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Conserved domains on  [gi|1736044238|gb|KAA0526548|]
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two-component system sensor histidine kinase RcsC [Enterobacter kobei]

Protein Classification

two-component system sensor histidine kinase RcsC( domain architecture ID 11484985)

two-component system sensor histidine kinase RcsC forms part of a phospho-relay signal transduction pathway with RcsD and RcsB, and plays a role in swarming behavior, biofilm formation, pathogenicity, motility, and cell division

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
33-947 0e+00

two-component system sensor histidine kinase RcsC;


:

Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 1939.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238  33 SVFYIVNALHKKEAEIRQEFNLSSDQAQRYIQRTSDVMKELKYIAENRLTAENGILALRGRNDKTEVPDFQPLFPDSDCS 112
Cdd:PRK10841   10 SVFYIVNALHERESEIRQEFNLSSDQAQRYIRHTSDVMRELKYIAENRLSAENGVLSPRGRETKTDVPAFEPLFADSDCS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 113 TMSNTWRGSLESLAWFMRYWRDNFSAAYDLNRVFLIGSENLCMADFGLRDVPVERDDALKSLHERIVKYRNAPQDERGNN 192
Cdd:PRK10841   90 AMSNTWRGSLESLAWFMRYWRDNFSAAYDLNRVFLIGSDNLCMANFGLRNMPVERDTALKALHERINKYRNAPQQDKGSN 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 193 IFWISQGPRMGVGYFYALTPVYLGNRLQALLGIEQTIRMENFFTPGSLPMGVTILDENGHQLISLAGPDNRLNVDPHWMQ 272
Cdd:PRK10841  170 LYWISPGARPGVGYFYALTPVYLANRLQALLGIEQTIRLENFFTPGTLPMGVTLLDENGHPLLSLTGPESKIKADPRWPQ 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 273 ERSWFGYTSGFRELVLKKSLPPSSLSIVYSLPVDMVLERIRILIMNAILLNLLVGGALFTLARMYERRIFIPAESDAQRL 352
Cdd:PRK10841  250 ERSWFGYTDGFRELVLKKNLPPSSLSIVYSVPVDKVLERIRMLILNAILLNVLSAIVLFTLARLFERRIFIPAESNALRL 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 353 EEHEQFNRKIVASAPVGICILRTQDGTNILSNELAHNYLNMLTHEDRQRLTQIICGQQVNFVDVLTSTHTNLQISFVHSR 432
Cdd:PRK10841  330 EEHEQFNRKIVASAPVGICILRTSDGTNILSNELAHNYLNMLTHEDRQRLTQIICGQQVNFVDVLTSNNTNLQISFVHSR 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 433 YRNENVAICVLVDVSARVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMN 512
Cdd:PRK10841  410 YRNENVAICVLVDVSARVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMN 489
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 513 NSSSLLLKIISDILDFSKIESEQLKIEPREFSPREVMNHISANYLPLVVRKQLGLYCFIEPDVPLTLHGDPMRLQQVISN 592
Cdd:PRK10841  490 NSSSLLLKIISDILDFSKIESEQLKIEPREFSPREVINHITANYLPLVVKKRLGLYCFIEPDVPVALNGDPMRLQQVISN 569
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 593 LLSNAIKFTDIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLVSMMDGDI 672
Cdd:PRK10841  570 LLSNAIKFTDTGCIVLHVRVDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDI 649
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 673 SVDTEPGMGSQFTIRIPLYSAQYPAKATVDGLSDKRCWLAVNNASLNDYLTALLTHSGVRVCRYEDQTPDADDVLIADEM 752
Cdd:PRK10841  650 SVDSEPGMGSQFTIRIPLYGAQYPQKKGVEGLQGKRCWLAVRNASLEQFLETLLQRSGIQVQRYEGQEPTPEDVLITDDP 729
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 753 PEQAWQGRGTVLFCRRHIGIPVERAPGEWVHSVATPHELLSLLARIYKVQLEENDGAGELPSPEGLASVNDDMMILVVDD 832
Cdd:PRK10841  730 VQKKWQGRAVITFCRRHIGIPLEIAPGEWVHSTATPHELPALLARIYRIELESDDSANALPSTDKAVSDNDDMMILVVDD 809
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 833 HPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANALAEEKQ 912
Cdd:PRK10841  810 HPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVTANALAEEKQ 889
                         890       900       910
                  ....*....|....*....|....*....|....*
gi 1736044238 913 RCLESGMDSCLSKPVTLDVLKQTLSVYAERVRKTR 947
Cdd:PRK10841  890 RCLEAGMDSCLSKPVTLDVLKQTLTVYAERVRKSR 924
 
Name Accession Description Interval E-value
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
33-947 0e+00

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 1939.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238  33 SVFYIVNALHKKEAEIRQEFNLSSDQAQRYIQRTSDVMKELKYIAENRLTAENGILALRGRNDKTEVPDFQPLFPDSDCS 112
Cdd:PRK10841   10 SVFYIVNALHERESEIRQEFNLSSDQAQRYIRHTSDVMRELKYIAENRLSAENGVLSPRGRETKTDVPAFEPLFADSDCS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 113 TMSNTWRGSLESLAWFMRYWRDNFSAAYDLNRVFLIGSENLCMADFGLRDVPVERDDALKSLHERIVKYRNAPQDERGNN 192
Cdd:PRK10841   90 AMSNTWRGSLESLAWFMRYWRDNFSAAYDLNRVFLIGSDNLCMANFGLRNMPVERDTALKALHERINKYRNAPQQDKGSN 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 193 IFWISQGPRMGVGYFYALTPVYLGNRLQALLGIEQTIRMENFFTPGSLPMGVTILDENGHQLISLAGPDNRLNVDPHWMQ 272
Cdd:PRK10841  170 LYWISPGARPGVGYFYALTPVYLANRLQALLGIEQTIRLENFFTPGTLPMGVTLLDENGHPLLSLTGPESKIKADPRWPQ 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 273 ERSWFGYTSGFRELVLKKSLPPSSLSIVYSLPVDMVLERIRILIMNAILLNLLVGGALFTLARMYERRIFIPAESDAQRL 352
Cdd:PRK10841  250 ERSWFGYTDGFRELVLKKNLPPSSLSIVYSVPVDKVLERIRMLILNAILLNVLSAIVLFTLARLFERRIFIPAESNALRL 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 353 EEHEQFNRKIVASAPVGICILRTQDGTNILSNELAHNYLNMLTHEDRQRLTQIICGQQVNFVDVLTSTHTNLQISFVHSR 432
Cdd:PRK10841  330 EEHEQFNRKIVASAPVGICILRTSDGTNILSNELAHNYLNMLTHEDRQRLTQIICGQQVNFVDVLTSNNTNLQISFVHSR 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 433 YRNENVAICVLVDVSARVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMN 512
Cdd:PRK10841  410 YRNENVAICVLVDVSARVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMN 489
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 513 NSSSLLLKIISDILDFSKIESEQLKIEPREFSPREVMNHISANYLPLVVRKQLGLYCFIEPDVPLTLHGDPMRLQQVISN 592
Cdd:PRK10841  490 NSSSLLLKIISDILDFSKIESEQLKIEPREFSPREVINHITANYLPLVVKKRLGLYCFIEPDVPVALNGDPMRLQQVISN 569
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 593 LLSNAIKFTDIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLVSMMDGDI 672
Cdd:PRK10841  570 LLSNAIKFTDTGCIVLHVRVDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDI 649
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 673 SVDTEPGMGSQFTIRIPLYSAQYPAKATVDGLSDKRCWLAVNNASLNDYLTALLTHSGVRVCRYEDQTPDADDVLIADEM 752
Cdd:PRK10841  650 SVDSEPGMGSQFTIRIPLYGAQYPQKKGVEGLQGKRCWLAVRNASLEQFLETLLQRSGIQVQRYEGQEPTPEDVLITDDP 729
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 753 PEQAWQGRGTVLFCRRHIGIPVERAPGEWVHSVATPHELLSLLARIYKVQLEENDGAGELPSPEGLASVNDDMMILVVDD 832
Cdd:PRK10841  730 VQKKWQGRAVITFCRRHIGIPLEIAPGEWVHSTATPHELPALLARIYRIELESDDSANALPSTDKAVSDNDDMMILVVDD 809
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 833 HPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANALAEEKQ 912
Cdd:PRK10841  810 HPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVTANALAEEKQ 889
                         890       900       910
                  ....*....|....*....|....*....|....*
gi 1736044238 913 RCLESGMDSCLSKPVTLDVLKQTLSVYAERVRKTR 947
Cdd:PRK10841  890 RCLEAGMDSCLSKPVTLDVLKQTLTVYAERVRKSR 924
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
372-690 3.18e-75

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 249.83  E-value: 3.18e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 372 ILRTQDGTNILSNELAHNYLNMLTHEDRQRLTQIICGQQVNFVDVLTSTHTNLQISFVHSRYRNENVAICVLVDVSARVK 451
Cdd:COG0642    12 LLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 452 MEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQtKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKI 531
Cdd:COG0642    92 LLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLL-EELDEEQREYLETILRSADRLLRLINDLLDLSRL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 532 ESEQLKIEPREFSPREVMNHISANYLPLVVRKQLGLYCFIEPDVPlTLHGDPMRLQQVISNLLSNAIKFTDIG-CIVLHV 610
Cdd:COG0642   171 EAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLSNAIKYTPEGgTVTVSV 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 611 CRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGvqRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIPL 690
Cdd:COG0642   250 RREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLPL 327
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
461-939 3.29e-75

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: 266.26  E-value: 3.29e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 461 QAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEP 540
Cdd:TIGR02956 455 AEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISP 534
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 541 REFSPREVMNHISANYLPLVVRKQLGLYCFIEPDVPLTLHGDPMRLQQVISNLLSNAIKFTDIGCIVLHVCRAGD-YLSI 619
Cdd:TIGR02956 535 RPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDsSLLF 614
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 620 RVRDTGVGIPAKEVVRLFDPFFQVgTGvQRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIPLysaqypaka 699
Cdd:TIGR02956 615 EVEDTGCGIAEEEQATLFDAFTQA-DG-RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPL--------- 683
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 700 tvdglsdkrcwlavnnaslndyltallthsgvrvCRYEDQTPDADDVliadempeqawqgrgtvlfcrrHIGIPVERapg 779
Cdd:TIGR02956 684 ----------------------------------TRGKPAEDSATLT----------------------VIDLPPQR--- 704
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 780 ewvhsvatphellsllariykvqleendgagelpspeglasvnddmmILVVDDHPINRRLLADQLGSLGYQCKTANDGVD 859
Cdd:TIGR02956 705 -----------------------------------------------VLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQS 737
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 860 ALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQL---GLTLPVVGVTANALAEEKQRCLESGMDSCLSKPVTLDVLKQTL 936
Cdd:TIGR02956 738 ALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIygaKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMI 817

                  ...
gi 1736044238 937 SVY 939
Cdd:TIGR02956 818 AVI 820
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
586-690 8.10e-47

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: 162.66  E-value: 8.10e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 586 LQQVISNLLSNAIKFTDIGCIVLHVCRAGD-----YLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAI 660
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEeedgvQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1736044238 661 CEKLVSMMDGDISVDTEPGMGSQFTIRIPL 690
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
RcsC pfam09456
RcsC Alpha-Beta-Loop (ABL); This domain is found in the C-terminus of the phospho-relay kinase ...
709-799 8.59e-40

RcsC Alpha-Beta-Loop (ABL); This domain is found in the C-terminus of the phospho-relay kinase RcsC between pfam00512 and pfam00072, and forms a discrete alpha/beta/loop structure.


Pssm-ID: 462804 [Multi-domain]  Cd Length: 91  Bit Score: 141.67  E-value: 8.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 709 CWLAVNNASLNDYLTALLTHSGVRVCRYEDQTPDADDVLIADEMPEQAWQGRGTVLFCRRHIGIPVERAPGEWVHSVATP 788
Cdd:pfam09456   1 CWLDIRNASLEEYLLRLLQQSGLTVTRYEGQEPDADDVLISDYPLAIAWPVRAYIEFSRRHIGSPQETRPGYWLHSTATL 80
                          90
                  ....*....|.
gi 1736044238 789 HELLSLLARIY 799
Cdd:pfam09456  81 HELPALLERIY 91
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
581-690 8.26e-39

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 139.71  E-value: 8.26e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238  581 GDPMRLQQVISNLLSNAIKFT-DIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVqRNFQGTGLGLA 659
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRS-RKIGGTGLGLS 79
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1736044238  660 ICEKLVSMMDGDISVDTEPGMGSQFTIRIPL 690
Cdd:smart00387  80 IVKKLVELHGGEISVESEPGGGTTFTITLPL 110
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
440-690 9.92e-30

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: 125.63  E-value: 9.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 440 ICVLVDVSARVKMEeslqemaqaaeqasQSKSMFLATVSHELRTPLYGIIGNLDLL-----QTKEL-PKGVDrlVTamNN 513
Cdd:NF033092  356 IAVLHDVTEQEKIE--------------QERREFVANVSHELRTPLTTMRSYLEALadgawKDPELaPRFLG--VT--QN 417
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 514 SSSLLLKIISDILDFSKIESE--QLKIEPREFSprEVMNHIsANYLPLVVRKQlgLYCFIE--PDVPLTLHGDPMRLQQV 589
Cdd:NF033092  418 ETERMIRLVNDLLQLSRMDSKdyKLNKEWVNFN--EFFNYI-IDRFEMILKNK--NITFKRefPKRDLWVEIDTDKITQV 492
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 590 ISNLLSNAIKFT-DIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLVSMM 668
Cdd:NF033092  493 LDNIISNAIKYSpEGGTITFRLLETHNRIIISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAH 572
                         250       260
                  ....*....|....*....|..
gi 1736044238 669 DGDISVDTEPGMGSQFTIRIPL 690
Cdd:NF033092  573 GGRIWAESEEGKGTTIYFTLPY 594
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
451-689 1.05e-28

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 120.70  E-value: 1.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 451 KMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQtkelpKGVDRL----VTAMNNSSSLLLKIISDIL 526
Cdd:NF012163  221 KLAQDFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRAELEAIQ-----DGIRKFtpesLDSLQAEVGTLTKLVDDLH 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 527 DFSKIESEQLKIEPREFSPREVMNHISANYLPLVVRKQLGLYcFIEPDVPLTLhGDPMRLQQVISNLLSNAIKFTDI-GC 605
Cdd:NF012163  296 DLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELE-VSLPDSSLVF-GDRDRLMQLFNNLLENSLRYTDSgGS 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 606 IVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFT 685
Cdd:NF012163  374 LHISASQRPKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIV 453

                  ....
gi 1736044238 686 IRIP 689
Cdd:NF012163  454 VTLP 457
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
451-689 1.90e-25

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 111.66  E-value: 1.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 451 KMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLL--QTKELPKGVDRLVTAMNNSSSLLLKIISDILDF 528
Cdd:NF040691  252 QMADSLQRQIRQLEELSRLQQRFVSDVSHELRTPLTTIRMAADVIhdSRDDFDPATARSAELLHTELDRFESLLSDLLEI 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 529 SKIE--SEQLKIEPREFSP--REVMNHISanylPLVVRKQLGLYcFIEPDVPLTLHGDPMRLQQVISNLLSNAIKFTDIG 604
Cdd:NF040691  332 SRFDagAAELDVEPVDLRPlvRRVVDALR----QLAERAGVELR-VDAPGTPVVAEVDPRRVERVLRNLVVNAIEHGEGK 406
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 605 CIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQF 684
Cdd:NF040691  407 PVVVTVAQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQF 486

                  ....*
gi 1736044238 685 TIRIP 689
Cdd:NF040691  487 RLTLP 491
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
445-690 8.21e-18

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


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 86.20  E-value: 8.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 445 DVSARV-----------KMEESLQEMAQAAEQASQSKSMFLATVSHELRTP-------LYGIIGNL---DLLQTKELPKG 503
Cdd:NF012226  102 DLSARAedsqihsaeisELMHNFNDMAQKLESSVKNAQVWNAAIAHELRTPitilqgrLQGILDGVfepDPALFKSLLNQ 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 504 VDRLvtamnnssSLLlkiISDILDFSKIESEQLKIEPREFSPREVMNHISANYLPLVVRKQLglycFIEPDVPLTL-HGD 582
Cdd:NF012226  182 VEGL--------SHL---VEDLRTLSLVENQQLRLNYESVDLKDSIEKVLKMFEDRLEQAQL----TIVLNLTATPvFCD 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 583 PMRLQQVISNLLSNAIKFTDIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICE 662
Cdd:NF012226  247 RRRIEQVLIALIDNAIRYANAGKLKISSSVIQDDWILQIEDEGPGIAEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVH 326
                         250       260
                  ....*....|....*....|....*...
gi 1736044238 663 KLVSMMDGDISVdTEPGMGSQFTIRIPL 690
Cdd:NF012226  327 AIVIAHKGSIEY-SNSQGNSVFTIKLPA 353
 
Name Accession Description Interval E-value
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
33-947 0e+00

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 1939.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238  33 SVFYIVNALHKKEAEIRQEFNLSSDQAQRYIQRTSDVMKELKYIAENRLTAENGILALRGRNDKTEVPDFQPLFPDSDCS 112
Cdd:PRK10841   10 SVFYIVNALHERESEIRQEFNLSSDQAQRYIRHTSDVMRELKYIAENRLSAENGVLSPRGRETKTDVPAFEPLFADSDCS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 113 TMSNTWRGSLESLAWFMRYWRDNFSAAYDLNRVFLIGSENLCMADFGLRDVPVERDDALKSLHERIVKYRNAPQDERGNN 192
Cdd:PRK10841   90 AMSNTWRGSLESLAWFMRYWRDNFSAAYDLNRVFLIGSDNLCMANFGLRNMPVERDTALKALHERINKYRNAPQQDKGSN 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 193 IFWISQGPRMGVGYFYALTPVYLGNRLQALLGIEQTIRMENFFTPGSLPMGVTILDENGHQLISLAGPDNRLNVDPHWMQ 272
Cdd:PRK10841  170 LYWISPGARPGVGYFYALTPVYLANRLQALLGIEQTIRLENFFTPGTLPMGVTLLDENGHPLLSLTGPESKIKADPRWPQ 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 273 ERSWFGYTSGFRELVLKKSLPPSSLSIVYSLPVDMVLERIRILIMNAILLNLLVGGALFTLARMYERRIFIPAESDAQRL 352
Cdd:PRK10841  250 ERSWFGYTDGFRELVLKKNLPPSSLSIVYSVPVDKVLERIRMLILNAILLNVLSAIVLFTLARLFERRIFIPAESNALRL 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 353 EEHEQFNRKIVASAPVGICILRTQDGTNILSNELAHNYLNMLTHEDRQRLTQIICGQQVNFVDVLTSTHTNLQISFVHSR 432
Cdd:PRK10841  330 EEHEQFNRKIVASAPVGICILRTSDGTNILSNELAHNYLNMLTHEDRQRLTQIICGQQVNFVDVLTSNNTNLQISFVHSR 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 433 YRNENVAICVLVDVSARVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMN 512
Cdd:PRK10841  410 YRNENVAICVLVDVSARVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMN 489
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 513 NSSSLLLKIISDILDFSKIESEQLKIEPREFSPREVMNHISANYLPLVVRKQLGLYCFIEPDVPLTLHGDPMRLQQVISN 592
Cdd:PRK10841  490 NSSSLLLKIISDILDFSKIESEQLKIEPREFSPREVINHITANYLPLVVKKRLGLYCFIEPDVPVALNGDPMRLQQVISN 569
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 593 LLSNAIKFTDIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLVSMMDGDI 672
Cdd:PRK10841  570 LLSNAIKFTDTGCIVLHVRVDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDI 649
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 673 SVDTEPGMGSQFTIRIPLYSAQYPAKATVDGLSDKRCWLAVNNASLNDYLTALLTHSGVRVCRYEDQTPDADDVLIADEM 752
Cdd:PRK10841  650 SVDSEPGMGSQFTIRIPLYGAQYPQKKGVEGLQGKRCWLAVRNASLEQFLETLLQRSGIQVQRYEGQEPTPEDVLITDDP 729
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 753 PEQAWQGRGTVLFCRRHIGIPVERAPGEWVHSVATPHELLSLLARIYKVQLEENDGAGELPSPEGLASVNDDMMILVVDD 832
Cdd:PRK10841  730 VQKKWQGRAVITFCRRHIGIPLEIAPGEWVHSTATPHELPALLARIYRIELESDDSANALPSTDKAVSDNDDMMILVVDD 809
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 833 HPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANALAEEKQ 912
Cdd:PRK10841  810 HPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVTANALAEEKQ 889
                         890       900       910
                  ....*....|....*....|....*....|....*
gi 1736044238 913 RCLESGMDSCLSKPVTLDVLKQTLSVYAERVRKTR 947
Cdd:PRK10841  890 RCLEAGMDSCLSKPVTLDVLKQTLTVYAERVRKSR 924
PRK15347 PRK15347
two component system sensor kinase;
456-941 2.68e-88

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 302.33  E-value: 2.68e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 456 LQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKEL-PKGVDRLVTAMNNSSSLLlKIISDILDFSKIESE 534
Cdd:PRK15347  384 LAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLtAEQMDLADTARQCTLSLL-AIINNLLDFSRIESG 462
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 535 QLKIEPREFSPREVMNHISANYLPLVVRKQLGLYCFIEPDVPLTLHGDPMRLQQVISNLLSNAIKFTDIGCIVLHVCRAG 614
Cdd:PRK15347  463 QMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGGIRLRVKRHE 542
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 615 DYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTgvqrNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIPL--YS 692
Cdd:PRK15347  543 QQLCFTVEDTGCGIDIQQQQQIFTPFYQADT----HSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPLneYA 618
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 693 AQYPAKATVDglsdkrcwlavnnASLNdyLTALLTHSGVRvCRYEDQTPDADDvliadempeqawqgrgtvlfcrrhigi 772
Cdd:PRK15347  619 PPEPLKGELS-------------APLA--LHRQLSAWGIT-CQPGHQNPALLD--------------------------- 655
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 773 pverapgewvhsvatpHELLSLLARIYKVQLEENDGAGELPSpEGLASVNDDMMILVVDDHPINRRLLADQLGSLGYQCK 852
Cdd:PRK15347  656 ----------------PELAYLPGRLYDLLQQIIQGAPNEPV-INLPLQPWQLQILLVDDVETNRDIIGMMLVELGQQVT 718
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 853 TANDGVDALnVLSKNHI-DIVLSDVNMPNMDGYRLTQRIRQ----LGLTLPVVGVTANALAEEKQRCLESGMDSCLSKPV 927
Cdd:PRK15347  719 TAASGTEAL-ELGRQHRfDLVLMDIRMPGLDGLETTQLWRDdpnnLDPDCMIVALTANAAPEEIHRCKKAGMNHYLTKPV 797
                         490
                  ....*....|....
gi 1736044238 928 TLDVLKQTLSVYAE 941
Cdd:PRK15347  798 TLAQLARALELAAE 811
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
463-942 1.89e-82

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 285.97  E-value: 1.89e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 463 AEQASQSKSMFLATVSHELRTPLYGIIG-NLDLLQTKELPKGVDRLVT---AMNNssslLLKIISDILDFSKIESEQLKI 538
Cdd:PRK11107  286 AQEAARIKSEFLANMSHELRTPLNGVIGfTRQTLKTPLTPTQRDYLQTierSANN----LLAIINDILDFSKLEAGKLVL 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 539 EPREFSPREVMNHI------SANylplvvRKQLGLYCFIEPDVPLTLHGDPMRLQQVISNLLSNAIKFTDIGCIVLHV-C 611
Cdd:PRK11107  362 ENIPFSLRETLDEVvtllahSAH------EKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVeL 435
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 612 RAGD----YLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIR 687
Cdd:PRK11107  436 RALSntkvQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFH 515
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 688 IPLYSAQYPA--KATVDGLSDKRCWLAVNNASLNDYLTALLTHSGVRVC------RYEDQTPDADDVLIADEMPEQAWQG 759
Cdd:PRK11107  516 LPLDLNPNPIidGLPTDCLAGKRLLYVEPNSAAAQATLDILSETPLEVTysptlsQLPEAHYDILLLGLPVTFREPLTML 595
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 760 RGTVLFCRRH-----IGIP------VERAPGEWVHSV----ATPHELLSLLAriykvqleENDGAGELPSPEGLASVNDD 824
Cdd:PRK11107  596 HERLAKAKSMtdfliLALPcheqvlAEQLKQDGADAClskpLSHTRLLPALL--------EPCHHKQPPLLPPTDESRLP 667
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 825 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGL--TLPVVGV 902
Cdd:PRK11107  668 LTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHnqNTPIIAV 747
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 1736044238 903 TANALAEEKQRCLESGMDSCLSKPVTLDVLKQTLSVYAER 942
Cdd:PRK11107  748 TAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKPG 787
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
372-690 3.18e-75

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 249.83  E-value: 3.18e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 372 ILRTQDGTNILSNELAHNYLNMLTHEDRQRLTQIICGQQVNFVDVLTSTHTNLQISFVHSRYRNENVAICVLVDVSARVK 451
Cdd:COG0642    12 LLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 452 MEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQtKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKI 531
Cdd:COG0642    92 LLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLL-EELDEEQREYLETILRSADRLLRLINDLLDLSRL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 532 ESEQLKIEPREFSPREVMNHISANYLPLVVRKQLGLYCFIEPDVPlTLHGDPMRLQQVISNLLSNAIKFTDIG-CIVLHV 610
Cdd:COG0642   171 EAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLSNAIKYTPEGgTVTVSV 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 611 CRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGvqRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIPL 690
Cdd:COG0642   250 RREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLPL 327
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
461-939 3.29e-75

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: 266.26  E-value: 3.29e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 461 QAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEP 540
Cdd:TIGR02956 455 AEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISP 534
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 541 REFSPREVMNHISANYLPLVVRKQLGLYCFIEPDVPLTLHGDPMRLQQVISNLLSNAIKFTDIGCIVLHVCRAGD-YLSI 619
Cdd:TIGR02956 535 RPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDsSLLF 614
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 620 RVRDTGVGIPAKEVVRLFDPFFQVgTGvQRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIPLysaqypaka 699
Cdd:TIGR02956 615 EVEDTGCGIAEEEQATLFDAFTQA-DG-RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPL--------- 683
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 700 tvdglsdkrcwlavnnaslndyltallthsgvrvCRYEDQTPDADDVliadempeqawqgrgtvlfcrrHIGIPVERapg 779
Cdd:TIGR02956 684 ----------------------------------TRGKPAEDSATLT----------------------VIDLPPQR--- 704
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 780 ewvhsvatphellsllariykvqleendgagelpspeglasvnddmmILVVDDHPINRRLLADQLGSLGYQCKTANDGVD 859
Cdd:TIGR02956 705 -----------------------------------------------VLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQS 737
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 860 ALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQL---GLTLPVVGVTANALAEEKQRCLESGMDSCLSKPVTLDVLKQTL 936
Cdd:TIGR02956 738 ALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIygaKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMI 817

                  ...
gi 1736044238 937 SVY 939
Cdd:TIGR02956 818 AVI 820
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
456-693 4.57e-70

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 232.49  E-value: 4.57e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 456 LQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKE--LPKGVDRLVTAMNNSSSLLLKIISDILDFSKIES 533
Cdd:COG2205     2 LEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEdlSPEERRELLEIIRESAERLLRLIEDLLDLSRLES 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 534 EQLKIEPREFSPREVMNHISANYLPLVVRKQLGLYCFIEPDvPLTLHGDPMRLQQVISNLLSNAIKFTDIGC-IVLHVCR 612
Cdd:COG2205    82 GKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPE-LPLVYADPELLEQVLANLLDNAIKYSPPGGtITISARR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 613 AGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTgvQRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIPLYS 692
Cdd:COG2205   161 EGDGVRISVSDNGPGIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLAE 238

                  .
gi 1736044238 693 A 693
Cdd:COG2205   239 S 239
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
307-693 9.64e-67

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 228.67  E-value: 9.64e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 307 MVLERIRILIMNAILLNLLVGGALFTLARMYERRIFIPAESDAQRLEEHEQFNRKIVASAPVGICILRTQDGTNILSNEL 386
Cdd:COG5002     3 LLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 387 AHNYLNMLTHEDRQRLTQIICGQQVNFVDVLTSTHTNLQISFVHSRYRNENVAIcVLVDVSARVKMEESLQEMAQAAEQA 466
Cdd:COG5002    83 LLLLALLLLLLLLLLLLALLILLLLLALLILLAALLLLLSELLLLLLLLGRLSL-RLSALLLGLLLLAAVERDITELERL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 467 SQSKSMFLATVSHELRTPLYGIIGNLDLLQT--KELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEPREFS 544
Cdd:COG5002   162 EQMRREFVANVSHELRTPLTSIRGYLELLLDgaADDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 545 PREVMNHISANYLPLVVRKQLGLYCFIEPDvPLTLHGDPMRLQQVISNLLSNAIKFTDIG-CIVLHVCRAGDYLSIRVRD 623
Cdd:COG5002   242 LAELLEEVVEELRPLAEEKGIELELDLPED-PLLVLGDPDRLEQVLTNLLDNAIKYTPEGgTITVSLREEDDQVRISVRD 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 624 TGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIPLYSA 693
Cdd:COG5002   321 TGIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPLARE 390
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
438-937 2.17e-58

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 218.45  E-value: 2.17e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238  438 VAICVLVDVSARVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKG--VDRLVTAMNNSS 515
Cdd:PRK09959   680 VYICGWQDITETRDLIHALEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEqrVEAISLAYATGQ 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238  516 SLLlKIISDILDFSKIESEQLKIEPREFSPREVMNHISANYLPLVVRKQLGLYCFIE-PDVPLtLHGDPMRLQQVISNLL 594
Cdd:PRK09959   760 SLL-GLIGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTfPDHYL-VKIDPQAFKQVLSNLL 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238  595 SNAIKFTDIGCI-----VLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNfqGTGLGLAICEKLVSMMD 669
Cdd:PRK09959   838 SNALKFTTEGAVkittsLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQT--GSGLGLMICKELIKNMQ 915
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238  670 GDISVDTEPGMGSQFTIRIPLysaqypakatvdglsdkrcwlavnnaslndyltallthsgvrvcryedqtpdaddvlia 749
Cdd:PRK09959   916 GDLSLESHPGIGTTFTITIPV----------------------------------------------------------- 936
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238  750 dempeqawqgrgtvlfcrrhigipverapgewvhsvatphELLSLLARIykvqleENDGAGELPSPEGLAsvnddmmILV 829
Cdd:PRK09959   937 ----------------------------------------EISQQVATV------EAKAEQPITLPEKLS-------ILI 963
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238  830 VDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANALAE 909
Cdd:PRK09959   964 ADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANAQAN 1043
                          490       500
                   ....*....|....*....|....*...
gi 1736044238  910 EKQRCLESGMDSCLSKPVTLDVLKQTLS 937
Cdd:PRK09959  1044 EREKGLSCGMNLCLFKPLTLDVLKTHLS 1071
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
445-936 1.90e-50

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 191.31  E-value: 1.90e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 445 DVSARVKMEESLqemaqaaEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISD 524
Cdd:PRK11091  265 DITERKRYQDAL-------EKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFND 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 525 ILDFSKIESEQLKIEPREFSPREVMNHISaNYLPLVVrKQLGLYCFIEPDVPL--TLHGDPMRLQQVISNLLSNAIKFTD 602
Cdd:PRK11091  338 IIDMDKMERRKLQLDNQPIDFTDFLADLE-NLSGLQA-EQKGLRFDLEPLLPLphKVITDGTRLRQILWNLISNAVKFTQ 415
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 603 IGCIVLHV-CRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQ-GTGLGLAICEKLVSMMDGDISVDTEPGM 680
Cdd:PRK11091  416 QGGVTVRVrYEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHGGKPAtGTGIGLAVSKRLAQAMGGDITVTSEEGK 495
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 681 GSQFTIRIPLysaqyPAKATVdglsdkrcwlavnnaslndyltallthsgvrvcryedqtpdADDVLIADEMPeqawqgr 760
Cdd:PRK11091  496 GSCFTLTIHA-----PAVAEE-----------------------------------------VEDAFDEDDMP------- 522
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 761 gtvlfcrrhigipverapgewvhsvatphellsllariykvqleendgageLPSpeglasvnddMMILVVDDHPINRRLL 840
Cdd:PRK11091  523 ---------------------------------------------------LPA----------LNILLVEDIELNVIVA 541
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 841 ADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQ--LGLTL-PVVGVTANALAEEKQRcLES 917
Cdd:PRK11091  542 RSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELREryPREDLpPLVALTANVLKDKKEY-LDA 620
                         490
                  ....*....|....*....
gi 1736044238 918 GMDSCLSKPVTLDVLKQTL 936
Cdd:PRK11091  621 GMDDVLSKPLSVPALTAMI 639
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
445-755 1.96e-49

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 189.35  E-value: 1.96e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 445 DVSARVKMEES-LQEMA----QA---AEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSS 516
Cdd:PRK11466  411 QLAAQVKARTAeLQELViehrQAraeAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGE 490
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 517 LLLKIISDILDFSKIE--SEQLKIEPREFSPREVMNHISANYLPLVVRKQLGLYCFIEPDVPLTLHGDPMRLQQVISNLL 594
Cdd:PRK11466  491 SLLTILNDILDYSAIEagGKNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLL 570
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 595 SNAIKFTDIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTgvQRNfqGTGLGLAICEKLVSMMDGDISV 674
Cdd:PRK11466  571 SNALRFTDEGSIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFVQVSG--KRG--GTGLGLTISSRLAQAMGGELSA 646
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 675 DTEPGMGSQFTIRIPLYSAQYPAKATVD---GLSDKRCWLAVNNAsLNDYLTA-LLTHSGVRV-----------CRYEDQ 739
Cdd:PRK11466  647 TSTPEVGSCFCLRLPLRVATAPVPKTVNqavRLDGLRLLLIEDNP-LTQRITAeMLNTSGAQVvavgnaaqaleTLQNSE 725
                         330       340
                  ....*....|....*....|....*.
gi 1736044238 740 T----------PDADDVLIADEMPEQ 755
Cdd:PRK11466  726 PfaaalvdfdlPDYDGITLARQLAQQ 751
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
586-690 8.10e-47

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: 162.66  E-value: 8.10e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 586 LQQVISNLLSNAIKFTDIGCIVLHVCRAGD-----YLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAI 660
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEeedgvQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1736044238 661 CEKLVSMMDGDISVDTEPGMGSQFTIRIPL 690
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
827-936 1.21e-46

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: 162.25  E-value: 1.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGL---TLPVVGVT 903
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGggrRTPIIALT 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1736044238 904 ANALAEEKQRCLESGMDSCLSKPVTLDVLKQTL 936
Cdd:cd17546    81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
299-693 6.95e-46

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 172.66  E-value: 6.95e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 299 IVYSLPVDMVLERIRILIMNAILLNLLVGGALFTLARMYERRIFIPAESDAQRLEEHEQFNRKIVASAPVGICILRTQDG 378
Cdd:COG4251   122 LLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLL 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 379 TNILSNELAHNYLNMLTHEDRQRLTQIICGQQVNFVDVLTSTHTNLQISFVHSRYRNEnvaicvlvdvsARVKMEESLQE 458
Cdd:COG4251   202 LLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRL-----------ELEELEEELEE 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 459 MAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTK---ELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQ 535
Cdd:COG4251   271 RTAELERSNEELEQFAYVASHDLREPLRKISGFSQLLEEDygdKLDEEGREYLERIRDAAERMQALIDDLLAYSRVGRQE 350
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 536 LKIEPreFSPREVMNHISANYLPLVVRKQLGlycfIEPDVPLTLHGDPMRLQQVISNLLSNAIKFTD---IGCIVLHVCR 612
Cdd:COG4251   351 LEFEP--VDLNELLEEVLEDLEPRIEERGAE----IEVGPLPTVRGDPTLLRQVFQNLISNAIKYSRpgePPRIEIGAER 424
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 613 AGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTgvQRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIPLYS 692
Cdd:COG4251   425 EGGEWVFSVRDNGIGIDPEYAEKIFEIFQRLHS--RDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLPKAP 502

                  .
gi 1736044238 693 A 693
Cdd:COG4251   503 A 503
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
350-690 4.12e-44

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: 165.52  E-value: 4.12e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 350 QRLEEHEQFNRKIVASAPVGICILrTQDGTNILSNELAHNYLNMLTHEDRQRLTQIICGQQ--VNFVDVLTSTHTNLQIS 427
Cdd:COG5000    83 EELEERRRYLETILENLPAGVIVL-DADGRITLANPAAERLLGIPLEELIGKPLEELLPELdlAELLREALERGWQEEIE 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 428 FVHSRYRNENVAICVLVDVSARVKMEEsLQEMAQAAEQASQSKsmFLATVSHELRTPLYGIIGNLDLLQTKELPKG---- 503
Cdd:COG5000   162 LTRDGRRTLLVRASPLRDDGYVIVFDD-ITELLRAERLAAWGE--LARRIAHEIKNPLTPIQLSAERLRRKLADKLeedr 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 504 --VDRLVTAMNNSSSLLLKIISDILDFSKIEseqlKIEPREFSPREVMNHISANYLPLVVRKQLGLYCFIEPDVPLtLHG 581
Cdd:COG5000   239 edLERALDTIIRQVDRLKRIVDEFLDFARLP----EPQLEPVDLNELLREVLALYEPALKEKDIRLELDLDPDLPE-VLA 313
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 582 DPMRLQQVISNLLSNAIKFT-DIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFqvgTGVQrnfQGTGLGLAI 660
Cdd:COG5000   314 DRDQLEQVLINLLKNAIEAIeEGGEIEVSTRREDGRVRIEVSDNGPGIPEEVLERIFEPFF---TTKP---KGTGLGLAI 387
                         330       340       350
                  ....*....|....*....|....*....|
gi 1736044238 661 CEKLVSMMDGDISVDTEPGMGSQFTIRIPL 690
Cdd:COG5000   388 VKKIVEEHGGTIELESRPGGGTTFTIRLPL 417
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
351-697 2.48e-43

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 161.55  E-value: 2.48e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 351 RLEEHEQFNRKIVASAPVGICILrTQDGTNILSNELAHNYLNM---------------LTHEDRQRLTQIICGQQVNF-- 413
Cdd:COG3852     1 ALRESEELLRAILDSLPDAVIVL-DADGRITYVNPAAERLLGLsaeellgrplaelfpEDSPLRELLERALAEGQPVTer 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 414 -VDVLTSTHTNLQISFVHSRYRNENVAICVLV---DVSARVKMEESLQEMAQAAeqasqSKSMFLATVSHELRTPLYGII 489
Cdd:COG3852    80 eVTLRRKDGEERPVDVSVSPLRDAEGEGGVLLvlrDITERKRLERELRRAEKLA-----AVGELAAGLAHEIRNPLTGIR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 490 GNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKieseQLKIEPREFSPREVMNHIsanyLPLV---VRKQLG 566
Cdd:COG3852   155 GAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSR----PRPPEREPVNLHEVLERV----LELLraeAPKNIR 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 567 LYCFIEPDVPLtLHGDPMRLQQVISNLLSNAIK-FTDIGCIVL----------HVCRAGDYLSIRVRDTGVGIPAKEVVR 635
Cdd:COG3852   227 IVRDYDPSLPE-VLGDPDQLIQVLLNLVRNAAEaMPEGGTITIrtrverqvtlGGLRPRLYVRIEVIDNGPGIPEEILDR 305
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1736044238 636 LFDPFFqvgTGvqrNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIPLYSAQYPA 697
Cdd:COG3852   306 IFEPFF---TT---KEKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQAEEEP 361
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
329-696 6.79e-43

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: 163.61  E-value: 6.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 329 ALFTLARMYERRIFIPAEsdaqrLEEHEQFNRKIVASAPVGICILrTQDGTNILSNELA-------------HNYLNMLT 395
Cdd:COG5809   118 GMLAISRDITERKRMEEA-----LRESEEKFRLIFNHSPDGIIVT-DLDGRIIYANPAAckllgisieeligKSILELIH 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 396 HEDRQRLTQIIC-----GQQVNFVDVLTSTHTN---LQISFVH-SRYRNENVAICVLVDVSARVKMEESLQemaqaaeqA 466
Cdd:COG5809   192 SDDQENVAAFISqllkdGGIAQGEVRFWTKDGRwrlLEASGAPiKKNGEVDGIVIIFRDITERKKLEELLR--------K 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 467 SQSKSM---FLATVSHELRTPLYGIIGNLDLLQ--------------TKELpkgvDRlvtaMNNssslllkIISDILDFS 529
Cdd:COG5809   264 SEKLSVvgeLAAGIAHEIRNPLTSLKGFIQLLKdtideeqktyldimLSEL----DR----IES-------IISEFLVLA 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 530 KIESeqlkIEPREFSPREVMNHISANYLPLVVRKQLGLYCFIEPDVPLTLhGDPMRLQQVISNLLSNAIKFT-DIGCIVL 608
Cdd:COG5809   329 KPQA----IKYEPKDLNTLIEEVIPLLQPQALLKNVQIELELEDDIPDIL-GDENQLKQVFINLLKNAIEAMpEGGNITI 403
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 609 HV-CRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQvgtgvqRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIR 687
Cdd:COG5809   404 ETkAEDDDKVVISVTDEGCGIPEERLKKLGEPFYT------TKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSIT 477

                  ....*....
gi 1736044238 688 IPLYSAQYP 696
Cdd:COG5809   478 LPIKLSEQV 486
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
827-945 1.83e-42

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 150.77  E-value: 1.83e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQL--GLTLPVVGVTA 904
Cdd:COG0784     8 ILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALprLPDIPIIALTA 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKPVTLDVLKQTLSVYAERVRK 945
Cdd:COG0784    88 YADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
445-690 7.45e-42

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 157.27  E-value: 7.45e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 445 DVSARVKMEESLQEMAQAAEQASQSKSM--FLATVSHELRTPLYGIIGNLDLLQTK--------ELPKGVDRLVTAMNNS 514
Cdd:COG4191   115 DITELERAEEELRELQEQLVQSEKLAALgeLAAGIAHEINNPLAAILGNAELLRRRledepdpeELREALERILEGAERA 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 515 SslllKIISDILDFSKIESEqlkiEPREFSPREVMN---HISANYLP---LVVRKQLGlycfiePDVPLtLHGDPMRLQQ 588
Cdd:COG4191   195 A----EIVRSLRAFSRRDEE----EREPVDLNELIDealELLRPRLKargIEVELDLP------PDLPP-VLGDPGQLEQ 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 589 VISNLLSNAI---KFTDIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFF---QVGtgvqrnfQGTGLGLAICE 662
Cdd:COG4191   260 VLLNLLINAIdamEEGEGGRITISTRREGDYVVISVRDNGPGIPPEVLERIFEPFFttkPVG-------KGTGLGLSISY 332
                         250       260
                  ....*....|....*....|....*...
gi 1736044238 663 KLVSMMDGDISVDTEPGMGSQFTIRIPL 690
Cdd:COG4191   333 GIVEKHGGRIEVESEPGGGTTFTITLPL 360
RcsC pfam09456
RcsC Alpha-Beta-Loop (ABL); This domain is found in the C-terminus of the phospho-relay kinase ...
709-799 8.59e-40

RcsC Alpha-Beta-Loop (ABL); This domain is found in the C-terminus of the phospho-relay kinase RcsC between pfam00512 and pfam00072, and forms a discrete alpha/beta/loop structure.


Pssm-ID: 462804 [Multi-domain]  Cd Length: 91  Bit Score: 141.67  E-value: 8.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 709 CWLAVNNASLNDYLTALLTHSGVRVCRYEDQTPDADDVLIADEMPEQAWQGRGTVLFCRRHIGIPVERAPGEWVHSVATP 788
Cdd:pfam09456   1 CWLDIRNASLEEYLLRLLQQSGLTVTRYEGQEPDADDVLISDYPLAIAWPVRAYIEFSRRHIGSPQETRPGYWLHSTATL 80
                          90
                  ....*....|.
gi 1736044238 789 HELLSLLARIY 799
Cdd:pfam09456  81 HELPALLERIY 91
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
581-690 8.26e-39

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 139.71  E-value: 8.26e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238  581 GDPMRLQQVISNLLSNAIKFT-DIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVqRNFQGTGLGLA 659
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRS-RKIGGTGLGLS 79
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1736044238  660 ICEKLVSMMDGDISVDTEPGMGSQFTIRIPL 690
Cdd:smart00387  80 IVKKLVELHGGEISVESEPGGGTTFTITLPL 110
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
352-688 2.77e-38

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: 146.20  E-value: 2.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 352 LEEHEQFnRKIVASAPVGICILRtQDGTNILSNELAHNYLNMLTHED-RQRLTQIIcgQQVNFVDVLTSTHTnlQISFVH 430
Cdd:TIGR02966   2 SALLSRF-RAAAQALPDAVVVLD-EEGQIEWCNPAAERLLGLRWPDDlGQRITNLI--RHPEFVEYLAAGRF--SEPLEL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 431 SRYRNENVaicvlvDVSARVK--MEESLQEMAQ---AAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQ--TKELPKG 503
Cdd:TIGR02966  76 PSPINSER------VLEIRIApyGEEQKLLVARdvtRLRRLEQMRRDFVANVSHELRTPLTVLRGYLETLAdgPDEDPEE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 504 VDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEPREFSPREVMNHISANYLPLVVRKQLGLYCFIEPDVPltLHGDP 583
Cdd:TIGR02966 150 WNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALLDHLRDEAEALSQGKNHQITFEIDGGVD--VLGDE 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 584 MRLQQVISNLLSNAIKFT-DIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICE 662
Cdd:TIGR02966 228 DELRSAFSNLVSNAIKYTpEGGTITVRWRRDGGGAEFSVTDTGIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVK 307
                         330       340
                  ....*....|....*....|....*.
gi 1736044238 663 KLVSMMDGDISVDTEPGMGSQFTIRI 688
Cdd:TIGR02966 308 HVLSRHHARLEIESELGKGSTFSFIF 333
KinD COG5808
Sporulation sensor histidine kinase D [Cell cycle control, cell division, chromosome ...
453-693 9.75e-36

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


Pssm-ID: 444510 [Multi-domain]  Cd Length: 454  Bit Score: 141.81  E-value: 9.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 453 EESLQEMAQAA--EQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSK 530
Cdd:COG5808   222 RKTLLERVIQEinTQKLELIGTFAASTAHEIRNPLTSIKGFIQLLQEKYPELEDQKYFDIIQEEIQRINQIVSEFLVLGK 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 531 IESEQLKIEprefSPREVMNHISANYLPLVVRKQLGLYcFIEPDVPLTLHGDPMRLQQVISNLLSNAIKFT-DIGCIVLH 609
Cdd:COG5808   302 PTAKKLELD----DLNELIEEILSIIDSEANLKNIRVE-KQSLDEPLHIKCDKDRIKQVLLNLIKNAIEAMkEGGKLTIS 376
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 610 VCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGvqrnfqGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIP 689
Cdd:COG5808   377 IENDDEKAVIEVIDNGEGIPEDIIDEIFEPFVTTKEG------GTGLGLSVCKRIVEMHGGEIDIESEEGKGTTFTIRLP 450

                  ....
gi 1736044238 690 LYSA 693
Cdd:COG5808   451 LKKE 454
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
827-936 9.63e-35

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: 130.80  E-value: 9.63e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT--LPVVGVTA 904
Cdd:COG3706     4 ILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTadIPIIFLTA 83
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKPVTLDVLKQTL 936
Cdd:COG3706    84 LDDEEDRARALEAGADDYLTKPFDPEELLARV 115
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
581-690 9.75e-34

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: 125.17  E-value: 9.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 581 GDPMRLQQVISNLLSNAIKFTDI-GCIVLHVcRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTgvqRNFQGTGLGLA 659
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKaGEITVTL-SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADK---RGGGGTGLGLS 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1736044238 660 ICEKLVSMMDGDISVDTEPGMGSQFTIRIPL 690
Cdd:pfam02518  77 IVRKLVELLGGTITVESEPGGGTTVTLTLPL 107
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
827-936 2.97e-33

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: 123.80  E-value: 2.97e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANA 906
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1736044238 907 LAEEKQRCLESGMDSCLSKPVTLDVLKQTL 936
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAI 110
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
827-948 5.33e-33

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: 126.61  E-value: 5.33e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANA 906
Cdd:COG0745     4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTARD 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1736044238 907 LAEEKQRCLESGMDSCLSKPVTLDVLKQTLSVYAERVRKTRI 948
Cdd:COG0745    84 DEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAAEVL 125
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
291-756 7.35e-32

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 133.90  E-value: 7.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 291 SLPPSSLSIVYSLP-----VDMVLERIRILIMNAILLNLLVGGaLFTLARMYERrifiPAESDAQRLEEHEQFNRKIVAS 365
Cdd:PRK10618  277 ALNSTPLKLVYQVPlgtllLDLLQNNLWPLLLNLGLLALSLFG-YYTFRHQYGR----PTESMSHELRILRALNEEIVSN 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 366 APVGICILRTQDGTNILSNELAHNylnMLTHEDRQRLTQIicGQQVNFVDVLTSTHTNLQISFVHSRYRNEnVAICVLVD 445
Cdd:PRK10618  352 LPLGLLVYDFESNRTVISNKIADH---LLPHLNLQKITTM--AEQHQGVIQATINNELYEIRMFRSQLAPR-TQLFLLRD 425
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 446 VSARVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDI 525
Cdd:PRK10618  426 QDREVLVNKKLQQAQREYEKNQQARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNI 505
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 526 LDFSKIESEQLKIEPREFSPREVMNHISANYLPLVVRKQLGLYCFIEPDVPLTLHGDPMRLQQVISNLLSNAIKFTDIGC 605
Cdd:PRK10618  506 QLLNMLETQDWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYGK 585
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 606 IVLHVCRAGDY---LSIRVRDTGVGIPAKEVVRLFDPFFQvGTGVQRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGS 682
Cdd:PRK10618  586 ITLEVDQDESSpdrLTIRILDTGAGVSIKELDNLHFPFLN-QTQGDRYGKASGLTFFLCNQLCRKLGGHLTIKSREGLGT 664
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1736044238 683 QFTIRIPLYSAQYPAKATVDGLSDKRC-WLAVNNASLNDYLTALLTHSGVRVCRYEDQTPDAD-DVLIADeMPEQA 756
Cdd:PRK10618  665 RYSIHLKMLAADPEVEEEEEKLLDGVTvLLDITSEEVRKIVTRQLENWGATCITPDERLISQEyDIFLTD-NPSNL 739
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
827-947 7.52e-32

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: 124.12  E-value: 7.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT--LPVVGVTA 904
Cdd:COG3437     9 VLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTrdIPVIFLTA 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKPVTLDVLKQTLSVYAERVRKTR 947
Cdd:COG3437    89 LADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQR 131
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
452-689 1.59e-30

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: 126.35  E-value: 1.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 452 MEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKelPKGVDRLVTAMnnSSSL-----LLKIISDIL 526
Cdd:TIGR01386 223 LAQSFNAMLGRLEDAFQRLSQFSADLAHELRTPLTNLLGQTQVALSQ--PRTGEEYREVL--ESNLeelerLSRMVSDML 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 527 DFSKIESEQLKIEPREFSPREVMNHISANYLPLVVRKQLGlycfIEPDVPLTLHGDPMRLQQVISNLLSNAIKFT-DIGC 605
Cdd:TIGR01386 299 FLARADNGQLALERVRLDLAAELAKVAEYFEPLAEERGVR----IRVEGEGLVRGDPQMFRRAISNLLSNALRHTpDGGT 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 606 IVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMgSQFT 685
Cdd:TIGR01386 375 ITVRIERRSDEVRVSVSNPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAESPDGK-TRFI 453

                  ....
gi 1736044238 686 IRIP 689
Cdd:TIGR01386 454 LRFP 457
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
440-690 9.92e-30

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: 125.63  E-value: 9.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 440 ICVLVDVSARVKMEeslqemaqaaeqasQSKSMFLATVSHELRTPLYGIIGNLDLL-----QTKEL-PKGVDrlVTamNN 513
Cdd:NF033092  356 IAVLHDVTEQEKIE--------------QERREFVANVSHELRTPLTTMRSYLEALadgawKDPELaPRFLG--VT--QN 417
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 514 SSSLLLKIISDILDFSKIESE--QLKIEPREFSprEVMNHIsANYLPLVVRKQlgLYCFIE--PDVPLTLHGDPMRLQQV 589
Cdd:NF033092  418 ETERMIRLVNDLLQLSRMDSKdyKLNKEWVNFN--EFFNYI-IDRFEMILKNK--NITFKRefPKRDLWVEIDTDKITQV 492
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 590 ISNLLSNAIKFT-DIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLVSMM 668
Cdd:NF033092  493 LDNIISNAIKYSpEGGTITFRLLETHNRIIISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAH 572
                         250       260
                  ....*....|....*....|..
gi 1736044238 669 DGDISVDTEPGMGSQFTIRIPL 690
Cdd:NF033092  573 GGRIWAESEEGKGTTIYFTLPY 594
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
828-926 1.10e-29

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: 113.48  E-value: 1.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 828 LVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANAL 907
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80
                          90
                  ....*....|....*....
gi 1736044238 908 AEEKQRCLESGMDSCLSKP 926
Cdd:cd00156    81 EEDAVRALELGADDYLVKP 99
PRK09303 PRK09303
histidine kinase;
457-691 5.41e-29

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 120.06  E-value: 5.41e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 457 QEMAQAAEQAsQSKSMFLATVSHELRTPLYGI---IGNLDLLQTKEL----PKGVDRLVTAMNNSSSLLLKIISDILDFS 529
Cdd:PRK09303  139 QENETLLEQL-KFKDRVLAMLAHDLRTPLTAAslaLETLELGQIDEDtelkPALIEQLQDQARRQLEEIERLITDLLEVG 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 530 KIESEQLKIEPREFSPREVMNHISANYLPLVVRKQLGLYCFIEPDVPlTLHGDPMRLQQVISNLLSNAIKFT----DIGC 605
Cdd:PRK09303  218 RTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSDLP-SVYADQERIRQVLLNLLDNAIKYTpeggTITL 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 606 IVLHvcRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVgtgvQRNFQ--GTGLGLAICEKLVSMMDGDISVDTEPGMGSQ 683
Cdd:PRK09303  297 SMLH--RTTQKVQVSICDTGPGIPEEEQERIFEDRVRL----PRDEGteGYGIGLSVCRRIVRVHYGQIWVDSEPGQGSC 370

                  ....*...
gi 1736044238 684 FTIRIPLY 691
Cdd:PRK09303  371 FHFTLPVY 378
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
451-689 1.05e-28

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 120.70  E-value: 1.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 451 KMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQtkelpKGVDRL----VTAMNNSSSLLLKIISDIL 526
Cdd:NF012163  221 KLAQDFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRAELEAIQ-----DGIRKFtpesLDSLQAEVGTLTKLVDDLH 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 527 DFSKIESEQLKIEPREFSPREVMNHISANYLPLVVRKQLGLYcFIEPDVPLTLhGDPMRLQQVISNLLSNAIKFTDI-GC 605
Cdd:NF012163  296 DLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELE-VSLPDSSLVF-GDRDRLMQLFNNLLENSLRYTDSgGS 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 606 IVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFT 685
Cdd:NF012163  374 LHISASQRPKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIV 453

                  ....
gi 1736044238 686 IRIP 689
Cdd:NF012163  454 VTLP 457
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
349-690 1.15e-28

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 122.38  E-value: 1.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 349 AQRLEEHEQFNRKIVASAPVGIcILRTQDGTNILSNELAHNYLNMLTHEdrqrltqiICGQQVN--------FVDVLTST 420
Cdd:PRK11360  254 AQALRETRSLNELILESIADGV-IAIDRQGKITTMNPAAEVITGLQRHE--------LVGKPYSelfppntpFASPLLDT 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 421 ------HTNLQISFVH-----------SRYRN--ENV--AICVLVDVSARVKMEEslqEMAQAAEQASQSKSMflATVSH 479
Cdd:PRK11360  325 lehgteHVDLEISFPGrdrtielsvstSLLHNthGEMigALVIFSDLTERKRLQR---RVARQERLAALGELV--AGVAH 399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 480 ELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKieseqlkiePREFSPREVmnhisanYLPL 559
Cdd:PRK11360  400 EIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEFSR---------PRESQWQPV-------SLNA 463
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 560 VVRKQLGLY------------CFIEPDVPLTLhGDPMRLQQVISNLLSNAIK-FTDIGCIVLHVCRAGD-YLSIRVRDTG 625
Cdd:PRK11360  464 LVEEVLQLFqtagvqarvdfeTELDNELPPIW-ADPELLKQVLLNILINAVQaISARGKIRIRTWQYSDgQVAVSIEDNG 542
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1736044238 626 VGIPAKEVVRLFDPFFQVGTgvqrnfQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIPL 690
Cdd:PRK11360  543 CGIDPELLKKIFDPFFTTKA------KGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPI 601
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
475-691 5.32e-28

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: 117.66  E-value: 5.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 475 ATVSHELRTPLYGIIGNLDLLQTKELPKgvDRLVTAMnnssSLLLK-------IISDILDFSKIESEqlKIEPREFSprE 547
Cdd:COG5806   206 ASIAHEVRNPLTVVRGFIQLLQEPELSD--EKRKQYI----RIALEeldraeaIITDYLTFAKPQPE--KLEKIDVS--E 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 548 VMNHISANYLPLVVRKQLGLYCFIEPdvPLTLHGDPMRLQQVISNLLSNAIK-FTDIGCIVLHVCRAGDYLSIRVRDTGV 626
Cdd:COG5806   276 ELEHVIDVLSPYANMNNVEIQTELEP--GLYIEGDRQKLQQCLINIIKNGIEaMPNGGTLTIDVSIDKNKVIISIKDTGV 353
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1736044238 627 GIPAKEVVRLFDPFFQVGTgvqrnfQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIPLY 691
Cdd:COG5806   354 GMTKEQLERLGEPYFSTKE------KGTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFTITLPLA 412
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
827-947 4.74e-27

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: 115.06  E-value: 4.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANA 906
Cdd:COG2204     5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGYG 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1736044238 907 LAEEKQRCLESGMDSCLSKPVTLDVLKQTLSVYAERVRKTR 947
Cdd:COG2204    85 DVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRR 125
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
475-690 1.50e-26

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 114.11  E-value: 1.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 475 ATVSHELRTPLYGIIGNLDLLQTKELPKGVDR-LVTAMNNSSSLLLKIISDILDFSKieseqlkiePREFSPREV-MNHI 552
Cdd:PRK10364  242 AGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHqLAQVMAKEADRLNRVVSELLELVK---------PTHLALQAVdLNDL 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 553 SANYLPLVVR----KQLGLYCFIEPDVPLtLHGDPMRLQQVISNLLSNAIKFTDI-GCIVLHVCRAGDYLSIRVRDTGVG 627
Cdd:PRK10364  313 INHSLQLVSQdansREIQLRFTANDTLPE-IQADPDRLTQVLLNLYLNAIQAIGQhGVISVTASESGAGVKISVTDSGKG 391
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1736044238 628 IPAKEVVRLFDPFFQVGTgvqrnfQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIPL 690
Cdd:PRK10364  392 IAADQLEAIFTPYFTTKA------EGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLPV 448
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
827-936 2.81e-26

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: 104.08  E-value: 2.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQL--GLTLPVVGVTA 904
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELpwLANTPAIALTG 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKPVTLDVLKQTL 936
Cdd:cd17580    81 YGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
827-927 3.37e-26

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: 103.35  E-value: 3.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT--LPVVGVTA 904
Cdd:cd17538     2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETrhIPVIMITA 81
                          90       100
                  ....*....|....*....|...
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKPV 927
Cdd:cd17538    82 LDDREDRIRGLEAGADDFLSKPI 104
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
828-926 7.78e-26

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: 102.10  E-value: 7.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 828 LVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANAL 907
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80
                          90
                  ....*....|....*....
gi 1736044238 908 AEEKQRCLESGMDSCLSKP 926
Cdd:cd17574    81 EEDKVLGLELGADDYITKP 99
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
826-937 1.59e-25

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


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 101.85  E-value: 1.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 826 MILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT--LPVVGVT 903
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATrdIPVIALT 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1736044238 904 ANALAEEKQRCLESGMDSCLSKPVTLDVLKQTLS 937
Cdd:cd17548    81 AYAMKGDREKILEAGCDGYISKPIDTREFLETVA 114
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
451-689 1.90e-25

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 111.66  E-value: 1.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 451 KMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLL--QTKELPKGVDRLVTAMNNSSSLLLKIISDILDF 528
Cdd:NF040691  252 QMADSLQRQIRQLEELSRLQQRFVSDVSHELRTPLTTIRMAADVIhdSRDDFDPATARSAELLHTELDRFESLLSDLLEI 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 529 SKIE--SEQLKIEPREFSP--REVMNHISanylPLVVRKQLGLYcFIEPDVPLTLHGDPMRLQQVISNLLSNAIKFTDIG 604
Cdd:NF040691  332 SRFDagAAELDVEPVDLRPlvRRVVDALR----QLAERAGVELR-VDAPGTPVVAEVDPRRVERVLRNLVVNAIEHGEGK 406
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 605 CIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQF 684
Cdd:NF040691  407 PVVVTVAQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQF 486

                  ....*
gi 1736044238 685 TIRIP 689
Cdd:NF040691  487 RLTLP 491
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
352-690 7.09e-25

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: 109.44  E-value: 7.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 352 LEEHEQFNRKIVASAPVGIC-------ILRTQDG----TNILSNELA----HNYLNMLTHEDRQRLTQIICGQQVNFVDV 416
Cdd:COG5805   152 LQEQEERLQTLIENSPDLICvidtdgrILFINESierlFGAPREELIgknlLELLHPCDKEEFKERIESITEVWQEFIIE 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 417 LTSTHTNLQISFVHSRY-------RNENVAICVLVDVSARVKMEESL---QEMAQAAEQAsqsksmflATVSHELRTPLY 486
Cdd:COG5805   232 REIITKDGRIRYFEAVIvplidtdGSVKGILVILRDITEKKEAEELMarsEKLSIAGQLA--------AGIAHEIRNPLT 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 487 GIIGNLDLLQ-TKELPKGVDRLvtaMNNSSSLLLKIISDILDFSKIESEQLKIEPREFSPREVMNHISANylPLVVRKQL 565
Cdd:COG5805   304 SIKGFLQLLQpGIEDKEEYFDI---MLSELDRIESIISEFLALAKPQAVNKEKENINELIQDVVTLLETE--AILHNIQI 378
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 566 GlycFIEPDVPLTLHGDPMRLQQVISNLLSNAIK-FTDIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVG 644
Cdd:COG5805   379 R---LELLDEDPFIYCDENQIKQVFINLIKNAIEaMPNGGTITIHTEEEDNSVIIRVIDEGIGIPEERLKKLGEPFFTTK 455
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1736044238 645 TgvqrnfQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIPL 690
Cdd:COG5805   456 E------KGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLPL 495
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
823-947 8.25e-24

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 98.12  E-value: 8.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 823 DDMMILVVDDHPINRRLLADQLGSL-GYQ-CKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVV 900
Cdd:COG4565     2 KMIRVLIVEDDPMVAELLRRYLERLpGFEvVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVI 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1736044238 901 GVTANALAEEKQRCLESGMDSCLSKPVTLDVLKQTLSVYAERVRKTR 947
Cdd:COG4565    82 VITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLR 128
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
827-926 2.22e-22

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: 92.53  E-value: 2.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSL-GYQ-CKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTA 904
Cdd:COG4753     2 VLIVDDEPLIREGLKRILEWEaGFEvVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILSG 81
                          90       100
                  ....*....|....*....|..
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKP 926
Cdd:COG4753    82 YSDFEYAQEAIKLGADDYLLKP 103
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
825-936 4.96e-22

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: 92.02  E-value: 4.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 825 MMILVVDDHPINRRLLADQLGSLGYQ-CKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIR---QLGlTLPVV 900
Cdd:cd19923     1 MKVLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRadgALS-HLPVL 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1736044238 901 GVTANALAEEKQRCLESGMDSCLSKPVTLDVLKQTL 936
Cdd:cd19923    80 MVTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKL 115
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
582-689 7.84e-22

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: 91.40  E-value: 7.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 582 DPMRLQQVISNLLSNAIKFTDIGCIVLHVCRAGD--YLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLA 659
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTPDGGRIRCILEKFRlnRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGLGLS 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1736044238 660 ICEKLVSMMDGDISVDTEPGMGSQFTIRIP 689
Cdd:cd16925    81 IVKEFVELHGGTVTVSDAPGGGALFQVELP 110
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
456-692 4.17e-21

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 97.61  E-value: 4.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 456 LQEMAQAAEqasqskSMFLA------------TVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIIS 523
Cdd:PRK11100  236 LRELAQALE------SMRVKlegkayveqyvqTLTHELKSPLAAIRGAAELLQEDPPPEDRARFTGNILTQSARLQQLID 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 524 DILDFSKIESEQlKIEPRE-FSPREVMNHISANYLPLVVRKQLGLYcfIEPDvPLTLHGDPMRLQQVISNLLSNAIKFT- 601
Cdd:PRK11100  310 RLLELARLEQRQ-ELEVLEpVALAALLEELVEAREAQAAAKGITLR--LRPD-DARVLGDPFLLRQALGNLLDNAIDFSp 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 602 DIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQV---GTGVqrnfQGTGLGLAICEKLVSMMDGDISVDTEP 678
Cdd:PRK11100  386 EGGTITLSAEVDGEQVALSVEDQGPGIPDYALPRIFERFYSLprpANGR----KSTGLGLAFVREVARLHGGEVTLRNRP 461
                         250
                  ....*....|....
gi 1736044238 679 GMGSQFTIRIPLYS 692
Cdd:PRK11100  462 EGGVLATLTLPRHF 475
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
582-689 4.97e-21

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: 89.06  E-value: 4.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 582 DPMRLQQVISNLLSNAIKFTDIGCIV-LHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAI 660
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTGGKLrIRAAQTPQEVRLDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGLGLAI 80
                          90       100
                  ....*....|....*....|....*....
gi 1736044238 661 CEKLVSMMDGDISVDTEPGMGSQFTIRIP 689
Cdd:cd16946    81 CHNIALAHGGTISAEHSPLGGLRLVLTLP 109
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
583-690 6.34e-21

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


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 88.63  E-value: 6.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 583 PMRLQQVISNLLSNAIKFTD-IGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFF---QVGtgvqrnfQGTGLGL 658
Cdd:cd16943     1 PSQLNQVLLNLLVNAAQAMEgRGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPFFttkPVG-------EGTGLGL 73
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1736044238 659 AICEKLVSMMDGDISVDTEPGMGSQFTIRIPL 690
Cdd:cd16943    74 SLSYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
295-690 7.28e-21

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 96.07  E-value: 7.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 295 SSLSIVYSLPVDMVLERIRILIMNAILLNLLVGGALFTLARMYERRIFIPAESDAQRLEEHEQFnrkIVASAPVGIcILR 374
Cdd:COG3290    25 LLIILLLILLLVLLLLLFLLFVIILLLLLLILLLILLLLLLLLLAALLLKLLEEIARLVEEREA---VLESIREGV-IAV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 375 TQDGTNILSNELAHNYLNmlthedrqrLTQIICGQQVNFVDVLTSTHTNLQISFVHSRYRNENVAICVLVDVSARVKMEE 454
Cdd:COG3290   101 DRDGRITLINDAARRLLG---------LDAIGRPIDEVLAEVLETGERDEEILLNGRVLVVNRVPIRDDGRVVGAVATFR 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 455 SLQEMAQAAEQASQSKSMF--LATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNN-SSSLLLKIISDILD---F 528
Cdd:COG3290   172 DRTELERLEEELEGVKELAeaLRAQRHDFRNHLHTISGLLQLGEYDEALEYIDEISEELQElIDSLLSRIGNPVLAallL 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 529 SKI-ESEQLKIEprefsprevmnhisanylplvvrkqlgLYCFIEPDVPlTLHGDPMRLQQVISNLLSNAI-----KFTD 602
Cdd:COG3290   252 GKAaRARERGID---------------------------LTIDIDSDLP-DLPLSDTDLVTILGNLLDNAIeavekLPEE 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 603 IGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGvqrnfQGTGLGLAICEKLVSMMDGDISVDTEPGMGS 682
Cdd:COG3290   304 ERRVELSIRDDGDELVIEVEDSGPGIPEELLEKIFERGFSTKLG-----EGRGLGLALVKQIVEKYGGTIEVESEEGEGT 378

                  ....*...
gi 1736044238 683 QFTIRIPL 690
Cdd:COG3290   379 VFTVRLPK 386
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
827-926 8.64e-21

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: 88.20  E-value: 8.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSK---------NHIDIVLSDVNMPNMDGYRLTQRIRQ--LGL 895
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENlakegndlsKELDLIITDIEMPKMDGYELTFELRDdpRLA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1736044238 896 TLPVVGVTANALAEEKQRCLESGMDSCLSKP 926
Cdd:cd19924    81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
825-927 8.87e-21

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: 88.65  E-value: 8.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 825 MMILVVDDHPINRRLLADQLGSLGY-QCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQL--GLTLPVVG 901
Cdd:cd17551     1 MRILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALpgLEDVPIVM 80
                          90       100
                  ....*....|....*....|....*.
gi 1736044238 902 VTANALAEEKQRCLESGMDSCLSKPV 927
Cdd:cd17551    81 ITADTDREVRLRALEAGATDFLTKPF 106
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
445-692 1.28e-20

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 96.24  E-value: 1.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 445 DVSARV---------KMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQtkelpKGVDRLVTAMNNS- 514
Cdd:PRK10549  206 DFTTRVtptsrdelgRLAQDFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRGELEAIQ-----DGVRKFTPESVASl 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 515 ---SSLLLKIISDI--LDFSKIESEQLKIEPREFSPreVMNHISANYLPLVVRKQLGLYCFIEPDVPltLHGDPMRLQQV 589
Cdd:PRK10549  281 qaeVGTLTKLVDDLhqLSLSDEGALAYRKTPVDLVP--LLEVAGGAFRERFASRGLTLQLSLPDSAT--VFGDPDRLMQL 356
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 590 ISNLLSNAIKFTDIGCiVLHV--CRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLVSM 667
Cdd:PRK10549  357 FNNLLENSLRYTDSGG-SLHIsaEQRDKTLRLTFADSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEA 435
                         250       260
                  ....*....|....*....|....*
gi 1736044238 668 MDGDISVDTEPGMGSQFTIRIPLYS 692
Cdd:PRK10549  436 HNGRIIAAHSPFGGVSITVELPLER 460
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
827-918 2.84e-20

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: 86.41  E-value: 2.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT--LPVVGVTA 904
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATrhIPVIFLTA 80
                          90
                  ....*....|....
gi 1736044238 905 NALAEEKQRCLESG 918
Cdd:cd19920    81 LTDTEDKVKGFELG 94
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
827-933 4.40e-20

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: 86.53  E-value: 4.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKN--HIDIVLSDVNMPNMDGYRLTQRIRqLGLTLPVVGVTA 904
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENkdEFDLVITDVHMPDMDGFEFLELIR-LEMDLPVIMMSA 79
                          90       100
                  ....*....|....*....|....*....
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKPVTLDVLK 933
Cdd:cd17584    80 DGSTSTVMKGLAHGACDYLLKPVSIEDLK 108
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
825-939 4.74e-20

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 86.39  E-value: 4.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 825 MM--ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGV 902
Cdd:COG5803     1 MMkkILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPDIPVIMM 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1736044238 903 TANALAEEKQRCLESGMDSCLSKPVTLDVLKQTLSVY 939
Cdd:COG5803    81 TAYGELDMVEEAKELGAKGYFTKPFDIDELREAVNKL 117
envZ PRK09467
osmolarity sensor protein; Provisional
459-690 8.80e-20

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 93.05  E-value: 8.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 459 MAQAAEQASQSKSMFLATVSHELRTPLYGIignldllqtkelpkgvdRLVTAMNNSSSLLLK--IISDILDFSKIESEQL 536
Cdd:PRK09467  218 MAAGIKQLEDDRTLLMAGVSHDLRTPLTRI-----------------RLATEMMSEEDGYLAesINKDIEECNAIIEQFI 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 537 K-IEPREFSPREV--MNHISANylplVVRKQLGLYCFIE---PDVPLTLHGDPMRLQQVISNLLSNAIKFTDiGCIVLHV 610
Cdd:PRK09467  281 DyLRTGQEMPMEMadLNALLGE----VIAAESGYEREIEtalQPGPIEVPMNPIAIKRALANLVVNAARYGN-GWIKVSS 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 611 CRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGvqRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIPL 690
Cdd:PRK09467  356 GTEGKRAWFQVEDDGPGIPPEQLKHLFQPFTRGDSA--RGSSGTGLGLAIVKRIVDQHNGKVELGNSEEGGLSARAWLPL 433
PRK10610 PRK10610
chemotaxis protein CheY;
821-943 1.03e-19

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 85.80  E-value: 1.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 821 VNDDMMILVVDDHPINRRLLADQLGSLGYQ-CKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLG--LTL 897
Cdd:PRK10610    2 ADKELKFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGamSAL 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1736044238 898 PVVGVTANALAEEKQRCLESGMDSCLSKPVTLDVLKQTLSVYAERV 943
Cdd:PRK10610   82 PVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKL 127
pleD PRK09581
response regulator PleD; Reviewed
827-927 1.89e-19

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 92.27  E-value: 1.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT--LPVVGVTA 904
Cdd:PRK09581    5 ILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATthIPVVMVTA 84
                          90       100
                  ....*....|....*....|...
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKPV 927
Cdd:PRK09581   85 LDDPEDRVRGLEAGADDFLTKPI 107
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
570-700 3.32e-19

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 93.20  E-value: 3.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 570 FIEPDVPLTLHGDPMRLQQVISNLLSNAIK-FTDIGCIVLHVCR---------------AGDYLSIRVRDTGVGIPAKEV 633
Cdd:PRK13837  545 FDQDQEPAVVEGNPAELQQVLMNLCSNAAQaMDGAGRVDISLSRaklrapkvlshgvlpPGRYVLLRVSDTGAGIDEAVL 624
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1736044238 634 VRLFDPFFQVGTGvqrnfqGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIPLYSAQYPAKAT 700
Cdd:PRK13837  625 PHIFEPFFTTRAG------GTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLPPSSKVPVAPQA 685
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
455-689 4.98e-19

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 91.37  E-value: 4.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 455 SLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLD--LLQTKElPKGVDRLVTAMNNSSSLLLKIISDILDFSKIE 532
Cdd:PRK09835  247 SFNHMIERIEDVFTRQSNFSADIAHEIRTPITNLITQTEiaLSQSRS-QKELEDVLYSNLEELTRMAKMVSDMLFLAQAD 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 533 SEQLKIEPREFSPREVMNHISANYLPLVVRKQL-----GLYCFIEpdvpltlhGDPMRLQQVISNLLSNAIKFTDIG-CI 606
Cdd:PRK09835  326 NNQLIPEKKMLDLADEVGKVFDFFEAWAEERGVelrfvGDPCQVA--------GDPLMLRRAISNLLSNALRYTPAGeAI 397
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 607 VLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLVSMMDGDISVDTEPgMGSQFTI 686
Cdd:PRK09835  398 TVRCQEVDHQVQLVVENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRFVI 476

                  ...
gi 1736044238 687 RIP 689
Cdd:PRK09835  477 SLP 479
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
825-937 6.50e-19

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: 83.36  E-value: 6.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 825 MMILVVDDHPINRRLLADQLGSlGYQCKT--ANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGV 902
Cdd:cd17593     1 MKVLICDDSSMARKQLARALPA-DWDVEItfAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVV 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1736044238 903 TANALAEEKQRCLESGMDSCLSKPVTLDVLKQTLS 937
Cdd:cd17593    80 SGDVQPEAKERVLELGALAFLKKPFDPEKLAQLLE 114
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
827-926 1.51e-18

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: 81.66  E-value: 1.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGL--TLPVVGVTA 904
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADfdTIPVIFLTA 80
                          90       100
                  ....*....|....*....|..
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKP 926
Cdd:cd19927    81 KGMTSDRIKGYNAGCDGYLSKP 102
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-690 1.73e-18

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: 81.60  E-value: 1.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 586 LQQVISNLLSNAIKFTDiGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLV 665
Cdd:cd16949     1 LARALENVLRNALRYSP-SKILLDISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAIAERAI 79
                          90       100
                  ....*....|....*....|....*
gi 1736044238 666 SMMDGDISVDTEPGMGSQFTIRIPL 690
Cdd:cd16949    80 EQHGGKIKASNRKPGGLRVRIWLPA 104
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
827-936 2.98e-18

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: 81.40  E-value: 2.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINR----RLLADQLGS--LGyqckTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVV 900
Cdd:cd17535     1 VLIVDDHPLVReglrRLLESEPDIevVG----EAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVI 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1736044238 901 GVTANALAEEKQRCLESGMDSCLSKPVTLDVLKQTL 936
Cdd:cd17535    77 VLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAI 112
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-689 5.33e-18

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: 80.06  E-value: 5.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 586 LQQVISNLLSNAIKFT--------DIGCIvlhvcRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTgvQRNFQGTGLG 657
Cdd:cd16921     1 LGQVLTNLLGNAIKFRrprrppriEVGAE-----DVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRLHS--REEYEGTGVG 73
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1736044238 658 LAICEKLVSMMDGDISVDTEPGMGSQFTIRIP 689
Cdd:cd16921    74 LAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
823-947 8.17e-18

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: 82.70  E-value: 8.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 823 DDMMILVVDDHPINRRLLADQLGSLGYQ-CKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLtLPVVG 901
Cdd:COG3707     2 RGLRVLVVDDEPLRRADLREGLREAGYEvVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP-APVIL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1736044238 902 VTANALAEEKQRCLESGMDSCLSKPVTLDVLKQTLSVYAERVRKTR 947
Cdd:COG3707    81 LTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARFRELR 126
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
445-690 8.21e-18

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


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 86.20  E-value: 8.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 445 DVSARV-----------KMEESLQEMAQAAEQASQSKSMFLATVSHELRTP-------LYGIIGNL---DLLQTKELPKG 503
Cdd:NF012226  102 DLSARAedsqihsaeisELMHNFNDMAQKLESSVKNAQVWNAAIAHELRTPitilqgrLQGILDGVfepDPALFKSLLNQ 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 504 VDRLvtamnnssSLLlkiISDILDFSKIESEQLKIEPREFSPREVMNHISANYLPLVVRKQLglycFIEPDVPLTL-HGD 582
Cdd:NF012226  182 VEGL--------SHL---VEDLRTLSLVENQQLRLNYESVDLKDSIEKVLKMFEDRLEQAQL----TIVLNLTATPvFCD 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 583 PMRLQQVISNLLSNAIKFTDIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICE 662
Cdd:NF012226  247 RRRIEQVLIALIDNAIRYANAGKLKISSSVIQDDWILQIEDEGPGIAEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVH 326
                         250       260
                  ....*....|....*....|....*...
gi 1736044238 663 KLVSMMDGDISVdTEPGMGSQFTIRIPL 690
Cdd:NF012226  327 AIVIAHKGSIEY-SNSQGNSVFTIKLPA 353
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
827-932 1.06e-17

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


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 79.73  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANA 906
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80
                          90       100
                  ....*....|....*....|....*.
gi 1736044238 907 LAEEKQRCLESGMDSCLSKPVTLDVL 932
Cdd:cd17627    81 SVSDRVAGLDAGADDYLVKPFALEEL 106
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
573-688 3.13e-17

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: 78.71  E-value: 3.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 573 PDVPLTLHGDPMRLQQVISNLLSNAIKFTDIGCIVLHVCRAGD-YLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNF 651
Cdd:cd16947     8 PDRPIYANANTEALQRILKNLISNAIKYGSDGKFLGMTLREDEkHVYIDIWDKGKGISETEKDHVFERLYTLEDSRNSAK 87
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1736044238 652 QGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRI 688
Cdd:cd16947    88 QGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
827-926 3.57e-17

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 78.09  E-value: 3.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANA 906
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80
                          90       100
                  ....*....|....*....|
gi 1736044238 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:cd19934    81 SWQDKVEGLDAGADDYLTKP 100
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
469-534 4.78e-17

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 76.10  E-value: 4.78e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1736044238 469 SKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESE 534
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
PRK10604 PRK10604
sensor protein RstB; Provisional
459-693 5.86e-17

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 84.65  E-value: 5.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 459 MAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQ--TKELPKGVDRLVTAMNnssslllKIISDILDFSKIESEQL 536
Cdd:PRK10604  201 MADNINALIASKKQLIDGIAHELRTPLVRLRYRLEMSDnlSAAESQALNRDIGQLE-------ALIEELLTYARLDRPQN 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 537 KIEPREFSprevmnhisanyLPLVVRKQLGLYCFIEPDVPLTL----HGDP----MRL-QQVISNLLSNAIKFTDiGCIV 607
Cdd:PRK10604  274 ELHLSEPD------------LPAWLSTHLADIQAVTPEKTVRLdtphQGDYgaldMRLmERVLDNLLNNALRYAH-SRVR 340
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 608 LHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIR 687
Cdd:PRK10604  341 VSLLLDGNQACLIVEDDGPGIPPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSFS 420

                  ....*.
gi 1736044238 688 IPLYSA 693
Cdd:PRK10604  421 WPVWHN 426
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
827-926 6.90e-17

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: 77.37  E-value: 6.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIR-QLGL-TLPVVGVTA 904
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKsDPDLkDIPVILLTT 80
                          90       100
                  ....*....|....*....|..
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKP 926
Cdd:cd17598    81 LSDPRDVIRGLECGADNFITKP 102
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
827-932 7.02e-17

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: 77.34  E-value: 7.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGL--TLPVVGVTA 904
Cdd:cd17562     3 ILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAykFTPILMLTT 82
                          90       100
                  ....*....|....*....|....*...
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKPVTLDVL 932
Cdd:cd17562    83 ESSDEKKQEGKAAGATGWLVKPFDPEQL 110
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-689 9.67e-17

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: 76.67  E-value: 9.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 586 LQQVISNLLSNAIK-FTDIGC----IVLHVCRAGD-YLSIRVRDTGVGIPAKEVVRLFDPFFQVGTgvqrnfQGTGLGLA 659
Cdd:cd16920     1 IQQVLINLVRNGIEaMSEGGCerreLTIRTSPADDrAVTISVKDTGPGIAEEVAGQLFDPFYTTKS------EGLGMGLS 74
                          90       100       110
                  ....*....|....*....|....*....|
gi 1736044238 660 ICEKLVSMMDGDISVDTEPGMGSQFTIRIP 689
Cdd:cd16920    75 ICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-689 1.12e-16

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: 76.47  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 586 LQQVISNLLSNAIKFTdigcivlhvcRAGDYLSIR-----------VRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGT 654
Cdd:cd16952     1 LRSAFSNLVSNAVKYT----------PPSDTITVRwsqeesgarlsVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGT 70
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1736044238 655 GLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIP 689
Cdd:cd16952    71 GLGLAIVKHVMSRHDARLLIASELGKGSRFTCLFP 105
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
469-534 2.19e-16

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 74.14  E-value: 2.19e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1736044238  469 SKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESE 534
Cdd:smart00388   1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
827-904 2.75e-16

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: 75.72  E-value: 2.75e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTA 904
Cdd:cd17554     3 ILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTA 80
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
827-926 3.66e-16

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


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 74.78  E-value: 3.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANA 906
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTARD 80
                          90       100
                  ....*....|....*....|
gi 1736044238 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:cd19935    81 SVEDRVKGLDLGADDYLVKP 100
PRK10490 PRK10490
sensor protein KdpD; Provisional
454-690 4.47e-16

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 83.16  E-value: 4.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 454 ESLQeMAQAAEQA------SQSKSMFLATVSHELRTPLYGIIGN-----LDL--------LQTKELPKGV---DRLVtam 511
Cdd:PRK10490  643 ERLT-LTASEEQArlaserEQLRNALLAALSHDLRTPLTVLFGQaeiltLDLasegsphaRQASEIRQQVlntTRLV--- 718
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 512 NNssslllkiisdILDFSKIESEQLKIEPREFSPREVMNHISANYLPLVVRKQLGLYcfIEPDVPLtLHGDPMRLQQVIS 591
Cdd:PRK10490  719 NN-----------LLDMARIQSGGFNLRKEWLTLEEVVGSALQMLEPGLSGHPINLS--LPEPLTL-IHVDGPLFERVLI 784
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 592 NLLSNAIKFTD----IGcIVLHVcrAGDYLSIRVRDTGVGIPAKEVVRLFDPFfqvGTGVQRN-FQGTGLGLAICEKLVS 666
Cdd:PRK10490  785 NLLENAVKYAGaqaeIG-IDAHV--EGERLQLDVWDNGPGIPPGQEQLIFDKF---ARGNKESaIPGVGLGLAICRAIVE 858
                         250       260
                  ....*....|....*....|....
gi 1736044238 667 MMDGDISVDTEPGMGSQFTIRIPL 690
Cdd:PRK10490  859 VHGGTIWAENRPEGGACFRVTLPL 882
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
589-689 4.64e-16

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: 74.63  E-value: 4.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 589 VISNLLSNAIKFTDIGC-IVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFqvgTG-VQRNFQ-GTGLGLAICEKLV 665
Cdd:cd16948     9 IIGQIVSNALKYSKQGGkIEIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKGF---TGeNGRNFQeSTGMGLYLVKKLC 85
                          90       100
                  ....*....|....*....|....
gi 1736044238 666 SMMDGDISVDTEPGMGSQFTIRIP 689
Cdd:cd16948    86 DKLGHKIDVESEVGEGTTFTITFP 109
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-686 4.72e-16

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: 74.42  E-value: 4.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 586 LQQVISNLLSNAI----KFTDiGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFF---QVGtgvqrnfQGTGLGL 658
Cdd:cd16976     1 IQQVLMNLLQNALdamgKVEN-PRIRIAARRLGGRLVLVVRDNGPGIAEEHLSRVFDPFFttkPVG-------KGTGLGL 72
                          90       100
                  ....*....|....*....|....*...
gi 1736044238 659 AICEKLVSMMDGDISVDTEPGMGSQFTI 686
Cdd:cd16976    73 SISYGIVEEHGGRLSVANEEGAGARFTF 100
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
473-689 4.83e-16

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 81.60  E-value: 4.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 473 FLATVSHELRTPLYGIIGNLDLLQTKELPKGV-DRLVTAMNNSSSLLLKIISDILDFSKIESeqlkieprefSPREVMNH 551
Cdd:PRK11006  207 FFANVSHELRTPLTVLQGYLEMMQDQPLEGALrEKALHTMREQTQRMEGLVKQLLTLSKIEA----------APTIDLNE 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 552 ISAnyLPL---VVRKQL-----GLYCFI-EPDVPLTLHGDPMRLQQVISNLLSNAIKFTDIGC-IVLHVCRAGDYLSIRV 621
Cdd:PRK11006  277 KVD--VPMmlrVLEREAqtlsqGKHTITfEVDNSLKVFGNEDQLRSAISNLVYNAVNHTPEGThITVRWQRVPQGAEFSV 354
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1736044238 622 RDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIP 689
Cdd:PRK11006  355 EDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLP 422
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
827-926 7.84e-16

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: 73.74  E-value: 7.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLgLTLPVVGVTANA 906
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREW-SAVPVIVLSARD 79
                          90       100
                  ....*....|....*....|
gi 1736044238 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:cd17620    80 EESDKIAALDAGADDYLTKP 99
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
827-936 7.96e-16

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: 74.36  E-value: 7.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNH--IDIVLSDVNMPNMDGYRLTQRIRQLGLT---LPVVG 901
Cdd:cd19933     3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEhsFQLVLLDLCMPEMDGFEVALRIRKLFGRrerPLIVA 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1736044238 902 VTANALAEEKQRCLESGMDSCLSKPVTLDVLKQTL 936
Cdd:cd19933    83 LTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
455-693 9.73e-16

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 80.75  E-value: 9.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 455 SLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKElpkGVDRLVTAMNNSSSLLLKIISDILDFSKIese 534
Cdd:PRK09470  228 SFNQMVTALERMMTSQQRLLSDISHELRTPLTRLQLATALLRRRQ---GESKELERIETEAQRLDSMINDLLVLSRN--- 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 535 QLKieprefsprevmNHISANYLPL------VVR------KQLGLYCFIEPDV-PLTLHGDPMRLQQVISNLLSNAIKFT 601
Cdd:PRK09470  302 QQK------------NHLERETFKAnslwseVLEdakfeaEQMGKSLTVSAPPgPWPINGNPNALASALENIVRNALRYS 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 602 DiGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMG 681
Cdd:PRK09470  370 H-TKIEVAFSVDKDGLTITVDDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAIVENAIQQHRGWVKAEDSPLGG 448
                         250
                  ....*....|..
gi 1736044238 682 SQFTIRIPLYSA 693
Cdd:PRK09470  449 LRLTIWLPLYKR 460
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
827-926 1.24e-15

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: 74.09  E-value: 1.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLsKNHIDI--VLSDVNMPNMDGYRLTQRIRQL--GLTLPVVGV 902
Cdd:cd17544     3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVL-EQHPDIklVITDYNMPEMDGFELVREIRKKysRDQLAIIGI 81
                          90       100
                  ....*....|....*....|....
gi 1736044238 903 TANALAEEKQRCLESGMDSCLSKP 926
Cdd:cd17544    82 SASGDNALSARFIKAGANDFLTKP 105
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
827-936 1.50e-15

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: 73.53  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQL--GSLGYQ-CKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVT 903
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIdwEELGFEvVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILS 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1736044238 904 ANALAEEKQRCLESGMDSCLSKPVTLDVLKQTL 936
Cdd:cd17536    81 GYDDFEYAQKAIRLGVVDYLLKPVDEEELEEAL 113
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
827-936 1.78e-15

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: 73.21  E-value: 1.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQ-CKTANDGVDALNVLSKNHIDIVLSDVNMP-NMDGYRLTQRIRQLgLTLPVVGVTA 904
Cdd:cd17534     3 ILIVEDEAIIALDLKEILESLGYEvVGIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREK-FDIPVIFLTA 81
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKPVTLDVLKQTL 936
Cdd:cd17534    82 YSDEETLERAKETNPYGYLVKPFNERELKAAI 113
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
827-932 2.87e-15

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: 72.77  E-value: 2.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANA 906
Cdd:cd17615     2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAKD 81
                          90       100
                  ....*....|....*....|....*.
gi 1736044238 907 LAEEKQRCLESGMDSCLSKPVTLDVL 932
Cdd:cd17615    82 SVEDRIAGLTAGGDDYVTKPFSLEEV 107
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
827-893 3.91e-15

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


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 72.44  E-value: 3.91e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQL 893
Cdd:cd17569     3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRER 69
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
825-879 4.29e-15

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 70.29  E-value: 4.29e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1736044238  825 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMP 879
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
825-945 5.89e-15

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 75.24  E-value: 5.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 825 MM-ILVVDDHPINRRLLADQLGSL-GYQC-KTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVG 901
Cdd:COG3279     1 MMkILIVDDEPLARERLERLLEKYpDLEVvGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIF 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1736044238 902 VTA-----------NALAeekqrclesgmdsCLSKPVTLDVLKQTLsvyaERVRK 945
Cdd:COG3279    81 TTAydeyaleafevNAVD-------------YLLKPIDEERLAKAL----EKAKE 118
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
827-932 1.51e-14

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: 70.59  E-value: 1.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANA 906
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80
                          90       100
                  ....*....|....*....|....*.
gi 1736044238 907 LAEEKQRCLESGMDSCLSKPVTLDVL 932
Cdd:cd17624    81 GVDDRVAGLDAGADDYLVKPFALEEL 106
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
827-900 1.83e-14

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: 70.60  E-value: 1.83e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVV 900
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVI 74
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
827-932 4.68e-14

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


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 69.20  E-value: 4.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT--LPVVGVTA 904
Cdd:cd17618     3 ILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTrdIPIIMLTA 82
                          90       100
                  ....*....|....*....|....*...
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKPVTLDVL 932
Cdd:cd17618    83 RGEEEDKVRGLEAGADDYITKPFSPREL 110
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
827-904 5.84e-14

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: 69.44  E-value: 5.84e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTA 904
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITG 78
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
576-687 7.17e-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: 68.59  E-value: 7.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 576 PLTLHGDPMRLQQVISNLLSNAIKFTDIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTgvqRNFQGTG 655
Cdd:cd16940     4 DIQVQGDALLLFLLLRNLVDNAVRYSPQGSRVEIKLSADDGAVIRVEDNGPGIDEEELEALFERFYRSDG---QNYGGSG 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1736044238 656 LGLAICEKLVSMMDGDISVDTEPGMGSQFTIR 687
Cdd:cd16940    81 LGLSIVKRIVELHGGQIFLGNAQGGGLEAWVR 112
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
612-689 7.69e-14

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: 68.56  E-value: 7.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 612 RAGDYLSIRVRDTGVGIPAKEVVRLFDPFF---QVGtgvqrnfQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRI 688
Cdd:cd16919    43 IPGNYVCLEVSDTGSGMPAEVLRRAFEPFFttkEVG-------KGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYL 115

                  .
gi 1736044238 689 P 689
Cdd:cd16919   116 P 116
orf27 CHL00148
Ycf27; Reviewed
822-926 8.37e-14

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 72.06  E-value: 8.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 822 NDDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVVG 901
Cdd:CHL00148    4 NSKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKES-DVPIIM 82
                          90       100
                  ....*....|....*....|....*
gi 1736044238 902 VTANALAEEKQRCLESGMDSCLSKP 926
Cdd:CHL00148   83 LTALGDVSDRITGLELGADDYVVKP 107
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
827-927 1.12e-13

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 67.76  E-value: 1.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKN-HIDIVLSDVNMPN-MDGYRLTQRIRQLGLTLPVVGVTA 904
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGpDIDLLVTDVIMPGgMNGSQLAEEARRRRPDLKVLLTSG 80
                          90       100
                  ....*....|....*....|...
gi 1736044238 905 NALAEEKQRCLESGMDsCLSKPV 927
Cdd:cd18161    81 YAENAIEGGDLAPGVD-VLSKPF 102
PRK15115 PRK15115
response regulator GlrR; Provisional
827-932 1.31e-13

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 74.10  E-value: 1.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANA 906
Cdd:PRK15115    8 LLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTAHG 87
                          90       100
                  ....*....|....*....|....*.
gi 1736044238 907 LAEEKQRCLESGMDSCLSKPVTLDVL 932
Cdd:PRK15115   88 SIPDAVAATQQGVFSFLTKPVDRDAL 113
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
827-936 1.41e-13

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


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 68.21  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCK--TANDGVDALNVLSKN-------HIDIVLSDVNMPNMDGYRLTQRIRQLGLT- 896
Cdd:cd17557     2 ILLVEDNPGDAELIQEAFKEAGVPNElhVVRDGEEALDFLRGEgeyadapRPDLILLDLNMPRMDGFEVLREIKADPDLr 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1736044238 897 -LPVVGVTANALAEEKQRCLESGMDSCLSKPVTLDVLKQTL 936
Cdd:cd17557    82 rIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAI 122
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
467-530 2.06e-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: 2.06e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1736044238 467 SQSKSMFLATVSHELRTPLYGIIGNLDLLQ-TKELPKGVDRLVTAMNNSSSLLLKIISDILDFSK 530
Cdd:cd00082     1 LQAKGEFLANVSHELRTPLTAIRGALELLEeELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
582-679 2.27e-13

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: 67.10  E-value: 2.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 582 DPMRLQQVISNLLSNAIKFT-DIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGvQRNFQGTGLGLAI 660
Cdd:cd16945     1 DPFLLRQAINNLLDNAIDFSpEGGLIALQLEADTEGIELLVFDEGSGIPDYALNRVFERFYSLPRP-HSGQKSTGLGLAF 79
                          90
                  ....*....|....*....
gi 1736044238 661 CEKLVSMMDGDISVDTEPG 679
Cdd:cd16945    80 VQEVAQLHGGRITLRNRPD 98
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
827-936 3.32e-13

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: 66.84  E-value: 3.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANA 906
Cdd:cd17555     3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSGAG 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1736044238 907 LAEEKQRCLESGMDSCLSKPVT-LDVLKQTL 936
Cdd:cd17555    83 VMSDAVEALRLGAWDYLTKPIEdLAVLEHAV 113
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
827-926 5.10e-13

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 66.65  E-value: 5.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGS------LGyqckTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTlPVV 900
Cdd:cd17541     3 VLIVDDSAVMRKLLSRILESdpdievVG----TARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERPT-PVV 77
                          90       100
                  ....*....|....*....|....*...
gi 1736044238 901 GVTA--NALAEEKQRCLESGMDSCLSKP 926
Cdd:cd17541    78 MVSSltEEGAEITLEALELGAVDFIAKP 105
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-689 5.14e-13

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


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 65.93  E-value: 5.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 586 LQQVISNLLSNAIKFTDiGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGvqRNFQGTGLGLAICEKLV 665
Cdd:cd16950     1 LKRVLSNLVDNALRYGG-GWVEVSSDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNA--RGTSGTGLGLAIVQRIS 77
                          90       100
                  ....*....|....*....|....
gi 1736044238 666 SMMDGDISVDTEPGMGSQFTIRIP 689
Cdd:cd16950    78 DAHGGSLTLANRAGGGLCARIELP 101
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-690 6.16e-13

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


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 65.91  E-value: 6.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 586 LQQVISNLLSNAIKFTDiGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLV 665
Cdd:cd16939     1 MARALDNLLRNALRYAH-RTVRIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAIVHRVA 79
                          90       100
                  ....*....|....*....|....*
gi 1736044238 666 SMMDGDISVDTEPGMGSQFTIRIPL 690
Cdd:cd16939    80 LWHGGHVECDDSELGGACFRLTWPR 104
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
827-933 8.40e-13

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 71.80  E-value: 8.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANA 906
Cdd:PRK11361    7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAYA 86
                          90       100
                  ....*....|....*....|....*..
gi 1736044238 907 LAEEKQRCLESGMDSCLSKPVTLDVLK 933
Cdd:PRK11361   87 EVETAVEALRCGAFDYVIKPFDLDELN 113
PRK15479 PRK15479
transcriptional regulator TctD;
825-936 1.04e-12

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 68.59  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 825 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTA 904
Cdd:PRK15479    1 MRLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTA 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKPVTLDVLKQTL 936
Cdd:PRK15479   81 RSAVADRVKGLNVGADDYLPKPFELEELDARL 112
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
827-926 1.88e-12

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 64.72  E-value: 1.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVVGVTANA 906
Cdd:cd17619     3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQS-EVGIILVTGRD 81
                          90       100
                  ....*....|....*....|
gi 1736044238 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:cd17619    82 DEVDRIVGLEIGADDYVTKP 101
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
828-926 2.38e-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: 64.60  E-value: 2.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 828 LVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT--LPVVGVTAN 905
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTssIPIIMLTAK 80
                          90       100
                  ....*....|....*....|.
gi 1736044238 906 ALAEEKQRCLESGMDSCLSKP 926
Cdd:cd19937    81 GEEFDKVLGLELGADDYITKP 101
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
821-936 2.50e-12

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 70.06  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 821 VNDDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVV 900
Cdd:PRK10365    2 THDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVL 81
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1736044238 901 GVTANALAEEKQRCLESGMDSCLSKPVTLDVLKQTL 936
Cdd:PRK10365   82 IMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATL 117
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-689 4.81e-12

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: 63.36  E-value: 4.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 586 LQQVISNLLSNAIKFT--DIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEK 663
Cdd:cd16953     1 LGQVLRNLIGNAISFSppDTGRITVSAMPTGKMVTISVEDEGPGIPQEKLESIFDRFYTERPANEAFGQHSGLGLSISRQ 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1736044238 664 LVSmMDGDISVD---TEPGM--GSQFTIRIP 689
Cdd:cd16953    81 IIE-AHGGISVAenhNQPGQviGARFTVQLP 110
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
581-690 6.06e-12

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: 63.06  E-value: 6.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 581 GDPMRLQQVISNLLSNAIKFTDI--GCIVLHVC----RAGD-----YLSIRVRDTGVGIPAKEVVRLFDPffqvGTGVQR 649
Cdd:cd16932     2 GDQIRLQQVLADFLLNAVRFTPSpgGWVEIKVSptkkQIGDgvhviHLEFRITHPGQGLPEELVQEMFEE----NQWTTQ 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1736044238 650 NfqgtGLGLAICEKLVSMMDGDISVDTEPGMgSQFTIRIPL 690
Cdd:cd16932    78 E----GLGLSISRKLVKLMNGDVRYLREAGR-SYFLITLEL 113
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
827-940 9.22e-12

phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 62.65  E-value: 9.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGY--QCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTA 904
Cdd:cd19925     3 VLIVEDDPMVAEIHRAYVEQVPGftVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVVTA 82
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKPVTLDVLKQTLSVYA 940
Cdd:cd19925    83 ANDVETVREALRLGVVDYLIKPFTFERLRQRLERYR 118
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
826-906 1.25e-11

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: 64.74  E-value: 1.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 826 MILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTAN 905
Cdd:COG4566     1 TVYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGH 80

                  .
gi 1736044238 906 A 906
Cdd:COG4566    81 G 81
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
473-689 1.26e-11

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


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 68.62  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 473 FLATVSHELRTPLYGIIGNLDLLQTKELPK-----------GVDRLVTAMNNSSslllkiisdilDFSKIESEQLKIEPR 541
Cdd:TIGR03785 488 MSSRLSHELRTPVAVVRSSLENLELQALEQekqkylerareGTERLSMILNNMS-----------EATRLEQAIQSAEVE 556
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 542 EFSPREVMNHISANYLPLVVRKQLGLYCfiePDVPLTLHGDPMRLQQVISNLLSNAIKFT-DIGCIVLHVCRAGDYLSIR 620
Cdd:TIGR03785 557 DFDLSEVLSGCMQGYQMTYPPQRFELNI---PETPLVMRGSPELIAQMLDKLVDNAREFSpEDGLIEVGLSQNKSHALLT 633
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1736044238 621 VRDTGVGIPAKEVVRLFDPFFQVgtgvqRNFQGT-----GLGLAICEKLVSMMDGDISVDTEP-GMGSQFTIRIP 689
Cdd:TIGR03785 634 VSNEGPPLPEDMGEQLFDSMVSV-----RDQGAQdqphlGLGLYIVRLIADFHQGRIQAENRQqNDGVVFRISLP 703
PRK10816 PRK10816
two-component system response regulator PhoP;
825-930 1.35e-11

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 65.15  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 825 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTA 904
Cdd:PRK10816    1 MRVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTA 80
                          90       100
                  ....*....|....*....|....*.
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKPVTLD 930
Cdd:PRK10816   81 RESWQDKVEVLSAGADDYVTKPFHIE 106
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
827-926 1.59e-11

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: 61.79  E-value: 1.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANA 906
Cdd:cd19926     1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80
                          90       100
                  ....*....|....*....|
gi 1736044238 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:cd19926    81 SLDTAIEALKAGAFDFLTKP 100
PRK10643 PRK10643
two-component system response regulator PmrA;
825-933 1.73e-11

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 64.67  E-value: 1.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 825 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTA 904
Cdd:PRK10643    1 MKILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTA 80
                          90       100
                  ....*....|....*....|....*....
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKPVTLDVLK 933
Cdd:PRK10643   81 RDTLEDRVAGLDVGADDYLVKPFALEELH 109
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
827-939 1.79e-11

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 62.19  E-value: 1.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANA 906
Cdd:cd17553     3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAYG 82
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1736044238 907 LAEEKQRCLESGMDSCLSKPVTLDVLKQTLSVY 939
Cdd:cd17553    83 ELDMIQESKELGALTHFAKPFDIDEIRDAVKKY 115
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
827-936 2.35e-11

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: 61.83  E-value: 2.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANA 906
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1736044238 907 ---LAEEKQRcleSGMDSCLSKPVTLDVLKQTL 936
Cdd:cd17572    81 svdIAVEAMR---LGAYDFLEKPFDADRLRVTV 110
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
825-942 2.41e-11

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: 61.66  E-value: 2.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 825 MMILVVDDHPINRRLLADQLGSLGYQC-KTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTlPVVGVT 903
Cdd:cd19932     1 VRVLIAEDEALIRMDLREMLEEAGYEVvGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENIA-PIVLLT 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1736044238 904 ANALAEEKQRCLESGMDSCLSKPVTLDVLKQTLSVYAER 942
Cdd:cd19932    80 AYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAIAR 118
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
827-926 2.57e-11

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: 61.80  E-value: 2.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSL-GYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT--LPVVGVT 903
Cdd:cd17552     4 ILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETqsIPVILLT 83
                          90       100
                  ....*....|....*....|...
gi 1736044238 904 ANALAEEKQRCLESGMDSCLSKP 926
Cdd:cd17552    84 AKAQPSDRQRFASLGVAGVIAKP 106
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
472-670 3.03e-11

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 66.14  E-value: 3.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 472 MFLATVSHELRTPLYGIIGNLDLL------QTKELPKGVDRLvtaMNNSSSLL----------------LKIISDILDFS 529
Cdd:PRK10755  139 LFTADVAHELRTPLAGIRLHLELLekqhhiDVAPLIARLDQM---MHTVEQLLqlaragqsfssghyqtVKLLEDVILPS 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 530 KIESEQLkieprefsprevmnhisanylpLVVRKQLGLYcfIEPDVPLTLHGDPMRLQQVISNLLSNAIKFTDIG-CIVL 608
Cdd:PRK10755  216 QDELSEM----------------------LEQRQQTLLL--PESAADITVQGDATLLRLLLRNLVENAHRYSPEGsTITI 271
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1736044238 609 HVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGtgvQRnFQGTGLGLAICEKLVSMMDG 670
Cdd:PRK10755  272 KLSQEDGGAVLAVEDEGPGIDESKCGELSKAFVRMD---SR-YGGIGLGLSIVSRITQLHHG 329
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
827-933 5.70e-11

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: 60.84  E-value: 5.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVL-------SKNH----IDIVLSDVNMPNMDGYRLTQRIRQLG- 894
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLgledeedSSNFnepkVNMIITDYCMPGMTGYDLLKKVKESSa 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1736044238 895 -LTLPVVGVTANALAEEKQRCLESGMDSCLSKPVTL-DVLK 933
Cdd:cd17581    81 lKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLaDVKR 121
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
827-926 6.93e-11

phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is part of the CpxA/CpxR two-component regulatory system that mediates envelope stress responses that is key for virulence and antibiotic resistance in several Gram negative pathogens. CpxR is a transcription factor/response regulator that controls the expression of numerous genes, including those of the classical porins OmpF and OmpC. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 60.40  E-value: 6.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQlGLTLPVVGVTANa 906
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRK-TSQVPVLMLTAR- 78
                          90       100
                  ....*....|....*....|..
gi 1736044238 907 lAEEKQRC--LESGMDSCLSKP 926
Cdd:cd17623    79 -GDDIDRIlgLELGADDYLPKP 99
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
827-942 7.97e-11

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 65.66  E-value: 7.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANA 906
Cdd:PRK10923    6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1736044238 907 LAEEKQRCLESGMDSCLSKPVTLD----VLKQTLSVYAER 942
Cdd:PRK10923   86 DLDAAVSAYQQGAFDYLPKPFDIDeavaLVERAISHYQEQ 125
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
827-926 1.16e-10

phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 59.44  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVL-SKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTAN 905
Cdd:cd18160     2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLqQGKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISGG 81
                          90       100
                  ....*....|....*....|.
gi 1736044238 906 ALAEEKQRCLESGMDSCLSKP 926
Cdd:cd18160    82 AAAAPELLSDAVGDNATLKKP 102
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
446-674 1.19e-10

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 65.48  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 446 VSARVKMEESLQ----EMAQAAEQASQSKSMflATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLL-- 519
Cdd:COG4192   407 IEERKRIEKNLRqtqdELIQAAKMAVVGQTM--TSLAHELNQPLNAMSMYLFSAKKALEQENYAQLPTSLDKIEGLIErm 484
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 520 -KIISDILDFSKIESEQLKieprefsPREVMNHISANYLPLVVR---KQLGLYCFIEPDVPltlhGDPMRLQQVISNLLS 595
Cdd:COG4192   485 dKIIKSLRQFSRKSDTPLQ-------PVDLRQVIEQAWELVESRakpQQITLHIPDDLMVQ----GDQVLLEQVLVNLLV 553
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 596 NAIK-FTDIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEvvRLFDPFfqvgtgVQRNFQGTGLGLAICEKLVSMMDGDISV 674
Cdd:COG4192   554 NALDaVATQPQISVDLLSNAENLRVAISDNGNGWPLVD--KLFTPF------TTTKEVGLGLGLSICRSIMQQFGGDLYL 625
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
827-904 1.22e-10

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: 59.59  E-value: 1.22e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTA 904
Cdd:cd19919     3 VWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTA 80
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
828-932 1.29e-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: 59.54  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 828 LVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANAL 907
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80
                          90       100
                  ....*....|....*....|....*
gi 1736044238 908 AEEKQRCLESGMDSCLSKPVTLDVL 932
Cdd:cd17625    81 VEDRVKGLDLGADDYLPKPFSLAEL 105
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-689 1.37e-10

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


Pssm-ID: 340400 [Multi-domain]  Cd Length: 102  Bit Score: 58.94  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 586 LQQVISNLLSNAIKFTDIGCIV-LHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGvqRNFQGTGLGLAICEKL 664
Cdd:cd16923     1 LQRVFSNLLSNAIKYSPENTRIyITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNS--RNTEGAGLGLSIAKAI 78
                          90       100
                  ....*....|....*....|....*
gi 1736044238 665 VSMMDGDISVDTEpGMGSQFTIRIP 689
Cdd:cd16923    79 IELHGGSASAEYD-DNHDLFKVRLP 102
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
562-688 1.54e-10

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


Pssm-ID: 340430 [Multi-domain]  Cd Length: 135  Bit Score: 59.95  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 562 RKQLGLYCFIEPDvpLTLHGDPMRLQQVISNLLSNAIKFTDiGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFdpff 641
Cdd:cd16954    16 RKGVSISLDISPE--LRFPGERNDLMELLGNLLDNACKWCL-EFVEVTARQTDGGLHLIVDDDGPGVPESQRSKIF---- 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1736044238 642 QVGTGVQRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRI 688
Cdd:cd16954    89 QRGQRLDEQRPGQGLGLAIAKEIVEQYGGELSLSDSPLGGARFEVVF 135
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
823-937 2.14e-10

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: 60.70  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 823 DDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGV 902
Cdd:COG4567     3 EDRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVL 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1736044238 903 T-----ANALAEEKQrclesGMDSCLSKPVTLDVLKQTLS 937
Cdd:COG4567    83 TgyasiATAVEAIKL-----GADDYLAKPADADDLLAALE 117
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
825-890 2.23e-10

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 59.14  E-value: 2.23e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1736044238 825 MM-ILVVDDHPINRRLLADQLGSL-GYQ-CKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRI 890
Cdd:COG2197     1 MIrVLIVDDHPLVREGLRALLEAEpDIEvVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
827-926 2.71e-10

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: 58.23  E-value: 2.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVVGVTANA 906
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKS-TLPVIFLTSKD 79
                          90       100
                  ....*....|....*....|
gi 1736044238 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:cd19936    80 DEIDEVFGLRMGADDYITKP 99
ompR PRK09468
osmolarity response regulator; Provisional
827-926 5.76e-10

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 60.76  E-value: 5.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANa 906
Cdd:PRK09468    8 ILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPIIMLTAK- 86
                          90       100
                  ....*....|....*....|..
gi 1736044238 907 lAEEKQRC--LESGMDSCLSKP 926
Cdd:PRK09468   87 -GEEVDRIvgLEIGADDYLPKP 107
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-689 6.31e-10

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


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 57.41  E-value: 6.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 586 LQQVISNLLSNAIK-------------FTDIGCIVLHVcRAGDYLSIRVRDTGVGIPAKEVVRLFDPFfqvgtgVQRNFQ 652
Cdd:cd16918     1 LIQVFLNLVRNAAQalagsggeiilrtRTQRQVTLGHP-RHRLALRVSVIDNGPGIPPDLQDTIFYPM------VSGREN 73
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1736044238 653 GTGLGLAICEKLVSMMDGDISVDTEPGMgSQFTIRIP 689
Cdd:cd16918    74 GTGLGLAIAQNIVSQHGGVIECDSQPGH-TVFSVSLP 109
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
560-690 8.22e-10

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 62.23  E-value: 8.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 560 VVRKQLGLYC--FIEPDVPLTLHGDPMRLQQ--------VISNLLSNAIKF----TDIGCIVLHVCRAGDYLSIRVRDTG 625
Cdd:COG3920   364 YLRELLEPLRdsYGGRGIRIELDGPDVELPAdaavplglILNELVTNALKHaflsGEGGRIRVSWRREDGRLRLTVSDNG 443
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1736044238 626 VGIPAKEVVRlfdpffqvgtgvqrnfQGTGLGLAICEKLVSMMDGDISVDTEPGMgsQFTIRIPL 690
Cdd:COG3920   444 VGLPEDVDPP----------------ARKGLGLRLIRALVRQLGGTLELDRPEGT--RVRITFPL 490
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
575-686 1.02e-09

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: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 575 VPLTLHGDPMRLQQVISNLLSNAIKFTDIGCIVLHV--------------------CRAGDYLSIR--VRDTGVGIPAKE 632
Cdd:cd16938     1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGGGNITFRvfleggsedrsdrdwgpwrpSMSDESVEIRfeVEINDSGSPSIE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1736044238 633 VVRLFDpffQVGTGVQRNFQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTI 686
Cdd:cd16938    81 SASMRN---SLNRRYNLSELGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSL 131
PRK10766 PRK10766
two-component system response regulator TorR;
827-929 1.17e-09

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 59.28  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVVGVTANA 906
Cdd:PRK10766    5 ILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRS-TVGIILVTGRT 83
                          90       100
                  ....*....|....*....|...
gi 1736044238 907 LAEEKQRCLESGMDSCLSKPVTL 929
Cdd:PRK10766   84 DSIDRIVGLEMGADDYVTKPLEL 106
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
827-932 1.17e-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: 56.65  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANA 906
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80
                          90       100
                  ....*....|....*....|....*.
gi 1736044238 907 LAEEKQRCLESGMDSCLSKPVTLDVL 932
Cdd:cd17616    81 DIEDKVKGLGFGADDYMTKPFHKDEL 106
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
589-689 1.26e-09

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 61.85  E-value: 1.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 589 VISNLLSN---AIKFTDIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDpffqvgTGVQRNFQGTGLGLAICEKLV 665
Cdd:PRK11086  437 ILGNLIENaleAVGGEEGGEISVSLHYRNGWLHCEVSDDGPGIAPDEIDAIFD------KGYSTKGSNRGVGLYLVKQSV 510
                          90       100
                  ....*....|....*....|....
gi 1736044238 666 SMMDGDISVDTEPGMGSQFTIRIP 689
Cdd:PRK11086  511 ENLGGSIAVESEPGVGTQFFVQIP 534
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
827-936 1.48e-09

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


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 56.52  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQC-KTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTAN 905
Cdd:cd17542     3 VLIVDDAAFMRMMLKDILTKAGYEVvGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCSAM 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1736044238 906 ALAEEKQRCLESGMDSCLSKPV----TLDVLKQTL 936
Cdd:cd17542    83 GQEEMVKEAIKAGAKDFIVKPFqperVLEAVEKVL 117
PLN03029 PLN03029
type-a response regulator protein; Provisional
827-929 1.67e-09

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 58.89  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLS----------------KNH----IDIVLSDVNMPNMDGYRL 886
Cdd:PLN03029   11 VLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGlheddrsnpdtpsvspNSHqeveVNLIITDYCMPGMTGYDL 90
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1736044238 887 TQRIRQLG--LTLPVVGVTANALAEEKQRCLESGMDSCLSKPVTL 929
Cdd:PLN03029   91 LKKIKESSslRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQL 135
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
827-932 1.78e-09

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 56.06  E-value: 1.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANA 906
Cdd:cd17537     3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGHG 82
                          90       100
                  ....*....|....*....|....*.
gi 1736044238 907 LAEEKQRCLESGMDSCLSKPVTLDVL 932
Cdd:cd17537    83 DVPMAVEAMKAGAVDFLEKPFRDQVL 108
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
827-926 1.85e-09

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 56.23  E-value: 1.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVVGVTANa 906
Cdd:cd19938     2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFS-DVPIIMVTAR- 79
                          90       100
                  ....*....|....*....|..
gi 1736044238 907 lAEEKQRC--LESGMDSCLSKP 926
Cdd:cd19938    80 -VEEIDRLlgLELGADDYICKP 100
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
827-926 2.63e-09

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: 55.28  E-value: 2.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVVGVTANA 906
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARS-NVPVIMVTAKD 79
                          90       100
                  ....*....|....*....|
gi 1736044238 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:cd17621    80 SEIDKVVGLELGADDYVTKP 99
PRK13557 PRK13557
histidine kinase; Provisional
445-697 3.73e-09

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 60.45  E-value: 3.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 445 DVSARVKMEESLQEmAQAAEQASQsksmFLATVSHELRTPLYGIIGNLDLLQTK-ELPKG--------VDRLVTAMNNSS 515
Cdd:PRK13557  143 DVSRRRDAEDALRQ-AQKMEALGQ----LTGGIAHDFNNLLQVMSGYLDVIQAAlSHPDAdrgrmarsVENIRAAAERAA 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 516 SLllkiISDILDFSKIEseqlKIEPREFSprevMNHISANYLPLVvRKQLG----LYCFIEPDVPlTLHGDPMRLQQVIS 591
Cdd:PRK13557  218 TL----TQQLLAFARKQ----RLEGRVLN----LNGLVSGMGELA-ERTLGdavtIETDLAPDLW-NCRIDPTQAEVALL 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 592 NLLSNA----------------IKFTDIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQV-GTGvqrnfQGT 654
Cdd:PRK13557  284 NVLINArdampeggrvtirtrnVEIEDEDLAMYHGLPPGRYVSIAVTDTGSGMPPEILARVMDPFFTTkEEG-----KGT 358
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1736044238 655 GLGLAICEKLVSMMDGDISVDTEPGMGSqfTIRipLYsaqYPA 697
Cdd:PRK13557  359 GLGLSMVYGFAKQSGGAVRIYSEVGEGT--TVR--LY---FPA 394
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
827-932 4.39e-09

phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; Klebsiella pneumoniae RstA (kpRstA) is part of the RstA/RstB two-component regulatory system that may play a regulatory role in virulence. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 55.08  E-value: 4.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLgLTLPVVGVTANA 906
Cdd:cd17622     3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPK-YQGPILLLTALD 81
                          90       100
                  ....*....|....*....|....*.
gi 1736044238 907 LAEEKQRCLESGMDSCLSKPVTLDVL 932
Cdd:cd17622    82 SDIDHILGLELGADDYVVKPVEPAVL 107
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
603-689 5.31e-09

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


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 56.44  E-value: 5.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 603 IGCIVLHVCRAGDYLSIRVRDTGVGIpAKEVVR-------------------------LFDPFFQVGTGVQrNFQGTGLG 657
Cdd:cd16916    69 EGTITLRAEHQGNQVVIEVSDDGRGI-DREKIRekaierglitadeaatlsddevlnlIFAPGFSTAEQVT-DVSGRGVG 146
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1736044238 658 LAICEKLVSMMDGDISVDTEPGMGSQFTIRIP 689
Cdd:cd16916   147 MDVVKRSIESLGGTIEVESEPGQGTTFTIRLP 178
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
827-940 5.49e-09

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


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 55.14  E-value: 5.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGY-QCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVV---GV 902
Cdd:cd17530     3 VLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVIlmsGL 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1736044238 903 TANALAEEKQRCLESGMD--SCLSKPVTLDVLKQTLSVYA 940
Cdd:cd17530    83 DGGILESAETLAGANGLNllGTLSKPFSPEELTELLTKYT 122
PRK11517 PRK11517
DNA-binding response regulator HprR;
825-932 5.61e-09

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 57.60  E-value: 5.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 825 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTlPVVGVTA 904
Cdd:PRK11517    1 MKILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQT-PVICLTA 79
                          90       100
                  ....*....|....*....|....*...
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKPVTLDVL 932
Cdd:PRK11517   80 RDSVDDRVRGLDSGANDYLVKPFSFSEL 107
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
827-932 7.80e-09

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: 54.21  E-value: 7.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLgLTLPVVGVTANA 906
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQI-SNVPIIFISSRD 79
                          90       100
                  ....*....|....*....|....*.
gi 1736044238 907 LAEEKQRCLESGMDSCLSKPVTLDVL 932
Cdd:cd18159    80 DNMDQVMAINMGGDDYITKPFDLDVL 105
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
827-926 1.08e-08

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 57.00  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVVGVTANa 906
Cdd:PRK10710   13 ILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRFS-DIPIVMVTAK- 90
                          90       100
                  ....*....|....*....|..
gi 1736044238 907 lAEEKQRC--LESGMDSCLSKP 926
Cdd:PRK10710   91 -IEEIDRLlgLEIGADDYICKP 111
PRK10693 PRK10693
two-component system response regulator RssB;
854-936 1.11e-08

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 57.69  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 854 ANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANALAEEKQRCLESGMDSCLSKPVT-LDVL 932
Cdd:PRK10693    3 AANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKPVKdLNRL 82

                  ....
gi 1736044238 933 KQTL 936
Cdd:PRK10693   83 REMV 86
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
614-689 1.46e-08

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: 53.45  E-value: 1.46e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1736044238 614 GDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRnfqgtGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIP 689
Cdd:cd16915    34 GDDLVIEVRDTGPGIAPELRDKVFERGVSTKGQGER-----GIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
827-947 1.54e-08

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 53.70  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGY--QCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTA 904
Cdd:cd17532     1 ALIVDDEPLAREELRYLLEEHPDieIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFVTA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1736044238 905 -----------NALaeekqrclesgmDSCLsKPVTLDVLKQTLsvyaERVRKTR 947
Cdd:cd17532    81 ydeyaveafelNAV------------DYLL-KPFSEERLAEAL----AKLRKRL 117
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
827-936 2.59e-08

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 53.03  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGY-QCKTANDGVDALNVLSKNHIDIVLSDVNMPN-MDGYRLTQRIRQLGLTLP---VVG 901
Cdd:cd17589     1 FLIVDDQPTFRSMLKSMLRSLGVtRIDTASSGEEALRMCENKTYDIVLCDYNLGKgKNGQQLLEELRHKKLISPstvFIM 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1736044238 902 VTANALAEEKQRCLESGMDSCLSKPVTLDVLKQTL 936
Cdd:cd17589    81 VTGESSRAMVLSALELEPDDYLLKPFTVSELRERL 115
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
827-926 2.60e-08

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


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 52.81  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDH-PINRrLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVVGVTAN 905
Cdd:cd17614     1 ILVVDDEkPISD-ILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTS-NVPIIMLTAK 78
                          90       100
                  ....*....|....*....|.
gi 1736044238 906 ALAEEKQRCLESGMDSCLSKP 926
Cdd:cd17614    79 DSEVDKVLGLELGADDYVTKP 99
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
825-930 2.64e-08

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


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 52.83  E-value: 2.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 825 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVT- 903
Cdd:cd17563     1 KSLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTg 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1736044238 904 ----ANALAEEKqrcleSGMDSCLSKPVTLD 930
Cdd:cd17563    81 yasiATAVEAIK-----LGADDYLAKPADAD 106
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
350-690 3.00e-08

nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 57.22  E-value: 3.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 350 QRLEEHEQFNRKIVASAPVGICILRTQdGTNILSN-------------ELAHNYLNMLTHEDRQRLTQIIcGQQVNFvdv 416
Cdd:TIGR02938 123 QVVANQKLLIESVVDAAPVAFVLLDPT-GRVILDNqeykklatdlrvkEPAHTVLDLLREAWREALAENW-PQQLAF--- 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 417 ltsthTNLQISF------------VHSR-YRNENVA-------------ICVLVDVSARVKMEE-----SLQEMAQAAEQ 465
Cdd:TIGR02938 198 -----SNREARFdrgggrparwlsCTGSvIGMESDCadsffcaaeqpylLLTIADISNLREEQErarlsALQALMAEEER 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 466 ASQSKSMFLATVsHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDIldfskieSEQLKIEPREFSP 545
Cdd:TIGR02938 273 LEAIRETLSAAI-HRLQGPMNLISAAISVLQRRGDDAGNPASAAMLQQALSAGREHMEAL-------RQVIPQSPQEIVV 344
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 546 REVMNHISANYLPLVVRKQLGLYCFIE----PDVPlTLHGDPMRLQQVISNLLSNAIKFTDIGC-----IVLHVCRAGDY 616
Cdd:TIGR02938 345 PVNLNQILRDVITLSTPRLLAAGIVVDwqpaATLP-AILGRELQLRSLFKALVDNAIEAMNIKGwkrreLSITTALNGDL 423
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1736044238 617 LSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQrnfQGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIPL 690
Cdd:TIGR02938 424 IVVSILDSGPGIPQDLRYKVFEPFFTTKGGSR---KHIGMGLSVAQEIVADHGGIIDLDDDYSEGCRIIVEFRV 494
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
825-944 5.66e-08

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 55.93  E-value: 5.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 825 MMI--LVVDDHPINRRLLADQLGS------LGyqckTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT 896
Cdd:PRK00742    2 MKIrvLVVDDSAFMRRLISEILNSdpdievVG----TAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRPT 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1736044238 897 lPVVGVTanAL----AEEKQRCLESGMDSCLSKPVT-----LDVLKQTLsvyAERVR 944
Cdd:PRK00742   78 -PVVMVS--SLtergAEITLRALELGAVDFVTKPFLgislgMDEYKEEL---AEKVR 128
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
827-926 8.63e-08

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: 51.32  E-value: 8.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVVGVTANA 906
Cdd:cd17626     3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAES-GVPIVMLTAKS 81
                          90       100
                  ....*....|....*....|
gi 1736044238 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:cd17626    82 DTVDVVLGLESGADDYVAKP 101
fixJ PRK09390
response regulator FixJ; Provisional
823-932 1.06e-07

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 53.08  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 823 DDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGV 902
Cdd:PRK09390    2 DKGVVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVM 81
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1736044238 903 TANA---LAEEKQRcleSGMDSCLSKPVTLDVL 932
Cdd:PRK09390   82 TGHGdvpLAVEAMK---LGAVDFIEKPFEDERL 111
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
584-690 1.29e-07

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 51.07  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 584 MRLQQVISNLLSNAIK----FTDIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPffqvgtgvqrnFQGTGLGLA 659
Cdd:COG2172    33 DDLVLAVSEAVTNAVRhaygGDPDGPVEVELELDPDGLEIEVRDEGPGFDPEDLPDPYST-----------LAEGGRGLF 101
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1736044238 660 ICEKLvsmMDgDISVDTEPGmGSQFTIRIPL 690
Cdd:COG2172   102 LIRRL---MD-EVEYESDPG-GTTVRLVKRL 127
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
827-926 1.72e-07

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


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 50.20  E-value: 1.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANA 906
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80
                          90       100
                  ....*....|....*....|
gi 1736044238 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:cd19928    81 TLMTAVKAAERGAFEYLPKP 100
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
827-890 2.41e-07

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 49.71  E-value: 2.41e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLS--KNHIDIVLSDVNMPNMDGYRLTQRI 890
Cdd:cd17582     1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEdeQNEIDLILTEVDLPVSSGFKLLSYI 66
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
827-943 2.78e-07

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 52.41  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT--LPVVGVTA 904
Cdd:PRK10161    5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTrdIPVVMLTA 84
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKPVTLDVLKQTLSVYAERV 943
Cdd:PRK10161   85 RGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMRRI 123
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
594-689 3.54e-07

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


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 48.70  E-value: 3.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 594 LSNAIKFTDIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRlfdpffqvgtgvqrnfqGTGLGLAICEKLVSMMDGDIS 673
Cdd:cd16917     9 LTNALKHAGASRVRVTLSYTADELTLTVVDDGVGFDGPAPPG-----------------GGGFGLLGMRERAELLGGTLT 71
                          90
                  ....*....|....*.
gi 1736044238 674 VDTEPGMGSQFTIRIP 689
Cdd:cd16917    72 IGSRPGGGTRVTARLP 87
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
819-925 3.64e-07

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 51.95  E-value: 3.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 819 ASVNDDMMILVVDDHPINRR------LLADQLGSLGyqckTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQ 892
Cdd:PRK10651    1 MSNQEPATILLIDDHPMLRTgvkqliSMAPDITVVG----EASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLRE 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1736044238 893 LGLTLPVVGVTANALAEEKQRCLESGMDSCLSK 925
Cdd:PRK10651   77 KSLSGRIVVFSVSNHEEDVVTALKRGADGYLLK 109
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
593-690 4.40e-07

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 53.48  E-value: 4.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 593 LLSNAIKF-----TDIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGtgvqrnfQGTGLGLAICEKLVSM 667
Cdd:COG2972   344 LVENAIEHgiepkEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLLEELSSKG-------EGRGIGLRNVRERLKL 416
                          90       100
                  ....*....|....*....|....*.
gi 1736044238 668 MDGD---ISVDTEPGMGSQFTIRIPL 690
Cdd:COG2972   417 YYGEeygLEIESEPGEGTTVTIRIPL 442
glnL PRK11073
nitrogen regulation protein NR(II);
457-690 4.85e-07

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 52.78  E-value: 4.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 457 QEMAQAAEQasQSKSMFLATVSHELRTPLYGIIGNLDLLQtKELPkgvDRLVTamnnssslllkiisdilDFSKIESEQ- 535
Cdd:PRK11073  119 QEQLQHAQQ--VAARDLVRGLAHEIKNPLGGLRGAAQLLS-KALP---DPALT-----------------EYTKVIIEQa 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 536 --LK-IEPREFSPREVMNHISANYLPLV--VRKQLGLYC-----FI---EPDVPLTLHgDPMRLQQVISNLLSNA----- 597
Cdd:PRK11073  176 drLRnLVDRLLGPQRPGTHVTESIHKVAerVVQLVSLELpdnvrLIrdyDPSLPELAH-DPDQIEQVLLNIVRNAlqalg 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 598 -------IKFTDIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGvqrnfqGTGLGLAICEKLVSMMDG 670
Cdd:PRK11073  255 peggtitLRTRTAFQLTLHGERYRLAARIDIEDNGPGIPPHLQDTLFYPMVSGREG------GTGLGLSIARNLIDQHSG 328
                         250       260
                  ....*....|....*....|
gi 1736044238 671 DISVDTEPGMgSQFTIRIPL 690
Cdd:PRK11073  329 KIEFTSWPGH-TEFSVYLPI 347
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
582-689 6.08e-07

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: 48.69  E-value: 6.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 582 DPMRLQQVISNLLSNAI-----KFTDIGCIVLHV-CRAGDYLSIRVRDTGVGIPAKEVVRLFDPFfqvgtgVQRNFQGTG 655
Cdd:cd16944     1 DTTQISQVLTNILKNAAeaiegRPSDVGEVRIRVeADQDGRIVLIVCDNGKGFPREMRHRATEPY------VTTRPKGTG 74
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1736044238 656 LGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIP 689
Cdd:cd16944    75 LGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
HATPase_YpdA-YehU-LytS-like cd16924
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
583-689 6.84e-07

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


Pssm-ID: 340401 [Multi-domain]  Cd Length: 103  Bit Score: 48.60  E-value: 6.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 583 PMRLQQVISNLLSNAI-KFTDIGCIVLHVCRAGDYLSIRVRDTGVGIPAKevvrlfdpffQVGTGVQRNFQGTGLGLAIC 661
Cdd:cd16924     3 PFTLQPLVENAIQHGLsPLTDKGVVTISALKEDNHVMIEVEDNGRGIDPK----------VLNILGKKPKEGNGIGLYNV 72
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1736044238 662 EKLVSMMDGD---ISVDTEPGMGSQFTIRIP 689
Cdd:cd16924    73 HQRLILLFGEdygIHIASEPDKGTRITFTIP 103
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
827-926 7.41e-07

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 51.34  E-value: 7.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSkNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTlPVVGVTANA 906
Cdd:PRK10955    4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLD-DSIDLLLLDVMMPKKNGIDTLKELRQTHQT-PVIMLTARG 81
                          90       100
                  ....*....|....*....|
gi 1736044238 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:PRK10955   82 SELDRVLGLELGADDYLPKP 101
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
582-688 8.21e-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: 48.23  E-value: 8.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 582 DPMRLQQVISNLLSNAIKFTDIGCIV-LHVCRAGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGvqRNFQG-TGLGLA 659
Cdd:cd16975     1 DTLLLSRALINIISNACQYAPEGGTVsISIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTS--RRSGGhYGMGLY 78
                          90       100
                  ....*....|....*....|....*....
gi 1736044238 660 ICEKLVSMMDGDISVDTEPGMGSQFTIRI 688
Cdd:cd16975    79 IAKNLVEKHGGSLIIENSQKGGAEVTVKI 107
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
827-929 8.35e-07

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: 48.60  E-value: 8.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVVGVTANA 906
Cdd:cd17594     2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARS-DVPIIIISGDR 80
                          90       100
                  ....*....|....*....|....
gi 1736044238 907 LAEE-KQRCLESGMDSCLSKPVTL 929
Cdd:cd17594    81 RDEIdRVVGLELGADDYLAKPFGL 104
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
827-932 9.69e-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: 48.52  E-value: 9.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLgLTLPVVGVTANa 906
Cdd:cd19939     2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREH-SHVPILMLTAR- 79
                          90       100
                  ....*....|....*....|....*...
gi 1736044238 907 lAEEKQRCL--ESGMDSCLSKPVTLDVL 932
Cdd:cd19939    80 -TEEMDRVLglEMGADDYLCKPFSPREL 106
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
827-926 1.45e-06

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: 47.36  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGL--TLPVVGVTA 904
Cdd:cd17602     1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSAlkDTPIIMLTG 80
                          90       100
                  ....*....|....*....|..
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKP 926
Cdd:cd17602    81 KDGLVDRIRAKMAGASGYLTKP 102
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
853-936 1.92e-06

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 47.65  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 853 TANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANALAEEKQRCLESGMDSCLSKPVTLDVL 932
Cdd:cd19930    29 QASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTTFGRPGYFRRALAAGVDGYVLKDRPIEEL 108

                  ....
gi 1736044238 933 KQTL 936
Cdd:cd19930   109 ADAI 112
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
825-926 2.82e-06

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 49.54  E-value: 2.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 825 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTA 904
Cdd:PRK09836    1 MKLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTA 80
                          90       100
                  ....*....|....*....|..
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKP 926
Cdd:PRK09836   81 LGTIEHRVKGLELGADDYLVKP 102
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
827-937 4.62e-06

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 46.57  E-value: 4.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLAdQLGSLGYQCKT---ANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVT 903
Cdd:cd19931     1 VLLIDDHPLLRKGIK-QLIELDPDFTVvgeASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILT 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1736044238 904 ANALAEEKQRCLESGMDSCLSK---PVTL-DVLKQTLS 937
Cdd:cd19931    80 VSDAEDDVVTALRAGADGYLLKdmePEDLlEALKQAAS 117
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
827-932 5.18e-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: 46.27  E-value: 5.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTANA 906
Cdd:cd17573     1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSDNP 80
                          90       100
                  ....*....|....*....|....*.
gi 1736044238 907 LAEEKQRCLESGMDSCLSKPVTLDVL 932
Cdd:cd17573    81 KTEQEIEAFKEGADDYIAKPFDFKVL 106
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
827-927 5.95e-06

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 45.73  E-value: 5.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLA-----DQLGSLgyqCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVG 901
Cdd:cd17565     1 FYIVDDDKNIIKILSdiiedDDLGEV---VGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIM 77
                          90       100
                  ....*....|....*....|....*.
gi 1736044238 902 VTANALAEEKQRCLESGMDSCLSKPV 927
Cdd:cd17565    78 ISQVSDKEMIGKAYQAGIEFFINKPI 103
PRK10337 PRK10337
sensor protein QseC; Provisional
473-687 6.19e-06

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 49.65  E-value: 6.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 473 FLATVSHELRTPLYGI-----IGNL--DLLQTKE-----LPKGVDRLVtamnnssslllKIISDILDFSKIESE-QLK-I 538
Cdd:PRK10337  240 FTSDAAHELRSPLAALkvqteVAQLsdDDPQARKkallqLHAGIDRAT-----------RLVDQLLTLSRLDSLdNLQdV 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 539 EPREFSP---REVMNHIS-ANYLPLVVRKQLglycfiePDVPLTLHGDPMRLQQVISNLLSNAIKFTDIGCIVLHVCRAG 614
Cdd:PRK10337  309 AEIPLEDllqSAVMDIYHtAQQAGIDVRLTL-------NAHPVIRTGQPLLLSLLVRNLLDNAIRYSPQGSVVDVTLNAR 381
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1736044238 615 dylSIRVRDTGVGIPAKEVVRLFDPFF----QVGTgvqrnfqGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIR 687
Cdd:PRK10337  382 ---NFTVRDNGPGVTPEALARIGERFYrppgQEAT-------GSGLGLSIVRRIAKLHGMNVSFGNAPEGGFEAKVS 448
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
825-904 1.31e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 48.34  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 825 MMILVVDDHPINRRLLADQLGSL-GYQ-CKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTlPVVGV 902
Cdd:PRK12555    1 MRIGIVNDSPLAVEALRRALARDpDHEvVWVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAERPC-PILIV 79

                  ..
gi 1736044238 903 TA 904
Cdd:PRK12555   80 TS 81
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
827-944 1.38e-05

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 47.15  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLAdQLGSLGYQCKT---ANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVT 903
Cdd:PRK10403    9 VLIVDDHPLMRRGVR-QLLELDPGFEVvaeAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQIIILT 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1736044238 904 ANALAEEKQRCLESGMDSCLSKPVTLDVLKQTL-------SVYAERVR 944
Cdd:PRK10403   88 VSDASSDVFALIDAGADGYLLKDSDPEVLLEAIragakgsKVFSERVN 135
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
571-689 2.23e-05

Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain alpha-ketoacid dehydrogenase kinase and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of all four PDK isoforms (pyruvate dehydrogenase kinases 1-4) that have been described in mammals, and other PDKs including Saccharomyces Pkp1p and Pkp2p. PDKs and phosphatases tightly regulate the mitochondrial pyruvate dehydrogenase complex (PDC) by reversible phosphorylation. PDC catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA, connecting glycolysis and the TCA acid cycle. Also included in this family is mammalian branched-chain alpha-ketoacid dehydrogenase kinase (BDK), a mitochondrial protein kinase that phosphorylates a subunit of the branched-chain a-ketoacid dehydrogenase (BCKD) complex, which catalyzes the oxidative decarboxylation of branched-chain alpha-ketoacids derived from leucine, isoleucine, and valine, a rate-limiting step in the oxidative degradation of these branched-chain amino acids.


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 45.79  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 571 IEPDVPLTLHGDPMRLQQVISNLLSNAIKFT---------DIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRLF---- 637
Cdd:cd16929    29 IEGDPSIRFPYVPSHLYYILFELLKNAMRATveshgddsdDLPPIKVTVAKGDEDLTIKISDRGGGIPREDLARLFsymy 108
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1736044238 638 --------DPFFQVGTGVQRNF-QGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIP 689
Cdd:cd16929   109 stapqpslDDFSDLISGTQPSPlAGFGYGLPMSRLYAEYFGGDLDLQSMEGYGTDVYIYLK 169
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
584-689 2.29e-05

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


Pssm-ID: 340427 [Multi-domain]  Cd Length: 131  Bit Score: 45.10  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 584 MRLQQVISNLLSNAIK--FTD--IGCIVLHVCRAGDYLSIRVRDTGVGIPakevvrlfdpffQVGTGVQRNfqgtGLGLA 659
Cdd:cd16951    38 TAIGLVVNELLQNALKhaFSDreGGTITIRSVVDGDYLRITVIDDGVGLP------------QDEDWPNKG----SLGLQ 101
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1736044238 660 ICEKLVS-MMDGDISVDTEpGMGSQFTIRIP 689
Cdd:cd16951   102 IVRSLVEgELKAFLEVQSA-ENGTRVNIDIP 131
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
577-693 2.42e-05

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 46.92  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 577 LTLHGDPMRLQQVISN--------LLSNAIKFTDIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVrlfdpffqvgtgvq 648
Cdd:COG4585   146 LDVDGDPDRLPPEVELalyrivqeALTNALKHAGATRVTVTLEVDDGELTLTVRDDGVGFDPEAAP-------------- 211
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1736044238 649 rnfqGTGLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIPLYSA 693
Cdd:COG4585   212 ----GGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPLAAA 252
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
562-678 6.82e-05

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 46.55  E-value: 6.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 562 RKQLGLYCFIEPDVplTLHGDPMRLQQVISNLLSNAIK----FTDIGcivlhVCRAGDYLSIRVRDTGVGIP--AKEVVr 635
Cdd:PRK10815  357 RKGVNITLDISPEI--TFVGEKNDFMEVMGNVLDNACKycleFVEIS-----ARQTDEHLHIVVEDDGPGIPesKRELI- 428
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1736044238 636 lfdpfFQVGTGVQRNFQGTGLGLAICEKLVSMMDGDISVDTEP 678
Cdd:PRK10815  429 -----FDRGQRADTLRPGQGLGLSVAREITEQYEGKISAGDSP 466
PRK09483 PRK09483
response regulator; Provisional
827-890 7.75e-05

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 45.10  E-value: 7.75e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINR----RLLADQLG--SLGyqckTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRI 890
Cdd:PRK09483    4 VLLVDDHELVRagirRILEDIKGikVVG----EACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKI 69
PRK11173 PRK11173
two-component response regulator; Provisional
827-892 9.70e-05

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 45.01  E-value: 9.70e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQ 892
Cdd:PRK11173    6 ILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELRE 71
PRK13560 PRK13560
hypothetical protein; Provisional
589-693 1.05e-04

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 46.20  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 589 VISNLLSNAIK--FTDIGC--IVLHVCRAGD-YLSIRVRDTGVGIPAKevvrlFDpFFQVGTgvqrnfqgtgLGLAICEK 663
Cdd:PRK13560  715 IISELLSNALKhaFPDGAAgnIKVEIREQGDgMVNLCVADDGIGLPAG-----FD-FRAAET----------LGLQLVCA 778
                          90       100       110
                  ....*....|....*....|....*....|
gi 1736044238 664 LVSMMDGDISVDTEpgMGSQFTIRIPLYSA 693
Cdd:PRK13560  779 LVKQLDGEIALDSR--GGARFNIRFPMSPA 806
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
825-926 1.24e-04

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 44.57  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 825 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTA 904
Cdd:PRK11083    4 PTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFLTA 83
                          90       100
                  ....*....|....*....|....
gi 1736044238 905 NalAEEKQRC--LESGMDSCLSKP 926
Cdd:PRK11083   84 R--SDEVDRLvgLEIGADDYVAKP 105
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
827-925 1.70e-04

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 43.71  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINR---RLLADQLGSLGYQCKTaNDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVT 903
Cdd:PRK09935    6 VIIMDTHPIIRmsiEVLLQKNSELQIVLKT-DDYRITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQSTVKVLFLS 84
                          90       100
                  ....*....|....*....|..
gi 1736044238 904 ANALAEEKQRCLESGMDSCLSK 925
Cdd:PRK09935   85 SKSECFYAGRAIQAGANGFVSK 106
PRK10336 PRK10336
two-component system response regulator QseB;
825-929 1.89e-04

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 43.73  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 825 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVTA 904
Cdd:PRK10336    1 MRILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTA 80
                          90       100
                  ....*....|....*....|....*
gi 1736044238 905 NALAEEKQRCLESGMDSCLSKPVTL 929
Cdd:PRK10336   81 RDALAERVEGLRLGADDYLCKPFAL 105
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
825-925 1.94e-04

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 43.73  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 825 MMILVVDDHPINRRLLADQLGSLGYQCKTA-NDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVVGVT 903
Cdd:PRK09958    1 MNAIIIDDHPLAIAAIRNLLIKNDIEILAElTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIVS 80
                          90       100
                  ....*....|....*....|..
gi 1736044238 904 ANALAEEKQRCLESGMDSCLSK 925
Cdd:PRK09958   81 AKNDHFYGKHCADAGANGFVSK 102
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
827-891 2.58e-04

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


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 41.97  E-value: 2.58e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1736044238 827 ILVVDDHPIN----RRLLADQlgslgYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIR 891
Cdd:cd17596     3 ILVVDDEVRSlealRRTLEED-----FDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVR 66
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
603-690 3.03e-04

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 44.40  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 603 IGCIVLHVCRAGDYLSIRVRDTGVGI-PAK----------------------EVVRL-FDPFF----QVgtgvqRNFQGT 654
Cdd:COG0643   308 TGTITLSAYHEGGRVVIEVSDDGRGLdLEKirakaiekglitaeeaaalsdeELLELiFAPGFstaeEV-----TDLSGR 382
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1736044238 655 GLGLAICEKLVSMMDGDISVDTEPGMGSQFTIRIPL 690
Cdd:COG0643   383 GVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPL 418
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
589-679 8.20e-04

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


Pssm-ID: 340413 [Multi-domain]  Cd Length: 91  Bit Score: 39.56  E-value: 8.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 589 VISNLLSNAIKFTDIGC----IVLHVCRAGDYLSIRVRDTGVGIPakeVVRLFDPffqvgtgvQRNFQGTGLGLAICEKL 664
Cdd:cd16936     4 AVSEAVTNAVRHAYRHDgpgpVRLELDLDPDRLRVEVTDSGPGFD---PLRPADP--------DAGLREGGRGLALIRAL 72
                          90
                  ....*....|....*
gi 1736044238 665 vsmMDgDISVDTEPG 679
Cdd:cd16936    73 ---MD-EVGYRRTPG 83
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
827-942 9.02e-04

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 41.71  E-value: 9.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVVGVTANA 906
Cdd:PRK10529    4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQWS-AIPVIVLSARS 82
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1736044238 907 LAEEKQRCLESGMDSCLSKPVTLDVLKQTLSVYAER 942
Cdd:PRK10529   83 EESDKIAALDAGADDYLSKPFGIGELQARLRVALRR 118
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
853-926 9.91e-04

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


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 39.51  E-value: 9.91e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1736044238 853 TANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQL-GLTLPVVgVTANALAEEK--QRCLESGMDSCLSKP 926
Cdd:cd17561    32 VAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMrLEKRPKI-IMLTAFGQEDitQRAVELGASYYILKP 107
PRK10430 PRK10430
two-component system response regulator DcuR;
827-942 1.70e-03

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 41.25  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 827 ILVVDDHP----INRRLLAdQLGslGYQC-KTANDGVDALNVL--SKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPV 899
Cdd:PRK10430    4 VLIVDDDAmvaeLNRRYVA-QIP--GFQCcGTASTLEQAKEIIfnSDTPIDLILLDIYMQQENGLDLLPVLHEAGCKSDV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1736044238 900 VGVTANALAEEKQRCLESGMDSCLSKPVTLDVLKQTLSVYAER 942
Cdd:PRK10430   81 IVISSAADAATIKDSLHYGVVDYLIKPFQASRFEEALTGWRQK 123
PAS COG2202
PAS domain [Signal transduction mechanisms];
349-483 2.52e-03

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 40.78  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 349 AQRLEEHEQFNRKIVASAPVGICILRTqDGTNILSN------------ELAHNYLNMLTHED-----RQRLTQIICGQQV 411
Cdd:COG2202     3 EEALEESERRLRALVESSPDAIIITDL-DGRILYVNpaferltgysaeELLGKTLRDLLPPEdddefLELLRAALAGGGV 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1736044238 412 NFVDVL------TSTHTNLQISFVHSRYRNENVAICVLVDVSARVKMEESLQEMAQAAEQASQSKSMFLATVSHELRT 483
Cdd:COG2202    82 WRGELRnrrkdgSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRI 159
HATPase_SpoIIAB-like cd16942
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ...
586-687 4.62e-03

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


Pssm-ID: 340418 [Multi-domain]  Cd Length: 135  Bit Score: 38.29  E-value: 4.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736044238 586 LQQVISNLLSNAI----KFTDIGCIVLHVCRAGDYLSIRVRDTGVGIPAKEVVRlfDPFFQVGTGVQRnfqgTGLGLAIC 661
Cdd:cd16942    39 IKTVVSEAVTNAIihgyNNDPNGIVSISVIIEDGVVHLTVRDEGVGIPDIEEAR--QPLFTTKPELER----SGMGFTIM 112
                          90       100
                  ....*....|....*....|....*.
gi 1736044238 662 EklvSMMDgDISVDTEPGMGSQFTIR 687
Cdd:cd16942   113 E---NFMD-EVIVESEVNKGTTVYLK 134
 
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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