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Conserved domains on  [gi|1590033346|ref|WP_131447151|]
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ATP-binding protein [Parasulfuritortus cantonensis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TMAO_torS super family cl37193
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
325-777 9.52e-98

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: 325.19  E-value: 9.52e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 325 AGVVDIPeeaVDTR------QGGRRILHTRKLALRNAQGEAEFLLgmsediteakrTAEELQRHRENLEQLVEVRTAELS 398
Cdd:TIGR02956 372 LGDLDIS---LDARgddelaHMGRAIEAFRDTAAHNLKLQADERQ-----------VAQELQEHKESLEQLVAQRTQELA 437
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 399 ------------HAKEAAEA--ANVAKSAFLANMSHEIRTPLNAITGMAHLIRRGGLTDKQDDQLAKLEAAGAHLLNIIN 464
Cdd:TIGR02956 438 etnerlnaevknHAKARAEAeeANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILN 517
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 465 AILELSKIEAGKFQLEHVPVDVNDLVGNVVTMIQAGAQAKRLRLATEVAP-VPGVLYGDPTRLQQALLNYAGNAVKFTEA 543
Cdd:TIGR02956 518 DILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEqLPNWWQGDGPRIRQVLINLVGNAIKFTDR 597
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 544 GSVTLRVHAVEEAPeavlLRFEVTDTGIGLAPDTLAKLFTAFEQADNSttRKYGGTGLGLAVTRRLAELMGGGAGAESRP 623
Cdd:TIGR02956 598 GSVVLRVSLNDDSS----LLFEVEDTGCGIAEEEQATLFDAFTQADGR--RRSGGTGLGLAISQRLVEAMDGELGVESEL 671
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 624 GAGSTFWFTARLErragaggdaHAVAQSDAEARLLRDHRGARLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMA 703
Cdd:TIGR02956 672 GVGSCFWFTLPLT---------RGKPAEDSATLTVIDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECF 742
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1590033346 704 EANDYALILMDVQMPRLDGLEATRRIRCL-PRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:TIGR02956 743 HQHAFDLALLDINLPDGDGVTLLQQLRAIyGAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMI 817
PAS COG2202
PAS domain [Signal transduction mechanisms];
246-391 2.26e-20

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 91.62  E-value: 2.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 246 RNEAEIGAANRLLDSIVENIPNMIFLKRADDlRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALATA 325
Cdd:COG2202     1 TAEEALEESERRLRALVESSPDAIIITDLDG-RILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGG 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590033346 326 GVVDIpEEAVDTRQGGRRILHTRKLALRNAQGEAEFLLGMSEDITEAKRTAEELQRHRENLEQLVE 391
Cdd:COG2202    80 GVWRG-ELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVE 144
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
149-251 1.74e-06

Sensor histidine kinase YesM [Signal transduction mechanisms];


:

Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 51.17  E-value: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 149 TVITISTAELNDQKRSILLWGVLGSAFFVLLSSTSIVFLAQRLlTRRVDVSLGVLKEVEEGDVAaRIPVTYSDELGELQA 228
Cdd:COG2972   139 LVSLIPKSELFRGLFSLRRLILLIILLLLLLALLLSYLLSRSI-TRPIKRLKKAMKKVEKGDLV-RLEVSGNDEIGILAR 216
                          90       100
                  ....*....|....*....|...
gi 1590033346 229 GINSMTAKLGALLAVHQRNEAEI 251
Cdd:COG2972   217 SFNEMVERIKELIEEVYELELEK 239
 
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 ...
325-777 9.52e-98

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: 325.19  E-value: 9.52e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 325 AGVVDIPeeaVDTR------QGGRRILHTRKLALRNAQGEAEFLLgmsediteakrTAEELQRHRENLEQLVEVRTAELS 398
Cdd:TIGR02956 372 LGDLDIS---LDARgddelaHMGRAIEAFRDTAAHNLKLQADERQ-----------VAQELQEHKESLEQLVAQRTQELA 437
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 399 ------------HAKEAAEA--ANVAKSAFLANMSHEIRTPLNAITGMAHLIRRGGLTDKQDDQLAKLEAAGAHLLNIIN 464
Cdd:TIGR02956 438 etnerlnaevknHAKARAEAeeANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILN 517
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 465 AILELSKIEAGKFQLEHVPVDVNDLVGNVVTMIQAGAQAKRLRLATEVAP-VPGVLYGDPTRLQQALLNYAGNAVKFTEA 543
Cdd:TIGR02956 518 DILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEqLPNWWQGDGPRIRQVLINLVGNAIKFTDR 597
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 544 GSVTLRVHAVEEAPeavlLRFEVTDTGIGLAPDTLAKLFTAFEQADNSttRKYGGTGLGLAVTRRLAELMGGGAGAESRP 623
Cdd:TIGR02956 598 GSVVLRVSLNDDSS----LLFEVEDTGCGIAEEEQATLFDAFTQADGR--RRSGGTGLGLAISQRLVEAMDGELGVESEL 671
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 624 GAGSTFWFTARLErragaggdaHAVAQSDAEARLLRDHRGARLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMA 703
Cdd:TIGR02956 672 GVGSCFWFTLPLT---------RGKPAEDSATLTVIDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECF 742
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1590033346 704 EANDYALILMDVQMPRLDGLEATRRIRCL-PRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:TIGR02956 743 HQHAFDLALLDINLPDGDGVTLLQQLRAIyGAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMI 817
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
383-780 6.87e-96

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 319.10  E-value: 6.87e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 383 RENLEQLvEVRTAELSHAK-EAAEAANVaKSAFLANMSHEIRTPLNAITGMAHLIRRGGLTDKQDDQLAKLEAAGAHLLN 461
Cdd:PRK11107  266 RETLEQM-EIQNVELDLAKkRAQEAARI-KSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLA 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 462 IINAILELSKIEAGKFQLEHVPVDVNDLVGNVVTMIQAGAQAKRLRLATEVAP-VPGVLYGDPTRLQQALLNYAGNAVKF 540
Cdd:PRK11107  344 IINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPdVPDNVIGDPLRLQQIITNLVGNAIKF 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 541 TEAGSVTLRVHAVEEAPEAVLLRFEVTDTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGLGLAVTRRLAELMGGGAGAE 620
Cdd:PRK11107  424 TESGNIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFH 503
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 621 SRPGAGSTFWFTARLERRAGAGGD---------------------AHAV------------------------------- 648
Cdd:PRK11107  504 SQPNRGSTFWFHLPLDLNPNPIIDglptdclagkrllyvepnsaaAQATldilsetplevtysptlsqlpeahydilllg 583
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 649 ---------------------------------AQSDAEA-----------------RLLR----DHRGARLLLAEDEPI 674
Cdd:PRK11107  584 lpvtfrepltmlherlakaksmtdflilalpchEQVLAEQlkqdgadaclskplshtRLLPallePCHHKQPPLLPPTDE 663
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 675 NRE-ITVLLLDD--VGLK------------ADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGTP 739
Cdd:PRK11107  664 SRLpLTVMAVDDnpANLKligalleeqvehVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHNQNTP 743
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 1590033346 740 ILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATLLTW 780
Cdd:PRK11107  744 IIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRY 784
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
303-632 1.26e-72

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 240.20  E-value: 1.26e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 303 YDLFPAEQADALTARDREALATAGVVDIPEEAVDTRQGGRRILHTRKLALRNAQGEAEFLLGMSEDITEAKRTAEELQRH 382
Cdd:COG0642     2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 383 RENLEQLVEVRTAELSHAKEAAEAANVAKSAFLANMSHEIRTPLNAITGMAHLIRRGgLTDKQDDQLAKLEAAGAHLLNI 462
Cdd:COG0642    82 LLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE-LDEEQREYLETILRSADRLLRL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 463 INAILELSKIEAGKFQLEHVPVDVNDLVGNVVTMIQAGAQAKRLRLATEVAPVPGVLYGDPTRLQQALLNYAGNAVKFTE 542
Cdd:COG0642   161 INDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 543 AGS-VTLRVHAVEEApeavlLRFEVTDTGIGLAPDTLAKLFTAFEQADNSttRKYGGTGLGLAVTRRLAELMGGGAGAES 621
Cdd:COG0642   241 EGGtVTVSVRREGDR-----VRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVES 313
                         330
                  ....*....|.
gi 1590033346 622 RPGAGSTFWFT 632
Cdd:COG0642   314 EPGKGTTFTVT 324
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
526-635 1.05e-55

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: 186.54  E-value: 1.05e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 526 LQQALLNYAGNAVKFTEAGSVTLRVHAVEEAPEAVLLRFEVTDTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGLGLAV 605
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1590033346 606 TRRLAELMGGGAGAESRPGAGSTFWFTARL 635
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
521-636 3.65e-31

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 117.75  E-value: 3.65e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346  521 GDPTRLQQALLNYAGNAVKFTEA-GSVTLRVHAVEEApeavlLRFEVTDTGIGLAPDTLAKLFTAFEQADNsTTRKYGGT 599
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEgGRITVTLERDGDH-----VEITVEDNGPGIPPEDLEKIFEPFFRTDK-RSRKIGGT 74
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1590033346  600 GLGLAVTRRLAELMGGGAGAESRPGAGSTFWFTARLE 636
Cdd:smart00387  75 GLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
521-637 2.81e-27

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: 106.68  E-value: 2.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 521 GDPTRLQQALLNYAGNAVKFT-EAGSVTLRVHAVEEapeavlLRFEVTDTGIGLAPDTLAKLFTAFEQADnstTRKYGGT 599
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAaKAGEITVTLSEGGE------LTLTVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGGT 71
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1590033346 600 GLGLAVTRRLAELMGGGAGAESRPGAGSTFWFTARLER 637
Cdd:pfam02518  72 GLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
205-632 5.45e-26

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


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 113.69  E-value: 5.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 205 EVEEGDVAARIPVTYSDELGELQAGINSMTAKLGALLAVhqrNEAEigaaNRLLDSIvenIPNM----IflkrADD--LR 278
Cdd:NF033092  214 AMAKGDFSRKVKVYGNDEIGQLAEAFNNLTKRLQEAQAT---TESE----RRKLDSV---LSHMtdgvI----ATDrrGR 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 279 FVLFNRAGERLLGHARQELLGRTEYDL--FPAEQADALTARDREALatagVVDIPEEAVDTrqggrrILHtrklalrnA- 355
Cdd:NF033092  280 VILINDPALEMLNVSRETVLGQSILDVlgLEEEYTLRDLLEEQDSL----LLDFSTEEEPL------ILR--------An 341
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 356 ----QGEAEFLLGMS---EDITEAKRTaeELQRhREnleqlvevrtaelshakeaaeaanvaksaFLANMSHEIRTPLna 428
Cdd:NF033092  342 fsviQRESGFINGLIavlHDVTEQEKI--EQER-RE-----------------------------FVANVSHELRTPL-- 387
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 429 iTGM-----AhlirrggLTDK--QDDQLAKleaagaHLLNI-----------INAILELSKIEAGKFQLEHVPVDVNDLV 490
Cdd:NF033092  388 -TTMrsyleA-------LADGawKDPELAP------RFLGVtqnetermirlVNDLLQLSRMDSKDYKLNKEWVNFNEFF 453
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 491 GNVV---TMIqagAQAKRLRLATEVAPVPGVLYGDPTRLQQALLNYAGNAVKFT-EAGSVTLRVHAVEEapeavLLRFEV 566
Cdd:NF033092  454 NYIIdrfEMI---LKNKNITFKREFPKRDLWVEIDTDKITQVLDNIISNAIKYSpEGGTITFRLLETHN-----RIIISI 525
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590033346 567 TDTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGLGLAVTRRLAELMGGGAGAESRPGAGSTFWFT 632
Cdd:NF033092  526 SDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAESEEGKGTTIYFT 591
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
414-642 2.91e-24

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 107.42  E-value: 2.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 414 FLANMSHEIRTPLNAITGMAHLIRrggltdkqdDQLAKLEAA---GAHLLN--------IINAILELSKIEAGKFQLEHV 482
Cdd:NF040691  274 FVSDVSHELRTPLTTIRMAADVIH---------DSRDDFDPAtarSAELLHteldrfesLLSDLLEISRFDAGAAELDVE 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 483 PVDVNDLVGNVVTMIQAGAQAKRLRLATEVAPVPGVLYGDPTRLQQALLNYAGNAVKFTEAGSVTLRVHAveeAPEAVLL 562
Cdd:NF040691  345 PVDLRPLVRRVVDALRQLAERAGVELRVDAPGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTVAQ---DDTAVAV 421
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 563 RfeVTDTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGLGLAVTRRLAELMGGGAGAESRPGAGSTFWFTarLERRAGAG 642
Cdd:NF040691  422 T--VRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLT--LPRVAGDR 497
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
396-626 2.64e-23

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 103.75  E-value: 2.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 396 ELSHAKEAAEAANVAKSAFLANMSHEIRTPLNAITGMAHLIrRGGLTDKQDDQLAKLEAAGAHLLNIINAILELSKIEAG 475
Cdd:NF012163  225 DFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRAELEAI-QDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEG 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 476 KFQLEHVPVDvndlvgnVVTMIQAGAQAKRLRLAT------EVAPVPGVLYGDPTRLQQALLNYAGNAVKFTEAGSvTLR 549
Cdd:NF012163  304 ALAYQKASVD-------LVPLLEVEGGAFRERFASagleleVSLPDSSLVFGDRDRLMQLFNNLLENSLRYTDSGG-SLH 375
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590033346 550 VHAvEEAPEAVLLRFEvtDTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGLGLAVTRRLAELMGGGAGAESRPGAG 626
Cdd:NF012163  376 ISA-SQRPKEVTLTVA--DSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGG 449
PAS COG2202
PAS domain [Signal transduction mechanisms];
246-391 2.26e-20

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 91.62  E-value: 2.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 246 RNEAEIGAANRLLDSIVENIPNMIFLKRADDlRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALATA 325
Cdd:COG2202     1 TAEEALEESERRLRALVESSPDAIIITDLDG-RILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGG 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590033346 326 GVVDIpEEAVDTRQGGRRILHTRKLALRNAQGEAEFLLGMSEDITEAKRTAEELQRHRENLEQLVE 391
Cdd:COG2202    80 GVWRG-ELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVE 144
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
262-374 1.52e-16

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 75.91  E-value: 1.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 262 VENIPNMIFLKrADDLRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALATAGVVDIPEEAVDTrqGG 341
Cdd:pfam08448   1 LDSLPDALAVL-DPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLEELLLN--GE 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1590033346 342 RRILHTRKLALRNAQGEAEFLLGMSEDITEAKR 374
Cdd:pfam08448  78 ERHYELRLTPLRDPDGEVIGVLVISRDITERRR 110
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
260-379 1.55e-13

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 67.70  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 260 SIVENIPNMIFLKRADDlRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALATAGVVDIPEEAVDTRQ 339
Cdd:TIGR00229   7 AIFESSPDAIIVIDLEG-NILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRVRRKD 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1590033346 340 GGRRILHTRkLALRNAQGEAEFLLGMSEDITEAKRTAEEL 379
Cdd:TIGR00229  86 GSEIWVEVS-VSPIRTNGGELGVVGIVRDITERKEAEEAL 124
PRK13560 PRK13560
hypothetical protein; Provisional
245-391 1.61e-09

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 61.61  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 245 QRNEAEIGAANRLLDSIVENIPNMIFLKRADDLRFVLfNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALAT 324
Cdd:PRK13560  193 KRAEERIDEALHFLQQLLDNIADPAFWKDEDAKVFGC-NDAACLACGFRREEIIGMSIHDFAPAQPADDYQEADAAKFDA 271
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590033346 325 AGvVDIPEEAVDTRQGGRRILHTR--KLALRNAQGEAEFLLGMSEDITEAKRTAEELQRHRENLEQLVE 391
Cdd:PRK13560  272 DG-SQIIEAEFQNKDGRTRPVDVIfnHAEFDDKENHCAGLVGAITDISGRRAAERELLEKEDMLRAIIE 339
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
267-369 9.58e-08

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 50.71  E-value: 9.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 267 NMIFLKRADDLRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALATAGVVDIpEEAVDTRQGGRRILH 346
Cdd:cd00130     2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTL-EVRLRRKDGSVIWVL 80
                          90       100
                  ....*....|....*....|...
gi 1590033346 347 TRKLALRNAQGEAEFLLGMSEDI 369
Cdd:cd00130    81 VSLTPIRDEGGEVIGLLGVVRDI 103
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
256-323 4.96e-07

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 47.39  E-value: 4.96e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590033346  256 RLLDSIVENIPNMIFLkRADDLRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALA 323
Cdd:smart00091   1 ERLRAILESLPDGIFV-LDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
149-251 1.74e-06

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 51.17  E-value: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 149 TVITISTAELNDQKRSILLWGVLGSAFFVLLSSTSIVFLAQRLlTRRVDVSLGVLKEVEEGDVAaRIPVTYSDELGELQA 228
Cdd:COG2972   139 LVSLIPKSELFRGLFSLRRLILLIILLLLLLALLLSYLLSRSI-TRPIKRLKKAMKKVEKGDLV-RLEVSGNDEIGILAR 216
                          90       100
                  ....*....|....*....|...
gi 1590033346 229 GINSMTAKLGALLAVHQRNEAEI 251
Cdd:COG2972   217 SFNEMVERIKELIEEVYELELEK 239
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
202-237 4.65e-05

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


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 41.28  E-value: 4.65e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1590033346 202 VLKEVEEGDVAARIPVTYSDELGELQAGINSMTAKL 237
Cdd:cd06225    10 AARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
190-242 7.27e-05

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


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 41.08  E-value: 7.27e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1590033346  190 RLLTRRVDVSLGVLKEVEEGDVAARIPVTYSDELGELQAGINSMTAKLGALLA 242
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
HAMP pfam00672
HAMP domain;
190-237 1.44e-03

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 37.22  E-value: 1.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1590033346 190 RLLTRRVDVSLGVLKEVEEGDVAARIPVTYSDELGELQAGINSMTAKL 237
Cdd:pfam00672   4 RRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERL 51
 
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 ...
325-777 9.52e-98

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: 325.19  E-value: 9.52e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 325 AGVVDIPeeaVDTR------QGGRRILHTRKLALRNAQGEAEFLLgmsediteakrTAEELQRHRENLEQLVEVRTAELS 398
Cdd:TIGR02956 372 LGDLDIS---LDARgddelaHMGRAIEAFRDTAAHNLKLQADERQ-----------VAQELQEHKESLEQLVAQRTQELA 437
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 399 ------------HAKEAAEA--ANVAKSAFLANMSHEIRTPLNAITGMAHLIRRGGLTDKQDDQLAKLEAAGAHLLNIIN 464
Cdd:TIGR02956 438 etnerlnaevknHAKARAEAeeANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILN 517
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 465 AILELSKIEAGKFQLEHVPVDVNDLVGNVVTMIQAGAQAKRLRLATEVAP-VPGVLYGDPTRLQQALLNYAGNAVKFTEA 543
Cdd:TIGR02956 518 DILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEqLPNWWQGDGPRIRQVLINLVGNAIKFTDR 597
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 544 GSVTLRVHAVEEAPeavlLRFEVTDTGIGLAPDTLAKLFTAFEQADNSttRKYGGTGLGLAVTRRLAELMGGGAGAESRP 623
Cdd:TIGR02956 598 GSVVLRVSLNDDSS----LLFEVEDTGCGIAEEEQATLFDAFTQADGR--RRSGGTGLGLAISQRLVEAMDGELGVESEL 671
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 624 GAGSTFWFTARLErragaggdaHAVAQSDAEARLLRDHRGARLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMA 703
Cdd:TIGR02956 672 GVGSCFWFTLPLT---------RGKPAEDSATLTVIDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECF 742
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1590033346 704 EANDYALILMDVQMPRLDGLEATRRIRCL-PRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:TIGR02956 743 HQHAFDLALLDINLPDGDGVTLLQQLRAIyGAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMI 817
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
383-780 6.87e-96

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 319.10  E-value: 6.87e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 383 RENLEQLvEVRTAELSHAK-EAAEAANVaKSAFLANMSHEIRTPLNAITGMAHLIRRGGLTDKQDDQLAKLEAAGAHLLN 461
Cdd:PRK11107  266 RETLEQM-EIQNVELDLAKkRAQEAARI-KSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLA 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 462 IINAILELSKIEAGKFQLEHVPVDVNDLVGNVVTMIQAGAQAKRLRLATEVAP-VPGVLYGDPTRLQQALLNYAGNAVKF 540
Cdd:PRK11107  344 IINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPdVPDNVIGDPLRLQQIITNLVGNAIKF 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 541 TEAGSVTLRVHAVEEAPEAVLLRFEVTDTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGLGLAVTRRLAELMGGGAGAE 620
Cdd:PRK11107  424 TESGNIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFH 503
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 621 SRPGAGSTFWFTARLERRAGAGGD---------------------AHAV------------------------------- 648
Cdd:PRK11107  504 SQPNRGSTFWFHLPLDLNPNPIIDglptdclagkrllyvepnsaaAQATldilsetplevtysptlsqlpeahydilllg 583
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 649 ---------------------------------AQSDAEA-----------------RLLR----DHRGARLLLAEDEPI 674
Cdd:PRK11107  584 lpvtfrepltmlherlakaksmtdflilalpchEQVLAEQlkqdgadaclskplshtRLLPallePCHHKQPPLLPPTDE 663
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 675 NRE-ITVLLLDD--VGLK------------ADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGTP 739
Cdd:PRK11107  664 SRLpLTVMAVDDnpANLKligalleeqvehVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHNQNTP 743
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 1590033346 740 ILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATLLTW 780
Cdd:PRK11107  744 IIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRY 784
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
243-768 2.85e-81

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 276.44  E-value: 2.85e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 243 VHQRNEAEIGAANR--LLDSIVENIPNMIFLkRADDLRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDRE 320
Cdd:PRK11091  140 IKEREETQIELEQQssLLRSFLDASPDLVYY-RNEDGEFSGCNRAMELLTGKSEKQLIGLTPKDVYSPEAAEKVIETDEK 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 321 ALATaGVVDIPEEAVDTRQGGRRILHTRKLALRNAQGEAEFLLGMSEDITEAKRtaeelqrhrenleqlvevrtaelshA 400
Cdd:PRK11091  219 VFRH-NVSLTYEQWLDYPDGRKACFELRKVPFYDRVGKRHGLMGFGRDITERKR-------------------------Y 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 401 KEAAEAANVAKSAFLANMSHEIRTPLNAITGMAHLIRRGGLTDKQDDQLAKLEAAGAHLLNIINAILELSKIEAGKFQLE 480
Cdd:PRK11091  273 QDALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQLD 352
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 481 HVPVDVNDLVGNVVTMIQAGAQAKRLRLATE-VAPVPGVLYGDPTRLQQALLNYAGNAVKFTEAGSVTLRVHAVEEApea 559
Cdd:PRK11091  353 NQPIDFTDFLADLENLSGLQAEQKGLRFDLEpLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRYEEGD--- 429
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 560 vLLRFEVTDTGIGLAPDTLAKLFTAFEQADNST-TRKYGGTGLGLAVTRRLAELMGGGAGAESRPGAGSTFwftaRLERR 638
Cdd:PRK11091  430 -MLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHgGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCF----TLTIH 504
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 639 AGAGGDAHAVAQSDAEARLlrdhRGARLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMP 718
Cdd:PRK11091  505 APAVAEEVEDAFDEDDMPL----PALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLP 580
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1590033346 719 RLDGLEATRRIR-CLPRHAGTPILAMTANAFAeDKAVCFAAGMNDFIAKPV 768
Cdd:PRK11091  581 DMTGLDIARELReRYPREDLPPLVALTANVLK-DKKEYLDAGMDDVLSKPL 630
PRK15347 PRK15347
two component system sensor kinase;
379-777 3.09e-76

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 265.35  E-value: 3.09e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 379 LQRHRENLEQLVEVRTAELSHAKEAAEAANVAKSAFLANMSHEIRTPLNAITGMAHLIRRGGLTDKQDDQLAKLEAAGAH 458
Cdd:PRK15347  366 LNEQYDTLENKVAERTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLS 445
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 459 LLNIINAILELSKIEAGKFQLEHVPVDVNDLVGNVVTMIQAGAQAKRLRLATEVAP-VPGVLYGDPTRLQQALLNYAGNA 537
Cdd:PRK15347  446 LLAIINNLLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAhVPLYLHLDSLRLRQILVNLLGNA 525
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 538 VKFTEAGSVTLRVHAVEEapeavLLRFEVTDTGIGLAPDTLAKLFTAFEQADNSTtrkyGGTGLGLAVTRRLAELMGGGA 617
Cdd:PRK15347  526 VKFTETGGIRLRVKRHEQ-----QLCFTVEDTGCGIDIQQQQQIFTPFYQADTHS----QGTGLGLTIASSLAKMMGGEL 596
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 618 GAESRPGAGSTFWFTARLERRA----------------------GAGGDA--HAVAQSDAE-----ARLLRDHRGARL-- 666
Cdd:PRK15347  597 TLFSTPGVGSCFSLVLPLNEYAppeplkgelsaplalhrqlsawGITCQPghQNPALLDPElaylpGRLYDLLQQIIQga 676
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 667 -----------------LLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRI 729
Cdd:PRK15347  677 pnepvinlplqpwqlqiLLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLW 756
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1590033346 730 RCLP--RHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:PRK15347  757 RDDPnnLDPDCMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARAL 806
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
303-632 1.26e-72

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 240.20  E-value: 1.26e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 303 YDLFPAEQADALTARDREALATAGVVDIPEEAVDTRQGGRRILHTRKLALRNAQGEAEFLLGMSEDITEAKRTAEELQRH 382
Cdd:COG0642     2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 383 RENLEQLVEVRTAELSHAKEAAEAANVAKSAFLANMSHEIRTPLNAITGMAHLIRRGgLTDKQDDQLAKLEAAGAHLLNI 462
Cdd:COG0642    82 LLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE-LDEEQREYLETILRSADRLLRL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 463 INAILELSKIEAGKFQLEHVPVDVNDLVGNVVTMIQAGAQAKRLRLATEVAPVPGVLYGDPTRLQQALLNYAGNAVKFTE 542
Cdd:COG0642   161 INDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 543 AGS-VTLRVHAVEEApeavlLRFEVTDTGIGLAPDTLAKLFTAFEQADNSttRKYGGTGLGLAVTRRLAELMGGGAGAES 621
Cdd:COG0642   241 EGGtVTVSVRREGDR-----VRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVES 313
                         330
                  ....*....|.
gi 1590033346 622 RPGAGSTFWFT 632
Cdd:COG0642   314 EPGKGTTFTVT 324
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
396-632 1.45e-66

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 220.93  E-value: 1.45e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 396 ELSHAKEAAEAANVAKSAFLANMSHEIRTPLNAITGMAHLIRRGG--LTDKQDDQLAKLEAAGAHLLNIINAILELSKIE 473
Cdd:COG2205     1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEdlSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 474 AGKFQLEHVPVDVNDLVGNVVTMIQAGAQAKRLRLATEVAPVPGVLYGDPTRLQQALLNYAGNAVKFTEAGS-VTLRVHA 552
Cdd:COG2205    81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGtITISARR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 553 VEEApeavlLRFEVTDTGIGLAPDTLAKLFTAFEQADNstTRKYGGTGLGLAVTRRLAELMGGGAGAESRPGAGSTFWFT 632
Cdd:COG2205   161 EGDG-----VRISVSDNGPGIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVT 233
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
265-632 7.85e-65

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 221.35  E-value: 7.85e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 265 IPNMIFLKRADDLRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALATAGVVDIPEEAVDTRQGGRRI 344
Cdd:COG5002    15 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 345 LHTRKLALRNAQGEAEFLLGMSEDITEAKRTAEELQRHRENLEQLVEVRTAELSHAKE----AAEAANVAKSAFLANMSH 420
Cdd:COG5002    95 LLLLLALLILLLLLALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVErditELERLEQMRREFVANVSH 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 421 EIRTPLNAITGMAHLIRRGGLTDKQDDQ--LAKLEAAGAHLLNIINAILELSKIEAGKFQLEHVPVDVNDLVGNVVTMIQ 498
Cdd:COG5002   175 ELRTPLTSIRGYLELLLDGAADDPEERReyLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELR 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 499 AGAQAKRLRLATEVAPVPGVLYGDPTRLQQALLNYAGNAVKFTEAGS-VTLRVHAVEEApeavlLRFEVTDTGIGLAPDT 577
Cdd:COG5002   255 PLAEEKGIELELDLPEDPLLVLGDPDRLEQVLTNLLDNAIKYTPEGGtITVSLREEDDQ-----VRISVRDTGIGIPEED 329
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1590033346 578 LAKLFTAFEQADNSTTRKYGGTGLGLAVTRRLAELMGGGAGAESRPGAGSTFWFT 632
Cdd:COG5002   330 LPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTIT 384
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
163-632 3.43e-59

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: 207.12  E-value: 3.43e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 163 RSILLWGVLGSAFFVLLSSTSIVFLAQRLLTRRVDVSLGVLKEVEEGDVAARIPVTYSDELGELQAGINSMTAKLgalla 242
Cdd:COG5000     4 QILFLLLLLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARAFNRMTDQL----- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 243 vhQRNEAEIGAANRLLDSIVENIPNMIFLKRADDlRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREAL 322
Cdd:COG5000    79 --KEQREELEERRRYLETILENLPAGVIVLDADG-RITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLREALERG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 323 AtagvvdipEEAVDTRQGGRRILHTRKLALRNaqgeaEFLLGMSEDITeakrtaeelqrhrenleqlvevrtaELSHAKE 402
Cdd:COG5000   156 W--------QEEIELTRDGRRTLLVRASPLRD-----DGYVIVFDDIT-------------------------ELLRAER 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 403 AAEAANVAKSaflanMSHEIRTPLNAITGMAHLIRRgGLTDKQDDQLAKLEAA-------GAHLLNIINAILELSKIEAG 475
Cdd:COG5000   198 LAAWGELARR-----IAHEIKNPLTPIQLSAERLRR-KLADKLEEDREDLERAldtiirqVDRLKRIVDEFLDFARLPEP 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 476 KFQlehvPVDVNDLVGNVVTMIQAGAQAKRLRLATEVAPVPGVLYGDPTRLQQALLNYAGNAVKFTEA-GSVTLRVHAVE 554
Cdd:COG5000   272 QLE----PVDLNELLREVLALYEPALKEKDIRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEEgGEIEVSTRRED 347
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590033346 555 EApeavlLRFEVTDTGIGLAPDTLAKLFTAFEqadnsTTRKyGGTGLGLAVTRRLAELMGGGAGAESRPGAGSTFWFT 632
Cdd:COG5000   348 GR-----VRIEVSDNGPGIPEEVLERIFEPFF-----TTKP-KGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIR 414
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
526-635 1.05e-55

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: 186.54  E-value: 1.05e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 526 LQQALLNYAGNAVKFTEAGSVTLRVHAVEEAPEAVLLRFEVTDTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGLGLAV 605
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1590033346 606 TRRLAELMGGGAGAESRPGAGSTFWFTARL 635
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
253-629 2.14e-54

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 191.98  E-value: 2.14e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 253 AANRLLDSIVENIPNMIFLKRADdLRFVLFNRAGERLLGHARQELLGRTEYDLFPaeQADALTARDREALATAGVVDIPE 332
Cdd:COG3852     4 ESEELLRAILDSLPDAVIVLDAD-GRITYVNPAAERLLGLSAEELLGRPLAELFP--EDSPLRELLERALAEGQPVTERE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 333 EAVDTRQGGRRILHTRKLALRNAQGEAEFLLgMSEDITEAKRTAEELQRHrenleqlvevrtaelshakEAAEAAnvakS 412
Cdd:COG3852    81 VTLRRKDGEERPVDVSVSPLRDAEGEGGVLL-VLRDITERKRLERELRRA-------------------EKLAAV----G 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 413 AFLANMSHEIRTPLNAITGMAHLIRRgGLTDKQDDQLAKL-EAAGAHLLNIINAILELSKIEAGKFQlehvPVDVNDLVG 491
Cdd:COG3852   137 ELAAGLAHEIRNPLTGIRGAAQLLER-ELPDDELREYTQLiIEEADRLNNLVDRLLSFSRPRPPERE----PVNLHEVLE 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 492 NVVTMIQAGAqAKRLRLATEVAPVPGVLYGDPTRLQQALLNYAGNAVkftEA----GSVTLRVHAVEEAPEAVL-----L 562
Cdd:COG3852   212 RVLELLRAEA-PKNIRIVRDYDPSLPEVLGDPDQLIQVLLNLVRNAA---EAmpegGTITIRTRVERQVTLGGLrprlyV 287
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590033346 563 RFEVTDTGIGLAPDTLAKLFTAFEqadnsTTRKyGGTGLGLAVTRRLAELMGGGAGAESRPGAGSTF 629
Cdd:COG3852   288 RIEVIDNGPGIPEEILDRIFEPFF-----TTKE-KGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTF 348
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
371-729 2.12e-51

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 193.97  E-value: 2.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 371 EAKRTA-EELQRHRENLEQLVEVRTAELS-------HAKEAAEAANVAKSAFLANMSHEIRTPLNAITGMAHLIRRGGLT 442
Cdd:PRK11466  396 DAFRSNvHALNRHREQLAAQVKARTAELQelviehrQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPAL 475
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 443 DKQDDQLAKLEAAGAHLLNIINAILELSKIEAG--KFQLEHVPVDVNDLVGNVVTMIQAGAQAKRLRLATEVAP-VPGVL 519
Cdd:PRK11466  476 NAQRDDLRAITDSGESLLTILNDILDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADdLPTAL 555
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 520 YGDPTRLQQALLNYAGNAVKFTEAGSVTLRVHAVEEApeavlLRFEVTDTGIGLAPDTLAKLFTAFEQAdnstTRKYGGT 599
Cdd:PRK11466  556 MGDPRRIRQVITNLLSNALRFTDEGSIVLRSRTDGEQ-----WLVEVEDSGCGIDPAKLAEIFQPFVQV----SGKRGGT 626
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 600 GLGLAVTRRLAELMGGGAGAESRPGAGSTFWFtaRLERRAGAGGDAHAVAQSdaeARLLrdhrGARLLLAEDEPINREIT 679
Cdd:PRK11466  627 GLGLTISSRLAQAMGGELSATSTPEVGSCFCL--RLPLRVATAPVPKTVNQA---VRLD----GLRLLLIEDNPLTQRIT 697
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1590033346 680 VLLLDDVGLK-ADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRI 729
Cdd:PRK11466  698 AEMLNTSGAQvVAVGNAAQALETLQNSEPFAAALVDFDLPDYDGITLARQL 748
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
121-632 1.05e-49

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 182.68  E-value: 1.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 121 EELFVAGPDTLTAIRHIDAPDGGRPIYVTVITISTAELNDQKRSILLWGVLGSAFFVLLSSTSIVFLAQRlltRRVDVSL 200
Cdd:COG4251     7 LLLLLLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLA---ALALLLL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 201 GVLKEVEEGDVAARIPVTYSDELGELQAGINSMTAKLGALLAVHQRNEAEIGAANRLLDSIVENIPNMIFLKRADDLRFV 280
Cdd:COG4251    84 LLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 281 LFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALATAGVVDIPEEAVDTRQGGRRILHTRKLALRnaqgeAE 360
Cdd:COG4251   164 LALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLV-----LL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 361 FLLGMSEDITEAKRTAEELQRHRENLEQLVEVRTAELshakeaaEAANVAKSAFLANMSHEIRTPLNAITGMAHLIRR-- 438
Cdd:COG4251   239 LLLILLLLLLILVLELLELRLELEELEEELEERTAEL-------ERSNEELEQFAYVASHDLREPLRKISGFSQLLEEdy 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 439 -GGLTDKQDDQLAKLEAAGAHLLNIINAILELSKIeaGKFQLEHVPVDVNDLVGNVVTMIQAGAQAKRLRLatEVAPVPg 517
Cdd:COG4251   312 gDKLDEEGREYLERIRDAAERMQALIDDLLAYSRV--GRQELEFEPVDLNELLEEVLEDLEPRIEERGAEI--EVGPLP- 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 518 VLYGDPTRLQQALLNYAGNAVKFTEAGSV-TLRVHAVEEAPEAvllRFEVTDTGIGLAPDTLAKLFTAFEQADNSttRKY 596
Cdd:COG4251   387 TVRGDPTLLRQVFQNLISNAIKYSRPGEPpRIEIGAEREGGEW---VFSVRDNGIGIDPEYAEKIFEIFQRLHSR--DEY 461
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 1590033346 597 GGTGLGLAVTRRLAELMGGGAGAESRPGAGSTFWFT 632
Cdd:COG4251   462 EGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFT 497
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
245-632 1.08e-49

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: 182.48  E-value: 1.08e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 245 QRNEAEIGAANRLLDSIVENIPNMIFLKRADDlRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALAT 324
Cdd:COG5809   130 KRMEEALRESEEKFRLIFNHSPDGIIVTDLDG-RIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKD 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 325 AGVVDIpeEAVDTRQGGRRILHTRKLALRNAQGEAEFLLGMSEDITEAKRTAEELQRhrenleqlvevrtaelshakeaA 404
Cdd:COG5809   209 GGIAQG--EVRFWTKDGRWRLLEASGAPIKKNGEVDGIVIIFRDITERKKLEELLRK----------------------S 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 405 EAANVAkSAFLANMSHEIRTPLNAITGMAHLIRrGGLTDKQDDQLAKLEAAGAHLLNIINAILELSKIEAGKFQlehvPV 484
Cdd:COG5809   265 EKLSVV-GELAAGIAHEIRNPLTSLKGFIQLLK-DTIDEEQKTYLDIMLSELDRIESIISEFLVLAKPQAIKYE----PK 338
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 485 DVNDLVGNVVTMIQAGAQAKRLRLATEV-APVPGVlYGDPTRLQQALLNYAGNAVKFTEAGsVTLRVHAVEEAPEAVLLR 563
Cdd:COG5809   339 DLNTLIEEVIPLLQPQALLKNVQIELELeDDIPDI-LGDENQLKQVFINLLKNAIEAMPEG-GNITIETKAEDDDKVVIS 416
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590033346 564 feVTDTGIGLAPDTLAKLFTAFeqadnsTTRKYGGTGLGLAVTRRLAELMGGGAGAESRPGAGSTFWFT 632
Cdd:COG5809   417 --VTDEGCGIPEERLKKLGEPF------YTTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSIT 477
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
403-782 8.03e-48

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 183.25  E-value: 8.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 403 AAEAANVAKSAFLANMSHEIRTPLNAITGMAHLIRRGGLTDKQDDQLAKLEAAGAHLLNIINAILELSKIEAGKFQLE-- 480
Cdd:PRK10841  439 AAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEpr 518
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 481 -HVPVDV-NDLVGNVVTMIQAgaqaKRLRLATEVAP-VPGVLYGDPTRLQQALLNYAGNAVKFTEAGSVTLRVHAVEEap 557
Cdd:PRK10841  519 eFSPREViNHITANYLPLVVK----KRLGLYCFIEPdVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHVRVDGD-- 592
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 558 eavLLRFEVTDTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGLGLAVTRRLAELMGGGAGAESRPGAGSTF-------- 629
Cdd:PRK10841  593 ---YLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFtiriplyg 669
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 630 -----------------WFT---ARLER-------RAGAGGDAHAVAQSDAE------------------ARLLRDHRGA 664
Cdd:PRK10841  670 aqypqkkgveglqgkrcWLAvrnASLEQfletllqRSGIQVQRYEGQEPTPEdvlitddpvqkkwqgravITFCRRHIGI 749
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 -----------------------------------------------------RLLLAEDEPINREitvLLLDDVGlkad 691
Cdd:PRK10841  750 pleiapgewvhstatphelpallariyrielesddsanalpstdkavsdnddmMILVVDDHPINRR---LLADQLG---- 822
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 692 aaadgAEAVAMAEAND--YAL----------ILMDVQMPRLDGLEATRRIRCLPRHagTPILAMTANAFAEDKAVCFAAG 759
Cdd:PRK10841  823 -----SLGYQCKTANDgvDALnvlsknhidiVLTDVNMPNMDGYRLTQRLRQLGLT--LPVIGVTANALAEEKQRCLEAG 895
                         490       500
                  ....*....|....*....|...
gi 1590033346 760 MNDFIAKPVDPDQLYATLLTWLD 782
Cdd:PRK10841  896 MDSCLSKPVTLDVLKQTLTVYAE 918
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
394-777 1.02e-47

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 183.40  E-value: 1.02e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346  394 TAELSHAKEA----AEAANVAKSAFLANMSHEIRTPLNAITGMAHLIRRGGLTDKQDDQLAKLE-AAGAHLLNIINAILE 468
Cdd:PRK09959   691 TRDLIHALEVernkAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAyATGQSLLGLIGEILD 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346  469 LSKIEAGKFQLEHVPVDVNDLVGNVVTMIQAGAQAKRLRLA-TEVAPVPGVLYGDPTRLQQALLNYAGNAVKFTEAGSVT 547
Cdd:PRK09959   771 VDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALScSSTFPDHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVK 850
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346  548 LRVHAVEEAPEAVLLRFEVTDTGIGLAPDTLAKLFTAFEQAdnSTTRKYGGTGLGLAVTRRLAELMGGGAGAESRPGAGS 627
Cdd:PRK09959   851 ITTSLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQT--SAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGT 928
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346  628 TFWFTARLERRAGAggdahAVAQSDAEARLLRDHRgARLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEAND 707
Cdd:PRK09959   929 TFTITIPVEISQQV-----ATVEAKAEQPITLPEK-LSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQH 1002
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346  708 YALILMDVQMPRLDGLEATRRIRclPRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:PRK09959  1003 YDLLITDVNMPNMDGFELTRKLR--EQNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHL 1070
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
256-632 1.75e-38

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 146.87  E-value: 1.75e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 256 RLLDSIVENIPNMIFLKRADDLRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALATAGVVDIPEEAV 335
Cdd:COG4191     3 RLLLLLLLLLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 336 DTRQGGRRILHTRKLALRNAQGEAEFLLGMSEDITEAKRTAEELQRHREnleQLVEV-RTA---ELshakeaaeAANVAk 411
Cdd:COG4191    83 GLLLLLLLEALLLLLLAALDAEENAELEELERDITELERAEEELRELQE---QLVQSeKLAalgEL--------AAGIA- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 412 saflanmsHEIRTPLNAITGMAHLIRRGgLTDKQDDQ-----LAKLEAAGAHLLNIINAILELSKIEAGKFQlehvPVDV 486
Cdd:COG4191   151 --------HEINNPLAAILGNAELLRRR-LEDEPDPEelreaLERILEGAERAAEIVRSLRAFSRRDEEERE----PVDL 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 487 NDLVGNVVTMIQAGAQAKRLRLATEVAPVPGVLYGDPTRLQQALLNYAGNAVK-FTEAGSVTLRVHAVEEAPEAVLlrfE 565
Cdd:COG4191   218 NELIDEALELLRPRLKARGIEVELDLPPDLPPVLGDPGQLEQVLLNLLINAIDaMEEGEGGRITISTRREGDYVVI---S 294
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590033346 566 VTDTGIGLAPDTLAKLFTAFeqadnSTTRKYG-GTGLGLAVTRRLAELMGGGAGAESRPGAGSTFWFT 632
Cdd:COG4191   295 VRDNGPGIPPEVLERIFEPF-----FTTKPVGkGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTIT 357
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
167-643 3.19e-37

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 148.19  E-value: 3.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 167 LWGVLGSAFFVLLSSTSIVFLAQRLLTRRVDVSLGVLKE---VEEGDVAARIPVTySDELGELQAGINSMTAKLgalLAV 243
Cdd:PRK11360  185 AWKMDRRIYAVLAAGLVIGLLLIFLLSRRFSANVDIIKDglsTLENDLSTRLPPL-PGELGEISQAINNLAQAL---RET 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 244 HQRNEAeigaanrLLDSIVENIpnmIFLKRADDLrfVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDreALA 323
Cdd:PRK11360  261 RSLNEL-------ILESIADGV---IAIDRQGKI--TTMNPAAEVITGLQRHELVGKPYSELFPPNTPFASPLLD--TLE 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 324 TAGVVDIPEEAVDTRQGGRRILHTRKLaLRNAQGEAEFLLGMSEDITEAKRTAEELQRhRENLEQLVEVrtaelshakea 403
Cdd:PRK11360  327 HGTEHVDLEISFPGRDRTIELSVSTSL-LHNTHGEMIGALVIFSDLTERKRLQRRVAR-QERLAALGEL----------- 393
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 404 aeAANVAksaflanmsHEIRTPLNAITGMAHLIRrggltdKQDDQLAKLEAAGA------HLLNIINAILELSKIEAGKF 477
Cdd:PRK11360  394 --VAGVA---------HEIRNPLTAIRGYVQIWR------QQTSDPPSQEYLSVvlrevdRLNKVIDQLLEFSRPRESQW 456
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 478 QlehvPVDVNDLVGNVVTMIQAGAQAKRLRLATEVAP-VPGVlYGDPTRLQQALLNYAGNAVK-FTEAGSVTLRVHAVEE 555
Cdd:PRK11360  457 Q----PVSLNALVEEVLQLFQTAGVQARVDFETELDNeLPPI-WADPELLKQVLLNILINAVQaISARGKIRIRTWQYSD 531
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 556 APEAVllrfEVTDTGIGLAPDTLAKLFTAFeqadnsTTRKYGGTGLGLAVTRRLAELMGGGAGAESRPGAGSTfwFTARL 635
Cdd:PRK11360  532 GQVAV----SIEDNGCGIDPELLKKIFDPF------FTTKAKGTGLGLALSQRIINAHGGDIEVESEPGVGTT--FTLYL 599

                  ....*...
gi 1590033346 636 ERRAGAGG 643
Cdd:PRK11360  600 PINPQGNQ 607
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
215-629 1.96e-36

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: 144.10  E-value: 1.96e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 215 IPVTYSDELGELQAGINsmtaklgalLAVHQRNEAEIGAANRLLDSIVENIPNMIFLKRADDlRFVLFNRAGERLLGHAR 294
Cdd:COG5805   125 FPIYNQNGQAAILALRD---------ITKKKKIEEILQEQEERLQTLIENSPDLICVIDTDG-RILFINESIERLFGAPR 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 295 QELLGRTEYDLFPAEQADALTARDREaLATAGVVDIPEEAVDTRQGGRRILHTRKLALRNAQGEAEFLLGMSEDITEAKR 374
Cdd:COG5805   195 EELIGKNLLELLHPCDKEEFKERIES-ITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKE 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 375 TaEELQRHRENLEQLVEVrtaelshakeaaeAANVAksaflanmsHEIRTPLNAITGMAHLIRrGGLTDKQD------DQ 448
Cdd:COG5805   274 A-EELMARSEKLSIAGQL-------------AAGIA---------HEIRNPLTSIKGFLQLLQ-PGIEDKEEyfdimlSE 329
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 449 LAKLEAagahllnIINAILELSKIEAGKFQlehvPVDVNDLVGNVVTMIQAGAQAKRLRLATEV-APVPGVlYGDPTRLQ 527
Cdd:COG5805   330 LDRIES-------IISEFLALAKPQAVNKE----KENINELIQDVVTLLETEAILHNIQIRLELlDEDPFI-YCDENQIK 397
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 528 QALLNYAGNAVKFTEAGSvTLRVHAVEEAPEAVLlrfEVTDTGIGLAPDTLAKLFTAFeqadnsTTRKYGGTGLGLAVTR 607
Cdd:COG5805   398 QVFINLIKNAIEAMPNGG-TITIHTEEEDNSVII---RVIDEGIGIPEERLKKLGEPF------FTTKEKGTGLGLMVSY 467
                         410       420
                  ....*....|....*....|..
gi 1590033346 608 RLAELMGGGAGAESRPGAGSTF 629
Cdd:COG5805   468 KIIENHNGTIDIDSKVGKGTTF 489
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
258-632 6.91e-35

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: 135.80  E-value: 6.91e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 258 LDSIVENIPNMIFLKRADDlRFVLFNRAGERLLG-HARQELLGRTEYDLFPAEQADALTARDREalataGVVDIPEEAvd 336
Cdd:TIGR02966   8 FRAAAQALPDAVVVLDEEG-QIEWCNPAAERLLGlRWPDDLGQRITNLIRHPEFVEYLAAGRFS-----EPLELPSPI-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 337 trqGGRRILHTRKLALrnaqGEAEFLLgMSEDITEAKRtaeelqrhrenLEQLvevrtaelshakeaaeaanvaKSAFLA 416
Cdd:TIGR02966  80 ---NSERVLEIRIAPY----GEEQKLL-VARDVTRLRR-----------LEQM---------------------RRDFVA 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 417 NMSHEIRTPLNAITGMAHLIRRGGLTDKQDDQ--LAKLEAAGAHLLNIINAILELSKIEAGKFQLEHVPVDVNDLVGNVV 494
Cdd:TIGR02966 120 NVSHELRTPLTVLRGYLETLADGPDEDPEEWNraLEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALLDHLR 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 495 TMIQAGAQAKRLRLATEVAPVPGVLyGDPTRLQQALLNYAGNAVKFTEAGSvTLRVHAVEEAPEAvllRFEVTDTGIGLA 574
Cdd:TIGR02966 200 DEAEALSQGKNHQITFEIDGGVDVL-GDEDELRSAFSNLVSNAIKYTPEGG-TITVRWRRDGGGA---EFSVTDTGIGIA 274
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1590033346 575 PDTLAKLFTAFEQADNSTTRKYGGTGLGLAVTRRLAELMGGGAGAESRPGAGSTFWFT 632
Cdd:TIGR02966 275 PEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFSFI 332
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
666-777 1.33e-34

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


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 127.59  E-value: 1.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 666 LLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPR-HAGTPILAMT 744
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGgGRRTPIIALT 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1590033346 745 ANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:cd17546    81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
659-782 3.62e-34

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: 126.89  E-value: 3.62e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 659 RDHRGARLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGT 738
Cdd:COG0784     1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1590033346 739 PILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATLLTWLD 782
Cdd:COG0784    81 PIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLA 124
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
521-636 3.65e-31

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 117.75  E-value: 3.65e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346  521 GDPTRLQQALLNYAGNAVKFTEA-GSVTLRVHAVEEApeavlLRFEVTDTGIGLAPDTLAKLFTAFEQADNsTTRKYGGT 599
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEgGRITVTLERDGDH-----VEITVEDNGPGIPPEDLEKIFEPFFRTDK-RSRKIGGT 74
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1590033346  600 GLGLAVTRRLAELMGGGAGAESRPGAGSTFWFTARLE 636
Cdd:smart00387  75 GLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
664-777 1.33e-27

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: 110.00  E-value: 1.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 664 ARLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGTPILAM 743
Cdd:COG3706     2 ARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIFL 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1590033346 744 TANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:COG3706    82 TALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
521-637 2.81e-27

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: 106.68  E-value: 2.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 521 GDPTRLQQALLNYAGNAVKFT-EAGSVTLRVHAVEEapeavlLRFEVTDTGIGLAPDTLAKLFTAFEQADnstTRKYGGT 599
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAaKAGEITVTLSEGGE------LTLTVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGGT 71
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1590033346 600 GLGLAVTRRLAELMGGGAGAESRPGAGSTFWFTARLER 637
Cdd:pfam02518  72 GLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
205-632 5.45e-26

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


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 113.69  E-value: 5.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 205 EVEEGDVAARIPVTYSDELGELQAGINSMTAKLGALLAVhqrNEAEigaaNRLLDSIvenIPNM----IflkrADD--LR 278
Cdd:NF033092  214 AMAKGDFSRKVKVYGNDEIGQLAEAFNNLTKRLQEAQAT---TESE----RRKLDSV---LSHMtdgvI----ATDrrGR 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 279 FVLFNRAGERLLGHARQELLGRTEYDL--FPAEQADALTARDREALatagVVDIPEEAVDTrqggrrILHtrklalrnA- 355
Cdd:NF033092  280 VILINDPALEMLNVSRETVLGQSILDVlgLEEEYTLRDLLEEQDSL----LLDFSTEEEPL------ILR--------An 341
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 356 ----QGEAEFLLGMS---EDITEAKRTaeELQRhREnleqlvevrtaelshakeaaeaanvaksaFLANMSHEIRTPLna 428
Cdd:NF033092  342 fsviQRESGFINGLIavlHDVTEQEKI--EQER-RE-----------------------------FVANVSHELRTPL-- 387
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 429 iTGM-----AhlirrggLTDK--QDDQLAKleaagaHLLNI-----------INAILELSKIEAGKFQLEHVPVDVNDLV 490
Cdd:NF033092  388 -TTMrsyleA-------LADGawKDPELAP------RFLGVtqnetermirlVNDLLQLSRMDSKDYKLNKEWVNFNEFF 453
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 491 GNVV---TMIqagAQAKRLRLATEVAPVPGVLYGDPTRLQQALLNYAGNAVKFT-EAGSVTLRVHAVEEapeavLLRFEV 566
Cdd:NF033092  454 NYIIdrfEMI---LKNKNITFKREFPKRDLWVEIDTDKITQVLDNIISNAIKYSpEGGTITFRLLETHN-----RIIISI 525
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590033346 567 TDTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGLGLAVTRRLAELMGGGAGAESRPGAGSTFWFT 632
Cdd:NF033092  526 SDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAESEEGKGTTIYFT 591
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
383-629 7.97e-26

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


Pssm-ID: 444508 [Multi-domain]  Cd Length: 412  Bit Score: 110.73  E-value: 7.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 383 RENLEQLVEVRtaelshakeAAEAANVAkSAFLANMSHEIRTPLNAITGMAHLIRRGGLTDKQDDQ-----LAKLEAAGA 457
Cdd:COG5806   183 IENILLRKELQ---------RAEKLEVV-SELAASIAHEVRNPLTVVRGFIQLLQEPELSDEKRKQyiriaLEELDRAEA 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 458 hllnIINAILELSKIEAGKfqleHVPVDVNDLVGNVVTMIQAGAQAKRLRLATEVAPvPGVLYGDPTRLQQALLNYAGNA 537
Cdd:COG5806   253 ----IITDYLTFAKPQPEK----LEKIDVSEELEHVIDVLSPYANMNNVEIQTELEP-GLYIEGDRQKLQQCLINIIKNG 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 538 VKFTEAGSvTLRVHAVEEAPEAVLlrfEVTDTGIGLAPDTLAKLFTAFeqadNSTTRKygGTGLGLAVTRRLAELMGGGA 617
Cdd:COG5806   324 IEAMPNGG-TLTIDVSIDKNKVII---SIKDTGVGMTKEQLERLGEPY----FSTKEK--GTGLGTMVSYRIIEAMNGTI 393
                         250
                  ....*....|..
gi 1590033346 618 GAESRPGAGSTF 629
Cdd:COG5806   394 RVESEVGKGTTF 405
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
409-638 3.92e-25

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 109.49  E-value: 3.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 409 VAKSAFLANMSHEIRTPLNAITGMAHLIRRGGLTDKQDDQLAKLEAAGAHLLN-IINAILELSKieagKFQLEHVPVDVN 487
Cdd:PRK10364  235 VALGHLAAGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVMAKEADRLNrVVSELLELVK----PTHLALQAVDLN 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 488 DLVGNVVTMIQAGAQAKRLRLATEVAPVPGVLYGDPTRLQQALLNYAGNAVK-FTEAGSVTLrvhAVEEAPEAVLLRfeV 566
Cdd:PRK10364  311 DLINHSLQLVSQDANSREIQLRFTANDTLPEIQADPDRLTQVLLNLYLNAIQaIGQHGVISV---TASESGAGVKIS--V 385
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590033346 567 TDTGIGLAPDTLAKLFTAFeqadnsTTRKYGGTGLGLAVTRRLAELMGGGAGAESRPGAGSTF--WFTARLERR 638
Cdd:PRK10364  386 TDSGKGIAADQLEAIFTPY------FTTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFtlWLPVNITRR 453
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
414-642 2.91e-24

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 107.42  E-value: 2.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 414 FLANMSHEIRTPLNAITGMAHLIRrggltdkqdDQLAKLEAA---GAHLLN--------IINAILELSKIEAGKFQLEHV 482
Cdd:NF040691  274 FVSDVSHELRTPLTTIRMAADVIH---------DSRDDFDPAtarSAELLHteldrfesLLSDLLEISRFDAGAAELDVE 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 483 PVDVNDLVGNVVTMIQAGAQAKRLRLATEVAPVPGVLYGDPTRLQQALLNYAGNAVKFTEAGSVTLRVHAveeAPEAVLL 562
Cdd:NF040691  345 PVDLRPLVRRVVDALRQLAERAGVELRVDAPGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTVAQ---DDTAVAV 421
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 563 RfeVTDTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGLGLAVTRRLAELMGGGAGAESRPGAGSTFWFTarLERRAGAG 642
Cdd:NF040691  422 T--VRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLT--LPRVAGDR 497
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
667-777 1.80e-23

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 95.68  E-value: 1.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 667 LLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclPRHAGTPILAMTAN 746
Cdd:pfam00072   2 LIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIR--RRDPTTPVIILTAH 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1590033346 747 AFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:pfam00072  80 GDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
396-626 2.64e-23

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 103.75  E-value: 2.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 396 ELSHAKEAAEAANVAKSAFLANMSHEIRTPLNAITGMAHLIrRGGLTDKQDDQLAKLEAAGAHLLNIINAILELSKIEAG 475
Cdd:NF012163  225 DFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRAELEAI-QDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEG 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 476 KFQLEHVPVDvndlvgnVVTMIQAGAQAKRLRLAT------EVAPVPGVLYGDPTRLQQALLNYAGNAVKFTEAGSvTLR 549
Cdd:NF012163  304 ALAYQKASVD-------LVPLLEVEGGAFRERFASagleleVSLPDSSLVFGDRDRLMQLFNNLLENSLRYTDSGG-SLH 375
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590033346 550 VHAvEEAPEAVLLRFEvtDTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGLGLAVTRRLAELMGGGAGAESRPGAG 626
Cdd:NF012163  376 ISA-SQRPKEVTLTVA--DSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGG 449
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
664-777 7.20e-23

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: 97.33  E-value: 7.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 664 ARLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHagTPILAM 743
Cdd:COG0745     2 PRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSD--IPIIML 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1590033346 744 TANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:COG0745    80 TARDDEEDRVRGLEAGADDYLTKPFDPEELLARI 113
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
665-776 1.73e-22

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 92.99  E-value: 1.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGTPILAMT 744
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALT 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1590033346 745 ANAFAEDKAVCFAAGMNDFIAKPVDPDQLYAT 776
Cdd:cd17548    81 AYAMKGDREKILEAGCDGYISKPIDTREFLET 112
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
417-626 1.84e-22

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 101.46  E-value: 1.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 417 NMSHEIRTPLNAITGMAHLIRRGGLTDKQDDQLAKLEAAGAHLLNIINAILELSKIEAGKFQLEHVPVDVNDLVGNVVTM 496
Cdd:PRK11100  262 TLTHELKSPLAAIRGAAELLQEDPPPEDRARFTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEA 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 497 IQAGAQAKRLRLatEVAPVPGVLYGDPTRLQQALLNYAGNAVKFT-EAGSVTLRVHAVEEAPeavllRFEVTDTGIGlAP 575
Cdd:PRK11100  342 REAQAAAKGITL--RLRPDDARVLGDPFLLRQALGNLLDNAIDFSpEGGTITLSAEVDGEQV-----ALSVEDQGPG-IP 413
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1590033346 576 D-TLAKLFTAFEqadnSTTRKYGG---TGLGLAVTRRLAELMGGGAGAESRPGAG 626
Cdd:PRK11100  414 DyALPRIFERFY----SLPRPANGrksTGLGLAFVREVARLHGGEVTLRNRPEGG 464
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
658-782 3.72e-22

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: 95.62  E-value: 3.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 658 LRDHRGARLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHAG 737
Cdd:COG3437     1 MRTGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1590033346 738 TPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATLLTWLD 782
Cdd:COG3437    81 IPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALE 125
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
522-635 1.98e-20

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


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 87.13  E-value: 1.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 522 DPTRLQQALLNYAGNAVKFTEAGSvTLRVHAVEEaPEAVLLRFEvtDTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGL 601
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTGG-KLRIRAAQT-PQEVRLDVE--DSAPGVSDDQLARLFERFYRVESSRNRASGGSGL 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1590033346 602 GLAVTRRLAELMGGGAGAESRPGAGstFWFTARL 635
Cdd:cd16946    77 GLAICHNIALAHGGTISAEHSPLGG--LRLVLTL 108
PAS COG2202
PAS domain [Signal transduction mechanisms];
246-391 2.26e-20

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 91.62  E-value: 2.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 246 RNEAEIGAANRLLDSIVENIPNMIFLKRADDlRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALATA 325
Cdd:COG2202     1 TAEEALEESERRLRALVESSPDAIIITDLDG-RILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGG 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590033346 326 GVVDIpEEAVDTRQGGRRILHTRKLALRNAQGEAEFLLGMSEDITEAKRTAEELQRHRENLEQLVE 391
Cdd:COG2202    80 GVWRG-ELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVE 144
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
378-632 3.26e-20

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: 94.38  E-value: 3.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 378 ELQRHRENLEQLVEvrtaELSHAKEAAEAANVAKSAFLANMSHEIRTPLNaitgmaHLIRRGGLTDKQDDQLAKLEAAGA 457
Cdd:TIGR01386 212 DPSRAPAELRELAQ----SFNAMLGRLEDAFQRLSQFSADLAHELRTPLT------NLLGQTQVALSQPRTGEEYREVLE 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 458 -------HLLNIINAILELSKIEAGKFQLEHVPVDVNDLVGNVVTMIQAGAQAKRLRLATEVApvpGVLYGDPTRLQQAL 530
Cdd:TIGR01386 282 snleeleRLSRMVSDMLFLARADNGQLALERVRLDLAAELAKVAEYFEPLAEERGVRIRVEGE---GLVRGDPQMFRRAI 358
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 531 LNYAGNAVKFTEAGSvTLRVHaVEEAPEAVLLRfeVTDTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGLGLAVTRRLA 610
Cdd:TIGR01386 359 SNLLSNALRHTPDGG-TITVR-IERRSDEVRVS--VSNPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIM 434
                         250       260
                  ....*....|....*....|..
gi 1590033346 611 ELMGGGAGAESRPGAgSTFWFT 632
Cdd:TIGR01386 435 EAHGGRASAESPDGK-TRFILR 455
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
413-677 5.71e-20

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 95.13  E-value: 5.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 413 AFLANMSHEIRTPLNAITG---MAH-LIRRGGLTDkqdDQLAKLEAAGAHLLNIINAILELSKIEAGKFQlehvPVDVND 488
Cdd:PRK13837  452 TLASGIAHNFNNILGAILGyaeMALnKLARHSRAA---RYIDEIISAGARARLIIDQILAFGRKGERNTK----PFDLSE 524
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 489 LVGNVVTMIQAgAQAKRLRLATEVAPVPGVLYGDPTRLQQALLNYAGNAVK-FTEAGSVTLRV------------HAVEE 555
Cdd:PRK13837  525 LVTEIAPLLRV-SLPPGVELDFDQDQEPAVVEGNPAELQQVLMNLCSNAAQaMDGAGRVDISLsraklrapkvlsHGVLP 603
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 556 APEAVLLRfeVTDTGIGLAPDTLAKLFTAFeqadnSTTRKyGGTGLGLAVTRRLAELMGGGAGAESRPGAGSTfwFTARL 635
Cdd:PRK13837  604 PGRYVLLR--VSDTGAGIDEAVLPHIFEPF-----FTTRA-GGTGLGLATVHGIVSAHAGYIDVQSTVGRGTR--FDVYL 673
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1590033346 636 ERRAGAGGDAHAVAQSDAEARllrdHRGARLLLAEDEPINRE 677
Cdd:PRK13837  674 PPSSKVPVAPQAFFGPGPLPR----GRGETVLLVEPDDATLE 711
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
526-632 2.38e-19

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Methanosaeta harundinacea FilI and some hybrid sensor histidine kinases; This family includes FilI, the histidine kinase (HK) component of FilI-FilRs, a two-component signal transduction system (TCS) of the methanogenic archaeon, Methanosaeta harundinacea, which is involved in regulating methanogenesis. The cytoplasmic HK core consists of a C-terminal HK-like ATPase domain (represented here) and a histidine kinase dimerization and phosphoacceptor domain (HisKA) domain, which, in FilI, are coupled to CHASE, HAMP, PAS, and GAF sensor domains. FilI-FilRs catalyzes the phosphotransfer between FilI (HK) and FilRs (FilR1 and FilR2, response regulators) of the TCS. TCSs are predicted to be of bacterial origin, and acquired by archaea by horizontal gene transfer. This model also includes related HATPase domains such as that of Synechocystis sp. PCC6803 phytochrome-like protein Cph1. Proteins having this HATPase domain and HisKA domain also have accessory sensor domains such as CHASE, GAF, HAMP and PAS; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 83.92  E-value: 2.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 526 LQQALLNYAGNAVKFTEAGSV-TLRVHAVEEAPEAvllRFEVTDTGIGLAPDTLAKLFTAFEQADnsTTRKYGGTGLGLA 604
Cdd:cd16921     1 LGQVLTNLLGNAIKFRRPRRPpRIEVGAEDVGEEW---TFYVRDNGIGIDPEYAEKVFGIFQRLH--SREEYEGTGVGLA 75
                          90       100
                  ....*....|....*....|....*...
gi 1590033346 605 VTRRLAELMGGGAGAESRPGAGSTFWFT 632
Cdd:cd16921    76 IVRKIIERHGGRIWLESEPGEGTTFYFT 103
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
413-626 8.76e-19

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 90.08  E-value: 8.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 413 AFLANMSHEIRTPLNaitgmahlIRRGGLTDKQD-------DQLAKLEAAGAHLLNIINAILELSKIEAGKFQLEHVPVD 485
Cdd:PRK10549  242 DFMADISHELRTPLA--------VLRGELEAIQDgvrkftpESVASLQAEVGTLTKLVDDLHQLSLSDEGALAYRKTPVD 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 486 VNDLVGNVVTMIQAGAQAKRLRLATEVaPVPGVLYGDPTRLQQALLNYAGNAVKFTEAGSvTLRVHAVEEaPEAVLLRFE 565
Cdd:PRK10549  314 LVPLLEVAGGAFRERFASRGLTLQLSL-PDSATVFGDPDRLMQLFNNLLENSLRYTDSGG-SLHISAEQR-DKTLRLTFA 390
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1590033346 566 vtDTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGLGLAVTRRLAELMGGGAGAESRPGAG 626
Cdd:PRK10549  391 --DSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRIIAAHSPFGG 449
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
410-632 5.72e-18

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 87.37  E-value: 5.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 410 AKSAFLANMSHEIRTPLNAITG----MAHLIRRGGLTDK----QDDQLAKLEaagahllNIINAILELSKIEAGkfqleh 481
Cdd:PRK11006  203 ARRNFFANVSHELRTPLTVLQGylemMQDQPLEGALREKalhtMREQTQRME-------GLVKQLLTLSKIEAA------ 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 482 vP-VDVNDLVgNVVTM---IQAGAQA---KRLRLATEVAPVPGVlYGDPTRLQQALLNYAGNAVKFTEAGS-VTLRVHAV 553
Cdd:PRK11006  270 -PtIDLNEKV-DVPMMlrvLEREAQTlsqGKHTITFEVDNSLKV-FGNEDQLRSAISNLVYNAVNHTPEGThITVRWQRV 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 554 EEAPEavllrFEVTDTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGLGLAVTR--------RLAelmgggagAESRPGA 625
Cdd:PRK11006  347 PQGAE-----FSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKhalshhdsRLE--------IESEVGK 413

                  ....*..
gi 1590033346 626 GSTFWFT 632
Cdd:PRK11006  414 GTRFSFV 420
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
667-767 8.42e-18

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 79.19  E-value: 8.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 667 LLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHagTPILAMTAN 746
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPD--IPVIVLTAK 78
                          90       100
                  ....*....|....*....|.
gi 1590033346 747 AFAEDKAVCFAAGMNDFIAKP 767
Cdd:cd00156    79 ADEEDAVRALELGADDYLVKP 99
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
410-475 1.58e-17

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 77.25  E-value: 1.58e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590033346 410 AKSAFLANMSHEIRTPLNAITGMAHLIRRGGLTDKQDDQLAKLEAAGAHLLNIINAILELSKIEAG 475
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
410-475 1.98e-17

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 76.84  E-value: 1.98e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590033346  410 AKSAFLANMSHEIRTPLNAITGMAHLIRRGGLTDKQDDQLAKLEAAGAHLLNIINAILELSKIEAG 475
Cdd:smart00388   1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
PRK10490 PRK10490
sensor protein KdpD; Provisional
386-636 6.98e-17

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 85.47  E-value: 6.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 386 LEQLVEVRTAELshAKEAAEAANVaKSAFLANMSHEIRTPLNAITGMAH-----LIRRGGLTDKQDDQLAKleaagaHLL 460
Cdd:PRK10490  642 LERLTLTASEEQ--ARLASEREQL-RNALLAALSHDLRTPLTVLFGQAEiltldLASEGSPHARQASEIRQ------QVL 712
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 461 N---IINAILELSKIEAGKFQLEHVPVDVNDLVGNVVTMIQAGAQAKRLRLATevaPVPGVL-YGDPTRLQQALLNYAGN 536
Cdd:PRK10490  713 NttrLVNNLLDMARIQSGGFNLRKEWLTLEEVVGSALQMLEPGLSGHPINLSL---PEPLTLiHVDGPLFERVLINLLEN 789
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 537 AVKFT-EAGSVTLRVHAVEEApeavlLRFEVTDTGIGLAPDTLAKLFTAFEQADNSTTrkYGGTGLGLAVTRRLAELMGG 615
Cdd:PRK10490  790 AVKYAgAQAEIGIDAHVEGER-----LQLDVWDNGPGIPPGQEQLIFDKFARGNKESA--IPGVGLGLAICRAIVEVHGG 862
                         250       260
                  ....*....|....*....|.
gi 1590033346 616 GAGAESRPGAGSTFWFTARLE 636
Cdd:PRK10490  863 TIWAENRPEGGACFRVTLPLE 883
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
664-773 1.43e-16

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: 76.33  E-value: 1.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 664 ARLLLAEDEPINREI-TVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGTPILA 742
Cdd:cd17551     1 MRILIVDDNPTNLLLlEALLRSAGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVM 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1590033346 743 MTANafaEDKAVC---FAAGMNDFIAKPVDPDQL 773
Cdd:cd17551    81 ITAD---TDREVRlraLEAGATDFLTKPFDPVEL 111
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
262-374 1.52e-16

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 75.91  E-value: 1.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 262 VENIPNMIFLKrADDLRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALATAGVVDIPEEAVDTrqGG 341
Cdd:pfam08448   1 LDSLPDALAVL-DPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLEELLLN--GE 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1590033346 342 RRILHTRKLALRNAQGEAEFLLGMSEDITEAKR 374
Cdd:pfam08448  78 ERHYELRLTPLRDPDGEVIGVLVISRDITERRR 110
PRK09303 PRK09303
histidine kinase;
356-632 1.73e-16

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 82.31  E-value: 1.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 356 QGEAEFLLGMSED-----ITEAKRTAEELQ---------RHRENL-EQLvevrtaelsHAKEAaeaanvaksaFLANMSH 420
Cdd:PRK09303  100 QQEGATYSGLGENlqpseIDSGRYSQELLQlsdelfvlrQENETLlEQL---------KFKDR----------VLAMLAH 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 421 EIRTPLNAiTGMA----HLIRRGGLTDKQDDQLAKLEAAGAHLLNIINA----ILELSKIEAGKFQLEHVPVDVNDLVGN 492
Cdd:PRK09303  161 DLRTPLTA-ASLAletlELGQIDEDTELKPALIEQLQDQARRQLEEIERlitdLLEVGRTRWEALRFNPQKLDLGSLCQE 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 493 VVTMIQAGAQAKRLRLATEVAP-VPGVlYGDPTRLQQALLNYAGNAVKFTEA-GSVTLrvhaveeapeAVLLR------F 564
Cdd:PRK09303  240 VILELEKRWLAKSLEIQTDIPSdLPSV-YADQERIRQVLLNLLDNAIKYTPEgGTITL----------SMLHRttqkvqV 308
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 565 EVTDTGIGLAPDTLAKLFT-AFE-QADNSTTrkygGTGLGLAVTRRLAELMGGGAGAESRPGAGSTFWFT 632
Cdd:PRK09303  309 SICDTGPGIPEEEQERIFEdRVRlPRDEGTE----GYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFT 374
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
410-731 2.54e-16

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 83.44  E-value: 2.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 410 AKSAFLANMSHEIRTPLNAITGMAHLIRRGGLTDKQDDQLAKLEAAGAHLLNIINAILELSKIEAGKFQLEHVPVDVNDL 489
Cdd:PRK10618  449 ARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNMLETQDWKPEQELFSLQDL 528
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 490 VGNVVTMIQAGAQAKRLRLATEVAPVPGVLY-GDPTRLQQA---LLNYagnAVKFTEAGSVTLRVHAVEEAPEavLLRFE 565
Cdd:PRK10618  529 IDEVLPEVLPAIKRKGLQLLIHNHLKAEQLRiGDRDALRKIlllLLNY---AITTTAYGKITLEVDQDESSPD--RLTIR 603
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 566 VTDTGIGLAPDTLAKL---FTAFEQADnsttrKYG-GTGLGLAVTRRLAELMGGGAGAESRPGAGSTFWFTARLErraga 641
Cdd:PRK10618  604 ILDTGAGVSIKELDNLhfpFLNQTQGD-----RYGkASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLKML----- 673
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 642 ggdAHAVAQSDAEARLLRD---------------------HRGARLLLAEDEPINREITVLLLDDvglkadaaadgaeav 700
Cdd:PRK10618  674 ---AADPEVEEEEEKLLDGvtvllditseevrkivtrqleNWGATCITPDERLISQEYDIFLTDN--------------- 735
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1590033346 701 aMAEANDYALILMDvqmpRLDGLE--ATRRIRC 731
Cdd:PRK10618  736 -PSNLTASTLLLSD----DESGFRqiGPGQLRV 763
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
526-632 8.09e-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: 73.58  E-value: 8.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 526 LQQALLNYAGNAVKFTEAGSVTLRVHAVEEAPEAV-LLRFEVTDTGIGLAPDTLAKLFTAFeqadnsTTRKYGGTGLGLA 604
Cdd:cd16920     1 IQQVLINLVRNGIEAMSEGGCERRELTIRTSPADDrAVTISVKDTGPGIAEEVAGQLFDPF------YTTKSEGLGMGLS 74
                          90       100
                  ....*....|....*....|....*...
gi 1590033346 605 VTRRLAELMGGGAGAESRPGAGSTFWFT 632
Cdd:cd16920    75 ICRSIIEAHGGRLSVESPAGGGATFQFT 102
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
667-777 1.34e-15

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: 73.26  E-value: 1.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 667 LLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGTPILAMTAN 746
Cdd:cd17580     2 LVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTGY 81
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1590033346 747 AFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:cd17580    82 GQPEDRERALEAGFDAHLVKPVDPDELIELI 112
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
522-629 9.02e-15

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: 70.98  E-value: 9.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 522 DPTRLQQALLNYAGNAVKFTEAGSvtlRVHAVEEAPEAVLLRFEVTDTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGL 601
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTPDGG---RIRCILEKFRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGL 77
                          90       100
                  ....*....|....*....|....*...
gi 1590033346 602 GLAVTRRLAELMGGGAGAESRPGAGSTF 629
Cdd:cd16925    78 GLSIVKEFVELHGGTVTVSDAPGGGALF 105
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
521-630 4.25e-14

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: 68.97  E-value: 4.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 521 GDPTRLQQALLNYAGNAVKFTEAGSvtlRVHAVEEAPEAVLLRfeVTDTGIGLAPDTLAKLFTAFEQADNSTtrkYGGTG 600
Cdd:cd16940     9 GDALLLFLLLRNLVDNAVRYSPQGS---RVEIKLSADDGAVIR--VEDNGPGIDEEELEALFERFYRSDGQN---YGGSG 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1590033346 601 LGLAVTRRLAELMGGGAGAESRPGAGSTFW 630
Cdd:cd16940    81 LGLSIVKRIVELHGGQIFLGNAQGGGLEAW 110
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
662-777 4.39e-14

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: 75.00  E-value: 4.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 662 RGARLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclPRHAGTPIL 741
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELR--ALDPDLPVI 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1590033346 742 AMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:COG2204    79 LLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAV 114
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
386-639 4.39e-14

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 75.58  E-value: 4.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 386 LEQLVevrtAELSHAKEAAEAANVAKSAFLANMSHEIRTPL-NAITGMAHLIRRGGLTDKQDDQL-AKLEAAGaHLLNII 463
Cdd:PRK09835  241 LEQLV----LSFNHMIERIEDVFTRQSNFSADIAHEIRTPItNLITQTEIALSQSRSQKELEDVLySNLEELT-RMAKMV 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 464 NAILELSKIEAGKFQLEHVPVDVNDLVGNVVTMIQAGAQAKRLRLATEVAPVpgVLYGDPTRLQQALLNYAGNAVKFTEA 543
Cdd:PRK09835  316 SDMLFLAQADNNQLIPEKKMLDLADEVGKVFDFFEAWAEERGVELRFVGDPC--QVAGDPLMLRRAISNLLSNALRYTPA 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 544 G-SVTLRVHAVEEAPEAVllrfeVTDTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGLGLAVTRRLAELMGGGAGAESR 622
Cdd:PRK09835  394 GeAITVRCQEVDHQVQLV-----VENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSD 468
                         250
                  ....*....|....*..
gi 1590033346 623 PGAGStfwFTARLERRA 639
Cdd:PRK09835  469 ARGTR---FVISLPRLE 482
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
260-379 1.55e-13

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 67.70  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 260 SIVENIPNMIFLKRADDlRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALATAGVVDIPEEAVDTRQ 339
Cdd:TIGR00229   7 AIFESSPDAIIVIDLEG-NILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRVRRKD 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1590033346 340 GGRRILHTRkLALRNAQGEAEFLLGMSEDITEAKRTAEEL 379
Cdd:TIGR00229  86 GSEIWVEVS-VSPIRTNGGELGVVGIVRDITERKEAEEAL 124
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
667-767 1.68e-13

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: 67.05  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 667 LLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHagTPILAMTAN 746
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSD--IPIIMLTAK 78
                          90       100
                  ....*....|....*....|.
gi 1590033346 747 AFAEDKAVCFAAGMNDFIAKP 767
Cdd:cd17574    79 DEEEDKVLGLELGADDYITKP 99
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
408-471 1.79e-13

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


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 65.70  E-value: 1.79e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1590033346 408 NVAKSAFLANMSHEIRTPLNAITGMAHLIRRGGL-TDKQDDQLAKLEAAGAHLLNIINAILELSK 471
Cdd:cd00082     1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLdDEEQREYLERIREEAERLLRLINDLLDLSR 65
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
665-782 2.36e-13

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 67.69  E-value: 2.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDDVGLKADAAADGAEA--VAMAEANDYALILMDVQMPRLDGLEATRRIRClpRHAGTPILA 742
Cdd:COG4565     5 RVLIVEDDPMVAELLRRYLERLPGFEVVGVASSGEeaLALLAEHRPDLILLDIYLPDGDGLELLRELRA--RGPDVDVIV 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1590033346 743 MTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATLLTWLD 782
Cdd:COG4565    83 ITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLE 122
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
526-631 2.55e-13

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


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 66.84  E-value: 2.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 526 LQQALLNYAGNAVKFT-EAGSVTLRVHAVEEAPeavllRFEVTDTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGLGLA 604
Cdd:cd16952     1 LRSAFSNLVSNAVKYTpPSDTITVRWSQEESGA-----RLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLA 75
                          90       100
                  ....*....|....*....|....*..
gi 1590033346 605 VTRRLAELMGGGAGAESRPGAGSTFWF 631
Cdd:cd16952    76 IVKHVMSRHDARLLIASELGKGSRFTC 102
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
703-777 3.15e-13

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: 66.94  E-value: 3.15e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1590033346 703 AEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:cd17562    40 AQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILMLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVV 114
PRK13557 PRK13557
histidine kinase; Provisional
273-773 3.37e-13

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 72.78  E-value: 3.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 273 RADDLRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALATAgvVDIPEEAVDTRQGGRRILHtrklAL 352
Cdd:PRK13557   49 NQPDNPIVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDRATVAEVRDAIAER--REIATEILNYRKDGSSFWN----AL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 353 -----RNAQGEAEFLLGMSEDITEaKRTAEELQRHRENLEQLvevrtAELShakeaaeaanvaksaflANMSHEIRTPLN 427
Cdd:PRK13557  123 fvspvYNDAGDLVYFFGSQLDVSR-RRDAEDALRQAQKMEAL-----GQLT-----------------GGIAHDFNNLLQ 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 428 AITGMAHLIrrGGLTDKQDDQLAKLEAAGAHLLNIINAILELSK---IEAGKFQLEHVPVDVNDLVGNVVTMiqagaqAK 504
Cdd:PRK13557  180 VMSGYLDVI--QAALSHPDADRGRMARSVENIRAAAERAATLTQqllAFARKQRLEGRVLNLNGLVSGMGEL------AE 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 505 R-----LRLATEVAPVPGVLYGDPTRLQQALLNYAGNAVK-FTEAGSVTLRVHAVEEAPEAVLL-------RF---EVTD 568
Cdd:PRK13557  252 RtlgdaVTIETDLAPDLWNCRIDPTQAEVALLNVLINARDaMPEGGRVTIRTRNVEIEDEDLAMyhglppgRYvsiAVTD 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 569 TGIGLAPDTLAKLFTAFeqadnSTTRKYG-GTGLGLAVTRRLAELMGGGAGAESRPGAGST--FWFTArlerragAGGDA 645
Cdd:PRK13557  332 TGSGMPPEILARVMDPF-----FTTKEEGkGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTvrLYFPA-------SDQAE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 646 HAVAQSDAEARllRDHRGARLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEAN-DYALILMDVQMP-RLDGL 723
Cdd:PRK13557  400 NPEQEPKARAI--DRGGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHpEVDLLFTDLIMPgGMNGV 477
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1590033346 724 EATRRIRclPRHAGTPILAMTanAFAEDKAVCFAAGMNDF--IAKPVDPDQL 773
Cdd:PRK13557  478 MLAREAR--RRQPKIKVLLTT--GYAEASIERTDAGGSEFdiLNKPYRRAEL 525
PRK10604 PRK10604
sensor protein RstB; Provisional
409-631 4.17e-13

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 72.33  E-value: 4.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 409 VAKSAFLANMSHEIRTPLnaitgmAHLIRRGGLTDK-QDDQLAKLEAAGAHLLNIINAILELSKIEAGKFQLEHVPVDVN 487
Cdd:PRK10604  210 ASKKQLIDGIAHELRTPL------VRLRYRLEMSDNlSAAESQALNRDIGQLEALIEELLTYARLDRPQNELHLSEPDLP 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 488 DLVGNVVTMIQAGAQAKRLRLatEVAPVPGVLYGDPTRLQQALLNYAGNAVKFTEAgsvTLRVHAVEEAPEAVLlrfEVT 567
Cdd:PRK10604  284 AWLSTHLADIQAVTPEKTVRL--DTPHQGDYGALDMRLMERVLDNLLNNALRYAHS---RVRVSLLLDGNQACL---IVE 355
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590033346 568 DTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGLGLAVTRRLAELMGGGAGAESRPGAGSTFWF 631
Cdd:PRK10604  356 DDGPGIPPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSF 419
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
666-768 6.49e-13

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: 65.22  E-value: 6.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 666 LLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGTPILAMTA 745
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTA 80
                          90       100
                  ....*....|....*....|...
gi 1590033346 746 NAFAEDKAVCFAAGMNDFIAKPV 768
Cdd:cd19920    81 LTDTEDKVKGFELGAVDYITKPF 103
PAS COG2202
PAS domain [Signal transduction mechanisms];
246-379 9.70e-13

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 68.90  E-value: 9.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 246 RNEAEIGAANRLLDSIVENIPNMIFLKRADdLRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALATA 325
Cdd:COG2202   127 RAEEALRESEERLRLLVENAPDGIFVLDLD-GRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGG 205
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1590033346 326 GVVDIPEEAVDTRQGGRRILHTRKLALRNaQGEAEFLLGMSEDITEAKRTAEEL 379
Cdd:COG2202   206 RESYELELRLKDGDGRWVWVEASAVPLRD-GGEVIGVLGIVRDITERKRAEEAL 258
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
667-775 1.24e-12

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: 64.99  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 667 LLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGTPILAMTAN 746
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAK 80
                          90       100
                  ....*....|....*....|....*....
gi 1590033346 747 AFAEDKAVCFAAGMNDFIAKPVDPDQLYA 775
Cdd:cd19937    81 GEEFDKVLGLELGADDYITKPFSPRELLA 109
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
415-606 1.88e-12

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 70.35  E-value: 1.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 415 LANMSHEIRTPLNAITGMAHLIRRggltdKQDD--QLAKLEAAGAHLLNIINAILELSKIEAgKFQLEHVPVDVNDLVGN 492
Cdd:PRK09470  247 LSDISHELRTPLTRLQLATALLRR-----RQGEskELERIETEAQRLDSMINDLLVLSRNQQ-KNHLERETFKANSLWSE 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 493 VVTMIQAGAQAKRLRLATEVAPVPGVLYGDPTRLQQALLNYAGNAVKFTEAgSVTLRVHAVEEApeavlLRFEVTDTGIG 572
Cdd:PRK09470  321 VLEDAKFEAEQMGKSLTVSAPPGPWPINGNPNALASALENIVRNALRYSHT-KIEVAFSVDKDG-----LTITVDDDGPG 394
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1590033346 573 LAPDTLAKLFTAFEQADNSTTRKYGGTGLGLAVT 606
Cdd:PRK09470  395 VPEEEREQIFRPFYRVDEARDRESGGTGLGLAIV 428
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
526-626 1.98e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA; This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain.


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 63.88  E-value: 1.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 526 LQQALLNYAGNAVKFteagsvtlrvhaveeAPEAVLLRFE---------VTDTGIGLAPDTLAKLFTAFEQADNSTTRKY 596
Cdd:cd16949     1 LARALENVLRNALRY---------------SPSKILLDISqdgdqwtitITDDGPGVPEDQLEQIFLPFYRVDSARDRES 65
                          90       100       110
                  ....*....|....*....|....*....|
gi 1590033346 597 GGTGLGLAVTRRLAELMGGGAGAESRPGAG 626
Cdd:cd16949    66 GGTGLGLAIAERAIEQHGGKIKASNRKPGG 95
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
665-768 2.04e-12

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: 64.06  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGTPILAMT 744
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                          90       100
                  ....*....|....*....|....
gi 1590033346 745 ANAFAEDKAVCFAAGMNDFIAKPV 768
Cdd:cd17538    81 ALDDREDRIRGLEAGADDFLSKPI 104
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
374-615 3.50e-12

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 69.72  E-value: 3.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 374 RTAEELQRHRENLEQLVEVRTAELSHAKEAA--------EAANVAKSAFLA----NMSHEIRTPLNAITGMAHLIRRGgL 441
Cdd:COG4192   384 RIARLLRVFRDQAIEKTQELETEIEERKRIEknlrqtqdELIQAAKMAVVGqtmtSLAHELNQPLNAMSMYLFSAKKA-L 462
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 442 TDKQDDQLA----KLEAAGAHLLNIINAILELSKieagKFQLEHVPVDVNDLVGNVVTMIQAgaQAKRLRlATEVAPVPG 517
Cdd:COG4192   463 EQENYAQLPtsldKIEGLIERMDKIIKSLRQFSR----KSDTPLQPVDLRQVIEQAWELVES--RAKPQQ-ITLHIPDDL 535
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 518 VLYGDPTRLQQALLNYAGNAVkftEAgSVTLRVHAVEEAPEAVLLRFEVTDTGIGLApdTLAKLFTAFeqadnsTTRKYG 597
Cdd:COG4192   536 MVQGDQVLLEQVLVNLLVNAL---DA-VATQPQISVDLLSNAENLRVAISDNGNGWP--LVDKLFTPF------TTTKEV 603
                         250
                  ....*....|....*...
gi 1590033346 598 GTGLGLAVTRRLAELMGG 615
Cdd:COG4192   604 GLGLGLSICRSIMQQFGG 621
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
665-768 4.38e-12

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: 63.57  E-value: 4.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDDVGLKADAAADGAE--AVAMAEANDYALILMDVQMPRLDGLEATRRIRCL-PRHAGTPIL 741
Cdd:cd19933     2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEEclNLLASAEHSFQLVLLDLCMPEMDGFEVALRIRKLfGRRERPLIV 81
                          90       100
                  ....*....|....*....|....*..
gi 1590033346 742 AMTANAFAEDKAVCFAAGMNDFIAKPV 768
Cdd:cd19933    82 ALTANTDDSTREKCLSLGMNGVITKPV 108
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
523-629 4.74e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 AtoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli AtoS, an HK of the AtoS-AtoC TCS. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have accessory domains such as HAMP or PAS sensor domains or CBS-pair domains.


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 63.21  E-value: 4.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 523 PTRLQQALLNYAGNAVKFTEA-GSVTLRVHAVEEApeavlLRFEVTDTGIGLAPDTLAKLFTAFeqadnSTTRKYG-GTG 600
Cdd:cd16943     1 PSQLNQVLLNLLVNAAQAMEGrGRITIRTWAHVDQ-----VLIEVEDTGSGIDPEILGRIFDPF-----FTTKPVGeGTG 70
                          90       100
                  ....*....|....*....|....*....
gi 1590033346 601 LGLAVTRRLAELMGGGAGAESRPGAGSTF 629
Cdd:cd16943    71 LGLSLSYRIIQKHGGTIRVASVPGGGTRF 99
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
256-369 1.22e-11

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 62.05  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 256 RLLDSIVENIPNMIFLkRADDLRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALATAGVVDIPEEAV 335
Cdd:pfam00989   1 EDLRAILESLPDGIFV-VDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSF 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1590033346 336 DTRQGGRRILHTRKLALRNAQGEAEFLLGMSEDI 369
Cdd:pfam00989  80 RVPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
664-775 1.96e-11

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: 61.50  E-value: 1.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 664 ARLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGTPILAM 743
Cdd:cd17618     1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIML 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1590033346 744 TANAFAEDKAVCFAAGMNDFIAKPVDPDQLYA 775
Cdd:cd17618    81 TARGEEEDKVRGLEAGADDYITKPFSPRELVA 112
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
526-632 2.52e-11

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


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 60.91  E-value: 2.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 526 LQQALLNYAGNAVKFTEAgsvTLRVHAVEEAPEAVLlrfEVTDTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGLGLAV 605
Cdd:cd16939     1 MARALDNLLRNALRYAHR---TVRIALLVSGGRLTL---IVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAI 74
                          90       100
                  ....*....|....*....|....*..
gi 1590033346 606 TRRLAELMGGGAGAESRPGAGSTFWFT 632
Cdd:cd16939    75 VHRVALWHGGHVECDDSELGGACFRLT 101
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
526-629 2.61e-11

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: 61.24  E-value: 2.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 526 LQQALLNYAGNAVK-FTEAGSVTLRV----------HAVEEAPEAVLLRFEVTDTGIGLAPDTLAKLFTAFeqadnSTTR 594
Cdd:cd16919     1 LELAILNLAVNARDaMPEGGRLTIETsnqrvdadyaLNYRDLIPGNYVCLEVSDTGSGMPAEVLRRAFEPF-----FTTK 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1590033346 595 KYG-GTGLGLAVTRRLAELMGGGAGAESRPGAGSTF 629
Cdd:cd16919    76 EVGkGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTV 111
PRK10337 PRK10337
sensor protein QseC; Provisional
414-626 3.41e-11

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 66.21  E-value: 3.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 414 FLANMSHEIRTPLNAI---TGMAHLirrggltdKQDDQ------LAKLEAAGAHLLNIINAILELSKIEAGKFQLEHVPV 484
Cdd:PRK10337  240 FTSDAAHELRSPLAALkvqTEVAQL--------SDDDPqarkkaLLQLHAGIDRATRLVDQLLTLSRLDSLDNLQDVAEI 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 485 DVNDLVGNVVTMIQAGAQAKRLRLATEVAPVPGVLYGDPTRLQQALLNYAGNAVKFTEAGS-VTLRVHAveeapeavlLR 563
Cdd:PRK10337  312 PLEDLLQSAVMDIYHTAQQAGIDVRLTLNAHPVIRTGQPLLLSLLVRNLLDNAIRYSPQGSvVDVTLNA---------RN 382
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590033346 564 FEVTDTGIGLAPDTLAKLFTAFEQADNSTTrkyGGTGLGLAVTRRLAELMGGGAGAESRPGAG 626
Cdd:PRK10337  383 FTVRDNGPGVTPEALARIGERFYRPPGQEA---TGSGLGLSIVRRIAKLHGMNVSFGNAPEGG 442
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
665-773 1.40e-10

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: 59.27  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDDVGLKADAAADG-AEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGTPILAM 743
Cdd:cd19923     2 KVLVVDDFSTMRRIIKNLLKELGFNNVEEAEDgVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLMV 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 1590033346 744 TANAFAEDKAVCFAAGMNDFIAKPVDPDQL 773
Cdd:cd19923    82 TAEAKKENVIAAAQAGVNNYIVKPFTAATL 111
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
665-773 1.53e-10

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: 59.35  E-value: 1.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDDVGLKADAAADGAEavamAEANDY-------------ALILMDVQMPRLDGLEATRRIRC 731
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGVPNELHVVRDG----EEALDFlrgegeyadaprpDLILLDLNMPRMDGFEVLREIKA 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1590033346 732 LPRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQL 773
Cdd:cd17557    77 DPDLRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEF 118
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
665-767 4.54e-10

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: 57.09  E-value: 4.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDD------VG--------LKadaaadgaeavaMAEANDYALILMDVQMPRLDGLEATRRIR 730
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWeagfevVGeaengeeaLE------------LLEEHKPDLVITDINMPGMDGLELLEAIR 68
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1590033346 731 clPRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKP 767
Cdd:COG4753    69 --ELDPDTKIIILSGYSDFEYAQEAIKLGADDYLLKP 103
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
667-775 7.20e-10

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


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 57.23  E-value: 7.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 667 LLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclPRHAGTPILAMTAN 746
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLR--EEGIETPVLLLTAL 78
                          90       100
                  ....*....|....*....|....*....
gi 1590033346 747 AFAEDKAVCFAAGMNDFIAKPVDPDQLYA 775
Cdd:cd17625    79 DAVEDRVKGLDLGADDYLPKPFSLAELLA 107
envZ PRK09467
osmolarity sensor protein; Provisional
415-608 7.43e-10

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 61.85  E-value: 7.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 415 LANMSHEIRTPLNAI---TGMahlirrgglTDKQDDQLAKleaagahllNII------NAILE--LSKIEAGKfQLEHVP 483
Cdd:PRK09467  233 MAGVSHDLRTPLTRIrlaTEM---------MSEEDGYLAE---------SINkdieecNAIIEqfIDYLRTGQ-EMPMEM 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 484 VDVNDLVGNVVTmiqagAQAKRLR-LATEVAPVPGVLYGDPTRLQQALLNYAGNAVKFTEaGSVtlrvhAVEEAPEAVLL 562
Cdd:PRK09467  294 ADLNALLGEVIA-----AESGYEReIETALQPGPIEVPMNPIAIKRALANLVVNAARYGN-GWI-----KVSSGTEGKRA 362
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1590033346 563 RFEVTDTGIGLAPDTLAKLFTAFEQADnsTTRKYGGTGLGLAVTRR 608
Cdd:PRK09467  363 WFQVEDDGPGIPPEQLKHLFQPFTRGD--SARGSSGTGLGLAIVKR 406
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
515-629 7.69e-10

Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related domains; This family includes the histidine kinase-like ATPase domains (HATPase) of three out of the five receptors that recognize the plant hormone ethylene in Arabidopsis thaliana. These three proteins have been classified as belonging to subfamily 2: ETR2, ERS2, and EIN4. They lack most of the motifs characteristic of histidine kinases, and EIN4 is the only one in this group containing the conserved histidine that is phosphorylated in two-component and phosphorelay systems. This family also includes the HATPase domains of Escherichia coli RcsD phosphotransferase which is a component of the Rcs-signaling system, a complex multistep phosphorelay involving five proteins, and is involved in many transcriptional networks such as cell division, biofilm formation, and virulence, among others. Also included is Schizosaccharomyces pombe Mak3 (Phk1) which participates in a multi-step two-component related system which regulates H2O2-induced activation of the Sty1 stress-activated protein kinase pathway. Most proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a GAF sensor domain; most are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340415 [Multi-domain]  Cd Length: 133  Bit Score: 57.47  E-value: 7.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 515 VPGVLYGDPTRLQQALLNYAGNAVKFTE-AGSVTLRV---------HAVEEAP-------EAVLLRFEVTDTGIGLAPDT 577
Cdd:cd16938     1 LPDVVVGDERRVFQVLLHMLGNLLKMRNgGGNITFRVfleggsedrSDRDWGPwrpsmsdESVEIRFEVEINDSGSPSIE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1590033346 578 LAKLFtafeqadNSTTRKYG----GTGLGLAVTRRLAELMGGGAGAESRPGAGSTF 629
Cdd:cd16938    81 SASMR-------NSLNRRYNlselGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTM 129
PRK13560 PRK13560
hypothetical protein; Provisional
245-391 1.61e-09

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 61.61  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 245 QRNEAEIGAANRLLDSIVENIPNMIFLKRADDLRFVLfNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALAT 324
Cdd:PRK13560  193 KRAEERIDEALHFLQQLLDNIADPAFWKDEDAKVFGC-NDAACLACGFRREEIIGMSIHDFAPAQPADDYQEADAAKFDA 271
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590033346 325 AGvVDIPEEAVDTRQGGRRILHTR--KLALRNAQGEAEFLLGMSEDITEAKRTAEELQRHRENLEQLVE 391
Cdd:PRK13560  272 DG-SQIIEAEFQNKDGRTRPVDVIfnHAEFDDKENHCAGLVGAITDISGRRAAERELLEKEDMLRAIIE 339
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
702-767 2.64e-09

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


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 55.14  E-value: 2.64e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590033346 702 MAEANDYALILMDVQMPRLDGLEATRRIRclPRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKP 767
Cdd:cd19935    37 LALTNEYDLIILDVMLPGLDGLEVLRRLR--AAGKQTPVLMLTARDSVEDRVKGLDLGADDYLVKP 100
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
662-777 3.44e-09

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


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 57.27  E-value: 3.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 662 RGARLLLAEDEPINREITVLLLDDVGLK-ADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclpRHAGTPI 740
Cdd:COG3707     2 RGLRVLVVDDEPLRRADLREGLREAGYEvVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQIS---EERPAPV 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1590033346 741 LAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:COG3707    79 ILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPAL 115
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
710-767 3.48e-09

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: 55.48  E-value: 3.48e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 710 LILMDVQMPRLDGLEATRRIRclpRHAGTPILAMTANAFAEDKAV--CFAAGMNDFIAKP 767
Cdd:cd17541    49 VITLDIEMPVMDGLEALRRIM---AERPTPVVMVSSLTEEGAEITleALELGAVDFIAKP 105
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
521-629 4.73e-09

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: 55.21  E-value: 4.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 521 GDPTRLQQALLNYAGNAVKFTEAG---SVTLRVhavEEAPEAVllrfEVTDTGIGLAPDTLAKLFTAFEQADNSTTRKYG 597
Cdd:cd16947    16 ANTEALQRILKNLISNAIKYGSDGkflGMTLRE---DEKHVYI----DIWDKGKGISETEKDHVFERLYTLEDSRNSAKQ 88
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1590033346 598 GTGLGLAVTRRLAELMGGGAGAESRPGAGSTF 629
Cdd:cd16947    89 GNGLGLTITKRLAESMGGSIYVNSKPYEKTVF 120
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
246-635 5.15e-09

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 59.09  E-value: 5.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 246 RNEAEIGAANRLLDSIVENIPNMIFLKRADDlRFVLFNRAGERLLGharQELLGRTEYDLFPAeqadaltardrealata 325
Cdd:COG3290    74 KLLEEIARLVEEREAVLESIREGVIAVDRDG-RITLINDAARRLLG---LDAIGRPIDEVLAE----------------- 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 326 gVVDIPEEAVDTRQGGRRILHTRKLALRNaqGEAEFLLGMSEDITEAKRTAEELqrhrENLEQLVEVrtaelshakeaae 405
Cdd:COG3290   133 -VLETGERDEEILLNGRVLVVNRVPIRDD--GRVVGAVATFRDRTELERLEEEL----EGVKELAEA------------- 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 406 aanvaksafLANMSHEIRTPLNAITGMAHLIR----RGGLTDKQDDQLAKLEAAGAHLLN-IINAILeLSKIEAGK---- 476
Cdd:COG3290   193 ---------LRAQRHDFRNHLHTISGLLQLGEydeaLEYIDEISEELQELIDSLLSRIGNpVLAALL-LGKAARARergi 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 477 -------FQLEHVPVDVNDLV---GNvvtmiqagaqakrlrlatevapvpgvlygdptrlqqaLLNYAGNAVKFTEAGSV 546
Cdd:COG3290   263 dltididSDLPDLPLSDTDLVtilGN-------------------------------------LLDNAIEAVEKLPEEER 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 547 TLRVHAVEEAPEavlLRFEVTDTGIGLAPDTLAKLFTafeqaDNSTTRKYGGTGLGLAVTRRLAELMGGGAGAESRPGAG 626
Cdd:COG3290   306 RVELSIRDDGDE---LVIEVEDSGPGIPEELLEKIFE-----RGFSTKLGEGRGLGLALVKQIVEKYGGTIEVESEEGEG 377

                  ....*....
gi 1590033346 627 STfwFTARL 635
Cdd:COG3290   378 TV--FTVRL 384
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
526-626 6.09e-09

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: 53.99  E-value: 6.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 526 LQQALLNYAGNAVKFteaGSVTLRVHAVEEAPeavLLRFEVTDTGIGLAPDTLAKLFTAFEQADNSttRKYGGTGLGLAV 605
Cdd:cd16950     1 LKRVLSNLVDNALRY---GGGWVEVSSDGEGN---RTRIQVLDNGPGIAPEEVDELFQPFYRGDNA--RGTSGTGLGLAI 72
                          90       100
                  ....*....|....*....|.
gi 1590033346 606 TRRLAELMGGGAGAESRPGAG 626
Cdd:cd16950    73 VQRISDAHGGSLTLANRAGGG 93
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
702-773 6.76e-09

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: 54.44  E-value: 6.76e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590033346 702 MAEANDYALILMDVQMPRLDGLEATRRIRclPRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQL 773
Cdd:cd17535    39 LLRELRPDVVLMDLSMPGMDGIEALRRLR--RRYPDLKVIVLTAHDDPEYVLRALKAGAAGYLLKDSSPEEL 108
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
666-775 8.08e-09

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: 53.95  E-value: 8.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 666 LLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLprHAGTPILAMTA 745
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLA--KVKTPILILSG 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1590033346 746 NAFAEDKAVCFAAGMNDFIAKPVDPDQLYA 775
Cdd:cd17616    79 LADIEDKVKGLGFGADDYMTKPFHKDELVA 108
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
414-636 9.04e-09

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 58.06  E-value: 9.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 414 FLANMSHEIRTPLNAITGMAHLIRRGGLTDKQDdQLAKLEaagaHLLNIINAILELSKIE----AGKFQlehvPVDvndL 489
Cdd:PRK10755  140 FTADVAHELRTPLAGIRLHLELLEKQHHIDVAP-LIARLD----QMMHTVEQLLQLARAGqsfsSGHYQ----TVK---L 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 490 VGNVVTMIQAG----AQAKRLRLATEVAPVPGVLYGDPTRLQQALLNYAGNAVKFTEAGSvTLRVHAVEEAPEAVLlrfE 565
Cdd:PRK10755  208 LEDVILPSQDElsemLEQRQQTLLLPESAADITVQGDATLLRLLLRNLVENAHRYSPEGS-TITIKLSQEDGGAVL---A 283
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590033346 566 VTDTGIGLAPDTLAKLFTAFEQADnsttRKYGGTGLGLAVTRRLAELMGGGAGAESRPGAGST---FWFTARLE 636
Cdd:PRK10755  284 VEDEGPGIDESKCGELSKAFVRMD----SRYGGIGLGLSIVSRITQLHHGQFFLQNRQERSGTrawVWLPKAQN 353
PRK15479 PRK15479
transcriptional regulator TctD;
665-777 9.94e-09

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 56.27  E-value: 9.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDepiNREITVLL---LDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclPRHAGTPIL 741
Cdd:PRK15479    2 RLLLAED---NRELAHWLekaLVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLR--KRGQTLPVL 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1590033346 742 AMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:PRK15479   77 LLTARSAVADRVKGLNVGADDYLPKPFELEELDARL 112
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
665-777 1.59e-08

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: 53.19  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDDVGLKADAAADG-AEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclPRHAGtPILAM 743
Cdd:cd19932     2 RVLIAEDEALIRMDLREMLEEAGYEVVGEASDgEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIIT--SENIA-PIVLL 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1590033346 744 TanAFAEDKAVCFA--AGMNDFIAKPVDPDQLYATL 777
Cdd:cd19932    79 T--AYSQQDLVERAkeAGAMAYLVKPFSESDLIPAI 112
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
526-621 2.33e-08

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: 52.39  E-value: 2.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 526 LQQALLNYAGNAVKFTEAGSvtlRVHaVEEAPEAVLLRFEVTDTGIGLAPDTLAKLFTAFEQADNSttRKYGGTGLGLAV 605
Cdd:cd16923     1 LQRVFSNLLSNAIKYSPENT---RIY-ITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNS--RNTEGAGLGLSI 74
                          90
                  ....*....|....*.
gi 1590033346 606 TRRLAELMGGGAGAES 621
Cdd:cd16923    75 AKAIIELHGGSASAEY 90
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
666-769 2.80e-08

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: 52.71  E-value: 2.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 666 LLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGTPILAMTA 745
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                          90       100
                  ....*....|....*....|....
gi 1590033346 746 NAFAEDKAVCFAAGMNDFIAKPVD 769
Cdd:cd17598    81 LSDPRDVIRGLECGADNFITKPYD 104
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
666-767 3.67e-08

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: 52.00  E-value: 3.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 666 LLLAEDEPINREITVLLLDDVGLKADAA---------ADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHA 736
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAvdgeealnkLENLAKEGNDLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1590033346 737 GTPILAMTANAFAEDKAVCFAAGMNDFIAKP 767
Cdd:cd19924    81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
665-773 4.70e-08

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 52.17  E-value: 4.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDDV-GLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGTPILAM 743
Cdd:cd17552     3 RILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVILL 82
                          90       100       110
                  ....*....|....*....|....*....|
gi 1590033346 744 TANAFAEDKAVCFAAGMNDFIAKPVDPDQL 773
Cdd:cd17552    83 TAKAQPSDRQRFASLGVAGVIAKPFDPLTL 112
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
526-624 5.59e-08

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


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 51.63  E-value: 5.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 526 LQQALLNYAGNAVKFTEA--GSVTLRV---HAVEEAPEA--VLLRFEVTDTGIGLAPDTLAKLFTAFeqadnsTTRKYGG 598
Cdd:cd16918     1 LIQVFLNLVRNAAQALAGsgGEIILRTrtqRQVTLGHPRhrLALRVSVIDNGPGIPPDLQDTIFYPM------VSGRENG 74
                          90       100
                  ....*....|....*....|....*.
gi 1590033346 599 TGLGLAVTRRLAELMGGGAGAESRPG 624
Cdd:cd16918    75 TGLGLAIAQNIVSQHGGVIECDSQPG 100
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
702-777 5.67e-08

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: 51.61  E-value: 5.67e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590033346 702 MAEANDYALILMDVQMPRLDGLEATRRIRCLPRHagTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:cd17627    37 VISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGND--LPILVLTARDSVSDRVAGLDAGADDYLVKPFALEELLARV 110
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
522-627 8.47e-08

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: 51.00  E-value: 8.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 522 DPTRLQQALLNYAGNAVKFTEA-----GSVTLRVHAVEEAPEAVLlrfeVTDTGIGLAPDTLAKLFTAFeqadnsTTRKY 596
Cdd:cd16944     1 DTTQISQVLTNILKNAAEAIEGrpsdvGEVRIRVEADQDGRIVLI----VCDNGKGFPREMRHRATEPY------VTTRP 70
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1590033346 597 GGTGLGLAVTRRLAELMGGGAGAESRPGAGS 627
Cdd:cd16944    71 KGTGLGLAIVKKIMEEHGGRISLSNREAGGA 101
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
666-777 9.55e-08

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: 51.13  E-value: 9.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 666 LLLAEDE-PINREITVLLLDdVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRhaGTPILAMT 744
Cdd:cd19934     1 LLLVEDDaLLAAQLKEQLSD-AGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGR--ATPVLILT 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1590033346 745 ANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:cd19934    78 ARDSWQDKVEGLDAGADDYLTKPFHIEELLARL 110
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
267-369 9.58e-08

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 50.71  E-value: 9.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 267 NMIFLKRADDLRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALATAGVVDIpEEAVDTRQGGRRILH 346
Cdd:cd00130     2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTL-EVRLRRKDGSVIWVL 80
                          90       100
                  ....*....|....*....|...
gi 1590033346 347 TRKLALRNAQGEAEFLLGMSEDI 369
Cdd:cd00130    81 VSLTPIRDEGGEVIGLLGVVRDI 103
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
665-775 1.08e-07

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: 50.83  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclpRHAGTPILAMT 744
Cdd:cd19939     1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVR---EHSHVPILMLT 77
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1590033346 745 ANAFAEDKAVCFAAGMNDFIAKPVDPDQLYA 775
Cdd:cd19939    78 ARTEEMDRVLGLEMGADDYLCKPFSPRELLA 108
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
276-371 1.15e-07

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 50.15  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 276 DLRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALATAGVVdipEEAVDTRQGGRRILHTRKLALRNA 355
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAVREF---EVVLYRKDGEPFPVLVSLAPIRDD 77
                          90
                  ....*....|....*.
gi 1590033346 356 QGEAEFLLGMSEDITE 371
Cdd:pfam13426  78 GGELVGIIAILRDITE 93
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
247-383 1.56e-07

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 54.39  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 247 NEAEIGAANRLLDSIVENIPNMIFLkrAD-DLRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQAdaltardREALATA 325
Cdd:COG3829     2 EELELKELEEELEAILDSLDDGIIV--VDaDGRITYVNRAAERILGLPREEVIGKNVTELIPNSPL-------LEVLKTG 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1590033346 326 gvVDIPEEAVDTRQGGRRILHTRKLALRNaqGEAEFLLGMSEDITEAKRTAEELQRHR 383
Cdd:COG3829    73 --KPVTGVIQKTGGKGKTVIVTAIPIFED--GEVIGAVETFRDITELKRLERKLREEE 126
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
666-777 1.64e-07

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: 50.38  E-value: 1.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 666 LLLAEDEpinREITVLL---LDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclpRHAGTPILA 742
Cdd:cd17623     1 ILLIDDD---RELTELLteyLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELR---KTSQVPVLM 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1590033346 743 MTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:cd17623    75 LTARGDDIDRILGLELGADDYLPKPFNPRELVARI 109
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
664-777 2.17e-07

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


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 49.91  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 664 ARLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclPRHAGTPILAM 743
Cdd:cd17554     1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIR--EKKPDLPVIIC 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1590033346 744 TANAFAEDKAVCFAAGmnDFIAKPVDPDQLYATL 777
Cdd:cd17554    79 TAYSEYKSDFSSWAAD--AYVVKSSDLTELKETI 110
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
666-777 3.12e-07

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: 49.64  E-value: 3.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 666 LLLAEDEPINREitvlllddvGLKADAAADGAEAVAMAEANDYA------------LILMDVQMPRLDGLEATRRIRclP 733
Cdd:cd17536     1 VLIVDDEPLIRE---------GLKKLIDWEELGFEVVGEAENGEealelieehkpdIVITDIRMPGMDGLELIEKIR--E 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1590033346 734 RHAGTPILAMTanAFAEdkavcFA-------AGMNDFIAKPVDPDQLYATL 777
Cdd:cd17536    70 LYPDIKIIILS--GYDD-----FEyaqkairLGVVDYLLKPVDEEELEEAL 113
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
520-615 3.44e-07

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: 49.58  E-value: 3.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 520 YGDPTRLQQALLNYAGNAVKFT--EAGSVTLRV----HAVEEAPEAVLLRFEVTDTGIGLAPDTLAKLFtafeQADNSTT 593
Cdd:cd16932     1 YGDQIRLQQVLADFLLNAVRFTpsPGGWVEIKVsptkKQIGDGVHVIHLEFRITHPGQGLPEELVQEMF----EENQWTT 76
                          90       100
                  ....*....|....*....|..
gi 1590033346 594 RKyggtGLGLAVTRRLAELMGG 615
Cdd:cd16932    77 QE----GLGLSISRKLVKLMNG 94
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
665-777 3.63e-07

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: 49.30  E-value: 3.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclPRHAGtPILAMT 744
Cdd:cd17622     2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLR--PKYQG-PILLLT 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1590033346 745 ANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:cd17622    79 ALDSDIDHILGLELGADDYVVKPVEPAVLLARL 111
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
666-775 3.65e-07

phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF appears to play an important role in cell wall integrity in a wide range of gram-positive bacteria, and may also modulate cell membrane integrity. It functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. YycF belongs to the OmpR family of response regulators, which are characterized by a REC domain and a winged helix-turn-helix effector domain involved in DNA binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 49.34  E-value: 3.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 666 LLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclpRHAGTPILAMTA 745
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVR---KTSNVPIIMLTA 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 1590033346 746 NAFAEDKAVCFAAGMNDFIAKPVDPDQLYA 775
Cdd:cd17614    78 KDSEVDKVLGLELGADDYVTKPFSNRELLA 107
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
414-629 4.24e-07

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: 53.59  E-value: 4.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 414 FLANMS----HEIRTPLnAI--TGMAHLirRGGLTDKQDDQLAKLEAAGAHLLN-IINAILELSKIEAGKFQLEHVPVDV 486
Cdd:TIGR03785 484 YLENMSsrlsHELRTPV-AVvrSSLENL--ELQALEQEKQKYLERAREGTERLSmILNNMSEATRLEQAIQSAEVEDFDL 560
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 487 NDLVGNVVTMIQAGAQAKRLRLATEVAPVpgVLYGDPTRLQQALLNYAGNAVKFTEAGSVT-LRVHAVEEapEAVLlrfE 565
Cdd:TIGR03785 561 SEVLSGCMQGYQMTYPPQRFELNIPETPL--VMRGSPELIAQMLDKLVDNAREFSPEDGLIeVGLSQNKS--HALL---T 633
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1590033346 566 VTDTGIGLAPDTLAKLFTAFEQADNSTTRKYGGTGLGLAVTRRLAELMGGGAGAESRP-GAGSTF 629
Cdd:TIGR03785 634 VSNEGPPLPEDMGEQLFDSMVSVRDQGAQDQPHLGLGLYIVRLIADFHQGRIQAENRQqNDGVVF 698
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
710-773 4.37e-07

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 53.31  E-value: 4.37e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590033346 710 LILMDVQMPRLDGLEATRRIRclPRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQL 773
Cdd:PRK11361   51 VVLMDIRMPEMDGIKALKEMR--SHETRTPVILMTAYAEVETAVEALRCGAFDYVIKPFDLDEL 112
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
256-323 4.96e-07

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 47.39  E-value: 4.96e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590033346  256 RLLDSIVENIPNMIFLkRADDLRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALA 323
Cdd:smart00091   1 ERLRAILESLPDGIFV-LDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
522-631 5.21e-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: 48.61  E-value: 5.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 522 DPTRLQQALLNYAGNAVKFT-EAGSVTLRVHAVEEapeavLLRFEVTDTGIGLAPDTLAKLFTAFEQADNSTTRKyGGTG 600
Cdd:cd16975     1 DTLLLSRALINIISNACQYApEGGTVSISIYDEEE-----YLYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSG-GHYG 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1590033346 601 LGLAVTRRLAELMGGGAGAE--SRPGAGSTFWF 631
Cdd:cd16975    75 MGLYIAKNLVEKHGGSLIIEnsQKGGAEVTVKI 107
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
530-629 5.42e-07

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 48.44  E-value: 5.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 530 LLNYAGNAVKFTEAGSVTLRVHAVEEAPEAVLlrfEVTDTGIGLAPDTLAKLFTAfeqadNSTTRKYGGTGLGLAVTRRL 609
Cdd:cd16915     8 LIDNALDALAATGAPNKQVEVFLRDEGDDLVI---EVRDTGPGIAPELRDKVFER-----GVSTKGQGERGIGLALVRQS 79
                          90       100
                  ....*....|....*....|
gi 1590033346 610 AELMGGGAGAESRPGAGSTF 629
Cdd:cd16915    80 VERLGGSITVESEPGGGTTF 99
PRK11517 PRK11517
DNA-binding response regulator HprR;
665-775 5.71e-07

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 51.05  E-value: 5.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRhagTPILAMT 744
Cdd:PRK11517    2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQ---TPVICLT 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1590033346 745 ANAFAEDKAVCFAAGMNDFIAKPVDPDQLYA 775
Cdd:PRK11517   79 ARDSVDDRVRGLDSGANDYLVKPFSFSELLA 109
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
664-775 6.83e-07

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: 48.62  E-value: 6.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 664 ARLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclpRHAGTPILAM 743
Cdd:cd17626     1 ARILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIR---AESGVPIVML 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1590033346 744 TANAFAEDKAVCFAAGMNDFIAKPVDPDQLYA 775
Cdd:cd17626    78 TAKSDTVDVVLGLESGADDYVAKPFKPKELVA 109
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
666-767 1.01e-06

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: 47.76  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 666 LLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGTPILAMTA 745
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80
                          90       100
                  ....*....|....*....|..
gi 1590033346 746 NAFAEDKAVCFAAGMNDFIAKP 767
Cdd:cd19927    81 KGMTSDRIKGYNAGCDGYLSKP 102
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
666-777 1.64e-06

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: 47.48  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 666 LLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclPRHAGTPILAMTA 745
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWR--RQGQSLPVLILTA 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1590033346 746 NAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:cd17624    79 RDGVDDRVAGLDAGADDYLVKPFALEELLARL 110
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
665-777 1.70e-06

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 49.81  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDDV-GLKADAAAD-GAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHagTPILA 742
Cdd:COG3279     3 KILIVDDEPLARERLERLLEKYpDLEVVGEASnGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPP--PPIIF 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1590033346 743 MTA------NAFAEDkAVcfaagmnDFIAKPVDPDQLYATL 777
Cdd:COG3279    81 TTAydeyalEAFEVN-AV-------DYLLKPIDEERLAKAL 113
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
664-773 1.72e-06

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: 47.38  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 664 ARLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclpRHAGTPILAM 743
Cdd:cd17619     1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELR---EQSEVGIILV 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 1590033346 744 TANAFAEDKAVCFAAGMNDFIAKPVDPDQL 773
Cdd:cd17619    78 TGRDDEVDRIVGLEIGADDYVTKPFNPREL 107
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
149-251 1.74e-06

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 51.17  E-value: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 149 TVITISTAELNDQKRSILLWGVLGSAFFVLLSSTSIVFLAQRLlTRRVDVSLGVLKEVEEGDVAaRIPVTYSDELGELQA 228
Cdd:COG2972   139 LVSLIPKSELFRGLFSLRRLILLIILLLLLLALLLSYLLSRSI-TRPIKRLKKAMKKVEKGDLV-RLEVSGNDEIGILAR 216
                          90       100
                  ....*....|....*....|...
gi 1590033346 229 GINSMTAKLGALLAVHQRNEAEI 251
Cdd:COG2972   217 SFNEMVERIKELIEEVYELELEK 239
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
665-777 1.88e-06

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: 47.35  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclPRHAGTPILAMT 744
Cdd:cd17615     1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLR--ADGPDVPVLFLT 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1590033346 745 ANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:cd17615    79 AKDSVEDRIAGLTAGGDDYVTKPFSLEEVVARL 111
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
526-635 2.00e-06

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


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 47.18  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 526 LQQALLNYAGNAVKFTEAGSVTLRVHAveeAPEAVLLRFEVTDTGIGLAPDTLAKLFTAFeQADNSTTRKYG-GTGLGLA 604
Cdd:cd16953     1 LGQVLRNLIGNAISFSPPDTGRITVSA---MPTGKMVTISVEDEGPGIPQEKLESIFDRF-YTERPANEAFGqHSGLGLS 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1590033346 605 VTRRLAELMGGGAGAESR--PGAGSTFWFTARL 635
Cdd:cd16953    77 ISRQIIEAHGGISVAENHnqPGQVIGARFTVQL 109
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
522-630 2.21e-06

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: 47.07  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 522 DPTRLQQALLNYAGNAVKFT-EAGSVTLRVHAveEAPEAVLLrfeVTDTGIGLAPDTLAKLFTAFEqadnSTTRKYGG-- 598
Cdd:cd16945     1 DPFLLRQAINNLLDNAIDFSpEGGLIALQLEA--DTEGIELL---VFDEGSGIPDYALNRVFERFY----SLPRPHSGqk 71
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1590033346 599 -TGLGLAVTRRLAELMGGGAGAESRP-GAGSTFW 630
Cdd:cd16945    72 sTGLGLAFVQEVAQLHGGRITLRNRPdGVLAFLT 105
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
711-775 2.97e-06

phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The GGDEF response regulator WspR is part of the Wsp system that is homologous to chemotaxis systems and also includes the membrane-bound receptor protein WspA. In response to growth on surfaces, WspR is phosphorylated by the Wsp signal transduction complex and is activated, functioning as a diguanylate cyclase (DGC) that catalyzes c-di-GMP synthesis. WspR is a hybrid response regulator-diguanylate cyclase, containing an N-terminal REC domain and a C-terminal GGDEF domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 47.02  E-value: 2.97e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1590033346 711 ILMDVQMPRLDGLEATRRIRCLPRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYA 775
Cdd:cd17575    49 ILQDLVMPGVDGLTLVRFFRANPATRDIPIIVLSTKEEPEVKSEAFALGANDYLVKLPDKIELVA 113
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
664-768 3.09e-06

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: 46.81  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 664 ARLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclPRHAGTPILAM 743
Cdd:cd17555     1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQIT--KESPDTPVIVV 78
                          90       100
                  ....*....|....*....|....*
gi 1590033346 744 TANAFAEDKAVCFAAGMNDFIAKPV 768
Cdd:cd17555    79 SGAGVMSDAVEALRLGAWDYLTKPI 103
orf27 CHL00148
Ycf27; Reviewed
710-781 3.11e-06

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 49.33  E-value: 3.11e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590033346 710 LILMDVQMPRLDGLEATRRIRclpRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATLLTWL 781
Cdd:CHL00148   53 LVILDVMMPKLDGYGVCQEIR---KESDVPIIMLTALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVL 121
pleD PRK09581
response regulator PleD; Reviewed
702-775 4.22e-06

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 49.90  E-value: 4.22e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590033346 702 MAEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYA 775
Cdd:PRK09581   41 ICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVTALDDPEDRVRGLEAGADDFLTKPINDVALFA 114
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
526-631 4.89e-06

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: 45.91  E-value: 4.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 526 LQQALLNYAGNAvkFTEAGSVT---LRVHAVEEAPEAVLLrfeVTDTGIGLAPDTLAKLFTAFeqadnSTTRKYG-GTGL 601
Cdd:cd16976     1 IQQVLMNLLQNA--LDAMGKVEnprIRIAARRLGGRLVLV---VRDNGPGIAEEHLSRVFDPF-----FTTKPVGkGTGL 70
                          90       100       110
                  ....*....|....*....|....*....|
gi 1590033346 602 GLAVTRRLAELMGGGAGAESRPGAGSTFWF 631
Cdd:cd16976    71 GLSISYGIVEEHGGRLSVANEEGAGARFTF 100
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
707-775 5.04e-06

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 45.88  E-value: 5.04e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590033346 707 DYALILMDVQMPRLDGLEATRRIRclPRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYA 775
Cdd:cd17573    42 NYDLVLVSDKLPDGNGLSIVSRIK--EKHPSIVVIVLSDNPKTEQEIEAFKEGADDYIAKPFDFKVLVA 108
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
34-265 5.28e-06

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 50.02  E-value: 5.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346  34 RFSGALDERTRSRLQLVGDMIASDELAVHAIARQQLISEMLGAPYLDGMVIGGNGRIIVATDPGKLGQQVRETKGFDSRW 113
Cdd:COG0840    48 LLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAAL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 114 LAETGPHEELFVAGPDTLTAIRHIDAPDGGRPIYVTVITISTAELNDQKRSILLWGVLGSAFFVLLSSTSIVFLAQRLLT 193
Cdd:COG0840   128 AIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSIT 207
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590033346 194 RRVDVSLGVLKEVEEGDVAARIPVTYSDELGELQAGINSMTAKLGALLAVHQRNEAEIGAANRLLDSIVENI 265
Cdd:COG0840   208 RPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEEL 279
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
708-777 7.46e-06

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 49.26  E-value: 7.46e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 708 YALILMDVQMPRLDGLEATRRIRCLprHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:PRK10365   50 FDLVLCDVRMAEMDGIATLKEIKAL--NPAIPVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATL 117
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
38-513 1.30e-05

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 48.57  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346  38 ALDERTRSRLQLVGDMIASDELAVHAIARQQLISEMLGAPYLDGMVIGGNGRIIVATDPGKLGQQVRETKGFDSRWLAET 117
Cdd:COG2770    87 LAALLLALLLLLLLALLLLLAALLLLLLLAALALLLLLLLLLAALLALLLALALLALLLGLAAARLLLAALLALAAALAL 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 118 GPHEELFVAGPDTLTAIRHIDAPDGGRPIYVTVITISTAELNDQKRSILLWGVLGSAFFVLLSstsivFLAQRLLTRRVD 197
Cdd:COG2770   167 ALGAGELLLLADLAAAIAALLAALLLLLLGGLLLVVLLEAALAALLLLLLLALLALLLALLLA-----LLLARRITRPLR 241
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 198 VSLGVLKEVEEGDVAARIPVTYSDELGELQAGINSMTAKLGALLAVHQRNEAEIGAANRLLDSIVENIPNMIFLKRADDL 277
Cdd:COG2770   242 RLAEAARRIAAGDLDVRIPVSRKDEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALL 321
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 278 RFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALATAGVVDIPEEAVDTRQGGRRILHTRKLALRNAQG 357
Cdd:COG2770   322 LLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAA 401
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 358 EAEFLLGMSEDITEAKRTAEELQRHRENLEQLVEVRTAELSHAKEAAEAANVAKSAFLANMSHEIRTPLNAITGMAHLIR 437
Cdd:COG2770   402 LLLLELALEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLL 481
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590033346 438 RGGLTDKQDDQLAKLEAAGAHLLNIINAILELSKIEAGKFQLEHVPVDVNDLVGNVVTMIQAGAQAKRLRLATEVA 513
Cdd:COG2770   482 AALGALELLLLEEEEEAGAAAEELAEELLLLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAALLALLLA 557
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
536-632 1.57e-05

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: 44.58  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 536 NAVKFT-EAGSVTLRVhavEEAPEAVLLrfEVTDTGIGLAPDTLAKLFTAFEQADNSttRKYG-GTGLGLAVTRRLAELM 613
Cdd:cd16948    16 NALKYSkQGGKIEIYS---ETNEQGVVL--SIKDFGIGIPEEDLPRVFDKGFTGENG--RNFQeSTGMGLYLVKKLCDKL 88
                          90
                  ....*....|....*....
gi 1590033346 614 GGGAGAESRPGAGSTFWFT 632
Cdd:cd16948    89 GHKIDVESEVGEGTTFTIT 107
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
665-777 1.66e-05

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 47.02  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGTPILAMT 744
Cdd:PRK10161    4 RILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLT 83
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1590033346 745 ANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:PRK10161   84 ARGEEEDRVRGLETGADDYITKPFSPKELVARI 116
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
665-775 1.80e-05

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: 44.68  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclpRHAGTPILAMT 744
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIR---RFSDVPIIMVT 77
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1590033346 745 ANAFAEDKAVCFAAGMNDFIAKPVDPDQLYA 775
Cdd:cd19938    78 ARVEEIDRLLGLELGADDYICKPYSPREVVA 108
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
667-767 2.40e-05

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 43.68  E-value: 2.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 667 LLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclPRHAGTPILAMTAN 746
Cdd:cd19926     2 LVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQ--QRLPQTPVAVITAY 79
                          90       100
                  ....*....|....*....|.
gi 1590033346 747 AFAEDKAVCFAAGMNDFIAKP 767
Cdd:cd19926    80 GSLDTAIEALKAGAFDFLTKP 100
glnL PRK11073
nitrogen regulation protein NR(II);
254-624 2.47e-05

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 47.38  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 254 ANRLLDSIVENIpnmifLKRADDLRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADalTARDREALATA-GVVDipE 332
Cdd:PRK11073    9 AGQILNSLINSI-----LLLDDDLAIHYANPAAQQLLAQSSRKLFGTPLPELLSYFSLN--IELMRESLQAGqGFTD--N 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 333 EAVDTRQGGRRILHTrklalrNAQGEAE-FLLGMSEDITEAKRTAEELQRHrenleqlvevrtaelshakeaaeAANVAK 411
Cdd:PRK11073   80 EVTLVIDGRSHILSL------TAQRLPEgMILLEMAPMDNQRRLSQEQLQH-----------------------AQQVAA 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 412 SAFLANMSHEIRTPLNAITGMAHLIRRGgLTDKQDDQLAKLEAAGA-HLLNIINAILelskieaGKFQL-EHVPVDVNDL 489
Cdd:PRK11073  131 RDLVRGLAHEIKNPLGGLRGAAQLLSKA-LPDPALTEYTKVIIEQAdRLRNLVDRLL-------GPQRPgTHVTESIHKV 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 490 VGNVVTMIQAGAQAKrLRLATEVAPVPGVLYGDPTRLQQALLNYAGNAVKF--TEAGSVTLRVHAVEEAP-----EAVLL 562
Cdd:PRK11073  203 AERVVQLVSLELPDN-VRLIRDYDPSLPELAHDPDQIEQVLLNIVRNALQAlgPEGGTITLRTRTAFQLTlhgerYRLAA 281
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590033346 563 RFEVTDTGIGLAPDTLAKLFTAFeqadnsTTRKYGGTGLGLAVTRRLAELMGGGAGAESRPG 624
Cdd:PRK11073  282 RIDIEDNGPGIPPHLQDTLFYPM------VSGREGGTGLGLSIARNLIDQHSGKIEFTSWPG 337
ompR PRK09468
osmolarity response regulator; Provisional
708-775 3.40e-05

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 46.12  E-value: 3.40e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590033346 708 YALILMDVQMPRLDGLEATRRIRclPRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYA 775
Cdd:PRK09468   50 FHLMVLDLMLPGEDGLSICRRLR--SQNNPTPIIMLTAKGEEVDRIVGLEIGADDYLPKPFNPRELLA 115
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
710-777 4.05e-05

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: 43.42  E-value: 4.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 710 LILMDVQMPRLDGLEATRRIRCLprHAGTPILAMTANAFAE--DKAVcfAAGMNDFIAKPVDPDQLYATL 777
Cdd:cd17542    48 LVTMDITMPEMDGIEALKEIKKI--DPNAKVIMCSAMGQEEmvKEAI--KAGAKDFIVKPFQPERVLEAV 113
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
710-768 4.10e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 46.41  E-value: 4.10e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1590033346 710 LILMDVQMPRLDGLEATRRIRclpRHAGTPILAMTAN--AFAEDKAVCFAAGMNDFIAKPV 768
Cdd:PRK12555   49 VILMDLEMPRMDGVEATRRIM---AERPCPILIVTSLteRNASRVFEAMGAGALDAVDTPT 106
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
536-636 4.32e-05

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 46.93  E-value: 4.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 536 NAVKF---TEAGSVTLRVHAVEEAPEavlLRFEVTDTGIGLAPDTLAKLFTAFEqadnsttRKYGGTGLGLA-VTRRLAE 611
Cdd:COG2972   347 NAIEHgiePKEGGGTIRISIRKEGDR---LVITVEDNGVGMPEEKLEKLLEELS-------SKGEGRGIGLRnVRERLKL 416
                          90       100
                  ....*....|....*....|....*..
gi 1590033346 612 LMGGGAG--AESRPGAGstfwFTARLE 636
Cdd:COG2972   417 YYGEEYGleIESEPGEG----TTVTIR 439
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
202-237 4.65e-05

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


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 41.28  E-value: 4.65e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1590033346 202 VLKEVEEGDVAARIPVTYSDELGELQAGINSMTAKL 237
Cdd:cd06225    10 AARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
665-718 5.04e-05

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: 41.40  E-value: 5.04e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1590033346  665 RLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMP 718
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
709-772 5.75e-05

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: 43.03  E-value: 5.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590033346 709 ALILMDVQMPRLDGLEATRRIRclPRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQ 772
Cdd:cd19919    46 DVLISDIRMPGMDGLALLAQIK--QRHPDLPVIIMTAHSDLDSAVSAYQGGAFEYLPKPFDIDE 107
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
530-629 5.91e-05

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 46.44  E-value: 5.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 530 LLNYAGNAVKFTEAGSVTLRVHAVEEApeavlLRFEVTDTGIGLAPDTLAKLFT-AFeqadnSTtrKYGGTGLGLAVTRR 608
Cdd:PRK11086  441 LIENALEAVGGEEGGEISVSLHYRNGW-----LHCEVSDDGPGIAPDEIDAIFDkGY-----ST--KGSNRGVGLYLVKQ 508
                          90       100
                  ....*....|....*....|.
gi 1590033346 609 LAELMGGGAGAESRPGAGSTF 629
Cdd:PRK11086  509 SVENLGGSIAVESEPGVGTQF 529
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
190-242 7.27e-05

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


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 41.08  E-value: 7.27e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1590033346  190 RLLTRRVDVSLGVLKEVEEGDVAARIPVTYSDELGELQAGINSMTAKLGALLA 242
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
667-767 9.14e-05

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: 42.15  E-value: 9.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 667 LLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclpRHAGTPILAMTAN 746
Cdd:cd17620     2 LVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLR---EWSAVPVIVLSAR 78
                          90       100
                  ....*....|....*....|.
gi 1590033346 747 AFAEDKAVCFAAGMNDFIAKP 767
Cdd:cd17620    79 DEESDKIAALDAGADDYLTKP 99
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
710-775 9.99e-05

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 44.41  E-value: 9.99e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590033346 710 LILMDVQMPRLDGLEATRRIRclpRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYA 775
Cdd:PRK10955   47 LLLLDVMMPKKNGIDTLKELR---QTHQTPVIMLTARGSELDRVLGLELGADDYLPKPFNDRELVA 109
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
709-767 1.17e-04

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 41.97  E-value: 1.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1590033346 709 ALILMDVQMPRLDGLEATRRIRCLPRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKP 767
Cdd:cd17602    44 DLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTGKDGLVDRIRAKMAGASGYLTKP 102
PRK10610 PRK10610
chemotaxis protein CheY;
665-767 1.44e-04

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 42.27  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDDVGLKADAAADG-AEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGTPILAM 743
Cdd:PRK10610    7 KFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDgVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMV 86
                          90       100
                  ....*....|....*....|....
gi 1590033346 744 TANAFAEDKAVCFAAGMNDFIAKP 767
Cdd:PRK10610   87 TAEAKKENIIAAAQAGASGYVVKP 110
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
664-777 1.47e-04

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: 42.01  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 664 ARLLLAEDEPINREITVLLLDDVGLKADAAAD-GAEAVAMAEANDYALILMDVQMP-RLDGLEATRRIRclpRHAGTPIL 741
Cdd:cd17534     1 KKILIVEDEAIIALDLKEILESLGYEVVGIADsGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIR---EKFDIPVI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1590033346 742 AMTANAfaeDKAV------CFAAGmndFIAKPVDPDQLYATL 777
Cdd:cd17534    78 FLTAYS---DEETlerakeTNPYG---YLVKPFNERELKAAI 113
PRK15115 PRK15115
response regulator GlrR; Provisional
661-777 2.14e-04

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 44.44  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 661 HRGARLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclPRHAGTPI 740
Cdd:PRK15115    3 RKPAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQ--KVQPGMPV 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1590033346 741 LAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:PRK15115   81 IILTAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAI 117
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
657-781 2.30e-04

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 43.52  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 657 LLRDHRGARLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclpRHA 736
Cdd:PRK10710    4 LPIDENTPRILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIR---RFS 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1590033346 737 GTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATLLTWL 781
Cdd:PRK10710   81 DIPIVMVTAKIEEIDRLLGLEIGADDYICKPYSPREVVARVKTIL 125
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
710-778 2.57e-04

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: 41.37  E-value: 2.57e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1590033346 710 LILMDVQMPRLDGLE--ATRRIRCLPrhagTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATLL 778
Cdd:cd17593    48 VLFLDLTMPVMDGYEvlEALPVEQLE----TKVIVVSGDVQPEAKERVLELGALAFLKKPFDPEKLAQLLE 114
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
667-777 3.18e-04

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


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 41.32  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 667 LLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclPRHAGTPILAMTAN 746
Cdd:cd17549     2 LLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIR--ELDPDLPVILITGH 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1590033346 747 AfaeDKAVCFAA---GMNDFIAKPVDPDQLYATL 777
Cdd:cd17549    80 G---DVPMAVEAmraGAYDFLEKPFDPERLLDVV 110
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
665-781 3.27e-04

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 42.99  E-value: 3.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRhaGTPILAMT 744
Cdd:PRK09836    2 KLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANK--GMPILLLT 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1590033346 745 ANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATLLTWL 781
Cdd:PRK09836   80 ALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLL 116
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
665-729 3.40e-04

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: 41.42  E-value: 3.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590033346 665 RLLLAEDEPINRE-ITVLLLDDVGLKADAAAD-GAEAVAMAEANDYALILMDVQMPRLDGLEATRRI 729
Cdd:COG2197     3 RVLIVDDHPLVREgLRALLEAEPDIEVVGEAAdGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
703-773 3.46e-04

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: 42.39  E-value: 3.46e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590033346 703 AEANDYALILMDVQMPRLDGLEATRRIRclPRHAGTPILAMTANAfaeDKAVC---FAAGMNDFIAKPVDPDQL 773
Cdd:COG4566    39 LDPDRPGCLLLDVRMPGMSGLELQEELA--ARGSPLPVIFLTGHG---DVPMAvraMKAGAVDFLEKPFDDQAL 107
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
706-773 3.58e-04

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


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 40.69  E-value: 3.58e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 706 NDYALILMDVQMPRLDGLEATRRIRCLPRhagTPILAMTANafAEDKAV--CFAAGMNDFIAKPVDPDQL 773
Cdd:cd17584    43 DEFDLVITDVHMPDMDGFEFLELIRLEMD---LPVIMMSAD--GSTSTVmkGLAHGACDYLLKPVSIEDL 107
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
667-775 4.39e-04

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 40.51  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 667 LLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclpRHAGTPILAMTAN 746
Cdd:cd17594     3 LVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIR---ARSDVPIIIISGD 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 1590033346 747 AFAE-DKAVCFAAGMNDFIAKPVDPDQLYA 775
Cdd:cd17594    80 RRDEiDRVVGLELGADDYLAKPFGLRELLA 109
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
710-777 4.60e-04

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: 40.34  E-value: 4.60e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590033346 710 LILMDVQMPRLDGLEATRRIRclpRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:cd18159    45 LVLLDINLPYFDGFYWCREIR---QISNVPIIFISSRDDNMDQVMAINMGGDDYITKPFDLDVLLAKI 109
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
670-773 5.10e-04

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: 40.27  E-value: 5.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 670 EDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLPRHagTPILAMTANAFA 749
Cdd:cd17537     7 DDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSN--IPIIFITGHGDV 84
                          90       100
                  ....*....|....*....|....
gi 1590033346 750 EDKAVCFAAGMNDFIAKPVDPDQL 773
Cdd:cd17537    85 PMAVEAMKAGAVDFLEKPFRDQVL 108
PRK10643 PRK10643
two-component system response regulator PmrA;
704-775 6.16e-04

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 41.94  E-value: 6.16e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590033346 704 EANDYALILMDVQMPRLDGLEATRRIRclPRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYA 775
Cdd:PRK10643   41 ESGHYSLVVLDLGLPDEDGLHLLRRWR--QKKYTLPVLILTARDTLEDRVAGLDVGADDYLVKPFALEELHA 110
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
666-767 7.81e-04

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: 39.49  E-value: 7.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 666 LLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclpRHAGTPILAMTA 745
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLR---ARSNVPVIMVTA 77
                          90       100
                  ....*....|....*....|..
gi 1590033346 746 NAFAEDKAVCFAAGMNDFIAKP 767
Cdd:cd17621    78 KDSEIDKVVGLELGADDYVTKP 99
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
665-767 9.66e-04

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: 39.41  E-value: 9.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDDVG-LKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRCLprHAGTPILAM 743
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKKAGyAVTEAESGAEALEKLQQGKDIDIVVTDIVMPEMDGIELAREARKI--DPDVKILFI 78
                          90       100
                  ....*....|....*....|....
gi 1590033346 744 TANAFAEDKAVCFAAGMNDFIAKP 767
Cdd:cd18160    79 SGGAAAAPELLSDAVGDNATLKKP 102
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
711-767 1.03e-03

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 42.06  E-value: 1.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1590033346 711 ILMDVQMPRLDGLEATRRIRclpRHAGTPIL---AMT-ANAFAEDKAVcfAAGMNDFIAKP 767
Cdd:PRK00742   53 ITLDVEMPVMDGLDALEKIM---RLRPTPVVmvsSLTeRGAEITLRAL--ELGAVDFVTKP 108
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
665-777 1.36e-03

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


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 40.28  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclPRHAGTPILAMT 744
Cdd:COG4567     6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALR--ERDPDARIVVLT 83
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1590033346 745 -----ANAFAedkAVcfAAGMNDFIAKPVDPDQLYATL 777
Cdd:COG4567    84 gyasiATAVE---AI--KLGADDYLAKPADADDLLAAL 116
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
664-775 1.39e-03

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 41.10  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 664 ARLLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclPRHAGTPILAM 743
Cdd:PRK11083    4 PTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLL--AFHPALPVIFL 81
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1590033346 744 TANAFAEDKAVCFAAGMNDFIAKPVDPDQLYA 775
Cdd:PRK11083   82 TARSDEVDRLVGLEIGADDYVAKPFSPREVAA 113
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
704-777 1.42e-03

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: 39.02  E-value: 1.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590033346 704 EANDYALILMDVQMPRLDGLEATRRIRclPRHAGTPILAMTANAFAED--KAVcfAAGMNDFIAKPVDPDQLYATL 777
Cdd:cd17550    39 KERRPDLVLLDIWLPDMDGLELLKEIK--EKYPDLPVIMISGHGTIETavKAT--KLGAYDFIEKPLSLDRLLLTI 110
HAMP pfam00672
HAMP domain;
190-237 1.44e-03

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 37.22  E-value: 1.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1590033346 190 RLLTRRVDVSLGVLKEVEEGDVAARIPVTYSDELGELQAGINSMTAKL 237
Cdd:pfam00672   4 RRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERL 51
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
702-774 1.50e-03

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: 39.04  E-value: 1.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590033346 702 MAEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLY 774
Cdd:cd17544    40 LEQHPDIKLVITDYNMPEMDGFELVREIRKKYSRDQLAIIGISASGDNALSARFIKAGANDFLTKPFLPEEFY 112
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
710-777 2.21e-03

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: 38.72  E-value: 2.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590033346 710 LILMDVQMPRLDGLEATRRIRclPRHAGTPILAMTANAfAEDKAV-CFAAGMNDFIAKPVDPDQLYATL 777
Cdd:cd17572    45 VVLLDLKLPDMSGMEILKWIQ--ERSLPTSVIVITAHG-SVDIAVeAMRLGAYDFLEKPFDADRLRVTV 110
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
710-767 2.23e-03

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: 38.19  E-value: 2.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1590033346 710 LILMDVQMPRLDGLEATRRIRclpRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKP 767
Cdd:cd19936    45 LAILDIKMPRMDGMELLQRLR---QKSTLPVIFLTSKDDEIDEVFGLRMGADDYITKP 99
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
667-777 2.40e-03

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: 38.67  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 667 LLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYA--LILMDVQMPRLDGLEATRRIrclpRHAGTPILAMT 744
Cdd:cd17532     2 LIVDDEPLAREELRYLLEEHPDIEIVGEAENGEEALEAIEELKpdVVFLDIQMPGLDGLELAKKL----SKLAKPPLIVF 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1590033346 745 ANAFaEDKAV-CFAAGMNDFIAKPVDPDQLYATL 777
Cdd:cd17532    78 VTAY-DEYAVeAFELNAVDYLLKPFSEERLAEAL 110
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
52-439 2.58e-03

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


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 41.02  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346  52 DMIASDELAVHAIARQQLISEMLGAPYLDGMVIGGNGRIIVATDPGKLGQQVRETKGFDSRWLAETGPHEELFVAGPDTL 131
Cdd:COG3850     2 RELLLLALALLRLLLALLALLLLALLLLSLLALLLLLERTLLRLLSLLASAGLLAALLAALLLLLSLGLLALLLALLLLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 132 TAIRHIDAPDGGRPIYVTVITISTAELNDQKRSILLWGVLGSAFFVLLSSTSIVFLAQRLLTRRVDVSLGVLKEVEEGDV 211
Cdd:COG3850    82 LLLLLAALLSLLLLLLLLLLLLLLLLLLLLAAAINRKLALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGDF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 212 AARIPVTYSDELGELQAGINSMTAKLGALLAVHQRNEAEIGAANRLLDSIVENIPNMIFLKRADDLRFVLFNRAGERLLG 291
Cdd:COG3850   162 DARVPVSGRDELGTLARAFNRMADELQELYAELEEEEELEAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 292 HARQELLGRTEYDLFPAEQADALTARDREALATAGVVDIPEEAVDTRQGGRRILHTRKLALRNAQGEAEFLLGMSEDITE 371
Cdd:COG3850   242 LLLQDALAESELLALNILAGLLELLLALLLLLLASALLLLELELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQ 321
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590033346 372 AKRTAEELQRHRENLEQLVEVRTAELSHAKEAAEAANVAKSAFLANMSHEIRTPLNAITGMAHLIRRG 439
Cdd:COG3850   322 AIANASLLLIALASVVAALLELASILALQAALEAAAAGAALAAAAAAAGLARALAQAGADAAEALGLL 389
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
141-639 3.08e-03

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 41.04  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 141 DGGRPIYVTVITISTAELNDQKRSILLWGVLGSAFFVLLSSTSIVFLAQRLLTRRVDVSLGVLKEVEEGDVAARIPVTYS 220
Cdd:COG3920    20 AALLLLAAALLLALLALLLLALLLLALLLASALLALLALSAAALAAALAVALAAAVGAAAALLALLVLLLLLLLAAAALA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 221 DELGELQAGINSMTAKLGALLAVHQRNEAEIGAANRLLDSIVENIPNMIFLKRADDLRFVLFNRAGERLLGHARQELLGR 300
Cdd:COG3920   100 LALLLAALAGLLLLAALLLLRLVALLAALALLALLLLLLLLLAILALAELAVALAELAAALLLLAEELAALRLAAAALLL 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 301 TEYDLFP-----AEQADALTARDREALATAGVVDIPEEAVDTRQGGRRILHTRKLALRNAQGEAEFLLGMSEDITEAKRT 375
Cdd:COG3920   180 LLAALLDlglalAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVLEELERRRRARGLGRLLLLLLL 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 376 AEELQRHRENLEQLVEVRTAELSHAKEAAEAANVAKSAFLANMSHEIRTPLNAITGMAHLIRRGgltdkqddqlAKLEAA 455
Cdd:COG3920   260 LLLLLRALLLLAAGIRLVITERKRAEEELEASLEEKELLLRELHHRVKNNLQVVSSLLRLQARR----------ADDPEA 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 456 GAHLLNIINAILELSKI-----EAGKFQlehvPVDVNDLVGNVVTMIQAGAQAKRLRLATEVAPVpgvlygdPTRLQQA- 529
Cdd:COG3920   330 REALEESQNRIQALALVhellyQSEDWE----GVDLRDYLRELLEPLRDSYGGRGIRIELDGPDV-------ELPADAAv 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 530 ----LLN-YAGNAVKF----TEAGSVTLRVHAVEEApeavlLRFEVTDTGIGLAPDTLAKlftafeqadnsttrkyGGTG 600
Cdd:COG3920   399 plglILNeLVTNALKHaflsGEGGRIRVSWRREDGR-----LRLTVSDNGVGLPEDVDPP----------------ARKG 457
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 1590033346 601 LGLAVTRRLAELMGGgaGAESRPGAGSTFWFTARLERRA 639
Cdd:COG3920   458 LGLRLIRALVRQLGG--TLELDRPEGTRVRITFPLAELA 494
PRK13559 PRK13559
hypothetical protein; Provisional
273-399 3.21e-03

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 40.57  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 273 RADDLRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALATAGVVDIpeEAVDTRQGGRRILHTRKLA- 351
Cdd:PRK13559   62 HQPDLPIVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVV--ELLNYRKDGEPFWNALHLGp 139
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1590033346 352 LRNAQGEAEFLLGMSEDITEAKRtAEELQRHRENLeqlvevrTAELSH 399
Cdd:PRK13559  140 VYGEDGRLLYFFGSQWDVTDIRA-VRALEAHERRL-------AREVDH 179
PAS_8 pfam13188
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ...
256-320 3.23e-03

PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463802 [Multi-domain]  Cd Length: 65  Bit Score: 36.76  E-value: 3.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1590033346 256 RLLDSIVENIPNMIFLkRADDLRFVLFNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDRE 320
Cdd:pfam13188   1 ERLRALFESSPDGILV-LDEGGRIIYVNPAALELLGYELLGELLGELLDLLDPLLEDALELLREL 64
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
337-386 3.94e-03

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 40.81  E-value: 3.94e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1590033346  337 TRQGGRRilHTRKLA--LRNAQGEAEFLLGMSEDITEAKRTAEELQRHRENL 386
Cdd:PRK09776   489 VVKDGVR--HIRALAnrVLNKDGEVERLLGINMDMTEVRQLNEALFQEKERL 538
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
665-777 4.51e-03

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


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 38.12  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 665 RLLLAEDEPINREITVLLLDDvGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclPRHAGTPILAMT 744
Cdd:cd17596     2 TILVVDDEVRSLEALRRTLEE-DFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVR--ERWPEVVRIIIS 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1590033346 745 ANAFAEDK-AVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:cd17596    79 GYTDSEDIiAGINEAGIYQYLTKPWHPDQLLLTV 112
PRK10693 PRK10693
two-component system response regulator RssB;
710-781 6.45e-03

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 39.59  E-value: 6.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590033346 710 LILMDVQMPRLDGLEATRRIRClpRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPV-DPDQLYATLLTWL 781
Cdd:PRK10693   20 LIICDLAMPRMNGIEFVEHLRN--RGDQTPVLVISATENMADIAKALRLGVQDVLLKPVkDLNRLREMVFACL 90
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
702-777 6.54e-03

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 38.86  E-value: 6.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590033346 702 MAEANDYALILMDVQMPRLDGLEATRRIRclPRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:PRK10651   47 LAESLDPDLILLDLNMPGMNGLETLDKLR--EKSLSGRIVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKAL 120
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
666-777 7.27e-03

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 38.63  E-value: 7.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 666 LLLAEDEPINREITVLLLDDVGLKADAAADGAEAVAMAEANDYALILMDVQMPRLDGLEATRRIRclpRHAGTPILAMTA 745
Cdd:PRK10529    4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLR---QWSAIPVIVLSA 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1590033346 746 NAFAEDKAVCFAAGMNDFIAKPVDPDQLYATL 777
Cdd:PRK10529   81 RSEESDKIAALDAGADDYLSKPFGIGELQARL 112
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
282-379 8.83e-03

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 39.66  E-value: 8.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 282 FNRAGERLLGHARQELLGRTEYDLFPAEQADALTARDREALATAGVVDIPEEAVDTRQGGRRILHTRKLaLRNAQGEAE- 360
Cdd:PRK10060  136 FNRLCEEYTGLKEHDVIGQSVFKLFMSRREAAASRRNIRGFFRSGNAYEVERWIKTRKGQRLFLFRNKF-VHSGSGKNEi 214
                          90
                  ....*....|....*....
gi 1590033346 361 FLLGMSEDITEAKRTAEEL 379
Cdd:PRK10060  215 FLICSGTDITEERRAQERL 233
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
710-770 9.01e-03

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 36.96  E-value: 9.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1590033346 710 LILMDVQMPRLDGLEATRRIRCLPRHAGTPILAMTANAFAEDKAVCFAAGMNDFIAKPVDP 770
Cdd:cd17581    56 MIITDYCMPGMTGYDLLKKVKESSALKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKL 116
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
703-779 9.14e-03

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


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 36.91  E-value: 9.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033346 703 AEANDYALILMDVQMPRLDGLEATRRIRCLPRHAGTPILAMtanAFAEDKAVCFAA---GMNDFIAKPVDPDQLYATLLT 779
Cdd:cd17539    37 AAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQLPILAV---ADPGDRGRLIRAleiGVNDYLVRPIDPNELLARVRT 113
 
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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