278 ----MLEA--------------LSKLlryslskgdELVTLEEE---LELIKSYLEIQKLrF-----GDRLEVEIEIDEEL 331
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 496 PSCisLDPLRFSQVI--NNILSNAGKFTESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFtqadistTRKYGG 573
Cdd:COG2972   332 LDL--LIPKLILQPLveNAIEHGIEPKEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLLEEL-------SSKGEG 402
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 2738934608 574 TGLGLTISKRIIELMAGE---LKLTSQEGVGSEFTITMPVI 611
Cdd:COG2972   403 RGIGLRNVRERLKLYYGEeygLEIESEPGEGTTVTIRIPLE 443
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
618-750 3.98e-11

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 60.58  E-value: 3.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 618 VDNQstatpqlAGLNILLVEdnpvnqiVLKKMLHSTEcnlkQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIK 697
Cdd:COG5803     8 VDDQ-------AGIRMLLKE-------VLKKEGYEVF----QAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIK 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2738934608 698 -QNPHL-------YGQAIIIaitanafEEDQQRclvaGMDDFISKPINKDQLYACLNKWLK 750
Cdd:COG5803    70 eIDPDIpvimmtaYGELDMV-------EEAKEL----GAKGYFTKPFDIDELREAVNKLLK 119
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
632-747 4.32e-11

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: 60.49  E-value: 4.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 632 NILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQN-PHLygqaiiia 710
Cdd:cd17569     2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERyPDT-------- 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2738934608 711 itanafeedqQRCLVAGMDD---------------FISKPINKDQLYACLNK 747
Cdd:cd17569    74 ----------VRILLTGYADldaaieainegeiyrFLTKPWDDEELKETIRQ 115
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
389-454 4.92e-11

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 58.73  E-value: 4.92e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2738934608  389 KSQFLANMSHEIRTPLNGILGMTQLLLDnKDLAEEEHEELVMIHQSANNLLLILNDILDFSKIEAG 454
Cdd:smart00388   2 KREFLANLSHELRTPLTAIRGYLELLLD-TELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
PRK10337 PRK10337
sensor protein QseC; Provisional
270-607 1.16e-10

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 64.29  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 270 VMIIFIILLtsvfitqLSRWLTtPIRKLAEQIDKFEPENADTdtylpqtwLEVSRLQSQFSSLANKLALSFNRLHQAnhe 349
Cdd:PRK10337  173 IMLIILMVL-------LGRELA-PLKKLALALRMRDPDSETP--------LNATGVPSEVRPLVEALNQLFARTHAM--- 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 350 neLLNVRlkdfnaqlekqvddktnelveavraannanrtksQFLANMSHEIRTPLNGILGMT---QLLLDnkDLAEEEHE 426
Cdd:PRK10337  234 --MVRER----------------------------------RFTSDAAHELRSPLAALKVQTevaQLSDD--DPQARKKA 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 427 eLVMIHQSANNLLLILNDILDFSKIEAGALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNISDSvPSCISLDPLRF 506
Cdd:PRK10337  276 -LLQLHAGIDRATRLVDQLLTLSRLDSLDNLQDVAEIPLEDLLQSAVMDIYHTAQQAGIDVRLTLNAH-PVIRTGQPLLL 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 507 SQVINNILSNAGKFTESGDiTMSCTMVNDRMQIsiRDTGIGISSEQQAKLFTEFTqadisttRKYG----GTGLGLTISK 582
Cdd:PRK10337  354 SLLVRNLLDNAIRYSPQGS-VVDVTLNARNFTV--RDNGPGVTPEALARIGERFY-------RPPGqeatGSGLGLSIVR 423
                         330       340
                  ....*....|....*....|....*
gi 2738934608 583 RIIELMAGELKLTSQEGVGSEFTIT 607
Cdd:PRK10337  424 RIAKLHGMNVSFGNAPEGGFEAKVS 448
PDC1_DGC_like cd12914
first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this ...
72-167 1.97e-10

first PDC (PhoQ/DcuS/CitA) domain of diguanylate-cyclase and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the first PDC domain of Diguanylate-cyclases (DGCs), Histidine kinases (HKs), and other similar domains. Many members of this subfamily contain a C-terminal DGC (also called GGDEF) domain. DGCs regulate the turnover of cyclic diguanosine monophosphate. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350339  Cd Length: 123  Bit Score: 58.93  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608  72 LENMANLYPDFRTQIITDAFADVthfypqsLAVSLQQSNIRANVADRDYFIHAPSNKQG-YISTIFKGRGFGSlPIVAVS 150
Cdd:cd12914    32 LRRLLARLPEVRSIFVVDADGRV-------VASSGPGPAPGLDVSDRDYFQAARAGGGGlFISEPVISRVTGK-PVIPLS 103
                          90
                  ....*....|....*...
gi 2738934608 151 APIYIED-TFTGVVEGSL 167
Cdd:cd12914   104 RPIRDADgRFAGVVVASI 121
PRK10604 PRK10604
sensor protein RstB; Provisional
501-610 2.01e-10

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 63.47  E-value: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 501 LDPLRFSQVINNILSNAGKFTEsGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTGLGLTI 580
Cdd:PRK10604  315 LDMRLMERVLDNLLNNALRYAH-SRVRVSLLLDGNQACLIVEDDGPGIPPEERERVFEPFVRLDPSRDRATGGCGLGLAI 393
                          90       100       110
                  ....*....|....*....|....*....|
gi 2738934608 581 SKRIIELMAGELKLTSQEGVGSEFTITMPV 610
Cdd:PRK10604  394 VHSIALAMGGSVNCDESELGGARFSFSWPV 423
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
631-757 3.73e-10

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 60.60  E-value: 3.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 631 LNILLVEDNPVNQIVLKKMLHSTECN--LKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHL------ 702
Cdd:COG3279     2 MKILIVDDEPLARERLERLLEKYPDLevVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPppiift 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2738934608 703 --YGQAiiiaitanafeedqqrcLVAGMD----DFISKPINKDQLYACLNKwLKALLNEQQ 757
Cdd:COG3279    82 taYDEY-----------------ALEAFEvnavDYLLKPIDEERLAKALEK-AKERLEAKA 124
glnL PRK11073
nitrogen regulation protein NR(II);
396-610 3.84e-10

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 62.02  E-value: 3.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 396 MSHEIRTPLNGILGMTQLLldNKDLAEEEHEEL--VMIHQSannlllilndildfSKIEAGALKL---EYRAVEITKLLE 470
Cdd:PRK11073  137 LAHEIKNPLGGLRGAAQLL--SKALPDPALTEYtkVIIEQA--------------DRLRNLVDRLlgpQRPGTHVTESIH 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 471 QIA-KVFSSTSVKKGVTFKLnISDSVPSC--ISLDPLRFSQVINNILSNAGKF--TESGDITM------SCTMVNDR--- 536
Cdd:PRK11073  201 KVAeRVVQLVSLELPDNVRL-IRDYDPSLpeLAHDPDQIEQVLLNIVRNALQAlgPEGGTITLrtrtafQLTLHGERyrl 279
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2738934608 537 -MQISIRDTGIGISSEQQAKLFTEFTQAdisttrKYGGTGLGLTISKRIIELMAGELKLTSQEGvGSEFTITMPV 610
Cdd:PRK11073  280 aARIDIEDNGPGIPPHLQDTLFYPMVSG------REGGTGLGLSIARNLIDQHSGKIEFTSWPG-HTEFSVYLPI 347
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
633-736 5.30e-10

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: 57.76  E-value: 5.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEIL-----------QSYQADIILMDCQMPNMDGYQCTKEIKQNPH 701
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLgledeedssnfNEPKVNMIITDYCMPGMTGYDLLKKVKESSA 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2738934608 702 LyGQAIIIAITANAFEEDQQRCLVAGMDDFISKPI 736
Cdd:cd17581    81 L-KEIPVVIMSSENIPTRISRCLEEGAEDFLLKPV 114
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
509-609 9.22e-10

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


Pssm-ID: 340400 [Multi-domain]  Cd Length: 102  Bit Score: 56.24  E-value: 9.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 509 VINNILSNAGKFTESG---DITMSCTmvNDRMQISIRDTGIGISSEQQAKLFTEFTQADISttRKYGGTGLGLTISKRII 585
Cdd:cd16923     4 VFSNLLSNAIKYSPENtriYITSFLT--DDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNS--RNTEGAGLGLSIAKAII 79
                          90       100
                  ....*....|....*....|....
gi 2738934608 586 ELMAGELKLtSQEGVGSEFTITMP 609
Cdd:cd16923    80 ELHGGSASA-EYDDNHDLFKVRLP 102
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
633-743 9.36e-10

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 56.65  E-value: 9.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIK----QNPHLYGQAII 708
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRlakvKTPILILSGLA 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2738934608 709 IAitanafeEDQQRCLVAGMDDFISKPINKDQLYA 743
Cdd:cd17616    81 DI-------EDKVKGLGFGADDYMTKPFHKDELVA 108
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
633-750 1.03e-09

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: 56.62  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQnphlYGQAIIIAIT 712
Cdd:cd17622     3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRP----KYQGPILLLT 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2738934608 713 ANAFEEDQQRCLVAGMDDFISKPINKDQLYACLNKWLK 750
Cdd:cd17622    79 ALDSDIDHILGLELGADDYVVKPVEPAVLLARLRALLR 116
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
502-606 1.82e-09

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: 55.55  E-value: 1.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 502 DPLRFSQVINNILSNAGKFTESGDiTMSCTMVNDRMQIS--IRDTGIGISSEQQAKLFTEFTQADISTTRKyGGTGLGLT 579
Cdd:cd16975     1 DTLLLSRALINIISNACQYAPEGG-TVSISIYDEEEYLYfeIWDNGHGFSEQDLKKALELFYRDDTSRRSG-GHYGMGLY 78
                          90       100
                  ....*....|....*....|....*..
gi 2738934608 580 ISKRIIELMAGELKLTSQEGVGSEFTI 606
Cdd:cd16975    79 IAKNLVEKHGGSLIIENSQKGGAEVTV 105
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
502-606 1.90e-09

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


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 55.54  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 502 DPLRFSQVINNILSNAGKFT-ESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFtqadISTTRKYGG---TGLG 577
Cdd:cd16945     1 DPFLLRQAINNLLDNAIDFSpEGGLIALQLEADTEGIELLVFDEGSGIPDYALNRVFERF----YSLPRPHSGqksTGLG 76
                          90       100       110
                  ....*....|....*....|....*....|
gi 2738934608 578 LTISKRIIELMAGELKLTS-QEGVGSEFTI 606
Cdd:cd16945    77 LAFVQEVAQLHGGRITLRNrPDGVLAFLTL 106
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
631-698 2.24e-09

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: 55.88  E-value: 2.24e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2738934608 631 LNILLVEDNPVNQIVLKKMLHSTECN-LKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQ 698
Cdd:cd19932     1 VRVLIAEDEALIRMDLREMLEEAGYEvVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITS 69
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
467-607 2.47e-09

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


Pssm-ID: 340430 [Multi-domain]  Cd Length: 135  Bit Score: 56.10  E-value: 2.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 467 KLLEQIAKVFSSTSVKKGVTFKLNISDSVPscISLDPLRFSQVINNILSNAGKFTeSGDITMSCTMVNDRMQISIRDTGI 546
Cdd:cd16954     1 PLLDSLCSALNKVYQRKGVSISLDISPELR--FPGERNDLMELLGNLLDNACKWC-LEFVEVTARQTDGGLHLIVDDDGP 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2738934608 547 GISSEQQAKLFTEFTQADISTTrkygGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTIT 607
Cdd:cd16954    78 GVPESQRSKIFQRGQRLDEQRP----GQGLGLAIAKEIVEQYGGELSLSDSPLGGARFEVV 134
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
634-743 3.06e-09

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: 55.30  E-value: 3.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 634 LLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQN----PHLY----GQ 705
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEgietPVLLltalDA 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2738934608 706 aiiiaitanafEEDQQRCLVAGMDDFISKPINKDQLYA 743
Cdd:cd17625    81 -----------VEDRVKGLDLGADDYLPKPFSLAELLA 107
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
502-609 3.49e-09

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


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 54.85  E-value: 3.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 502 DPLRFSQVINNILSNAGKFTES-----GDITM-SCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTqadisTTRKyGGTG 575
Cdd:cd16944     1 DTTQISQVLTNILKNAAEAIEGrpsdvGEVRIrVEADQDGRIVLIVCDNGKGFPREMRHRATEPYV-----TTRP-KGTG 74
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2738934608 576 LGLTISKRIIELMAGELKLTSQEGVGSEFTITMP 609
Cdd:cd16944    75 LGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
633-742 4.58e-09

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: 54.83  E-value: 4.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYqADI--ILMDCQMPNMDGYQCTKEIKQNphlygqaiiia 710
Cdd:cd17544     3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQH-PDIklVITDYNMPEMDGFELVREIRKK----------- 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2738934608 711 itanaFEEDQ---------------QRCLVAGMDDFISKPINKDQLY 742
Cdd:cd17544    71 -----YSRDQlaiigisasgdnalsARFIKAGANDFLTKPFLPEEFY 112
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
630-745 7.49e-09

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: 56.12  E-value: 7.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 630 GLNILLVEDNPVNQIVLKKMLHSTECN-LKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHL------ 702
Cdd:COG3707     3 GLRVLVVDDEPLRRADLREGLREAGYEvVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERPApvillt 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2738934608 703 -YGQaiiiaitanafEEDQQRCLVAGMDDFISKPINKDQLYACL 745
Cdd:COG3707    83 aYSD-----------PELIERALEAGVSAYLVKPLDPEDLLPAL 115
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
631-696 7.65e-09

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: 54.51  E-value: 7.65e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2738934608 631 LNILLVEDNPVNQIVLKKMLHSTE--CNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEI 696
Cdd:COG2197     2 IRVLIVDDHPLVREGLRALLEAEPdiEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
632-741 8.08e-09

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: 8.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 632 NILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHLygqaIIIAI 711
Cdd:cd17619     2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSEV----GIILV 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 2738934608 712 TANAFEEDQQRCLVAGMDDFISKPINKDQL 741
Cdd:cd17619    78 TGRDDEVDRIVGLEIGADDYVTKPFNPREL 107
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
633-700 9.05e-09

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: 53.84  E-value: 9.05e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2738934608 633 ILLVEDNPVnqivLKKMLHSTecnLKQAN-------DGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNP 700
Cdd:cd17562     3 ILAVDDSAS----IRQMVSFT---LRGAGyevveaaDGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLP 70
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
633-743 1.03e-08

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: 53.58  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDN-PVNQIV---LKKMLHSTECnlkqANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHLygqaII 708
Cdd:cd17614     1 ILVVDDEkPISDILkfnLTKEGYEVVT----AYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSNV----PI 72
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2738934608 709 IAITANAFEEDQQRCLVAGMDDFISKPINKDQLYA 743
Cdd:cd17614    73 IMLTAKDSEVDKVLGLELGADDYVTKPFSNRELLA 107
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
345-596 1.80e-08

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 57.77  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 345 QANHENELLNVRLKDfNAQLEKQVDDKTNELVEAVRAAnnanrTKSQFLANMSHEIRTPLNGI---LGMTQLLLDNKDLA 421
Cdd:COG4192   395 QAIEKTQELETEIEE-RKRIEKNLRQTQDELIQAAKMA-----VVGQTMTSLAHELNQPLNAMsmyLFSAKKALEQENYA 468
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 422 EEEHEeLVMIHQSANNLLLILNDILDFSKIEAGALKleyrAVEITKLLEQIAKVFSSTSVKKGVTfkLNISDSVPscISL 501
Cdd:COG4192   469 QLPTS-LDKIEGLIERMDKIIKSLRQFSRKSDTPLQ----PVDLRQVIEQAWELVESRAKPQQIT--LHIPDDLM--VQG 539
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 502 DPLRFSQVINNILSNA-GKFTESGDITMSCTMVNDRMQISIRDTGIGISSEQqaKLFTEFTqadistTRKYGGTGLGLTI 580
Cdd:COG4192   540 DQVLLEQVLVNLLVNAlDAVATQPQISVDLLSNAENLRVAISDNGNGWPLVD--KLFTPFT------TTKEVGLGLGLSI 611
                         250
                  ....*....|....*.
gi 2738934608 581 SKRIIELMAGELKLTS 596
Cdd:COG4192   612 CRSIMQQFGGDLYLAS 627
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
508-609 1.87e-08

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: 52.96  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 508 QVINNILSNAGKFT--ESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFtQADISTTRKYG-GTGLGLTISKRI 584
Cdd:cd16953     3 QVLRNLIGNAISFSppDTGRITVSAMPTGKMVTISVEDEGPGIPQEKLESIFDRF-YTERPANEAFGqHSGLGLSISRQI 81
                          90       100
                  ....*....|....*....|....*....
gi 2738934608 585 IELMAG----ELKLTSQEGVGSEFTITMP 609
Cdd:cd16953    82 IEAHGGisvaENHNQPGQVIGARFTVQLP 110
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
633-757 1.93e-08

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 55.58  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSyQADIILMDCQMPNMDGYQCTKEIKQNPhlygQAIIIAIT 712
Cdd:PRK10955    4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDD-SIDLLLLDVMMPKKNGIDTLKELRQTH----QTPVIMLT 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2738934608 713 ANAFEEDQQRCLVAGMDDFISKPINKDQLYACLNKWL-KALLNEQQ 757
Cdd:PRK10955   79 ARGSELDRVLGLELGADDYLPKPFNDRELVARIRAILrRSHWSEQQ 124
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
459-610 3.46e-08

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 56.84  E-value: 3.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 459 EYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNISDsvpscISLDP---LRFSQVINNILSNAGKF----TESGDITMSCT 531
Cdd:COG3920   355 DWEGVDLRDYLRELLEPLRDSYGGRGIRIELDGPD-----VELPAdaaVPLGLILNELVTNALKHaflsGEGGRIRVSWR 429
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2738934608 532 MVNDRMQISIRDTGIGISseqqaklfteftqADISTTRkygGTGLGLTISKRIIELMAGELKLTSQEGVgsEFTITMPV 610
Cdd:COG3920   430 REDGRLRLTVSDNGVGLP-------------EDVDPPA---RKGLGLRLIRALVRQLGGTLELDRPEGT--RVRITFPL 490
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
632-753 4.65e-08

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: 51.87  E-value: 4.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 632 NILLVEDNPVnqivLKKMLHStecNLKQAN-------DGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPhLYG 704
Cdd:cd17618     2 TILIVEDEPA----IREMIAF---NLERAGfdvveaeDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDE-MTR 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2738934608 705 QAIIIAITANAFEEDQQRCLVAGMDDFISKPINKDQLYAclnkWLKALL 753
Cdd:cd17618    74 DIPIIMLTARGEEEDKVRGLEAGADDYITKPFSPRELVA----RIKAVL 118
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
512-580 4.73e-08

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 56.09  E-value: 4.73e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2738934608 512 NILSNAGKFTESgDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTGLGLTI 580
Cdd:PRK09470  360 NIVRNALRYSHT-KIEVAFSVDKDGLTITVDDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAI 427
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
631-749 8.67e-08

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 55.42  E-value: 8.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 631 LNILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQ-NPHLygqaIII 709
Cdd:PRK10365    6 IDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAlNPAI----PVL 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2738934608 710 AITANAFEEDQQRCLVAGMDDFISKPINKDQLYACLNKWL 749
Cdd:PRK10365   82 IMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKAL 121
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
631-689 9.44e-08

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: 51.29  E-value: 9.44e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 631 LNILLVEDNPVNQIVLKKMLHST-ECNLKQANDGLEALEILQSYQADIILMDCQMPNMDG 689
Cdd:cd17530     1 LRVLVLDDDPFQCMMAATILEDLgPGNVDEADDGREALVILLCNAPDIIICDLKMPDMDG 60
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
508-609 9.64e-08

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


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 50.86  E-value: 9.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 508 QVINNILSNAGKFTES--GDITMSC------TMVNDR----MQISIRDTGIGISSEQQAKLFTEFTqadistTRKYGGTG 575
Cdd:cd16918     3 QVFLNLVRNAAQALAGsgGEIILRTrtqrqvTLGHPRhrlaLRVSVIDNGPGIPPDLQDTIFYPMV------SGRENGTG 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2738934608 576 LGLTISKRIIELMAGELKLTSQEGvGSEFTITMP 609
Cdd:cd16918    77 LGLAIAQNIVSQHGGVIECDSQPG-HTVFSVSLP 109
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
539-609 1.06e-07

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: 50.84  E-value: 1.06e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2738934608 539 ISIRDTGIGISSEQQAKLFTEFTqadisTTRKYG-GTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMP 609
Cdd:cd16919    50 LEVSDTGSGMPAEVLRRAFEPFF-----TTKEVGkGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
633-753 1.29e-07

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: 50.46  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIK----QNPHLYGQAII 708
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRaagnDLPILVLTARD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2738934608 709 IAItanafeeDQQRCLVAGMDDFISKPINKDQLYAclnkWLKALL 753
Cdd:cd17627    81 SVS-------DRVAGLDAGADDYLVKPFALEELLA----RVRALL 114
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
633-750 1.43e-07

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: 50.66  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNphlygqaiiiait 712
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQER------------- 67
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2738934608 713 anafeedQQRCLV-----------------AGMDDFISKPINKDQLYACLNKWLK 750
Cdd:cd17572    68 -------SLPTSVivitahgsvdiaveamrLGAYDFLEKPFDADRLRVTVRNALK 115
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
391-652 1.46e-07

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 54.94  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 391 QFLANMSHEIRTPLNGILGMTQLLLDNKDlAEEEHEELVMIHQSANNLLLILNDILDFSKIEAGALKLEYRAVEITKLLE 470
Cdd:PRK10618  452 AFLQNIGDELKQPLQSLAQLAAQLRQTSD-EEQQQPELDQLAEQSDVLVRLVDNIQLLNMLETQDWKPEQELFSLQDLID 530
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 471 QIAKVFSSTSVKKGVTFKLNISDSVPSCISLDPLRFSQVINNILSNAGKFTESGDITMSCTMVN---DRMQISIRDTGIG 547
Cdd:PRK10618  531 EVLPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYGKITLEVDQDEsspDRLTIRILDTGAG 610
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 548 ISSEQQAKL---FTEFTQADisttrKYG-GTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMPVIISNSasvDNQST 623
Cdd:PRK10618  611 VSIKELDNLhfpFLNQTQGD-----RYGkASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLKMLAADP---EVEEE 682
                         250       260       270
                  ....*....|....*....|....*....|
gi 2738934608 624 ATPQLAGLNILL-VEDNPVNQIVLkKMLHS 652
Cdd:PRK10618  683 EEKLLDGVTVLLdITSEEVRKIVT-RQLEN 711
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
633-698 1.59e-07

phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; Pseudomonas aeruginosa RssB is an orphan atypical response regulator containing a REC domain and a PP2C-type protein phosphatase output domain. Its function is still unknown. Escherichia RssB, which is not included in this subfamily, is a ClpX adaptor protein which alters ClpX specificity by mediating a specific interaction between ClpX and the substrates such as RpoS, an RNA polymerase sigma factor. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 50.28  E-value: 1.59e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQ 698
Cdd:cd17555     3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITK 68
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
631-747 2.17e-07

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: 50.03  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 631 LNILLVEDNPVNQIVLKKMLHSTE-CNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHLYGQAIII 709
Cdd:cd19923     1 MKVLVVDDFSTMRRIIKNLLKELGfNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLM 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2738934608 710 AITANAfEEDQQRCLVAGMDDFISKPINKDQLYACLNK 747
Cdd:cd19923    81 VTAEAK-KENVIAAAQAGVNNYIVKPFTAATLKEKLEK 117
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
633-701 2.99e-07

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 49.46  E-value: 2.99e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2738934608 633 ILLVEDNPVNQIVLKKML--HSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPH 701
Cdd:cd17532     1 ALIVDDEPLAREELRYLLeeHPDIEIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAK 71
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
632-699 4.44e-07

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: 48.94  E-value: 4.44e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 632 NILLVEDNPVNQIVLKKMLHSTECN-LKQANDGLEALEILQSYQADIILMDCQMP-NMDGYQCTKEIKQN 699
Cdd:cd17534     2 KILIVEDEAIIALDLKEILESLGYEvVGIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREK 71
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
633-700 4.76e-07

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and similar domains; Thermotoga maritima RR468 (encoded by gene TM0468) is the cognate response regulator (RR) of the class I histidine kinase HK853 (product of gene TM0853). HK853/RR468 comprise a two-component system (TCS) that couples environmental stimuli to adaptive responses. This subfamily also includes Fremyella diplosiphon complementary adaptation response regulator homolog RcaF, a small RR that is involved in four-step phosphorelays of the complementary chromatic adaptation (CCA) system that occurs in many cyanobacteria. Both RR468 and RcaF are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 49.09  E-value: 4.76e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2738934608 633 ILLVEDNP----VNQIVLKKMlhsTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNP 700
Cdd:cd17552     4 ILVIDDEEdireVVQACLEKL---AGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANP 72
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
633-745 5.02e-07

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: 48.89  E-value: 5.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQN----PHLYGQAII 708
Cdd:cd17615     2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADgpdvPVLFLTAKD 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2738934608 709 IAitanafeEDQQRCLVAGMDDFISKPINKDQLYACL 745
Cdd:cd17615    82 SV-------EDRIAGLTAGGDDYVTKPFSLEEVVARL 111
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
633-746 5.08e-07

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: 48.82  E-value: 5.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHLygqaiiiait 712
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISNV---------- 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2738934608 713 ANAF------EEDQQRCLVAGMDDFISKPINKDQLYACLN 746
Cdd:cd18159    71 PIIFissrddNMDQVMAINMGGDDYITKPFDLDVLLAKIK 110
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
633-691 5.28e-07

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: 48.52  E-value: 5.28e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQ 691
Cdd:cd17602     1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYE 59
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
632-697 6.25e-07

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: 48.76  E-value: 6.25e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2738934608 632 NILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIK 697
Cdd:cd17554     2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIR 67
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
512-595 6.55e-07

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 52.28  E-value: 6.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 512 NILSNAGKFTESG-DITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADisttRKYGGTGLGLTISKRIIELMAG 590
Cdd:PRK10755  254 NLVENAHRYSPEGsTITIKLSQEDGGAVLAVEDEGPGIDESKCGELSKAFVRMD----SRYGGIGLGLSIVSRITQLHHG 329

                  ....*
gi 2738934608 591 ELKLT 595
Cdd:PRK10755  330 QFFLQ 334
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
633-735 9.23e-07

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: 47.82  E-value: 9.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKML----HSTECnlkqANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQN----PHLY- 703
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLteegYAVDV----AYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAgkqtPVLMl 76
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2738934608 704 ---GQAiiiaitanafeEDQQRCLVAGMDDFISKP 735
Cdd:cd19935    77 tarDSV-----------EDRVKGLDLGADDYLVKP 100
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
633-735 1.20e-06

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: 47.54  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQnphlYGQAIIIAIT 712
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLRE----WSAVPVIVLS 76
                          90       100
                  ....*....|....*....|...
gi 2738934608 713 ANAFEEDQQRCLVAGMDDFISKP 735
Cdd:cd17620    77 ARDEESDKIAALDAGADDYLTKP 99
PDC1_HK_sensor cd18773
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase ...
35-167 1.87e-06

first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase and similar domains; Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution.


Pssm-ID: 350341 [Multi-domain]  Cd Length: 125  Bit Score: 47.56  E-value: 1.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608  35 EKANEIARVIDSHLEHHKKGVVLTAKSIayglpkQVALENMANLYPDFRTQIITDAFADVTHFYPQSlavslQQSNIRAN 114
Cdd:cd18773     2 EEADLLLRSLASALEALAALGSADREEL------QALLRRLLERNPEISGIYVVDADGRVVASSDRD-----PGGGDDDD 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2738934608 115 VADRDYFIHAPSNKQGYISTIFKGRGFGSlPIVAVSAPIYIED-TFTGVVEGSL 167
Cdd:cd18773    71 DRDRFWYQAAKATGKLVISEPYISRVTGK-PVITLSRPIRDADgRFIGVVGADI 123
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
633-702 2.53e-06

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: 46.73  E-value: 2.53e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQA-DIILMDCQMPNMDGYQCTKEIKQ-NPHL 702
Cdd:cd18160     2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELAREARKiDPDV 73
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
633-750 3.09e-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: 46.53  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHLygqaiiIAIT 712
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTSQV------PVLM 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2738934608 713 ANAFEEDQQRC--LVAGMDDFISKPINKDQLYACLNKWLK 750
Cdd:cd17623    75 LTARGDDIDRIlgLELGADDYLPKPFNPRELVARIRAILR 114
PRK10610 PRK10610
chemotaxis protein CheY;
631-752 3.16e-06

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 46.89  E-value: 3.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 631 LNILLVEDNPVNQIVLKKMLHSTEC-NLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNphlyGQAIII 709
Cdd:PRK10610    6 LKFLVVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRAD----GAMSAL 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2738934608 710 AITANAFEEDQQRCLV---AGMDDFISKPINKDQLYACLNKWLKAL 752
Cdd:PRK10610   82 PVLMVTAEAKKENIIAaaqAGASGYVVKPFTAATLEEKLNKIFEKL 127
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
633-698 4.54e-06

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: 46.39  E-value: 4.54e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQ 698
Cdd:cd17553     3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKV 68
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
270-609 4.82e-06

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


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 50.13  E-value: 4.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 270 VMIIFIILLTSVFitqLSRWLTTPIRKLAEQIdkfepENA-DTDTYLPQTwLEVSRLQSQFSSLANKLALSFNRLHQANH 348
Cdd:TIGR03785 413 LAIMSIGTLALFG---FASWISWRIRRLSDDA-----EAAiDSQGRISGA-IPASRSRDEIGDLSRSFAQMVARLRQYTH 483
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 349 ENELLNVRLkdfnaqlekqvddktnelveavraannanrtksqflanmSHEIRTPlngiLGMTQLLLDNKDLAEEEHEEL 428
Cdd:TIGR03785 484 YLENMSSRL---------------------------------------SHELRTP----VAVVRSSLENLELQALEQEKQ 520
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 429 VMIHQSANNLLLILNDILDFSkiEAGALK--LEYRAVEITKLLEQIAKVFSS-TSVKKGVTFKLNISDSvPSCISLDPLR 505
Cdd:TIGR03785 521 KYLERAREGTERLSMILNNMS--EATRLEqaIQSAEVEDFDLSEVLSGCMQGyQMTYPPQRFELNIPET-PLVMRGSPEL 597
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 506 FSQVINNILSNAGKFT-ESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTGLGLTISKRI 584
Cdd:TIGR03785 598 IAQMLDKLVDNAREFSpEDGLIEVGLSQNKSHALLTVSNEGPPLPEDMGEQLFDSMVSVRDQGAQDQPHLGLGLYIVRLI 677
                         330       340
                  ....*....|....*....|....*.
gi 2738934608 585 IELMAGELKL-TSQEGVGSEFTITMP 609
Cdd:TIGR03785 678 ADFHQGRIQAeNRQQNDGVVFRISLP 703
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
397-609 5.14e-06

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 49.91  E-value: 5.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 397 SHEIRTPLNGILGMTQLlldnkdlaeEEHEEL-VMIHQSANNLllilndildfsKIEAGALKLEYRAVEITKLLeqIAKV 475
Cdd:PRK11086  347 SHEFMNKLHVILGLLHL---------KSYDQLeDYILKTANNY-----------QEEIGSLLGKIKSPVIAGFL--LGKI 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 476 fsSTSVKKGVTFKLNISDSVPSCISldplrfSQVIN-------NILSN---AGKFTESGDITMSCTMVNDRMQISIRDTG 545
Cdd:PRK11086  405 --SRARELGITLIISEDSQLPDSGD------EDQVHelitilgNLIENaleAVGGEEGGEISVSLHYRNGWLHCEVSDDG 476
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2738934608 546 IGISSEQQAKLFTEftqaDISTtrKYGGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMP 609
Cdd:PRK11086  477 PGIAPDEIDAIFDK----GYST--KGSNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIP 534
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
633-741 5.84e-06

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 49.46  E-value: 5.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNP-VNQI---VLKKMLHSTECnlkqANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNphlygQAII 708
Cdd:PRK11361    7 ILIVDDEDnVRRMlstAFALQGFETHC----ANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSH-----ETRT 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2738934608 709 IAITANAFEEDQQ--RCLVAGMDDFISKPINKDQL 741
Cdd:PRK11361   78 PVILMTAYAEVETavEALRCGAFDYVIKPFDLDEL 112
orf27 CHL00148
Ycf27; Reviewed
633-743 8.28e-06

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 47.79  E-value: 8.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQnphlygQAIIIAIT 712
Cdd:CHL00148    9 ILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRK------ESDVPIIM 82
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2738934608 713 ANAFEE--DQQRCLVAGMDDFISKPINKDQLYA 743
Cdd:CHL00148   83 LTALGDvsDRITGLELGADDYVVKPFSPKELEA 115
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
634-753 1.28e-05

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: 44.96  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 634 LLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHlYGQAIIIAITA 713
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPK-TSSIPIIMLTA 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2738934608 714 NAFEEDQQRCLVAGMDDFISKPINKDQLYAclnkWLKALL 753
Cdd:cd19937    80 KGEEFDKVLGLELGADDYITKPFSPRELLA----RVKAVL 115
PRK11173 PRK11173
two-component response regulator; Provisional
625-741 1.29e-05

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 47.32  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 625 TPQlaglnILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPH--- 701
Cdd:PRK11173    3 TPH-----ILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQANval 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2738934608 702 --LYGQAIiiaitanafEEDQQRCLVAGMDDFISKPINKDQL 741
Cdd:PRK11173   78 mfLTGRDN---------EVDKILGLEIGADDYITKPFNPREL 110
PRK15115 PRK15115
response regulator GlrR; Provisional
632-750 2.17e-05

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 47.52  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 632 NILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEI-KQNPHL-------Y 703
Cdd:PRK15115    7 HLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIqKVQPGMpviiltaH 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2738934608 704 GQAIIIAITAnafeedQQrclvaGMDDFISKPINKDQLYACLNKWLK 750
Cdd:PRK15115   87 GSIPDAVAAT------QQ-----GVFSFLTKPVDRDALYKAIDDALE 122
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
632-743 2.72e-05

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


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 45.29  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 632 NILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQnphlygqaiiiai 711
Cdd:COG4567     6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRE------------- 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2738934608 712 tanafEEDQQRCLV---------------AGMDDFISKPINKDQLYA 743
Cdd:COG4567    73 -----RDPDARIVVltgyasiataveaikLGADDYLAKPADADDLLA 114
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
633-698 3.72e-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: 3.72e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2738934608 633 ILLVEDNpvnQIVLKKM--LHSTECNLK---QANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQ 698
Cdd:cd19930     1 VLIAEDQ---EMVRGALaaLLELEDDLEvvaQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELRE 68
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
482-592 4.01e-05

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 46.93  E-value: 4.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 482 KKGVTFKLNISdsvPSCISL-DPLRFSQVINNILSNAGK----FTEsgditMSCTMVNDRMQISIRDTGIGISSEQQAKL 556
Cdd:PRK10815  357 RKGVNITLDIS---PEITFVgEKNDFMEVMGNVLDNACKycleFVE-----ISARQTDEHLHIVVEDDGPGIPESKRELI 428
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2738934608 557 FTEFTQADisTTRKygGTGLGLTISKRIIELMAGEL 592
Cdd:PRK10815  429 FDRGQRAD--TLRP--GQGLGLSVAREITEQYEGKI 460
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
633-735 4.82e-05

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: 42.96  E-value: 4.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHLygqaIIIAIT 712
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARSNV----PVIMVT 76
                          90       100
                  ....*....|....*....|...
gi 2738934608 713 ANAFEEDQQRCLVAGMDDFISKP 735
Cdd:cd17621    77 AKDSEIDKVVGLELGADDYVTKP 99
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
517-609 4.90e-05

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: 44.50  E-value: 4.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 517 AGKfTESGDITMSCTMVNDRMQISIRDTGIGIS--------------SEQQAKLFTEFT------QADISTTRKYG---G 573
Cdd:cd16916    64 AGK-PPEGTITLRAEHQGNQVVIEVSDDGRGIDrekirekaiergliTADEAATLSDDEvlnlifAPGFSTAEQVTdvsG 142
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2738934608 574 TGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMP 609
Cdd:cd16916   143 RGVGMDVVKRSIESLGGTIEVESEPGQGTTFTIRLP 178
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
632-696 5.76e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 46.03  E-value: 5.76e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2738934608 632 NILLVEDNPVNQIVLKKMLHSTECN--LKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEI 696
Cdd:PRK12555    2 RIGIVNDSPLAVEALRRALARDPDHevVWVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRI 68
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
633-735 5.85e-05

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: 42.43  E-value: 5.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHLygqaIIIAIT 712
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKSTL----PVIFLT 76
                          90       100
                  ....*....|....*....|...
gi 2738934608 713 ANAFEEDQQRCLVAGMDDFISKP 735
Cdd:cd19936    77 SKDDEIDEVFGLRMGADDYITKP 99
PRK15479 PRK15479
transcriptional regulator TctD;
631-757 7.51e-05

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 44.71  E-value: 7.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 631 LNILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNphlyGQAIIIA 710
Cdd:PRK15479    1 MRLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKR----GQTLPVL 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2738934608 711 ITANAFE-EDQQRCLVAGMDDFISKPINKDQLYAclnkWLKALLNEQQ 757
Cdd:PRK15479   77 LLTARSAvADRVKGLNVGADDYLPKPFELEELDA----RLRALLRRSA 120
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
632-745 7.95e-05

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: 42.43  E-value: 7.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 632 NILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQ-NPHLygqaiiia 710
Cdd:cd17563     2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRAlQPDA-------- 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2738934608 711 itanafeedqqRCLV---------------AGMDDFISKPINKDQLYACL 745
Cdd:cd17563    74 -----------RIVVltgyasiataveaikLGADDYLAKPADADEILAAL 112
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
633-743 8.27e-05

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: 42.46  E-value: 8.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNphlyGQAIIIAIT 712
Cdd:cd17626     3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAE----SGVPIVMLT 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2738934608 713 ANAFEEDQQRCLVAGMDDFISKPINKDQLYA 743
Cdd:cd17626    79 AKSDTVDVVLGLESGADDYVAKPFKPKELVA 109
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
633-699 9.44e-05

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: 42.48  E-value: 9.44e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQN 699
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEK 67
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
633-702 1.03e-04

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 41.95  E-value: 1.03e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQA-DIILMDCQMPN-MDGYQCTKEIKQN-PHL 702
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPDiDLLVTDVIMPGgMNGSQLAEEARRRrPDL 73
PRK11517 PRK11517
DNA-binding response regulator HprR;
631-743 1.11e-04

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 44.12  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 631 LNILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEI---KQNPHLYGQAI 707
Cdd:PRK11517    1 MKILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLrtaKQTPVICLTAR 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2738934608 708 IIAitanafeEDQQRCLVAGMDDFISKPINKDQLYA 743
Cdd:PRK11517   81 DSV-------DDRVRGLDSGANDYLVKPFSFSELLA 109
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
633-702 1.25e-04

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: 42.23  E-value: 1.25e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2738934608 633 ILLVEDNPVNQIVLKKML-----HSTECNlkqanDGLEALEILQSY--QADIILMDCQMPNMDGYQCTKEIKQNPHL 702
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLlrcgyQVTTCT-----DAEEALSMLRENkdEFDLVITDVHMPDMDGFEFLELIRLEMDL 72
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
659-696 1.48e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 44.76  E-value: 1.48e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2738934608 659 QANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEI 696
Cdd:PRK00742   34 TAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKI 71
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
633-741 1.73e-04

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 41.48  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTEC-NLKQANDGLEALEILQSYQADIILMDCQMPN-MDGYQCTKEIKQNphlygQAIIIA 710
Cdd:cd17589     1 FLIVDDQPTFRSMLKSMLRSLGVtRIDTASSGEEALRMCENKTYDIVLCDYNLGKgKNGQQLLEELRHK-----KLISPS 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2738934608 711 ITANAFEEDQQRCLVAGM-----DDFISKPINKDQL 741
Cdd:cd17589    76 TVFIMVTGESSRAMVLSAlelepDDYLLKPFTVSEL 111
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
633-697 2.27e-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: 2.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2738934608 633 ILLVEDNPVNQIVLKKMLhSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIK 697
Cdd:cd17596     3 ILVVDDEVRSLEALRRTL-EEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVR 66
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
468-610 2.28e-04

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 43.45  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 468 LLEQIAKVFSSTSVKKGVTFKLNISDSVPScisLDP------LRFSQ-VINNIL--SNAGKFTesgdITMSCTmvNDRMQ 538
Cdd:COG4585   125 LAAALEELAERLLRAAGIRVELDVDGDPDR---LPPevelalYRIVQeALTNALkhAGATRVT----VTLEVD--DGELT 195
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2738934608 539 ISIRDTGIGISSEQQAklfteftqadisttrkygGTGLGLT-ISKRIiELMAGELKLTSQEGVGSEFTITMPV 610
Cdd:COG4585   196 LTVRDDGVGFDPEAAP------------------GGGLGLRgMRERA-EALGGTLTIGSAPGGGTRVRATLPL 249
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
631-746 2.29e-04

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 42.96  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 631 LNILLVEDNPVNQIVLKKMLHSTECN-LKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIK------------ 697
Cdd:PRK09958    1 MNAIIIDDHPLAIAAIRNLLIKNDIEiLAELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRkrqysgiiiivs 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2738934608 698 -QNPHLYGqaiiiaitanafeedqQRCLVAGMDDFISKPINKDQLYACLN 746
Cdd:PRK09958   81 aKNDHFYG----------------KHCADAGANGFVSKKEGMNNIIAAIE 114
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
507-610 2.37e-04

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 41.44  E-value: 2.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 507 SQVINNILSNAGKFTESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFtqadisttrkyGGTGLGLTISKRiie 586
Cdd:COG2172    40 SEAVTNAVRHAYGGDPDGPVEVELELDPDGLEIEVRDEGPGFDPEDLPDPYSTL-----------AEGGRGLFLIRR--- 105
                          90       100
                  ....*....|....*....|....
gi 2738934608 587 lMAGELKLTSQEGvGSEFTITMPV 610
Cdd:COG2172   106 -LMDEVEYESDPG-GTTVRLVKRL 127
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
633-735 2.56e-04

phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is part of the BaeSR two-component system that is involved in regulating genes that confer multidrug and metal resistance. In Salmonella, BaeSR induces AcrD and MdtABC drug efflux systems, increasing multidrug and metal resistance. In Escherichia coli, BaeR stimulates multidrug resistance via mdtABC (multidrug transporter ABC, formerly known as yegMNO) genes, which encode a resistance-nodulation-cell division (RND) drug efflux system. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 41.21  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHLygqaiIIAIT 712
Cdd:cd19938     2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFSDV-----PIIMV 76
                          90       100
                  ....*....|....*....|....
gi 2738934608 713 ANAFEE-DQQRCLVAGMDDFISKP 735
Cdd:cd19938    77 TARVEEiDRLLGLELGADDYICKP 100
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
633-698 3.27e-04

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 40.79  E-value: 3.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2738934608 633 ILLVEDNPVNQIVLKKMLhSTECNLK---QANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQ 698
Cdd:cd19931     1 VLLIDDHPLLRKGIKQLI-ELDPDFTvvgEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALRE 68
PRK09483 PRK09483
response regulator; Provisional
631-701 3.41e-04

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 42.79  E-value: 3.41e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2738934608 631 LNILLVEDNPVNQIVLKKMLHSTEcNLK---QANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEI-KQNPH 701
Cdd:PRK09483    2 INVLLVDDHELVRAGIRRILEDIK-GIKvvgEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKIlRYTPD 75
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
660-689 3.76e-04

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


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 40.67  E-value: 3.76e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2738934608 660 ANDGLEALEILQSYQADIILMDCQMPNMDG 689
Cdd:cd17561    33 AHNGQEALELIEEKEPDVLLLDIIMPHLDG 62
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
633-743 4.19e-04

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 42.40  E-value: 4.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDN-PVNQIVLKkMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPhLYGQAIIIAI 711
Cdd:PRK10161    5 ILVVEDEaPIREMVCF-VLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRES-MTRDIPVVML 82
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2738934608 712 TANAFEEDQQRCLVAGMDDFISKPINKDQLYA 743
Cdd:PRK10161   83 TARGEEEDRVRGLETGADDYITKPFSPKELVA 114
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
633-702 6.27e-04

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: 39.95  E-value: 6.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQN-PHL 702
Cdd:cd19919     3 VWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRhPDL 73
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
502-607 8.29e-04

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: 39.56  E-value: 8.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 502 DPLRFSQVINNILSNAGKFTESGD----ITMSCT-------MVNDRMQISIRDTGIGISSEqqakLFTEFTQADISTTRK 570
Cdd:cd16932     3 DQIRLQQVLADFLLNAVRFTPSPGgwveIKVSPTkkqigdgVHVIHLEFRITHPGQGLPEE----LVQEMFEENQWTTQE 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2738934608 571 yggtGLGLTISKRIIELMAGELKLTSQEGVgSEFTIT 607
Cdd:cd16932    79 ----GLGLSISRKLVKLMNGDVRYLREAGR-SYFLIT 110
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
631-698 1.12e-03

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: 39.54  E-value: 1.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 631 LNILLVEDNPVNQIVLKKML--HSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQ 698
Cdd:cd19925     1 INVLIVEDDPMVAEIHRAYVeqVPGFTVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRA 70
PRK04069 PRK04069
serine-protein kinase RsbW; Provisional
507-608 1.15e-03

serine-protein kinase RsbW; Provisional


Pssm-ID: 235217 [Multi-domain]  Cd Length: 161  Bit Score: 40.29  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 507 SQVINNILSNAGKFTESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTGLGLtiskriIE 586
Cdd:PRK04069   48 SEACTNAVQHAYKEDEVGEIHIRFEIYEDRLEIVVADNGVSFDYETLKSKLGPYDISKPIEDLREGGLGLFL------IE 121
                          90       100
                  ....*....|....*....|..
gi 2738934608 587 LMAGELKLTSQEGVgsefTITM 608
Cdd:PRK04069  122 TLMDDVTVYKDSGV----TVSM 139
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
633-753 1.35e-03

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: 39.19  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPH------LYGQA 706
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRatpvliLTARD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2738934608 707 IiiaitanafEEDQQRCLVAGMDDFISKPINKDQLYACLNkwlkALL 753
Cdd:cd19934    81 S---------WQDKVEGLDAGADDYLTKPFHIEELLARLR----ALI 114
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
514-609 1.62e-03

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


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 38.30  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 514 LSNAGKFTESGDITMSCTMVNDRMQISIRDTGIGISSEQQAklfteftqadisttrkyGGTGLGLTISKRIIELMAGELK 593
Cdd:cd16917     9 LTNALKHAGASRVRVTLSYTADELTLTVVDDGVGFDGPAPP-----------------GGGGFGLLGMRERAELLGGTLT 71
                          90
                  ....*....|....*.
gi 2738934608 594 LTSQEGVGSEFTITMP 609
Cdd:cd16917    72 IGSRPGGGTRVTARLP 87
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
633-736 1.72e-03

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 38.41  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECN--LKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHlYGQAIIIA 710
Cdd:cd17565     1 FYIVDDDKNIIKILSDIIEDDDLGevVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGS-NGKFIMIS 79
                          90       100
                  ....*....|....*....|....*.
gi 2738934608 711 ITANafEEDQQRCLVAGMDDFISKPI 736
Cdd:cd17565    80 QVSD--KEMIGKAYQAGIEFFINKPI 103
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
633-698 1.73e-03

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 40.40  E-value: 1.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2738934608 633 ILLVEDNPVNQIVLKKMLhSTECNLK---QANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQ 698
Cdd:PRK10651    9 ILLIDDHPMLRTGVKQLI-SMAPDITvvgEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLRE 76
PRK10693 PRK10693
two-component system response regulator RssB;
659-689 1.83e-03

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 41.13  E-value: 1.83e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2738934608 659 QANDGLEALEILQSYQADIILMDCQMPNMDG 689
Cdd:PRK10693    2 LAANGVDALELLGGFTPDLIICDLAMPRMNG 32
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
495-608 2.57e-03

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: 38.59  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 495 VPSCISLDPLRFSQVINNILSNAGKFTESG--------------------DITMSCTMVNDRMQISIRdtgIGISSEQQA 554
Cdd:cd16938     1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGGgnitfrvfleggsedrsdrdWGPWRPSMSDESVEIRFE---VEINDSGSP 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2738934608 555 KLFTEFTQAdiSTTRKYG----GTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITM 608
Cdd:cd16938    78 SIESASMRN--SLNRRYNlselGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
633-753 2.96e-03

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: 38.23  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNP--VNQIV--LKKMLHSTECnlkqANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNphlyGQAII 708
Cdd:cd17624     1 ILLVEDDAllGDGLKtgLRKAGYAVDW----VRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQ----GQSLP 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2738934608 709 IAITANAFEEDQQ-RCLVAGMDDFISKPINKDQLYAclnkWLKALL 753
Cdd:cd17624    73 VLILTARDGVDDRvAGLDAGADDYLVKPFALEELLA----RLRALL 114
HATPase_YpdA-YehU-LytS-like cd16924
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
501-609 3.45e-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: 37.81  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 501 LDPLrfsqVINNILSNAGKFTESGDITMSCTMVNDRMQISIRDTGIGIsseqQAKLfteftqADISTTRKYGGTGLGL-T 579
Cdd:cd16924     6 LQPL----VENAIQHGLSPLTDKGVVTISALKEDNHVMIEVEDNGRGI----DPKV------LNILGKKPKEGNGIGLyN 71
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2738934608 580 ISKRIIELMaGE---LKLTSQEGVGSEFTITMP 609
Cdd:cd16924    72 VHQRLILLF-GEdygIHIASEPDKGTRITFTIP 103
PRK10766 PRK10766
two-component system response regulator TorR;
632-697 4.02e-03

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 39.64  E-value: 4.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2738934608 632 NILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIK 697
Cdd:PRK10766    4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELR 69
PLN03029 PLN03029
type-a response regulator protein; Provisional
631-736 4.05e-03

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 39.63  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 631 LNILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEIL--------------------QSYQADIILMDCQMPNMDGY 690
Cdd:PLN03029    9 FHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLglheddrsnpdtpsvspnshQEVEVNLIITDYCMPGMTGY 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2738934608 691 QCTKEIKQNPHLYgQAIIIAITANAFEEDQQRCLVAGMDDFISKPI 736
Cdd:PLN03029   89 DLLKKIKESSSLR-NIPVVIMSSENVPSRITRCLEEGAEEFFLKPV 133
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
633-747 5.88e-03

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: 37.43  E-value: 5.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLkkMLHSTECNLKQ--ANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQNPHLygqAIIIA 710
Cdd:cd17594     2 VLVVDDDAAMRHLL--ILYLRERGFDVtaAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARSDV---PIIII 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2738934608 711 ITANAFEEDQQRCLVAGMDDFISKPINKDQLYACLNK 747
Cdd:cd17594    77 SGDRRDEIDRVVGLELGADDYLAKPFGLRELLARVRA 113
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
632-702 5.95e-03

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 39.85  E-value: 5.95e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2738934608 632 NILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQ-NPHL 702
Cdd:PRK10923    5 IVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQrHPML 76
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
257-678 6.29e-03

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 40.10  E-value: 6.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 257 ANDVAVNAWGQSLVMIIFIILLTSVFITQLSRWLTTPIRKLAEQIDKFepENADTDTYLP-QTWLEVSRLQSQFSSLANK 335
Cdd:COG2770   203 LLEAALAALLLLLLLALLALLLALLLALLLARRITRPLRRLAEAARRI--AAGDLDVRIPvSRKDEIGELARAFNRMADS 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 336 LALSFNRLHQANHENELLNVRlkdfnaQLEKQVDDKTNELVEAVRAANNANRTKSQFLANMSHEIRTPLNGILGMTQLLL 415
Cdd:COG2770   281 LRESIEEAEEEEELAEAELAR------LLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADLLLAL 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 416 DNKDLAEEEHEELVMIHQSANNLLLILNDILDFSKIEAGALKLEYRAVEITKLLEQIAKVFSSTSVKKGVTFKLNISDSV 495
Cdd:COG2770   355 ALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALALLALAAAAAAAEAA 434
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 496 PSCISLDPLRFSQVINNILSNAGKFTESGDITMSCTMVNDRMQISIRDTGIGISSEQQAKLFTEFTQADISTTRKYGGTG 575
Cdd:COG2770   435 AAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEEEEEAGAAAEELAEELLLLEG 514
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 576 LGLTISKRIIELMAGELKLTSQEGVGSEFTITMPVIISNSASVDNQSTATPQLAGLNILLVEDNPVNQIVLKKMLHSTEC 655
Cdd:COG2770   515 LLLLLLLEAEALEVAEELLELEEAALLLAAAAELAALLALLLALAAVEAAALLLAALLLAAVAALLELAALLLLLLAAAE 594
                         410       420
                  ....*....|....*....|...
gi 2738934608 656 NLKQANDGLEALEILQSYQADII 678
Cdd:COG2770   595 ALAALELELAAAAEAALAEAELL 617
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
11-163 6.57e-03

first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the first PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350338  Cd Length: 139  Bit Score: 37.51  E-value: 6.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608  11 ILTSIVLTNNHYARIEYEVNAQLNEKANEIARVIDSHLEHHKKgvvltAKSIAYGLPKQVALENMANLYPDFRTQIITDA 90
Cdd:cd12913     1 FLEEAESIAEQLASTLESLVSSGSLDRELLENLLKQVLESNPD-----ILGVYVAFEPNAFSDETGRFAPYWYRDDGGII 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2738934608  91 FADVTHFYpqslavslqqsniraNVADRDYFIHAPSNKQGYISTIFKGRGFGSLPIVAVSAPIYIEDTFTGVV 163
Cdd:cd12913    76 DLDEPPDY---------------DYRTRDWYKLAKETGKPVWTEPYIDEVGTGVLMITISVPIYDNGKFIGVV 133
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
632-743 6.89e-03

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 38.63  E-value: 6.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 632 NILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQnphlYGQAIIIAI 711
Cdd:PRK10529    3 NVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQ----WSAIPVIVL 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2738934608 712 TANAFEEDQQRCLVAGMDDFISKPINKDQLYA 743
Cdd:PRK10529   79 SARSEESDKIAALDAGADDYLSKPFGIGELQA 110
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
633-735 6.96e-03

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 38.90  E-value: 6.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 633 ILLVEDNPVNQIVLKKMLHSTECNLKQANDGLEALEILQSYQADIILMDCQMPNMDGYQCTKEIKQnphlYGQAIIIAIT 712
Cdd:PRK10710   13 ILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRR----FSDIPIVMVT 88
                          90       100
                  ....*....|....*....|...
gi 2738934608 713 ANAFEEDQQRCLVAGMDDFISKP 735
Cdd:PRK10710   89 AKIEEIDRLLGLEIGADDYICKP 111
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
517-610 8.79e-03

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 39.39  E-value: 8.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 517 AGKfTESGDITMSCTMVNDRMQISIRDTGIGIS--------------SEQQAKLFTE-----------FTQA----DISt 567
Cdd:COG0643   303 AGK-PETGTITLSAYHEGGRVVIEVSDDGRGLDlekirakaiekgliTAEEAAALSDeellelifapgFSTAeevtDLS- 380
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2738934608 568 trkygGTGLGLTISKRIIELMAGELKLTSQEGVGSEFTITMPV 610
Cdd:COG0643   381 -----GRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPL 418
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
268-473 9.45e-03

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


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 39.10  E-value: 9.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 268 SLVMIIFIILLTSVFITQLSRWLTTPIRKLAEQIDKFepENADTDTYLPQTWL-EVSRLQSQFSSLANKLALSFNRLHQA 346
Cdd:COG3850   120 ALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERI--ARGDFDARVPVSGRdELGTLARAFNRMADELQELYAELEEE 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2738934608 347 NHENELLNVRLKDFNAQLEKQVDDKTNELVEAVRAANNANRTKSQFLANMSHEIRTPLNGILGMTQLLLDNKDLAEEEHE 426
Cdd:COG3850   198 EELEAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLLQDALAESELLALNILAGLLELLLALLLLLLASA 277
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2738934608 427 ELVMIHQSANNLLLILNDILDFSKIEAGALKLEYRAVEITKLLEQIA 473
Cdd:COG3850   278 LLLLELELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQAIA 324
 
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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