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Conserved domains on  [gi|503337118|ref|WP_013571779|]
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ATP-binding protein [Vibrio vulnificus]

Protein Classification

ATP-binding protein( domain architecture ID 1002581)

ATP-binding protein similar to the ATPase domains of hybrid sensor kinases that regulate diverse biological functions through distinct molecular mechanisms

CATH:  3.30.565.10
EC:  2.7.13.3
Gene Ontology:  GO:0000155|GO:0005524
PubMed:  10966457
SCOP:  4001957

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 ...
180-564 2.00e-93

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: 306.70  E-value: 2.00e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  180 ENKEKLQRIVELRTREL--------------ALAREESERANRAKSEFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHI 245
Cdd:TIGR02956 420 EHKESLEQLVAQRTQELaetnerlnaevknhAKARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQ 499
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  246 NLLSHMESSAGLLLAIISDILDLSKIESGEFSLSPQWININDTVTFVVSQQQLVAATKGLNIELSIElDDKRHYWL-DPS 324
Cdd:TIGR02956 500 QYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIP-EQLPNWWQgDGP 578
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  325 RLSQVLFNLIGNAVKFTQQGQIDIRVNLEND-ELSISVIDTGIGIEKDKISSLFTAFKQADSsiTRKFGGTGLGLAITKH 403
Cdd:TIGR02956 579 RIRQVLINLVGNAIKFTDRGSVVLRVSLNDDsSLLFEVEDTGCGIAEEEQATLFDAFTQADG--RRRSGGTGLGLAISQR 656
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  404 LVELMSGTVRVSSQFGKGSTFVVKIPVKSRKLIRLSQDGTTnKRDRALNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNG 483
Cdd:TIGR02956 657 LVEAMDGELGVESELGVGSCFWFTLPLTRGKPAEDSATLTV-IDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESG 735
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  484 SEAIEFIESNteSLDVVFMDVSMPVMDGLTATKILRA---KGFEVPIIALTAHALASDKQNCLDVGMDSFVAKPVRKQEL 560
Cdd:TIGR02956 736 QSALECFHQH--AFDLALLDINLPDGDGVTLLQQLRAiygAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQL 813

                  ....
gi 503337118  561 ANAI 564
Cdd:TIGR02956 814 TAMI 817
 
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 ...
180-564 2.00e-93

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: 306.70  E-value: 2.00e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  180 ENKEKLQRIVELRTREL--------------ALAREESERANRAKSEFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHI 245
Cdd:TIGR02956 420 EHKESLEQLVAQRTQELaetnerlnaevknhAKARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQ 499
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  246 NLLSHMESSAGLLLAIISDILDLSKIESGEFSLSPQWININDTVTFVVSQQQLVAATKGLNIELSIElDDKRHYWL-DPS 324
Cdd:TIGR02956 500 QYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIP-EQLPNWWQgDGP 578
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  325 RLSQVLFNLIGNAVKFTQQGQIDIRVNLEND-ELSISVIDTGIGIEKDKISSLFTAFKQADSsiTRKFGGTGLGLAITKH 403
Cdd:TIGR02956 579 RIRQVLINLVGNAIKFTDRGSVVLRVSLNDDsSLLFEVEDTGCGIAEEEQATLFDAFTQADG--RRRSGGTGLGLAISQR 656
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  404 LVELMSGTVRVSSQFGKGSTFVVKIPVKSRKLIRLSQDGTTnKRDRALNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNG 483
Cdd:TIGR02956 657 LVEAMDGELGVESELGVGSCFWFTLPLTRGKPAEDSATLTV-IDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESG 735
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  484 SEAIEFIESNteSLDVVFMDVSMPVMDGLTATKILRA---KGFEVPIIALTAHALASDKQNCLDVGMDSFVAKPVRKQEL 560
Cdd:TIGR02956 736 QSALECFHQH--AFDLALLDINLPDGDGVTLLQQLRAiygAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQL 813

                  ....
gi 503337118  561 ANAI 564
Cdd:TIGR02956 814 TAMI 817
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
172-564 7.55e-84

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 280.20  E-value: 7.55e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 172 IERAVIDIenKEKLQRIvELRTRELALAREESERANRAKSEFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHINLLSHM 251
Cdd:PRK11107 258 IDQATSDL--RETLEQM-EIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTI 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 252 ESSAGLLLAIISDILDLSKIESGEFSLSPQWININDTVTFVVSQQQLVAATKGLNIELSIELDDKRHYWLDPSRLSQVLF 331
Cdd:PRK11107 335 ERSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIIT 414
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 332 NLIGNAVKFTQQGQIDIRVNL-----ENDELSISVIDTGIGIEKDKISSLFTAFKQADSSITRKFGGTGLGLAITKHLVE 406
Cdd:PRK11107 415 NLVGNAIKFTESGNIDILVELralsnTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVN 494
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 407 LMSGTVRVSSQFGKGSTFVVKI---------------------------------------------------------- 428
Cdd:PRK11107 495 EMGGDISFHSQPNRGSTFWFHLpldlnpnpiidglptdclagkrllyvepnsaaaqatldilsetplevtysptlsqlpe 574
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 429 -------------------------------------------------------------PVKSRKLIRLSQDGTTNKR 447
Cdd:PRK11107 575 ahydilllglpvtfrepltmlherlakaksmtdflilalpcheqvlaeqlkqdgadaclskPLSHTRLLPALLEPCHHKQ 654
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 448 DR----------ALNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNteSLDVVFMDVSMPVMDGLTATKI 517
Cdd:PRK11107 655 PPllpptdesrlPLTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQR--PFDLILMDIQMPGMDGIRACEL 732
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 503337118 518 LRAKGF--EVPIIALTAHALASDKQNCLDVGMDSFVAKPVRKQELANAI 564
Cdd:PRK11107 733 IRQLPHnqNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVL 781
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
167-430 1.07e-75

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 243.28  E-value: 1.07e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 167 RFLPLIERAVIDIENKEKLQRIVELRTRELALAREESERANRAKSEFLAMMSHELRTPLNSVLGMLDVLKQsDMSAGHIN 246
Cdd:COG0642   67 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLE-ELDEEQRE 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 247 LLSHMESSAGLLLAIISDILDLSKIESGEFSLSPQWININDTVTFVVSQQQLVAATKGLNIELSIElDDKRHYWLDPSRL 326
Cdd:COG0642  146 YLETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLP-DDLPTVRGDPDRL 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 327 SQVLFNLIGNAVKFTQQG-QIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFKQADSSitRKFGGTGLGLAITKHLV 405
Cdd:COG0642  225 RQVLLNLLSNAIKYTPEGgTVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIV 302
                        250       260
                 ....*....|....*....|....*
gi 503337118 406 ELMSGTVRVSSQFGKGSTFVVKIPV 430
Cdd:COG0642  303 ELHGGTIEVESEPGKGTTFTVTLPL 327
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
326-430 1.19e-51

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: 172.29  E-value: 1.19e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 326 LSQVLFNLIGNAVKFTQQGQIDIRVNLENDE-----LSISVIDTGIGIEKDKISSLFTAFKQADSSITRKFGGTGLGLAI 400
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEedgvqLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 503337118 401 TKHLVELMSGTVRVSSQFGKGSTFVVKIPV 430
Cdd:cd16922   81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
322-431 1.81e-35

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 128.92  E-value: 1.81e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118   322 DPSRLSQVLFNLIGNAVKFT-QQGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFKQADSSiTRKFGGTGLGLAI 400
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGTGLGLSI 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 503337118   401 TKHLVELMSGTVRVSSQFGKGSTFVVKIPVK 431
Cdd:smart00387  81 VKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
322-431 9.48e-31

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


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 115.54  E-value: 9.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  322 DPSRLSQVLFNLIGNAVKFT-QQGQIDIRVNlENDELSISVIDTGIGIEKDKISSLFTAFKQADSsitRKFGGTGLGLAI 400
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAaKAGEITVTLS-EGGELTLTVEDNGIGIPPEDLPRIFEPFSTADK---RGGGGTGLGLSI 77
                          90       100       110
                  ....*....|....*....|....*....|.
gi 503337118  401 TKHLVELMSGTVRVSSQFGKGSTFVVKIPVK 431
Cdd:pfam02518  78 VRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
183-429 3.85e-27

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 115.12  E-value: 3.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 183 EKLQR-IVELrtrelalarEESERANRaksEFLAMMSHELRTPLNSVLGMLDVLKQS--DMSAGhinllshMESSAGLLL 259
Cdd:NF040691 255 DSLQRqIRQL---------EELSRLQQ---RFVSDVSHELRTPLTTIRMAADVIHDSrdDFDPA-------TARSAELLH 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 260 A-------IISDILDLSKIESGEFSLSPQWININDTVTFVVSQQQLVAATKGlnIELSIELDDKR-HYWLDPSRLSQVLF 331
Cdd:NF040691 316 TeldrfesLLSDLLEISRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAG--VELRVDAPGTPvVAEVDPRRVERVLR 393
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 332 NLIGNAVKFTQQGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFKQADSSITRKFGGTGLGLAITKHLVELMSGT 411
Cdd:NF040691 394 NLVVNAIEHGEGKPVVVTVAQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGW 473
                        250
                 ....*....|....*...
gi 503337118 412 VRVSSQFGKGSTFVVKIP 429
Cdd:NF040691 474 LEAWGRPGQGSQFRLTLP 491
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
195-429 7.99e-24

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 104.52  E-value: 7.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 195 ELALAREESERANRAkseFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHINLLShMESSAGLLLAIISDILDLSKIESG 274
Cdd:NF012163 228 QLASTLEKNEQMRRD---FMADISHELRTPLAVLRAELEAIQDGIRKFTPESLDS-LQAEVGTLTKLVDDLHDLSMSDEG 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 275 EFSLSPQWININDTVTFVVSQQQLVAATKGLNIElsIELDDKRHYWLDPSRLSQVLFNLIGNAVKFTQQ-GQIDIRVNLE 353
Cdd:NF012163 304 ALAYQKASVDLVPLLEVEGGAFRERFASAGLELE--VSLPDSSLVFGDRDRLMQLFNNLLENSLRYTDSgGSLHISASQR 381
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503337118 354 NDELSISVIDTGIGIEKDKISSLFTAFKQADSSITRKFGGTGLGLAITKHLVELMSGTVRVS-SQFGkGSTFVVKIP 429
Cdd:NF012163 382 PKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAhSPLG-GLRIVVTLP 457
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
215-429 9.63e-24

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


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 102.77  E-value: 9.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 215 AMMSHELRTPLnSVL-----GMLDVLKQSDmSAGHINLLSHMESsaglLLAIISDILDLSKIESGEFSLSPQWININDTV 289
Cdd:NF012226 143 AAIAHELRTPI-TILqgrlqGILDGVFEPD-PALFKSLLNQVEG----LSHLVEDLRTLSLVENQQLRLNYESVDLKDSI 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 290 TFVVSQQQLVAATKGLNIELSIELDDkrhYWLDPSRLSQVLFNLIGNAVKFTQQGQIDIRVNLENDELSISVIDTGIGIE 369
Cdd:NF012226 217 EKVLKMFEDRLEQAQLTIVLNLTATP---VFCDRRRIEQVLIALIDNAIRYANAGKLKISSSVIQDDWILQIEDEGPGIA 293
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 370 KDKISSLFTAFKQADSSITRKFGGTGLGLAITKHLVELMSGTVRVSSQFGkGSTFVVKIP 429
Cdd:NF012226 294 EEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEYSNSQG-NSVFTIKLP 352
 
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 ...
180-564 2.00e-93

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: 306.70  E-value: 2.00e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  180 ENKEKLQRIVELRTREL--------------ALAREESERANRAKSEFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHI 245
Cdd:TIGR02956 420 EHKESLEQLVAQRTQELaetnerlnaevknhAKARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQ 499
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  246 NLLSHMESSAGLLLAIISDILDLSKIESGEFSLSPQWININDTVTFVVSQQQLVAATKGLNIELSIElDDKRHYWL-DPS 324
Cdd:TIGR02956 500 QYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIP-EQLPNWWQgDGP 578
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  325 RLSQVLFNLIGNAVKFTQQGQIDIRVNLEND-ELSISVIDTGIGIEKDKISSLFTAFKQADSsiTRKFGGTGLGLAITKH 403
Cdd:TIGR02956 579 RIRQVLINLVGNAIKFTDRGSVVLRVSLNDDsSLLFEVEDTGCGIAEEEQATLFDAFTQADG--RRRSGGTGLGLAISQR 656
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  404 LVELMSGTVRVSSQFGKGSTFVVKIPVKSRKLIRLSQDGTTnKRDRALNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNG 483
Cdd:TIGR02956 657 LVEAMDGELGVESELGVGSCFWFTLPLTRGKPAEDSATLTV-IDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESG 735
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  484 SEAIEFIESNteSLDVVFMDVSMPVMDGLTATKILRA---KGFEVPIIALTAHALASDKQNCLDVGMDSFVAKPVRKQEL 560
Cdd:TIGR02956 736 QSALECFHQH--AFDLALLDINLPDGDGVTLLQQLRAiygAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQL 813

                  ....
gi 503337118  561 ANAI 564
Cdd:TIGR02956 814 TAMI 817
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
172-564 7.55e-84

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 280.20  E-value: 7.55e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 172 IERAVIDIenKEKLQRIvELRTRELALAREESERANRAKSEFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHINLLSHM 251
Cdd:PRK11107 258 IDQATSDL--RETLEQM-EIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTI 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 252 ESSAGLLLAIISDILDLSKIESGEFSLSPQWININDTVTFVVSQQQLVAATKGLNIELSIELDDKRHYWLDPSRLSQVLF 331
Cdd:PRK11107 335 ERSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIIT 414
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 332 NLIGNAVKFTQQGQIDIRVNL-----ENDELSISVIDTGIGIEKDKISSLFTAFKQADSSITRKFGGTGLGLAITKHLVE 406
Cdd:PRK11107 415 NLVGNAIKFTESGNIDILVELralsnTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVN 494
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 407 LMSGTVRVSSQFGKGSTFVVKI---------------------------------------------------------- 428
Cdd:PRK11107 495 EMGGDISFHSQPNRGSTFWFHLpldlnpnpiidglptdclagkrllyvepnsaaaqatldilsetplevtysptlsqlpe 574
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 429 -------------------------------------------------------------PVKSRKLIRLSQDGTTNKR 447
Cdd:PRK11107 575 ahydilllglpvtfrepltmlherlakaksmtdflilalpcheqvlaeqlkqdgadaclskPLSHTRLLPALLEPCHHKQ 654
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 448 DR----------ALNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNteSLDVVFMDVSMPVMDGLTATKI 517
Cdd:PRK11107 655 PPllpptdesrlPLTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQR--PFDLILMDIQMPGMDGIRACEL 732
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 503337118 518 LRAKGF--EVPIIALTAHALASDKQNCLDVGMDSFVAKPVRKQELANAI 564
Cdd:PRK11107 733 IRQLPHnqNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVL 781
PRK15347 PRK15347
two component system sensor kinase;
180-566 1.31e-83

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 279.60  E-value: 1.31e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 180 ENKEKLQRIVELRTRELALAREESERANRAKSEFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHINLLSHMESSAGLLL 259
Cdd:PRK15347 368 EQYDTLENKVAERTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLL 447
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 260 AIISDILDLSKIESGEFSLSPQWININDTVTFVVSQQQLVAATKGLNIELSIELDDKRHYWLDPSRLSQVLFNLIGNAVK 339
Cdd:PRK15347 448 AIINNLLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVK 527
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 340 FTQQGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFKQADSSItrkfGGTGLGLAITKHLVELMSGTVRVSSQFG 419
Cdd:PRK15347 528 FTETGGIRLRVKRHEQQLCFTVEDTGCGIDIQQQQQIFTPFYQADTHS----QGTGLGLTIASSLAKMMGGELTLFSTPG 603
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 420 KGSTFVVKIPVKS--------------------------------------------------RKLIRLSQDGTTNKRDR 449
Cdd:PRK15347 604 VGSCFSLVLPLNEyappeplkgelsaplalhrqlsawgitcqpghqnpalldpelaylpgrlyDLLQQIIQGAPNEPVIN 683
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 450 A------LNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFieSNTESLDVVFMDVSMPVMDGLTATKILR--AK 521
Cdd:PRK15347 684 LplqpwqLQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALEL--GRQHRFDLVLMDIRMPGLDGLETTQLWRddPN 761
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 503337118 522 GF--EVPIIALTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEA 566
Cdd:PRK15347 762 NLdpDCMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARALEL 808
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
199-567 1.35e-79

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 266.04  E-value: 1.35e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 199 AREESERANRAKSEFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHINLLSHMESSAGLLLAIISDILDLSKIESGEFSL 278
Cdd:PRK11091 272 YQDALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQL 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 279 SPQWININDTVTFVVSQQQLVAATKGLNIELSIELDDKRHYWLDPSRLSQVLFNLIGNAVKFTQQGQIDIRVNLE-NDEL 357
Cdd:PRK11091 352 DNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRYEeGDML 431
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 358 SISVIDTGIGIEKDKISSLFTAFKQA-DSSITRKFGGTGLGLAITKHLVELMSGTVRVSSQFGKGSTFVVKIPVKSRKLI 436
Cdd:PRK11091 432 TFEVEDSGIGIPEDELDKIFAMYYQVkDSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAPAVAEE 511
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 437 RLSQDGTTNKRDRALNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNteSLDVVFMDVSMPVMDGLTATK 516
Cdd:PRK11091 512 VEDAFDEDDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPD--EYDLVLLDIQLPDMTGLDIAR 589
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 503337118 517 ILRAK-GFE--VPIIALTAHALaSDKQNCLDVGMDSFVAKPVRKQELANAIEAL 567
Cdd:PRK11091 590 ELRERyPREdlPPLVALTANVL-KDKKEYLDAGMDDVLSKPLSVPALTAMIKKF 642
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
167-430 1.07e-75

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 243.28  E-value: 1.07e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 167 RFLPLIERAVIDIENKEKLQRIVELRTRELALAREESERANRAKSEFLAMMSHELRTPLNSVLGMLDVLKQsDMSAGHIN 246
Cdd:COG0642   67 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLE-ELDEEQRE 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 247 LLSHMESSAGLLLAIISDILDLSKIESGEFSLSPQWININDTVTFVVSQQQLVAATKGLNIELSIElDDKRHYWLDPSRL 326
Cdd:COG0642  146 YLETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLP-DDLPTVRGDPDRL 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 327 SQVLFNLIGNAVKFTQQG-QIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFKQADSSitRKFGGTGLGLAITKHLV 405
Cdd:COG0642  225 RQVLLNLLSNAIKYTPEGgTVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIV 302
                        250       260
                 ....*....|....*....|....*
gi 503337118 406 ELMSGTVRVSSQFGKGSTFVVKIPV 430
Cdd:COG0642  303 ELHGGTIEVESEPGKGTTFTVTLPL 327
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
195-555 5.17e-73

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 250.66  E-value: 5.17e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 195 ELALAreeSERANRAKSEFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHINLLSHMESSAGLLLAIISDILDLSKIESG 274
Cdd:PRK10841 435 EMAQA---AEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESE 511
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 275 EFSLSPQWININDTVTFVVSQQQLVAATKGLNIELSIELDDKRHYWLDPSRLSQVLFNLIGNAVKFTQQGQIDIRVNLEN 354
Cdd:PRK10841 512 QLKIEPREFSPREVINHITANYLPLVVKKRLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHVRVDG 591
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 355 DELSISVIDTGIGIEKDKISSLFTAFKQADSSITRKFGGTGLGLAITKHLVELMSGTVRVSSQFGKGSTFVVKIPV---- 430
Cdd:PRK10841 592 DYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIPLygaq 671
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 431 ---------------------------------------------------------------KSRKLIRLSQD------ 441
Cdd:PRK10841 672 ypqkkgveglqgkrcwlavrnasleqfletllqrsgiqvqryegqeptpedvlitddpvqkkwQGRAVITFCRRhigipl 751
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 442 ---------GT----------------------------TNKRDRALN----VLVVEDTHSNQMVIQLLLNKLGHNVFIA 480
Cdd:PRK10841 752 eiapgewvhSTatphelpallariyrielesddsanalpSTDKAVSDNddmmILVVDDHPINRRLLADQLGSLGYQCKTA 831
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503337118 481 NNGSEAIEFIESNteSLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTAHALASDKQNCLDVGMDSFVAKPV 555
Cdd:PRK10841 832 NDGVDALNVLSKN--HIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVTANALAEEKQRCLEAGMDSCLSKPV 904
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
195-432 1.19e-71

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 229.41  E-value: 1.19e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 195 ELALAREESERANRAKSEFLAMMSHELRTPLNSVLGMLDVLKQSD--MSAGHINLLSHMESSAGLLLAIISDILDLSKIE 272
Cdd:COG2205    1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEdlSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 273 SGEFSLSPQWININDTVTFVVSQQQLVAATKGLNIELSIELDDKRHYWlDPSRLSQVLFNLIGNAVKFTQQG-QIDIRVN 351
Cdd:COG2205   81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYA-DPELLEQVLANLLDNAIKYSPPGgTITISAR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 352 LENDELSISVIDTGIGIEKDKISSLFTAFKQADSsiTRKFGGTGLGLAITKHLVELMSGTVRVSSQFGKGSTFVVKIPVK 431
Cdd:COG2205  160 REGDGVRISVSDNGPGIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLA 237

                 .
gi 503337118 432 S 432
Cdd:COG2205  238 E 238
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
130-432 1.34e-69

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 229.44  E-value: 1.34e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 130 INSVLLTGIDAQVTQSVILLIGNTKGQFSIEAKETLKRFLPLIERAVIDIENKEKLQRIVELRTRELALAR--EESERAN 207
Cdd:COG5002   83 LLLLALLLLLLLLLLLLALLILLLLLALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERdiTELERLE 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 208 RAKSEFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHI--NLLSHMESSAGLLLAIISDILDLSKIESGEFSLSPQWINI 285
Cdd:COG5002  163 QMRREFVANVSHELRTPLTSIRGYLELLLDGAADDPEErrEYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDL 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 286 NDTVTFVVSQQQLVAATKGLNIELSIElDDKRHYWLDPSRLSQVLFNLIGNAVKFTQQG-QIDIRVNLENDELSISVIDT 364
Cdd:COG5002  243 AELLEEVVEELRPLAEEKGIELELDLP-EDPLLVLGDPDRLEQVLTNLLDNAIKYTPEGgTITVSLREEDDQVRISVRDT 321
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503337118 365 GIGIEKDKISSLFTAFKQADSSITRKFGGTGLGLAITKHLVELMSGTVRVSSQFGKGSTFVVKIPVKS 432
Cdd:COG5002  322 GIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPLAR 389
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
186-555 9.93e-56

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 203.04  E-value: 9.93e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  186 QRIVELR--TRELALAREESERANRAKSEFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGH-INLLSHMESSAGLLLAII 262
Cdd:PRK09959  686 QDITETRdlIHALEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQrVEAISLAYATGQSLLGLI 765
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  263 SDILDLSKIESGEFSLSPQWININDTVTFVVSQQQLVAATKGLNIELSIELDDKRHYWLDPSRLSQVLFNLIGNAVKFTQ 342
Cdd:PRK09959  766 GEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLSNALKFTT 845
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  343 QGQIDIRVNLENDE-----LSISVIDTGIGIEKDKISSLFTAFKQadSSITRKFGGTGLGLAITKHLVELMSGTVRVSSQ 417
Cdd:PRK09959  846 EGAVKITTSLGHIDdnhavIKMTIMDSGSGLSQEEQQQLFKRYSQ--TSAGRQQTGSGLGLMICKELIKNMQGDLSLESH 923
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  418 FGKGSTFVVKIPVKSRKLI-----RLSQDGTTNKRdraLNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIes 492
Cdd:PRK09959  924 PGIGTTFTITIPVEISQQVatveaKAEQPITLPEK---LSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKV-- 998
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503337118  493 NTESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTAHALASDKQNCLDVGMDSFVAKPV 555
Cdd:PRK09959  999 SMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPL 1061
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
182-564 1.08e-53

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 196.28  E-value: 1.08e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 182 KEKLQRIVELRTREL-AL------AREESERANRAKSEFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHINLLSHMESS 254
Cdd:PRK11466 409 REQLAAQVKARTAELqELviehrqARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDS 488
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 255 AGLLLAIISDILDLSKIESGEFSLSpqwinINDTvtfVVSQQQLVAAT--------KGLNIELSIELDDKRHYWL--DPS 324
Cdd:PRK11466 489 GESLLTILNDILDYSAIEAGGKNVS-----VSDE---PFEPRPLLESTlqlmsgrvKGRPIRLATDIADDLPTALmgDPR 560
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 325 RLSQVLFNLIGNAVKFTQQGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFKQAdssiTRKFGGTGLGLAITKHL 404
Cdd:PRK11466 561 RIRQVITNLLSNALRFTDEGSIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFVQV----SGKRGGTGLGLTISSRL 636
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 405 VELMSGTVRVSSQFGKGSTFVVKIPVK---------SRKLIRLSqdgttnkrdrALNVLVVEDTHSNQMVIQLLLNKLGH 475
Cdd:PRK11466 637 AQAMGGELSATSTPEVGSCFCLRLPLRvatapvpktVNQAVRLD----------GLRLLLIEDNPLTQRITAEMLNTSGA 706
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 476 NVFIANNGSEAIEFIeSNTESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTAHALASDKQNCLDVGMDSFVAKPV 555
Cdd:PRK11466 707 QVVAVGNAAQALETL-QNSEPFAAALVDFDLPDYDGITLARQLAQQYPSLVLIGFSAHVIDETLRQRTSSLFRGIIPKPV 785

                 ....*....
gi 503337118 556 RKQELANAI 564
Cdd:PRK11466 786 PREVLGQLL 794
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
326-430 1.19e-51

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: 172.29  E-value: 1.19e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 326 LSQVLFNLIGNAVKFTQQGQIDIRVNLENDE-----LSISVIDTGIGIEKDKISSLFTAFKQADSSITRKFGGTGLGLAI 400
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEedgvqLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 503337118 401 TKHLVELMSGTVRVSSQFGKGSTFVVKIPV 430
Cdd:cd16922   81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
171-433 1.52e-47

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 173.43  E-value: 1.52e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 171 LIERAVIDIENKEKLQRIVELRTRELALAREESERANRAKSEFLAMMSHELRTPLNSVLGMLDVLKQ---SDMSAGHINL 247
Cdd:COG4251  243 LLLLLLILVLELLELRLELEELEEELEERTAELERSNEELEQFAYVASHDLREPLRKISGFSQLLEEdygDKLDEEGREY 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 248 LSHMESSAGLLLAIISDILDLSKIESGEfsLSPQWININDTVTFVVSQQQLVAATKGLnielSIELDDKRHYWLDPSRLS 327
Cdd:COG4251  323 LERIRDAAERMQALIDDLLAYSRVGRQE--LEFEPVDLNELLEEVLEDLEPRIEERGA----EIEVGPLPTVRGDPTLLR 396
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 328 QVLFNLIGNAVKFT---QQGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFKQADSSitRKFGGTGLGLAITKHL 404
Cdd:COG4251  397 QVFQNLISNAIKYSrpgEPPRIEIGAEREGGEWVFSVRDNGIGIDPEYAEKIFEIFQRLHSR--DEYEGTGIGLAIVKKI 474
                        250       260
                 ....*....|....*....|....*....
gi 503337118 405 VELMSGTVRVSSQFGKGSTFVVKIPVKSR 433
Cdd:COG4251  475 VERHGGRIWVESEPGEGATFYFTLPKAPA 503
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
453-564 6.10e-43

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 149.16  E-value: 6.10e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRA---KGFEVPIIA 529
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKE--EPFDLVLMDLQMPVMDGLEATRRIRElegGGRRTPIIA 78
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 503337118 530 LTAHALASDKQNCLDVGMDSFVAKPVRKQELANAI 564
Cdd:cd17546   79 LTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
188-434 3.20e-40

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: 152.82  E-value: 3.20e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 188 IVELRTRELALarEESERANRAkSEFLAMMSHELRTPLNSVLGMLDVLKQSDMSAG--HINLlshMESSAGLLLAIISDI 265
Cdd:COG5809  251 ITERKKLEELL--RKSEKLSVV-GELAAGIAHEIRNPLTSLKGFIQLLKDTIDEEQktYLDI---MLSELDRIESIISEF 324
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 266 LDLSKIESGEFSLSPqwIN--INDTVTFVVSQQQLVaatkglNIELSIELDDKRHY-WLDPSRLSQVLFNLIGNAVKFT- 341
Cdd:COG5809  325 LVLAKPQAIKYEPKD--LNtlIEEVIPLLQPQALLK------NVQIELELEDDIPDiLGDENQLKQVFINLLKNAIEAMp 396
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 342 QQGQIDIRVN-LENDELSISVIDTGIGIEKDKISSLFTAFkqadssITRKFGGTGLGLAITKHLVELMSGTVRVSSQFGK 420
Cdd:COG5809  397 EGGNITIETKaEDDDKVVISVTDEGCGIPEERLKKLGEPF------YTTKEKGTGLGLMVSYKIIEEHGGKITVESEVGK 470
                        250
                 ....*....|....
gi 503337118 421 GSTFVVKIPVKSRK 434
Cdd:COG5809  471 GTTFSITLPIKLSE 484
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
170-428 9.22e-40

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: 147.74  E-value: 9.22e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  170 PLIERAVIDIEnkeklqRIVELR------TRELALARE--ESERANRAKSEFLAMMSHELRTPLNSVLGMLDVLKQS--- 238
Cdd:TIGR02966  72 PLELPSPINSE------RVLEIRiapygeEQKLLVARDvtRLRRLEQMRRDFVANVSHELRTPLTVLRGYLETLADGpde 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  239 --DMSAGHINLlshMESSAGLLLAIISDILDLSKIESGEFSLSPQWININDTVTFVVSQQQLVAATKGLNIELSIELDdk 316
Cdd:TIGR02966 146 dpEEWNRALEI---MLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALLDHLRDEAEALSQGKNHQITFEIDGG-- 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  317 rhYWL--DPSRLSQVLFNLIGNAVKFTQ-QGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFKQADSSITRKFGG 393
Cdd:TIGR02966 221 --VDVlgDEDELRSAFSNLVSNAIKYTPeGGTITVRWRRDGGGAEFSVTDTGIGIAPEHLPRLTERFYRVDKSRSRDTGG 298
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 503337118  394 TGLGLAITKHLVELMSGTVRVSSQFGKGSTFVVKI 428
Cdd:TIGR02966 299 TGLGLAIVKHVLSRHHARLEIESELGKGSTFSFIF 333
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
447-568 1.38e-38

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: 138.06  E-value: 1.38e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 447 RDRALNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRA--KGFE 524
Cdd:COG0784    2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRA--GPPDLILLDINMPGMDGLELLRRIRAlpRLPD 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 503337118 525 VPIIALTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:COG0784   80 IPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLL 123
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
322-431 1.81e-35

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 128.92  E-value: 1.81e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118   322 DPSRLSQVLFNLIGNAVKFT-QQGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFKQADSSiTRKFGGTGLGLAI 400
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGTGLGLSI 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 503337118   401 TKHLVELMSGTVRVSSQFGKGSTFVVKIPVK 431
Cdd:smart00387  81 VKKLVELHGGEISVESEPGGGTTFTITLPLE 111
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
163-431 2.38e-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: 2.38e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 163 ETLKRFLPLIERAVIDIENKEKLQRIVELR--TRELALAREESERANRAKS--EFLAMMSHELRTPLNSVLGMLDVLKQS 238
Cdd:COG4191   91 EALLLLLLAALDAEENAELEELERDITELEraEEELRELQEQLVQSEKLAAlgELAAGIAHEINNPLAAILGNAELLRRR 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 239 DMSAGH----INLLSHMESSAGLLLAIISDILDLSKIESGEfslsPQWININDTVTFVVSqqqLVAAT-KGLNIELSIEL 313
Cdd:COG4191  171 LEDEPDpeelREALERILEGAERAAEIVRSLRAFSRRDEEE----REPVDLNELIDEALE---LLRPRlKARGIEVELDL 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 314 DDKRHY-WLDPSRLSQVLFNLIGN---AVKFTQQGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAF---KQADss 386
Cdd:COG4191  244 PPDLPPvLGDPGQLEQVLLNLLINaidAMEEGEGGRITISTRREGDYVVISVRDNGPGIPPEVLERIFEPFfttKPVG-- 321
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 503337118 387 itrkfGGTGLGLAITKHLVELMSGTVRVSSQFGKGSTFVVKIPVK 431
Cdd:COG4191  322 -----KGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLPLA 361
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
188-434 4.18e-34

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 132.66  E-value: 4.18e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 188 IVELR--TRELALAREEsERANRAKS--EFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHINLLSHMESSAGLLLAIIS 263
Cdd:COG3852  110 LLVLRdiTERKRLEREL-RRAEKLAAvgELAAGLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVD 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 264 DILDLSKIESGEFslspQWININDTVTFVVsqqQLVAATKGLNIELSIELDDKRHY-WLDPSRLSQVLFNLIGNAVK-FT 341
Cdd:COG3852  189 RLLSFSRPRPPER----EPVNLHEVLERVL---ELLRAEAPKNIRIVRDYDPSLPEvLGDPDQLIQVLLNLVRNAAEaMP 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 342 QQGQIDIRVNLE----------NDELSISVIDTGIGIEKDKISSLFTAFkqadssITRKFGGTGLGLAITKHLVELMSGT 411
Cdd:COG3852  262 EGGTITIRTRVErqvtlgglrpRLYVRIEVIDNGPGIPEEILDRIFEPF------FTTKEKGTGLGLAIVQKIVEQHGGT 335
                        250       260
                 ....*....|....*....|...
gi 503337118 412 VRVSSQFGKGSTFVVKIPVKSRK 434
Cdd:COG3852  336 IEVESEPGKGTTFRIYLPLEQAE 358
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
205-430 2.30e-31

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: 126.23  E-value: 2.30e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 205 RANRAKS--EFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHIN------LLSHMESSAGLLLAIISDILDLSKIESgef 276
Cdd:COG5000  194 RAERLAAwgELARRIAHEIKNPLTPIQLSAERLRRKLADKLEEDredlerALDTIIRQVDRLKRIVDEFLDFARLPE--- 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 277 sLSPQWININDTVTFVVSQQQLVAATKGLNIELSIElDDKRHYWLDPSRLSQVLFNLIGNAVKFT-QQGQIDIRVNLEND 355
Cdd:COG5000  271 -PQLEPVDLNELLREVLALYEPALKEKDIRLELDLD-PDLPEVLADRDQLEQVLINLLKNAIEAIeEGGEIEVSTRREDG 348
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503337118 356 ELSISVIDTGIGIEKDKISSLFTAFkqadssITRKFGGTGLGLAITKHLVELMSGTVRVSSQFGKGSTFVVKIPV 430
Cdd:COG5000  349 RVRIEVSDNGPGIPEEVLERIFEPF------FTTKPKGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPL 417
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
322-431 9.48e-31

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


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 115.54  E-value: 9.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  322 DPSRLSQVLFNLIGNAVKFT-QQGQIDIRVNlENDELSISVIDTGIGIEKDKISSLFTAFKQADSsitRKFGGTGLGLAI 400
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAaKAGEITVTLS-EGGELTLTVEDNGIGIPPEDLPRIFEPFSTADK---RGGGGTGLGLSI 77
                          90       100       110
                  ....*....|....*....|....*....|.
gi 503337118  401 TKHLVELMSGTVRVSSQFGKGSTFVVKIPVK 431
Cdd:pfam02518  78 VRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
450-567 1.29e-30

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: 117.70  E-value: 1.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 450 ALNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNteSLDVVFMDVSMPVMDGLTATKILRA--KGFEVPI 527
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEH--RPDLILLDLEMPDMDGLELCRRLRAdpRTADIPI 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 503337118 528 IALTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEAL 567
Cdd:COG3706   79 IFLTALDDEEDRARALEAGADDYLTKPFDPEELLARVDLV 118
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
453-568 7.62e-30

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: 116.21  E-value: 7.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIEsnTESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:COG0745    4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLE--EERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTA 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 533 HALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:COG0745   82 RDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALL 117
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
453-565 8.64e-29

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 110.32  E-value: 8.64e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIEsnTESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLK--EERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 503337118  533 HALASDKQNCLDVGMDSFVAKPVRKQELANAIE 565
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
183-429 3.85e-27

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 115.12  E-value: 3.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 183 EKLQR-IVELrtrelalarEESERANRaksEFLAMMSHELRTPLNSVLGMLDVLKQS--DMSAGhinllshMESSAGLLL 259
Cdd:NF040691 255 DSLQRqIRQL---------EELSRLQQ---RFVSDVSHELRTPLTTIRMAADVIHDSrdDFDPA-------TARSAELLH 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 260 A-------IISDILDLSKIESGEFSLSPQWININDTVTFVVSQQQLVAATKGlnIELSIELDDKR-HYWLDPSRLSQVLF 331
Cdd:NF040691 316 TeldrfesLLSDLLEISRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAG--VELRVDAPGTPvVAEVDPRRVERVLR 393
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 332 NLIGNAVKFTQQGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFKQADSSITRKFGGTGLGLAITKHLVELMSGT 411
Cdd:NF040691 394 NLVVNAIEHGEGKPVVVTVAQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGW 473
                        250
                 ....*....|....*...
gi 503337118 412 VRVSSQFGKGSTFVVKIP 429
Cdd:NF040691 474 LEAWGRPGQGSQFRLTLP 491
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
187-569 1.06e-26

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 115.16  E-value: 1.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 187 RIVELRTRELALAREeSERANR--AKSEFLAMMSHELRTPLNSVLG---M-LDVLKQSDMSAGHINLLSHmesSAGLLLA 260
Cdd:PRK13837 426 ERRRLETERDALERR-LEHARRleAVGTLASGIAHNFNNILGAILGyaeMaLNKLARHSRAARYIDEIIS---AGARARL 501
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 261 IISDILDLSKieSGEFSLSPqwININDTVTFVVSqqqLVAATKGLNIELSIELDDKRHYWL-DPSRLSQVLFNLIGNAVK 339
Cdd:PRK13837 502 IIDQILAFGR--KGERNTKP--FDLSELVTEIAP---LLRVSLPPGVELDFDQDQEPAVVEgNPAELQQVLMNLCSNAAQ 574
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 340 -FTQQGQIDIRV----NLENDELS-----------ISVIDTGIGIEKDKISSLFTAFkqadssITRKFGGTGLGLAITKH 403
Cdd:PRK13837 575 aMDGAGRVDISLsrakLRAPKVLShgvlppgryvlLRVSDTGAGIDEAVLPHIFEPF------FTTRAGGTGLGLATVHG 648
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 404 LVELMSGTVRVSSQFGKGSTFVVKIPVKSRKLIRLSQDGTTNK--RDRALNVLVVEDTHSNQMVIQLLLNKLGHNVFIAN 481
Cdd:PRK13837 649 IVSAHAGYIDVQSTVGRGTRFDVYLPPSSKVPVAPQAFFGPGPlpRGRGETVLLVEPDDATLERYEEKLAALGYEPVGFS 728
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 482 NGSEAIEFIESNTESLDVVFMDVSMPVMDGLTATkiLRAKGFEVPIIALTAHALASDKQNCLDVGmDSFVAKPVRKQELA 561
Cdd:PRK13837 729 TLAAAIAWISKGPERFDLVLVDDRLLDEEQAAAA--LHAAAPTLPIILGGNSKTMALSPDLLASV-AEILAKPISSRTLA 805

                 ....*...
gi 503337118 562 NAIEALIV 569
Cdd:PRK13837 806 YALRTALA 813
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
194-434 1.21e-26

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 112.96  E-value: 1.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 194 RELALAREESERANRAKSEFLAM------MSHELRTPLNSVLGMLDVLKQSDMSAGHINLLSH-MESSAGLLLAIISDIL 266
Cdd:PRK10364 215 RRYLRSRQLLQDEMKRKEKLVALghlaagVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQvMAKEADRLNRVVSELL 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 267 DLSKIESgefsLSPQWININDTVTFVVsqqQLV---AATKGLNIELSIElDDKRHYWLDPSRLSQVLFNLIGNAVK-FTQ 342
Cdd:PRK10364 295 ELVKPTH----LALQAVDLNDLINHSL---QLVsqdANSREIQLRFTAN-DTLPEIQADPDRLTQVLLNLYLNAIQaIGQ 366
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 343 QGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFkqadssITRKFGGTGLGLAITKHLVELMSGTVRVSSQFGKGS 422
Cdd:PRK10364 367 HGVISVTASESGAGVKISVTDSGKGIAADQLEAIFTPY------FTTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGA 440
                        250
                 ....*....|..
gi 503337118 423 TFVVKIPVKSRK 434
Cdd:PRK10364 441 TFTLWLPVNITR 452
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
209-431 6.95e-26

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: 111.36  E-value: 6.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 209 AKSEFLAM-------MSHELRTPLNSVLGMLDVLKQSDMSAGHINLLshMESSAGLLLAIISDILDLSKIESGEFslspQ 281
Cdd:COG5805  279 ARSEKLSIagqlaagIAHEIRNPLTSIKGFLQLLQPGIEDKEEYFDI--MLSELDRIESIISEFLALAKPQAVNK----E 352
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 282 WININDTVTFVVSQQQLVAATKGLNIELsIELDDKRHYWLDPSRLSQVLFNLIGNAVK-FTQQGQIDIRVNLENDELSIS 360
Cdd:COG5805  353 KENINELIQDVVTLLETEAILHNIQIRL-ELLDEDPFIYCDENQIKQVFINLIKNAIEaMPNGGTITIHTEEEDNSVIIR 431
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503337118 361 VIDTGIGIEKDKISSLFTAFkqadssITRKFGGTGLGLAITKHLVELMSGTVRVSSQFGKGSTFVVKIPVK 431
Cdd:COG5805  432 VIDEGIGIPEERLKKLGEPF------FTTKEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLPLS 496
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
448-568 3.16e-25

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 104.09  E-value: 3.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 448 DRALNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRA--KGFEV 525
Cdd:COG3437    4 GQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLE--APPDLILLDVRMPGMDGFELLRLLRAdpSTRDI 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 503337118 526 PIIALTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:COG3437   82 PVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNAL 124
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
452-565 3.65e-25

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: 100.31  E-value: 3.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 452 NVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTesLDVVFMDVSMPVMDGLTATKILRA--KGFEVPIIA 529
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEK--PDLILMDIQLPGMDGLEATRLLKEdpATRDIPVIA 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 530 LTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIE 565
Cdd:cd17548   79 LTAYAMKGDREKILEAGCDGYISKPIDTREFLETVA 114
PRK10490 PRK10490
sensor protein KdpD; Provisional
193-432 4.71e-25

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 110.13  E-value: 4.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 193 TRELALAREESERaNRAKSEFLAMMSHELRTPLNSVLGMLDVLKQSDMSAG--HINLLSHMESSAGLLLAIISDILDLSK 270
Cdd:PRK10490 648 TASEEQARLASER-EQLRNALLAALSHDLRTPLTVLFGQAEILTLDLASEGspHARQASEIRQQVLNTTRLVNNLLDMAR 726
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 271 IESGEFSLSPQWININDTVTFVVsqQQLVAATKGLNIELSIElDDKRHYWLDPSRLSQVLFNLIGNAVKFT-QQGQIDIR 349
Cdd:PRK10490 727 IQSGGFNLRKEWLTLEEVVGSAL--QMLEPGLSGHPINLSLP-EPLTLIHVDGPLFERVLINLLENAVKYAgAQAEIGID 803
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 350 VNLENDELSISVIDTGIGIEKDKISSLFTAFKQAD--SSITrkfgGTGLGLAITKHLVELMSGTVRVSSQFGKGSTFVVK 427
Cdd:PRK10490 804 AHVEGERLQLDVWDNGPGIPPGQEQLIFDKFARGNkeSAIP----GVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVT 879

                 ....*
gi 503337118 428 IPVKS 432
Cdd:PRK10490 880 LPLET 884
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
204-429 6.06e-24

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


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 104.78  E-value: 6.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  204 ERANRAKSEFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHINLLshMESSA---GLLLAIISDILDLSKIESGEFSLSP 280
Cdd:TIGR01386 235 EDAFQRLSQFSADLAHELRTPLTNLLGQTQVALSQPRTGEEYREV--LESNLeelERLSRMVSDMLFLARADNGQLALER 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  281 QWININDTVTFVVSQQQLVAATKGLNIELSIELDDKrhywLDPSRLSQVLFNLIGNAVKFTQQGQ-IDIRVNLENDELSI 359
Cdd:TIGR01386 313 VRLDLAAELAKVAEYFEPLAEERGVRIRVEGEGLVR----GDPQMFRRAISNLLSNALRHTPDGGtITVRIERRSDEVRV 388
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  360 SVIDTGIGIEKDKISSLFTAFKQADSSITRKFGGTGLGLAITKHLVELMSGTVRVSSQFGKgSTFVVKIP 429
Cdd:TIGR01386 389 SVSNPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAESPDGK-TRFILRFP 457
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
195-429 7.99e-24

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 104.52  E-value: 7.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 195 ELALAREESERANRAkseFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHINLLShMESSAGLLLAIISDILDLSKIESG 274
Cdd:NF012163 228 QLASTLEKNEQMRRD---FMADISHELRTPLAVLRAELEAIQDGIRKFTPESLDS-LQAEVGTLTKLVDDLHDLSMSDEG 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 275 EFSLSPQWININDTVTFVVSQQQLVAATKGLNIElsIELDDKRHYWLDPSRLSQVLFNLIGNAVKFTQQ-GQIDIRVNLE 353
Cdd:NF012163 304 ALAYQKASVDLVPLLEVEGGAFRERFASAGLELE--VSLPDSSLVFGDRDRLMQLFNNLLENSLRYTDSgGSLHISASQR 381
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503337118 354 NDELSISVIDTGIGIEKDKISSLFTAFKQADSSITRKFGGTGLGLAITKHLVELMSGTVRVS-SQFGkGSTFVVKIP 429
Cdd:NF012163 382 PKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAhSPLG-GLRIVVTLP 457
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
215-429 9.63e-24

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


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 102.77  E-value: 9.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 215 AMMSHELRTPLnSVL-----GMLDVLKQSDmSAGHINLLSHMESsaglLLAIISDILDLSKIESGEFSLSPQWININDTV 289
Cdd:NF012226 143 AAIAHELRTPI-TILqgrlqGILDGVFEPD-PALFKSLLNQVEG----LSHLVEDLRTLSLVENQQLRLNYESVDLKDSI 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 290 TFVVSQQQLVAATKGLNIELSIELDDkrhYWLDPSRLSQVLFNLIGNAVKFTQQGQIDIRVNLENDELSISVIDTGIGIE 369
Cdd:NF012226 217 EKVLKMFEDRLEQAQLTIVLNLTATP---VFCDRRRIEQVLIALIDNAIRYANAGKLKISSSVIQDDWILQIEDEGPGIA 293
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 370 KDKISSLFTAFKQADSSITRKFGGTGLGLAITKHLVELMSGTVRVSSQFGkGSTFVVKIP 429
Cdd:NF012226 294 EEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEYSNSQG-NSVFTIKLP 352
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
454-554 1.97e-23

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: 94.60  E-value: 1.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 454 LVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTAH 533
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLRE--ERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAK 78
                         90       100
                 ....*....|....*....|.
gi 503337118 534 ALASDKQNCLDVGMDSFVAKP 554
Cdd:cd00156   79 ADEEDAVRALELGADDYLVKP 99
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
322-429 5.09e-23

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: 94.10  E-value: 5.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 322 DPSRLSQVLFNLIGNAVKFTQQGQIdIRVNLENDELS---ISVIDTGIGIEKDKISSLFTAFKQADSSITRKFGGTGLGL 398
Cdd:cd16925    1 DAEKYERVVLNLLSNAFKFTPDGGR-IRCILEKFRLNrflLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGLGL 79
                         90       100       110
                 ....*....|....*....|....*....|.
gi 503337118 399 AITKHLVELMSGTVRVSSQFGKGSTFVVKIP 429
Cdd:cd16925   80 SIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
195-430 2.93e-22

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 99.71  E-value: 2.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 195 ELALAREESERANRAkseFLAMMSHELRTPLNSVLGMLDVL----KQSDMSAghinlLSHMESSAGLLLAIISDILDLSK 270
Cdd:PRK10549 228 QLASTLEKNEQMRRD---FMADISHELRTPLAVLRGELEAIqdgvRKFTPES-----VASLQAEVGTLTKLVDDLHQLSL 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 271 IESGEFSLSPQWININDTVTFVVSQQQLVAATKGLNIELSieLDDKRHYWLDPSRLSQVLFNLIGNAVKFT-QQGQIDIR 349
Cdd:PRK10549 300 SDEGALAYRKTPVDLVPLLEVAGGAFRERFASRGLTLQLS--LPDSATVFGDPDRLMQLFNNLLENSLRYTdSGGSLHIS 377
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 350 VNLENDELSISVIDTGIGIEKDKISSLFTAFKQADSSITRKFGGTGLGLAITKHLVELMSGTVRVS-SQFGkGSTFVVKI 428
Cdd:PRK10549 378 AEQRDKTLRLTFADSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRIIAAhSPFG-GVSITVEL 456

                 ..
gi 503337118 429 PV 430
Cdd:PRK10549 457 PL 458
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
186-429 3.76e-22

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 99.31  E-value: 3.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 186 QRIVELRT------RELALARE-------ESERANrakseFLAMMSHELRTPLNSVLGMLDVLKQSDM-SAGHINLLSHM 251
Cdd:PRK11006 172 GRHLEIRVmpytegQLLMVARDvtqmhqlEGARRN-----FFANVSHELRTPLTVLQGYLEMMQDQPLeGALREKALHTM 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 252 ESSAGLLLAIISDILDLSKIESgefslSPQwININDTV----TFVVSQQQLVAATKGlNIELSIELDDKRHYWLDPSRLS 327
Cdd:PRK11006 247 REQTQRMEGLVKQLLTLSKIEA-----APT-IDLNEKVdvpmMLRVLEREAQTLSQG-KHTITFEVDNSLKVFGNEDQLR 319
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 328 QVLFNLIGNAVKFTQQG-QIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFKQADSSITRKFGGTGLGLAITKHLVE 406
Cdd:PRK11006 320 SAISNLVYNAVNHTPEGtHITVRWQRVPQGAEFSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALS 399
                        250       260
                 ....*....|....*....|...
gi 503337118 407 LMSGTVRVSSQFGKGSTFVVKIP 429
Cdd:PRK11006 400 HHDSRLEIESEVGKGTRFSFVLP 422
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
454-554 9.03e-22

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: 90.16  E-value: 9.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 454 LVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTesLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTAH 533
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQ--PDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAK 78
                         90       100
                 ....*....|....*....|.
gi 503337118 534 ALASDKQNCLDVGMDSFVAKP 554
Cdd:cd17574   79 DEEEDKVLGLELGADDYITKP 99
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
449-568 1.60e-21

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: 96.96  E-value: 1.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 449 RALNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKGFEVPII 528
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLRE--EPPDLVLLDLRMPGMDGLELLRELRALDPDLPVI 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 503337118 529 ALTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:COG2204   79 LLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERAL 118
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
452-554 1.68e-21

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: 89.45  E-value: 1.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 452 NVLVVEDTHSNQMVIQLLLNKLG--HNVFIANNGSEAIEFIESNteSLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIA 529
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEH--KPDLVITDINMPGMDGLELLEAIRELDPDTKIII 78
                         90       100
                 ....*....|....*....|....*
gi 503337118 530 LTAHALASDKQNCLDVGMDSFVAKP 554
Cdd:COG4753   79 LSGYSDFEYAQEAIKLGADDYLLKP 103
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
200-434 3.64e-21

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 97.35  E-value: 3.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 200 REESERANR--AKSEFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHINLLSHMESSAGLLLAIISDILDLSKieSGEFS 277
Cdd:PRK11360 378 QRRVARQERlaALGELVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEFSR--PRESQ 455
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 278 LSPqwININDTVTFVVsqqQLVAATKGLN-IELSIELD-DKRHYWLDPSRLSQVLFNLIGNAVK-FTQQGQIDIRVNLEN 354
Cdd:PRK11360 456 WQP--VSLNALVEEVL---QLFQTAGVQArVDFETELDnELPPIWADPELLKQVLLNILINAVQaISARGKIRIRTWQYS 530
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 355 D-ELSISVIDTGIGIEKDKISSLFTAFkqadssITRKFGGTGLGLAITKHLVELMSGTVRVSSQFGKGSTFVVKIPVKSR 433
Cdd:PRK11360 531 DgQVAVSIEDNGCGIDPELLKKIFDPF------FTTKAKGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPINPQ 604

                 .
gi 503337118 434 K 434
Cdd:PRK11360 605 G 605
PRK13557 PRK13557
histidine kinase; Provisional
283-568 3.84e-21

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 97.05  E-value: 3.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 283 ININDTVTfvvSQQQLVAATKGLNIELSIELD-DKRHYWLDPSRLSQVLFNLIGNAVKFTQQGQiDIRVNLENDEL---- 357
Cdd:PRK13557 237 LNLNGLVS---GMGELAERTLGDAVTIETDLApDLWNCRIDPTQAEVALLNVLINARDAMPEGG-RVTIRTRNVEIeded 312
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 358 -------------SISVIDTGIGIEKDKISSL----FTafkqadssiTRKFG-GTGLGLAITKHLVELMSGTVRVSSQFG 419
Cdd:PRK13557 313 lamyhglppgryvSIAVTDTGSGMPPEILARVmdpfFT---------TKEEGkGTGLGLSMVYGFAKQSGGAVRIYSEVG 383
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 420 KGSTFVVKIPVkSRKLIRLSQDGTTNKRDRALN--VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTEsL 497
Cdd:PRK13557 384 EGTTVRLYFPA-SDQAENPEQEPKARAIDRGGTetILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHPE-V 461
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503337118 498 DVVFMDVSMP-VMDGLTATKILRAKGFEVPIIALTAHALASDKQNclDVGMDSF--VAKPVRKQELANAIEALI 568
Cdd:PRK13557 462 DLLFTDLIMPgGMNGVMLAREARRRQPKIKVLLTTGYAEASIERT--DAGGSEFdiLNKPYRRAELARRVRMVL 533
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
453-564 4.26e-21

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 88.67  E-value: 4.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIEsnTESLDVVFMDVSMPVMDGLTATKILRA--KGFEVPIIAL 530
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQ--RFRPDVILSDIGMPGMDGYELARRLRElpWLANTPAIAL 78
                         90       100       110
                 ....*....|....*....|....*....|....
gi 503337118 531 TAHALASDKQNCLDVGMDSFVAKPVRKQELANAI 564
Cdd:cd17580   79 TGYGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
326-429 5.25e-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: 85.07  E-value: 5.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 326 LSQVLFNLIGNAVKFTQQG---QIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFKQADSSitRKFGGTGLGLAITK 402
Cdd:cd16921    1 LGQVLTNLLGNAIKFRRPRrppRIEVGAEDVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRLHSR--EEYEGTGVGLAIVR 78
                         90       100
                 ....*....|....*....|....*..
gi 503337118 403 HLVELMSGTVRVSSQFGKGSTFVVKIP 429
Cdd:cd16921   79 KIIERHGGRIWLESEPGEGTTFYFTLP 105
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
449-568 9.38e-20

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 85.79  E-value: 9.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 449 RALNVLVVEDTHSNQMVIQLLLNKLG--HNVFIANNGSEAIEFIESNTesLDVVFMDVSMPVMDGLTATKILRAKGFEVP 526
Cdd:COG4565    2 KMIRVLIVEDDPMVAELLRRYLERLPgfEVVGVASSGEEALALLAEHR--PDLILLDIYLPDGDGLELLRELRARGPDVD 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 503337118 527 IIALTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:COG4565   80 VIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYL 121
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
454-568 1.10e-19

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: 84.58  E-value: 1.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 454 LVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTAH 533
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALS--GIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTAL 78
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 503337118 534 ALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:cd17625   79 DAVEDRVKGLDLGADDYLPKPFSLAELLARIRALL 113
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
322-429 2.13e-19

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: 83.67  E-value: 2.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 322 DPSRLSQVLFNLIGNAVKFTQQG-QIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFKQADSSITRKFGGTGLGLAI 400
Cdd:cd16946    1 DRDRLQQLFVNLLENSLRYTDTGgKLRIRAAQTPQEVRLDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGLGLAI 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 503337118 401 TKHLVELMSGTVRVS-SQFGkGSTFVVKIP 429
Cdd:cd16946   81 CHNIALAHGGTISAEhSPLG-GLRLVLTLP 109
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
323-430 2.29e-19

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: 83.24  E-value: 2.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 323 PSRLSQVLFNLIGNAVK-FTQQGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFkqadsSITRKFG-GTGLGLAI 400
Cdd:cd16943    1 PSQLNQVLLNLLVNAAQaMEGRGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPF-----FTTKPVGeGTGLGLSL 75
                         90       100       110
                 ....*....|....*....|....*....|
gi 503337118 401 TKHLVELMSGTVRVSSQFGKGSTFVVKIPV 430
Cdd:cd16943   76 SYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
PRK10604 PRK10604
sensor protein RstB; Provisional
218-432 2.66e-19

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 90.43  E-value: 2.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 218 SHELRTPLNSV---LGMLDVLKQSDMSAghinllshMESSAGLLLAIISDILDLSKIESGEFSLSPQWININDTVTFVVS 294
Cdd:PRK10604 220 AHELRTPLVRLryrLEMSDNLSAAESQA--------LNRDIGQLEALIEELLTYARLDRPQNELHLSEPDLPAWLSTHLA 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 295 QQQLVAATKglniELSIELDDKRHYW-LDPSRLSQVLFNLIGNAVKFTQQgQIDIRVNLENDELSISVIDTGIGIEKDKI 373
Cdd:PRK10604 292 DIQAVTPEK----TVRLDTPHQGDYGaLDMRLMERVLDNLLNNALRYAHS-RVRVSLLLDGNQACLIVEDDGPGIPPEER 366
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 503337118 374 SSLFTAFKQADSSITRKFGGTGLGLAITKHLVELMSGTVRVSSQFGKGSTFVVKIPVKS 432
Cdd:PRK10604 367 ERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSFSWPVWH 425
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
453-555 4.17e-18

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: 79.85  E-value: 4.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRA--KGFEVPIIAL 530
Cdd:cd17538    2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEE--ELPDLILLDVMMPGMDGFEVCRRLKEdpETRHIPVIMI 79
                         90       100
                 ....*....|....*....|....*
gi 503337118 531 TAHALASDKQNCLDVGMDSFVAKPV 555
Cdd:cd17538   80 TALDDREDRIRGLEAGADDFLSKPI 104
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
332-429 4.71e-18

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: 79.94  E-value: 4.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 332 NLIGNAVKFT-QQGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFKQADSSITRKFGGTGLGLAITKHLVELMSG 410
Cdd:cd16952    7 NLVSNAVKYTpPSDTITVRWSQEESGARLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAIVKHVMSRHDA 86
                         90
                 ....*....|....*....
gi 503337118 411 TVRVSSQFGKGSTFVVKIP 429
Cdd:cd16952   87 RLLIASELGKGSRFTCLFP 105
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
453-568 8.20e-18

phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The Mycobacterium tuberculosis PrrA is part of the PrrA/PrrB two-component system (TCS) that has been implicated in early intracellular multiplication and is essential for viability. Also included in this subfamily is Mycobacterium tuberculosis MprA, part of the MprAB TCS that regulates EspR, a key regulator of the ESX-1 secretion system, and is required for establishment and maintenance of persistent infection in a tissue- and stage-specific fashion. PrrA and MprA belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 79.35  E-value: 8.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTesLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNR--PDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTA 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 533 HALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:cd17627   79 RDSVSDRVAGLDAGADDYLVKPFALEELLARVRALL 114
PRK09303 PRK09303
histidine kinase;
208-430 2.80e-17

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 83.85  E-value: 2.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 208 RAKSEFLAMMSHELRTPLNSVLGMLDVLKQ-------SDMSAGHINLLSHMESSAGLLLAIISDILDLSKIESGEFSLSP 280
Cdd:PRK09303 149 KFKDRVLAMLAHDLRTPLTAASLALETLELgqidedtELKPALIEQLQDQARRQLEEIERLITDLLEVGRTRWEALRFNP 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 281 QWININDTVTFVVSQQQLVAATKGLNIELSIELDDKRHYwLDPSRLSQVLFNLIGNAVKFTQQGQIdIRVNL---ENDEL 357
Cdd:PRK09303 229 QKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSDLPSVY-ADQERIRQVLLNLLDNAIKYTPEGGT-ITLSMlhrTTQKV 306
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503337118 358 SISVIDTGIGIEKDKISSLFT-AFK-QADSSITrkfgGTGLGLAITKHLVELMSGTVRVSSQFGKGSTFVVKIPV 430
Cdd:PRK09303 307 QVSICDTGPGIPEEEQERIFEdRVRlPRDEGTE----GYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFTLPV 377
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
453-568 2.90e-17

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 77.71  E-value: 2.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAieFIESNTESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEA--LFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTA 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 533 HALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:cd19934   79 RDSWQDKVEGLDAGADDYLTKPFHIEELLARLRALI 114
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
218-434 4.65e-17

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 83.83  E-value: 4.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 218 SHELRTPLNSvLGMLDVL---KQsdmsaGHINLLSHMESSAGLLLAIISDILDLSK------IESGEFSLSPQWININDT 288
Cdd:PRK09470 251 SHELRTPLTR-LQLATALlrrRQ-----GESKELERIETEAQRLDSMINDLLVLSRnqqknhLERETFKANSLWSEVLED 324
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 289 VTFVVSQqqlvaatkgLNIELSIELDDKRHYWL-DPSRLSQVLFNLIGNAVKFTQQgQIDIRVNLENDELSISVIDTGIG 367
Cdd:PRK09470 325 AKFEAEQ---------MGKSLTVSAPPGPWPINgNPNALASALENIVRNALRYSHT-KIEVAFSVDKDGLTITVDDDGPG 394
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503337118 368 IEKDKISSLFTAFKQADSSITRKFGGTGLGLAITKHLVELMSGTVRVS-SQFGkGSTFVVKIPVKSRK 434
Cdd:PRK09470 395 VPEEEREQIFRPFYRVDEARDRESGGTGLGLAIVENAIQQHRGWVKAEdSPLG-GLRLTIWLPLYKRS 461
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
449-568 7.20e-17

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: 79.23  E-value: 7.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 449 RALNVLVVEDTHSNQMVIQLLLNKLGHNVF-IANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKGfEVPI 527
Cdd:COG3707    2 RGLRVLVVDDEPLRRADLREGLREAGYEVVaEAADGEDAVELVRE--LKPDLVIVDIDMPDRDGLEAARQISEER-PAPV 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 503337118 528 IALTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:COG3707   79 ILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELAL 119
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
452-565 7.27e-17

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: 76.68  E-value: 7.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 452 NVLVVEDTHSNQMVIQLLLNKLGHNVF-IANNGSEAIEFIESNTEslDVVFMDVSMP-VMDGLTATKILRAKgFEVPIIA 529
Cdd:cd17534    2 KILIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEENKP--DLILMDINLKgDMDGIEAAREIREK-FDIPVIF 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 530 LTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIE 565
Cdd:cd17534   79 LTAYSDEETLERAKETNPYGYLVKPFNERELKAAIE 114
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
453-566 7.74e-17

phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators; The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 76.40  E-value: 7.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGH--NVFIANNGSEAIEFIEsnTESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIAL 530
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLESEPDieVVGEAADGEEALALLR--ELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVL 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 531 TAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEA 566
Cdd:cd17535   79 TAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRA 114
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
320-421 1.07e-16

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


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 75.91  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 320 WLDPSRLSQVLFNLIGNAVKFTQQG-QIDIRVNlENDELSISVIDTGIGIEKDKISSLFTAFKQADSSITrkfGGTGLGL 398
Cdd:cd16940    8 QGDALLLFLLLRNLVDNAVRYSPQGsRVEIKLS-ADDGAVIRVEDNGPGIDEEELEALFERFYRSDGQNY---GGSGLGL 83
                         90       100
                 ....*....|....*....|...
gi 503337118 399 AITKHLVELMSGTVRVSSQFGKG 421
Cdd:cd16940   84 SIVKRIVELHGGQIFLGNAQGGG 106
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
326-429 1.16e-16

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: 75.83  E-value: 1.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 326 LSQVLFNLIGNAVKFTQQgQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFKQADSSITRKFGGTGLGLAITKHLV 405
Cdd:cd16949    1 LARALENVLRNALRYSPS-KILLDISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAIAERAI 79
                         90       100
                 ....*....|....*....|....
gi 503337118 406 ELMSGTVRVSSQFGKGSTFVVKIP 429
Cdd:cd16949   80 EQHGGKIKASNRKPGGLRVRIWLP 103
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
162-433 1.19e-16

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 82.20  E-value: 1.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 162 KETLKRFLPLIERAVIDIENKEKLQRIVELRTRELALAREESERANRAKSEFLAMMSHELRTPLNSVLGMLDvLKQSDMS 241
Cdd:COG3290  141 EEILLNGRVLVVNRVPIRDDGRVVGAVATFRDRTELERLEEELEGVKELAEALRAQRHDFRNHLHTISGLLQ-LGEYDEA 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 242 AGHIN-LLSHMESSAGLLLAIISD-ILD---LSKIEsgefslspqwinindtvtfvvsqqqlVAATKGlnIELSIELDDK 316
Cdd:COG3290  220 LEYIDeISEELQELIDSLLSRIGNpVLAallLGKAA--------------------------RARERG--IDLTIDIDSD 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 317 -RHYWLDPSRLSQVLFNLIGNAV-----KFTQQGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTafkqaDSSITRK 390
Cdd:COG3290  272 lPDLPLSDTDLVTILGNLLDNAIeavekLPEEERRVELSIRDDGDELVIEVEDSGPGIPEELLEKIFE-----RGFSTKL 346
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 503337118 391 FGGTGLGLAITKHLVELMSGTVRVSSQFGKGSTFVVKIPVKSR 433
Cdd:COG3290  347 GEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKEGE 389
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
453-568 1.22e-16

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: 76.22  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDthsNQMV---IQLLLNKLGHN---VFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKGFEVP 526
Cdd:cd17536    1 VLIVDD---EPLIregLKKLIDWEELGfevVGEAENGEEALELIEE--HKPDIVITDIRMPGMDGLELIEKIRELYPDIK 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 503337118 527 IIALTAHalaSDK---QNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:cd17536   76 IIILSGY---DDFeyaQKAIRLGVVDYLLKPVDEEELEEALEKAK 117
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
453-568 1.24e-16

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


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 75.98  E-value: 1.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDthsNQMV---IQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIA 529
Cdd:cd17624    1 ILLVED---DALLgdgLKTGLRKAGYAVDWVRTGAEAEAALAS--GPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLI 75
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 503337118 530 LTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:cd17624   76 LTARDGVDDRVAGLDAGADDYLVKPFALEELLARLRALL 114
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
453-568 2.07e-16

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: 75.15  E-value: 2.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIEsnTESLDVVFMDVSMPVMDGLTATKILRAKgFEVPIIALTA 532
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVE--EEQPDLILLDLMLPEKDGLEVCREVRKT-SNVPIIMLTA 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 533 HALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:cd17614   78 KDSEVDKVLGLELGADDYVTKPFSNRELLARVKANL 113
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
326-429 2.60e-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: 74.74  E-value: 2.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 326 LSQVLFNLIGNAVKFTQQG-----QIDIRVNL-ENDELSISVIDTGIGIEKDKISSLFTAFkqadssITRKFGGTGLGLA 399
Cdd:cd16920    1 IQQVLINLVRNGIEAMSEGgcerrELTIRTSPaDDRAVTISVKDTGPGIAEEVAGQLFDPF------YTTKSEGLGMGLS 74
                         90       100       110
                 ....*....|....*....|....*....|
gi 503337118 400 ITKHLVELMSGTVRVSSQFGKGSTFVVKIP 429
Cdd:cd16920   75 ICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
209-274 3.19e-16

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 72.98  E-value: 3.19e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503337118   209 AKSEFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHINLLSHMESSAGLLLAIISDILDLSKIESG 274
Cdd:smart00388   1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
190-432 6.22e-16

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 80.27  E-value: 6.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 190 ELRTRELA-LARE-ESER---ANRAKSE-FLAMMSHELRTPLNSVLGMLDVLkQSDMSAG-HINLLSHMESSAGLLLAII 262
Cdd:PRK11100 230 KLGSSELReLAQAlESMRvklEGKAYVEqYVQTLTHELKSPLAAIRGAAELL-QEDPPPEdRARFTGNILTQSARLQQLI 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 263 SDILDLSKIESGEFSLSPQWININDTVTFVVSQQQLVAATKGLNIELSIelDDKRHYWlDPSRLSQVLFNLIGNAVKFT- 341
Cdd:PRK11100 309 DRLLELARLEQRQELEVLEPVALAALLEELVEAREAQAAAKGITLRLRP--DDARVLG-DPFLLRQALGNLLDNAIDFSp 385
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 342 QQGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFkqadSSITRKFGG---TGLGLAITKHLVELMSGTVRVSSQF 418
Cdd:PRK11100 386 EGGTITLSAEVDGEQVALSVEDQGPGIPDYALPRIFERF----YSLPRPANGrksTGLGLAFVREVARLHGGEVTLRNRP 461
                        250
                 ....*....|....
gi 503337118 419 GKGSTFVVKIPVKS 432
Cdd:PRK11100 462 EGGVLATLTLPRHF 475
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
453-555 7.54e-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: 73.31  E-value: 7.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRA--KGFEVPIIAL 530
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQA--EPPDLILLDVMMPGMDGFEVCRRLKAdpATRHIPVIFL 78
                         90       100
                 ....*....|....*....|....*
gi 503337118 531 TAHALASDKQNCLDVGMDSFVAKPV 555
Cdd:cd19920   79 TALTDTEDKVKGFELGAVDYITKPF 103
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
308-428 9.49e-16

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


Pssm-ID: 340423 [Multi-domain]  Cd Length: 125  Bit Score: 73.70  E-value: 9.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 308 ELSIELDDKRHYWL-DPSRLSQVLFNLIGNAVKFTQQGQIdIRVNLENDE--LSISVIDTGIGIEKDKISSLFTAFKQAD 384
Cdd:cd16947    2 QVEINIPDRPIYANaNTEALQRILKNLISNAIKYGSDGKF-LGMTLREDEkhVYIDIWDKGKGISETEKDHVFERLYTLE 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 503337118 385 SSITRKFGGTGLGLAITKHLVELMSGTVRVSSQFGKGSTFVVKI 428
Cdd:cd16947   81 DSRNSAKQGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
451-564 1.39e-15

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


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 73.20  E-value: 1.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 451 LNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTESLDVVFMDVSMPVMDGL-TATKILRAKGFEVP--I 527
Cdd:cd19933    1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHSFQLVLLDLCMPEMDGFeVALRIRKLFGRRERplI 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 503337118 528 IALTAHALASDKQNCLDVGMDSFVAKPVRKQELANAI 564
Cdd:cd19933   81 VALTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
453-567 3.73e-15

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: 71.81  E-value: 3.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKL-GHNVFIANNGSEAIEFIEsnTESLDVVFMDVSMPVMDGLTATKILRAKGF--EVPIIA 529
Cdd:cd17552    4 ILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAA--TEQPDAILLDVMMPDMDGLATLKKLQANPEtqSIPVIL 81
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 503337118 530 LTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEAL 567
Cdd:cd17552   82 LTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKL 119
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
209-274 4.10e-15

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 69.93  E-value: 4.10e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503337118  209 AKSEFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHINLLSHMESSAGLLLAIISDILDLSKIESG 274
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
452-567 4.71e-15

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


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 71.68  E-value: 4.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 452 NVLVVEDTHSNQMVIQLLL--NKLGHNVFIANNGSEAIEFIE-----SNTESLDVVFMDVSMPVMDGLTATKILRA---- 520
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFkeAGVPNELHVVRDGEEALDFLRgegeyADAPRPDLILLDLNMPRMDGFEVLREIKAdpdl 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 503337118 521 KgfEVPIIALTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEAL 567
Cdd:cd17557   81 R--RIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSL 125
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
453-554 6.64e-15

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: 70.55  E-value: 6.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIEsnTESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLAL--TNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTA 78
                         90       100
                 ....*....|....*....|..
gi 503337118 533 HALASDKQNCLDVGMDSFVAKP 554
Cdd:cd19935   79 RDSVEDRVKGLDLGADDYLVKP 100
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
451-565 8.04e-15

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 74.08  E-value: 8.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 451 LNVLVVEDTHSNQMVIQLLLNKLGHN--VFIANNGSEAIEFIESNteSLDVVFMDVSMPVMDGLTATKILRAKGFEVPII 528
Cdd:COG3279    2 MKILIVDDEPLARERLERLLEKYPDLevVGEASNGEEALELLEEH--KPDLVFLDIQMPGLDGFELARQLRELDPPPPII 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 503337118 529 ALTAH---ALASDKQNCLDvgmdsFVAKPVRKQELANAIE 565
Cdd:COG3279   80 FTTAYdeyALEAFEVNAVD-----YLLKPIDEERLAKALE 114
envZ PRK09467
osmolarity sensor protein; Provisional
214-415 2.13e-14

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 75.33  E-value: 2.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 214 LAMMSHELRTPLNsvlgmldvlkqsdmsagHINLLSHMESSAGLLLA--IISDILDLSKIESgEF--------SLSPQWI 283
Cdd:PRK09467 233 MAGVSHDLRTPLT-----------------RIRLATEMMSEEDGYLAesINKDIEECNAIIE-QFidylrtgqEMPMEMA 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 284 NINDTVTFVVSQQqlvaatkgLNIELSIELDDKRH---YWLDPSRLSQVLFNLIGNAVKFTQqGQIDIRVNLENDELSIS 360
Cdd:PRK09467 295 DLNALLGEVIAAE--------SGYEREIETALQPGpieVPMNPIAIKRALANLVVNAARYGN-GWIKVSSGTEGKRAWFQ 365
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 503337118 361 VIDTGIGIEKDKISSLFTAFKQADSSitRKFGGTGLGLAITKHLVELMSGTVRVS 415
Cdd:PRK09467 366 VEDDGPGIPPEQLKHLFQPFTRGDSA--RGSSGTGLGLAIVKRIVDQHNGKVELG 418
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
453-565 2.97e-14

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: 69.53  E-value: 2.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNteSLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQ--PPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITA 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 503337118 533 HAlasdkqnCLDVGMDS-------FVAKPVRKQEL----ANAIE 565
Cdd:cd17572   79 HG-------SVDIAVEAmrlgaydFLEKPFDADRLrvtvRNALK 115
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
465-567 3.59e-14

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


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 69.10  E-value: 3.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 465 VIQLLLNKLGHNVFIANNGSEAIEFIESNteSLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTAHALASDKQNCLD 544
Cdd:cd17593   16 LARALPADWDVEITFAENGEEALEILREG--RIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVSGDVQPEAKERVLE 93
                         90       100
                 ....*....|....*....|...
gi 503337118 545 VGMDSFVAKPVRKQELANAIEAL 567
Cdd:cd17593   94 LGALAFLKKPFDPEKLAQLLEEL 116
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
210-429 5.14e-14

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 74.42  E-value: 5.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 210 KSEFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHIN--LLSHMESsAGLLLAIISDILDLSKIESGEFSLSPQWININD 287
Cdd:PRK09835 262 QSNFSADIAHEIRTPITNLITQTEIALSQSRSQKELEdvLYSNLEE-LTRMAKMVSDMLFLAQADNNQLIPEKKMLDLAD 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 288 TVTFVVSQQQLVAATKglniELSIELDDKRHY-WLDPSRLSQVLFNLIGNAVKFTQQGQ-IDIRVNLENDELSISVIDTG 365
Cdd:PRK09835 341 EVGKVFDFFEAWAEER----GVELRFVGDPCQvAGDPLMLRRAISNLLSNALRYTPAGEaITVRCQEVDHQVQLVVENPG 416
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503337118 366 IGIEKDKISSLFTAFKQADSSITRKFGGTGLGLAITKHLVELMSGTVRVSSQFgKGSTFVVKIP 429
Cdd:PRK09835 417 TPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRFVISLP 479
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
452-568 6.85e-14

phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate methylesterase CheB and similar chemotaxis proteins; Methylesterase CheB is a chemotaxis response regulator with an N-terminal REC domain and a C-terminal methylesterase domain. Chemotaxis is a behavior known in motile bacteria that directs their movement in response to chemical gradients. CheB is a phosphorylation-activated response regulator involved in the reversible modification of bacterial chemotaxis receptors. It catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. The CheB REC domain packs against the active site of the C-terminal domain and inhibits methylesterase activity by directly restricting access to the active site. Also included in this family is chemotaxis response regulator CheY, which contains a stand-alone REC domain, and an uncharacterized subfamily composed of proteins containing an N-terminal REC domain and a C-terminal CheY-P phosphatase (CheC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 68.57  E-value: 6.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 452 NVLVVEDTHSNQMVIQLLLNKLGH--NVFIANNGSEAIEFIESNTEslDVVFMDVSMPVMDGLTATKILRAKgFEVPIIA 529
Cdd:cd17541    2 RVLIVDDSAVMRKLLSRILESDPDieVVGTARDGEEALEKIKELKP--DVITLDIEMPVMDGLEALRRIMAE-RPTPVVM 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 503337118 530 LTAHALASDKQ--NCLDVGMDSFVAKPV--RKQELANAIEALI 568
Cdd:cd17541   79 VSSLTEEGAEItlEALELGAVDFIAKPSggISLDLEEIAEELI 121
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
452-560 2.07e-13

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: 66.70  E-value: 2.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 452 NVLVVEDTHSNQMVIQLLLNKLG-HNVFIANNGSEAIEFIESNTesLDVVFMDVSMPVMDGLTATKILRAK--GFEVPII 528
Cdd:cd17551    2 RILIVDDNPTNLLLLEALLRSAGyLEVVSFTDPREALAWCRENP--PDLILLDYMMPGMDGLEFIRRLRALpgLEDVPIV 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 503337118 529 ALTAHALASDKQNCLDVGMDSFVAKPVRKQEL 560
Cdd:cd17551   80 MITADTDREVRLRALEAGATDFLTKPFDPVEL 111
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
454-568 2.72e-13

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: 66.53  E-value: 2.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 454 LVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNteSLDVVFMDVSMPVMDGLTATKILR--AKGFEVPIIALT 531
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDE--KPDLIILDLMLPGIDGLEVCRILRsdPKTSSIPIIMLT 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 503337118 532 AHALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:cd19937   79 AKGEEFDKVLGLELGADDYITKPFSPRELLARVKAVL 115
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
452-567 2.86e-13

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


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 66.50  E-value: 2.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 452 NVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIEsnTESLDVVFMDVSMPVMDGLTATKILR--AKGFEVPIIA 529
Cdd:cd17618    2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIV--EPRPDLILLDWMLPGGSGIQFIRRLKrdEMTRDIPIIM 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 503337118 530 LTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEAL 567
Cdd:cd17618   80 LTARGEEEDKVRGLEAGADDYITKPFSPRELVARIKAV 117
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
326-430 3.05e-13

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


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 65.91  E-value: 3.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 326 LSQVLFNLIGNAVKFTQQgQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFKQADSSITRKFGGTGLGLAITKHLV 405
Cdd:cd16939    1 MARALDNLLRNALRYAHR-TVRIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAIVHRVA 79
                         90       100
                 ....*....|....*....|....*.
gi 503337118 406 ELMSGTVRV-SSQFGkGSTFVVKIPV 430
Cdd:cd16939   80 LWHGGHVECdDSELG-GACFRLTWPR 104
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
453-568 3.30e-13

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: 66.22  E-value: 3.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTEslDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:cd17615    2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRP--DAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTA 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 533 HALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:cd17615   80 KDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALL 115
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
207-270 3.38e-13

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


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 64.54  E-value: 3.38e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503337118 207 NRAKSEFLAMMSHELRTPLNSVLGMLDVLKQS-DMSAGHINLLSHMESSAGLLLAIISDILDLSK 270
Cdd:cd00082    1 LQAKGEFLANVSHELRTPLTAIRGALELLEEElLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
326-429 3.62e-13

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: 65.49  E-value: 3.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 326 LSQVLFNLIGNAVKFT-QQGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFKQADSSitRKFGGTGLGLAITKHL 404
Cdd:cd16923    1 LQRVFSNLLSNAIKYSpENTRIYITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNS--RNTEGAGLGLSIAKAI 78
                         90       100
                 ....*....|....*....|....*
gi 503337118 405 VELMSGTVRVSSQfGKGSTFVVKIP 429
Cdd:cd16923   79 IELHGGSASAEYD-DNHDLFKVRLP 102
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
326-421 4.35e-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: 65.55  E-value: 4.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 326 LSQVLFNLIGNAVKFTQqGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFKQADSSitRKFGGTGLGLAITKHLV 405
Cdd:cd16950    1 LKRVLSNLVDNALRYGG-GWVEVSSDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNA--RGTSGTGLGLAIVQRIS 77
                         90
                 ....*....|....*.
gi 503337118 406 ELMSGTVRVSSQFGKG 421
Cdd:cd16950   78 DAHGGSLTLANRAGGG 93
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
453-554 5.07e-13

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: 65.26  E-value: 5.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIefIESNTESLDVVFMDVSMPVMDGLTATKILRaKGFEVPIIALTA 532
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGL--LEAATRKPDLIILDLGLPDMDGLEVIRRLR-EWSAVPVIVLSA 77
                         90       100
                 ....*....|....*....|..
gi 503337118 533 HALASDKQNCLDVGMDSFVAKP 554
Cdd:cd17620   78 RDEESDKIAALDAGADDYLTKP 99
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
453-569 5.90e-13

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: 65.42  E-value: 5.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTESLdvVFMDVSMPVMDGLTATKILRA-KGF-EVPIIAL 530
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTL--VISDIVMPEMDGYELCRKIKSdPDLkDIPVILL 78
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 503337118 531 TAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEALIV 569
Cdd:cd17598   79 TTLSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYILV 117
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
191-429 6.02e-13

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 71.89  E-value: 6.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 191 LRTRELALAREESERANRAKSEFLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHINLLSHMESSAGLLLAIISDILDLSK 270
Cdd:PRK10618 431 LVNKKLQQAQREYEKNQQARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNM 510
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 271 IESGEFSLSPQWININDTVTFVVSQQQLVAATKGLNIELSIELDDKRHYWLDPSRLSQVLFNLIGNAVKFTQQGQIDIRV 350
Cdd:PRK10618 511 LETQDWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYGKITLEV 590
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 351 NLEN---DELSISVIDTGIGIEKDKISSL---FTAFKQADssitrKFG-GTGLGLAITKHLVELMSGTVRVSSQFGKGST 423
Cdd:PRK10618 591 DQDEsspDRLTIRILDTGAGVSIKELDNLhfpFLNQTQGD-----RYGkASGLTFFLCNQLCRKLGGHLTIKSREGLGTR 665

                 ....*.
gi 503337118 424 FVVKIP 429
Cdd:PRK10618 666 YSIHLK 671
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
451-565 9.64e-13

phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes Mycobacterium tuberculosis PdtaR, also called Rv1626, and similar proteins containing a REC domain and an ANTAR (AmiR and NasR transcription antitermination regulators) RNA-binding output domain. PdtaR is a response regulator that acts at the level of transcriptional antitermination and is a member of the PdtaR/PdtaS two-component regulatory system. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 65.13  E-value: 9.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 451 LNVLVVEDTHSNQMVIQLLLNKLGHNVFI-ANNGSEAIEFIEsnTESLDVVFMDVSMPVMDGLTATKILRAKGFeVPIIA 529
Cdd:cd19932    1 VRVLIAEDEALIRMDLREMLEEAGYEVVGeASDGEEAVELAK--KHKPDLVIMDVKMPRLDGIEAAKIITSENI-APIVL 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 530 LTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIE 565
Cdd:cd19932   78 LTAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIE 113
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
453-562 1.48e-12

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: 64.19  E-value: 1.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTESLDVVFMDVSMPVMDGLTATKILRaKGFEVPIIALTA 532
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDEFDLVITDVHMPDMDGFEFLELIR-LEMDLPVIMMSA 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 503337118 533 HALASDKQNCLDVGMDSFVAKPVRKQELAN 562
Cdd:cd17584   80 DGSTSTVMKGLAHGACDYLLKPVSIEDLKN 109
orf27 CHL00148
Ycf27; Reviewed
453-568 2.09e-12

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 67.05  E-value: 2.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIEsnTESLDVVFMDVSMPVMDGLTATKILRAKGfEVPIIALTA 532
Cdd:CHL00148   9 ILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFR--KEQPDLVILDVMMPKLDGYGVCQEIRKES-DVPIIMLTA 85
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 533 HALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:CHL00148  86 LGDVSDRITGLELGADDYVVKPFSPKELEARIRSVL 121
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
452-532 2.13e-12

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains; Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 63.78  E-value: 2.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 452 NVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALT 531
Cdd:cd17554    2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLES--EDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICT 79

                 .
gi 503337118 532 A 532
Cdd:cd17554   80 A 80
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
452-565 2.43e-12

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


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 63.84  E-value: 2.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 452 NVLVVEDTHSNQMVIQLLLNKLGHNVFI-ANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIAL 530
Cdd:cd17542    2 KVLIVDDAAFMRMMLKDILTKAGYEVVGeAANGEEAVEKYKE--LKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMC 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 503337118 531 TA---HALASDkqnCLDVGMDSFVAKPVRKQELANAIE 565
Cdd:cd17542   80 SAmgqEEMVKE---AIKAGAKDFIVKPFQPERVLEAVE 114
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
453-568 2.71e-12

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 66.75  E-value: 2.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESnteSLDVVFMDVSMPVMDGLTATKILRaKGFEVPIIALTA 532
Cdd:PRK10955   4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDD---SIDLLLLDVMMPKKNGIDTLKELR-QTHQTPVIMLTA 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 533 HALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:PRK10955  80 RGSELDRVLGLELGADDYLPKPFNDRELVARIRAIL 115
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
452-560 2.91e-12

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 63.56  E-value: 2.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 452 NVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKGfEVPIIALT 531
Cdd:cd17619    2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILAR--QDIDLVLLDINLPGKDGLSLTRELREQS-EVGIILVT 78
                         90       100
                 ....*....|....*....|....*....
gi 503337118 532 AHALASDKQNCLDVGMDSFVAKPVRKQEL 560
Cdd:cd17619   79 GRDDEVDRIVGLEIGADDYVTKPFNPREL 107
PRK10643 PRK10643
two-component system response regulator PmrA;
453-568 3.19e-12

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 66.21  E-value: 3.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTESLdvVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:PRK10643   3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSL--VVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTA 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 533 HALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:PRK10643  81 RDTLEDRVAGLDVGADDYLVKPFALEELHARIRALI 116
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
453-560 3.38e-12

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 68.72  E-value: 3.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIE-FIESNTeslDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALT 531
Cdd:PRK11361   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHlFADIHP---DVVLMDIRMPEMDGIKALKEMRSHETRTPVILMT 83
                         90       100
                 ....*....|....*....|....*....
gi 503337118 532 AHALASDKQNCLDVGMDSFVAKPVRKQEL 560
Cdd:PRK11361  84 AYAEVETAVEALRCGAFDYVIKPFDLDEL 112
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
326-426 6.71e-12

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


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 62.09  E-value: 6.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 326 LSQVLFNLIGNA---VKFTQQGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFkqadsSITRKFG-GTGLGLAIT 401
Cdd:cd16976    1 IQQVLMNLLQNAldaMGKVENPRIRIAARRLGGRLVLVVRDNGPGIAEEHLSRVFDPF-----FTTKPVGkGTGLGLSIS 75
                         90       100
                 ....*....|....*....|....*
gi 503337118 402 KHLVELMSGTVRVSSQFGKGSTFVV 426
Cdd:cd16976   76 YGIVEEHGGRLSVANEEGAGARFTF 100
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
453-568 7.12e-12

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: 62.43  E-value: 7.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFieSNTESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDL--GKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSG 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 533 HALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:cd17616   79 LADIEDKVKGLGFGADDYMTKPFHKDELVARIHAIV 114
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
453-568 9.51e-12

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


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 62.01  E-value: 9.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIesNTESLDVVFMDVSMPVMDGLTATKILRAKgFEVPIIALTA 532
Cdd:cd19939    2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRI--IDEQPSLVVLDIMLPGMDGLTVCREVREH-SHVPILMLTA 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 533 HALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:cd19939   79 RTEEMDRVLGLEMGADDYLCKPFSPRELLARVRALL 114
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
453-554 1.08e-11

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 61.45  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNteSLDVVFMDVSMPVMDGLTATKILRAKGfEVPIIALTA 532
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRA--GADIVLLDLMLPGLSGTEVCRQLRARS-NVPVIMVTA 77
                         90       100
                 ....*....|....*....|..
gi 503337118 533 HALASDKQNCLDVGMDSFVAKP 554
Cdd:cd17621   78 KDSEIDKVVGLELGADDYVTKP 99
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
453-534 1.46e-11

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


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 61.36  E-value: 1.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKE--RRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISG 78

                 ..
gi 503337118 533 HA 534
Cdd:cd17550   79 HG 80
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
453-568 1.60e-11

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: 61.55  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEfiESNTESLDVVFMDVSMPVMDGLTATKILRAK-GFE-VPIIAL 530
Cdd:cd17562    3 ILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALS--KAQSKKFDLIITDQNMPNMDGIELIKELRKLpAYKfTPILML 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 503337118 531 TAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:cd17562   81 TTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
326-429 1.83e-11

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: 61.05  E-value: 1.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 326 LSQVLFNLIGNAVKFT--QQGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFkQADSSITRKFG-GTGLGLAITK 402
Cdd:cd16953    1 LGQVLRNLIGNAISFSppDTGRITVSAMPTGKMVTISVEDEGPGIPQEKLESIFDRF-YTERPANEAFGqHSGLGLSISR 79
                         90       100       110
                 ....*....|....*....|....*....|.
gi 503337118 403 HLVELMSGTV----RVSSQFGKGSTFVVKIP 429
Cdd:cd16953   80 QIIEAHGGISvaenHNQPGQVIGARFTVQLP 110
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
453-566 1.96e-11

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: 61.33  E-value: 1.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEfiESNTESLDVVFMDVSMPVMDGLTATKILRAKGfEVPIIALTA 532
Cdd:cd17626    3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALA--AFREVRPDLVLLDLMLPGIDGIEVCRQIRAES-GVPIVMLTA 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 503337118 533 HALASDKQNCLDVGMDSFVAKPVRKQELANAIEA 566
Cdd:cd17626   80 KSDTVDVVLGLESGADDYVAKPFKPKELVARIRA 113
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
453-568 2.44e-11

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: 60.78  E-value: 2.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEfiESNTESLDVVFMDVSMPVMDGLTATKILRaKGFEVPIIALTA 532
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLA--ALLEGSPDLVVLDVMLPKMNGLDVLKELR-KTSQVPVLMLTA 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 533 HALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:cd17623   78 RGDDIDRILGLELGADDYLPKPFNPRELVARIRAIL 113
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
326-429 3.40e-11

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


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 60.38  E-value: 3.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 326 LSQVLFNLIGNAVKFTQQ-GQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFkqADSSITRKFG-GTGLGLAITKH 403
Cdd:cd16948    6 LSFIIGQIVSNALKYSKQgGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKG--FTGENGRNFQeSTGMGLYLVKK 83
                         90       100
                 ....*....|....*....|....*.
gi 503337118 404 LVELMSGTVRVSSQFGKGSTFVVKIP 429
Cdd:cd16948   84 LCDKLGHKIDVESEVGEGTTFTITFP 109
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
453-554 3.73e-11

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: 60.08  E-value: 3.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESN-------TESLDVVFMDVSMPVMDGLTATKILRA--KGF 523
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLakegndlSKELDLIITDIEMPKMDGYELTFELRDdpRLA 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 503337118 524 EVPIIALTAHALASDKQNCLDVGMDSFVAKP 554
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
453-554 3.93e-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: 59.70  E-value: 3.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIesNTESLDVVFMDVSMPVMDGLTATKILR--AKGFEVPIIAL 530
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLL--NQYIPDLIISDIIMPGVDGYSLLGKLRknADFDTIPVIFL 78
                         90       100
                 ....*....|....*....|....
gi 503337118 531 TAHALASDKQNCLDVGMDSFVAKP 554
Cdd:cd19927   79 TAKGMTSDRIKGYNAGCDGYLSKP 102
PRK10816 PRK10816
two-component system response regulator PhoP;
451-568 4.55e-11

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 62.83  E-value: 4.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 451 LNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTEslDVVFMDVSMPVMDGLTATKILRAKGFEVPIIAL 530
Cdd:PRK10816   1 MRVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLP--DIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVL 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 503337118 531 TAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:PRK10816  79 TARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALM 116
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
329-433 4.66e-11

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 65.32  E-value: 4.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 329 VLFNLIGN---AVKFTQQGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTafkQADSSitrKFGGTGLGLAITKHLV 405
Cdd:PRK11086 437 ILGNLIENaleAVGGEEGGEISVSLHYRNGWLHCEVSDDGPGIAPDEIDAIFD---KGYST---KGSNRGVGLYLVKQSV 510
                         90       100
                 ....*....|....*....|....*...
gi 503337118 406 ELMSGTVRVSSQFGKGSTFVVKIPVKSR 433
Cdd:PRK11086 511 ENLGGSIAVESEPGVGTQFFVQIPWDGE 538
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
453-564 4.89e-11

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: 59.98  E-value: 4.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHsnqMVIQLL--LNKLGHNVFI---ANNGSEAIEFIEsnTESLDVVFMDVSMPVMDGLTATKILRAKGFEVPI 527
Cdd:cd19930    1 VLIAEDQE---MVRGALaaLLELEDDLEVvaqASNGQEALRLVL--KHSPDVAILDIEMPGRTGLEVAAELREELPDTKV 75
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 503337118 528 IALTAHALASDKQNCLDVGMDSFVAKPVRKQELANAI 564
Cdd:cd19930   76 LIVTTFGRPGYFRRALAAGVDGYVLKDRPIEELADAI 112
PRK15479 PRK15479
transcriptional regulator TctD;
451-568 5.20e-11

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 62.43  E-value: 5.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 451 LNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIEsnTESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIAL 530
Cdd:PRK15479   1 MRLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQ--SEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLL 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 503337118 531 TAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:PRK15479  79 TARSAVADRVKGLNVGADDYLPKPFELEELDARLRALL 116
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
451-565 6.63e-11

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: 59.66  E-value: 6.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 451 LNVLVVEDTHSNQMVIQLLLNKLGH-NVFIANNGSEAIEFIESNteSLDVVFMDVSMPVMDGLTATKILRAKG--FEVPI 527
Cdd:cd19923    1 MKVLVVDDFSTMRRIIKNLLKELGFnNVEEAEDGVDALEKLKAG--GFDFVITDWNMPNMDGLELLKTIRADGalSHLPV 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 503337118 528 IALTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIE 565
Cdd:cd19923   79 LMVTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLE 116
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
326-429 1.02e-10

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


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 58.95  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 326 LSQVLFNLIGNAVKFT--QQGQIDIRVNLEND----------ELSISVIDTGIGIEKDKISSLFTAFkqadssITRKFGG 393
Cdd:cd16918    1 LIQVFLNLVRNAAQALagSGGEIILRTRTQRQvtlghprhrlALRVSVIDNGPGIPPDLQDTIFYPM------VSGRENG 74
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 394 TGLGLAITKHLVELMSGTVRVSSQFGKgSTFVVKIP 429
Cdd:cd16918   75 TGLGLAIAQNIVSQHGGVIECDSQPGH-TVFSVSLP 109
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
451-565 1.28e-10

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 63.51  E-value: 1.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 451 LNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTesLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIAL 530
Cdd:PRK10365   6 IDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQV--FDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIM 83
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 503337118 531 TAHALASDKQNCLDVGMDSFVAKPVRKQELANAIE 565
Cdd:PRK10365  84 TAYSSVETAVEALKTGALDYLIKPLDFDNLQATLE 118
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
213-410 2.50e-10

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 62.29  E-value: 2.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 213 FLAMMSHELRTPLNSVLGMLDVLKQSdmsaGHIN---LLSHMESsaglLLAIISDILDLSKIESGEFSLSPQWININDTV 289
Cdd:PRK10755 140 FTADVAHELRTPLAGIRLHLELLEKQ----HHIDvapLIARLDQ----MMHTVEQLLQLARAGQSFSSGHYQTVKLLEDV 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 290 tFVVSQQQL--VAATKGLNIELSIELDDKRHYWlDPSRLSQVLFNLIGNAVKFTQQG-QIDIRVNLENDELSISVIDTGI 366
Cdd:PRK10755 212 -ILPSQDELseMLEQRQQTLLLPESAADITVQG-DATLLRLLLRNLVENAHRYSPEGsTITIKLSQEDGGAVLAVEDEGP 289
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 503337118 367 GIEKDKISSLFTAFKQADSsitrKFGGTGLGLAITKHLVELMSG 410
Cdd:PRK10755 290 GIDESKCGELSKAFVRMDS----RYGGIGLGLSIVSRITQLHHG 329
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
332-429 3.86e-10

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: 56.91  E-value: 3.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 332 NLIGNAV-----KFTQQGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFtafKQADSsiTRKFGGTGLGLAITKHLVE 406
Cdd:cd16915    7 NLIDNALdalaaTGAPNKQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVF---ERGVS--TKGQGERGIGLALVRQSVE 81
                         90       100
                 ....*....|....*....|...
gi 503337118 407 LMSGTVRVSSQFGKGSTFVVKIP 429
Cdd:cd16915   82 RLGGSITVESEPGGGTTFSIRIP 104
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
451-507 4.23e-10

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 55.27  E-value: 4.23e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 503337118   451 LNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTEslDVVFMDVSMP 507
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKP--DLILLDIMMP 55
ompR PRK09468
osmolarity response regulator; Provisional
443-566 4.73e-10

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 59.99  E-value: 4.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 443 TTNKRDRalnVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKG 522
Cdd:PRK09468   1 MMQENYK---ILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTR--ESFHLMVLDLMLPGEDGLSICRRLRSQN 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 503337118 523 FEVPIIALTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEA 566
Cdd:PRK09468  76 NPTPIIMLTAKGEEVDRIVGLEIGADDYLPKPFNPRELLARIRA 119
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
453-554 7.35e-10

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: 56.36  E-value: 7.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNtESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQG-KDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80
                         90       100
                 ....*....|....*....|..
gi 503337118 533 HALASDKQNCLDVGMDSFVAKP 554
Cdd:cd18160   81 GAAAAPELLSDAVGDNATLKKP 102
PRK10610 PRK10610
chemotaxis protein CheY;
448-554 1.00e-09

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 56.52  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 448 DRALNVLVVEDTHSNQMVIQLLLNKLG-HNVFIANNGSEAIEFIESNteSLDVVFMDVSMPVMDGLTATKILRAKG--FE 524
Cdd:PRK10610   3 DKELKFLVVDDFSTMRRIVRNLLKELGfNNVEEAEDGVDALNKLQAG--GFGFVISDWNMPNMDGLELLKTIRADGamSA 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 503337118 525 VPIIALTAHALASDKQNCLDVGMDSFVAKP 554
Cdd:PRK10610  81 LPVLMVTAEAKKENIIAAAQAGASGYVVKP 110
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
453-555 1.12e-09

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: 56.06  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:cd17555    3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRS--EQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSG 80
                         90       100
                 ....*....|....*....|...
gi 503337118 533 HALASDKQNCLDVGMDSFVAKPV 555
Cdd:cd17555   81 AGVMSDAVEALRLGAWDYLTKPI 103
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
453-568 1.15e-09

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 56.06  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTESldVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:cd17537    3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPG--CLVLDVRMPGMSGLELQDELLARGSNIPIIFITG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 503337118 533 H-----ALASDKQNCLDvgmdsFVAKPVRKQELANAIEALI 568
Cdd:cd17537   81 HgdvpmAVEAMKAGAVD-----FLEKPFRDQVLLDAIEQAL 116
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
179-429 1.27e-09

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 60.86  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 179 IENKEKLQRIVELRTR-ELALAREESERANRAKSEFL--AMMS--HELRTPLNSVLGMLDVLKQSDMSAGHINL---LSH 250
Cdd:COG4192  397 IEKTQELETEIEERKRiEKNLRQTQDELIQAAKMAVVgqTMTSlaHELNQPLNAMSMYLFSAKKALEQENYAQLptsLDK 476
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 251 MESSAGLLLAIISDILDLSKieSGEFSLSPQWIN--INDTVTFVVSQQQLVAATKGLNIELSIELDDkrhywldpSRLSQ 328
Cdd:COG4192  477 IEGLIERMDKIIKSLRQFSR--KSDTPLQPVDLRqvIEQAWELVESRAKPQQITLHIPDDLMVQGDQ--------VLLEQ 546
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 329 VLFNLIGNAVK-FTQQGQIDIRVNLENDELSISVIDTGIGIekDKISSLFTAFkqadssITRKFGGTGLGLAITKHLVEL 407
Cdd:COG4192  547 VLVNLLVNALDaVATQPQISVDLLSNAENLRVAISDNGNGW--PLVDKLFTPF------TTTKEVGLGLGLSICRSIMQQ 618
                        250       260
                 ....*....|....*....|..
gi 503337118 408 MSGTVRVSSQFGKGSTFVVKIP 429
Cdd:COG4192  619 FGGDLYLASTLERGAMVILEFN 640
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
453-566 1.30e-09

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


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 57.80  E-value: 1.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTESldVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:COG4566    2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPG--CLLLDVRMPGMSGLELQEELAARGSPLPVIFLTG 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 503337118 533 HAlasdkqnclDVGM----------DsFVAKPVRKQELANAIEA 566
Cdd:COG4566   80 HG---------DVPMavramkagavD-FLEKPFDDQALLDAVRR 113
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
453-566 1.35e-09

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: 55.92  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKGfEVPIIALTA 532
Cdd:cd17594    2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLH--RRVDLVLLDLRLGQESGLDLLRTIRARS-DVPIIIISG 78
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 503337118 533 HAL-ASDKQNCLDVGMDSFVAKPVRKQELANAIEA 566
Cdd:cd17594   79 DRRdEIDRVVGLELGADDYLAKPFGLRELLARVRA 113
pleD PRK09581
response regulator PleD; Reviewed
453-555 1.71e-09

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 60.30  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNqmvIQLLLNKLG---HNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRA--KGFEVPI 527
Cdd:PRK09581   5 ILVVDDIPAN---VKLLEAKLLaeyYTVLTASSGAEAIAICER--EQPDIILLDVMMPGMDGFEVCRRLKSdpATTHIPV 79
                         90       100
                 ....*....|....*....|....*...
gi 503337118 528 IALTAHALASDKQNCLDVGMDSFVAKPV 555
Cdd:PRK09581  80 VMVTALDDPEDRVRGLEAGADDFLTKPI 107
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
453-567 2.21e-09

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 59.39  E-value: 2.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKlgHN----VFIANNGSEAIEFIEsnTESLDVVFMDVSMPVMDGLTAT-KILRAKgfEVPI 527
Cdd:PRK00742   6 VLVVDDSAFMRRLISEILNS--DPdievVGTAPDGLEAREKIK--KLNPDVITLDVEMPVMDGLDALeKIMRLR--PTPV 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503337118 528 I---ALTaHALASDKQNCLDVGMDSFVAKPVR---------KQELANAIEAL 567
Cdd:PRK00742  80 VmvsSLT-ERGAEITLRALELGAVDFVTKPFLgislgmdeyKEELAEKVRAA 130
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
453-568 2.40e-09

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: 55.08  E-value: 2.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTEslDVVFMDVSMPVMDGLTATKILRAKGfEVPIIALTA 532
Cdd:cd19938    2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPP--DLILLDLMLPGTDGLTLCREIRRFS-DVPIIMVTA 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 533 HALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:cd19938   79 RVEEIDRLLGLELGADDYICKPYSPREVVARVKAIL 114
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
322-429 2.77e-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: 2.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 322 DPSRLSQVLFNLIGNAVKFTQ-----QGQIDIRVNLENDE-LSISVIDTGIGIEKDKISSLFtafkqaDSSITRKFGGTG 395
Cdd:cd16944    1 DTTQISQVLTNILKNAAEAIEgrpsdVGEVRIRVEADQDGrIVLIVCDNGKGFPREMRHRAT------EPYVTTRPKGTG 74
                         90       100       110
                 ....*....|....*....|....*....|....
gi 503337118 396 LGLAITKHLVELMSGTVRVSSQFGKGSTFVVKIP 429
Cdd:cd16944   75 LGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
PRK10766 PRK10766
two-component system response regulator TorR;
452-560 3.48e-09

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 57.36  E-value: 3.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 452 NVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEfiESNTESLDVVFMDVSMPVMDGLTATKILRAKGfEVPIIALT 531
Cdd:PRK10766   4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMRE--IMQNQHVDLILLDINLPGEDGLMLTRELRSRS-TVGIILVT 80
                         90       100
                 ....*....|....*....|....*....
gi 503337118 532 AHALASDKQNCLDVGMDSFVAKPVRKQEL 560
Cdd:PRK10766  81 GRTDSIDRIVGLEMGADDYVTKPLELREL 109
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
213-429 4.39e-09

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


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 59.37  E-value: 4.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  213 FLAMMSHELRTPLNSVLGMLDVLKQSDMSAGHINLLSHMESSAGLLLAIISDILDLSKIESGEFSLSPQWININDTVTFV 292
Cdd:TIGR03785 488 MSSRLSHELRTPVAVVRSSLENLELQALEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLSEVLSGC 567
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118  293 VSQQQLVAATKglNIELSIELDDKRhywLD--PSRLSQVLFNLIGNAVKFTQQ-GQIDIRVNLENDELSISVIDTGIGIE 369
Cdd:TIGR03785 568 MQGYQMTYPPQ--RFELNIPETPLV---MRgsPELIAQMLDKLVDNAREFSPEdGLIEVGLSQNKSHALLTVSNEGPPLP 642
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503337118  370 KDKISSLFTAFKQADSSITRKFGGTGLGLAITKHLVELMSGTVRVSSQF-GKGSTFVVKIP 429
Cdd:TIGR03785 643 EDMGEQLFDSMVSVRDQGAQDQPHLGLGLYIVRLIADFHQGRIQAENRQqNDGVVFRISLP 703
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
452-532 5.97e-09

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 57.97  E-value: 5.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 452 NVLVVEDThsnQMVIQLLLNKL----GHNV-FIANNGSEAIEFIESNTEslDVVFMDVSMPVMDGLTAT-KILRAKgfEV 525
Cdd:PRK12555   2 RIGIVNDS---PLAVEALRRALardpDHEVvWVATDGAQAVERCAAQPP--DVILMDLEMPRMDGVEATrRIMAER--PC 74

                 ....*..
gi 503337118 526 PIIALTA 532
Cdd:PRK12555  75 PILIVTS 81
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
453-568 6.33e-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: 53.92  E-value: 6.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKgFEVPIIALTA 532
Cdd:cd17622    3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAR--EKPDAVLLDIMLPGIDGLTLCRDLRPK-YQGPILLLTA 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 533 HALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:cd17622   80 LDSDIDHILGLELGADDYVVKPVEPAVLLARLRALL 115
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
322-414 8.25e-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: 53.23  E-value: 8.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 322 DPSRLSQVLFNLIGNAVKFTQQ-GQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFkqadSSITRKFGG---TGLG 397
Cdd:cd16945    1 DPFLLRQAINNLLDNAIDFSPEgGLIALQLEADTEGIELLVFDEGSGIPDYALNRVFERF----YSLPRPHSGqksTGLG 76
                         90
                 ....*....|....*..
gi 503337118 398 LAITKHLVELMSGTVRV 414
Cdd:cd16945   77 LAFVQEVAQLHGGRITL 93
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
453-555 1.09e-08

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 52.73  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTEsLDVVFMDVSMP-VMDGLTATKILRAKGFEVPIIALT 531
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPD-IDLLVTDVIMPgGMNGSQLAEEARRRRPDLKVLLTS 79
                         90       100
                 ....*....|....*....|....
gi 503337118 532 AHALASDKQNCLDVGMDsFVAKPV 555
Cdd:cd18161   80 GYAENAIEGGDLAPGVD-VLSKPF 102
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
307-433 1.82e-08

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 56.95  E-value: 1.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 307 IELSIELDDKRHYWLDPSRLSQVLfnlIGNAVKF-----TQQGQIDIRVNLENDELSISVIDTGIGIEKDKISSLFtafk 381
Cdd:COG2972  321 LEVEIEIDEELLDLLIPKLILQPL---VENAIEHgiepkEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLL---- 393
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 503337118 382 qadSSITRKFGGTGLGLAITKHLVELMSG---TVRVSSQFGKGSTFVVKIPVKSR 433
Cdd:COG2972  394 ---EELSSKGEGRGIGLRNVRERLKLYYGeeyGLEIESEPGEGTTVTIRIPLEEE 445
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
452-565 1.90e-08

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: 52.79  E-value: 1.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 452 NVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIEsnTESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALT 531
Cdd:cd17569    2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILK--QEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLT 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 503337118 532 AHAlasDKQNCLDV----GMDSFVAKPVRKQELANAIE 565
Cdd:cd17569   80 GYA---DLDAAIEAinegEIYRFLTKPWDDEELKETIR 114
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
480-565 2.05e-08

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: 52.54  E-value: 2.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 480 ANNGSEAIEFIESNteSLDVVFMDVSMPVMDGLTATKILRaKGFEVP-IIALTAH---ALASDKQNCLDvgmdsFVAKPV 555
Cdd:cd17532   30 AENGEEALEAIEEL--KPDVVFLDIQMPGLDGLELAKKLS-KLAKPPlIVFVTAYdeyAVEAFELNAVD-----YLLKPF 101
                         90
                 ....*....|
gi 503337118 556 RKQELANAIE 565
Cdd:cd17532  102 SEERLAEALA 111
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
453-560 2.08e-08

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: 52.52  E-value: 2.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTEsLDVVFMDVSMPVMDGLTATKILRAK--GFEVPIIAL 530
Cdd:cd17544    3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPD-IKLVITDYNMPEMDGFELVREIRKKysRDQLAIIGI 81
                         90       100       110
                 ....*....|....*....|....*....|
gi 503337118 531 TAHALASDKQNCLDVGMDSFVAKPVRKQEL 560
Cdd:cd17544   82 SASGDNALSARFIKAGANDFLTKPFLPEEF 111
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
452-560 2.52e-08

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 54.81  E-value: 2.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 452 NVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIefIESNTESLDVVFMDVSMPVMDGLTATKILRaKGFEVPIIALT 531
Cdd:PRK10529   3 NVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGL--LEAATRKPDLIILDLGLPDGDGIEFIRDLR-QWSAIPVIVLS 79
                         90       100
                 ....*....|....*....|....*....
gi 503337118 532 AHALASDKQNCLDVGMDSFVAKPVRKQEL 560
Cdd:PRK10529  80 ARSEESDKIAALDAGADDYLSKPFGIGEL 108
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
453-565 3.93e-08

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


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 52.11  E-value: 3.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTEslDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFP--GVVISDIRMPGMDGLELLAQIRELDPDLPVILITG 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 503337118 533 H-----ALASDKQNCLDvgmdsFVAKPVRKQELANAIE 565
Cdd:cd17549   79 HgdvpmAVEAMRAGAYD-----FLEKPFDPERLLDVVR 111
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
343-429 4.30e-08

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: 52.97  E-value: 4.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 343 QGQIDIRVNLENDELSISVIDTGIGIEKDKISS------------------------LFTA-FKQADSsITrKFGGTGLG 397
Cdd:cd16916   69 EGTITLRAEHQGNQVVIEVSDDGRGIDREKIREkaierglitadeaatlsddevlnlIFAPgFSTAEQ-VT-DVSGRGVG 146
                         90       100       110
                 ....*....|....*....|....*....|..
gi 503337118 398 LAITKHLVELMSGTVRVSSQFGKGSTFVVKIP 429
Cdd:cd16916  147 MDVVKRSIESLGGTIEVESEPGQGTTFTIRLP 178
PRK15115 PRK15115
response regulator GlrR; Provisional
449-566 5.12e-08

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 55.61  E-value: 5.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 449 RALNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIesNTESLDVVFMDVSMPVMDGLTATKILRAKGFEVPII 528
Cdd:PRK15115   4 KPAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVL--NREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVI 81
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 503337118 529 ALTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEA 566
Cdd:PRK15115  82 ILTAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDD 119
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
175-433 5.29e-08

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 54.24  E-value: 5.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 175 AVIDIENKEKLQRIVELRTRELALAREEsERaNRakseflamMSHELRtplNSVLGMLDVLKqsdMSAGhiNLLSHMESS 254
Cdd:COG4585   25 VLLRARRAERAAELERELAARAEEAREE-ER-RR--------IARELH---DGVGQSLSAIK---LQLE--AARRLLDAD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 255 AGLLLAIISDILDLSKIESGE-----FSLSPQwinINDTVTFVVSQQQLVA---ATKGLNIELSIELDDKRhywLDPSRL 326
Cdd:COG4585   87 PEAAREELEEIRELAREALAElrrlvRGLRPP---ALDDLGLAAALEELAErllRAAGIRVELDVDGDPDR---LPPEVE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 327 SQVLFNL---IGNAVKFTQQGQIDIRVNLENDELSISVIDTGIGIEKDKISslftafkqadssitrkfgGTGLGLAITKH 403
Cdd:COG4585  161 LALYRIVqeaLTNALKHAGATRVTVTLEVDDGELTLTVRDDGVGFDPEAAP------------------GGGLGLRGMRE 222
                        250       260       270
                 ....*....|....*....|....*....|
gi 503337118 404 LVELMSGTVRVSSQFGKGSTFVVKIPVKSR 433
Cdd:COG4585  223 RAEALGGTLTIGSAPGGGTRVRATLPLAAA 252
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
453-568 6.48e-08

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: 51.02  E-value: 6.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:cd17553    3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTK--ERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTA 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 533 HALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:cd17553   81 YGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
PRK11173 PRK11173
two-component response regulator; Provisional
452-560 7.27e-08

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 53.48  E-value: 7.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 452 NVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTesLDVVFMDVSMPVMDGLTATKILRAKGfEVPIIALT 531
Cdd:PRK11173   5 HILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSEND--INLVIMDINLPGKNGLLLARELREQA-NVALMFLT 81
                         90       100
                 ....*....|....*....|....*....
gi 503337118 532 AHALASDKQNCLDVGMDSFVAKPVRKQEL 560
Cdd:PRK11173  82 GRDNEVDKILGLEIGADDYITKPFNPREL 110
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
453-568 1.05e-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: 50.36  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAI-EFIESNTeslDVVFMDVSMPVMDGLTATKILRAKGfEVPIIALT 531
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLeEFLQFKP---DLVLLDINLPYFDGFYWCREIRQIS-NVPIIFIS 76
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 503337118 532 AHALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:cd18159   77 SRDDNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
PRK10336 PRK10336
two-component system response regulator QseB;
451-568 1.09e-07

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 52.59  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 451 LNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIAL 530
Cdd:PRK10336   1 MRILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYS--APYDAVILDLTLPGMDGRDILREWREKGQREPVLIL 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 503337118 531 TAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:PRK10336  79 TARDALAERVEGLRLGADDYLCKPFALIEVAARLEALM 116
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
453-556 1.11e-07

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 50.44  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTESLDVVF--MDVSMPV----MDGLTATKILR-----AK 521
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGLEDEEDSSNFnePKVNMIItdycMPGMTGYDLLKkvkesSA 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 503337118 522 GFEVPIIALTAHALASDKQNCLDVGMDSFVAKPVR 556
Cdd:cd17581   81 LKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVK 115
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
322-428 1.61e-07

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


Pssm-ID: 340434 [Multi-domain]  Cd Length: 107  Bit Score: 49.77  E-value: 1.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 322 DPSRLSQVLFNLIGNAVKFTQQGQ-IDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFKQADSSITRKfGGTGLGLAI 400
Cdd:cd16975    1 DTLLLSRALINIISNACQYAPEGGtVSISIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSG-GHYGMGLYI 79
                         90       100
                 ....*....|....*....|....*...
gi 503337118 401 TKHLVELMSGTVRVSSQFGKGSTFVVKI 428
Cdd:cd16975   80 AKNLVEKHGGSLIIENSQKGGAEVTVKI 107
PRK09483 PRK09483
response regulator; Provisional
451-566 1.73e-07

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 52.03  E-value: 1.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 451 LNVLVVEDTHSNQMVIQLLLNKL-GHNVF-IANNGSEAIEFIESNteSLDVVFMDVSMPVMDGLTAT-KILRAKGfEVPI 527
Cdd:PRK09483   2 INVLLVDDHELVRAGIRRILEDIkGIKVVgEACCGEDAVKWCRTN--AVDVVLMDMNMPGIGGLEATrKILRYTP-DVKI 78
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 503337118 528 IALTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEA 566
Cdd:PRK09483  79 IMLTVHTENPLPAKVMQAGAAGYLSKGAAPQEVVSAIRS 117
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
297-428 2.86e-07

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: 49.94  E-value: 2.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 297 QLVAATKGLNIELSIeldDKRHYWL-DPSRLSQVLFNLIGNAVKFTQqGQIDIRVNLENDELSISVIDTGIGIEKDKISS 375
Cdd:cd16954   11 NKVYQRKGVSISLDI---SPELRFPgERNDLMELLGNLLDNACKWCL-EFVEVTARQTDGGLHLIVDDDGPGVPESQRSK 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 503337118 376 LFTAFKQADSSITrkfgGTGLGLAITKHLVELMSGTVRVSSQFGKGSTFVVKI 428
Cdd:cd16954   87 IFQRGQRLDEQRP----GQGLGLAIAKEIVEQYGGELSLSDSPLGGARFEVVF 135
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
453-554 2.94e-07

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 48.94  E-value: 2.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTESLDVVFMDVSMPVMDGLTA-TKILRAKGFE-VPIIAL 530
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNEIDLILTEVDLPVSSGFKLlSYIMRHKICKnIPVIMM 80
                         90       100
                 ....*....|....*....|....
gi 503337118 531 TAHALASDKQNCLDVGMDSFVAKP 554
Cdd:cd17582   81 SSQDSVGVVFKCLSKGAADYLVKP 104
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
453-534 3.20e-07

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: 49.19  E-value: 3.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTEslDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:cd19919    3 VWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQP--DVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTA 80

                 ..
gi 503337118 533 HA 534
Cdd:cd19919   81 HS 82
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
326-429 4.30e-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: 48.92  E-value: 4.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 326 LSQVLFNLIGNAVKFTQQG----------QIDIRVNLENDEL------SISVIDTGIGIEKDKISSLFTAFkqadsSITR 389
Cdd:cd16919    1 LELAILNLAVNARDAMPEGgrltietsnqRVDADYALNYRDLipgnyvCLEVSDTGSGMPAEVLRRAFEPF-----FTTK 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 503337118 390 KFG-GTGLGLAITKHLVELMSGTVRVSSQFGKGSTFVVKIP 429
Cdd:cd16919   76 EVGkGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
glnL PRK11073
nitrogen regulation protein NR(II);
322-431 4.73e-07

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 52.01  E-value: 4.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 322 DPSRLSQVLFNLIGNAVKFTQQ--GQIDIR------VNLENDEL----SISVIDTGIGIEKDKISSLFTAFkqadssITR 389
Cdd:PRK11073 234 DPDQIEQVLLNIVRNALQALGPegGTITLRtrtafqLTLHGERYrlaaRIDIEDNGPGIPPHLQDTLFYPM------VSG 307
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 503337118 390 KFGGTGLGLAITKHLVELMSGTVRVSSQFGKgSTFVVKIPVK 431
Cdd:PRK11073 308 REGGTGLGLSIARNLIDQHSGKIEFTSWPGH-TEFSVYLPIR 348
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
452-567 6.12e-07

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 50.73  E-value: 6.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 452 NVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALT 531
Cdd:PRK11083   5 TILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQ--QPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFLT 82
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 532 AHALASDKQNCLDVGMDSFVAKPVRKQELANAIEAL 567
Cdd:PRK11083  83 ARSDEVDRLVGLEIGADDYVAKPFSPREVAARVRTI 118
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
451-566 8.02e-07

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: 48.01  E-value: 8.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 451 LNVLVVEDthsNQMVIQL---LLNKLG--HNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKGFEV 525
Cdd:cd19925    1 INVLIVED---DPMVAEIhraYVEQVPgfTVIGTAGTGEEALKLLKE--RQPDLILLDIYLPDGNGLDLLRELRAAGHDV 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 503337118 526 PIIALTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEA 566
Cdd:cd19925   76 DVIVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRLER 116
PRK10693 PRK10693
two-component system response regulator RssB;
480-556 9.18e-07

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 50.76  E-value: 9.18e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503337118 480 ANNGSEAIEFIESNTEslDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTAHALASDKQNCLDVGMDSFVAKPVR 556
Cdd:PRK10693   3 AANGVDALELLGGFTP--DLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKPVK 77
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
451-518 1.61e-06

DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 47.58  E-value: 1.61e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503337118 451 LNVLVVEDthsNQMVIQLLLNKLGHN-----VFIANNGSEAIEFIESNteSLDVVFMDVSMPVMDGLTATKIL 518
Cdd:COG2197    2 IRVLIVDD---HPLVREGLRALLEAEpdievVGEAADGEEALELLEEL--RPDVVLLDIRMPGMDGLEALRRL 69
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
450-568 2.02e-06

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 48.95  E-value: 2.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 450 ALNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEfiESNTESLDVVFMDVSMPVMDGLTATKILRAKGF--EVPI 527
Cdd:PRK10161   2 ARRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVN--QLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMtrDIPV 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 503337118 528 IALTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:PRK10161  80 VMLTARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVM 120
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
453-554 5.67e-06

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: 45.13  E-value: 5.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIesNTESLDVVFMDVSMPVMDGLTATKILRAKGfEVPIIALTA 532
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGL--NARPPDLAILDIKMPRMDGMELLQRLRQKS-TLPVIFLTS 77
                         90       100
                 ....*....|....*....|..
gi 503337118 533 HALASDKQNCLDVGMDSFVAKP 554
Cdd:cd19936   78 KDDEIDEVFGLRMGADDYITKP 99
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
452-566 5.76e-06

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


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 46.83  E-value: 5.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 452 NVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIEsnTESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALT 531
Cdd:COG4567    6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLE--QAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVLT 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 503337118 532 -----AHALASDKQNCLDvgmdsFVAKPVRKQELANAIEA 566
Cdd:COG4567   84 gyasiATAVEAIKLGADD-----YLAKPADADDLLAALER 118
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
322-428 7.44e-06

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


Pssm-ID: 340409 [Multi-domain]  Cd Length: 113  Bit Score: 44.95  E-value: 7.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 322 DPSRLSQVLFNLIGNAVKFTQ--QGQIDIRV---------NLENDELSISVIDTGIGIEKDKISSLFtafkQADSSITRK 390
Cdd:cd16932    3 DQIRLQQVLADFLLNAVRFTPspGGWVEIKVsptkkqigdGVHVIHLEFRITHPGQGLPEELVQEMF----EENQWTTQE 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 503337118 391 fggtGLGLAITKHLVELMSGTVRVSSQFGKgSTFVVKI 428
Cdd:cd16932   79 ----GLGLSISRKLVKLMNGDVRYLREAGR-SYFLITL 111
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
296-433 8.20e-06

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 48.75  E-value: 8.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 296 QQLVAATKGLNIELSIELDDKRhywLDPSR---LSQVLFNLIGNAVKF----TQQGQIDIRVNLENDELSISVIDTGIGI 368
Cdd:COG3920  370 EPLRDSYGGRGIRIELDGPDVE---LPADAavpLGLILNELVTNALKHaflsGEGGRIRVSWRREDGRLRLTVSDNGVGL 446
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503337118 369 EKDkisslftafkqadssiTRKFGGTGLGLAITKHLVELMSGTVRVSSqfGKGSTFVVKIPVKSR 433
Cdd:COG3920  447 PED----------------VDPPARKGLGLRLIRALVRQLGGTLELDR--PEGTRVRITFPLAEL 493
PLN03029 PLN03029
type-a response regulator protein; Provisional
448-560 1.06e-05

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 46.95  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 448 DRALNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFI------ESNTES------------LDVVFMDVSMPVM 509
Cdd:PLN03029   6 ESQFHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLglheddRSNPDTpsvspnshqeveVNLIITDYCMPGM 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 503337118 510 DGLTATKILRAKGF--EVPIIALTAHALASDKQNCLDVGMDSFVAKPVRKQEL 560
Cdd:PLN03029  86 TGYDLLKKIKESSSlrNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDL 138
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
322-426 1.10e-05

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: 45.14  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 322 DPSRLSQVLFNLIGNAVKFTQQ-GQIDIRVNLENDELSISVIDTG----------------IGIEKDKISSLFTAFKQAD 384
Cdd:cd16938    8 DERRVFQVLLHMLGNLLKMRNGgGNITFRVFLEGGSEDRSDRDWGpwrpsmsdesveirfeVEINDSGSPSIESASMRNS 87
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 503337118 385 SSitRKFG----GTGLGLAITKHLVELMSGTVRVSSQFGKGSTFVV 426
Cdd:cd16938   88 LN--RRYNlselGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSL 131
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
453-566 1.13e-05

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 46.77  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDtHS--NQMVIQLLLNKLGHNVFI-ANNGSEAIEFieSNTESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIA 529
Cdd:PRK10403   9 VLIVDD-HPlmRRGVRQLLELDPGFEVVAeAGDGASAIDL--ANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQIII 85
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 503337118 530 LTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEA 566
Cdd:PRK10403  86 LTVSDASSDVFALIDAGADGYLLKDSDPEVLLEAIRA 122
PRK11517 PRK11517
DNA-binding response regulator HprR;
451-566 2.14e-05

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 46.04  E-value: 2.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 451 LNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTESLdvVFMDVSMPVMDGLTATKILRAKGfEVPIIAL 530
Cdd:PRK11517   1 MKILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYAL--IILDIMLPGMDGWQILQTLRTAK-QTPVICL 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 503337118 531 TAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEA 566
Cdd:PRK11517  78 TARDSVDDRVRGLDSGANDYLVKPFSFSELLARVRA 113
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
336-429 2.21e-05

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


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 42.93  E-value: 2.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 336 NAVKFTQQGQIDIRVNLENDELSISVIDTGIGIEKDkisslftafkqadssitRKFGGTGLGLAITKHLVELMSGTVRVS 415
Cdd:cd16917   11 NALKHAGASRVRVTLSYTADELTLTVVDDGVGFDGP-----------------APPGGGGFGLLGMRERAELLGGTLTIG 73
                         90
                 ....*....|....
gi 503337118 416 SQFGKGSTFVVKIP 429
Cdd:cd16917   74 SRPGGGTRVTARLP 87
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
480-565 2.28e-05

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: 43.88  E-value: 2.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 480 ANNGSEAIEFieSNTESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTAHALASDKQNCLDVGMDSFVAKPVRKQE 559
Cdd:cd19931   30 ASSGEEGIEL--AERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILTVSDAEDDVVTALRAGADGYLLKDMEPED 107

                 ....*.
gi 503337118 560 LANAIE 565
Cdd:cd19931  108 LLEALK 113
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
451-554 2.32e-05

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: 43.75  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 451 LNVLVVEDTHS-NQMVIQLLLNKLGHNVF-IANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKGFE--VP 526
Cdd:cd17561    2 IKVLIADDNREfVQLLEEYLNSQPDMEVVgVAHNGQEALELIEE--KEPDVLLLDIIMPHLDGIGVLEKLRRMRLEkrPK 79
                         90       100
                 ....*....|....*....|....*...
gi 503337118 527 IIALTAHALASDKQNCLDVGMDSFVAKP 554
Cdd:cd17561   80 IIMLTAFGQEDITQRAVELGASYYILKP 107
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
451-568 3.71e-05

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 45.30  E-value: 3.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 451 LNVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFieSNTESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIAL 530
Cdd:PRK09836   1 MKLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHL--AMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLL 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 503337118 531 TAHALASDKQNCLDVGMDSFVAKPVRKQELANAIEALI 568
Cdd:PRK09836  79 TALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLL 116
PRK15369 PRK15369
two component system response regulator;
498-565 4.23e-05

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 45.07  E-value: 4.23e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503337118 498 DVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTAHALASDKQNCLDVGMDSFVAKPVRKQELANAIE 565
Cdd:PRK15369  51 DIVILDLGLPGMNGLDVIPQLHQRWPAMNILVLTARQEEHMASRTLAAGALGYVLKKSPQQILLAAIQ 118
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
480-566 1.09e-04

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 43.86  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 480 ANNGSEAIEFIESNTEslDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTAHALASDKQNCLDVGMDSFVAKPVRKQE 559
Cdd:PRK10651  38 ASNGEQGIELAESLDP--DLILLDLNMPGMNGLETLDKLREKSLSGRIVVFSVSNHEEDVVTALKRGADGYLLKDMEPED 115

                 ....*..
gi 503337118 560 LANAIEA 566
Cdd:PRK10651 116 LLKALQQ 122
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
451-567 1.48e-04

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 43.35  E-value: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 451 LNVLVVEDTHSNQMVIQLLLNKLGHNVFIA-NNGSEAIEFIESNTEslDVVFMDVSMPVMDGLTATKILRAKGFEVPIIA 529
Cdd:PRK09958   1 MNAIIIDDHPLAIAAIRNLLIKNDIEILAElTEGGSAVQRVETLKP--DIVIIDVDIPGVNGIQVLETLRKRQYSGIIII 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 503337118 530 LTAHALASDKQNCLDVGMDSFVAKpvrKQELANAIEAL 567
Cdd:PRK09958  79 VSAKNDHFYGKHCADAGANGFVSK---KEGMNNIIAAI 113
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
455-555 1.49e-04

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: 41.10  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 455 VVEDTHSNQMVIQLLL--NKLGHNVFIANNGSEAIEfiESNTESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:cd17565    3 IVDDDKNIIKILSDIIedDDLGEVVGEADNGAQAYD--EILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMISQ 80
                         90       100
                 ....*....|....*....|...
gi 503337118 533 HALASDKQNCLDVGMDSFVAKPV 555
Cdd:cd17565   81 VSDKEMIGKAYQAGIEFFINKPI 103
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
343-430 2.06e-04

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 44.02  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 343 QGQIDIRVNLENDELSISVIDTGIGIEKDKISS------LFTAfkQADSSITRK------F--G-----------GTGLG 397
Cdd:COG0643  308 TGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAkaiekgLITA--EEAAALSDEelleliFapGfstaeevtdlsGRGVG 385
                         90       100       110
                 ....*....|....*....|....*....|...
gi 503337118 398 LAITKHLVELMSGTVRVSSQFGKGSTFVVKIPV 430
Cdd:COG0643  386 MDVVKTNIEALGGTIEIESEPGKGTTFTLRLPL 418
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
321-429 2.30e-04

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 44.05  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 321 LDPSRLSQVLFNLIGNAVKF---TQQG--QIDIRVNLENDELSISVIDTGIGIE---KDKIsslftaFKQADSSITRKFG 392
Cdd:PRK15053 428 LDSTEFAAIVGNLLDNAFEAslrSDEGnkIVELFLSDEGDDVVIEVADQGCGVPeslRDKI------FEQGVSTRADEPG 501
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 503337118 393 GTGLGLAITKHLVELMSGTVRVSSQFGKGSTFVVKIP 429
Cdd:PRK15053 502 EHGIGLYLIASYVTRCGGVITLEDNDPCGTLFSIFIP 538
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
452-534 2.54e-04

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 43.71  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 452 NVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTEslDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALT 531
Cdd:PRK10923   5 IVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTP--DVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMT 82

                 ...
gi 503337118 532 AHA 534
Cdd:PRK10923  83 AHS 85
fixJ PRK09390
response regulator FixJ; Provisional
452-566 3.26e-04

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 42.30  E-value: 3.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 452 NVLVVEDTHSNQMVIQLLLNKLGHNVFIANNgseAIEFIESNTE-SLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIAL 530
Cdd:PRK09390   5 VVHVVDDDEAMRDSLAFLLDSAGFEVRLFES---AQAFLDALPGlRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVM 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 503337118 531 TAHA---LASD--KQNCLDvgmdsFVAKPVRKQELANAIEA 566
Cdd:PRK09390  82 TGHGdvpLAVEamKLGAVD-----FIEKPFEDERLIGAIER 117
PRK10337 PRK10337
sensor protein QseC; Provisional
219-428 3.54e-04

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 43.10  E-value: 3.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 219 HELRTPLNSVLGMLDV--LKQSDMSAGHINLlshMESSAGLLLA--IISDILDLSKIESGEFSLSPQWININDTVTFVVS 294
Cdd:PRK10337 246 HELRSPLAALKVQTEVaqLSDDDPQARKKAL---LQLHAGIDRAtrLVDQLLTLSRLDSLDNLQDVAEIPLEDLLQSAVM 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 295 QQQLVAATKGlnIELSIELDD---KRHywLDPSRLSQVLFNLIGNAVKFTQQG-QIDIRVNlendELSISVIDTGIGIEK 370
Cdd:PRK10337 323 DIYHTAQQAG--IDVRLTLNAhpvIRT--GQPLLLSLLVRNLLDNAIRYSPQGsVVDVTLN----ARNFTVRDNGPGVTP 394
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503337118 371 DKISSLFTAF----KQADSsitrkfgGTGLGLAITKHLVELMSGTVRVSSQFGKGstFVVKI 428
Cdd:PRK10337 395 EALARIGERFyrppGQEAT-------GSGLGLSIVRRIAKLHGMNVSFGNAPEGG--FEAKV 447
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
453-554 3.84e-04

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 39.83  E-value: 3.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLAS--EPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITA 78
                         90       100
                 ....*....|....*....|..
gi 503337118 533 HALASDKQNCLDVGMDSFVAKP 554
Cdd:cd19926   79 YGSLDTAIEALKAGAFDFLTKP 100
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
453-547 1.04e-03

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 41.16  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKgFEVPIIALTa 532
Cdd:PRK10701   4 IVFVEDDAEVGSLIAAYLAKHDIDVTVEPRGDRAEATILR--EQPDLVLLDIMLPGKDGMTICRDLRPK-WQGPIVLLT- 79
                         90
                 ....*....|....*
gi 503337118 533 hALASDKQNCLDVGM 547
Cdd:PRK10701  80 -SLDSDMNHILALEM 93
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
453-554 1.51e-03

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 38.57  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIesNTESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYI--DIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSD 78
                         90       100
                 ....*....|....*....|..
gi 503337118 533 HALASDKQNCLDVGMDSFVAKP 554
Cdd:cd17573   79 NPKTEQEIEAFKEGADDYIAKP 100
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
333-405 1.52e-03

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 38.74  E-value: 1.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503337118 333 LIGNAVKFTQQ----GQIDIRVNLENDELSISVIDTGIGIEKDKISSLFTAFKqadssitrkfgGTGLGLAITKHLV 405
Cdd:COG2172   42 AVTNAVRHAYGgdpdGPVEVELELDPDGLEIEVRDEGPGFDPEDLPDPYSTLA-----------EGGRGLFLIRRLM 107
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
326-429 1.53e-03

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


Pssm-ID: 340427 [Multi-domain]  Cd Length: 131  Bit Score: 38.94  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 326 LSQVLFNLIGNAVKFTQQGQIDIRVNLENDELSISVIDTGIGIEKDkisslFTAFKQADssitrkfggtgLGLAITKHLV 405
Cdd:cd16951   44 VNELLQNALKHAFSDREGGTITIRSVVDGDYLRITVIDDGVGLPQD-----EDWPNKGS-----------LGLQIVRSLV 107
                         90       100
                 ....*....|....*....|....
gi 503337118 406 ELMSGTVRVSSQFGKGSTFVVKIP 429
Cdd:cd16951  108 EGELKAFLEVQSAENGTRVNIDIP 131
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
453-564 2.32e-03

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


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 38.50  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 453 VLVVEDTHSNQMVIQLLLNKlGHNVFIANNGSEAIEFIESntESLDVVFMDVSMPVMDGLTATKILRAKGFEVPIIALTA 532
Cdd:cd17596    3 ILVVDDEVRSLEALRRTLEE-DFDVLTAASAEEALAILEE--EWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISG 79
                         90       100       110
                 ....*....|....*....|....*....|...
gi 503337118 533 HALASDKQNCL-DVGMDSFVAKPVRKQELANAI 564
Cdd:cd17596   80 YTDSEDIIAGInEAGIYQYLTKPWHPDQLLLTV 112
HATPase_SpoIIAB-like cd16942
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ...
326-427 4.62e-03

Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of SpoIIAB, an anti sigma-F factor and a serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli where, early in sporulation, the cell divides into two unequal compartments: a larger mother cell and a smaller forespore. Sigma-F transcription factor is activated in the forespore directly after the asymmetric septum forms, and its spatial and temporal activation is required for sporulation. Free sigma-F can associate with the RNA polymerase core and activate transcription of the sigma-F regulon, its regulation may comprise a partner-switching mechanism involving SpoIIAB, SpoIIAA, and sigma-F as follows: SpoIIAB can form alternative complexes with either: i) sigma-F, holding it in an inactive form and preventing its association with RNA polymerase, or ii) unphosphorylated SpoIIAA and a nucleotide, either ATP or ADP. In the presence of ATP, SpoIIAB acts as a kinase to specifically phosphorylate a serine residue of SpoIIAA; this phosphorylated form has low affinity for SpoIIAB and dissociates, making SpoIIAB available to capture sigma-F. SpoIIAA may then be dephosphorylated by a SpoIIE serine phosphatase and be free to attack the SpoIIAB sigma-F complex to induce the release of sigma-F.


Pssm-ID: 340418 [Multi-domain]  Cd Length: 135  Bit Score: 37.52  E-value: 4.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 326 LSQVLFNLIGNAVKFTQQGQIDIRVNLENDELSISVIDTGIGIE--KDKISSLFTAFKQADSSitrkfggtGLGLAITKH 403
Cdd:cd16942   43 VSEAVTNAIIHGYNNDPNGIVSISVIIEDGVVHLTVRDEGVGIPdiEEARQPLFTTKPELERS--------GMGFTIMEN 114
                         90       100
                 ....*....|....*....|....
gi 503337118 404 LVElmsgTVRVSSQFGKGSTFVVK 427
Cdd:cd16942  115 FMD----EVIVESEVNKGTTVYLK 134
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
452-563 5.43e-03

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: 37.04  E-value: 5.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 452 NVLVVEDTHSNQMVIQLLLNKLGHNVFIANNGSEAIEFIESNTESLDVVfmDVSMPVMDGLTATKILRAKGFEVPIIALT 531
Cdd:cd17563    2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVL--DLRLGGDSGLDLIPPLRALQPDARIVVLT 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 503337118 532 -----AHALASDKQncldvGMDSFVAKPVRKQELANA 563
Cdd:cd17563   80 gyasiATAVEAIKL-----GADDYLAKPADADEILAA 111
REC_LytTR_AgrA-like cd17533
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; ...
451-533 7.05e-03

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; 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 AgrA-like group of LytTR/AlgR family response regulators are Staphylococcus aureus accessory gene regulator protein A (AgrA) and Streptococcus pneumoniae response regulator ComE, which are members of two-component regulatory systems. AgrA is a global regulator that controls the synthesis of virulence factors and other exoproteins. ComE is part of the ComD-ComE system that is part of a quorum-sensing signaling pathway that controls the development of competence, a physiological state required for genetic transformation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381088 [Multi-domain]  Cd Length: 131  Bit Score: 36.83  E-value: 7.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503337118 451 LNVLVVEDTHSNQMVIQ------LLLNKLGHNVFIANNGSEAIEFI-ESNTESLDVVFMDVSMPVMDGLTATKILRAKGF 523
Cdd:cd17533    1 MNIFILEDDKIQRVRLEeiieniLKIENIEYVIELTGKTEELLEKIkERGKNGIYFLDIDIKMEEKNGLEVAQKIRKYDP 80
                         90
                 ....*....|
gi 503337118 524 EVPIIALTAH 533
Cdd:cd17533   81 YAIIIFVTTH 90
 
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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