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Conserved domains on  [gi|145698285|ref|NP_416722|]
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histidine kinase RcsC [Escherichia coli str. K-12 substr. MG1655]

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;
24-947 0e+00

two-component system sensor histidine kinase RcsC;


:

Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 1973.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  24 VLWLLIAFSSVFYIVNALHQRESEIRQEFNLSSDQAQRFIQRTSDVMKELKYIAENRLSAENGVLSPRGRETQADVPAFE 103
Cdd:PRK10841   1 MLWLLGALLSVFYIVNALHERESEIRQEFNLSSDQAQRYIRHTSDVMRELKYIAENRLSAENGVLSPRGRETKTDVPAFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 104 PLFADSDCSAMSNTWRGSLESLAWFMRYWRDNFSAAYDLNRVFLIGSDNLCMANFGLRDMPVERDTALKALHERINKYRN 183
Cdd:PRK10841  81 PLFADSDCSAMSNTWRGSLESLAWFMRYWRDNFSAAYDLNRVFLIGSDNLCMANFGLRNMPVERDTALKALHERINKYRN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 184 APQDDSGSNLYWISEGPRPGVGYFYALTPVYLANRLQALLGVEQTIRMENFFLPGTLPMGVTILDENGHTLISLTGPESK 263
Cdd:PRK10841 161 APQQDKGSNLYWISPGARPGVGYFYALTPVYLANRLQALLGIEQTIRLENFFTPGTLPMGVTLLDENGHPLLSLTGPESK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 264 IKGDPRWMQERSWFGYTEGFRELVLKKNLPPSSLSIVYSVPVDKVLERIRMLILNAILLNVLAGAALFTLARMYERRIFI 343
Cdd:PRK10841 241 IKADPRWPQERSWFGYTDGFRELVLKKNLPPSSLSIVYSVPVDKVLERIRMLILNAILLNVLSAIVLFTLARLFERRIFI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 344 PAESDALRLEEHEQFNRKIVASAPVGICILRTADGVNILSNELAHTYLNMLTHEDRQRLTQIICGQQVNFVDVLTSNNTN 423
Cdd:PRK10841 321 PAESNALRLEEHEQFNRKIVASAPVGICILRTSDGTNILSNELAHNYLNMLTHEDRQRLTQIICGQQVNFVDVLTSNNTN 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 424 LQISFVHSRYRNENVAICVLVDVSSRVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKG 503
Cdd:PRK10841 401 LQISFVHSRYRNENVAICVLVDVSARVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKG 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 504 VDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEPREFSPREVMNHITANYLPLVVRKQLGLYCFIEPDVPVALNGDP 583
Cdd:PRK10841 481 VDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEPREFSPREVINHITANYLPLVVKKRLGLYCFIEPDVPVALNGDP 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 584 MRLQQVISNLLSNAIKFTDTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEK 663
Cdd:PRK10841 561 MRLQQVISNLLSNAIKFTDTGCIVLHVRVDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEK 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 664 LISMMDGDISVDSEPGMGSQFTVRIPLYGAQYPQKKGVEGLSGKRCWLAVRNASLCQFLETSLQRSGIVVTTYEGQEPTP 743
Cdd:PRK10841 641 LINMMDGDISVDSEPGMGSQFTIRIPLYGAQYPQKKGVEGLQGKRCWLAVRNASLEQFLETLLQRSGIQVQRYEGQEPTP 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 744 EDVLITDEVVSKKWQGRAVVTFCRRHIGIPLEKAPGEWVHSVAAPHELPALLARIYLIEMESDDPANALPSTDKAVSDND 823
Cdd:PRK10841 721 EDVLITDDPVQKKWQGRAVITFCRRHIGIPLEIAPGEWVHSTATPHELPALLARIYRIELESDDSANALPSTDKAVSDND 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 824 DMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVT 903
Cdd:PRK10841 801 DMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVT 880
                        890       900       910       920
                 ....*....|....*....|....*....|....*....|....
gi 145698285 904 ANALAEEKQRCLESGMDSCLSKPVTLDVIKQTLTLYAERVRKSR 947
Cdd:PRK10841 881 ANALAEEKQRCLEAGMDSCLSKPVTLDVLKQTLTVYAERVRKSR 924
 
Name Accession Description Interval E-value
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
24-947 0e+00

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 1973.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  24 VLWLLIAFSSVFYIVNALHQRESEIRQEFNLSSDQAQRFIQRTSDVMKELKYIAENRLSAENGVLSPRGRETQADVPAFE 103
Cdd:PRK10841   1 MLWLLGALLSVFYIVNALHERESEIRQEFNLSSDQAQRYIRHTSDVMRELKYIAENRLSAENGVLSPRGRETKTDVPAFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 104 PLFADSDCSAMSNTWRGSLESLAWFMRYWRDNFSAAYDLNRVFLIGSDNLCMANFGLRDMPVERDTALKALHERINKYRN 183
Cdd:PRK10841  81 PLFADSDCSAMSNTWRGSLESLAWFMRYWRDNFSAAYDLNRVFLIGSDNLCMANFGLRNMPVERDTALKALHERINKYRN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 184 APQDDSGSNLYWISEGPRPGVGYFYALTPVYLANRLQALLGVEQTIRMENFFLPGTLPMGVTILDENGHTLISLTGPESK 263
Cdd:PRK10841 161 APQQDKGSNLYWISPGARPGVGYFYALTPVYLANRLQALLGIEQTIRLENFFTPGTLPMGVTLLDENGHPLLSLTGPESK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 264 IKGDPRWMQERSWFGYTEGFRELVLKKNLPPSSLSIVYSVPVDKVLERIRMLILNAILLNVLAGAALFTLARMYERRIFI 343
Cdd:PRK10841 241 IKADPRWPQERSWFGYTDGFRELVLKKNLPPSSLSIVYSVPVDKVLERIRMLILNAILLNVLSAIVLFTLARLFERRIFI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 344 PAESDALRLEEHEQFNRKIVASAPVGICILRTADGVNILSNELAHTYLNMLTHEDRQRLTQIICGQQVNFVDVLTSNNTN 423
Cdd:PRK10841 321 PAESNALRLEEHEQFNRKIVASAPVGICILRTSDGTNILSNELAHNYLNMLTHEDRQRLTQIICGQQVNFVDVLTSNNTN 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 424 LQISFVHSRYRNENVAICVLVDVSSRVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKG 503
Cdd:PRK10841 401 LQISFVHSRYRNENVAICVLVDVSARVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKG 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 504 VDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEPREFSPREVMNHITANYLPLVVRKQLGLYCFIEPDVPVALNGDP 583
Cdd:PRK10841 481 VDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEPREFSPREVINHITANYLPLVVKKRLGLYCFIEPDVPVALNGDP 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 584 MRLQQVISNLLSNAIKFTDTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEK 663
Cdd:PRK10841 561 MRLQQVISNLLSNAIKFTDTGCIVLHVRVDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEK 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 664 LISMMDGDISVDSEPGMGSQFTVRIPLYGAQYPQKKGVEGLSGKRCWLAVRNASLCQFLETSLQRSGIVVTTYEGQEPTP 743
Cdd:PRK10841 641 LINMMDGDISVDSEPGMGSQFTIRIPLYGAQYPQKKGVEGLQGKRCWLAVRNASLEQFLETLLQRSGIQVQRYEGQEPTP 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 744 EDVLITDEVVSKKWQGRAVVTFCRRHIGIPLEKAPGEWVHSVAAPHELPALLARIYLIEMESDDPANALPSTDKAVSDND 823
Cdd:PRK10841 721 EDVLITDDPVQKKWQGRAVITFCRRHIGIPLEIAPGEWVHSTATPHELPALLARIYRIELESDDSANALPSTDKAVSDND 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 824 DMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVT 903
Cdd:PRK10841 801 DMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVT 880
                        890       900       910       920
                 ....*....|....*....|....*....|....*....|....
gi 145698285 904 ANALAEEKQRCLESGMDSCLSKPVTLDVIKQTLTLYAERVRKSR 947
Cdd:PRK10841 881 ANALAEEKQRCLEAGMDSCLSKPVTLDVLKQTLTVYAERVRKSR 924
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
461-936 3.82e-77

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: 272.04  E-value: 3.82e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  461 QAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEP 540
Cdd:TIGR02956 455 AEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISP 534
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  541 REFSPREVMNHITANYLPLVVRKQLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHVRADGD-YLSI 619
Cdd:TIGR02956 535 RPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDsSLLF 614
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  620 RVRDTGVGIPAKEVVRLFDPFFQVgTGvQRNFQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIPLygaqyPQKK 699
Cdd:TIGR02956 615 EVEDTGCGIAEEEQATLFDAFTQA-DG-RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPL-----TRGK 687
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  700 GVEGLSGkrcwlavrnaslcqfletslqrsgivvttyegqeptpedvlitdevvskkwqgravvtfcRRHIGIPlekapg 779
Cdd:TIGR02956 688 PAEDSAT------------------------------------------------------------LTVIDLP------ 701
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  780 ewvhsvaaphelpallariyliemesddPANalpstdkavsdnddmmILVVDDHPINRRLLADQLGSLGYQCKTANDGVD 859
Cdd:TIGR02956 702 ----------------------------PQR----------------VLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQS 737
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  860 ALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQL---GLTLPVIGVTANALAEEKQRCLESGMDSCLSKPVTLDVIKQTL 936
Cdd:TIGR02956 738 ALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIygaKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMI 817
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
372-690 5.88e-77

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 254.45  E-value: 5.88e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 372 ILRTADGVNILSNELAHTYLNMLTHEDRQRLTQIICGQQVNFVDVLTSNNTNLQISFVHSRYRNENVAICVLVDVSSRVK 451
Cdd:COG0642   12 LLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 452 MEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQtKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKI 531
Cdd:COG0642   92 LLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLL-EELDEEQREYLETILRSADRLLRLINDLLDLSRL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 532 ESEQLKIEPREFSPREVMNHITANYLPLVVRKQLGLYCFIEPDVPVaLNGDPMRLQQVISNLLSNAIKFTDTG-CIVLHV 610
Cdd:COG0642  171 EAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPT-VRGDPDRLRQVLLNLLSNAIKYTPEGgTVTVSV 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 611 RADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGvqRNFQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIPL 690
Cdd:COG0642  250 RREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLPL 327
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
586-690 5.48e-50

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: 171.52  E-value: 5.48e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 586 LQQVISNLLSNAIKFTDTGCIVLHVRADGD-----YLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAI 660
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEeedgvQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 145698285 661 CEKLISMMDGDISVDSEPGMGSQFTVRIPL 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 1.17e-45

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: 158.62  E-value: 1.17e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  709 CWLAVRNASLCQFLETSLQRSGIVVTTYEGQEPTPEDVLITDEVVSKKWQGRAVVTFCRRHIGIPLEKAPGEWVHSVAAP 788
Cdd:pfam09456   1 CWLDIRNASLEEYLLRLLQQSGLTVTRYEGQEPDADDVLISDYPLAIAWPVRAYIEFSRRHIGSPQETRPGYWLHSTATL 80
                          90
                  ....*....|.
gi 145698285  789 HELPALLARIY 799
Cdd:pfam09456  81 HELPALLERIY 91
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
581-690 2.44e-40

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 144.33  E-value: 2.44e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285   581 GDPMRLQQVISNLLSNAIKFTDT-GCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVqRNFQGTGLGLA 659
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEgGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRS-RKIGGTGLGLS 79
                           90       100       110
                   ....*....|....*....|....*....|.
gi 145698285   660 ICEKLISMMDGDISVDSEPGMGSQFTVRIPL 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 2.94e-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: 127.18  E-value: 2.94e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 440 ICVLVDVSSRVKMEeslqemaqaaeqasQSKSMFLATVSHELRTPLYGIIGNLDLL-----QTKEL-PKGVDrlVTamNN 513
Cdd:NF033092 356 IAVLHDVTEQEKIE--------------QERREFVANVSHELRTPLTTMRSYLEALadgawKDPELaPRFLG--VT--QN 417
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 514 SSSLLLKIISDILDFSKIESE--QLKIEPREFSprEVMNHI---------TANYlpLVVRKqlglycFIEPDVPVALngD 582
Cdd:NF033092 418 ETERMIRLVNDLLQLSRMDSKdyKLNKEWVNFN--EFFNYIidrfemilkNKNI--TFKRE------FPKRDLWVEI--D 485
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 583 PMRLQQVISNLLSNAIKFT-DTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAIC 661
Cdd:NF033092 486 TDKITQVLDNIISNAIKYSpEGGTITFRLLETHNRIIISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIA 565
                        250       260
                 ....*....|....*....|....*....
gi 145698285 662 EKLISMMDGDISVDSEPGMGSQFTVRIPL 690
Cdd:NF033092 566 KEVVEAHGGRIWAESEEGKGTTIYFTLPY 594
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
451-689 1.17e-28

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 120.70  E-value: 1.17e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 451 KMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQtkelpKGVDRL----VTAMNNSSSLLLKIISDIL 526
Cdd:NF012163 221 KLAQDFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRAELEAIQ-----DGIRKFtpesLDSLQAEVGTLTKLVDDLH 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 527 DFSKIESEQLKIEPREFSPREVMNHITANYLPLVVRKQLGLYcFIEPDVPVALnGDPMRLQQVISNLLSNAIKFTDT-GC 605
Cdd:NF012163 296 DLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELE-VSLPDSSLVF-GDRDRLMQLFNNLLENSLRYTDSgGS 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 606 IVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFT 685
Cdd:NF012163 374 LHISASQRPKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIV 453

                 ....
gi 145698285 686 VRIP 689
Cdd:NF012163 454 VTLP 457
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
451-689 2.97e-28

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 120.13  E-value: 2.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 451 KMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLL--QTKELPKGVDRLVTAMNNSSSLLLKIISDILDF 528
Cdd:NF040691 252 QMADSLQRQIRQLEELSRLQQRFVSDVSHELRTPLTTIRMAADVIhdSRDDFDPATARSAELLHTELDRFESLLSDLLEI 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 529 SKIESEQLKIEPREFSPREVMNHITANYLPLVVRKQLGLYcFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIVL 608
Cdd:NF040691 332 SRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELR-VDAPGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVV 410
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 609 HVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRI 688
Cdd:NF040691 411 TVAQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTL 490

                 .
gi 145698285 689 P 689
Cdd:NF040691 491 P 491
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
459-690 6.84e-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: 6.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 459 MAQAAEQASQSKSMFLATVSHELRTP-------LYGIIGNL---DLLQTKELPKGVDRLvtamnnssSLLlkiISDILDF 528
Cdd:NF012226 127 MAQKLESSVKNAQVWNAAIAHELRTPitilqgrLQGILDGVfepDPALFKSLLNQVEGL--------SHL---VEDLRTL 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 529 SKIESEQLKIEPREFSPREVMNHITANYLPLVVRKQLglycFIEPDVPVAL-NGDPMRLQQVISNLLSNAIKFTDTGCIV 607
Cdd:NF012226 196 SLVENQQLRLNYESVDLKDSIEKVLKMFEDRLEQAQL----TIVLNLTATPvFCDRRRIEQVLIALIDNAIRYANAGKLK 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 608 LHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLISMMDGDISVdSEPGMGSQFTVR 687
Cdd:NF012226 272 ISSSVIQDDWILQIEDEGPGIAEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEY-SNSQGNSVFTIK 350

                 ...
gi 145698285 688 IPL 690
Cdd:NF012226 351 LPA 353
 
Name Accession Description Interval E-value
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
24-947 0e+00

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 1973.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  24 VLWLLIAFSSVFYIVNALHQRESEIRQEFNLSSDQAQRFIQRTSDVMKELKYIAENRLSAENGVLSPRGRETQADVPAFE 103
Cdd:PRK10841   1 MLWLLGALLSVFYIVNALHERESEIRQEFNLSSDQAQRYIRHTSDVMRELKYIAENRLSAENGVLSPRGRETKTDVPAFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 104 PLFADSDCSAMSNTWRGSLESLAWFMRYWRDNFSAAYDLNRVFLIGSDNLCMANFGLRDMPVERDTALKALHERINKYRN 183
Cdd:PRK10841  81 PLFADSDCSAMSNTWRGSLESLAWFMRYWRDNFSAAYDLNRVFLIGSDNLCMANFGLRNMPVERDTALKALHERINKYRN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 184 APQDDSGSNLYWISEGPRPGVGYFYALTPVYLANRLQALLGVEQTIRMENFFLPGTLPMGVTILDENGHTLISLTGPESK 263
Cdd:PRK10841 161 APQQDKGSNLYWISPGARPGVGYFYALTPVYLANRLQALLGIEQTIRLENFFTPGTLPMGVTLLDENGHPLLSLTGPESK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 264 IKGDPRWMQERSWFGYTEGFRELVLKKNLPPSSLSIVYSVPVDKVLERIRMLILNAILLNVLAGAALFTLARMYERRIFI 343
Cdd:PRK10841 241 IKADPRWPQERSWFGYTDGFRELVLKKNLPPSSLSIVYSVPVDKVLERIRMLILNAILLNVLSAIVLFTLARLFERRIFI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 344 PAESDALRLEEHEQFNRKIVASAPVGICILRTADGVNILSNELAHTYLNMLTHEDRQRLTQIICGQQVNFVDVLTSNNTN 423
Cdd:PRK10841 321 PAESNALRLEEHEQFNRKIVASAPVGICILRTSDGTNILSNELAHNYLNMLTHEDRQRLTQIICGQQVNFVDVLTSNNTN 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 424 LQISFVHSRYRNENVAICVLVDVSSRVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKG 503
Cdd:PRK10841 401 LQISFVHSRYRNENVAICVLVDVSARVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKG 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 504 VDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEPREFSPREVMNHITANYLPLVVRKQLGLYCFIEPDVPVALNGDP 583
Cdd:PRK10841 481 VDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEPREFSPREVINHITANYLPLVVKKRLGLYCFIEPDVPVALNGDP 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 584 MRLQQVISNLLSNAIKFTDTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEK 663
Cdd:PRK10841 561 MRLQQVISNLLSNAIKFTDTGCIVLHVRVDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEK 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 664 LISMMDGDISVDSEPGMGSQFTVRIPLYGAQYPQKKGVEGLSGKRCWLAVRNASLCQFLETSLQRSGIVVTTYEGQEPTP 743
Cdd:PRK10841 641 LINMMDGDISVDSEPGMGSQFTIRIPLYGAQYPQKKGVEGLQGKRCWLAVRNASLEQFLETLLQRSGIQVQRYEGQEPTP 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 744 EDVLITDEVVSKKWQGRAVVTFCRRHIGIPLEKAPGEWVHSVAAPHELPALLARIYLIEMESDDPANALPSTDKAVSDND 823
Cdd:PRK10841 721 EDVLITDDPVQKKWQGRAVITFCRRHIGIPLEIAPGEWVHSTATPHELPALLARIYRIELESDDSANALPSTDKAVSDND 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 824 DMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVT 903
Cdd:PRK10841 801 DMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVT 880
                        890       900       910       920
                 ....*....|....*....|....*....|....*....|....
gi 145698285 904 ANALAEEKQRCLESGMDSCLSKPVTLDVIKQTLTLYAERVRKSR 947
Cdd:PRK10841 881 ANALAEEKQRCLEAGMDSCLSKPVTLDVLKQTLTVYAERVRKSR 924
PRK15347 PRK15347
two component system sensor kinase;
177-941 1.22e-88

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 303.10  E-value: 1.22e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 177 RINKYRNAPQDDSGSNLYWISEGPRPGVGYFYAltpVYLANRLQALLGVeqTIRMENFFLPGTLPMGVTI---LDENGHT 253
Cdd:PRK15347 155 RPLELKQLPLQPTHNGIYWGKPEYIPGGGWHVS---VAVADKQGVLVGF--TVKLNDLISYNHPVLDDDInlwLDQNGEL 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 254 LISLTGPES-----KIKGDPRWMQERSWFGYTEGFreLVLKKNLPPSSLSIVYSVPVDKVLERIRMLILN----AILLNV 324
Cdd:PRK15347 230 LPFSTIPLSsnqlqKILNQLENVKLHDGWQQIPDY--LVLRTQLKGPGWQQVTLYPRRNLANEALKPALQqlpfALLILV 307
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 325 LAGAALFTLARMYERRifipaesdalrleeheqfnrkivasaPVGicilrtaDGVNILSNELAHTYLNMLTHEDRQRLTQ 404
Cdd:PRK15347 308 LLTSVLFLLLRRYLAK--------------------------PLW-------RFVDIINKTGPAALEPRLPENRLDELGS 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 405 IicGQQVN-FVDVLTSNNTNLQiSFVHSRYRnenvaicvlvdvssrvkmeeSLQEMAQAAEQASQSKSMFLATVSHELRT 483
Cdd:PRK15347 355 I--AKAYNqLLDTLNEQYDTLE-NKVAERTQ--------------------ALAEAKQRAEQANKRKSEHLTTISHEIRT 411
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 484 PLYGIIGNLDLLQTKEL-PKGVDRLVTAMNNSSSLLlKIISDILDFSKIESEQLKIEPREFSPREVMNHITANYLPLVVR 562
Cdd:PRK15347 412 PLNGVLGALELLQNTPLtAEQMDLADTARQCTLSLL-AIINNLLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQS 490
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 563 KQLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQ 642
Cdd:PRK15347 491 KSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGGIRLRVKRHEQQLCFTVEDTGCGIDIQQQQQIFTPFYQ 570
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 643 VGTgvqrNFQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIPLYGAQYPQKkgvegLSGKrcwLAvrnASLCqfL 722
Cdd:PRK15347 571 ADT----HSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPLNEYAPPEP-----LKGE---LS---APLA--L 633
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 723 ETSLQRSGIvvttyEGQEPTPEDVLITDEvvskkwqgravvtfcrrhigipLEKAPGE-WVHSVAAPHELPAllariyli 801
Cdd:PRK15347 634 HRQLSAWGI-----TCQPGHQNPALLDPE----------------------LAYLPGRlYDLLQQIIQGAPN-------- 678
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 802 emESDDPANALPSTdkavsdnddMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALnVLSKNHI-DIVLSDVNMPN 880
Cdd:PRK15347 679 --EPVINLPLQPWQ---------LQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEAL-ELGRQHRfDLVLMDIRMPG 746
                        730       740       750       760       770       780
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145698285 881 MDGYRLTQRIRQ----LGLTLPVIGVTANALAEEKQRCLESGMDSCLSKPVTLDVIKQTLTLYAE 941
Cdd:PRK15347 747 LDGLETTQLWRDdpnnLDPDCMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARALELAAE 811
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
463-942 1.06e-83

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 289.44  E-value: 1.06e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 463 AEQASQSKSMFLATVSHELRTPLYGIIG-NLDLLQTKELPKGVDRLVT---AMNNssslLLKIISDILDFSKIESEQLKI 538
Cdd:PRK11107 286 AQEAARIKSEFLANMSHELRTPLNGVIGfTRQTLKTPLTPTQRDYLQTierSANN----LLAIINDILDFSKLEAGKLVL 361
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 539 EPREFSPREVMNHiTANYL-PLVVRKQLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHV--RA-DG 614
Cdd:PRK11107 362 ENIPFSLRETLDE-VVTLLaHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVelRAlSN 440
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 615 DYLSIR--VRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIPLYG 692
Cdd:PRK11107 441 TKVQLEvqIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDL 520
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 693 AQYPQKKG--VEGLSGKRCWLAVRNASLCQFLETSLQRSGIVVTTYEGQEPTPED----VLI-------TDEVVSKKWqg 759
Cdd:PRK11107 521 NPNPIIDGlpTDCLAGKRLLYVEPNSAAAQATLDILSETPLEVTYSPTLSQLPEAhydiLLLglpvtfrEPLTMLHER-- 598
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 760 raVVTFCRR----HIGIP--------LEKAPGewVHS-----VAAPHELPALLA--RIYLIEMESDDPANALPstdkavs 820
Cdd:PRK11107 599 --LAKAKSMtdflILALPcheqvlaeQLKQDG--ADAclskpLSHTRLLPALLEpcHHKQPPLLPPTDESRLP------- 667
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 821 dnddMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGL--TLP 898
Cdd:PRK11107 668 ----LTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHnqNTP 743
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 145698285 899 VIGVTANALAEEKQRCLESGMDSCLSKPVTLDVIKQTLTLYAER 942
Cdd:PRK11107 744 IIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKPG 787
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
461-936 3.82e-77

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: 272.04  E-value: 3.82e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  461 QAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEP 540
Cdd:TIGR02956 455 AEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISP 534
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  541 REFSPREVMNHITANYLPLVVRKQLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHVRADGD-YLSI 619
Cdd:TIGR02956 535 RPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDsSLLF 614
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  620 RVRDTGVGIPAKEVVRLFDPFFQVgTGvQRNFQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIPLygaqyPQKK 699
Cdd:TIGR02956 615 EVEDTGCGIAEEEQATLFDAFTQA-DG-RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPL-----TRGK 687
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  700 GVEGLSGkrcwlavrnaslcqfletslqrsgivvttyegqeptpedvlitdevvskkwqgravvtfcRRHIGIPlekapg 779
Cdd:TIGR02956 688 PAEDSAT------------------------------------------------------------LTVIDLP------ 701
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  780 ewvhsvaaphelpallariyliemesddPANalpstdkavsdnddmmILVVDDHPINRRLLADQLGSLGYQCKTANDGVD 859
Cdd:TIGR02956 702 ----------------------------PQR----------------VLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQS 737
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  860 ALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQL---GLTLPVIGVTANALAEEKQRCLESGMDSCLSKPVTLDVIKQTL 936
Cdd:TIGR02956 738 ALECFHQHAFDLALLDINLPDGDGVTLLQQLRAIygaKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMI 817
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
372-690 5.88e-77

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 254.45  E-value: 5.88e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 372 ILRTADGVNILSNELAHTYLNMLTHEDRQRLTQIICGQQVNFVDVLTSNNTNLQISFVHSRYRNENVAICVLVDVSSRVK 451
Cdd:COG0642   12 LLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 452 MEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQtKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKI 531
Cdd:COG0642   92 LLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLL-EELDEEQREYLETILRSADRLLRLINDLLDLSRL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 532 ESEQLKIEPREFSPREVMNHITANYLPLVVRKQLGLYCFIEPDVPVaLNGDPMRLQQVISNLLSNAIKFTDTG-CIVLHV 610
Cdd:COG0642  171 EAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPT-VRGDPDRLRQVLLNLLSNAIKYTPEGgTVTVSV 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 611 RADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGvqRNFQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIPL 690
Cdd:COG0642  250 RREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLPL 327
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
456-690 2.93e-72

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 238.27  E-value: 2.93e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 456 LQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKE--LPKGVDRLVTAMNNSSSLLLKIISDILDFSKIES 533
Cdd:COG2205    2 LEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEdlSPEERRELLEIIRESAERLLRLIEDLLDLSRLES 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 534 EQLKIEPREFSPREVMNHITANYLPLVVRKQLGLYCFIEPDVPVaLNGDPMRLQQVISNLLSNAIKFTDTGC-IVLHVRA 612
Cdd:COG2205   82 GKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPL-VYADPELLEQVLANLLDNAIKYSPPGGtITISARR 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145698285 613 DGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTgvQRNFQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIPL 690
Cdd:COG2205  161 EGDGVRISVSDNGPGIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPL 236
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
310-690 3.33e-70

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 238.30  E-value: 3.33e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 310 ERIRMLILNAILLNVLAGAALFTLARMYERRIFIPAESDALRLEEHEQFNRKIVASAPVGICILRTADGVNILSNELAHT 389
Cdd:COG5002    1 LLLLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 390 YLNMLTHEDRQRLTQIICGQQVNFVDVLTSNNTNLQISFVHSRYRNENVAICVLVDVSSRVKMEESLQEMAQ----AAEQ 465
Cdd:COG5002   81 LALLLLALLLLLLLLLLLLALLILLLLLALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVErditELER 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 466 ASQSKSMFLATVSHELRTPLYGIIGNLDLLQT--KELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEPREF 543
Cdd:COG5002  161 LEQMRREFVANVSHELRTPLTSIRGYLELLLDgaADDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 544 SPREVMNHITANYLPLVVRKQLGLYCFIEPDvPVALNGDPMRLQQVISNLLSNAIKFTDTG-CIVLHVRADGDYLSIRVR 622
Cdd:COG5002  241 DLAELLEEVVEELRPLAEEKGIELELDLPED-PLLVLGDPDRLEQVLTNLLDNAIKYTPEGgTITVSLREEDDQVRISVR 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145698285 623 DTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIPL 690
Cdd:COG5002  320 DTGIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPL 387
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
438-937 1.85e-60

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 225.00  E-value: 1.85e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  438 VAICVLVDVSSRVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKG--VDRLVTAMNNSS 515
Cdd:PRK09959  680 VYICGWQDITETRDLIHALEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEqrVEAISLAYATGQ 759
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  516 SLLlKIISDILDFSKIESEQLKIEPREFSPREVMNHITANYLPLVVRKQLGLYCFIEPDVPVALNGDPMRLQQVISNLLS 595
Cdd:PRK09959  760 SLL-GLIGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLS 838
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  596 NAIKFTDTGCI-----VLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNfqGTGLGLAICEKLISMMDG 670
Cdd:PRK09959  839 NALKFTTEGAVkittsLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQT--GSGLGLMICKELIKNMQG 916
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  671 DISVDSEPGMGSQFTVRIPLygaqypqkkgveglsgkrcwlavrnaslcqfletslqrsgivvttyegqeptpedvlitd 750
Cdd:PRK09959  917 DLSLESHPGIGTTFTITIPV------------------------------------------------------------ 936
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  751 evvskkwqgravvtfcrrhigiplekapgEWVHSVAAphelpallariylIEMESDDPAnALPstdkavsdnDDMMILVV 830
Cdd:PRK09959  937 -----------------------------EISQQVAT-------------VEAKAEQPI-TLP---------EKLSILIA 964
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  831 DDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANALAEE 910
Cdd:PRK09959  965 DDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANAQANE 1044
                         490       500
                  ....*....|....*....|....*..
gi 145698285  911 KQRCLESGMDSCLSKPVTLDVIKQTLT 937
Cdd:PRK09959 1045 REKGLSCGMNLCLFKPLTLDVLKTHLS 1071
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
445-934 1.60e-52

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 197.47  E-value: 1.60e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 445 DVSSRVKMEESLqemaqaaEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISD 524
Cdd:PRK11091 265 DITERKRYQDAL-------EKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFND 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 525 ILDFSKIESEQLKIEPREFSPREVMNHITaNYLPLVVrKQLGLYCFIEP--DVPVALNGDPMRLQQVISNLLSNAIKFTD 602
Cdd:PRK11091 338 IIDMDKMERRKLQLDNQPIDFTDFLADLE-NLSGLQA-EQKGLRFDLEPllPLPHKVITDGTRLRQILWNLISNAVKFTQ 415
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 603 TGCIVLHVRAD-GDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQ-GTGLGLAICEKLISMMDGDISVDSEPGM 680
Cdd:PRK11091 416 QGGVTVRVRYEeGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHGGKPAtGTGIGLAVSKRLAQAMGGDITVTSEEGK 495
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 681 GSQFTVRIPLygaqypqkkgveglsgkrcwlavrnaslcqfletslqrsgIVVTTYEGQEPTPEDVlitdevvskkwqgr 760
Cdd:PRK11091 496 GSCFTLTIHA----------------------------------------PAVAEEVEDAFDEDDM-------------- 521
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 761 avvtfcrrhigiplekapgewvhsvaaphELPALlariyliemesddpanalpstdkavsdnddmMILVVDDHPINRRLL 840
Cdd:PRK11091 522 -----------------------------PLPAL-------------------------------NILLVEDIELNVIVA 541
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 841 ADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQ--LGLTL-PVIGVTANALAEEKQRcLES 917
Cdd:PRK11091 542 RSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELREryPREDLpPLVALTANVLKDKKEY-LDA 620
                        490       500
                 ....*....|....*....|.
gi 145698285 918 GMDSCLSKPVTL----DVIKQ 934
Cdd:PRK11091 621 GMDDVLSKPLSVpaltAMIKK 641
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
445-750 2.37e-50

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 192.43  E-value: 2.37e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 445 DVSSRVKMEES-LQEMA----QA---AEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSS 516
Cdd:PRK11466 411 QLAAQVKARTAeLQELViehrQAraeAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGE 490
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 517 LLLKIISDILDFSKIE--SEQLKIEPREFSPREVMNHITANYLPLVVRKQLGLYCFIEPDVPVALNGDPMRLQQVISNLL 594
Cdd:PRK11466 491 SLLTILNDILDYSAIEagGKNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLL 570
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 595 SNAIKFTDTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTgvQRNfqGTGLGLAICEKLISMMDGDISV 674
Cdd:PRK11466 571 SNALRFTDEGSIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFVQVSG--KRG--GTGLGLTISSRLAQAMGGELSA 646
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 675 DSEPGMGSQFTVRIPLYGAQYPQKKGVE---GLSGKRCWLAVRNASLCQFLETSLQRSGIVVTTYEG--------QEPTP 743
Cdd:PRK11466 647 TSTPEVGSCFCLRLPLRVATAPVPKTVNqavRLDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNaaqaletlQNSEP 726

                 ....*..
gi 145698285 744 EDVLITD 750
Cdd:PRK11466 727 FAAALVD 733
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
586-690 5.48e-50

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: 171.52  E-value: 5.48e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 586 LQQVISNLLSNAIKFTDTGCIVLHVRADGD-----YLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAI 660
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEeedgvQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 145698285 661 CEKLISMMDGDISVDSEPGMGSQFTVRIPL 690
Cdd:cd16922   81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
305-689 2.45e-47

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 177.28  E-value: 2.45e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 305 VDKVLERIRMLILNAILLNVLAGAALFTLARMYERRIFIPAESDALRLEEHEQFNRKIVASAPVGICILRTADGVNILSN 384
Cdd:COG4251  128 LLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLL 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 385 ELAHTYLNMLTHEDRQRLTQIICGQQVNFVDVLTSNNTNLQISFVHSRYRNENVAicvlvdvssrvKMEESLQEMAQAAE 464
Cdd:COG4251  208 ELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRLELE-----------ELEEELEERTAELE 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 465 QASQSKSMFLATVSHELRTPLYGIIGNLDLLQTK---ELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEPr 541
Cdd:COG4251  277 RSNEELEQFAYVASHDLREPLRKISGFSQLLEEDygdKLDEEGREYLERIRDAAERMQALIDDLLAYSRVGRQELEFEP- 355
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 542 eFSPREVMNHITANYLPLVVRKQlglYCFIEPDVPVaLNGDPMRLQQVISNLLSNAIKFTD---TGCIVLHVRADGDYLS 618
Cdd:COG4251  356 -VDLNELLEEVLEDLEPRIEERG---AEIEVGPLPT-VRGDPTLLRQVFQNLISNAIKYSRpgePPRIEIGAEREGGEWV 430
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145698285 619 IRVRDTGVGIPAKEVVRLFDPFFQVGTgvQRNFQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIP 689
Cdd:COG4251  431 FSVRDNGIGIDPEYAEKIFEIFQRLHS--RDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLP 499
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
314-697 2.67e-47

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: 176.70  E-value: 2.67e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 314 MLILNAILLNVLAGAALFTLARMYERRIFIPAEsdalrLEEHEQFNRKIVASAPVGICILrTADGVNILSNELA------ 387
Cdd:COG5809  103 SSKLSPIFDQNGDIEGMLAISRDITERKRMEEA-----LRESEEKFRLIFNHSPDGIIVT-DLDGRIIYANPAAckllgi 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 388 -------HTYLNMLTHEDRQRLTQIIC-----GQQVNF-VDVLTSNNTNLQISF---VHSRYRNENVAICVLVDVSSRVK 451
Cdd:COG5809  177 sieeligKSILELIHSDDQENVAAFISqllkdGGIAQGeVRFWTKDGRWRLLEAsgaPIKKNGEVDGIVIIFRDITERKK 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 452 MEESLQemaqaaeqASQSKSM---FLATVSHELRTPLYGIIGNLDLLQ--------------TKELpkgvDRlvtaMNNs 514
Cdd:COG5809  257 LEELLR--------KSEKLSVvgeLAAGIAHEIRNPLTSLKGFIQLLKdtideeqktyldimLSEL----DR----IES- 319
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 515 sslllkIISDILDFSKIESeqlkIEPREFSPREVMNHITANYLPLVVRKQLGLYCFIEPDVPVALnGDPMRLQQVISNLL 594
Cdd:COG5809  320 ------IISEFLVLAKPQA----IKYEPKDLNTLIEEVIPLLQPQALLKNVQIELELEDDIPDIL-GDENQLKQVFINLL 388
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 595 SNAIKFTDT-GCIVLHVRA-DGDYLSIRVRDTGVGIPAKEVVRLFDPFFQvgtgvqRNFQGTGLGLAICEKLISMMDGDI 672
Cdd:COG5809  389 KNAIEAMPEgGNITIETKAeDDDKVVISVTDEGCGIPEERLKKLGEPFYT------TKEKGTGLGLMVSYKIIEEHGGKI 462
                        410       420
                 ....*....|....*....|....*
gi 145698285 673 SVDSEPGMGSQFTVRIPLYGAQYPQ 697
Cdd:COG5809  463 TVESEVGKGTTFSITLPIKLSEQVS 487
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
827-936 2.00e-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: 161.48  E-value: 2.00e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGL---TLPVIGVT 903
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGggrRTPIIALT 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 145698285 904 ANALAEEKQRCLESGMDSCLSKPVTLDVIKQTL 936
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
RcsC pfam09456
RcsC Alpha-Beta-Loop (ABL); This domain is found in the C-terminus of the phospho-relay kinase ...
709-799 1.17e-45

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: 158.62  E-value: 1.17e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  709 CWLAVRNASLCQFLETSLQRSGIVVTTYEGQEPTPEDVLITDEVVSKKWQGRAVVTFCRRHIGIPLEKAPGEWVHSVAAP 788
Cdd:pfam09456   1 CWLDIRNASLEEYLLRLLQQSGLTVTRYEGQEPDADDVLISDYPLAIAWPVRAYIEFSRRHIGSPQETRPGYWLHSTATL 80
                          90
                  ....*....|.
gi 145698285  789 HELPALLARIY 799
Cdd:pfam09456  81 HELPALLERIY 91
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
351-691 6.46e-45

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 166.18  E-value: 6.46e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 351 RLEEHEQFNRKIVASAPVGICILrTADG----VN--------ILSNELAHTYLNMLTHED---RQRLTQIICGQQVNF-- 413
Cdd:COG3852    1 ALRESEELLRAILDSLPDAVIVL-DADGrityVNpaaerllgLSAEELLGRPLAELFPEDsplRELLERALAEGQPVTer 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 414 -VDVLTSNNTNLQISFVHSRYRNENVAICVLV---DVSSRVKMEESLQEMAQAAeqasqSKSMFLATVSHELRTPLYGII 489
Cdd:COG3852   80 eVTLRRKDGEERPVDVSVSPLRDAEGEGGVLLvlrDITERKRLERELRRAEKLA-----AVGELAAGLAHEIRNPLTGIR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 490 GNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKieseQLKIEPREFSPREVMNHItanyLPLV---VRKQLG 566
Cdd:COG3852  155 GAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSR----PRPPEREPVNLHEVLERV----LELLraeAPKNIR 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 567 LYCFIEPDVPvALNGDPMRLQQVISNLLSNAIK-FTDTGCIVLHVRAD----------GDYLSIRVRDTGVGIPAKEVVR 635
Cdd:COG3852  227 IVRDYDPSLP-EVLGDPDQLIQVLLNLVRNAAEaMPEGGTITIRTRVErqvtlgglrpRLYVRIEVIDNGPGIPEEILDR 305
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 145698285 636 LFDPFFqvgTGvqrNFQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIPLY 691
Cdd:COG3852  306 IFEPFF---TT---KEKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLE 355
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
351-690 8.12e-45

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: 167.45  E-value: 8.12e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 351 RLEEHEQFNRKIVASAPVGICILrTADGVNILSNELAHTYLNMLTHEDRQRLTQIICGQQ--VNFVDVLTSNNTNLQISF 428
Cdd:COG5000   84 ELEERRRYLETILENLPAGVIVL-DADGRITLANPAAERLLGIPLEELIGKPLEELLPELdlAELLREALERGWQEEIEL 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 429 VHSRYRNENVAICVLVDvSSRVKMEESLQEMAQAAEQASQSKsmFLATVSHELRTPLYGIIGNLDLLQTKELPKG----- 503
Cdd:COG5000  163 TRDGRRTLLVRASPLRD-DGYVIVFDDITELLRAERLAAWGE--LARRIAHEIKNPLTPIQLSAERLRRKLADKLeedre 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 504 -VDRLVTAMNNSSSLLLKIISDILDFSKIEseqlKIEPREFSPREVMNHITANYLPLVVRKQLGLYCFIEPDVPVaLNGD 582
Cdd:COG5000  240 dLERALDTIIRQVDRLKRIVDEFLDFARLP----EPQLEPVDLNELLREVLALYEPALKEKDIRLELDLDPDLPE-VLAD 314
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 583 PMRLQQVISNLLSNAIKFT-DTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFqvgTGVQrnfQGTGLGLAIC 661
Cdd:COG5000  315 RDQLEQVLINLLKNAIEAIeEGGEIEVSTRREDGRVRIEVSDNGPGIPEEVLERIFEPFF---TTKP---KGTGLGLAIV 388
                        330       340
                 ....*....|....*....|....*....
gi 145698285 662 EKLISMMDGDISVDSEPGMGSQFTVRIPL 690
Cdd:COG5000  389 KKIVEEHGGTIELESRPGGGTTFTIRLPL 417
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
326-690 1.70e-43

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 161.89  E-value: 1.70e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 326 AGAALFTLARMYERRIFIPAESDALRLEEHEQFNRKIVASAPVGICILRTADGVNILSNELAHTYLNMLTHEDRQRLTQI 405
Cdd:COG4191    2 LRLLLLLLLLLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 406 icgqqvnFVDVLTSNNTNLQISFVHSRYRNENVAICVLV-DVSSRVKMEESLQEMAQAAEQASQSKSM--FLATVSHELR 482
Cdd:COG4191   82 -------LGLLLLLLLEALLLLLLAALDAEENAELEELErDITELERAEEELRELQEQLVQSEKLAALgeLAAGIAHEIN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 483 TPLYGIIGNLDLLQTK--------ELPKGVDRLVTAMNNSSslllKIISDILDFSKIESEqlkiEPREFSPREVMN---H 551
Cdd:COG4191  155 NPLAAILGNAELLRRRledepdpeELREALERILEGAERAA----EIVRSLRAFSRRDEE----EREPVDLNELIDealE 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 552 ITANYLP---LVVRKQLGlycfiePDVPvALNGDPMRLQQVISNLLSNAI---KFTDTGCIVLHVRADGDYLSIRVRDTG 625
Cdd:COG4191  227 LLRPRLKargIEVELDLP------PDLP-PVLGDPGQLEQVLLNLLINAIdamEEGEGGRITISTRREGDYVVISVRDNG 299
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145698285 626 VGIPAKEVVRLFDPFF---QVGtgvqrnfQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIPL 690
Cdd:COG4191  300 PGIPPEVLERIFEPFFttkPVG-------KGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLPL 360
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
827-945 3.44e-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: 150.00  E-value: 3.44e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQL--GLTLPVIGVTA 904
Cdd:COG0784    8 ILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALprLPDIPIIALTA 87
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 145698285 905 NALAEEKQRCLESGMDSCLSKPVTLDVIKQTLTLYAERVRK 945
Cdd:COG0784   88 YADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
352-688 4.41e-41

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: 154.29  E-value: 4.41e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  352 LEEHEQFnRKIVASAPVGICILRTADGVnILSNELAHTYLNMLTHED-RQRLTQIIcgQQVNFVDVLTS----------- 419
Cdd:TIGR02966   2 SALLSRF-RAAAQALPDAVVVLDEEGQI-EWCNPAAERLLGLRWPDDlGQRITNLI--RHPEFVEYLAAgrfseplelps 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  420 -NNTNLQISFVHSRYrNENVAICVLVDVSSrvkmeeslqemaqaAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQ-- 496
Cdd:TIGR02966  78 pINSERVLEIRIAPY-GEEQKLLVARDVTR--------------LRRLEQMRRDFVANVSHELRTPLTVLRGYLETLAdg 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  497 TKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEPREFSPREVMNHITANYLPLVVRKQLGLYcfIEPDVP 576
Cdd:TIGR02966 143 PDEDPEEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALLDHLRDEAEALSQGKNHQIT--FEIDGG 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  577 VALNGDPMRLQQVISNLLSNAIKFT-DTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTG 655
Cdd:TIGR02966 221 VDVLGDEDELRSAFSNLVSNAIKYTpEGGTITVRWRRDGGGAEFSVTDTGIGIAPEHLPRLTERFYRVDKSRSRDTGGTG 300
                         330       340       350
                  ....*....|....*....|....*....|...
gi 145698285  656 LGLAICEKLISMMDGDISVDSEPGMGSQFTVRI 688
Cdd:TIGR02966 301 LGLAIVKHVLSRHHARLEIESELGKGSTFSFIF 333
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
581-690 2.44e-40

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 144.33  E-value: 2.44e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285   581 GDPMRLQQVISNLLSNAIKFTDT-GCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVqRNFQGTGLGLA 659
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEgGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRS-RKIGGTGLGLS 79
                           90       100       110
                   ....*....|....*....|....*....|.
gi 145698285   660 ICEKLISMMDGDISVDSEPGMGSQFTVRIPL 690
Cdd:smart00387  80 IVKKLVELHGGEISVESEPGGGTTFTITLPL 110
KinD COG5808
Sporulation sensor histidine kinase D [Cell cycle control, cell division, chromosome ...
453-690 3.40e-39

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: 151.83  E-value: 3.40e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 453 EESLQEMAQAA--EQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSK 530
Cdd:COG5808  222 RKTLLERVIQEinTQKLELIGTFAASTAHEIRNPLTSIKGFIQLLQEKYPELEDQKYFDIIQEEIQRINQIVSEFLVLGK 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 531 IESEQLKIEprefSPREVMNHITANYLPLVVRKQLGLYcFIEPDVPVALNGDPMRLQQVISNLLSNAIKFT-DTGCIVLH 609
Cdd:COG5808  302 PTAKKLELD----DLNELIEEILSIIDSEANLKNIRVE-KQSLDEPLHIKCDKDRIKQVLLNLIKNAIEAMkEGGKLTIS 376
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 610 VRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGvqrnfqGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIP 689
Cdd:COG5808  377 IENDDEKAVIEVIDNGEGIPEDIIDEIFEPFVTTKEG------GTGLGLSVCKRIVEMHGGEIDIESEEGKGTTFTIRLP 450

                 .
gi 145698285 690 L 690
Cdd:COG5808  451 L 451
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
581-690 1.14e-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: 127.87  E-value: 1.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  581 GDPMRLQQVISNLLSNAIKFT-DTGCIVLHVRaDGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTgvqRNFQGTGLGLA 659
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAaKAGEITVTLS-EGGELTLTVEDNGIGIPPEDLPRIFEPFSTADK---RGGGGTGLGLS 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 145698285  660 ICEKLISMMDGDISVDSEPGMGSQFTVRIPL 690
Cdd:pfam02518  77 IVRKLVELLGGTITVESEPGGGTTVTLTLPL 107
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
827-940 1.24e-34

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: 130.41  E-value: 1.24e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT--LPVIGVTA 904
Cdd:COG3706    4 ILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTadIPIIFLTA 83
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 145698285 905 NALAEEKQRCLESGMDSCLSKPVTLDVIKQTLTLYA 940
Cdd:COG3706   84 LDDEEDRARALEAGADDYLTKPFDPEELLARVDLVA 119
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
827-936 1.29e-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: 124.96  E-value: 1.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANA 906
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 145698285  907 LAEEKQRCLESGMDSCLSKPVTLDVIKQTL 936
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAI 110
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
827-947 7.07e-32

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: 123.53  E-value: 7.07e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANA 906
Cdd:COG0745    4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTARD 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 145698285 907 LAEEKQRCLESGMDSCLSKPVTLDVIKQTLTLYAERVRKSR 947
Cdd:COG0745   84 DEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAAEV 124
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
291-690 7.44e-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: 7.44e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 291 NLPPSSLSIVYSVP-----VDKVLERIRMLILNAILLnVLAGAALFTLARMYERrifiPAESDALRLEEHEQFNRKIVAS 365
Cdd:PRK10618 277 ALNSTPLKLVYQVPlgtllLDLLQNNLWPLLLNLGLL-ALSLFGYYTFRHQYGR----PTESMSHELRILRALNEEIVSN 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 366 APVGICILRTADGVNILSNELAHtylNMLTHEDRQRLTQIicGQQVNFVDVLTSNNTNLQISFVHSRYRNEnVAICVLVD 445
Cdd:PRK10618 352 LPLGLLVYDFESNRTVISNKIAD---HLLPHLNLQKITTM--AEQHQGVIQATINNELYEIRMFRSQLAPR-TQLFLLRD 425
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 446 VSSRVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDI 525
Cdd:PRK10618 426 QDREVLVNKKLQQAQREYEKNQQARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNI 505
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 526 LDFSKIESEQLKIEPREFSPREVMNHITANYLPLVVRKQLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGC 605
Cdd:PRK10618 506 QLLNMLETQDWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYGK 585
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 606 IVLHVRADGDY---LSIRVRDTGVGIPAKEVVRLFDPFFQVGTGvQRNFQGTGLGLAICEKLISMMDGDISVDSEPGMGS 682
Cdd:PRK10618 586 ITLEVDQDESSpdrLTIRILDTGAGVSIKELDNLHFPFLNQTQG-DRYGKASGLTFFLCNQLCRKLGGHLTIKSREGLGT 664

                 ....*...
gi 145698285 683 QFTVRIPL 690
Cdd:PRK10618 665 RYSIHLKM 672
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
820-947 2.78e-31

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: 122.58  E-value: 2.78e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 820 SDNDDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT--L 897
Cdd:COG3437    2 RTGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTrdI 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 145698285 898 PVIGVTANALAEEKQRCLESGMDSCLSKPVT----LDVIKQTLTLYAERVRKSR 947
Cdd:COG3437   82 PVIFLTALADPEDRERALEAGADDYLTKPFDpeelLARVRNALELRRLQRELDD 135
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
440-690 2.94e-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: 127.18  E-value: 2.94e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 440 ICVLVDVSSRVKMEeslqemaqaaeqasQSKSMFLATVSHELRTPLYGIIGNLDLL-----QTKEL-PKGVDrlVTamNN 513
Cdd:NF033092 356 IAVLHDVTEQEKIE--------------QERREFVANVSHELRTPLTTMRSYLEALadgawKDPELaPRFLG--VT--QN 417
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 514 SSSLLLKIISDILDFSKIESE--QLKIEPREFSprEVMNHI---------TANYlpLVVRKqlglycFIEPDVPVALngD 582
Cdd:NF033092 418 ETERMIRLVNDLLQLSRMDSKdyKLNKEWVNFN--EFFNYIidrfemilkNKNI--TFKRE------FPKRDLWVEI--D 485
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 583 PMRLQQVISNLLSNAIKFT-DTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAIC 661
Cdd:NF033092 486 TDKITQVLDNIISNAIKYSpEGGTITFRLLETHNRIIISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIA 565
                        250       260
                 ....*....|....*....|....*....
gi 145698285 662 EKLISMMDGDISVDSEPGMGSQFTVRIPL 690
Cdd:NF033092 566 KEVVEAHGGRIWAESEEGKGTTIYFTLPY 594
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
828-926 4.00e-30

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: 114.63  E-value: 4.00e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 828 LVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANAL 907
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80
                         90
                 ....*....|....*....
gi 145698285 908 AEEKQRCLESGMDSCLSKP 926
Cdd:cd00156   81 EEDAVRALELGADDYLVKP 99
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
452-689 8.44e-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: 124.04  E-value: 8.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  452 MEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKelPKGVDRLVTAMnnSSSL-----LLKIISDIL 526
Cdd:TIGR01386 223 LAQSFNAMLGRLEDAFQRLSQFSADLAHELRTPLTNLLGQTQVALSQ--PRTGEEYREVL--ESNLeelerLSRMVSDML 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  527 DFSKIESEQLKIEPREFSPREVMNHITANYLPLVVRKQLGlycfIEPDVPVALNGDPMRLQQVISNLLSNAIKFT-DTGC 605
Cdd:TIGR01386 299 FLARADNGQLALERVRLDLAAELAKVAEYFEPLAEERGVR----IRVEGEGLVRGDPQMFRRAISNLLSNALRHTpDGGT 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  606 IVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLISMMDGDISVDSEPGMgSQFT 685
Cdd:TIGR01386 375 ITVRIERRSDEVRVSVSNPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAESPDGK-TRFI 453

                  ....
gi 145698285  686 VRIP 689
Cdd:TIGR01386 454 LRFP 457
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
475-691 1.40e-29

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: 122.28  E-value: 1.40e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 475 ATVSHELRTPLYGIIGNLDLLQTKELPKgvDRLVTAMnnssSLLLK-------IISDILDFSKIESEqlKIEPREFSprE 547
Cdd:COG5806  206 ASIAHEVRNPLTVVRGFIQLLQEPELSD--EKRKQYI----RIALEeldraeaIITDYLTFAKPQPE--KLEKIDVS--E 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 548 VMNHITANYLPLVVRKQLGLYCFIEPdvPVALNGDPMRLQQVISNLLSNAIK-FTDTGCIVLHVRADGDYLSIRVRDTGV 626
Cdd:COG5806  276 ELEHVIDVLSPYANMNNVEIQTELEP--GLYIEGDRQKLQQCLINIIKNGIEaMPNGGTLTIDVSIDKNKVIISIKDTGV 353
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145698285 627 GIPAKEVVRLFDPFFQVGTgvqrnfQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIPLY 691
Cdd:COG5806  354 GMTKEQLERLGEPYFSTKE------KGTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFTITLPLA 412
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
451-689 1.17e-28

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 120.70  E-value: 1.17e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 451 KMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQtkelpKGVDRL----VTAMNNSSSLLLKIISDIL 526
Cdd:NF012163 221 KLAQDFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRAELEAIQ-----DGIRKFtpesLDSLQAEVGTLTKLVDDLH 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 527 DFSKIESEQLKIEPREFSPREVMNHITANYLPLVVRKQLGLYcFIEPDVPVALnGDPMRLQQVISNLLSNAIKFTDT-GC 605
Cdd:NF012163 296 DLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELE-VSLPDSSLVF-GDRDRLMQLFNNLLENSLRYTDSgGS 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 606 IVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFT 685
Cdd:NF012163 374 LHISASQRPKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIV 453

                 ....
gi 145698285 686 VRIP 689
Cdd:NF012163 454 VTLP 457
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
451-689 2.97e-28

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 120.13  E-value: 2.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 451 KMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLL--QTKELPKGVDRLVTAMNNSSSLLLKIISDILDF 528
Cdd:NF040691 252 QMADSLQRQIRQLEELSRLQQRFVSDVSHELRTPLTTIRMAADVIhdSRDDFDPATARSAELLHTELDRFESLLSDLLEI 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 529 SKIESEQLKIEPREFSPREVMNHITANYLPLVVRKQLGLYcFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIVL 608
Cdd:NF040691 332 SRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELR-VDAPGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVV 410
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 609 HVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRI 688
Cdd:NF040691 411 TVAQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTL 490

                 .
gi 145698285 689 P 689
Cdd:NF040691 491 P 491
PRK09303 PRK09303
histidine kinase;
457-691 3.51e-28

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 117.74  E-value: 3.51e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 457 QEMAQAAEQAsQSKSMFLATVSHELRTPLYGI---IGNLDLLQTKEL----PKGVDRLVTAMNNSSSLLLKIISDILDFS 529
Cdd:PRK09303 139 QENETLLEQL-KFKDRVLAMLAHDLRTPLTAAslaLETLELGQIDEDtelkPALIEQLQDQARRQLEEIERLITDLLEVG 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 530 KIESEQLKIEPREFSPREVMNHITANYLPLVVRKQLGLYCFIEPDVPvALNGDPMRLQQVISNLLSNAIKFT-DTGCI-- 606
Cdd:PRK09303 218 RTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSDLP-SVYADQERIRQVLLNLLDNAIKYTpEGGTItl 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 607 -VLHvRADgDYLSIRVRDTGVGIPAKEVVRLFDPFFQVgtgvQRNFQ--GTGLGLAICEKLISMMDGDISVDSEPGMGSQ 683
Cdd:PRK09303 297 sMLH-RTT-QKVQVSICDTGPGIPEEEQERIFEDRVRL----PRDEGteGYGIGLSVCRRIVRVHYGQIWVDSEPGQGSC 370

                 ....*...
gi 145698285 684 FTVRIPLY 691
Cdd:PRK09303 371 FHFTLPVY 378
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
827-948 3.16e-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: 115.45  E-value: 3.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANA 906
Cdd:COG2204    5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGYG 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 145698285 907 LAEEKQRCLESGMDSCLSKPVTLDVIKQTLTLYAERVRKSRD 948
Cdd:COG2204   85 DVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRE 126
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
475-694 3.73e-27

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 116.04  E-value: 3.73e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 475 ATVSHELRTPLYGIIGNLDLLQTKELPKGVDR-LVTAMNNSSSLLLKIISDILDFSKieseqlkiePREFSPREV-MNHI 552
Cdd:PRK10364 242 AGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHqLAQVMAKEADRLNRVVSELLELVK---------PTHLALQAVdLNDL 312
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 553 TANYLPLVVR----KQLGLYCFIEPDVPvALNGDPMRLQQVISNLLSNAIKFTDT-GCIVLHVRADGDYLSIRVRDTGVG 627
Cdd:PRK10364 313 INHSLQLVSQdansREIQLRFTANDTLP-EIQADPDRLTQVLLNLYLNAIQAIGQhGVISVTASESGAGVKISVTDSGKG 391
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145698285 628 IPAKEVVRLFDPFFQVGTgvqrnfQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIPLYGAQ 694
Cdd:PRK10364 392 IAADQLEAIFTPYFTTKA------EGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLPVNITR 452
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
424-690 4.53e-27

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 117.38  E-value: 4.53e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 424 LQISFVHSRYRN--ENV--AICVLVDVSSRVKMEEslqEMAQAAEQASQSKSMflATVSHELRTPLYGIIGNLDLLQTKE 499
Cdd:PRK11360 345 IELSVSTSLLHNthGEMigALVIFSDLTERKRLQR---RVARQERLAALGELV--AGVAHEIRNPLTAIRGYVQIWRQQT 419
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 500 LPKGVDRLVTAMNNSSSLLLKIISDILDFSKieseqlkiePREFSPREVmnhitanYLPLVVRKQLGLY----------- 568
Cdd:PRK11360 420 SDPPSQEYLSVVLREVDRLNKVIDQLLEFSR---------PRESQWQPV-------SLNALVEEVLQLFqtagvqarvdf 483
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 569 -CFIEPDVPvALNGDPMRLQQVISNLLSNAIK-FTDTGCIVLHVRADGD-YLSIRVRDTGVGIPAKEVVRLFDPFFQVGT 645
Cdd:PRK11360 484 eTELDNELP-PIWADPELLKQVLLNILINAVQaISARGKIRIRTWQYSDgQVAVSIEDNGCGIDPELLKKIFDPFFTTKA 562
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 145698285 646 gvqrnfQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIPL 690
Cdd:PRK11360 563 ------KGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPI 601
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
828-926 8.67e-27

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: 105.18  E-value: 8.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 828 LVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANAL 907
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80
                         90
                 ....*....|....*....
gi 145698285 908 AEEKQRCLESGMDSCLSKP 926
Cdd:cd17574   81 EEDKVLGLELGADDYITKP 99
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
352-690 1.19e-26

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 115.21  E-value: 1.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 352 LEEHEQFNRKIVASAPVGIC-------ILRTADG----VNILSNELA----HTYLNMLTHEDRQRLTQIICGQQVNF--- 413
Cdd:COG5805  152 LQEQEERLQTLIENSPDLICvidtdgrILFINESierlFGAPREELIgknlLELLHPCDKEEFKERIESITEVWQEFiie 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 414 VDVLTSNN----TNLQISFVHSRYRNENVAICVLVDVSSRVKMEESL---QEMAQAAEQAsqsksmflATVSHELRTPLY 486
Cdd:COG5805  232 REIITKDGriryFEAVIVPLIDTDGSVKGILVILRDITEKKEAEELMarsEKLSIAGQLA--------AGIAHEIRNPLT 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 487 GIIGNLDLLQ-TKELPKGVDRLvtaMNNSSSLLLKIISDILDFSKIESEQLKIEPREFSPREVMNHITANylPLVVRKQL 565
Cdd:COG5805  304 SIKGFLQLLQpGIEDKEEYFDI---MLSELDRIESIISEFLALAKPQAVNKEKENINELIQDVVTLLETE--AILHNIQI 378
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 566 GLYcFIEPDVPValNGDPMRLQQVISNLLSNAIK-FTDTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVG 644
Cdd:COG5805  379 RLE-LLDEDPFI--YCDENQIKQVFINLIKNAIEaMPNGGTITIHTEEEDNSVIIRVIDEGIGIPEERLKKLGEPFFTTK 455
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 145698285 645 TgvqrnfQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIPL 690
Cdd:COG5805  456 E------KGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLPL 495
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
827-927 1.60e-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: 104.50  E-value: 1.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT--LPVIGVTA 904
Cdd:cd17538    2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETrhIPVIMITA 81
                         90       100
                 ....*....|....*....|...
gi 145698285 905 NALAEEKQRCLESGMDSCLSKPV 927
Cdd:cd17538   82 LDDREDRIRGLEAGADDFLSKPI 104
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
827-936 6.68e-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: 102.92  E-value: 6.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQL--GLTLPVIGVTA 904
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELpwLANTPAIALTG 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 145698285 905 NALAEEKQRCLESGMDSCLSKPVTLDVIKQTL 936
Cdd:cd17580   81 YGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
826-927 2.61e-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: 101.46  E-value: 2.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 826 MILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT--LPVIGVT 903
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATrdIPVIALT 80
                         90       100
                 ....*....|....*....|....
gi 145698285 904 ANALAEEKQRCLESGMDSCLSKPV 927
Cdd:cd17548   81 AYAMKGDREKILEAGCDGYISKPI 104
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
823-949 2.46e-24

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 99.27  E-value: 2.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 823 DDMMILVVDDHPINRRLLADQLGSL-GYQ-CKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVI 900
Cdd:COG4565    2 KMIRVLIVEDDPMVAELLRRYLERLpGFEvVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVI 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 145698285 901 GVTANALAEEKQRCLESGMDSCLSKPVTLDVIKQTLTLYAERVRKSRDS 949
Cdd:COG4565   82 VITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLRED 130
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
582-689 5.27e-23

Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas putida TodS and Thauera aromatica TutC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) such Pseudomonas putida TodS HK of the TodS-TodT two-component regulatory system (TCS) which controls the expression of a toluene degradation pathway. Thauera aromatica TutC may be part of a TCS that is involved in anaerobic toluene metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), PAS sensor domain(s) and a REC domain.


Pssm-ID: 340402 [Multi-domain]  Cd Length: 110  Bit Score: 94.87  E-value: 5.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 582 DPMRLQQVISNLLSNAIKFTDTG----CIVlhVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLG 657
Cdd:cd16925    1 DAEKYERVVLNLLSNAFKFTPDGgrirCIL--EKFRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGLG 78
                         90       100       110
                 ....*....|....*....|....*....|..
gi 145698285 658 LAICEKLISMMDGDISVDSEPGMGSQFTVRIP 689
Cdd:cd16925   79 LSIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
583-690 5.81e-23

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: 94.41  E-value: 5.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 583 PMRLQQVISNLLSNAIKFTDT-GCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFF---QVGtgvqrnfQGTGLGL 658
Cdd:cd16943    1 PSQLNQVLLNLLVNAAQAMEGrGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPFFttkPVG-------EGTGLGL 73
                         90       100       110
                 ....*....|....*....|....*....|..
gi 145698285 659 AICEKLISMMDGDISVDSEPGMGSQFTVRIPL 690
Cdd:cd16943   74 SLSYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
827-926 6.06e-23

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: 94.07  E-value: 6.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSL-GYQ-CKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTA 904
Cdd:COG4753    2 VLIVDDEPLIREGLKRILEWEaGFEvVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILSG 81
                         90       100
                 ....*....|....*....|..
gi 145698285 905 NALAEEKQRCLESGMDSCLSKP 926
Cdd:COG4753   82 YSDFEYAQEAIKLGADDYLLKP 103
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
456-692 3.86e-22

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 101.07  E-value: 3.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 456 LQEMAQAAEqasqskSMFLA------------TVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIIS 523
Cdd:PRK11100 236 LRELAQALE------SMRVKlegkayveqyvqTLTHELKSPLAAIRGAAELLQEDPPPEDRARFTGNILTQSARLQQLID 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 524 DILDFSKIESEQlKIEPRE-FSPREVMNHITANYLPLVVRKQLGLYcfIEPDvPVALNGDPMRLQQVISNLLSNAIKFTD 602
Cdd:PRK11100 310 RLLELARLEQRQ-ELEVLEpVALAALLEELVEAREAQAAAKGITLR--LRPD-DARVLGDPFLLRQALGNLLDNAIDFSP 385
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 603 TG-CIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQV---GTGVqrnfQGTGLGLAICEKLISMMDGDISVDSEP 678
Cdd:PRK11100 386 EGgTITLSAEVDGEQVALSVEDQGPGIPDYALPRIFERFYSLprpANGR----KSTGLGLAFVREVARLHGGEVTLRNRP 461
                        250
                 ....*....|....
gi 145698285 679 GMGSQFTVRIPLYG 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 5.54e-22

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: 91.76  E-value: 5.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 582 DPMRLQQVISNLLSNAIKFTDTGCiVLHVRA--DGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLA 659
Cdd:cd16946    1 DRDRLQQLFVNLLENSLRYTDTGG-KLRIRAaqTPQEVRLDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGLGLA 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 145698285 660 ICEKLISMMDGDISVDSEPGMGSQFTVRIP 689
Cdd:cd16946   80 ICHNIALAHGGTISAEHSPLGGLRLVLTLP 109
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
825-936 7.83e-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: 91.63  E-value: 7.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 825 MMILVVDDHPINRRLLADQLGSLGYQ-CKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIR---QLGlTLPVI 900
Cdd:cd19923    1 MKVLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRadgALS-HLPVL 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 145698285 901 GVTANALAEEKQRCLESGMDSCLSKPVTLDVIKQTL 936
Cdd:cd19923   80 MVTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKL 115
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
295-690 1.37e-21

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 98.00  E-value: 1.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 295 SSLSIVYSVPVDKVLERIRMLILNAILLNVLAGAALFTLARMYERRIFIPAESDALRLEEHEQFnrkIVASAPVGIcILR 374
Cdd:COG3290   25 LLIILLLILLLVLLLLLFLLFVIILLLLLLILLLILLLLLLLLLAALLLKLLEEIARLVEEREA---VLESIREGV-IAV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 375 TADGVNILSNELAhtylnmlthedRQRLTQIICGQQVN--FVDVLTSNNTNLQISFVHSRYRNENVAICVLVDVSSRVKM 452
Cdd:COG3290  101 DRDGRITLINDAA-----------RRLLGLDAIGRPIDevLAEVLETGERDEEILLNGRVLVVNRVPIRDDGRVVGAVAT 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 453 EESLQEMAQAAEQASQSKSMF--LATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNN-SSSLLLKIISDILD-- 527
Cdd:COG3290  170 FRDRTELERLEEELEGVKELAeaLRAQRHDFRNHLHTISGLLQLGEYDEALEYIDEISEELQElIDSLLSRIGNPVLAal 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 528 -FSKI-ESEQLKIEprefsprevmnhitanylplvvrkqlgLYCFIEPDVPVaLNGDPMRLQQVISNLLSNAI-----KF 600
Cdd:COG3290  250 lLGKAaRARERGID---------------------------LTIDIDSDLPD-LPLSDTDLVTILGNLLDNAIeavekLP 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 601 TDTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGvqrnfQGTGLGLAICEKLISMMDGDISVDSEPGM 680
Cdd:COG3290  302 EEERRVELSIRDDGDELVIEVEDSGPGIPEELLEKIFERGFSTKLG-----EGRGLGLALVKQIVEKYGGTIEVESEEGE 376
                        410
                 ....*....|
gi 145698285 681 GSQFTVRIPL 690
Cdd:COG3290  377 GTVFTVRLPK 386
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
444-691 1.55e-21

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 98.94  E-value: 1.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 444 VDVSSRVKMEESLQEMAQAA---EQASQSKSMFLATVSHELRTPLYGIIGNLDLLQtkelpKGVDRLVTAMNNS----SS 516
Cdd:PRK10549 211 VTPTSRDELGRLAQDFNQLAstlEKNEQMRRDFMADISHELRTPLAVLRGELEAIQ-----DGVRKFTPESVASlqaeVG 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 517 LLLKIISDI--LDFSKIESEQLKIEPREFSPreVMNHITANYLPLVVRKQLGLYCFIEPDVPVAlnGDPMRLQQVISNLL 594
Cdd:PRK10549 286 TLTKLVDDLhqLSLSDEGALAYRKTPVDLVP--LLEVAGGAFRERFASRGLTLQLSLPDSATVF--GDPDRLMQLFNNLL 361
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 595 SNAIKFTDTGCiVLHVRA--DGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLISMMDGDI 672
Cdd:PRK10549 362 ENSLRYTDSGG-SLHISAeqRDKTLRLTFADSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRI 440
                        250
                 ....*....|....*....
gi 145698285 673 SVDSEPGMGSQFTVRIPLY 691
Cdd:PRK10549 441 IAAHSPFGGVSITVELPLE 459
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
827-918 2.12e-21

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: 89.88  E-value: 2.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT--LPVIGVTA 904
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATrhIPVIFLTA 80
                         90
                 ....*....|....
gi 145698285 905 NALAEEKQRCLESG 918
Cdd:cd19920   81 LTDTEDKVKGFELG 94
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
827-926 3.34e-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: 89.74  E-value: 3.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSK---------NHIDIVLSDVNMPNMDGYRLTQRIRQ--LGL 895
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENlakegndlsKELDLIITDIEMPKMDGYELTFELRDdpRLA 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 145698285 896 TLPVIGVTANALAEEKQRCLESGMDSCLSKP 926
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
825-927 6.77e-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: 89.04  E-value: 6.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 825 MMILVVDDHPINRRLLADQLGSLGY-QCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQL--GLTLPVIG 901
Cdd:cd17551    1 MRILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALpgLEDVPIVM 80
                         90       100
                 ....*....|....*....|....*.
gi 145698285 902 VTANALAEEKQRCLESGMDSCLSKPV 927
Cdd:cd17551   81 ITADTDREVRLRALEAGATDFLTKPF 106
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
573-688 1.12e-20

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: 88.72  E-value: 1.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 573 PDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIV-LHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNF 651
Cdd:cd16947    8 PDRPIYANANTEALQRILKNLISNAIKYGSDGKFLgMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRNSAK 87
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 145698285 652 QGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRI 688
Cdd:cd16947   88 QGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
envZ PRK09467
osmolarity sensor protein; Provisional
459-690 1.53e-20

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 95.75  E-value: 1.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 459 MAQAAEQASQSKSMFLATVSHELRTPLYGIignldllqtkelpkgvdRLVTAMNNSSSLLLK--IISDILDFSKIESEQL 536
Cdd:PRK09467 218 MAAGIKQLEDDRTLLMAGVSHDLRTPLTRI-----------------RLATEMMSEEDGYLAesINKDIEECNAIIEQFI 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 537 K-IEPREFSPREV--MNHITANylplVVRKQLGLYCFIE---PDVPVALNGDPMRLQQVISNLLSNAIKFTdTGCIVLHV 610
Cdd:PRK09467 281 DyLRTGQEMPMEMadLNALLGE----VIAAESGYEREIEtalQPGPIEVPMNPIAIKRALANLVVNAARYG-NGWIKVSS 355
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 611 RADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGvqRNFQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIPL 690
Cdd:PRK09467 356 GTEGKRAWFQVEDDGPGIPPEQLKHLFQPFTRGDSA--RGSSGTGLGLAIVKRIVDQHNGKVELGNSEEGGLSARAWLPL 433
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
825-937 2.10e-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: 87.54  E-value: 2.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 825 MM--ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGV 902
Cdd:COG5803    1 MMkkILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPDIPVIMM 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 145698285 903 TANALAEEKQRCLESGMDSCLSKPVTLDVIKQTLT 937
Cdd:COG5803   81 TAYGELDMVEEAKELGAKGYFTKPFDIDELREAVN 115
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
455-689 2.56e-20

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 95.22  E-value: 2.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 455 SLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLD--LLQTKElPKGVDRLVTAMNNSSSLLLKIISDILDFSKIE 532
Cdd:PRK09835 247 SFNHMIERIEDVFTRQSNFSADIAHEIRTPITNLITQTEiaLSQSRS-QKELEDVLYSNLEELTRMAKMVSDMLFLAQAD 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 533 SEQLKIEPREFSPREVMNHITANYLPLVVRKQLGLYcFIepDVPVALNGDPMRLQQVISNLLSNAIKFTDTG-CIVLHVR 611
Cdd:PRK09835 326 NNQLIPEKKMLDLADEVGKVFDFFEAWAEERGVELR-FV--GDPCQVAGDPLMLRRAISNLLSNALRYTPAGeAITVRCQ 402
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145698285 612 ADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLISMMDGDISVDSEPgMGSQFTVRIP 689
Cdd:PRK09835 403 EVDHQVQLVVENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRFVISLP 479
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
827-933 2.66e-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: 87.30  E-value: 2.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKN--HIDIVLSDVNMPNMDGYRLTQRIRqLGLTLPVIGVTA 904
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENkdEFDLVITDVHMPDMDGFEFLELIR-LEMDLPVIMMSA 79
                         90       100
                 ....*....|....*....|....*....
gi 145698285 905 NALAEEKQRCLESGMDSCLSKPVTLDVIK 933
Cdd:cd17584   80 DGSTSTVMKGLAHGACDYLLKPVSIEDLK 108
pleD PRK09581
response regulator PleD; Reviewed
827-927 2.76e-19

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 91.89  E-value: 2.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT--LPVIGVTA 904
Cdd:PRK09581   5 ILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATthIPVVMVTA 84
                         90       100
                 ....*....|....*....|...
gi 145698285 905 NALAEEKQRCLESGMDSCLSKPV 927
Cdd:PRK09581  85 LDDPEDRVRGLEAGADDFLTKPI 107
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
455-693 2.83e-19

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 91.92  E-value: 2.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 455 SLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKElpkGVDRLVTAMNNSSSLLLKIISDILDFSKIese 534
Cdd:PRK09470 228 SFNQMVTALERMMTSQQRLLSDISHELRTPLTRLQLATALLRRRQ---GESKELERIETEAQRLDSMINDLLVLSRN--- 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 535 QLKieprefsprevmNHITANYLPL------VVR------KQLGLYCFIEPDV-PVALNGDPMRLQQVISNLLSNAIKFT 601
Cdd:PRK09470 302 QQK------------NHLERETFKAnslwseVLEdakfeaEQMGKSLTVSAPPgPWPINGNPNALASALENIVRNALRYS 369
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 602 DTGcIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLISMMDGDISVDSEPGMG 681
Cdd:PRK09470 370 HTK-IEVAFSVDKDGLTITVDDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAIVENAIQQHRGWVKAEDSPLGG 448
                        250
                 ....*....|..
gi 145698285 682 SQFTVRIPLYGA 693
Cdd:PRK09470 449 LRLTIWLPLYKR 460
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-689 3.09e-19

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


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 83.92  E-value: 3.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 586 LQQVISNLLSNAIKFTDTG---CIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTgvQRNFQGTGLGLAICE 662
Cdd:cd16921    1 LGQVLTNLLGNAIKFRRPRrppRIEVGAEDVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRLHS--REEYEGTGVGLAIVR 78
                         90       100
                 ....*....|....*....|....*..
gi 145698285 663 KLISMMDGDISVDSEPGMGSQFTVRIP 689
Cdd:cd16921   79 KIIERHGGRIWLESEPGEGTTFYFTLP 105
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
827-926 3.66e-19

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: 83.58  E-value: 3.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGL--TLPVIGVTA 904
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADfdTIPVIFLTA 80
                         90       100
                 ....*....|....*....|..
gi 145698285 905 NALAEEKQRCLESGMDSCLSKP 926
Cdd:cd19927   81 KGMTSDRIKGYNAGCDGYLSKP 102
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
825-936 5.85e-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: 5.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 825 MMILVVDDHPINRRLLADQLGSlGYQCKT--ANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGV 902
Cdd:cd17593    1 MKVLICDDSSMARKQLARALPA-DWDVEItfAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVV 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 145698285 903 TANALAEEKQRCLESGMDSCLSKPVTLDVIKQTL 936
Cdd:cd17593   80 SGDVQPEAKERVLELGALAFLKKPFDPEKLAQLL 113
PRK10610 PRK10610
chemotaxis protein CheY;
822-943 6.49e-19

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 83.87  E-value: 6.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 822 NDDMMILVVDDHPINRRLLADQLGSLGYQ-CKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLG--LTLP 898
Cdd:PRK10610   3 DKELKFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGamSALP 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 145698285 899 VIGVTANALAEEKQRCLESGMDSCLSKPVTLDVIKQTLTLYAERV 943
Cdd:PRK10610  83 VLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKL 127
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-690 6.54e-19

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: 82.76  E-value: 6.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 586 LQQVISNLLSNAIKFTDTGcIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLI 665
Cdd:cd16949    1 LARALENVLRNALRYSPSK-ILLDISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAIAERAI 79
                         90       100
                 ....*....|....*....|....*
gi 145698285 666 SMMDGDISVDSEPGMGSQFTVRIPL 690
Cdd:cd16949   80 EQHGGKIKASNRKPGGLRVRIWLPA 104
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
570-690 7.84e-19

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 92.05  E-value: 7.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 570 FIEPDVPVALNGDPMRLQQVISNLLSNAIK-FTDTGCIVLHVRA---------------DGDYLSIRVRDTGVGIPAKEV 633
Cdd:PRK13837 545 FDQDQEPAVVEGNPAELQQVLMNLCSNAAQaMDGAGRVDISLSRaklrapkvlshgvlpPGRYVLLRVSDTGAGIDEAVL 624
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145698285 634 VRLFDPFFQVGTGvqrnfqGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIPL 690
Cdd:PRK13837 625 PHIFEPFFTTRAG------GTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLPP 675
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-689 1.11e-18

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: 82.06  E-value: 1.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 586 LQQVISNLLSNAIKFTDTGC------IVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTgvqrnfQGTGLGLA 659
Cdd:cd16920    1 IQQVLINLVRNGIEAMSEGGcerrelTIRTSPADDRAVTISVKDTGPGIAEEVAGQLFDPFYTTKS------EGLGMGLS 74
                         90       100       110
                 ....*....|....*....|....*....|
gi 145698285 660 ICEKLISMMDGDISVDSEPGMGSQFTVRIP 689
Cdd:cd16920   75 ICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
827-936 3.13e-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: 3.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINR----RLLADQLGS--LGyqckTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVI 900
Cdd:cd17535    1 VLIVDDHPLVReglrRLLESEPDIevVG----EAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVI 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 145698285 901 GVTANALAEEKQRCLESGMDSCLSKPVTLDVIKQTL 936
Cdd:cd17535   77 VLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAI 112
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-689 4.23e-18

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


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 80.71  E-value: 4.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 586 LQQVISNLLSNAIKFT-DTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKL 664
Cdd:cd16952    1 LRSAFSNLVSNAVKYTpPSDTITVRWSQEESGARLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAIVKHV 80
                         90       100
                 ....*....|....*....|....*
gi 145698285 665 ISMMDGDISVDSEPGMGSQFTVRIP 689
Cdd:cd16952   81 MSRHDARLLIASELGKGSRFTCLFP 105
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
459-690 6.84e-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: 6.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 459 MAQAAEQASQSKSMFLATVSHELRTP-------LYGIIGNL---DLLQTKELPKGVDRLvtamnnssSLLlkiISDILDF 528
Cdd:NF012226 127 MAQKLESSVKNAQVWNAAIAHELRTPitilqgrLQGILDGVfepDPALFKSLLNQVEGL--------SHL---VEDLRTL 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 529 SKIESEQLKIEPREFSPREVMNHITANYLPLVVRKQLglycFIEPDVPVAL-NGDPMRLQQVISNLLSNAIKFTDTGCIV 607
Cdd:NF012226 196 SLVENQQLRLNYESVDLKDSIEKVLKMFEDRLEQAQL----TIVLNLTATPvFCDRRRIEQVLIALIDNAIRYANAGKLK 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 608 LHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLISMMDGDISVdSEPGMGSQFTVR 687
Cdd:NF012226 272 ISSSVIQDDWILQIEDEGPGIAEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEY-SNSQGNSVFTIK 350

                 ...
gi 145698285 688 IPL 690
Cdd:NF012226 351 LPA 353
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
827-936 8.71e-18

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: 80.04  E-value: 8.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGL--TLPVIGVTA 904
Cdd:cd17562    3 ILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAykFTPILMLTT 82
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 145698285 905 NALAEEKQRCLESGMDSCLSKPVT----LDVIKQTL 936
Cdd:cd17562   83 ESSDEKKQEGKAAGATGWLVKPFDpeqlLEVVKKVL 118
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
827-930 1.55e-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: 79.35  E-value: 1.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANA 906
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80
                         90       100
                 ....*....|....*....|....
gi 145698285 907 LAEEKQRCLESGMDSCLSKPVTLD 930
Cdd:cd17627   81 SVSDRVAGLDAGADDYLVKPFALE 104
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
827-926 1.71e-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: 79.29  E-value: 1.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIR-QLGL-TLPVIGVTA 904
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKsDPDLkDIPVILLTT 80
                         90       100
                 ....*....|....*....|..
gi 145698285 905 NALAEEKQRCLESGMDSCLSKP 926
Cdd:cd17598   81 LSDPRDVIRGLECGADNFITKP 102
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
827-926 1.81e-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: 79.25  E-value: 1.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANA 906
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80
                         90       100
                 ....*....|....*....|
gi 145698285 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:cd19934   81 SWQDKVEGLDAGADDYLTKP 100
PRK10604 PRK10604
sensor protein RstB; Provisional
447-691 2.33e-17

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 85.81  E-value: 2.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 447 SSRVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQ--TKELPKGVDRLVTAMNnssslllKIISD 524
Cdd:PRK10604 189 SSLERLGVAFNQMADNINALIASKKQLIDGIAHELRTPLVRLRYRLEMSDnlSAAESQALNRDIGQLE-------ALIEE 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 525 ILDFSKIESEQLKIEPREFSprevmnhitanyLPLVVRKQLGLYCFIEPDVPVALN---------GDPMRLQQVISNLLS 595
Cdd:PRK10604 262 LLTYARLDRPQNELHLSEPD------------LPAWLSTHLADIQAVTPEKTVRLDtphqgdygaLDMRLMERVLDNLLN 329
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 596 NAIKFTdTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLISMMDGDISVD 675
Cdd:PRK10604 330 NALRYA-HSRVRVSLLLDGNQACLIVEDDGPGIPPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCD 408
                        250
                 ....*....|....*.
gi 145698285 676 SEPGMGSQFTVRIPLY 691
Cdd:PRK10604 409 ESELGGARFSFSWPVW 424
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
823-944 2.39e-17

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


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 81.16  E-value: 2.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 823 DDMMILVVDDHPINRRLLADQLGSLGYQ-CKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLtLPVIG 901
Cdd:COG3707    2 RGLRVLVVDDEPLRRADLREGLREAGYEvVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP-APVIL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 145698285 902 VTANALAEEKQRCLESGMDSCLSKPVTLDVIKQTLTLYAERVR 944
Cdd:COG3707   81 LTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARFR 123
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
589-689 2.69e-17

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: 78.48  E-value: 2.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 589 VISNLLSNAIKFTD-TGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFqvgTG-VQRNFQ-GTGLGLAICEKLI 665
Cdd:cd16948    9 IIGQIVSNALKYSKqGGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKGF---TGeNGRNFQeSTGMGLYLVKKLC 85
                         90       100
                 ....*....|....*....|....
gi 145698285 666 SMMDGDISVDSEPGMGSQFTVRIP 689
Cdd:cd16948   86 DKLGHKIDVESEVGEGTTFTITFP 109
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
469-534 3.64e-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: 76.48  E-value: 3.64e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145698285  469 SKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESE 534
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
PRK10490 PRK10490
sensor protein KdpD; Provisional
454-690 4.37e-17

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 86.63  E-value: 4.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 454 ESLQeMAQAAEQA------SQSKSMFLATVSHELRTPLYGIIGN-----LDL--------LQTKELPKGV---DRLVtam 511
Cdd:PRK10490 643 ERLT-LTASEEQArlaserEQLRNALLAALSHDLRTPLTVLFGQaeiltLDLasegsphaRQASEIRQQVlntTRLV--- 718
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 512 NNssslllkiisdILDFSKIESEQLKIEPREFSPREVMNHITANYLPLVVRKQLGLYCfiePDVPVALNGDPMRLQQVIS 591
Cdd:PRK10490 719 NN-----------LLDMARIQSGGFNLRKEWLTLEEVVGSALQMLEPGLSGHPINLSL---PEPLTLIHVDGPLFERVLI 784
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 592 NLLSNAIKFTDTGC-IVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFfqvGTGVQRN-FQGTGLGLAICEKLISMMD 669
Cdd:PRK10490 785 NLLENAVKYAGAQAeIGIDAHVEGERLQLDVWDNGPGIPPGQEQLIFDKF---ARGNKESaIPGVGLGLAICRAIVEVHG 861
                        250       260
                 ....*....|....*....|.
gi 145698285 670 GDISVDSEPGMGSQFTVRIPL 690
Cdd:PRK10490 862 GTIWAENRPEGGACFRVTLPL 882
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
827-926 5.39e-17

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: 77.10  E-value: 5.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANA 906
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTARD 80
                         90       100
                 ....*....|....*....|
gi 145698285 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:cd19935   81 SVEDRVKGLDLGADDYLVKP 100
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
473-689 9.25e-17

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 83.91  E-value: 9.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 473 FLATVSHELRTPLYGIIGNLDLLQTKELPKGV-DRLVTAMNNSSSLLLKIISDILDFSKIESE-------------QLKI 538
Cdd:PRK11006 207 FFANVSHELRTPLTVLQGYLEMMQDQPLEGALrEKALHTMREQTQRMEGLVKQLLTLSKIEAAptidlnekvdvpmMLRV 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 539 EPRE-FSPREVMNHITANylplvVRKQLGLYcfiepdvpvalnGDPMRLQQVISNLLSNAIKFTDTGCIVlHVR----AD 613
Cdd:PRK11006 287 LEREaQTLSQGKHTITFE-----VDNSLKVF------------GNEDQLRSAISNLVYNAVNHTPEGTHI-TVRwqrvPQ 348
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145698285 614 GDYLSirVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIP 689
Cdd:PRK11006 349 GAEFS--VEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLP 422
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
827-904 1.16e-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: 76.49  E-value: 1.16e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTA 904
Cdd:cd17554    3 ILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTA 80
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
582-679 1.17e-16

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: 76.35  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 582 DPMRLQQVISNLLSNAIKFT-DTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGvQRNFQGTGLGLAI 660
Cdd:cd16945    1 DPFLLRQAINNLLDNAIDFSpEGGLIALQLEADTEGIELLVFDEGSGIPDYALNRVFERFYSLPRP-HSGQKSTGLGLAF 79
                         90
                 ....*....|....*....
gi 145698285 661 CEKLISMMDGDISVDSEPG 679
Cdd:cd16945   80 VQEVAQLHGGRITLRNRPD 98
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
827-926 1.39e-16

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: 76.79  E-value: 1.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLsKNHIDI--VLSDVNMPNMDGYRLTQRIRQL--GLTLPVIGV 902
Cdd:cd17544    3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVL-EQHPDIklVITDYNMPEMDGFELVREIRKKysRDQLAIIGI 81
                         90       100
                 ....*....|....*....|....
gi 145698285 903 TANALAEEKQRCLESGMDSCLSKP 926
Cdd:cd17544   82 SASGDNALSARFIKAGANDFLTKP 105
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
827-926 1.40e-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: 76.05  E-value: 1.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLgLTLPVIGVTANA 906
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREW-SAVPVIVLSARD 79
                         90       100
                 ....*....|....*....|
gi 145698285 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:cd17620   80 EESDKIAALDAGADDYLTKP 99
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
469-534 1.80e-16

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 74.52  E-value: 1.80e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145698285   469 SKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESE 534
Cdd:smart00388   1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-686 2.21e-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: 75.57  E-value: 2.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 586 LQQVISNLLSNAI----KFTDTGCIVLHVRADGDyLSIRVRDTGVGIPAKEVVRLFDPFF---QVGtgvqrnfQGTGLGL 658
Cdd:cd16976    1 IQQVLMNLLQNALdamgKVENPRIRIAARRLGGR-LVLVVRDNGPGIAEEHLSRVFDPFFttkPVG-------KGTGLGL 72
                         90       100
                 ....*....|....*....|....*...
gi 145698285 659 AICEKLISMMDGDISVDSEPGMGSQFTV 686
Cdd:cd16976   73 SISYGIVEEHGGRLSVANEEGAGARFTF 100
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
827-936 9.32e-16

phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response regulators; This family is composed of uncharacterized response regulators that contain a REC domain and a AraC family helix-turn-helix (HTH) DNA-binding output domain, including Bacillus subtilis uncharacterized transcriptional regulatory protein YesN and Staphylococcus aureus uncharacterized response regulatory protein SAR0214. YesN is a member of the two-component regulatory system YesM/YesN and SAR0214 is a member of the probable two-component regulatory system SAR0215/SAR0214. Also included in this family is the AlgR-like group of LytTR/AlgR family response, which includes Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR and Bacillus subtilis sensory transduction protein LytT, among others. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 74.30  E-value: 9.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQL--GSLGYQ-CKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVT 903
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIdwEELGFEvVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILS 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 145698285 904 ANALAEEKQRCLESGMDSCLSKPVTLDVIKQTL 936
Cdd:cd17536   81 GYDDFEYAQKAIRLGVVDYLLKPVDEEELEEAL 113
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
827-938 1.60e-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: 73.60  E-value: 1.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQ-CKTANDGVDALNVLSKNHIDIVLSDVNMP-NMDGYRLTQRIRQLgLTLPVIGVTA 904
Cdd:cd17534    3 ILIVEDEAIIALDLKEILESLGYEvVGIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREK-FDIPVIFLTA 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 145698285 905 NALAEEKQRCLESGMDSCLSKPVTLDVIKQTLTL 938
Cdd:cd17534   82 YSDEETLERAKETNPYGYLVKPFNERELKAAIEL 115
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
827-936 2.56e-15

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


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 72.82  E-value: 2.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNH--IDIVLSDVNMPNMDGYRLTQRIRQLGLT---LPVIG 901
Cdd:cd19933    3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEhsFQLVLLDLCMPEMDGFEVALRIRKLFGRrerPLIVA 82
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 145698285 902 VTANALAEEKQRCLESGMDSCLSKPVTLDVIKQTL 936
Cdd:cd19933   83 LTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
827-930 2.58e-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: 73.16  E-value: 2.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANA 906
Cdd:cd17615    2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAKD 81
                         90       100
                 ....*....|....*....|....
gi 145698285 907 LAEEKQRCLESGMDSCLSKPVTLD 930
Cdd:cd17615   82 SVEDRIAGLTAGGDDYVTKPFSLE 105
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
825-879 3.05e-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: 70.68  E-value: 3.05e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 145698285   825 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMP 879
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
825-949 3.38e-15

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 76.01  E-value: 3.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 825 MM-ILVVDDHPINRRLLADQLGSL-GYQC-KTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIG 901
Cdd:COG3279    1 MMkILIVDDEPLARERLERLLEKYpDLEVvGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIF 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 145698285 902 VTA-----------NALAeekqrclesgmdsCLSKPVTLDVIKQTLTLYAERVRKSRDS 949
Cdd:COG3279   81 TTAydeyaleafevNAVD-------------YLLKPIDEERLAKALEKAKERLEAKAAA 126
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
827-893 3.59e-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: 3.59e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQL 893
Cdd:cd17569    3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRER 69
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
827-926 1.03e-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: 70.98  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANA 906
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80
                         90       100
                 ....*....|....*....|
gi 145698285 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:cd17624   81 GVDDRVAGLDAGADDYLVKP 100
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
827-900 1.10e-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: 70.99  E-value: 1.10e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVI 900
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVI 74
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
827-926 1.13e-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: 71.13  E-value: 1.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT--LPVIGVTA 904
Cdd:cd17618    3 ILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTrdIPIIMLTA 82
                         90       100
                 ....*....|....*....|..
gi 145698285 905 NALAEEKQRCLESGMDSCLSKP 926
Cdd:cd17618   83 RGEEEDKVRGLEAGADDYITKP 104
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
827-904 1.48e-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: 71.37  E-value: 1.48e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTA 904
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITG 78
orf27 CHL00148
Ycf27; Reviewed
822-926 1.77e-14

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 73.98  E-value: 1.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 822 NDDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVIG 901
Cdd:CHL00148   4 NSKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKES-DVPIIM 82
                         90       100
                 ....*....|....*....|....*
gi 145698285 902 VTANALAEEKQRCLESGMDSCLSKP 926
Cdd:CHL00148  83 LTALGDVSDRITGLELGADDYVVKP 107
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-690 3.11e-14

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


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 69.38  E-value: 3.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 586 LQQVISNLLSNAIKFTDTGcIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLI 665
Cdd:cd16939    1 MARALDNLLRNALRYAHRT-VRIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAIVHRVA 79
                         90       100
                 ....*....|....*....|....*
gi 145698285 666 SMMDGDISVDSEPGMGSQFTVRIPL 690
Cdd:cd16939   80 LWHGGHVECDDSELGGACFRLTWPR 104
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
827-927 4.48e-14

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: 68.91  E-value: 4.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKN-HIDIVLSDVNMPN-MDGYRLTQRIRQLGLTLPVIGVTA 904
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGpDIDLLVTDVIMPGgMNGSQLAEEARRRRPDLKVLLTSG 80
                         90       100
                 ....*....|....*....|...
gi 145698285 905 NALAEEKQRCLESGMDsCLSKPV 927
Cdd:cd18161   81 YAENAIEGGDLAPGVD-VLSKPF 102
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
827-928 1.19e-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: 68.00  E-value: 1.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANA 906
Cdd:cd17555    3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSGAG 82
                         90       100
                 ....*....|....*....|..
gi 145698285 907 LAEEKQRCLESGMDSCLSKPVT 928
Cdd:cd17555   83 VMSDAVEALRLGAWDYLTKPIE 104
PRK15115 PRK15115
response regulator GlrR; Provisional
827-932 1.52e-13

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 74.10  E-value: 1.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANA 906
Cdd:PRK15115   8 LLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTAHG 87
                         90       100
                 ....*....|....*....|....*.
gi 145698285 907 LAEEKQRCLESGMDSCLSKPVTLDVI 932
Cdd:PRK15115  88 SIPDAVAATQQGVFSFLTKPVDRDAL 113
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
467-530 1.64e-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: 66.08  E-value: 1.64e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145698285 467 SQSKSMFLATVSHELRTPLYGIIGNLDLLQ-TKELPKGVDRLVTAMNNSSSLLLKIISDILDFSK 530
Cdd:cd00082    1 LQAKGEFLANVSHELRTPLTAIRGALELLEeELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-689 1.78e-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: 67.09  E-value: 1.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 586 LQQVISNLLSNAIKFTdTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGvqRNFQGTGLGLAICEKLI 665
Cdd:cd16950    1 LKRVLSNLVDNALRYG-GGWVEVSSDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNA--RGTSGTGLGLAIVQRIS 77
                         90       100
                 ....*....|....*....|....
gi 145698285 666 SMMDGDISVDSEPGMGSQFTVRIP 689
Cdd:cd16950   78 DAHGGSLTLANRAGGGLCARIELP 101
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
827-926 3.79e-13

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: 66.64  E-value: 3.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVIGVTANA 906
Cdd:cd17619    3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQS-EVGIILVTGRD 81
                         90       100
                 ....*....|....*....|
gi 145698285 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:cd17619   82 DEVDRIVGLEIGADDYVTKP 101
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
614-689 4.29e-13

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: 66.63  E-value: 4.29e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145698285 614 GDYLSIRVRDTGVGIPAKEVVRLFDPFF---QVGtgvqrnfQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIP 689
Cdd:cd16919   45 GNYVCLEVSDTGSGMPAEVLRRAFEPFFttkEVG-------KGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-689 4.50e-13

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: 66.44  E-value: 4.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 586 LQQVISNLLSNAIKFT--DTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEK 663
Cdd:cd16953    1 LGQVLRNLIGNAISFSppDTGRITVSAMPTGKMVTISVEDEGPGIPQEKLESIFDRFYTERPANEAFGQHSGLGLSISRQ 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 145698285 664 LISmMDGDISVD---SEPGM--GSQFTVRIP 689
Cdd:cd16953   81 IIE-AHGGISVAenhNQPGQviGARFTVQLP 110
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
827-930 4.68e-13

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


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 66.67  E-value: 4.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCK--TANDGVDALNVLSKN-------HIDIVLSDVNMPNMDGYRLTQRIRQLGLT- 896
Cdd:cd17557    2 ILLVEDNPGDAELIQEAFKEAGVPNElhVVRDGEEALDFLRGEgeyadapRPDLILLDLNMPRMDGFEVLREIKADPDLr 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 145698285 897 -LPVIGVTANALAEEKQRCLESGMDSCLSKPVTLD 930
Cdd:cd17557   82 rIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFE 116
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
827-926 4.68e-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: 4.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGS------LGyqckTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTlPVI 900
Cdd:cd17541    3 VLIVDDSAVMRKLLSRILESdpdievVG----TARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERPT-PVV 77
                         90       100
                 ....*....|....*....|....*...
gi 145698285 901 GVTA--NALAEEKQRCLESGMDSCLSKP 926
Cdd:cd17541   78 MVSSltEEGAEITLEALELGAVDFIAKP 105
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
828-926 4.80e-13

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 66.53  E-value: 4.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 828 LVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT--LPVIGVTAN 905
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTssIPIIMLTAK 80
                         90       100
                 ....*....|....*....|.
gi 145698285 906 ALAEEKQRCLESGMDSCLSKP 926
Cdd:cd19937   81 GEEFDKVLGLELGADDYITKP 101
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
827-933 4.88e-13

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 72.57  E-value: 4.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANA 906
Cdd:PRK11361   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAYA 86
                         90       100
                 ....*....|....*....|....*..
gi 145698285 907 LAEEKQRCLESGMDSCLSKPVTLDVIK 933
Cdd:PRK11361  87 EVETAVEALRCGAFDYVIKPFDLDELN 113
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
576-687 1.14e-12

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: 65.12  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 576 PVALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTgvqRNFQGTG 655
Cdd:cd16940    4 DIQVQGDALLLFLLLRNLVDNAVRYSPQGSRVEIKLSADDGAVIRVEDNGPGIDEEELEALFERFYRSDG---QNYGGSG 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 145698285 656 LGLAICEKLISMMDGDISVDSEPGMGSQFTVR 687
Cdd:cd16940   81 LGLSIVKRIVELHGGQIFLGNAQGGGLEAWVR 112
PRK15479 PRK15479
transcriptional regulator TctD;
825-930 1.19e-12

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 68.21  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 825 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTA 904
Cdd:PRK15479   1 MRLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTA 80
                         90       100
                 ....*....|....*....|....*.
gi 145698285 905 NALAEEKQRCLESGMDSCLSKPVTLD 930
Cdd:PRK15479  81 RSAVADRVKGLNVGADDYLPKPFELE 106
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-689 1.79e-12

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: 64.33  E-value: 1.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 586 LQQVISNLLSNAIKFTDTGCIV-LHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGvqRNFQGTGLGLAICEKL 664
Cdd:cd16923    1 LQRVFSNLLSNAIKYSPENTRIyITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNS--RNTEGAGLGLSIAKAI 78
                         90       100
                 ....*....|....*....|....*
gi 145698285 665 ISMMDGDISVDSEpGMGSQFTVRIP 689
Cdd:cd16923   79 IELHGGSASAEYD-DNHDLFKVRLP 102
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
826-947 1.92e-12

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: 67.05  E-value: 1.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 826 MILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTAN 905
Cdd:COG4566    1 TVYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGH 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 145698285 906 ALAEEKQRCLESGMDSCLSKPVT----LDVIKQTLTLYAERVRKSR 947
Cdd:COG4566   81 GDVPMAVRAMKAGAVDFLEKPFDdqalLDAVRRALARDRARRAERA 126
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
580-690 3.10e-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: 64.21  E-value: 3.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 580 NGDPMRLQQVISNLLSNAIKFTDT--GCIVLHVR------ADGD---YLSIRVRDTGVGIPAKEVVRLFDPffqvGTGVQ 648
Cdd:cd16932    1 YGDQIRLQQVLADFLLNAVRFTPSpgGWVEIKVSptkkqiGDGVhviHLEFRITHPGQGLPEELVQEMFEE----NQWTT 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 145698285 649 RNfqgtGLGLAICEKLISMMDGDISVDSEPGMgSQFTVRIPL 690
Cdd:cd16932   77 QE----GLGLSISRKLVKLMNGDVRYLREAGR-SYFLITLEL 113
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
827-940 4.72e-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: 63.80  E-value: 4.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGY--QCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTA 904
Cdd:cd19925    3 VLIVEDDPMVAEIHRAYVEQVPGftVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVVTA 82
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 145698285 905 NALAEEKQRCLESGMDSCLSKPVTLDVIKQTLTLYA 940
Cdd:cd19925   83 ANDVETVREALRLGVVDYLIKPFTFERLRQRLERYR 118
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
589-689 5.03e-12

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 69.56  E-value: 5.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 589 VISNLLSN---AIKFTDTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDpffqvgTGVQRNFQGTGLGLAICEKLI 665
Cdd:PRK11086 437 ILGNLIENaleAVGGEEGGEISVSLHYRNGWLHCEVSDDGPGIAPDEIDAIFD------KGYSTKGSNRGVGLYLVKQSV 510
                         90       100
                 ....*....|....*....|....
gi 145698285 666 SMMDGDISVDSEPGMGSQFTVRIP 689
Cdd:PRK11086 511 ENLGGSIAVESEPGVGTQFFVQIP 534
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
823-936 5.43e-12

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 68.90  E-value: 5.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 823 DDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGV 902
Cdd:PRK10365   4 DNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIM 83
                         90       100       110
                 ....*....|....*....|....*....|....
gi 145698285 903 TANALAEEKQRCLESGMDSCLSKPVTLDVIKQTL 936
Cdd:PRK10365  84 TAYSSVETAVEALKTGALDYLIKPLDFDNLQATL 117
PRK10816 PRK10816
two-component system response regulator PhoP;
825-932 7.89e-12

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 65.92  E-value: 7.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 825 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTA 904
Cdd:PRK10816   1 MRVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTA 80
                         90       100
                 ....*....|....*....|....*...
gi 145698285 905 NALAEEKQRCLESGMDSCLSKPVTLDVI 932
Cdd:PRK10816  81 RESWQDKVEVLSAGADDYVTKPFHIEEV 108
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
827-939 7.92e-12

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: 62.96  E-value: 7.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANA 906
Cdd:cd17553    3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAYG 82
                         90       100       110
                 ....*....|....*....|....*....|...
gi 145698285 907 LAEEKQRCLESGMDSCLSKPVTLDVIKQTLTLY 939
Cdd:cd17553   83 ELDMIQESKELGALTHFAKPFDIDEIRDAVKKY 115
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
586-689 9.11e-12

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: 62.42  E-value: 9.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 586 LQQVISNLLSNAIKFTDT--GCIVLHVRADGDY----------LSIRVRDTGVGIPAKEVVRLFDPFfqvgtgVQRNFQG 653
Cdd:cd16918    1 LIQVFLNLVRNAAQALAGsgGEIILRTRTQRQVtlghprhrlaLRVSVIDNGPGIPPDLQDTIFYPM------VSGRENG 74
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 145698285 654 TGLGLAICEKLISMMDGDISVDSEPGMgSQFTVRIP 689
Cdd:cd16918   75 TGLGLAIAQNIVSQHGGVIECDSQPGH-TVFSVSLP 109
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
827-926 1.06e-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: 62.57  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSL-GYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT--LPVIGVT 903
Cdd:cd17552    4 ILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETqsIPVILLT 83
                         90       100
                 ....*....|....*....|...
gi 145698285 904 ANALAEEKQRCLESGMDSCLSKP 926
Cdd:cd17552   84 AKAQPSDRQRFASLGVAGVIAKP 106
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
458-676 1.76e-11

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 68.17  E-value: 1.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 458 EMAQAAEQASQSKSMflATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLL---KIISDILDFSKIESE 534
Cdd:COG4192  423 ELIQAAKMAVVGQTM--TSLAHELNQPLNAMSMYLFSAKKALEQENYAQLPTSLDKIEGLIErmdKIIKSLRQFSRKSDT 500
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 535 QLKieprefsPREVMNHITANYLPLVVR-KQLGLYCFIEPDVPValNGDPMRLQQVISNLLSNAIK-FTDTGCIVLHVRA 612
Cdd:COG4192  501 PLQ-------PVDLRQVIEQAWELVESRaKPQQITLHIPDDLMV--QGDQVLLEQVLVNLLVNALDaVATQPQISVDLLS 571
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145698285 613 DGDYLSIRVRDTGVGIPAKEvvRLFDPFfqvgtgVQRNFQGTGLGLAICEKLISMMDGDISVDS 676
Cdd:COG4192  572 NAENLRVAISDNGNGWPLVD--KLFTPF------TTTKEVGLGLGLSICRSIMQQFGGDLYLAS 627
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
827-926 2.14e-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: 61.40  E-value: 2.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANA 906
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80
                         90       100
                 ....*....|....*....|
gi 145698285 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:cd19926   81 SLDTAIEALKAGAFDFLTKP 100
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
827-926 2.14e-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: 61.55  E-value: 2.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQlGLTLPVIGVTANa 906
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRK-TSQVPVLMLTAR- 78
                         90       100
                 ....*....|....*....|..
gi 145698285 907 lAEEKQRC--LESGMDSCLSKP 926
Cdd:cd17623   79 -GDDIDRIlgLELGADDYLPKP 99
PRK10643 PRK10643
two-component system response regulator PmrA;
825-930 2.70e-11

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 64.29  E-value: 2.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 825 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTA 904
Cdd:PRK10643   1 MKILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTA 80
                         90       100
                 ....*....|....*....|....*.
gi 145698285 905 NALAEEKQRCLESGMDSCLSKPVTLD 930
Cdd:PRK10643  81 RDTLEDRVAGLDVGADDYLVKPFALE 106
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
473-689 2.81e-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: 67.46  E-value: 2.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  473 FLATVSHELRTPLYGIIGNLDLLQTKELPK-----------GVDRLVTAMNNSSslllkiisdilDFSKIESEQLKIEPR 541
Cdd:TIGR03785 488 MSSRLSHELRTPVAVVRSSLENLELQALEQekqkylerareGTERLSMILNNMS-----------EATRLEQAIQSAEVE 556
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  542 EFSPREVMNHITANYLPLVVRKQLGLYCfiePDVPVALNGDPMRLQQVISNLLSNAIKFT-DTGCIVLHVRADGDYLSIR 620
Cdd:TIGR03785 557 DFDLSEVLSGCMQGYQMTYPPQRFELNI---PETPLVMRGSPELIAQMLDKLVDNAREFSpEDGLIEVGLSQNKSHALLT 633
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145698285  621 VRDTGVGIPAKEVVRLFDPFFQVgtgvqRNFQGT-----GLGLAICEKLISMMDGDISVDSEP-GMGSQFTVRIP 689
Cdd:TIGR03785 634 VSNEGPPLPEDMGEQLFDSMVSV-----RDQGAQdqphlGLGLYIVRLIADFHQGRIQAENRQqNDGVVFRISLP 703
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
827-936 3.08e-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: 61.44  E-value: 3.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANA 906
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 145698285 907 ---LAEEKQRcleSGMDSCLSKPVTLDVIKQTL 936
Cdd:cd17572   81 svdIAVEAMR---LGAYDFLEKPFDADRLRVTV 110
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
827-904 3.19e-11

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: 61.13  E-value: 3.19e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTA 904
Cdd:cd19919    3 VWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTA 80
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
589-689 3.27e-11

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


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 60.76  E-value: 3.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 589 VISNLLSNAIK-FTDTGC----IVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRnfqgtGLGLAICEK 663
Cdd:cd16915    4 IVGNLIDNALDaLAATGApnkqVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVFERGVSTKGQGER-----GIGLALVRQ 78
                         90       100
                 ....*....|....*....|....*.
gi 145698285 664 LISMMDGDISVDSEPGMGSQFTVRIP 689
Cdd:cd16915   79 SVERLGGSITVESEPGGGTTFSIRIP 104
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
827-942 3.94e-11

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 66.43  E-value: 3.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANA 906
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 145698285 907 LAEEKQRCLESGMDSCLSKPVTLD----VIKQTLTLYAER 942
Cdd:PRK10923  86 DLDAAVSAYQQGAFDYLPKPFDIDeavaLVERAISHYQEQ 125
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
828-930 5.39e-11

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: 60.70  E-value: 5.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 828 LVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANAL 907
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80
                         90       100
                 ....*....|....*....|...
gi 145698285 908 AEEKQRCLESGMDSCLSKPVTLD 930
Cdd:cd17625   81 VEDRVKGLDLGADDYLPKPFSLA 103
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
827-926 7.29e-11

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: 59.77  E-value: 7.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVIGVTANA 906
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKS-TLPVIFLTSKD 79
                         90       100
                 ....*....|....*....|
gi 145698285 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:cd19936   80 DEIDEVFGLRMGADDYITKP 99
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
827-926 1.01e-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: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVL-SKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTAN 905
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLqQGKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISGG 81
                         90       100
                 ....*....|....*....|.
gi 145698285 906 ALAEEKQRCLESGMDSCLSKP 926
Cdd:cd18160   82 AAAAPELLSDAVGDNATLKKP 102
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
825-927 1.60e-10

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: 59.35  E-value: 1.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 825 MMILVVDDHPINRRLLADQLGSLGYQC-KTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTlPVIGVT 903
Cdd:cd19932    1 VRVLIAEDEALIRMDLREMLEEAGYEVvGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENIA-PIVLLT 79
                         90       100
                 ....*....|....*....|....
gi 145698285 904 ANALAEEKQRCLESGMDSCLSKPV 927
Cdd:cd19932   80 AYSQQDLVERAKEAGAMAYLVKPF 103
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
827-931 1.61e-10

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 59.30  E-value: 1.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVL-------SKNH----IDIVLSDVNMPNMDGYRLTQRIRQLG- 894
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLgledeedSSNFnepkVNMIITDYCMPGMTGYDLLKKVKESSa 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 145698285 895 -LTLPVIGVTANALAEEKQRCLESGMDSCLSKPVTL-DV 931
Cdd:cd17581   81 lKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLaDV 119
ompR PRK09468
osmolarity response regulator; Provisional
827-926 1.72e-10

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 62.30  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANa 906
Cdd:PRK09468   8 ILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPIIMLTAK- 86
                         90       100
                 ....*....|....*....|..
gi 145698285 907 lAEEKQRC--LESGMDSCLSKP 926
Cdd:PRK09468  87 -GEEVDRIvgLEIGADDYLPKP 107
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
825-890 1.95e-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: 59.52  E-value: 1.95e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145698285 825 MM-ILVVDDHPINRRLLADQLGSL-GYQ-CKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRI 890
Cdd:COG2197    1 MIrVLIVDDHPLVREGLRALLEAEpDIEvVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
827-936 2.09e-10

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: 58.76  E-value: 2.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANA 906
Cdd:cd17537    3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGHG 82
                         90       100       110
                 ....*....|....*....|....*....|....
gi 145698285 907 LAEEKQRCLESGMDSCLSKPVT----LDVIKQTL 936
Cdd:cd17537   83 DVPMAVEAMKAGAVDFLEKPFRdqvlLDAIEQAL 116
PRK10766 PRK10766
two-component system response regulator TorR;
827-929 2.31e-10

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 61.59  E-value: 2.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVIGVTANA 906
Cdd:PRK10766   5 ILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRS-TVGIILVTGRT 83
                         90       100
                 ....*....|....*....|...
gi 145698285 907 LAEEKQRCLESGMDSCLSKPVTL 929
Cdd:PRK10766  84 DSIDRIVGLEMGADDYVTKPLEL 106
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
472-660 2.33e-10

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 63.45  E-value: 2.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 472 MFLATVSHELRTPLYGIIGNLDLL------QTKELPKGVDRLvtaMNNSSSLL----------------LKIISDILDFS 529
Cdd:PRK10755 139 LFTADVAHELRTPLAGIRLHLELLekqhhiDVAPLIARLDQM---MHTVEQLLqlaragqsfssghyqtVKLLEDVILPS 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 530 KIESEQLkieprefsprevmnhitanylpLVVRKQLGLYCFIEPDVPValNGDPMRLQQVISNLLSNAIKFTDTG-CIVL 608
Cdd:PRK10755 216 QDELSEM----------------------LEQRQQTLLLPESAADITV--QGDATLLRLLLRNLVENAHRYSPEGsTITI 271
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 145698285 609 HVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGtgvQRnFQGTGLGLAI 660
Cdd:PRK10755 272 KLSQEDGGAVLAVEDEGPGIDESKCGELSKAFVRMD---SR-YGGIGLGLSI 319
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
823-942 2.40e-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: 60.32  E-value: 2.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 823 DDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGV 902
Cdd:COG4567    3 EDRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVL 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 145698285 903 T-----ANALAEEKQrclesGMDSCLSKPVTLDVIKQTLTLYAER 942
Cdd:COG4567   83 TgyasiATAVEAIKL-----GADDYLAKPADADDLLAALERAEGD 122
PRK13557 PRK13557
histidine kinase; Provisional
445-688 3.90e-10

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 63.54  E-value: 3.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 445 DVSSRVKMEESLQEmAQAAEQASQsksmFLATVSHELRTPLYGIIGNLDLLQTK-ELPKG--------VDRLVTAMNNSS 515
Cdd:PRK13557 143 DVSRRRDAEDALRQ-AQKMEALGQ----LTGGIAHDFNNLLQVMSGYLDVIQAAlSHPDAdrgrmarsVENIRAAAERAA 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 516 SLllkiISDILDFSKIEseqlKIEPREFSprevMNHITANYLPLVvRKQLGLYCFIEPDVPVALNG---DPMRLQQVISN 592
Cdd:PRK13557 218 TL----TQQLLAFARKQ----RLEGRVLN----LNGLVSGMGELA-ERTLGDAVTIETDLAPDLWNcriDPTQAEVALLN 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 593 LLSNA----------------IKFTDTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQV-GTGvqrnfQGTG 655
Cdd:PRK13557 285 VLINArdampeggrvtirtrnVEIEDEDLAMYHGLPPGRYVSIAVTDTGSGMPPEILARVMDPFFTTkEEG-----KGTG 359
                        250       260       270
                 ....*....|....*....|....*....|...
gi 145698285 656 LGLAICEKLISMMDGDISVDSEPGMGSqfTVRI 688
Cdd:PRK13557 360 LGLSMVYGFAKQSGGAVRIYSEVGEGT--TVRL 390
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
573-686 3.93e-10

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


Pssm-ID: 340415 [Multi-domain]  Cd Length: 133  Bit Score: 58.62  E-value: 3.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 573 PDVPValnGDPMRLQQVISNLLSNAIKFTDTGC-IVLHVRA-------------------DGDYLSIR--VRDTGVGIPA 630
Cdd:cd16938    2 PDVVV---GDERRVFQVLLHMLGNLLKMRNGGGnITFRVFLeggsedrsdrdwgpwrpsmSDESVEIRfeVEINDSGSPS 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 145698285 631 KEVVRLFDpffQVGTGVQRNFQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTV 686
Cdd:cd16938   79 IESASMRN---SLNRRYNLSELGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSL 131
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
560-690 4.53e-10

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 63.00  E-value: 4.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 560 VVRKQLGLYC--FIEPDVPVALNGDPMRLQQ--------VISNLLSNAIKF----TDTGCIVLHVRADGDYLSIRVRDTG 625
Cdd:COG3920  364 YLRELLEPLRdsYGGRGIRIELDGPDVELPAdaavplglILNELVTNALKHaflsGEGGRIRVSWRREDGRLRLTVSDNG 443
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145698285 626 VGIPAKEVVRlfdpffqvgtgvqrnfQGTGLGLAICEKLISMMDGDISVDSEPGMgsQFTVRIPL 690
Cdd:COG3920  444 VGLPEDVDPP----------------ARKGLGLRLIRALVRQLGGTLELDRPEGT--RVRITFPL 490
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
562-688 5.20e-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: 58.41  E-value: 5.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 562 RKQLGLYCFIEPDVpvALNGDPMRLQQVISNLLSNAIKFTDtGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFdpff 641
Cdd:cd16954   16 RKGVSISLDISPEL--RFPGERNDLMELLGNLLDNACKWCL-EFVEVTARQTDGGLHLIVDDDGPGVPESQRSKIF---- 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 145698285 642 QVGTGVQRNFQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRI 688
Cdd:cd16954   89 QRGQRLDEQRPGQGLGLAIAKEIVEQYGGELSLSDSPLGGARFEVVF 135
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
827-936 7.94e-10

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: 57.29  E-value: 7.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQC-KTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTAN 905
Cdd:cd17542    3 VLIVDDAAFMRMMLKDILTKAGYEVvGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCSAM 82
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 145698285 906 ALAEEKQRCLESGMDSCLSKPV----TLDVIKQTL 936
Cdd:cd17542   83 GQEEMVKEAIKAGAKDFIVKPFqperVLEAVEKVL 117
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
827-926 8.09e-10

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 57.03  E-value: 8.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANA 906
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80
                         90       100
                 ....*....|....*....|
gi 145698285 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:cd17616   81 DIEDKVKGLGFGADDYMTKP 100
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
827-926 8.68e-10

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: 57.00  E-value: 8.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVIGVTANa 906
Cdd:cd19938    2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFS-DVPIIMVTAR- 79
                         90       100
                 ....*....|....*....|..
gi 145698285 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 1.18e-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: 56.44  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVIGVTANA 906
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARS-NVPVIMVTAKD 79
                         90       100
                 ....*....|....*....|
gi 145698285 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:cd17621   80 SEIDKVVGLELGADDYVTKP 99
PLN03029 PLN03029
type-a response regulator protein; Provisional
818-929 1.50e-09

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 59.28  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 818 AVSDNDDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLS----------------KNH----IDIVLSDVN 877
Cdd:PLN03029   2 GITTESQFHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGlheddrsnpdtpsvspNSHqeveVNLIITDYC 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 145698285 878 MPNMDGYRLTQRIRQLG--LTLPVIGVTANALAEEKQRCLESGMDSCLSKPVTL 929
Cdd:PLN03029  82 MPGMTGYDLLKKIKESSslRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQL 135
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
827-940 1.60e-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: 56.68  E-value: 1.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGY-QCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVI---GV 902
Cdd:cd17530    3 VLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVIlmsGL 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 145698285 903 TANALAEEKQRCLESGMD--SCLSKPVTLDVIKQTLTLYA 940
Cdd:cd17530   83 DGGILESAETLAGANGLNllGTLSKPFSPEELTELLTKYT 122
PRK11517 PRK11517
DNA-binding response regulator HprR;
825-926 2.42e-09

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 58.37  E-value: 2.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 825 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTlPVIGVTA 904
Cdd:PRK11517   1 MKILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQT-PVICLTA 79
                         90       100
                 ....*....|....*....|..
gi 145698285 905 NALAEEKQRCLESGMDSCLSKP 926
Cdd:PRK11517  80 RDSVDDRVRGLDSGANDYLVKP 101
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
584-690 2.47e-09

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 56.07  E-value: 2.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 584 MRLQQVISNLLSNAIK----FTDTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPffqvgtgvqrnFQGTGLGLA 659
Cdd:COG2172   33 DDLVLAVSEAVTNAVRhaygGDPDGPVEVELELDPDGLEIEVRDEGPGFDPEDLPDPYST-----------LAEGGRGLF 101
                         90       100       110
                 ....*....|....*....|....*....|.
gi 145698285 660 ICEKLismMDgDISVDSEPGmGSQFTVRIPL 690
Cdd:COG2172  102 LIRRL---MD-EVEYESDPG-GTTVRLVKRL 127
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
810-926 4.51e-09

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 58.16  E-value: 4.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 810 NALPSTDKAVSdnddmmILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQR 889
Cdd:PRK10710   2 TELPIDENTPR------ILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCRE 75
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 145698285 890 IRQLGlTLPVIGVTANalAEEKQRC--LESGMDSCLSKP 926
Cdd:PRK10710  76 IRRFS-DIPIVMVTAK--IEEIDRLlgLEIGADDYICKP 111
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
827-927 5.65e-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: 54.69  E-value: 5.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLgLTLPVIGVTANA 906
Cdd:cd17622    3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPK-YQGPILLLTALD 81
                         90       100
                 ....*....|....*....|.
gi 145698285 907 LAEEKQRCLESGMDSCLSKPV 927
Cdd:cd17622   82 SDIDHILGLELGADDYVVKPV 102
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
827-932 6.37e-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: 54.60  E-value: 6.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLgLTLPVIGVTANA 906
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQI-SNVPIIFISSRD 79
                         90       100
                 ....*....|....*....|....*.
gi 145698285 907 LAEEKQRCLESGMDSCLSKPVTLDVI 932
Cdd:cd18159   80 DNMDQVMAINMGGDDYITKPFDLDVL 105
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
827-926 7.44e-09

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: 54.35  E-value: 7.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDH-PINRrLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVIGVTAN 905
Cdd:cd17614    1 ILVVDDEkPISD-ILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTS-NVPIIMLTAK 78
                         90       100
                 ....*....|....*....|.
gi 145698285 906 ALAEEKQRCLESGMDSCLSKP 926
Cdd:cd17614   79 DSEVDKVLGLELGADDYVTKP 99
PRK10693 PRK10693
two-component system response regulator RssB;
854-936 8.01e-09

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 58.08  E-value: 8.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 854 ANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANALAEEKQRCLESGMDSCLSKPVT-LDVI 932
Cdd:PRK10693   3 AANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKPVKdLNRL 82

                 ....
gi 145698285 933 KQTL 936
Cdd:PRK10693  83 REMV 86
glnL PRK11073
nitrogen regulation protein NR(II);
457-690 1.13e-08

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 58.17  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 457 QEMAQAAEQasQSKSMFLATVSHELRTPLYGIIGNLDLLQtKELPkgvDRLVTamnnssslllkiisdilDFSKIESEQ- 535
Cdd:PRK11073 119 QEQLQHAQQ--VAARDLVRGLAHEIKNPLGGLRGAAQLLS-KALP---DPALT-----------------EYTKVIIEQa 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 536 --LK-IEPREFSPREVMNHITANYLPLV--VRKQLGLYC-----FI---EPDVPvALNGDPMRLQQVISNLLSNAIKFTD 602
Cdd:PRK11073 176 drLRnLVDRLLGPQRPGTHVTESIHKVAerVVQLVSLELpdnvrLIrdyDPSLP-ELAHDPDQIEQVLLNIVRNALQALG 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 603 T--GCIVLHVRADGDYL----------SIRVRDTGVGIPAKEVVRLFDPFFQVGTGvqrnfqGTGLGLAICEKLISMMDG 670
Cdd:PRK11073 255 PegGTITLRTRTAFQLTlhgeryrlaaRIDIEDNGPGIPPHLQDTLFYPMVSGREG------GTGLGLSIARNLIDQHSG 328
                        250       260
                 ....*....|....*....|
gi 145698285 671 DISVDSEPGMgSQFTVRIPL 690
Cdd:PRK11073 329 KIEFTSWPGH-TEFSVYLPI 347
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
442-690 1.20e-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: 58.76  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  442 VLVDVSSRVKMEE-----SLQEMAQAAEQASQSKSMFLATVsHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSS 516
Cdd:TIGR02938 244 TIADISNLREEQErarlsALQALMAEEERLEAIRETLSAAI-HRLQGPMNLISAAISVLQRRGDDAGNPASAAMLQQALS 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  517 LLLKIISDIldfskieSEQLKIEPREFSPREVMNHITANYLPLVVRKQLGLYCFIE----PDVPvALNGDPMRLQQVISN 592
Cdd:TIGR02938 323 AGREHMEAL-------RQVIPQSPQEIVVPVNLNQILRDVITLSTPRLLAAGIVVDwqpaATLP-AILGRELQLRSLFKA 394
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285  593 LLSNAIKFTDTGC-----IVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQrnfQGTGLGLAICEKLISM 667
Cdd:TIGR02938 395 LVDNAIEAMNIKGwkrreLSITTALNGDLIVVSILDSGPGIPQDLRYKVFEPFFTTKGGSR---KHIGMGLSVAQEIVAD 471
                         250       260
                  ....*....|....*....|...
gi 145698285  668 MDGDISVDSEPGMGSQFTVRIPL 690
Cdd:TIGR02938 472 HGGIIDLDDDYSEGCRIIVEFRV 494
PRK10337 PRK10337
sensor protein QseC; Provisional
473-687 1.23e-08

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 58.51  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 473 FLATVSHELRTPLYGI-----IGNL--DLLQTKE-----LPKGVDRLVtamnnssslllKIISDILDFSKIESE-QLK-I 538
Cdd:PRK10337 240 FTSDAAHELRSPLAALkvqteVAQLsdDDPQARKkallqLHAGIDRAT-----------RLVDQLLTLSRLDSLdNLQdV 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 539 EPREFSP---REVMNHI-TANYLPLVVRKQLglycfiePDVPVALNGDPMRLQQVISNLLSNAIKFTDTG---CIVLHVR 611
Cdd:PRK10337 309 AEIPLEDllqSAVMDIYhTAQQAGIDVRLTL-------NAHPVIRTGQPLLLSLLVRNLLDNAIRYSPQGsvvDVTLNAR 381
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 612 adgdylSIRVRDTGVGIPAKEVVRLFDPFF----QVGTgvqrnfqGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVR 687
Cdd:PRK10337 382 ------NFTVRDNGPGVTPEALARIGERFYrppgQEAT-------GSGLGLSIVRRIAKLHGMNVSFGNAPEGGFEAKVS 448
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
582-689 1.28e-08

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


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 53.70  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 582 DPMRLQQVISNLLSNAI-----KFTDTGCIVLHVRADGDY-LSIRVRDTGVGIPAKEVVRLFDPFfqvgtgVQRNFQGTG 655
Cdd:cd16944    1 DTTQISQVLTNILKNAAeaiegRPSDVGEVRIRVEADQDGrIVLIVCDNGKGFPREMRHRATEPY------VTTRPKGTG 74
                         90       100       110
                 ....*....|....*....|....*....|....
gi 145698285 656 LGLAICEKLISMMDGDISVDSEPGMGSQFTVRIP 689
Cdd:cd16944   75 LGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
594-689 1.45e-08

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: 52.56  E-value: 1.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 594 LSNAIKFTDTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRlfdpffqvgtgvqrnfqGTGLGLAICEKLISMMDGDIS 673
Cdd:cd16917    9 LTNALKHAGASRVRVTLSYTADELTLTVVDDGVGFDGPAPPG-----------------GGGFGLLGMRERAELLGGTLT 71
                         90
                 ....*....|....*.
gi 145698285 674 VDSEPGMGSQFTVRIP 689
Cdd:cd16917   72 IGSRPGGGTRVTARLP 87
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
593-690 1.67e-08

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 58.11  E-value: 1.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 593 LLSNAIKF-----TDTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGtgvqrnfQGTGLGLAICEKLISM 667
Cdd:COG2972  344 LVENAIEHgiepkEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLLEELSSKG-------EGRGIGLRNVRERLKL 416
                         90       100
                 ....*....|....*....|....*.
gi 145698285 668 MDGD---ISVDSEPGMGSQFTVRIPL 690
Cdd:COG2972  417 YYGEeygLEIESEPGEGTTVTIRIPL 442
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
603-689 1.76e-08

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


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 54.90  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 603 TGCIVLHVRADGDYLSIRVRDTGVGIpAKEVVR-------------------------LFDPFFQVGTGVQrNFQGTGLG 657
Cdd:cd16916   69 EGTITLRAEHQGNQVVIEVSDDGRGI-DREKIRekaierglitadeaatlsddevlnlIFAPGFSTAEQVT-DVSGRGVG 146
                         90       100       110
                 ....*....|....*....|....*....|..
gi 145698285 658 LAICEKLISMMDGDISVDSEPGMGSQFTVRIP 689
Cdd:cd16916  147 MDVVKRSIESLGGTIEVESEPGQGTTFTIRLP 178
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
825-936 2.24e-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: 2.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 825 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVT- 903
Cdd:cd17563    1 KSLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTg 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 145698285 904 ----ANALAEEKqrcleSGMDSCLSKPVTLDVIKQTL 936
Cdd:cd17563   81 yasiATAVEAIK-----LGADDYLAKPADADEILAAL 112
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
825-944 3.19e-08

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 56.70  E-value: 3.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 825 MMI--LVVDDHPINRRLLADQLGS------LGyqckTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT 896
Cdd:PRK00742   2 MKIrvLVVDDSAFMRRLISEILNSdpdievVG----TAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRPT 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145698285 897 lPVIGVTanAL----AEEKQRCLESGMDSCLSKPVT-----LDVIKQTLtlyAERVR 944
Cdd:PRK00742  78 -PVVMVS--SLtergAEITLRALELGAVDFVTKPFLgislgMDEYKEEL---AEKVR 128
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
827-936 4.87e-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: 52.26  E-value: 4.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGY-QCKTANDGVDALNVLSKNHIDIVLSDVNMPN-MDGYRLTQRIRQLGLTLP---VIG 901
Cdd:cd17589    1 FLIVDDQPTFRSMLKSMLRSLGVtRIDTASSGEEALRMCENKTYDIVLCDYNLGKgKNGQQLLEELRHKKLISPstvFIM 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 145698285 902 VTANALAEEKQRCLESGMDSCLSKPVTLDVIKQTL 936
Cdd:cd17589   81 VTGESSRAMVLSALELEPDDYLLKPFTVSELRERL 115
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
827-904 5.02e-08

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 52.15  E-value: 5.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGY--QCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTA 904
Cdd:cd17532    1 ALIVDDEPLAREELRYLLEEHPDieIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFVTA 80
fixJ PRK09390
response regulator FixJ; Provisional
823-949 5.17e-08

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 54.24  E-value: 5.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 823 DDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGV 902
Cdd:PRK09390   2 DKGVVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVM 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 145698285 903 TANA---LAEEKQRcleSGMDSCLSKP----VTLDVIKQTLTLYAERVRKSRDS 949
Cdd:PRK09390  82 TGHGdvpLAVEAMK---LGAVDFIEKPfedeRLIGAIERALAQAPEAAKSEAVA 132
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
827-926 6.50e-08

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: 51.35  E-value: 6.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANA 906
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80
                         90       100
                 ....*....|....*....|
gi 145698285 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:cd19928   81 TLMTAVKAAERGAFEYLPKP 100
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
827-926 9.29e-08

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: 50.86  E-value: 9.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLS--KNHIDIVLSDVNMPNMDGYRLTQRI-RQLGL-TLPVIGV 902
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEdeQNEIDLILTEVDLPVSSGFKLLSYImRHKICkNIPVIMM 80
                         90       100
                 ....*....|....*....|....
gi 145698285 903 TANALAEEKQRCLESGMDSCLSKP 926
Cdd:cd17582   81 SSQDSVGVVFKCLSKGAADYLVKP 104
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
827-926 1.07e-07

phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is part of MtrA/MtrB (or MtrAB), a highly conserved two-component system (TCS) implicated in the regulation of cell division in the actinobacteria. In unicellular Mycobacterium tuberculosis, MtrAB coordinates DNA replication with cell division and regulates the transcription of resuscitation-promoting factor B. In filamentous Streptomyces venezuelae, it links antibiotic production to sporulation. MtrA belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 51.32  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVIGVTANA 906
Cdd:cd17626    3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAES-GVPIVMLTAKS 81
                         90       100
                 ....*....|....*....|
gi 145698285 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:cd17626   82 DTVDVVLGLESGADDYVAKP 101
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
827-929 1.70e-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: 50.52  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVIGVTANA 906
Cdd:cd17594    2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARS-DVPIIIISGDR 80
                         90       100
                 ....*....|....*....|....
gi 145698285 907 LAEE-KQRCLESGMDSCLSKPVTL 929
Cdd:cd17594   81 RDEIdRVVGLELGADDYLAKPFGL 104
HATPase_YpdA-YehU-LytS-like cd16924
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
583-689 1.91e-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: 50.14  E-value: 1.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 583 PMRLQQVISNLLSNAI-KFTDTGCIVLHVRADGDYLSIRVRDTGVGIPAKevvrlfdpffQVGTGVQRNFQGTGLGLAIC 661
Cdd:cd16924    3 PFTLQPLVENAIQHGLsPLTDKGVVTISALKEDNHVMIEVEDNGRGIDPK----------VLNILGKKPKEGNGIGLYNV 72
                         90       100       110
                 ....*....|....*....|....*....|.
gi 145698285 662 EKLISMMDGD---ISVDSEPGMGSQFTVRIP 689
Cdd:cd16924   73 HQRLILLFGEdygIHIASEPDKGTRITFTIP 103
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
827-926 2.14e-07

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 52.88  E-value: 2.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSkNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTlPVIGVTANA 906
Cdd:PRK10955   4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLD-DSIDLLLLDVMMPKKNGIDTLKELRQTHQT-PVIMLTARG 81
                         90       100
                 ....*....|....*....|
gi 145698285 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:PRK10955  82 SELDRVLGLELGADDYLPKP 101
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
593-693 2.55e-07

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 53.08  E-value: 2.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 593 LLSNAIKFTDTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVrlfdpffqvgtgvqrnfqGTGLGLAICEKLISMMDGDI 672
Cdd:COG4585  170 ALTNALKHAGATRVTVTLEVDDGELTLTVRDDGVGFDPEAAP------------------GGGLGLRGMRERAEALGGTL 231
                         90       100
                 ....*....|....*....|.
gi 145698285 673 SVDSEPGMGSQFTVRIPLYGA 693
Cdd:COG4585  232 TIGSAPGGGTRVRATLPLAAA 252
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
827-927 3.03e-07

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


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 50.06  E-value: 3.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLgLTLPVIGVTANa 906
Cdd:cd19939    2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREH-SHVPILMLTAR- 79
                         90       100
                 ....*....|....*....|...
gi 145698285 907 lAEEKQRCL--ESGMDSCLSKPV 927
Cdd:cd19939   80 -TEEMDRVLglEMGADDYLCKPF 101
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
827-928 4.80e-07

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 51.64  E-value: 4.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLT--LPVIGVTA 904
Cdd:PRK10161   5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTrdIPVVMLTA 84
                         90       100
                 ....*....|....*....|....
gi 145698285 905 NALAEEKQRCLESGMDSCLSKPVT 928
Cdd:PRK10161  85 RGEEEDRVRGLETGADDYITKPFS 108
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
822-925 4.82e-07

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 51.57  E-value: 4.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 822 NDDMMILVVDDHPINRR------LLADQLGSLGyqckTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGL 895
Cdd:PRK10651   4 QEPATILLIDDHPMLRTgvkqliSMAPDITVVG----EASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSL 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 145698285 896 TLPVIGVTANALAEEKQRCLESGMDSCLSK 925
Cdd:PRK10651  80 SGRIVVFSVSNHEEDVVTALKRGADGYLLK 109
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
582-688 5.91e-07

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


Pssm-ID: 340434 [Multi-domain]  Cd Length: 107  Bit Score: 49.00  E-value: 5.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 582 DPMRLQQVISNLLSNAIKFTDTGCIV-LHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGvqRNFQG-TGLGLA 659
Cdd:cd16975    1 DTLLLSRALINIISNACQYAPEGGTVsISIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTS--RRSGGhYGMGLY 78
                         90       100
                 ....*....|....*....|....*....
gi 145698285 660 ICEKLISMMDGDISVDSEPGMGSQFTVRI 688
Cdd:cd16975   79 IAKNLVEKHGGSLIIENSQKGGAEVTVKI 107
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
827-926 7.40e-07

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 48.52  E-value: 7.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGL--TLPVIGVTA 904
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSAlkDTPIIMLTG 80
                         90       100
                 ....*....|....*....|..
gi 145698285 905 NALAEEKQRCLESGMDSCLSKP 926
Cdd:cd17602   81 KDGLVDRIRAKMAGASGYLTKP 102
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
825-926 2.08e-06

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 49.92  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 825 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTA 904
Cdd:PRK09836   1 MKLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTA 80
                         90       100
                 ....*....|....*....|..
gi 145698285 905 NALAEEKQRCLESGMDSCLSKP 926
Cdd:PRK09836  81 LGTIEHRVKGLELGADDYLVKP 102
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
827-927 2.73e-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: 46.88  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLA-----DQLGSLgyqCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIG 901
Cdd:cd17565    1 FYIVDDDKNIIKILSdiiedDDLGEV---VGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIM 77
                         90       100
                 ....*....|....*....|....*.
gi 145698285 902 VTANALAEEKQRCLESGMDSCLSKPV 927
Cdd:cd17565   78 ISQVSDKEMIGKAYQAGIEFFINKPI 103
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
584-689 4.64e-06

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: 47.03  E-value: 4.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 584 MRLQQVISNLLSNAIK--FTD--TGCIVLHVRADGDYLSIRVRDTGVGIPakevvrlfdpffQVGTGVQRNfqgtGLGLA 659
Cdd:cd16951   38 TAIGLVVNELLQNALKhaFSDreGGTITIRSVVDGDYLRITVIDDGVGLP------------QDEDWPNKG----SLGLQ 101
                         90       100       110
                 ....*....|....*....|....*....|.
gi 145698285 660 ICEKLIS-MMDGDISVDSEpGMGSQFTVRIP 689
Cdd:cd16951  102 IVRSLVEgELKAFLEVQSA-ENGTRVNIDIP 131
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
827-937 6.19e-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: 46.19  E-value: 6.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLAdQLGSLGYQCKT---ANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVT 903
Cdd:cd19931    1 VLLIDDHPLLRKGIK-QLIELDPDFTVvgeASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILT 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 145698285 904 ANALAEEKQRCLESGMDSCLSK---PVTL-DVIKQTLT 937
Cdd:cd19931   80 VSDAEDDVVTALRAGADGYLLKdmePEDLlEALKQAAS 117
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
853-936 9.33e-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: 45.73  E-value: 9.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 853 TANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANALAEEKQRCLESGMDSCLSKPVTLDVI 932
Cdd:cd19930   29 QASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTTFGRPGYFRRALAAGVDGYVLKDRPIEEL 108

                 ....
gi 145698285 933 KQTL 936
Cdd:cd19930  109 ADAI 112
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
827-944 1.31e-05

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 47.15  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLAdQLGSLGYQCKT---ANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVT 903
Cdd:PRK10403   9 VLIVDDHPLMRRGVR-QLLELDPGFEVvaeAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQIIILT 87
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 145698285 904 ANALAEEKQRCLESGMDSCL---SKP-VTLDVIKQTLT---LYAERVR 944
Cdd:PRK10403  88 VSDASSDVFALIDAGADGYLlkdSDPeVLLEAIRAGAKgskVFSERVN 135
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
827-932 1.36e-05

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 45.11  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANA 906
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSDNP 80
                         90       100
                 ....*....|....*....|....*.
gi 145698285 907 LAEEKQRCLESGMDSCLSKPVTLDVI 932
Cdd:cd17573   81 KTEQEIEAFKEGADDYIAKPFDFKVL 106
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
580-688 1.39e-05

Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine/threonine-protein kinase RsbT, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of Bacillus subtilis serine/threonine-protein kinase RsbT, a component of the stressosome signaling complex of Bacillus subtilis. The stressosome is formed from multiple copies of three proteins, a sensor protein RsbR, a scaffold protein RsbS, and RsbT, and responds to environmental changes by initiating a protein partner switching cascade. Stress perception increases the phosphorylation of RsbR and RsbS, by RsbT. Subsequent dissociation of RsbT from the stressosome activates the sigma-B cascade, leading to the release of the alternative sigma factor, sigma-B.


Pssm-ID: 340411 [Multi-domain]  Cd Length: 117  Bit Score: 45.05  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 580 NGDPMRLQQVISNLLSNAIKFTDTGCIVLHVRADGDY--LSIRVRDTGVGIPAKEVVRLfDPFFQVGtgvqrnfqGTGLG 657
Cdd:cd16934   20 EVRQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGRvaLEILAVDQGPGIADVDEALR-DGFSTGG--------GLGLG 90
                         90       100       110
                 ....*....|....*....|....*....|.
gi 145698285 658 LAICEKLIsmmdGDISVDSEPGMGSQFTVRI 688
Cdd:cd16934   91 LGGVRRLA----DEFDLHSAPGRGTVVVARK 117
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
588-699 1.89e-05

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 48.48  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 588 QVISNLLSNAIKFtdtgC---IVLHVRADGDYLSIRVRDTGVGIP--AKEVVrlfdpfFQVGTGVQRNFQGTGLGLAICE 662
Cdd:PRK10815 381 EVMGNVLDNACKY----ClefVEISARQTDEHLHIVVEDDGPGIPesKRELI------FDRGQRADTLRPGQGLGLSVAR 450
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 145698285 663 KLISMMDGDISVDSEPGMGSQFTVripLYGAQYPQKK 699
Cdd:PRK10815 451 EITEQYEGKISAGDSPLGGARMEV---IFGRQHSTPK 484
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
825-904 2.51e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 47.57  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 825 MMILVVDDHPINRRLLADQLGSL-GYQ-CKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTlPVIGV 902
Cdd:PRK12555   1 MRIGIVNDSPLAVEALRRALARDpDHEvVWVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAERPC-PILIV 79

                 ..
gi 145698285 903 TA 904
Cdd:PRK12555  80 TS 81
PRK11173 PRK11173
two-component response regulator; Provisional
827-926 3.11e-05

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 46.55  E-value: 3.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVIGVTANA 906
Cdd:PRK11173   6 ILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQA-NVALMFLTGRD 84
                         90       100
                 ....*....|....*....|
gi 145698285 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:PRK11173  85 NEVDKILGLEIGADDYITKP 104
PRK13560 PRK13560
hypothetical protein; Provisional
571-693 3.15e-05

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 47.74  E-value: 3.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 571 IEPDVPVALngdpmrlqqVISNLLSNAIK--FTDTGC--IVLHVRADGD-YLSIRVRDTGVGIPAKevvrlFDpFFQVGT 645
Cdd:PRK13560 706 IDKAIPCGL---------IISELLSNALKhaFPDGAAgnIKVEIREQGDgMVNLCVADDGIGLPAG-----FD-FRAAET 770
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 145698285 646 gvqrnfqgtgLGLAICEKLISMMDGDISVDSEpgMGSQFTVRIPLYGA 693
Cdd:PRK13560 771 ----------LGLQLVCALVKQLDGEIALDSR--GGARFNIRFPMSPA 806
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
825-926 3.84e-05

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 46.11  E-value: 3.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 825 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTA 904
Cdd:PRK11083   4 PTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFLTA 83
                         90       100
                 ....*....|....*....|....
gi 145698285 905 NalAEEKQRC--LESGMDSCLSKP 926
Cdd:PRK11083  84 R--SDEVDRLvgLEIGADDYVAKP 105
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
603-690 4.12e-05

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 47.48  E-value: 4.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 603 TGCIVLHVRADGDYLSIRVRDTGVGI-PAK----------------------EVVRL-FDPFF----QVgtgvqRNFQGT 654
Cdd:COG0643  308 TGTITLSAYHEGGRVVIEVSDDGRGLdLEKirakaiekglitaeeaaalsdeELLELiFAPGFstaeEV-----TDLSGR 382
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 145698285 655 GLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIPL 690
Cdd:COG0643  383 GVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPL 418
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
571-689 5.12e-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: 44.64  E-value: 5.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 571 IEPDVPVALNGDPMRLQQVISNLLSNA----IKFTDTGC-----IVLHVRADGDYLSIRVRDTGVGIPAKEVVRLF---- 637
Cdd:cd16929   29 IEGDPSIRFPYVPSHLYYILFELLKNAmratVESHGDDSddlppIKVTVAKGDEDLTIKISDRGGGIPREDLARLFsymy 108
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145698285 638 --------DPFFQVGTGVQRNF-QGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIP 689
Cdd:cd16929  109 stapqpslDDFSDLISGTQPSPlAGFGYGLPMSRLYAEYFGGDLDLQSMEGYGTDVYIYLK 169
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
825-925 7.48e-05

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 44.89  E-value: 7.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 825 MMILVVDDHPINRRLLADQLGSLGYQCKTA-NDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVT 903
Cdd:PRK09958   1 MNAIIIDDHPLAIAAIRNLLIKNDIEILAElTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIVS 80
                         90       100
                 ....*....|....*....|..
gi 145698285 904 ANALAEEKQRCLESGMDSCLSK 925
Cdd:PRK09958  81 AKNDHFYGKHCADAGANGFVSK 102
PRK09483 PRK09483
response regulator; Provisional
827-890 7.62e-05

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 45.10  E-value: 7.62e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINR----RLLADQLG--SLGyqckTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRI 890
Cdd:PRK09483   4 VLLVDDHELVRagirRILEDIKGikVVG----EACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKI 69
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
589-679 1.07e-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: 41.87  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 589 VISNLLSNAIKFTDTGC----IVLHVRADGDYLSIRVRDTGVGIPakeVVRLFDPffqvgtgvQRNFQGTGLGLAICEKL 664
Cdd:cd16936    4 AVSEAVTNAVRHAYRHDgpgpVRLELDLDPDRLRVEVTDSGPGFD---PLRPADP--------DAGLREGGRGLALIRAL 72
                         90
                 ....*....|....*
gi 145698285 665 ismMDgDISVDSEPG 679
Cdd:cd16936   73 ---MD-EVGYRRTPG 83
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
827-925 1.34e-04

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 44.10  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINR---RLLADQLGSLGYQCKTaNDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVT 903
Cdd:PRK09935   6 VIIMDTHPIIRmsiEVLLQKNSELQIVLKT-DDYRITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQSTVKVLFLS 84
                         90       100
                 ....*....|....*....|..
gi 145698285 904 ANALAEEKQRCLESGMDSCLSK 925
Cdd:PRK09935  85 SKSECFYAGRAIQAGANGFVSK 106
PRK10336 PRK10336
two-component system response regulator QseB;
825-929 1.50e-04

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 44.12  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 825 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTA 904
Cdd:PRK10336   1 MRILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTA 80
                         90       100
                 ....*....|....*....|....*
gi 145698285 905 NALAEEKQRCLESGMDSCLSKPVTL 929
Cdd:PRK10336  81 RDALAERVEGLRLGADDYLCKPFAL 105
PRK10430 PRK10430
two-component system response regulator DcuR;
827-942 2.11e-04

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 43.94  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHP----INRRLLAdQLGslGYQC-KTANDGVDALNVL--SKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPV 899
Cdd:PRK10430   4 VLIVDDDAmvaeLNRRYVA-QIP--GFQCcGTASTLEQAKEIIfnSDTPIDLILLDIYMQQENGLDLLPVLHEAGCKSDV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 145698285 900 IGVTANALAEEKQRCLESGMDSCLSKPVTLDVIKQTLTLYAER 942
Cdd:PRK10430  81 IVISSAADAATIKDSLHYGVVDYLIKPFQASRFEEALTGWRQK 123
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
827-891 2.42e-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: 2.42e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145698285 827 ILVVDDHPIN----RRLLADQlgslgYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIR 891
Cdd:cd17596    3 ILVVDDEVRSlealRRTLEED-----FDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVR 66
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
853-926 3.54e-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: 41.05  E-value: 3.54e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145698285 853 TANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQL-GLTLP-VIGVTanALAEEK--QRCLESGMDSCLSKP 926
Cdd:cd17561   32 VAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMrLEKRPkIIMLT--AFGQEDitQRAVELGASYYILKP 107
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
827-926 6.10e-04

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 42.48  E-value: 6.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 827 ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGlTLPVIGVTANA 906
Cdd:PRK10529   4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQWS-AIPVIVLSARS 82
                         90       100
                 ....*....|....*....|
gi 145698285 907 LAEEKQRCLESGMDSCLSKP 926
Cdd:PRK10529  83 EESDKIAALDAGADDYLSKP 102
HATPase_SpoIIAB-like cd16942
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ...
586-687 8.60e-04

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: 40.60  E-value: 8.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 586 LQQVISNLLSNAI----KFTDTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRlfDPFFQVGTGVQRnfqgTGLGLAIC 661
Cdd:cd16942   39 IKTVVSEAVTNAIihgyNNDPNGIVSISVIIEDGVVHLTVRDEGVGIPDIEEAR--QPLFTTKPELER----SGMGFTIM 112
                         90       100
                 ....*....|....*....|....*.
gi 145698285 662 EkliSMMDgDISVDSEPGMGSQFTVR 687
Cdd:cd16942  113 E---NFMD-EVIVESEVNKGTTVYLK 134
HATPase_LytS-like cd16957
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
583-689 8.67e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis LytS and Staphylococcus aureus LytS; 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. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), and a GAF sensor domain; most contain a DUF3816 domain.


Pssm-ID: 340433 [Multi-domain]  Cd Length: 106  Bit Score: 39.72  E-value: 8.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 583 PMRLQQVISNLLSNAIKFTDTGC-IVLHVRADGDYLSIRVRDTGVGIPaKEVVRlfdpffQVGTGVQRNFQGTGLGLA-I 660
Cdd:cd16957    3 PFALQVLVENAIRHAFPKRKENNeVRVVVKKDQHKVHVSVSDNGQGIP-EERLD------LLGKTTVTSEKGTGTALEnL 75
                         90       100       110
                 ....*....|....*....|....*....|.
gi 145698285 661 CEKLISMM--DGDISVDSEPGMGSQFTVRIP 689
Cdd:cd16957   76 NRRLIGLFgsEACLHIESEVHGGTEVWFVIP 106
PAS COG2202
PAS domain [Signal transduction mechanisms];
349-483 6.80e-03

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 39.62  E-value: 6.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145698285 349 ALRLEEHEQFNRKIVASAPVGICILrTADGVNILSN------------ELAHTYLNMLTHED-----RQRLTQIICGQQV 411
Cdd:COG2202    3 EEALEESERRLRALVESSPDAIIIT-DLDGRILYVNpaferltgysaeELLGKTLRDLLPPEdddefLELLRAALAGGGV 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145698285 412 NFVDV--LTSNNTNLQISFVHSRYRNEN----VAICVLVDVSSRVKMEESLQEMAQAAEQASQSKSMFLATVSHELRT 483
Cdd:COG2202   82 WRGELrnRRKDGSLFWVELSISPVRDEDgeitGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRI 159
 
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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