NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|489048494|ref|WP_002958711|]
View 

MULTISPECIES: two-component sensor histidine kinase BarA [Pseudoalteromonas]

Protein Classification

sensor histidine kinase family protein( domain architecture ID 1001650)

sensor histidine kinase family protein, part of a two-component regulatory system, functions as a protein kinase that phosphorylates a target protein in response to various signals; may be a hybrid sensor histidine kinase/response regulator

CATH:  3.30.565.10
EC:  2.7.13.3
PubMed:  10637609|10339418
SCOP:  4001957

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK11107 super family cl35992
hybrid sensory histidine kinase BarA; Provisional
1-917 0e+00

hybrid sensory histidine kinase BarA; Provisional


The actual alignment was detected with superfamily member PRK11107:

Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 1303.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494   1 MTKLGLRDSVLTLTLIPTVIIGLLLGGYFTINRYIELDEILYQQGTTISEPLAIALEQPMLEKNKQLLNRLISYTHNKHS 80
Cdd:PRK11107   1 MTKYSLRARVMILILAPTLLIGLLLSSFFVVNRYNELQRQLIDAGASIIEPLAIASEYGMTLQNRESVRQLISVLHRRHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  81 PTIKSIAIFDKNNALLMTSNYHRSFEKLISQKTLINLKTTHVQKSDELVTFFTPIINHTSHDSKWDPSAFQSS---LGTV 157
Cdd:PRK11107  81 DIVRSIAVFDENNQLFVTSNYHLDFESMRLPEGLPIPRLLSVERDGDSLILRTPIISESYSPDESASSDAKNSqnmLGYI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 158 IIQLNKDQAVIGQQRALLISGIVIILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLNDNMIGEFELLREGL 237
Cdd:PRK11107 161 AIELDLKSVRLQQYREIFIAFLMLLLGIGLALLFAFRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGNMLGELDMLKNGI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 238 NTIAHTMVMQKDEMQKNIDQATSDYRETLEQYETSNIELSFAKKEAQDANRVKSDFLAKMSHELRTPLNGVIGFTRQLYK 317
Cdd:PRK11107 241 NAMAMSLSAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 318 TPLNKHQKDYLDTIMLSANSLMTIISDILDFSKLEAGAMELESIQFQLRDAVNEVMTLLAPSAHDKQLELSIYINQQVPD 397
Cdd:PRK11107 321 TPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPD 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 398 DLTGDPTRFKQVLINLLSNAIKFTEKGSIKVDISHRLLDDERTSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFG 477
Cdd:PRK11107 401 NVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHG 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 478 GTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTFNSVFSLPNHVFTNDLPTKSLIGKRILYLEPHEHTHHAVLSLLTQWE 557
Cdd:PRK11107 481 GTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPNPIIDGLPTDCLAGKRLLYVEPNSAAAQATLDILSETP 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 558 SNVTACFNETSFldaiknTEHKYDVCLIGH-MASVDDMQQLKSYVKAVRESTDYLYLMLNTVSHNMREAFIGSGADACLS 636
Cdd:PRK11107 561 LEVTYSPTLSQL------PEAHYDILLLGLpVTFREPLTMLHERLAKAKSMTDFLILALPCHEQVLAEQLKQDGADACLS 634
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 637 KPLNHRKLCEVLAAPYRLDHPtHNIEQNDQALLPLKVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYD 716
Cdd:PRK11107 635 KPLSHTRLLPALLEPCHHKQP-PLLPPTDESRLPLTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFD 713
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 717 IIFMDIQMPIMDGITACKLIQESSLNEDTPIIAVTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIISDHSPQTPVNRD 796
Cdd:PRK11107 714 LILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKPGPKFTSR 793
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 797 KAKTDtPQSPAPFQSSRIDWAQALQRAGGKSELALEMLNMLLLSVPETLTLLAKAIESNDCQQVLSIVHKFHGACCYTGV 876
Cdd:PRK11107 794 VVAPE-PPEPVHFPNATLDWQLALRQAAGKPDLARDMLQMLLDFLPEVRNKVEEALAGEDPEGLLDLIHKLHGSCSYSGV 872
                        890       900       910       920
                 ....*....|....*....|....*....|....*....|.
gi 489048494 877 PKLKSLAETIETSLKNKCLLENIEPELFELQDELENLLADA 917
Cdd:PRK11107 873 PRLKKLCQLIEQQLRSGTSVEDLEPELLELLDEMENVARAA 913
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
1-917 0e+00

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 1303.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494   1 MTKLGLRDSVLTLTLIPTVIIGLLLGGYFTINRYIELDEILYQQGTTISEPLAIALEQPMLEKNKQLLNRLISYTHNKHS 80
Cdd:PRK11107   1 MTKYSLRARVMILILAPTLLIGLLLSSFFVVNRYNELQRQLIDAGASIIEPLAIASEYGMTLQNRESVRQLISVLHRRHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  81 PTIKSIAIFDKNNALLMTSNYHRSFEKLISQKTLINLKTTHVQKSDELVTFFTPIINHTSHDSKWDPSAFQSS---LGTV 157
Cdd:PRK11107  81 DIVRSIAVFDENNQLFVTSNYHLDFESMRLPEGLPIPRLLSVERDGDSLILRTPIISESYSPDESASSDAKNSqnmLGYI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 158 IIQLNKDQAVIGQQRALLISGIVIILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLNDNMIGEFELLREGL 237
Cdd:PRK11107 161 AIELDLKSVRLQQYREIFIAFLMLLLGIGLALLFAFRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGNMLGELDMLKNGI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 238 NTIAHTMVMQKDEMQKNIDQATSDYRETLEQYETSNIELSFAKKEAQDANRVKSDFLAKMSHELRTPLNGVIGFTRQLYK 317
Cdd:PRK11107 241 NAMAMSLSAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 318 TPLNKHQKDYLDTIMLSANSLMTIISDILDFSKLEAGAMELESIQFQLRDAVNEVMTLLAPSAHDKQLELSIYINQQVPD 397
Cdd:PRK11107 321 TPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPD 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 398 DLTGDPTRFKQVLINLLSNAIKFTEKGSIKVDISHRLLDDERTSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFG 477
Cdd:PRK11107 401 NVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHG 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 478 GTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTFNSVFSLPNHVFTNDLPTKSLIGKRILYLEPHEHTHHAVLSLLTQWE 557
Cdd:PRK11107 481 GTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPNPIIDGLPTDCLAGKRLLYVEPNSAAAQATLDILSETP 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 558 SNVTACFNETSFldaiknTEHKYDVCLIGH-MASVDDMQQLKSYVKAVRESTDYLYLMLNTVSHNMREAFIGSGADACLS 636
Cdd:PRK11107 561 LEVTYSPTLSQL------PEAHYDILLLGLpVTFREPLTMLHERLAKAKSMTDFLILALPCHEQVLAEQLKQDGADACLS 634
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 637 KPLNHRKLCEVLAAPYRLDHPtHNIEQNDQALLPLKVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYD 716
Cdd:PRK11107 635 KPLSHTRLLPALLEPCHHKQP-PLLPPTDESRLPLTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFD 713
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 717 IIFMDIQMPIMDGITACKLIQESSLNEDTPIIAVTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIISDHSPQTPVNRD 796
Cdd:PRK11107 714 LILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKPGPKFTSR 793
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 797 KAKTDtPQSPAPFQSSRIDWAQALQRAGGKSELALEMLNMLLLSVPETLTLLAKAIESNDCQQVLSIVHKFHGACCYTGV 876
Cdd:PRK11107 794 VVAPE-PPEPVHFPNATLDWQLALRQAAGKPDLARDMLQMLLDFLPEVRNKVEEALAGEDPEGLLDLIHKLHGSCSYSGV 872
                        890       900       910       920
                 ....*....|....*....|....*....|....*....|.
gi 489048494 877 PKLKSLAETIETSLKNKCLLENIEPELFELQDELENLLADA 917
Cdd:PRK11107 873 PRLKKLCQLIEQQLRSGTSVEDLEPELLELLDEMENVARAA 913
BarA5 COG4999
Uncharacterized domain of signal transduction histidine kinase BarA [Signal transduction ...
1-917 8.97e-175

Uncharacterized domain of signal transduction histidine kinase BarA [Signal transduction mechanisms];


Pssm-ID: 444023 [Multi-domain]  Cd Length: 921  Bit Score: 531.11  E-value: 8.97e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494   1 MTKLGLRDSVLTLTLIPTVIIGLLLGGYFTINRYIELDEILYQQGTTISEPLAIALEQPMLEKNKQLLNRLISYTHNKHS 80
Cdd:COG4999    3 MTLRRRRRIILLLLLLLLILLLLLLFFFFFVYRYQLLQQQLSASIIIIIAAAAASSEYLMNKRRREQLLLLLLRRHHRHS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  81 PTIKSIAIFDKNNALLMTSNYHRSFEKLISQKTLINLKTTHVQKSDELVTFFTPIINHTSHDskwDPSAFQSS--LGTVI 158
Cdd:COG4999   83 IIISAIDDNNNLNNLSNNNNNNLNLLLLQLPPPSPPLLLLTRSDLILLLIPPISIIYEDESS---EPSDNTAAnpLGYIA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 159 IQLNKDQAVIGQQRALLISGIVIILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLNDNMIGEFELLREGLN 238
Cdd:COG4999  160 IELDLSSDRLQQYQEQFVATLLLLLLLLLALLFAYRLMRDVTVPITNMVNVVDRIRRRRLDSRVEGGMLGELLLLKNGIN 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 239 TIAHTMVMQKDEMQKNIDQATSDYRETLEQYETSNIELSFAKKEAQDANRVKSDFLAKMSHELRTPLNGVIGFTRQLYKT 318
Cdd:COG4999  240 NMAMSLAAYHEEMQQNIDQATSDLRETLEQLEIQNVELDLAKKRAQEAARAKSEFLANMSHELRTPLNGVIGFTRQTLKT 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 319 PLNKHQKDYLDTIMLSANSLMTIISDILDFSKLEAGAMELESIQFQLRDAVNEVMTLLAPSAHDKQLELSIYINQQVPDD 398
Cdd:COG4999  320 TLTPTQTDYLQTIERSANNLLNIINDILDFSKLEAGKLLLELIPFPFRDTLDEVVVLLALLAHEKGLELTLLLDNDVPED 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 399 LTGDPTRFKQVLINLLSNAIKFTEKGSIKVDISHRLLDDERTSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGG 478
Cdd:COG4999  400 VIGDPLRIQQILQNLLGNAIKFTETGNIDIIVELRTQRQNSVELQVQVRDTGIGISERQQAQLFQAFFQADASISRRRGG 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 479 TGLGLIITKHIVEAMSGRITLNSAPGNGTCFTFNSVFSLPNHVFTND-LPTKSLIGKRILYLEPHEHTHHAVLSLLTQWE 557
Cdd:COG4999  480 TGGGLVITQKLVKEMGGEIGFISRLSQGSTFWFTFFLLLNLAPALSDpLPLDRLQGKRLLYVEPNPAAAQATLDLLSQTP 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 558 SNVTACFNETSFldaiknTEHKYDVCLIGHMAS-VDDMQQLKSYVKAVRESTDYLYLMLNTVSHNMREAFIGSGADACLS 636
Cdd:COG4999  560 LEVTYSPTLEQL------PEAHYDILLIGLPVTyRNTLADLTDKLAQALRMADCVILALPSTAQVLAEQLKAAGARACLS 633
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 637 KPLNHRKLCEVLAAPYRLDHPThNIEQNDQALLPLKVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYD 716
Cdd:COG4999  634 KPLSATRLLPLLLDECLFELPL-PAATPEAPLPPLVVAVVDDNANNLLLIALLLELVVQVVVCCSSGEAAAAAAAQQLDD 712
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 717 IIFMDIQMPIMDGITACKLIQESSLNEDTPIIAVTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIISDH-SPQTPVNR 795
Cdd:COG4999  713 ILIMDIQMPMMDGIAAEEIIRQLPHNNTTPIVAVAAAAAAGREELLLAGGMDDYLAKPIEEELLLLLLLRYqPGPHTVPS 792
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 796 DKAKTDTPQSPAPFQSSR--IDWAQALQRAGGKSELALEMLNMLLLSVPETLTLLAKAIESNDCQqvlsIVHKFHGACCY 873
Cdd:COG4999  793 PPPVPPSLAPLVLLQASQlsLDAAAALQQALDALLLLLELLLLLLLELLEVLILRQEIDLLGALD----LLHGLHSSLLC 868
                        890       900       910       920
                 ....*....|....*....|....*....|....*....|....
gi 489048494 874 TGVPKLKSLAETIETSLKNKCLLENIEPELFELQDELENLLADA 917
Cdd:COG4999  869 SGLLRLKGLLSLQLQLEPEELLLLEEEEELLEELDEELLLESEE 912
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
171-892 4.36e-81

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: 282.44  E-value: 4.36e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  171 QRALLISGIVIILSLVFaaILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLN-------DNMIGEFELLREglnTIAHT 243
Cdd:TIGR02956 330 QFGLLITGMLGLVILVF--IMWRVVYRSVILRLNQHTQALLRLALGDLDISLDargddelAHMGRAIEAFRD---TAAHN 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  244 MVMQKDEMQknIDQATSDYRETLEQ-YETSNIELSF--------------AKKEAQDANRVKSDFLAKMSHELRTPLNGV 308
Cdd:TIGR02956 405 LKLQADERQ--VAQELQEHKESLEQlVAQRTQELAEtnerlnaevknhakARAEAEEANRAKSAFLATMSHEIRTPLNGI 482
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  309 IGFTRQLYKTPLNKHQKDYLDTIMLSANSLMTIISDILDFSKLEAGAMELESIQFQLRDAVNEVMTLLAPSAHDKQLELS 388
Cdd:TIGR02956 483 LGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLR 562
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  389 IYINQQVPDDLTGDPTRFKQVLINLLSNAIKFTEKGSIKVDIShrlLDDERTsLLVSVTDTGVGIPMDKQDSLFTPFGQA 468
Cdd:TIGR02956 563 LNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVS---LNDDSS-LLFEVEDTGCGIAEEEQATLFDAFTQA 638
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  469 DSSitRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTFnsvfslpnhvftndlptksligkrilylephehthha 548
Cdd:TIGR02956 639 DGR--RRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWF------------------------------------- 679
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  549 vlslltqwesnvtacfnetsfldaikntehkydvclighmasvddmqqlksyvkavrestdylylmlntvshnmreafig 628
Cdd:TIGR02956     --------------------------------------------------------------------------------
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  629 sgadaclSKPLNHRKLCEVLAAPYRLDHPthnieqndqallPLKVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYS 708
Cdd:TIGR02956 680 -------TLPLTRGKPAEDSATLTVIDLP------------PQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALE 740
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  709 LSKSHKYDIIFMDIQMPIMDGIT-ACKLIQESSLNEDTPIIAVTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQII--- 784
Cdd:TIGR02956 741 CFHQHAFDLALLDINLPDGDGVTlLQQLRAIYGAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIavi 820
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  785 ---SDHSPQTPVNRDK------AKTDTPQSPAPFQSSRIDW--------AQALQRAGgkSELALEMLNMLLLSVPETLTL 847
Cdd:TIGR02956 821 lagGKSNTEAPVLSASpsfdsaSVIENAQADDIPESNQASEflldeeqlQQDIEVLG--VEKVRQLVALFKTSSAEQLEE 898
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*
gi 489048494  848 LAKAIESNDCQQVLSIVHKFHGACCYTGVPKLKSLAETIETSLKN 892
Cdd:TIGR02956 899 LSAARAVDDDAQIKKLAHKLKGSAGSLGLTQLTQLCQQLEKQGKT 943
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
406-511 8.77e-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: 170.75  E-value: 8.77e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 406 FKQVLINLLSNAIKFTEKGSIKVDISHRLLDDERTSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGGTGLGLII 485
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                         90       100
                 ....*....|....*....|....*.
gi 489048494 486 TKHIVEAMSGRITLNSAPGNGTCFTF 511
Cdd:cd16922   81 SKKLVELMGGDISVESEPGQGSTFTF 106
sCache_4 pfam09984
Single cache domain 4; Members of this family of domains are found in various BarA-like signal ...
31-174 2.13e-47

Single cache domain 4; Members of this family of domains are found in various BarA-like signal transduction histidine kinases, which are involved in the regulation of carbon metabolism via the csrA/csrB regulatory system. The role of this domain has not, as yet, been established.


Pssm-ID: 430966  Cd Length: 146  Bit Score: 165.49  E-value: 2.13e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494   31 INRYIELDEILYQQGTTISEPLAIALEQPMLEKNKQLLNRLISYTHNKHSPTIKSIAIFDKNNALLMTSNYHRSFEKLIS 110
Cdd:pfam09984   1 INRYYELEDQLIDRGTSIIEPLAIASEYGLTTRNRESLRRLISALHRKNSPIVRSIAIFDANNQLFVTSNYHRDFESLRL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489048494  111 QKTLINLKTTHVQKSDELVTFFTPIINHTSHDSKWDPSA--FQSSLGTVIIQLNKDQAVIGQQRAL 174
Cdd:pfam09984  81 PEGAPIPTLTTVEHSGDSLILRTPIISEGLSLPGLPATAesAQRPLGYIAIELNLDSARLQQYREI 146
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
401-511 6.61e-34

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 125.84  E-value: 6.61e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494   401 GDPTRFKQVLINLLSNAIKFTEKGSiKVDIShrlLDDERTSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSiTRKFGGTG 480
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGG-RITVT---LERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGTG 75
                           90       100       110
                   ....*....|....*....|....*....|.
gi 489048494   481 LGLIITKHIVEAMSGRITLNSAPGNGTCFTF 511
Cdd:smart00387  76 LGLSIVKKLVELHGGEISVESEPGGGTTFTI 106
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
170-506 1.36e-28

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 120.32  E-value: 1.36e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 170 QQRALLIsgiVIILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLNDNMIGEFELLREGLNTIAhtmvmqkd 249
Cdd:NF012163 162 QKRASWL---IVALALLLAALAAFLLARGLLAPVKRLVEATHRLAAGDYTTRVTPTSNDELGKLAQDFNQLA-------- 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 250 emqknidqatsdyrETLEQYEtsnielsfakkeaqdanRVKSDFLAKMSHELRTPLnGVIGFTRQLYKTPLNKHQKDYLD 329
Cdd:NF012163 231 --------------STLEKNE-----------------QMRRDFMADISHELRTPL-AVLRAELEAIQDGIRKFTPESLD 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 330 TIMLSANSLMTIISDILDFSKLEAGAMELESIQFQLRDAVNEVMTLLAPSAHDKQLELSIyinqQVPDDLT--GDPTRFK 407
Cdd:NF012163 279 SLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEV----SLPDSSLvfGDRDRLM 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 408 QVLINLLSNAIKFTEKGSiKVDISHRLLDDErtsLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGGTGLGLIITK 487
Cdd:NF012163 355 QLFNNLLENSLRYTDSGG-SLHISASQRPKE---VTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISL 430
                        330
                 ....*....|....*....
gi 489048494 488 HIVEAMSGRITLNSAPGNG 506
Cdd:NF012163 431 NIVQAHGGTLHAAHSPLGG 449
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
178-510 3.74e-23

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


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 102.00  E-value: 3.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 178 GIVIILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLNDNMIGEFEL--LREGLNTIAhtmvmqkdemqkni 255
Cdd:NF012226  63 FTVILCGSVISLIIGMKLAQRFIVPINFLADAAKKISQGDLSARAEDSQIHSAEIseLMHNFNDMA-------------- 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 256 dqatsdyretlEQYETSnielsfaKKEAQDANrvksdflAKMSHELRTP-----------LNGVIGFTRQLYKTPLNK-- 322
Cdd:NF012226 129 -----------QKLESS-------VKNAQVWN-------AAIAHELRTPitilqgrlqgiLDGVFEPDPALFKSLLNQve 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 323 ---HQKDYLDTIMLSANSLMTiisdildfskleagaMELESIQFQlrDAVNEVMTLLAPSAHDKQLElsiyINQQVPDDL 399
Cdd:NF012226 184 glsHLVEDLRTLSLVENQQLR---------------LNYESVDLK--DSIEKVLKMFEDRLEQAQLT----IVLNLTATP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 400 -TGDPTRFKQVLINLLSNAIKFTEKGSIKvdISHRLLDDErtsLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGG 478
Cdd:NF012226 243 vFCDRRRIEQVLIALIDNAIRYANAGKLK--ISSSVIQDD---WILQIEDEGPGIAEEYQQDLFNPFFRLEQSRNKEFGG 317
                        330       340       350
                 ....*....|....*....|....*....|..
gi 489048494 479 TGLGLIITKHIVEAMSGRITLnSAPGNGTCFT 510
Cdd:NF012226 318 TGLGLAVVHAIVIAHKGSIEY-SNSQGNSVFT 348
resp_reg_YycF NF040534
response regulator YycF;
672-774 6.81e-08

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 54.34  E-value: 6.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLH-TLLSEQIEVIeTAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESslnEDTPIIAV 750
Cdd:NF040534   2 KILVVDDEKPIADILEfNLKKEGYEVF-CAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVRKK---YDMPIIML 77
                         90       100
                 ....*....|....*....|....
gi 489048494 751 TAHALQSEKEQLLKDGFKGYLTKP 774
Cdd:NF040534  78 TAKDSEIDKVLGLELGADDYVTKP 101
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
1-917 0e+00

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 1303.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494   1 MTKLGLRDSVLTLTLIPTVIIGLLLGGYFTINRYIELDEILYQQGTTISEPLAIALEQPMLEKNKQLLNRLISYTHNKHS 80
Cdd:PRK11107   1 MTKYSLRARVMILILAPTLLIGLLLSSFFVVNRYNELQRQLIDAGASIIEPLAIASEYGMTLQNRESVRQLISVLHRRHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  81 PTIKSIAIFDKNNALLMTSNYHRSFEKLISQKTLINLKTTHVQKSDELVTFFTPIINHTSHDSKWDPSAFQSS---LGTV 157
Cdd:PRK11107  81 DIVRSIAVFDENNQLFVTSNYHLDFESMRLPEGLPIPRLLSVERDGDSLILRTPIISESYSPDESASSDAKNSqnmLGYI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 158 IIQLNKDQAVIGQQRALLISGIVIILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLNDNMIGEFELLREGL 237
Cdd:PRK11107 161 AIELDLKSVRLQQYREIFIAFLMLLLGIGLALLFAFRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGNMLGELDMLKNGI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 238 NTIAHTMVMQKDEMQKNIDQATSDYRETLEQYETSNIELSFAKKEAQDANRVKSDFLAKMSHELRTPLNGVIGFTRQLYK 317
Cdd:PRK11107 241 NAMAMSLSAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 318 TPLNKHQKDYLDTIMLSANSLMTIISDILDFSKLEAGAMELESIQFQLRDAVNEVMTLLAPSAHDKQLELSIYINQQVPD 397
Cdd:PRK11107 321 TPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPD 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 398 DLTGDPTRFKQVLINLLSNAIKFTEKGSIKVDISHRLLDDERTSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFG 477
Cdd:PRK11107 401 NVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHG 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 478 GTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTFNSVFSLPNHVFTNDLPTKSLIGKRILYLEPHEHTHHAVLSLLTQWE 557
Cdd:PRK11107 481 GTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPNPIIDGLPTDCLAGKRLLYVEPNSAAAQATLDILSETP 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 558 SNVTACFNETSFldaiknTEHKYDVCLIGH-MASVDDMQQLKSYVKAVRESTDYLYLMLNTVSHNMREAFIGSGADACLS 636
Cdd:PRK11107 561 LEVTYSPTLSQL------PEAHYDILLLGLpVTFREPLTMLHERLAKAKSMTDFLILALPCHEQVLAEQLKQDGADACLS 634
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 637 KPLNHRKLCEVLAAPYRLDHPtHNIEQNDQALLPLKVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYD 716
Cdd:PRK11107 635 KPLSHTRLLPALLEPCHHKQP-PLLPPTDESRLPLTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFD 713
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 717 IIFMDIQMPIMDGITACKLIQESSLNEDTPIIAVTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIISDHSPQTPVNRD 796
Cdd:PRK11107 714 LILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKPGPKFTSR 793
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 797 KAKTDtPQSPAPFQSSRIDWAQALQRAGGKSELALEMLNMLLLSVPETLTLLAKAIESNDCQQVLSIVHKFHGACCYTGV 876
Cdd:PRK11107 794 VVAPE-PPEPVHFPNATLDWQLALRQAAGKPDLARDMLQMLLDFLPEVRNKVEEALAGEDPEGLLDLIHKLHGSCSYSGV 872
                        890       900       910       920
                 ....*....|....*....|....*....|....*....|.
gi 489048494 877 PKLKSLAETIETSLKNKCLLENIEPELFELQDELENLLADA 917
Cdd:PRK11107 873 PRLKKLCQLIEQQLRSGTSVEDLEPELLELLDEMENVARAA 913
BarA5 COG4999
Uncharacterized domain of signal transduction histidine kinase BarA [Signal transduction ...
1-917 8.97e-175

Uncharacterized domain of signal transduction histidine kinase BarA [Signal transduction mechanisms];


Pssm-ID: 444023 [Multi-domain]  Cd Length: 921  Bit Score: 531.11  E-value: 8.97e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494   1 MTKLGLRDSVLTLTLIPTVIIGLLLGGYFTINRYIELDEILYQQGTTISEPLAIALEQPMLEKNKQLLNRLISYTHNKHS 80
Cdd:COG4999    3 MTLRRRRRIILLLLLLLLILLLLLLFFFFFVYRYQLLQQQLSASIIIIIAAAAASSEYLMNKRRREQLLLLLLRRHHRHS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  81 PTIKSIAIFDKNNALLMTSNYHRSFEKLISQKTLINLKTTHVQKSDELVTFFTPIINHTSHDskwDPSAFQSS--LGTVI 158
Cdd:COG4999   83 IIISAIDDNNNLNNLSNNNNNNLNLLLLQLPPPSPPLLLLTRSDLILLLIPPISIIYEDESS---EPSDNTAAnpLGYIA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 159 IQLNKDQAVIGQQRALLISGIVIILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLNDNMIGEFELLREGLN 238
Cdd:COG4999  160 IELDLSSDRLQQYQEQFVATLLLLLLLLLALLFAYRLMRDVTVPITNMVNVVDRIRRRRLDSRVEGGMLGELLLLKNGIN 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 239 TIAHTMVMQKDEMQKNIDQATSDYRETLEQYETSNIELSFAKKEAQDANRVKSDFLAKMSHELRTPLNGVIGFTRQLYKT 318
Cdd:COG4999  240 NMAMSLAAYHEEMQQNIDQATSDLRETLEQLEIQNVELDLAKKRAQEAARAKSEFLANMSHELRTPLNGVIGFTRQTLKT 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 319 PLNKHQKDYLDTIMLSANSLMTIISDILDFSKLEAGAMELESIQFQLRDAVNEVMTLLAPSAHDKQLELSIYINQQVPDD 398
Cdd:COG4999  320 TLTPTQTDYLQTIERSANNLLNIINDILDFSKLEAGKLLLELIPFPFRDTLDEVVVLLALLAHEKGLELTLLLDNDVPED 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 399 LTGDPTRFKQVLINLLSNAIKFTEKGSIKVDISHRLLDDERTSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGG 478
Cdd:COG4999  400 VIGDPLRIQQILQNLLGNAIKFTETGNIDIIVELRTQRQNSVELQVQVRDTGIGISERQQAQLFQAFFQADASISRRRGG 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 479 TGLGLIITKHIVEAMSGRITLNSAPGNGTCFTFNSVFSLPNHVFTND-LPTKSLIGKRILYLEPHEHTHHAVLSLLTQWE 557
Cdd:COG4999  480 TGGGLVITQKLVKEMGGEIGFISRLSQGSTFWFTFFLLLNLAPALSDpLPLDRLQGKRLLYVEPNPAAAQATLDLLSQTP 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 558 SNVTACFNETSFldaiknTEHKYDVCLIGHMAS-VDDMQQLKSYVKAVRESTDYLYLMLNTVSHNMREAFIGSGADACLS 636
Cdd:COG4999  560 LEVTYSPTLEQL------PEAHYDILLIGLPVTyRNTLADLTDKLAQALRMADCVILALPSTAQVLAEQLKAAGARACLS 633
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 637 KPLNHRKLCEVLAAPYRLDHPThNIEQNDQALLPLKVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYD 716
Cdd:COG4999  634 KPLSATRLLPLLLDECLFELPL-PAATPEAPLPPLVVAVVDDNANNLLLIALLLELVVQVVVCCSSGEAAAAAAAQQLDD 712
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 717 IIFMDIQMPIMDGITACKLIQESSLNEDTPIIAVTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIISDH-SPQTPVNR 795
Cdd:COG4999  713 ILIMDIQMPMMDGIAAEEIIRQLPHNNTTPIVAVAAAAAAGREELLLAGGMDDYLAKPIEEELLLLLLLRYqPGPHTVPS 792
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 796 DKAKTDTPQSPAPFQSSR--IDWAQALQRAGGKSELALEMLNMLLLSVPETLTLLAKAIESNDCQqvlsIVHKFHGACCY 873
Cdd:COG4999  793 PPPVPPSLAPLVLLQASQlsLDAAAALQQALDALLLLLELLLLLLLELLEVLILRQEIDLLGALD----LLHGLHSSLLC 868
                        890       900       910       920
                 ....*....|....*....|....*....|....*....|....
gi 489048494 874 TGVPKLKSLAETIETSLKNKCLLENIEPELFELQDELENLLADA 917
Cdd:COG4999  869 SGLLRLKGLLSLQLQLEPEELLLLEEEEELLEELDEELLLESEE 912
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
171-892 4.36e-81

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: 282.44  E-value: 4.36e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  171 QRALLISGIVIILSLVFaaILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLN-------DNMIGEFELLREglnTIAHT 243
Cdd:TIGR02956 330 QFGLLITGMLGLVILVF--IMWRVVYRSVILRLNQHTQALLRLALGDLDISLDargddelAHMGRAIEAFRD---TAAHN 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  244 MVMQKDEMQknIDQATSDYRETLEQ-YETSNIELSF--------------AKKEAQDANRVKSDFLAKMSHELRTPLNGV 308
Cdd:TIGR02956 405 LKLQADERQ--VAQELQEHKESLEQlVAQRTQELAEtnerlnaevknhakARAEAEEANRAKSAFLATMSHEIRTPLNGI 482
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  309 IGFTRQLYKTPLNKHQKDYLDTIMLSANSLMTIISDILDFSKLEAGAMELESIQFQLRDAVNEVMTLLAPSAHDKQLELS 388
Cdd:TIGR02956 483 LGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLR 562
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  389 IYINQQVPDDLTGDPTRFKQVLINLLSNAIKFTEKGSIKVDIShrlLDDERTsLLVSVTDTGVGIPMDKQDSLFTPFGQA 468
Cdd:TIGR02956 563 LNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVS---LNDDSS-LLFEVEDTGCGIAEEEQATLFDAFTQA 638
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  469 DSSitRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTFnsvfslpnhvftndlptksligkrilylephehthha 548
Cdd:TIGR02956 639 DGR--RRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWF------------------------------------- 679
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  549 vlslltqwesnvtacfnetsfldaikntehkydvclighmasvddmqqlksyvkavrestdylylmlntvshnmreafig 628
Cdd:TIGR02956     --------------------------------------------------------------------------------
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  629 sgadaclSKPLNHRKLCEVLAAPYRLDHPthnieqndqallPLKVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYS 708
Cdd:TIGR02956 680 -------TLPLTRGKPAEDSATLTVIDLP------------PQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALE 740
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  709 LSKSHKYDIIFMDIQMPIMDGIT-ACKLIQESSLNEDTPIIAVTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQII--- 784
Cdd:TIGR02956 741 CFHQHAFDLALLDINLPDGDGVTlLQQLRAIYGAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIavi 820
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  785 ---SDHSPQTPVNRDK------AKTDTPQSPAPFQSSRIDW--------AQALQRAGgkSELALEMLNMLLLSVPETLTL 847
Cdd:TIGR02956 821 lagGKSNTEAPVLSASpsfdsaSVIENAQADDIPESNQASEflldeeqlQQDIEVLG--VEKVRQLVALFKTSSAEQLEE 898
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*
gi 489048494  848 LAKAIESNDCQQVLSIVHKFHGACCYTGVPKLKSLAETIETSLKN 892
Cdd:TIGR02956 899 LSAARAVDDDAQIKKLAHKLKGSAGSLGLTQLTQLCQQLEKQGKT 943
PRK15347 PRK15347
two component system sensor kinase;
255-785 8.35e-77

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 269.59  E-value: 8.35e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 255 IDQATSDYRETL-EQYET-------SNIELSFAKKEAQDANRVKSDFLAKMSHELRTPLNGVIGFTRQLYKTPLNKHQKD 326
Cdd:PRK15347 355 IAKAYNQLLDTLnEQYDTlenkvaeRTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMD 434
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 327 YLDTIMLSANSLMTIISDILDFSKLEAGAMELESIQFQLRDAVNEVMTLLAPSAHDKQLELSIYINQQVPDDLTGDPTRF 406
Cdd:PRK15347 435 LADTARQCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRL 514
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 407 KQVLINLLSNAIKFTEKGSIKVDISHRlldDERtsLLVSVTDTGVGIPMDKQDSLFTPFGQADSSItrkfGGTGLGLIIT 486
Cdd:PRK15347 515 RQILVNLLGNAVKFTETGGIRLRVKRH---EQQ--LCFTVEDTGCGIDIQQQQQIFTPFYQADTHS----QGTGLGLTIA 585
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 487 KHIVEAMSGRITLNSAPGNGTCFTFnsvfslpnhvftnDLPTKSligkrilYLEPHehthhavlslltqwesnvtaCFNE 566
Cdd:PRK15347 586 SSLAKMMGGELTLFSTPGVGSCFSL-------------VLPLNE-------YAPPE--------------------PLKG 625
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 567 TsfLDAIKntehkydvCLIghmasvddmQQLKSYVKAVRESTDYLYLMLNTVSHnmreaFIGsgadaclskplnhrKLCE 646
Cdd:PRK15347 626 E--LSAPL--------ALH---------RQLSAWGITCQPGHQNPALLDPELAY-----LPG--------------RLYD 667
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 647 VLaapYRLDHPTHNIEQNDQALLP--LKVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQM 724
Cdd:PRK15347 668 LL---QQIIQGAPNEPVINLPLQPwqLQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRM 744
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489048494 725 PIMDGITACKLIQESSLNEDT--PIIAVTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIIS 785
Cdd:PRK15347 745 PGLDGLETTQLWRDDPNNLDPdcMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARALE 807
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
181-511 7.23e-72

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 240.58  E-value: 7.23e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 181 IILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLNDNMIGEFELLREGLNTIAHTMVMQKDEMQKNIDQATS 260
Cdd:COG0642    1 LLLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 261 DYRETLEQYETSNIELSFAKKEAQDANRVKSDFLAKMSHELRTPLNGVIGFTRQLYKTPlNKHQKDYLDTIMLSANSLMT 340
Cdd:COG0642   81 LLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEEL-DEEQREYLETILRSADRLLR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 341 IISDILDFSKLEAGAMELESIQFQLRDAVNEVMTLLAPSAHDKQLELSIYINQQVPdDLTGDPTRFKQVLINLLSNAIKF 420
Cdd:COG0642  160 LINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLSNAIKY 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 421 TEKGSiKVDIShrlLDDERTSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSitRKFGGTGLGLIITKHIVEAMSGRITLN 500
Cdd:COG0642  239 TPEGG-TVTVS---VRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVE 312
                        330
                 ....*....|.
gi 489048494 501 SAPGNGTCFTF 511
Cdd:COG0642  313 SEPGKGTTFTV 323
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
275-518 9.42e-67

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 223.25  E-value: 9.42e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 275 ELSFAKKEAQDANRVKSDFLAKMSHELRTPLNGVIGFTRQL--YKTPLNKHQKDYLDTIMLSANSLMTIISDILDFSKLE 352
Cdd:COG2205    1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLldEEDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 353 AGAMELESIQFQLRDAVNEVMTLLAPSAHDKQLELSIYINQQVPDdLTGDPTRFKQVLINLLSNAIKFTEKGSiKVDISH 432
Cdd:COG2205   81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPL-VYADPELLEQVLANLLDNAIKYSPPGG-TITISA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 433 RLLDDErtsLLVSVTDTGVGIPMDKQDSLFTPFGQADSsiTRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTfn 512
Cdd:COG2205  159 RREGDG---VRISVSDNGPGIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFT-- 231

                 ....*.
gi 489048494 513 svFSLP 518
Cdd:COG2205  232 --VTLP 235
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
149-511 1.07e-64

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 222.89  E-value: 1.07e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 149 AFQSSLGTVIIQLNKDQAVIGQQRALLISGIVIILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLNDNMIG 228
Cdd:COG5002   31 LLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLAL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 229 EFELLREGLNTIAHTMVMQKDEMQKNIDQATSDYRETLEQYETSNIELsfakkeaQDANRVKSDFLAKMSHELRTPLNGV 308
Cdd:COG5002  111 LILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITEL-------ERLEQMRREFVANVSHELRTPLTSI 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 309 IGFTR--QLYKTPLNKHQKDYLDTIMLSANSLMTIISDILDFSKLEAGAMELESIQFQLRDAVNEVMTLLAPSAHDKQLE 386
Cdd:COG5002  184 RGYLEllLDGAADDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIE 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 387 LSIYINQQVPDdLTGDPTRFKQVLINLLSNAIKFTEKGSiKVDIShrlLDDERTSLLVSVTDTGVGIPMDKQDSLFTPFG 466
Cdd:COG5002  264 LELDLPEDPLL-VLGDPDRLEQVLTNLLDNAIKYTPEGG-TITVS---LREEDDQVRISVRDTGIGIPEEDLPRIFERFY 338
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 489048494 467 QADSSITRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTF 511
Cdd:COG5002  339 RVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTI 383
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
282-788 1.26e-62

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 229.09  E-value: 1.26e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 282 EAQDANRVKSDFLAKMSHELRTPLNGVIGfTRQLYKTPLNKHQKDYLDTIMLSANSLM-TIISDILDFSKLEAGAMELES 360
Cdd:PRK10841 439 AAEQASQSKSMFLATVSHELRTPLYGIIG-NLDLLQTKELPKGVDRLVTAMNNSSSLLlKIISDILDFSKIESEQLKIEP 517
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 361 IQFQLRDAVNEVMTLLAPSAHDKQLELSIYINQQVPDDLTGDPTRFKQVLINLLSNAIKFTEKGSIkvdISHRLLDDERt 440
Cdd:PRK10841 518 REFSPREVINHITANYLPLVVKKRLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCI---VLHVRVDGDY- 593
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 441 sLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTFNsvFSLPNH 520
Cdd:PRK10841 594 -LSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIR--IPLYGA 670
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 521 VFTNDLPTKSLIGKRI------LYLEphehthHAVLSLLTQWESNVTACFNETSFLDAIkntehkydvcLIghmasVDDM 594
Cdd:PRK10841 671 QYPQKKGVEGLQGKRCwlavrnASLE------QFLETLLQRSGIQVQRYEGQEPTPEDV----------LI-----TDDP 729
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 595 QQLKSYVKA-VRESTDYL---------YLMLNTVSHNMreafigsgadacLSKPLNH--RKLCEVLAAPYRLDHPTHNIE 662
Cdd:PRK10841 730 VQKKWQGRAvITFCRRHIgipleiapgEWVHSTATPHE------------LPALLARiyRIELESDDSANALPSTDKAVS 797
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 663 QNDQallpLKVLVVDDNDANLKllhtLLSEQIEVI----ETAHNGSQAYS-LSKSHkYDIIFMDIQMPIMDGITACKLIQ 737
Cdd:PRK10841 798 DNDD----MMILVVDDHPINRR----LLADQLGSLgyqcKTANDGVDALNvLSKNH-IDIVLTDVNMPNMDGYRLTQRLR 868
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489048494 738 EssLNEDTPIIAVTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIISDHS 788
Cdd:PRK10841 869 Q--LGLTLPVIGVTANALAEEKQRCLEAGMDSCLSKPVTLDVLKQTLTVYA 917
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
280-888 3.27e-57

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 210.95  E-value: 3.27e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 280 KKEAQD----ANRVKSDFLAKMSHELRTPLNGVIGFTRQLYKTPLNKHQKDYLDTIMLSANSLMTIISDILDFSKLEAGA 355
Cdd:PRK11091 269 RKRYQDalekASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRK 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 356 MELESIQFQLRDAVNEVMTLLAPSAHDKQLELSIYINQQVPDDLTGDPTRFKQVLINLLSNAIKFTEKGSIKVDISHrll 435
Cdd:PRK11091 349 LQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRY--- 425
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 436 dDERTSLLVSVTDTGVGIPMDKQDSLFTPFGQA-DSSITRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTFnsv 514
Cdd:PRK11091 426 -EEGDMLTFEVEDSGIGIPEDELDKIFAMYYQVkDSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTL--- 501
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 515 fslpnhvftndlptksligkrilylephehthhavlslltqwesnvtacfnetsfldaikntehkydvclighmasvddm 594
Cdd:PRK11091     --------------------------------------------------------------------------------
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 595 qqlksyvkavrestdylylmlntvshnmreafigsgadaclskplnhrklceVLAAPYRLDHPTHNIEQNDQALLPLKVL 674
Cdd:PRK11091 502 ----------------------------------------------------TIHAPAVAEEVEDAFDEDDMPLPALNIL 529
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 675 VVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGI-TACKLIQESSLNEDTPIIAVTAH 753
Cdd:PRK11091 530 LVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLdIARELRERYPREDLPPLVALTAN 609
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 754 ALQSEKEqLLKDGFKGYLTKPIDEDMLKQIISD--HSPQTPVNRDKAKTDTPQSpapfqssridwaQALqraggkseLAL 831
Cdd:PRK11091 610 VLKDKKE-YLDAGMDDVLSKPLSVPALTAMIKKfwDTQDDEESTVTTEESSKAN------------EAL--------LDI 668
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489048494 832 EMLNMLLLSV----------------PETLTLLAKAIESNDCQQVLSIVHKFHGACCYTGVPKLKSLAETIET 888
Cdd:PRK11091 669 PMLEQYVELVgpklitdslavfekmmPGYLSVLDSNLTARDQKGIVEEAHKIKGAAGSVGLRHLQQLAQQIQS 741
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
171-668 3.07e-54

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 203.98  E-value: 3.07e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 171 QRALLISGIVIILSLVFaaILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLNDNMiGEFEL-----LREGLNTIAHTMV 245
Cdd:PRK11466 330 QYSLLLLGMVSLCALIL--ILWRVVYRSVTRPLAEQTQALQRLLDGDIDSPFPETA-GVRELdtigrLMDAFRSNVHALN 406
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 246 MQKDEMQKNIDQATSDYRETLeqyetsnIELSFAKKEAQDANRVKSDFLAKMSHELRTPLNGVIGFTRQLYKTPLNKHQK 325
Cdd:PRK11466 407 RHREQLAAQVKARTAELQELV-------IEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQR 479
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 326 DYLDTIMLSANSLMTIISDILDFSKLEAGA--MELESIQFQLRDAVNEVMTLLAPSAHDKQLELSIYINQQVPDDLTGDP 403
Cdd:PRK11466 480 DDLRAITDSGESLLTILNDILDYSAIEAGGknVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDP 559
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 404 TRFKQVLINLLSNAIKFTEKGSIKVdishRLLDDErTSLLVSVTDTGVGIPMDKQDSLFTPFGQAdssiTRKFGGTGLGL 483
Cdd:PRK11466 560 RRIRQVITNLLSNALRFTDEGSIVL----RSRTDG-EQWLVEVEDSGCGIDPAKLAEIFQPFVQV----SGKRGGTGLGL 630
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 484 IITKHIVEAMSGRITLNSAPGNGTCFTFNsvfsLPNHVFTNDLPTK-----SLIGKRILYLEPHEHTHHAVLSLLTQWES 558
Cdd:PRK11466 631 TISSRLAQAMGGELSATSTPEVGSCFCLR----LPLRVATAPVPKTvnqavRLDGLRLLLIEDNPLTQRITAEMLNTSGA 706
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 559 NVTACFNETSFLDAIKNTEhKYDVCLIG-HMASVDDM---QQLKSYVKAVRESTDYLYLMLNTVSHNMREAFIGsgadaC 634
Cdd:PRK11466 707 QVVAVGNAAQALETLQNSE-PFAAALVDfDLPDYDGItlaRQLAQQYPSLVLIGFSAHVIDETLRQRTSSLFRG-----I 780
                        490       500       510
                 ....*....|....*....|....*....|....
gi 489048494 635 LSKPLNHRKLCEVLAapyrldHPTHNIEQNDQAL 668
Cdd:PRK11466 781 IPKPVPREVLGQLLA------HYLQLQVNNDQPL 808
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
173-518 6.45e-50

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 184.60  E-value: 6.45e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 173 ALLISGIVIILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLNDNMIGEFELLREGLNTIAHTMVMQKDEMQ 252
Cdd:COG4251  179 ELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELR 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 253 KNIDQATSDYRETLEQYETSNIELSfakkeaqdanrvksDFLAKMSHELRTPLNGVIGFTRQL---YKTPLNKHQKDYLD 329
Cdd:COG4251  259 LELEELEEELEERTAELERSNEELE--------------QFAYVASHDLREPLRKISGFSQLLeedYGDKLDEEGREYLE 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 330 TIMLSANSLMTIISDILDFSKLEAGAMELESIQfqLRDAVNEVMTLLAPSAHDKQLELSIyinQQVPDdLTGDPTRFKQV 409
Cdd:COG4251  325 RIRDAAERMQALIDDLLAYSRVGRQELEFEPVD--LNELLEEVLEDLEPRIEERGAEIEV---GPLPT-VRGDPTLLRQV 398
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 410 LINLLSNAIKFTEKGSI-KVDISHRLLDDERTsllVSVTDTGVGIPMDKQDSLFTPFGQADSSitRKFGGTGLGLIITKH 488
Cdd:COG4251  399 FQNLISNAIKYSRPGEPpRIEIGAEREGGEWV---FSVRDNGIGIDPEYAEKIFEIFQRLHSR--DEYEGTGIGLAIVKK 473
                        330       340       350
                 ....*....|....*....|....*....|
gi 489048494 489 IVEAMSGRITLNSAPGNGTCFTfnsvFSLP 518
Cdd:COG4251  474 IVERHGGRIWVESEPGEGATFY----FTLP 499
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
406-511 8.77e-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: 170.75  E-value: 8.77e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 406 FKQVLINLLSNAIKFTEKGSIKVDISHRLLDDERTSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGGTGLGLII 485
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                         90       100
                 ....*....|....*....|....*.
gi 489048494 486 TKHIVEAMSGRITLNSAPGNGTCFTF 511
Cdd:cd16922   81 SKKLVELMGGDISVESEPGQGSTFTF 106
sCache_4 pfam09984
Single cache domain 4; Members of this family of domains are found in various BarA-like signal ...
31-174 2.13e-47

Single cache domain 4; Members of this family of domains are found in various BarA-like signal transduction histidine kinases, which are involved in the regulation of carbon metabolism via the csrA/csrB regulatory system. The role of this domain has not, as yet, been established.


Pssm-ID: 430966  Cd Length: 146  Bit Score: 165.49  E-value: 2.13e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494   31 INRYIELDEILYQQGTTISEPLAIALEQPMLEKNKQLLNRLISYTHNKHSPTIKSIAIFDKNNALLMTSNYHRSFEKLIS 110
Cdd:pfam09984   1 INRYYELEDQLIDRGTSIIEPLAIASEYGLTTRNRESLRRLISALHRKNSPIVRSIAIFDANNQLFVTSNYHRDFESLRL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489048494  111 QKTLINLKTTHVQKSDELVTFFTPIINHTSHDSKWDPSA--FQSSLGTVIIQLNKDQAVIGQQRAL 174
Cdd:pfam09984  81 PEGAPIPTLTTVEHSGDSLILRTPIISEGLSLPGLPATAesAQRPLGYIAIELNLDSARLQQYREI 146
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
280-522 3.49e-44

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: 167.46  E-value: 3.49e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 280 KKEAQDANRVKSDFLAKMSHELRTPLNGVIGFTrQLYKTPLNKHQKDYLDTIMLSANSLMTIISDILDFSKLEAGAMEle 359
Cdd:COG5809  260 LLRKSEKLSVVGELAAGIAHEIRNPLTSLKGFI-QLLKDTIDEEQKTYLDIMLSELDRIESIISEFLVLAKPQAIKYE-- 336
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 360 siQFQLRDAVNEVMTLLAPSA--HDKQLELSIyiNQQVPDdLTGDPTRFKQVLINLLSNAIKFTEKGSiKVDISHRLLDD 437
Cdd:COG5809  337 --PKDLNTLIEEVIPLLQPQAllKNVQIELEL--EDDIPD-ILGDENQLKQVFINLLKNAIEAMPEGG-NITIETKAEDD 410
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 438 erTSLLVSVTDTGVGIPMDKQDSLFTPFgqadssITRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTfnsvFSL 517
Cdd:COG5809  411 --DKVVISVTDEGCGIPEERLKKLGEPF------YTTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFS----ITL 478

                 ....*
gi 489048494 518 PNHVF 522
Cdd:COG5809  479 PIKLS 483
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
170-510 3.07e-41

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: 157.05  E-value: 3.07e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 170 QQRALLISGIVIILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLNDNMIGEFELLREGLNTIAHTMVMQKD 249
Cdd:COG5000    4 QILFLLLLLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARAFNRMTDQLKEQRE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 250 EMQ------------------------------------------KNIDQATSDY----------RETLEQYETSNIELS 277
Cdd:COG5000   84 ELEerrryletilenlpagvivldadgritlanpaaerllgipleELIGKPLEELlpeldlaellREALERGWQEEIELT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 278 FAKK-----------------------EAQDANRVKS--DFLAKMSHELRTPLNGVIGFT---RQLYKTPLNKHQKD--- 326
Cdd:COG5000  164 RDGRrtllvrasplrddgyvivfdditELLRAERLAAwgELARRIAHEIKNPLTPIQLSAerlRRKLADKLEEDREDler 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 327 YLDTIMLSANSLMTIISDILDFSKLEAGAMELESiqfqLRDAVNEVMTLLAPSAHDKQLELSIYINQQVPDdLTGDPTRF 406
Cdd:COG5000  244 ALDTIIRQVDRLKRIVDEFLDFARLPEPQLEPVD----LNELLREVLALYEPALKEKDIRLELDLDPDLPE-VLADRDQL 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 407 KQVLINLLSNAIKFTE-KGSIKVDISHrllddERTSLLVSVTDTGVGIPMDKQDSLFTPFgqadssITRKFGGTGLGLII 485
Cdd:COG5000  319 EQVLINLLKNAIEAIEeGGEIEVSTRR-----EDGRVRIEVSDNGPGIPEEVLERIFEPF------FTTKPKGTGLGLAI 387
                        410       420
                 ....*....|....*....|....*
gi 489048494 486 TKHIVEAMSGRITLNSAPGNGTCFT 510
Cdd:COG5000  388 VKKIVEEHGGTIELESRPGGGTTFT 412
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
673-784 3.42e-38

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


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 137.99  E-value: 3.42e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLI-QESSLNEDTPIIAVT 751
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIrELEGGGRRTPIIALT 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489048494 752 AHALQSEKEQLLKDGFKGYLTKPIDEDMLKQII 784
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
164-518 3.89e-38

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 146.48  E-value: 3.89e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 164 DQAVIGQQRALLISGIVIILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLNDNMIGEFELLREGLNTIAHT 243
Cdd:COG4191    7 LLLLLLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 244 MVMQKDEMQKNIDQATSDYRETLEQYETSNIELSFAKKEAQDANR--VKSdflAKMS----------HELRTPLNGVIGF 311
Cdd:COG4191   87 LLLLEALLLLLLAALDAEENAELEELERDITELERAEEELRELQEqlVQS---EKLAalgelaagiaHEINNPLAAILGN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 312 T---RQLYKTPLNKHQ-KDYLDTIMLSANSLMTIISDILDFSKLEAGAMELesiqFQLRDAVNEVMTLLAPSAHDKQLEL 387
Cdd:COG4191  164 AellRRRLEDEPDPEElREALERILEGAERAAEIVRSLRAFSRRDEEEREP----VDLNELIDEALELLRPRLKARGIEV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 388 SIYINQQVPDdLTGDPTRFKQVLINLLSNAIK-FTEKGSIKVDISHRLLDDErtsLLVSVTDTGVGIPMDKQDSLFTPFg 466
Cdd:COG4191  240 ELDLPPDLPP-VLGDPGQLEQVLLNLLINAIDaMEEGEGGRITISTRREGDY---VVISVRDNGPGIPPEVLERIFEPF- 314
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489048494 467 qadssITRKF--GGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTfnsvFSLP 518
Cdd:COG4191  315 -----FTTKPvgKGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFT----ITLP 359
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
288-511 1.42e-37

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: 143.89  E-value: 1.42e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  288 RVKSDFLAKMSHELRTPLNGVIGFTRQLYKTPL--NKHQKDYLDtIMLSANSLM-TIISDILDFSKLEAGAMELESIQFQ 364
Cdd:TIGR02966 112 QMRRDFVANVSHELRTPLTVLRGYLETLADGPDedPEEWNRALE-IMLEQSQRMqSLVEDLLTLSRLESAASPLEDEPVD 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  365 LRDAVNEVMTLLAPSAHDKQLELSIYINQQVpdDLTGDPTRFKQVLINLLSNAIKFTEKGSiKVDISHRLLDDErtsLLV 444
Cdd:TIGR02966 191 MPALLDHLRDEAEALSQGKNHQITFEIDGGV--DVLGDEDELRSAFSNLVSNAIKYTPEGG-TITVRWRRDGGG---AEF 264
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489048494  445 SVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTF 511
Cdd:TIGR02966 265 SVTDTGIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFSF 331
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
670-787 2.06e-36

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: 133.44  E-value: 2.06e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 670 PLKVLVVDDNDANLKLLHTLLSEQ-IEVIeTAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPII 748
Cdd:COG0784    5 GKRILVVDDNPDNRELLRRLLERLgYEVT-TAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPII 83
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489048494 749 AVTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIISDH 787
Cdd:COG0784   84 ALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRL 122
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
276-916 4.24e-35

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 144.88  E-value: 4.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  276 LSFAKKEAQDANRVKSDFLAKMSHELRTPLNGVIGFTRQLYKTPLNKHQK-DYLDTIMLSANSLMTIISDILDFSKLEAG 354
Cdd:PRK09959  698 LEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRvEAISLAYATGQSLLGLIGEILDVDKIESG 777
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  355 AMELESIQFQLRDAVNEVMTLLAPSAHDKQLELSIyiNQQVPDD--LTGDPTRFKQVLINLLSNAIKFTEKGSIKVDISH 432
Cdd:PRK09959  778 NYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSC--SSTFPDHylVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSL 855
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  433 RLLDDERTSLLVSVTDTGVGIPMDKQDSLFTPFGQadSSITRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTfn 512
Cdd:PRK09959  856 GHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQ--TSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFT-- 931
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  513 svFSLPnhvftndlptksligkrilylephehthhavlslltqwesnvtacfnetsfldaikntehkydvclighmasVD 592
Cdd:PRK09959  932 --ITIP------------------------------------------------------------------------VE 937
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  593 DMQQlksyvkavrestdylylmlntvshnmreafigsgadaclskplnhrklceVLAAPYRLDHPTHNIEQndqallpLK 672
Cdd:PRK09959  938 ISQQ--------------------------------------------------VATVEAKAEQPITLPEK-------LS 960
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESslNEDTPIIAVTA 752
Cdd:PRK09959  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQ--NSSLPIWGLTA 1038
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  753 HALQSEKEQLLKDGFKGYLTKPIDEDMLKQIISDHSPQTPVnrdkaktdTPqspapfQSSRIDWAQALQRAGGKSELALE 832
Cdd:PRK09959 1039 NAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHI--------AP------QYRHLDIEALKNNTANDLQLMQE 1104
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  833 MLNMLLLSVPETLTLLAKAIESNDCQQVLSIVHKFHGACCYTGVPKLKSLAETIETSlknkCLLENIEPELFELQDELEN 912
Cdd:PRK09959 1105 ILMTFQHETHKDLPAAFHALEAGDNRTFHQCIHRIHGAANILNLQKLINISHQLEIT----PVSDDSKPEILQLLNSVKE 1180

                  ....
gi 489048494  913 LLAD 916
Cdd:PRK09959 1181 HIAE 1184
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
295-510 2.25e-34

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 135.36  E-value: 2.25e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 295 AKMSHELRTPLNGVIGFTRQLYKTPLNKHQKDYLDTIMLSANSLMTIISDILDFSKLEAGAMElesiQFQLRDAVNEVMT 374
Cdd:COG3852  140 AGLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPERE----PVNLHEVLERVLE 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 375 LLAPSAhDKQLELSIYINQQVPDdLTGDPTRFKQVLINLLSNAIK-FTEKGSIKV----DISHRLLDDE-RTSLLVSVTD 448
Cdd:COG3852  216 LLRAEA-PKNIRIVRDYDPSLPE-VLGDPDQLIQVLLNLVRNAAEaMPEGGTITIrtrvERQVTLGGLRpRLYVRIEVID 293
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489048494 449 TGVGIPMDKQDSLFTPFgqadssITRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFT 510
Cdd:COG3852  294 NGPGIPEEILDRIFEPF------FTTKEKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFR 349
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
401-511 6.61e-34

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 125.84  E-value: 6.61e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494   401 GDPTRFKQVLINLLSNAIKFTEKGSiKVDIShrlLDDERTSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSiTRKFGGTG 480
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGG-RITVT---LERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGTG 75
                           90       100       110
                   ....*....|....*....|....*....|.
gi 489048494   481 LGLIITKHIVEAMSGRITLNSAPGNGTCFTF 511
Cdd:smart00387  76 LGLSIVKKLVELHGGEISVESEPGGGTTFTI 106
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
672-785 1.55e-32

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: 121.88  E-value: 1.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLL-SEQIEVIETAhNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPIIAV 750
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLeSAGYEVLEAA-DGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIAL 79
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489048494 751 TAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIIS 785
Cdd:cd17548   80 TAYAMKGDREKILEAGCDGYISKPIDTREFLETVA 114
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
670-784 3.46e-32

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: 123.48  E-value: 3.46e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 670 PLKVLVVDDNDANLKLLHTLL-SEQIEVIEtAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPII 748
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLeAAGYEVVE-AADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPII 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489048494 749 AVTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQII 784
Cdd:COG3706   80 FLTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
401-511 5.85e-30

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: 114.39  E-value: 5.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  401 GDPTRFKQVLINLLSNAIKFTEK-GSIKVDISHrllDDErtsLLVSVTDTGVGIPMDKQDSLFTPFGQADSsitRKFGGT 479
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKaGEITVTLSE---GGE---LTLTVEDNGIGIPPEDLPRIFEPFSTADK---RGGGGT 71
                          90       100       110
                  ....*....|....*....|....*....|..
gi 489048494  480 GLGLIITKHIVEAMSGRITLNSAPGNGTCFTF 511
Cdd:pfam02518  72 GLGLSIVRKLVELLGGTITVESEPGGGTTVTL 103
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
170-506 1.36e-28

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 120.32  E-value: 1.36e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 170 QQRALLIsgiVIILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLNDNMIGEFELLREGLNTIAhtmvmqkd 249
Cdd:NF012163 162 QKRASWL---IVALALLLAALAAFLLARGLLAPVKRLVEATHRLAAGDYTTRVTPTSNDELGKLAQDFNQLA-------- 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 250 emqknidqatsdyrETLEQYEtsnielsfakkeaqdanRVKSDFLAKMSHELRTPLnGVIGFTRQLYKTPLNKHQKDYLD 329
Cdd:NF012163 231 --------------STLEKNE-----------------QMRRDFMADISHELRTPL-AVLRAELEAIQDGIRKFTPESLD 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 330 TIMLSANSLMTIISDILDFSKLEAGAMELESIQFQLRDAVNEVMTLLAPSAHDKQLELSIyinqQVPDDLT--GDPTRFK 407
Cdd:NF012163 279 SLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEV----SLPDSSLvfGDRDRLM 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 408 QVLINLLSNAIKFTEKGSiKVDISHRLLDDErtsLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGGTGLGLIITK 487
Cdd:NF012163 355 QLFNNLLENSLRYTDSGG-SLHISASQRPKE---VTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISL 430
                        330
                 ....*....|....*....
gi 489048494 488 HIVEAMSGRITLNSAPGNG 506
Cdd:NF012163 431 NIVQAHGGTLHAAHSPLGG 449
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
673-784 3.00e-27

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: 106.85  E-value: 3.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQEssLNEDTPIIAVTA 752
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRR--RDPTTPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 489048494  753 HALQSEKEQLLKDGFKGYLTKPIDEDMLKQII 784
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
293-511 3.05e-27

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 118.15  E-value: 3.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 293 FLAKMSHELRTPLNGVIGFTRQLYKTPLNKHQKDYLDTIMLSANSLMTIISDILDFSKLEAGAMElesiQFQLRDAVNEV 372
Cdd:PRK11360 393 LVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEFSRPRESQWQ----PVSLNALVEEV 468
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 373 MTLLAPSAHDKQLELSIYINQQVPDdLTGDPTRFKQVLINLLSNAIK-FTEKGSIKVDIsHRLLDDErtsLLVSVTDTGV 451
Cdd:PRK11360 469 LQLFQTAGVQARVDFETELDNELPP-IWADPELLKQVLLNILINAVQaISARGKIRIRT-WQYSDGQ---VAVSIEDNGC 543
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 452 GIPMDKQDSLFTPFgqadssITRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTF 511
Cdd:PRK11360 544 GIDPELLKKIFDPF------FTTKAKGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTL 597
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
670-787 1.35e-26

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: 108.71  E-value: 1.35e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 670 PLKVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPIIA 749
Cdd:COG3437    6 APTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPVIF 85
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489048494 750 VTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIISDH 787
Cdd:COG3437   86 LTALADPEDRERALEAGADDYLTKPFDPEELLARVRNA 123
PRK09303 PRK09303
histidine kinase;
252-511 2.37e-26

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 111.97  E-value: 2.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 252 QKNIDQATSDYRETLEQYETSNIELSFAKKEAQDANRVKSDFLAKMSHELRTPL--------------NGVIGFTRQLYK 317
Cdd:PRK09303 113 LQPSEIDSGRYSQELLQLSDELFVLRQENETLLEQLKFKDRVLAMLAHDLRTPLtaaslaletlelgqIDEDTELKPALI 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 318 TPLNKHQKDYLDTImlsaNSLmtiISDILDFSKLEAGAMELESIQFQLRDAVNEVMTLLapsaHDKQLELSIYINQQVPD 397
Cdd:PRK09303 193 EQLQDQARRQLEEI----ERL---ITDLLEVGRTRWEALRFNPQKLDLGSLCQEVILEL----EKRWLAKSLEIQTDIPS 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 398 DLT---GDPTRFKQVLINLLSNAIKFTEK-GSIKVDISHrllddeRTS--LLVSVTDTGVGIPMDKQDSLFTpfG----Q 467
Cdd:PRK09303 262 DLPsvyADQERIRQVLLNLLDNAIKYTPEgGTITLSMLH------RTTqkVQVSICDTGPGIPEEEQERIFE--DrvrlP 333
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 489048494 468 ADSSITrkfgGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTF 511
Cdd:PRK09303 334 RDEGTE----GYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHF 373
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
284-504 2.93e-26

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: 113.25  E-value: 2.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  284 QDANRVKSDFLAKMSHELRTPLNGVIGFTRQLYKTPlnKHQKDYLDTIMLSA---NSLMTIISDILDFSKLEAGAMELES 360
Cdd:TIGR01386 235 EDAFQRLSQFSADLAHELRTPLTNLLGQTQVALSQP--RTGEEYREVLESNLeelERLSRMVSDMLFLARADNGQLALER 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  361 IQFQLRDAVNEVMTLLAPSAHDKQLELSIYINQQVPddltGDPTRFKQVLINLLSNAIKFTEKGS-IKVDISHRllddeR 439
Cdd:TIGR01386 313 VRLDLAAELAKVAEYFEPLAEERGVRIRVEGEGLVR----GDPQMFRRAISNLLSNALRHTPDGGtITVRIERR-----S 383
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489048494  440 TSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGGTGLGLIITKHIVEAMSGRITLNSAPG 504
Cdd:TIGR01386 384 DEVRVSVSNPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAESPDG 448
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
673-784 1.62e-25

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: 101.77  E-value: 1.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPIIAVTA 752
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTG 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 489048494 753 HALQSEKEQLLKDGFKGYLTKPIDEDMLKQII 784
Cdd:cd17580   81 YGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
672-774 2.16e-25

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: 101.00  E-value: 2.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQ--IEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQEssLNEDTPIIA 749
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEWEagFEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRE--LDPDTKIII 78
                         90       100
                 ....*....|....*....|....*
gi 489048494 750 VTAHALQSEKEQLLKDGFKGYLTKP 774
Cdd:COG4753   79 LSGYSDFEYAQEAIKLGADDYLLKP 103
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
670-780 5.42e-25

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: 103.50  E-value: 5.42e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 670 PLKVLVVDDNDANLKLLHTLLSEQ-IEVIeTAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESslNEDTPII 748
Cdd:COG0745    1 MPRILVVEDDPDIRELLADALEREgYEVD-TAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRAR--PSDIPII 77
                         90       100       110
                 ....*....|....*....|....*....|..
gi 489048494 749 AVTAHALQSEKEQLLKDGFKGYLTKPIDEDML 780
Cdd:COG0745   78 MLTARDDEEDRVRGLEAGADDYLTKPFDPEEL 109
HPtr COG2198
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
83-915 5.79e-25

HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];


Pssm-ID: 441800 [Multi-domain]  Cd Length: 871  Bit Score: 112.06  E-value: 5.79e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  83 IKSIAIFDKNNALLMTSNYHRSFEKLISQKTLINLKTTHVQKSDELVTFFTPIINHTSHDSKWDPSAFQSSLGTVIIQLN 162
Cdd:COG2198   26 LALLLLLLLAALALLLLLLLLLALLALLLLLVALALLLALLLLLLGVLLLLLDLLELLLLLLLLLLLLLLLLLLLLLALL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 163 KDQAVIGQQRALLISGIVIILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLNDNMIGEFELLREGLNTIAH 242
Cdd:COG2198  106 LLLLLLLALLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLVLAALLLLLLLALLLALLLLVLLVLLLLLLLLL 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 243 TMVMQKDEMQKNIDQATSDYRETLEQYETSNIELSFAKKEAQDANRVKSDFLAKMSHELRTPLNGVIGFTRQLYKTPLNK 322
Cdd:COG2198  186 LLLLLLLLLLLLLLLALTLAALLELLAAELALEALLAELAAEAAAALAAELALAELAALLLLLLLLLLLLILLLLLLLLL 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 323 HQKDYLDTIMLSANSLMTIISDILDFSKLEAGAMELESIQFQLRDAVNEVMTLLAPSAHDKQLELSIYINQQVPDDLTGD 402
Cdd:COG2198  266 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLELLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 345
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 403 PTRFKQVLINLLSNAIKFTEKGSIKVDISHRLLDDERTSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGGTGLG 482
Cdd:COG2198  346 LLLLALLLLALLLALLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLLLLLLSLLLSLLLLLLLLLLLLLLLL 425
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 483 LIITKHIVEAMSGRITLNSAPGNGTCFTFNSVFSLPNHVFT-----------NDLPTKSLIGKRILYLEPHEHTHHAVLS 551
Cdd:COG2198  426 LLLLLLLLLLLLLLLGLLLLLLLLLGLLLLLLLGLLLLALLlllllllllllLLLLLLLLLLLLLLLLLLLLLLLLLLLL 505
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 552 LLTQWESNVTACFNETSFLDAIKNTEHKYDVCLIGHMASVDDMQQLKSYVKAVRESTDYLYLMLNTVSHNMREAFIGSGA 631
Cdd:COG2198  506 LVAAALAALALLLLLALLLLLLLDLLILGLLLILLLLLLGLLALGLAALLLLLALLLGLGLLLGLLLGGLLLLLLLLLLL 585
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 632 DACLSKPLNHRKLCEVLAAPYRLDHPTHNIEQNDQALLPLKVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSK 711
Cdd:COG2198  586 LLLLLLLLLLLLLLLALLLALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAVLLAAAAAAAAL 665
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 712 SHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPIIAVTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIisdhsPQT 791
Cdd:COG2198  666 AALDLLLDLDDMMMMLDDMMAEAARARALAARAAAIAAAAAAAAAAAAAAAAAAAALLAALLLLLLLLLLLL-----LLL 740
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 792 PVNRDKAKTDTPQSPAPFQSSRIDWaQALQRAGGKSELALEMLNMLLLSVPETLTLLAKAIESNDCQQVLSIVHKFHGAC 871
Cdd:COG2198  741 LLLLLAAAAAAAASPAAPALPVLDL-EALRRLGGDPELLRELLELFLEELPELLAELRQALAAGDLEALARLAHKLKGSA 819
                        810       820       830       840
                 ....*....|....*....|....*....|....*....|....
gi 489048494 872 CYTGVPKLKSLAETIETSLKNKcLLENIEPELFELQDELENLLA 915
Cdd:COG2198  820 GNLGAPRLAELAAELEQAARAG-DLEEAEELLAELEAELERVLA 862
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
295-510 6.16e-25

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


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 109.82  E-value: 6.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 295 AKMSHELRTPLNGVIGFTrQLYKTPLNKhQKDYLDtIMLSANSLM-TIISDILDFSKLEAGAMELESIQfqlrDAVNEVM 373
Cdd:COG5805  292 AGIAHEIRNPLTSIKGFL-QLLQPGIED-KEEYFD-IMLSELDRIeSIISEFLALAKPQAVNKEKENIN----ELIQDVV 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 374 TLLAPSA--HDKQLELSIyiNQQVPDdLTGDPTRFKQVLINLLSNAIKFTEKGSIkVDISHRLLDDertSLLVSVTDTGV 451
Cdd:COG5805  365 TLLETEAilHNIQIRLEL--LDEDPF-IYCDENQIKQVFINLIKNAIEAMPNGGT-ITIHTEEEDN---SVIIRVIDEGI 437
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489048494 452 GIPMDKQDSLFTPFgqadssITRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFT 510
Cdd:COG5805  438 GIPEERLKKLGEPF------FTTKEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFT 490
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
674-774 6.90e-25

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: 99.61  E-value: 6.90e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 674 LVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQEssLNEDTPIIAVTAH 753
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRE--LPPDIPVIVLTAK 78
                         90       100
                 ....*....|....*....|.
gi 489048494 754 ALQSEKEQLLKDGFKGYLTKP 774
Cdd:cd00156   79 ADEEDAVRALELGADDYLVKP 99
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
295-510 1.18e-23

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 105.25  E-value: 1.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 295 AKMSHELRTPLNGVIGFTR---QLYKTPLNKHQkdyLDTIMLS-ANSLMTIISDILDFSKleagAMELESIQFQLRDAVN 370
Cdd:PRK10364 242 AGVAHEIRNPLSSIKGLAKyfaERAPAGGEAHQ---LAQVMAKeADRLNRVVSELLELVK----PTHLALQAVDLNDLIN 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 371 EVMTLLAPSAHDKQLELSIYINQQVPDdLTGDPTRFKQVLINLLSNAIK-FTEKGSIKVDIShrlldDERTSLLVSVTDT 449
Cdd:PRK10364 315 HSLQLVSQDANSREIQLRFTANDTLPE-IQADPDRLTQVLLNLYLNAIQaIGQHGVISVTAS-----ESGAGVKISVTDS 388
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489048494 450 GVGIPMDKQDSLFTPFgqadssITRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFT 510
Cdd:PRK10364 389 GKGIAADQLEAIFTPY------FTTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFT 443
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
178-510 3.74e-23

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


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 102.00  E-value: 3.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 178 GIVIILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLNDNMIGEFEL--LREGLNTIAhtmvmqkdemqkni 255
Cdd:NF012226  63 FTVILCGSVISLIIGMKLAQRFIVPINFLADAAKKISQGDLSARAEDSQIHSAEIseLMHNFNDMA-------------- 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 256 dqatsdyretlEQYETSnielsfaKKEAQDANrvksdflAKMSHELRTP-----------LNGVIGFTRQLYKTPLNK-- 322
Cdd:NF012226 129 -----------QKLESS-------VKNAQVWN-------AAIAHELRTPitilqgrlqgiLDGVFEPDPALFKSLLNQve 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 323 ---HQKDYLDTIMLSANSLMTiisdildfskleagaMELESIQFQlrDAVNEVMTLLAPSAHDKQLElsiyINQQVPDDL 399
Cdd:NF012226 184 glsHLVEDLRTLSLVENQQLR---------------LNYESVDLK--DSIEKVLKMFEDRLEQAQLT----IVLNLTATP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 400 -TGDPTRFKQVLINLLSNAIKFTEKGSIKvdISHRLLDDErtsLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGG 478
Cdd:NF012226 243 vFCDRRRIEQVLIALIDNAIRYANAGKLK--ISSSVIQDD---WILQIEDEGPGIAEEYQQDLFNPFFRLEQSRNKEFGG 317
                        330       340       350
                 ....*....|....*....|....*....|..
gi 489048494 479 TGLGLIITKHIVEAMSGRITLnSAPGNGTCFT 510
Cdd:NF012226 318 TGLGLAVVHAIVIAHKGSIEY-SNSQGNSVFT 348
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
670-786 4.80e-23

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: 102.73  E-value: 4.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 670 PLKVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQEssLNEDTPIIA 749
Cdd:COG2204    2 MARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRA--LDPDLPVIL 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489048494 750 VTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIISD 786
Cdd:COG2204   80 LTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVER 116
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
670-805 1.13e-22

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 94.65  E-value: 1.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 670 PLKVLVVDDNDANLKLLHTLLSEQ--IEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQEssLNEDTPI 747
Cdd:COG4565    3 MIRVLIVEDDPMVAELLRRYLERLpgFEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRA--RGPDVDV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489048494 748 IAVTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIISDHSPQTPVNRDKAKTDTPQS 805
Cdd:COG4565   81 IVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQEEDLPEA 138
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
402-510 1.79e-22

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


Pssm-ID: 340402 [Multi-domain]  Cd Length: 110  Bit Score: 92.94  E-value: 1.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 402 DPTRFKQVLINLLSNAIKFTEKGSIkvdISHRLLDDERTSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGGTGL 481
Cdd:cd16925    1 DAEKYERVVLNLLSNAFKFTPDGGR---IRCILEKFRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGL 77
                         90       100
                 ....*....|....*....|....*....
gi 489048494 482 GLIITKHIVEAMSGRITLNSAPGNGTCFT 510
Cdd:cd16925   78 GLSIVKEFVELHGGTVTVSDAPGGGALFQ 106
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
170-506 3.63e-22

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 100.86  E-value: 3.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 170 QQRalLISGIVIILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLNDNMIGEFELLREGLNTIAHTMvmqkd 249
Cdd:PRK10549 161 QQR--RTSWLIVALSTLLAALATFLLARGLLAPVKRLVEGTHKLAAGDFTTRVTPTSRDELGRLAQDFNQLASTL----- 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 250 emQKNidqatsdyretlEQyetsnielsfakkeaqdanrVKSDFLAKMSHELRTPL-----------NGVigftRQLykT 318
Cdd:PRK10549 234 --EKN------------EQ--------------------MRRDFMADISHELRTPLavlrgeleaiqDGV----RKF--T 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 319 PlnkhqkDYLDTIMLSANSLMTIISDILDFSKLEAGAMELEsiqfqlRDAVNEVMTLLAPSA------HDKQLELSIYIN 392
Cdd:PRK10549 274 P------ESVASLQAEVGTLTKLVDDLHQLSLSDEGALAYR------KTPVDLVPLLEVAGGafrerfASRGLTLQLSLP 341
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 393 QQVPddLTGDPTRFKQVLINLLSNAIKFTEKGSiKVDISHRLLDDertSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSI 472
Cdd:PRK10549 342 DSAT--VFGDPDRLMQLFNNLLENSLRYTDSGG-SLHISAEQRDK---TLRLTFADSAPGVSDEQLQKLFERFYRTEGSR 415
                        330       340       350
                 ....*....|....*....|....*....|....
gi 489048494 473 TRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNG 506
Cdd:PRK10549 416 NRASGGSGLGLAICLNIVEAHNGRIIAAHSPFGG 449
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
673-784 4.27e-22

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: 92.40  E-value: 4.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQ---IEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQEssLNEDTPIIA 749
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIDWEelgFEVVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRE--LYPDIKIII 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489048494 750 VTAHalqSEKE---QLLKDGFKGYLTKPIDEDMLKQII 784
Cdd:cd17536   79 LSGY---DDFEyaqKAIRLGVVDYLLKPVDEEELEEAL 113
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
670-784 5.21e-22

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 95.65  E-value: 5.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 670 PLKVLVVDDNDANLKLLHTLLSE--QIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQEssLNEDTPI 747
Cdd:COG3279    1 MMKILIVDDEPLARERLERLLEKypDLEVVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRE--LDPPPPI 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489048494 748 IAVTAHalqsekEQLLKDGFK----GYLTKPIDEDMLKQII 784
Cdd:COG3279   79 IFTTAY------DEYALEAFEvnavDYLLKPIDEERLAKAL 113
PRK10490 PRK10490
sensor protein KdpD; Provisional
276-518 5.80e-22

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 102.04  E-value: 5.80e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 276 LSFAKKEAQ---DANR--VKSDFLAKMSHELRTPLNGVIGFTRQL----------YKTPLNKHQKDYLDTIMLsanslmt 340
Cdd:PRK10490 645 LTLTASEEQarlASEReqLRNALLAALSHDLRTPLTVLFGQAEILtldlasegspHARQASEIRQQVLNTTRL------- 717
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 341 iISDILDFSKLEAGAMELESIQFQLRDAVNEVMTLLAPSAHDKQLELSIyinqqvPDDLT---GDPTRFKQVLINLLSNA 417
Cdd:PRK10490 718 -VNNLLDMARIQSGGFNLRKEWLTLEEVVGSALQMLEPGLSGHPINLSL------PEPLTlihVDGPLFERVLINLLENA 790
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 418 IKFT-EKGSIKVDIShrlLDDERtsLLVSVTDTGVGIPMDKQDSLFTPF--GQADSSITrkfgGTGLGLIITKHIVEAMS 494
Cdd:PRK10490 791 VKYAgAQAEIGIDAH---VEGER--LQLDVWDNGPGIPPGQEQLIFDKFarGNKESAIP----GVGLGLAICRAIVEVHG 861
                        250       260
                 ....*....|....*....|....
gi 489048494 495 GRITLNSAPGNGTCFtfnsVFSLP 518
Cdd:PRK10490 862 GTIWAENRPEGGACF----RVTLP 881
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
673-775 6.87e-22

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: 91.03  E-value: 6.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPIIAVTA 752
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTA 80
                         90       100
                 ....*....|....*....|...
gi 489048494 753 HALQSEKEQLLKDGFKGYLTKPI 775
Cdd:cd19920   81 LTDTEDKVKGFELGAVDYITKPF 103
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-518 8.90e-22

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: 90.85  E-value: 8.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 408 QVLINLLSNAIKFTEKGSIK-VDISHRLLDDERTsllVSVTDTGVGIPMDKQDSLFTPFGQADSSitRKFGGTGLGLIIT 486
Cdd:cd16921    3 QVLTNLLGNAIKFRRPRRPPrIEVGAEDVGEEWT---FYVRDNGIGIDPEYAEKVFGIFQRLHSR--EEYEGTGVGLAIV 77
                         90       100       110
                 ....*....|....*....|....*....|..
gi 489048494 487 KHIVEAMSGRITLNSAPGNGTCFTfnsvFSLP 518
Cdd:cd16921   78 RKIIERHGGRIWLESEPGEGTTFY----FTLP 105
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
670-784 6.98e-21

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: 91.56  E-value: 6.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 670 PLKVLVVDDNDANLKLLHTLLSEQ-IEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLnedTPII 748
Cdd:COG3707    3 GLRVLVVDDEPLRRADLREGLREAgYEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP---APVI 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489048494 749 AVTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQII 784
Cdd:COG3707   80 LLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPAL 115
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
672-775 7.21e-21

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


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 88.32  E-value: 7.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLS-EQIEVIeTAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPIIAV 750
Cdd:cd17538    1 KILVVDDEPANRELLEALLSaEGYEVL-TADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMI 79
                         90       100
                 ....*....|....*....|....*..
gi 489048494 751 TahALQSEKEQL--LKDGFKGYLTKPI 775
Cdd:cd17538   80 T--ALDDREDRIrgLEAGADDFLSKPI 104
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
228-509 2.29e-20

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 97.06  E-value: 2.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 228 GEFELLREGLNTIAHTMVMQKDEMQKNIDQATSDYRETLEQYETsnielsfakkeaqdanrvksdFLAKMSHELRTPLNG 307
Cdd:PRK13837 409 GELQLLELALDCLAHAIERRRLETERDALERRLEHARRLEAVGT---------------------LASGIAHNFNNILGA 467
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 308 VIGFTR-QLYKTPLNKHQKDYLDTIMLSANSLMTIISDILDFSKLEAGAMElesiQFQLRDAVNEVMTLLApSAHDKQLE 386
Cdd:PRK13837 468 ILGYAEmALNKLARHSRAARYIDEIISAGARARLIIDQILAFGRKGERNTK----PFDLSELVTEIAPLLR-VSLPPGVE 542
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 387 LSIyinQQVPDDL--TGDPTRFKQVLINLLSNAIK-FTEKGSIKVDISHRLLDDERTS----------LLVSVTDTGVGI 453
Cdd:PRK13837 543 LDF---DQDQEPAvvEGNPAELQQVLMNLCSNAAQaMDGAGRVDISLSRAKLRAPKVLshgvlppgryVLLRVSDTGAGI 619
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489048494 454 PMDKQDSLFTPFgqadssITRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCF 509
Cdd:PRK13837 620 DEAVLPHIFEPF------FTTRAGGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRF 669
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
673-783 4.12e-20

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: 86.41  E-value: 4.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQ--IEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQesSLNEDTPIIAV 750
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLESEpdIEVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLR--RRYPDLKVIVL 78
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489048494 751 TAHALQSEKEQLLKDGFKGYLTKPID-EDMLKQI 783
Cdd:cd17535   79 TAHDDPEYVLRALKAGAAGYLLKDSSpEELIEAI 112
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
407-518 6.93e-20

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: 85.53  E-value: 6.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 407 KQVLINLLSNAIK-FTEKGSIKVDISHRLLDDERTSLLVSVTDTGVGIPMDKQDSLFTPFgqadssITRKFGGTGLGLII 485
Cdd:cd16920    2 QQVLINLVRNGIEaMSEGGCERRELTIRTSPADDRAVTISVKDTGPGIAEEVAGQLFDPF------YTTKSEGLGMGLSI 75
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489048494 486 TKHIVEAMSGRITLNSAPGNGTCFTfnsvFSLP 518
Cdd:cd16920   76 CRSIIEAHGGRLSVESPAGGGATFQ----FTLP 104
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
402-506 2.29e-19

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


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 84.05  E-value: 2.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 402 DPTRFKQVLINLLSNAIKFTEKGSiKVDISHRLLDDERTsllVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGGTGL 481
Cdd:cd16946    1 DRDRLQQLFVNLLENSLRYTDTGG-KLRIRAAQTPQEVR---LDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGL 76
                         90       100
                 ....*....|....*....|....*
gi 489048494 482 GLIITKHIVEAMSGRITLNSAPGNG 506
Cdd:cd16946   77 GLAICHNIALAHGGTISAEHSPLGG 101
PRK10604 PRK10604
sensor protein RstB; Provisional
298-527 7.00e-19

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 90.43  E-value: 7.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 298 SHELRTPLngvigfTRQLYKTPLNKHqkdyldtimLSANSLMTIISDI----------LDFSKLEAGAMEL--ESIQFQ- 364
Cdd:PRK10604 220 AHELRTPL------VRLRYRLEMSDN---------LSAAESQALNRDIgqlealieelLTYARLDRPQNELhlSEPDLPa 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 365 -LRDAVNEVMTLlapsAHDKQLELSIyinQQVPDDLTGDPTRFKQVLINLLSNAIKFTEKgsiKVDIShRLLDDERTSLL 443
Cdd:PRK10604 285 wLSTHLADIQAV----TPEKTVRLDT---PHQGDYGALDMRLMERVLDNLLNNALRYAHS---RVRVS-LLLDGNQACLI 353
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 444 VSvtDTGVGIPMDKQDSLFTPFGQADSSITRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTfnsvFSLPNHVFT 523
Cdd:PRK10604 354 VE--DDGPGIPPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFS----FSWPVWHNL 427

                 ....
gi 489048494 524 NDLP 527
Cdd:PRK10604 428 PQFT 431
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
290-520 7.60e-19

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 90.60  E-value: 7.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 290 KSDFLAKMSHELRTPLNGVIGFTR-QLYKTPLNKHQKDYLDTIMLSANSLMTIISDILDFSKLEAGAMELESIQFQLRDA 368
Cdd:PRK09835 262 QSNFSADIAHEIRTPITNLITQTEiALSQSRSQKELEDVLYSNLEELTRMAKMVSDMLFLAQADNNQLIPEKKMLDLADE 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 369 VNEVMTLLAPSAHDKQLELSIyinQQVPDDLTGDPTRFKQVLINLLSNAIKFTEKGSikvDISHRLLDDERTSLLVsVTD 448
Cdd:PRK09835 342 VGKVFDFFEAWAEERGVELRF---VGDPCQVAGDPLMLRRAISNLLSNALRYTPAGE---AITVRCQEVDHQVQLV-VEN 414
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489048494 449 TGVGIPMDKQDSLFTPFGQADSSITRKFGGTGLGLIITKHIVEAMSGRITLNSAPgNGTCFTfnsvFSLPNH 520
Cdd:PRK09835 415 PGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRFV----ISLPRL 481
pleD PRK09581
response regulator PleD; Reviewed
672-780 1.41e-18

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 89.57  E-value: 1.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHT-LLSEQIEVIeTAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPIIAV 750
Cdd:PRK09581   4 RILVVDDIPANVKLLEAkLLAEYYTVL-TASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMV 82
                         90       100       110
                 ....*....|....*....|....*....|
gi 489048494 751 TAHALQSEKEQLLKDGFKGYLTKPIDEDML 780
Cdd:PRK09581  83 TALDDPEDRVRGLEAGADDFLTKPINDVAL 112
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
672-776 2.36e-18

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: 81.72  E-value: 2.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQ--IEVIETAhNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPIIA 749
Cdd:cd17551    2 RILIVDDNPTNLLLLEALLRSAgyLEVVSFT-DPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVM 80
                         90       100
                 ....*....|....*....|....*..
gi 489048494 750 VTAHALQSEKEQLLKDGFKGYLTKPID 776
Cdd:cd17551   81 ITADTDREVRLRALEAGATDFLTKPFD 107
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
674-774 4.23e-18

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: 80.14  E-value: 4.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 674 LVVDDNDANLKLLHTLLS-EQIEVIeTAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESslNEDTPIIAVTA 752
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEkEGYEVD-TAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREK--GSDIPIIMLTA 77
                         90       100
                 ....*....|....*....|..
gi 489048494 753 HALQSEKEQLLKDGFKGYLTKP 774
Cdd:cd17574   78 KDEEEDKVLGLELGADDYITKP 99
envZ PRK09467
osmolarity sensor protein; Provisional
294-508 5.88e-18

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 87.66  E-value: 5.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 294 LAKMSHELRTPLngvigfTRQLYKTPLNKHQKDYL-DTIMLSANSLMTIISDILDFSKLEAgamELESIQFQLRDAVNEV 372
Cdd:PRK09467 233 MAGVSHDLRTPL------TRIRLATEMMSEEDGYLaESINKDIEECNAIIEQFIDYLRTGQ---EMPMEMADLNALLGEV 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 373 mtLLAPSAHDKQLELSIyinQQVPDDLTGDPTRFKQVLINLLSNAIKFTeKGSIKVDISHrllddERTSLLVSVTDTGVG 452
Cdd:PRK09467 304 --IAAESGYEREIETAL---QPGPIEVPMNPIAIKRALANLVVNAARYG-NGWIKVSSGT-----EGKRAWFQVEDDGPG 372
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489048494 453 IPMDKQDSLFTPFGQADSSitRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTC 508
Cdd:PRK09467 373 IPPEQLKHLFQPFTRGDSA--RGSSGTGLGLAIVKRIVDQHNGKVELGNSEEGGLS 426
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
672-786 1.37e-17

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: 79.24  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQ-IEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQEssLNEDTPIIAV 750
Cdd:cd17542    2 KVLIVDDAAFMRMMLKDILTKAgYEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKK--IDPNAKVIMC 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489048494 751 TAHAlqseKEQLLKD----GFKGYLTKPIDEDMLKQIISD 786
Cdd:cd17542   80 SAMG----QEEMVKEaikaGAKDFIVKPFQPERVLEAVEK 115
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
290-354 1.39e-17

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 77.64  E-value: 1.39e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489048494  290 KSDFLAKMSHELRTPLNGVIGFTRQLYKTPLNKHQKDYLDTIMLSANSLMTIISDILDFSKLEAG 354
Cdd:pfam00512   2 KSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
151-502 3.71e-17

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 86.28  E-value: 3.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 151 QSSLGTVIIQLNKD----QAVIGQQRALLIsgIVIILSLVFAAILA-LRLSRMFMTPLNKLVLATDKLVEGKRSTGL--- 222
Cdd:COG4192  300 SGLVGNSREQLVALnqetAQLVQQSGILLL--AIALLSLLLAVLINyFYVRRRLVKRLNALSDAMAAIAAGDLDVPIpvd 377
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 223 -NDNmIGEF-ELLREGLNTIAhtmvmqkdEMQKNIDQATSDYRETLEQYETSNIELSFAKKEAqdanrVKSDFLAKMSHE 300
Cdd:COG4192  378 gNDE-IGRIaRLLRVFRDQAI--------EKTQELETEIEERKRIEKNLRQTQDELIQAAKMA-----VVGQTMTSLAHE 443
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 301 LRTPLNG----VIGFTRQLYKTPLNKHQkDYLDTIMLSANSLMTIISDILDFSKLEAGAMELESiqfqLRDAVNEVMTLL 376
Cdd:COG4192  444 LNQPLNAmsmyLFSAKKALEQENYAQLP-TSLDKIEGLIERMDKIIKSLRQFSRKSDTPLQPVD----LRQVIEQAWELV 518
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 377 APSAHDKQLELSIYINQQVPddltGDPTRFKQVLINLLSNAIK-FTEKGSIKVDishrlLDDERTSLLVSVTDTGVGIPM 455
Cdd:COG4192  519 ESRAKPQQITLHIPDDLMVQ----GDQVLLEQVLVNLLVNALDaVATQPQISVD-----LLSNAENLRVAISDNGNGWPL 589
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 489048494 456 dkQDSLFTPFgqadssITRKFGGTGLGLIITKHIVEAMSGRITLNSA 502
Cdd:COG4192  590 --VDKLFTPF------TTTKEVGLGLGLSICRSIMQQFGGDLYLAST 628
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
406-511 4.86e-17

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


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 77.37  E-value: 4.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 406 FKQVLINLLSNAIKFTeKGSIKVDISHrllddERTSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGGTGLGLII 485
Cdd:cd16949    1 LARALENVLRNALRYS-PSKILLDISQ-----DGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAI 74
                         90       100
                 ....*....|....*....|....*.
gi 489048494 486 TKHIVEAMSGRITLNSAPGNGTCFTF 511
Cdd:cd16949   75 AERAIEQHGGKIKASNRKPGGLRVRI 100
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
292-521 5.49e-17

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 84.68  E-value: 5.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 292 DFLAKMSHELRTPLNGVIGFTRQLYKTPLNKHQKD-YLDTIMLSANSLMTIISDILDFSKLEAGAMelesiqFQLRDAVN 370
Cdd:PRK11006 206 NFFANVSHELRTPLTVLQGYLEMMQDQPLEGALREkALHTMREQTQRMEGLVKQLLTLSKIEAAPT------IDLNEKVD 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 371 EVMTLL-----APSAHDKQLELSIYINQQVpdDLTGDPTRFKQVLINLLSNAIKFTEKGSiKVDISHRllddeRTS--LL 443
Cdd:PRK11006 280 VPMMLRvlereAQTLSQGKHTITFEVDNSL--KVFGNEDQLRSAISNLVYNAVNHTPEGT-HITVRWQ-----RVPqgAE 351
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489048494 444 VSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTfnsvFSLPNHV 521
Cdd:PRK11006 352 FSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFS----FVLPERL 425
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
409-511 6.05e-17

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: 77.09  E-value: 6.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 409 VLINLLSNAIKFTEKgsiKVDISHRLLDDertSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGGTGLGLIITKH 488
Cdd:cd16939    4 ALDNLLRNALRYAHR---TVRIALLVSGG---RLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAIVHR 77
                         90       100
                 ....*....|....*....|...
gi 489048494 489 IVEAMSGRITLNSAPGNGTCFTF 511
Cdd:cd16939   78 VALWHGGHVECDDSELGGACFRL 100
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
170-520 6.65e-17

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 84.51  E-value: 6.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 170 QQRALLISGIVIILSLVFAAILALRLSRmfmtPLNKLVLATDKLVEGKRStglndnmigEFELLREG-LNTIAHTMvmqk 248
Cdd:PRK11100 181 ERRILWAGALLLGIALLIGAGVVWWLNR----SIRRLTRYADAVTEGKPV---------PLPKLGSSeLRELAQAL---- 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 249 DEMqknidqatsdyRETLE--QYetsnIElsfakkeaqdanrvksDFLAKMSHELRTPLNGVIGFTRQLYKTPLNKHQKD 326
Cdd:PRK11100 244 ESM-----------RVKLEgkAY----VE----------------QYVQTLTHELKSPLAAIRGAAELLQEDPPPEDRAR 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 327 YLDTIMLSANSLMTIISDILDFSKLEAGAMELESIQFQLRDAVNEVMTLLAPSAHDKQLELsiyinQQVPDDLT--GDPT 404
Cdd:PRK11100 293 FTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEAREAQAAAKGITL-----RLRPDDARvlGDPF 367
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 405 RFKQVLINLLSNAIKFT-EKGSIKVDIShrlLDDERtsLLVSVTDTGVGIPMDKQDSLFTPFgqadSSITRKFGG---TG 480
Cdd:PRK11100 368 LLRQALGNLLDNAIDFSpEGGTITLSAE---VDGEQ--VALSVEDQGPGIPDYALPRIFERF----YSLPRPANGrksTG 438
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 489048494 481 LGLIITKHIVEAMSGRITLNSAPGNGTCFTFNsvfsLPNH 520
Cdd:PRK11100 439 LGLAFVREVARLHGGEVTLRNRPEGGVLATLT----LPRH 474
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
290-354 7.16e-17

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 75.68  E-value: 7.16e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489048494   290 KSDFLAKMSHELRTPLNGVIGFTRQLYKTPLNKHQKDYLDTIMLSANSLMTIISDILDFSKLEAG 354
Cdd:smart00388   2 KREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-511 1.08e-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: 76.34  E-value: 1.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 408 QVLINLLSNAIKFTEKGSI-KVDISHRLLDDErtsLLVSVTDTGVGIPMDKQDSLFTPFgqadsSITRKFG-GTGLGLII 485
Cdd:cd16976    3 QVLMNLLQNALDAMGKVENpRIRIAARRLGGR---LVLVVRDNGPGIAEEHLSRVFDPF-----FTTKPVGkGTGLGLSI 74
                         90       100
                 ....*....|....*....|....*.
gi 489048494 486 TKHIVEAMSGRITLNSAPGNGTCFTF 511
Cdd:cd16976   75 SYGIVEEHGGRLSVANEEGAGARFTF 100
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
403-510 1.27e-16

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: 76.31  E-value: 1.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 403 PTRFKQVLINLLSNAIK-FTEKGSIKVDISHrllDDERtsLLVSVTDTGVGIPMDKQDSLFTPFgqadsSITRKFG-GTG 480
Cdd:cd16943    1 PSQLNQVLLNLLVNAAQaMEGRGRITIRTWA---HVDQ--VLIEVEDTGSGIDPEILGRIFDPF-----FTTKPVGeGTG 70
                         90       100       110
                 ....*....|....*....|....*....|
gi 489048494 481 LGLIITKHIVEAMSGRITLNSAPGNGTCFT 510
Cdd:cd16943   71 LGLSLSYRIIQKHGGTIRVASVPGGGTRFT 100
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
401-510 1.74e-16

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


Pssm-ID: 340423 [Multi-domain]  Cd Length: 125  Bit Score: 76.40  E-value: 1.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 401 GDPTRFKQVLINLLSNAIKFTEKGSIkvdISHRLLDDERtSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGGTG 480
Cdd:cd16947   16 ANTEALQRILKNLISNAIKYGSDGKF---LGMTLREDEK-HVYIDIWDKGKGISETEKDHVFERLYTLEDSRNSAKQGNG 91
                         90       100       110
                 ....*....|....*....|....*....|
gi 489048494 481 LGLIITKHIVEAMSGRITLNSAPGNGTCFT 510
Cdd:cd16947   92 LGLTITKRLAESMGGSIYVNSKPYEKTVFT 121
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
671-780 2.19e-16

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: 75.91  E-value: 2.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 671 LKVLVVDDnDANLKL-LHTLLSEQ-IEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQEsslNEDTPII 748
Cdd:cd19932    1 VRVLIAED-EALIRMdLREMLEEAgYEVVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITS---ENIAPIV 76
                         90       100       110
                 ....*....|....*....|....*....|..
gi 489048494 749 AVTAHALQSEKEQLLKDGFKGYLTKPIDEDML 780
Cdd:cd19932   77 LLTAYSQQDLVERAKEAGAMAYLVKPFSESDL 108
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
672-784 4.07e-16

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 82.20  E-value: 4.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQEssLNEDTPIIAVT 751
Cdd:PRK11361   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRS--HETRTPVILMT 83
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489048494 752 AHALQSEKEQLLKDGFKGYLTKPIDEDMLKQII 784
Cdd:PRK11361  84 AYAEVETAVEALRCGAFDYVIKPFDLDELNLIV 116
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
672-784 5.30e-16

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: 74.75  E-value: 5.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDN---DANLKLlhTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMP-IMDGITACKLIQEsslNEDTPI 747
Cdd:cd17534    2 KILIVEDEaiiALDLKE--ILESLGYEVVGIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIRE---KFDIPV 76
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489048494 748 IAVTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQII 784
Cdd:cd17534   77 IFLTAYSDEETLERAKETNPYGYLVKPFNERELKAAI 113
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
672-784 6.25e-16

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: 74.64  E-value: 6.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLH-TLLSEQIEVIEtAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPIIAV 750
Cdd:cd17562    2 KILAVDDSASIRQMVSfTLRGAGYEVVE-AADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILML 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489048494 751 TAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQII 784
Cdd:cd17562   81 TTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVV 114
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
402-508 8.42e-16

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: 74.11  E-value: 8.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 402 DPTRFKQVLINLLSNA---IKFTEKGSIKVDIshRLLDDERTSLLVSVTDTGVGIPMDKQDSLFTPFgqadssITRKFGG 478
Cdd:cd16944    1 DTTQISQVLTNILKNAaeaIEGRPSDVGEVRI--RVEADQDGRIVLIVCDNGKGFPREMRHRATEPY------VTTRPKG 72
                         90       100       110
                 ....*....|....*....|....*....|
gi 489048494 479 TGLGLIITKHIVEAMSGRITLNSAPGNGTC 508
Cdd:cd16944   73 TGLGLAIVKKIMEEHGGRISLSNREAGGAC 102
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
672-754 1.10e-15

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: 74.35  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSE--QIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSlneDTPIIA 749
Cdd:cd17541    2 RVLIVDDSAVMRKLLSRILESdpDIEVVGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAER---PTPVVM 78

                 ....*
gi 489048494 750 VTAHA 754
Cdd:cd17541   79 VSSLT 83
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
400-507 1.25e-15

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


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 73.59  E-value: 1.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 400 TGDPTRFKQVLINLLSNAIKFTEKGSIkVDIShrlLDDERTSLLVsVTDTGVGIPMDKQDSLFTPFGQADSSITrkfGGT 479
Cdd:cd16940    8 QGDALLLFLLLRNLVDNAVRYSPQGSR-VEIK---LSADDGAVIR-VEDNGPGIDEEELEALFERFYRSDGQNY---GGS 79
                         90       100
                 ....*....|....*....|....*...
gi 489048494 480 GLGLIITKHIVEAMSGRITLNSAPGNGT 507
Cdd:cd16940   80 GLGLSIVKRIVELHGGQIFLGNAQGGGL 107
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
671-784 1.36e-15

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: 73.91  E-value: 1.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 671 LKVLVVDDNDANLKLLHTLLSE-QIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPIIA 749
Cdd:cd19923    1 MKVLVVDDFSTMRRIIKNLLKElGFNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLM 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489048494 750 VTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQII 784
Cdd:cd19923   81 VTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKL 115
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
407-508 6.33e-15

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: 71.33  E-value: 6.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 407 KQVLINLLSNAIKFtekGSIKVDISHrllDDERTSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSitRKFGGTGLGLIIT 486
Cdd:cd16950    2 KRVLSNLVDNALRY---GGGWVEVSS---DGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNA--RGTSGTGLGLAIV 73
                         90       100
                 ....*....|....*....|..
gi 489048494 487 KHIVEAMSGRITLNSAPGNGTC 508
Cdd:cd16950   74 QRISDAHGGSLTLANRAGGGLC 95
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
670-814 9.07e-15

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 76.73  E-value: 9.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 670 PLKVLVVDDNDANLKLLHTLLSEQ--IEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSlneDTPI 747
Cdd:PRK00742   3 KIRVLVVDDSAFMRRLISEILNSDpdIEVVGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLR---PTPV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 748 IAVTAHALQSEKEQL--LKDGFKGYLTKP---IDEDMLK---------------QIISDHSPQTPVNRDKAKTDTPQSPA 807
Cdd:PRK00742  80 VMVSSLTERGAEITLraLELGAVDFVTKPflgISLGMDEykeelaekvraaaraRVRALPPRAAAAARAAAAAPAALAAA 159

                 ....*..
gi 489048494 808 PFQSSRI 814
Cdd:PRK00742 160 PLLSSKL 166
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
672-786 1.24e-14

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 71.04  E-value: 1.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLsEQI---EVIeTAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPII 748
Cdd:cd17552    3 RILVIDDEEDIREVVQACL-EKLagwEVL-TASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVI 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489048494 749 AVTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIISD 786
Cdd:cd17552   81 LLTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAK 118
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
412-511 1.36e-14

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


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 70.69  E-value: 1.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 412 NLLSNAIKFT-EKGSIKVdishRLLDDERTSLLvSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGGTGLGLIITKHIV 490
Cdd:cd16952    7 NLVSNAVKYTpPSDTITV----RWSQEESGARL-SVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAIVKHVM 81
                         90       100
                 ....*....|....*....|.
gi 489048494 491 EAMSGRITLNSAPGNGTCFTF 511
Cdd:cd16952   82 SRHDARLLIASELGKGSRFTC 102
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
673-782 3.05e-14

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: 69.87  E-value: 3.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSE--QIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIqeSSLNEDTPIIAV 750
Cdd:cd17532    1 ALIVDDEPLAREELRYLLEEhpDIEIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKL--SKLAKPPLIVFV 78
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489048494 751 TAH---ALQSEKEQLLkdgfkGYLTKPIDEDMLKQ 782
Cdd:cd17532   79 TAYdeyAVEAFELNAV-----DYLLKPFSEERLAE 108
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
674-775 4.54e-14

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: 69.22  E-value: 4.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 674 LVVDDNDANLKLL-HTLLSEQIEVIeTAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPIIAVTA 752
Cdd:cd19937    1 LVVDDEEDIVELLkYNLEKEGYEVV-TAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTA 79
                         90       100
                 ....*....|....*....|...
gi 489048494 753 HALQSEKEQLLKDGFKGYLTKPI 775
Cdd:cd19937   80 KGEEFDKVLGLELGADDYITKPF 102
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
293-512 7.37e-14

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 76.12  E-value: 7.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 293 FLAKMSHELRTPLNGVIGFTRQLYKTPLNKHQKDYLDTIMLSANSLMTIISDILDFSKLEAGAMELESIQFQLRDAVNEV 372
Cdd:PRK10618 453 FLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNMLETQDWKPEQELFSLQDLIDEV 532
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 373 MTLLAPSAHDKQLELSIYINQQVPDDLTGDPTRFKQVLINLLSNAIKFTEKGSIKVDISHRLLDDERtsLLVSVTDTGVG 452
Cdd:PRK10618 533 LPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYGKITLEVDQDESSPDR--LTIRILDTGAG 610
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489048494 453 IPMDKQDSLFTPF-GQADSSitrKFG-GTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTFN 512
Cdd:PRK10618 611 VSIKELDNLHFPFlNQTQGD---RYGkASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIH 669
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
672-784 7.85e-14

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: 68.40  E-value: 7.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQEssLNEDTPIIAVT 751
Cdd:cd17554    2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIRE--KKPDLPVIICT 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489048494 752 AHalqSEkeqlLKDGFK-----GYLTKPIDEDMLKQII 784
Cdd:cd17554   80 AY---SE----YKSDFSswaadAYVVKSSDLTELKETI 110
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-518 1.08e-13

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: 68.20  E-value: 1.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 408 QVLINLLSNAIKFTEKGSIKVDISHR-------LLDDERTSLLVSVTDTGVGIPMDKQDSLFTPFgqadssITRKFGGTG 480
Cdd:cd16918    3 QVFLNLVRNAAQALAGSGGEIILRTRtqrqvtlGHPRHRLALRVSVIDNGPGIPPDLQDTIFYPM------VSGRENGTG 76
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489048494 481 LGLIITKHIVEAMSGRITLNSAPGNgTCFTfnsvFSLP 518
Cdd:cd16918   77 LGLAIAQNIVSQHGGVIECDSQPGH-TVFS----VSLP 109
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
293-510 1.12e-13

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: 75.16  E-value: 1.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  293 FLAKMSHELRTPLNGVIGFTRQLYKTPLNKHQKDYLDTIMLSANSLMTIISDILDFSKLEAGAMELESIQFQLRDAVNEV 372
Cdd:TIGR03785 488 MSSRLSHELRTPVAVVRSSLENLELQALEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLSEVLSGC 567
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  373 MTLLAPSAHDKQLELSIYINQQVpddLTGDPTRFKQVLINLLSNAIKFTEKGSIkVDISHRLLDDERtslLVSVTDTGVG 452
Cdd:TIGR03785 568 MQGYQMTYPPQRFELNIPETPLV---MRGSPELIAQMLDKLVDNAREFSPEDGL-IEVGLSQNKSHA---LLTVSNEGPP 640
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  453 IPMDKQDSLFTPF-GQADSSITRKfGGTGLGLIITKHIVEAMSGRITL-NSAPGNGTCFT 510
Cdd:TIGR03785 641 LPEDMGEQLFDSMvSVRDQGAQDQ-PHLGLGLYIVRLIADFHQGRIQAeNRQQNDGVVFR 699
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
294-511 1.54e-13

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 73.81  E-value: 1.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 294 LAKMSHELRTPLngvigfTR-QLYKTPLNKHQKDY--LDTIMLSANSLMTIISDILDFSK------LEAGAMELESIQFQ 364
Cdd:PRK09470 247 LSDISHELRTPL------TRlQLATALLRRRQGESkeLERIETEAQRLDSMINDLLVLSRnqqknhLERETFKANSLWSE 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 365 -LRDAVNEVmtllapsahdKQLELSIYINQQV-PDDLTGDPTRFKQVLINLLSNAIKFTeKGSIKVDIShrlldDERTSL 442
Cdd:PRK09470 321 vLEDAKFEA----------EQMGKSLTVSAPPgPWPINGNPNALASALENIVRNALRYS-HTKIEVAFS-----VDKDGL 384
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489048494 443 LVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTF 511
Cdd:PRK09470 385 TITVDDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAIVENAIQQHRGWVKAEDSPLGGLRLTI 453
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
673-774 3.23e-13

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: 67.02  E-value: 3.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESslNEDTPIIAVTA 752
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAA--GNDLPILVLTA 78
                         90       100
                 ....*....|....*....|..
gi 489048494 753 HALQSEKEQLLKDGFKGYLTKP 774
Cdd:cd17627   79 RDSVSDRVAGLDAGADDYLVKP 100
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
380-510 3.79e-13

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 72.19  E-value: 3.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 380 AHDKQLELSIYINQQVPDdLTGDPTRFKQVLINLLSNAI-----KFTEKGSIKVDIShrlldDERTSLLVSVTDTGVGIP 454
Cdd:COG3290  257 ARERGIDLTIDIDSDLPD-LPLSDTDLVTILGNLLDNAIeavekLPEEERRVELSIR-----DDGDELVIEVEDSGPGIP 330
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489048494 455 MDKQDSLFTP-FgqadssITRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFT 510
Cdd:COG3290  331 EELLEKIFERgF------STKLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFT 381
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
287-350 4.84e-13

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


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 64.54  E-value: 4.84e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489048494 287 NRVKSDFLAKMSHELRTPLNGVIGFTRQLYKTPLNKH-QKDYLDTIMLSANSLMTIISDILDFSK 350
Cdd:cd00082    1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEeQREYLERIREEAERLLRLINDLLDLSR 65
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
671-848 4.96e-13

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 72.37  E-value: 4.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 671 LKVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQesSLNEDTPIIAV 750
Cdd:PRK10365   6 IDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIK--ALNPAIPVLIM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 751 TAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIISdhspQTPVNRDKAKTDTPQSPAPfQSSRIdwaqalqragGKSELA 830
Cdd:PRK10365  84 TAYSSVETAVEALKTGALDYLIKPLDFDNLQATLE----KALAHTHSIDAETPAVTAS-QFGMV----------GKSPAM 148
                        170
                 ....*....|....*...
gi 489048494 831 LEMLNMLLLSVPETLTLL 848
Cdd:PRK10365 149 QHLLSEIALVAPSEATVL 166
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
673-774 5.49e-13

phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a component of the KdpD/KdpE two-component system (TCS) and is activated when histidine kinase KdpD senses a drop in external K+ concentration or upshift in ionic osmolarity, resulting in the expression of a heterooligomeric transporter KdpFABC. In addition, the KdpD/KdpE TCS is also an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. KdpE is a member of the OmpR family of DNA-binding response regulators that contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 65.65  E-value: 5.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSlneDTPIIAVTA 752
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWS---AVPVIVLSA 77
                         90       100
                 ....*....|....*....|..
gi 489048494 753 HALQSEKEQLLKDGFKGYLTKP 774
Cdd:cd17620   78 RDEESDKIAALDAGADDYLTKP 99
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
673-754 1.00e-12

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: 65.60  E-value: 1.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLneDTPIIAVTA 752
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYP--DLPVIMISG 78

                 ..
gi 489048494 753 HA 754
Cdd:cd17550   79 HG 80
glnL PRK11073
nitrogen regulation protein NR(II);
297-510 1.09e-12

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 70.49  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 297 MSHELRTPLNGVIGFTRQLYKTPLNKHQKDYLDTIMLSANSLMTIISDILDFSKLeaGAMELESIQfQLRDAVNEVMTLL 376
Cdd:PRK11073 137 LAHEIKNPLGGLRGAAQLLSKALPDPALTEYTKVIIEQADRLRNLVDRLLGPQRP--GTHVTESIH-KVAERVVQLVSLE 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 377 APSahdkQLELSIYINQQVPDdLTGDPTRFKQVLINLLSNAIK-FTEKG---SIKVDISHRL-LDDERTSLL--VSVTDT 449
Cdd:PRK11073 214 LPD----NVRLIRDYDPSLPE-LAHDPDQIEQVLLNIVRNALQaLGPEGgtiTLRTRTAFQLtLHGERYRLAarIDIEDN 288
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489048494 450 GVGIPMDKQDSLFTPFgqadssITRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNgTCFT 510
Cdd:PRK11073 289 GPGIPPHLQDTLFYPM------VSGREGGTGLGLSIARNLIDQHSGKIEFTSWPGH-TEFS 342
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
670-805 1.85e-12

sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a transcription factor critical for the initiation of sporulation. It contains a response regulator receiver domain (pfam00072). In Bacillus subtilis, it works together with response regulator Spo0F and the phosphotransferase Spo0B, both of which are missing from at least some sporulating species and thus not part of the endospore forming bacteria minimal gene set. Spo0A, however, is universal among endospore-forming species. [Cellular processes, Sporulation and germination]


Pssm-ID: 131922 [Multi-domain]  Cd Length: 262  Bit Score: 68.67  E-value: 1.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  670 PLKVLVVDDNDANLKLLHTLLSEQ--IEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPI 747
Cdd:TIGR02875   2 KIRIVIADDNKEFCNLLKEYLAAQpdMEVVGVAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNEIELSARPRV 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489048494  748 IAVTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIISDHSPQTPVNRDKAKTDTPQS 805
Cdd:TIGR02875  82 IMLSAFGQEKITQRAVALGADYYVLKPFDLEILAARIRQLAWGTNADILADSPTVPPA 139
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
673-787 2.17e-12

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


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 64.57  E-value: 2.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSL--SKSHKYDIIFMDIQMPIMDGITACKLIQESSlneDTPIIAV 750
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMlrENKDEFDLVITDVHMPDMDGFEFLELIRLEM---DLPVIMM 77
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489048494 751 TAHALQSEKEQLLKDGFKGYLTKPIDEDMLKqIISDH 787
Cdd:cd17584   78 SADGSTSTVMKGLAHGACDYLLKPVSIEDLK-NIWQH 113
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
832-915 3.66e-12

Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072).


Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 62.75  E-value: 3.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  832 EMLNMLLLSVPETLTLLAKAIESNDCQQVLSIVHKFHGACCYTGVPKLKSLAETIETSLKNKcLLENIEPELFELQDELE 911
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLLREG-ELPLDPELLEALRDLLE 79

                  ....
gi 489048494  912 NLLA 915
Cdd:pfam01627  80 ALRA 83
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
670-736 4.06e-12

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: 64.14  E-value: 4.06e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489048494 670 PLKVLVVDDNDANLKLLHTLLSEQ--IEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLI 736
Cdd:COG2197    1 MIRVLIVDDHPLVREGLRALLEAEpdIEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
670-774 6.48e-12

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: 63.01  E-value: 6.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 670 PLKVLVVDDNDANLKLLHTLLSEQ--IEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPI 747
Cdd:cd17561    1 KIKVLIADDNREFVQLLEEYLNSQpdMEVVGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPKI 80
                         90       100
                 ....*....|....*....|....*..
gi 489048494 748 IAVTAHALQSEKEQLLKDGFKGYLTKP 774
Cdd:cd17561   81 IMLTAFGQEDITQRAVELGASYYILKP 107
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
293-508 6.90e-12

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 68.07  E-value: 6.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 293 FLAKMSHELRTPLNGVigftrqlyKTPLNKHQKDY-LDTIMLSA--NSLMTIISDILDFSKLEagaMELESIQFQLRDAV 369
Cdd:PRK10755 140 FTADVAHELRTPLAGI--------RLHLELLEKQHhIDVAPLIArlDQMMHTVEQLLQLARAG---QSFSSGHYQTVKLL 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 370 NEVMT--------LLApsAHDKQLELsiyinQQVPDDLT--GDPTRFKQVLINLLSNAIKFTEKGSikvDISHRLLDDER 439
Cdd:PRK10755 209 EDVILpsqdelseMLE--QRQQTLLL-----PESAADITvqGDATLLRLLLRNLVENAHRYSPEGS---TITIKLSQEDG 278
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 440 TSLLvSVTDTGVGIPMDKQDSLFTPFGQADSsitrKFGGTGLGLIITKHIVEAMSGRITL-NSAPGNGTC 508
Cdd:PRK10755 279 GAVL-AVEDEGPGIDESKCGELSKAFVRMDS----RYGGIGLGLSIVSRITQLHHGQFFLqNRQERSGTR 343
ompR PRK09468
osmolarity response regulator; Provisional
672-774 8.76e-12

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 66.15  E-value: 8.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDnDANLK-LLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESslNEDTPIIAV 750
Cdd:PRK09468   7 KILVVDD-DMRLRaLLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQ--NNPTPIIML 83
                         90       100
                 ....*....|....*....|....
gi 489048494 751 TAHALQSEKEQLLKDGFKGYLTKP 774
Cdd:PRK09468  84 TAKGEEVDRIVGLEIGADDYLPKP 107
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
671-725 9.27e-12

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 60.66  E-value: 9.27e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 489048494   671 LKVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMP 725
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
673-780 1.88e-11

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: 61.96  E-value: 1.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPIIAVTA 752
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489048494 753 halQSEKEQLLKD---GFKGYLTKPIDEDML 780
Cdd:cd17598   81 ---LSDPRDVIRGlecGADNFITKPYDEKYL 108
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
671-775 1.90e-11

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: 62.03  E-value: 1.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 671 LKVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSL--SKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTP-I 747
Cdd:cd19933    1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLlaSAEHSFQLVLLDLCMPEMDGFEVALRIRKLFGRRERPlI 80
                         90       100
                 ....*....|....*....|....*...
gi 489048494 748 IAVTAHALQSEKEQLLKDGFKGYLTKPI 775
Cdd:cd19933   81 VALTANTDDSTREKCLSLGMNGVITKPV 108
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
672-774 2.02e-11

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: 61.77  E-value: 2.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQ-IEVIEtAHNGSQAYSLSKSHKyDI--IFMDIQMPIMDGITACKLIQESSLNEDTPII 748
Cdd:cd17544    2 KVLVVDDSATSRNHLRALLRRHnFQVLE-AANGQEALEVLEQHP-DIklVITDYNMPEMDGFELVREIRKKYSRDQLAII 79
                         90       100
                 ....*....|....*....|....*.
gi 489048494 749 AVTAHALQSEKEQLLKDGFKGYLTKP 774
Cdd:cd17544   80 GISASGDNALSARFIKAGANDFLTKP 105
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
673-787 2.49e-11

phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex aeolicus and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include Aquifex aeolicus NtrC1 and Vibrio quorum-sensing signal integrator LuxO. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 61.83  E-value: 2.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNedTPIIAVTA 752
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLP--TSVIVITA 78
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489048494 753 HALQSEKEQLLKDGFKGYLTKPIDEDMLKQIISDH 787
Cdd:cd17572   79 HGSVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNA 113
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
380-510 2.71e-11

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 67.25  E-value: 2.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 380 AHDKQLELSIYINQQVPDdlTGDPtRFKQVLI----NLLSN---AIKFTEKGSIKVDISHRlldDERtsLLVSVTDTGVG 452
Cdd:PRK11086 407 ARELGITLIISEDSQLPD--SGDE-DQVHELItilgNLIENaleAVGGEEGGEISVSLHYR---NGW--LHCEVSDDGPG 478
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489048494 453 IPMDKQDSLFTpfgQADSSitrKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFT 510
Cdd:PRK11086 479 IAPDEIDAIFD---KGYST---KGSNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFF 530
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
672-774 3.41e-11

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


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 61.11  E-value: 3.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQ-IEVIEtAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPIIAV 750
Cdd:cd17618    2 TILIVEDEPAIREMIAFNLERAgFDVVE-AEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIML 80
                         90       100
                 ....*....|....*....|....
gi 489048494 751 TAHALQSEKEQLLKDGFKGYLTKP 774
Cdd:cd17618   81 TARGEEEDKVRGLEAGADDYITKP 104
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
673-774 4.17e-11

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: 60.15  E-value: 4.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESslNEDTPIIAVTA 752
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAA--GKQTPVLMLTA 78
                         90       100
                 ....*....|....*....|..
gi 489048494 753 HALQSEKEQLLKDGFKGYLTKP 774
Cdd:cd19935   79 RDSVEDRVKGLDLGADDYLVKP 100
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
672-774 4.50e-11

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: 60.83  E-value: 4.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESslNEDTPIIAVT 751
Cdd:cd17615    1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRAD--GPDVPVLFLT 78
                         90       100
                 ....*....|....*....|...
gi 489048494 752 AHALQSEKEQLLKDGFKGYLTKP 774
Cdd:cd17615   79 AKDSVEDRIAGLTAGGDDYVTKP 101
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
671-787 7.30e-11

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: 60.24  E-value: 7.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 671 LKVLVVDDNDANLKLLHTLLSEQIEV-IETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLneDTPIIA 749
Cdd:cd17593    1 MKVLICDDSSMARKQLARALPADWDVeITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQL--ETKVIV 78
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489048494 750 VTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIISDH 787
Cdd:cd17593   79 VSGDVQPEAKERVLELGALAFLKKPFDPEKLAQLLEEL 116
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
672-752 7.55e-11

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 64.52  E-value: 7.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQ--IEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSlneDTPIIA 749
Cdd:PRK12555   2 RIGIVNDSPLAVEALRRALARDpdHEVVWVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAER---PCPILI 78

                 ...
gi 489048494 750 VTA 752
Cdd:PRK12555  79 VTS 81
PRK15115 PRK15115
response regulator GlrR; Provisional
670-798 7.62e-11

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 65.24  E-value: 7.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 670 PLKVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQEssLNEDTPIIA 749
Cdd:PRK15115   5 PAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQK--VQPGMPVII 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489048494 750 VTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIISDHSPQTPVNRDKA 798
Cdd:PRK15115  83 LTAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQSAPATDER 131
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
673-774 8.78e-11

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


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 59.70  E-value: 8.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSK---------SHKYDIIFMDIQMPIMDGITACKLIQESSLNE 743
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLEnlakegndlSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489048494 744 DTPIIAVTAHALQSEKEQLLKDGFKGYLTKP 774
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
673-777 9.90e-11

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 59.98  E-value: 9.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLS--EQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLneDTPIIAV 750
Cdd:cd19930    1 VLIAEDQEMVRGALAALLEleDDLEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELP--DTKVLIV 78
                         90       100
                 ....*....|....*....|....*....
gi 489048494 751 TAHALQSEKEQLLKDGFKGYLTK--PIDE 777
Cdd:cd19930   79 TTFGRPGYFRRALAAGVDGYVLKdrPIEE 107
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
673-774 1.29e-10

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: 59.36  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSlneDTPIIAVTA 752
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTS---NVPIIMLTA 77
                         90       100
                 ....*....|....*....|..
gi 489048494 753 HALQSEKEQLLKDGFKGYLTKP 774
Cdd:cd17614   78 KDSEVDKVLGLELGADDYVTKP 99
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
406-509 1.33e-10

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: 59.32  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 406 FKQVLINLLSNAIK-FTEKGSIKVDISHRLLDDERTS----------LLVSVTDTGVGIPMDKQDSLFTPFgqadsSITR 474
Cdd:cd16919    1 LELAILNLAVNARDaMPEGGRLTIETSNQRVDADYALnyrdlipgnyVCLEVSDTGSGMPAEVLRRAFEPF-----FTTK 75
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489048494 475 KFG-GTGLGLIITKHIVEAMSGRITLNSAPGNGTCF 509
Cdd:cd16919   76 EVGkGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTV 111
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
672-779 1.37e-10

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: 59.52  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDA-NLKLLHTLLSEQIEVIEtAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSlnEDTPIIAV 750
Cdd:cd17555    2 TILVIDDDEVvRESIAAYLEDSGFQVLQ-AADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKES--PDTPVIVV 78
                         90       100
                 ....*....|....*....|....*....
gi 489048494 751 TAHALQSEKEQLLKDGFKGYLTKPIdEDM 779
Cdd:cd17555   79 SGAGVMSDAVEALRLGAWDYLTKPI-EDL 106
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
402-506 1.38e-10

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: 59.01  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 402 DPTRFKQVLINLLSNAIKFTEKGSIkVDISHRlLDDERTSLLvsVTDTGVGIPMDKQDSLFTPFgqadSSITRKFGG--- 478
Cdd:cd16945    1 DPFLLRQAINNLLDNAIDFSPEGGL-IALQLE-ADTEGIELL--VFDEGSGIPDYALNRVFERF----YSLPRPHSGqks 72
                         90       100
                 ....*....|....*....|....*...
gi 489048494 479 TGLGLIITKHIVEAMSGRITLNSAPGNG 506
Cdd:cd16945   73 TGLGLAFVQEVAQLHGGRITLRNRPDGV 100
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
672-784 1.80e-10

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: 58.95  E-value: 1.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLL-HTLLSEQIEVIeTAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQEssLNEDTPIIAV 750
Cdd:cd17569    2 TILLVDDEPNILKALkRLLRREGYEVL-TATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRE--RYPDTVRILL 78
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489048494 751 TAHAlqsEKEQLLK---DG--FKgYLTKPIDEDMLKQII 784
Cdd:cd17569   79 TGYA---DLDAAIEainEGeiYR-FLTKPWDDEELKETI 113
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
673-774 1.99e-10

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: 58.54  E-value: 1.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPIIAVTA 752
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80
                         90       100
                 ....*....|....*....|..
gi 489048494 753 HALQSEKEQLLKDGFKGYLTKP 774
Cdd:cd19927   81 KGMTSDRIKGYNAGCDGYLSKP 102
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
673-776 2.12e-10

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: 58.86  E-value: 2.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSlneDTPIIAVTA 752
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTS---QVPVLMLTA 77
                         90       100
                 ....*....|....*....|....
gi 489048494 753 HALQSEKEQLLKDGFKGYLTKPID 776
Cdd:cd17623   78 RGDDIDRILGLELGADDYLPKPFN 101
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
412-510 2.34e-10

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


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 58.45  E-value: 2.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 412 NLLSNAIKFTEKGSIKVDISHRLLDDERTSLLVSVTDTGVGIPMDKQDSLFtpfgQADSSiTRKFGGTGLGLIITKHIVE 491
Cdd:cd16915    7 NLIDNALDALAATGAPNKQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVF----ERGVS-TKGQGERGIGLALVRQSVE 81
                         90
                 ....*....|....*....
gi 489048494 492 AMSGRITLNSAPGNGTCFT 510
Cdd:cd16915   82 RLGGSITVESEPGGGTTFS 100
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
674-780 2.45e-10

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


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 58.77  E-value: 2.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 674 LVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESslNEDTPIIAVTAH 753
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREE--GIETPVLLLTAL 78
                         90       100
                 ....*....|....*....|....*..
gi 489048494 754 ALQSEKEQLLKDGFKGYLTKPIDEDML 780
Cdd:cd17625   79 DAVEDRVKGLDLGADDYLPKPFSLAEL 105
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
672-836 4.17e-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: 59.54  E-value: 4.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQ-IEViETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQEssLNEDTPIIAV 750
Cdd:COG4567    6 SLLLVDDDEAFARVLARALERRgFEV-TTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRE--RDPDARIVVL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 751 TAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIISDHSPQTPVNrdkakTDTPQSPAPFQSSRIDwaQALQRAGGKSELA 830
Cdd:COG4567   83 TGYASIATAVEAIKLGADDYLAKPADADDLLAALERAEGDAPAP-----PENPMSLDRLEWEHIQ--RVLAECDGNISAT 155

                 ....*.
gi 489048494 831 LEMLNM 836
Cdd:COG4567  156 ARALGM 161
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
672-774 6.36e-10

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: 57.48  E-value: 6.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSlneDTPIIAVT 751
Cdd:cd17626    2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAES---GVPIVMLT 78
                         90       100
                 ....*....|....*....|...
gi 489048494 752 AHALQSEKEQLLKDGFKGYLTKP 774
Cdd:cd17626   79 AKSDTVDVVLGLESGADDYVAKP 101
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
673-774 6.46e-10

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: 57.68  E-value: 6.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNdanlKLLHTLLSEQIE----VIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITackLIQE-SSLNEDTPI 747
Cdd:cd19934    1 LLLVEDD----ALLAAQLKEQLSdagyVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLS---VLRRwRSEGRATPV 73
                         90       100
                 ....*....|....*....|....*..
gi 489048494 748 IAVTAHALQSEKEQLLKDGFKGYLTKP 774
Cdd:cd19934   74 LILTARDSWQDKVEGLDAGADDYLTKP 100
PRK10610 PRK10610
chemotaxis protein CheY;
671-785 8.05e-10

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 57.68  E-value: 8.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 671 LKVLVVDDNDANLKLLHTLLSE-QIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPIIA 749
Cdd:PRK10610   6 LKFLVVDDFSTMRRIVRNLLKElGFNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLM 85
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489048494 750 VTAHAlqsEKEQLL---KDGFKGYLTKPIDEDMLKQIIS 785
Cdd:PRK10610  86 VTAEA---KKENIIaaaQAGASGYVVKPFTAATLEEKLN 121
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
409-509 8.84e-10

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


Pssm-ID: 340400 [Multi-domain]  Cd Length: 102  Bit Score: 56.63  E-value: 8.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 409 VLINLLSNAIKFTEKGSIkVDIShRLLDDERTSllVSVTDTGVGIPMDKQDSLFTPFGQADSSitRKFGGTGLGLIITKH 488
Cdd:cd16923    4 VFSNLLSNAIKYSPENTR-IYIT-SFLTDDVVN--IMFKNPSSHPLDFKLEKLFERFYRGDNS--RNTEGAGLGLSIAKA 77
                         90       100
                 ....*....|....*....|.
gi 489048494 489 IVEAMSGRITLNSApGNGTCF 509
Cdd:cd16923   78 IIELHGGSASAEYD-DNHDLF 97
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
672-784 1.14e-09

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: 57.04  E-value: 1.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSE-QIEV-IETAHNGSQA--YsLSKSHKY------DIIFMDIQMPIMDGITACKLIQESSL 741
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEaGVPNeLHVVRDGEEAldF-LRGEGEYadaprpDLILLDLNMPRMDGFEVLREIKADPD 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489048494 742 NEDTPIIAVTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQII 784
Cdd:cd17557   80 LRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAI 122
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-510 2.06e-09

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: 56.04  E-value: 2.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 408 QVLINLLSNAIKFTEKGSIKVDIShrlLDDERTSLLVSVTDTGVGIPMDKQDSLFTPFgQADSSITRKFG-GTGLGLIIT 486
Cdd:cd16953    3 QVLRNLIGNAISFSPPDTGRITVS---AMPTGKMVTISVEDEGPGIPQEKLESIFDRF-YTERPANEAFGqHSGLGLSIS 78
                         90       100
                 ....*....|....*....|....*...
gi 489048494 487 KHIVEAMSGRITLN--SAPGN--GTCFT 510
Cdd:cd16953   79 RQIIEAHGGISVAEnhNQPGQviGARFT 106
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
382-509 2.19e-09

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


Pssm-ID: 340430 [Multi-domain]  Cd Length: 135  Bit Score: 56.49  E-value: 2.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 382 DKQLELSIYInqqvPDDLT--GDPTRFKQVLINLLSNAIKFTEKgsiKVDISHRLLDDErtsLLVSVTDTGVGIPMDKQD 459
Cdd:cd16954   16 RKGVSISLDI----SPELRfpGERNDLMELLGNLLDNACKWCLE---FVEVTARQTDGG---LHLIVDDDGPGVPESQRS 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489048494 460 SLFTPFGQADSSITrkfgGTGLGLIITKHIVEAMSGRITLNSAPGNGTCF 509
Cdd:cd16954   86 KIFQRGQRLDEQRP----GQGLGLAIAKEIVEQYGGELSLSDSPLGGARF 131
orf27 CHL00148
Ycf27; Reviewed
672-774 2.92e-09

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 58.57  E-value: 2.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSlneDTPIIAVT 751
Cdd:CHL00148   8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKES---DVPIIMLT 84
                         90       100
                 ....*....|....*....|...
gi 489048494 752 AHALQSEKEQLLKDGFKGYLTKP 774
Cdd:CHL00148  85 ALGDVSDRITGLELGADDYVVKP 107
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
672-774 4.65e-09

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: 54.82  E-value: 4.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHK-YDIIFMDIQMPIMDGITACKLIQEssLNEDTPIIAV 750
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKdIDIVVTDIVMPEMDGIELAREARK--IDPDVKILFI 78
                         90       100
                 ....*....|....*....|....
gi 489048494 751 TAHALQSEKEQLLKDGFKGYLTKP 774
Cdd:cd18160   79 SGGAAAAPELLSDAVGDNATLKKP 102
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
671-782 4.83e-09

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: 54.94  E-value: 4.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 671 LKVLVVDDnDANLKLLHTLLSEQIE---VIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGItacKLIQE-SSLNEDTP 746
Cdd:cd19925    1 INVLIVED-DPMVAEIHRAYVEQVPgftVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGL---DLLRElRAAGHDVD 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489048494 747 IIAVTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQ 782
Cdd:cd19925   77 VIVVTAANDVETVREALRLGVVDYLIKPFTFERLRQ 112
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
673-774 8.57e-09

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: 53.91  E-value: 8.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPIIAVTA 752
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTG 80
                         90       100
                 ....*....|....*....|..
gi 489048494 753 HALQSEKEQLLKDGFKGYLTKP 774
Cdd:cd17602   81 KDGLVDRIRAKMAGASGYLTKP 102
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
145-499 9.69e-09

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


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 58.74  E-value: 9.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 145 WDPSAFQSSLGTVIIQLNKDQAVIGQQRALLISGIVIILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLND 224
Cdd:COG3850   88 ALLSLLLLLLLLLLLLLLLLLLLLAAAINRKLALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGDFDARVPV 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 225 NMIGEFELLREGLNTIAHTMvmqkdemqknidqatSDYRETLEQYEtsnielsfAKKEAQDANRVKSDFLAKMSHELRTP 304
Cdd:COG3850  168 SGRDELGTLARAFNRMADEL---------------QELYAELEEEE--------ELEAELELLALLDELLLLAALLLLLA 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 305 LNGVIGFTRQLYKTPLNKHQKDYLDTIMLSANSLMTIISDILDFSKLEAGAMELESIQFQLRDAVNEVMTLLAPSAHDKQ 384
Cdd:COG3850  225 LLLALLLAALLAALLLLLLLQDALAESELLALNILAGLLELLLALLLLLLASALLLLELELLALLLELVELLALAAAEEA 304
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 385 LELSIYINQQVPDDLTGDPTRFKQVLINLLSNAIKFTEKGSIKVDISHRLLDDERTSLLVSVTDTGVGIPMDKQDSLFTP 464
Cdd:COG3850  305 LLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELASILALQAALEAAAAGAALAAAAAAAGLARALAQAGADAAE 384
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 489048494 465 FGQADSSITRKFGGTGLGLIITKHIVEAMSGRITL 499
Cdd:COG3850  385 ALGLLAEASEGAAGQGAGLVDVEGGVAGEGGLVVL 419
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
670-783 1.30e-08

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 56.19  E-value: 1.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 670 PLKVLVVDDNDANLKLLHTLLS--EQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLneDTPI 747
Cdd:PRK10651   6 PATILLIDDHPMLRTGVKQLISmaPDITVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSL--SGRI 83
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489048494 748 IAVTAHALQSEKEQLLKDGFKGYLTKPID-EDMLKQI 783
Cdd:PRK10651  84 VVFSVSNHEEDVVTALKRGADGYLLKDMEpEDLLKAL 120
PRK09483 PRK09483
response regulator; Provisional
671-811 2.82e-08

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 55.11  E-value: 2.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 671 LKVLVVDDNDANLKLLHTLLSEQ--IEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESslNEDTPII 748
Cdd:PRK09483   2 INVLLVDDHELVRAGIRRILEDIkgIKVVGEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKILRY--TPDVKII 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489048494 749 AVTAHALQSEKEQLLKDGFKGYLTK-PIDEDMLKQIISDHSPQTPVNRDKAKTD-----TPQSPAPFQS 811
Cdd:PRK09483  80 MLTVHTENPLPAKVMQAGAAGYLSKgAAPQEVVSAIRSVHSGQRYIASDIAQQMalsqiEPATENPFAS 148
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
672-780 5.83e-08

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 54.42  E-value: 5.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKShKYDIIFMDIQMPIMDGITACKLIQEsslNEDTPIIAVT 751
Cdd:PRK10955   3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDD-SIDLLLLDVMMPKKNGIDTLKELRQ---THQTPVIMLT 78
                         90       100
                 ....*....|....*....|....*....
gi 489048494 752 AHALQSEKEQLLKDGFKGYLTKPIDEDML 780
Cdd:PRK10955  79 ARGSELDRVLGLELGADDYLPKPFNDREL 107
resp_reg_YycF NF040534
response regulator YycF;
672-774 6.81e-08

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 54.34  E-value: 6.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLH-TLLSEQIEVIeTAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESslnEDTPIIAV 750
Cdd:NF040534   2 KILVVDDEKPIADILEfNLKKEGYEVF-CAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVRKK---YDMPIIML 77
                         90       100
                 ....*....|....*....|....
gi 489048494 751 TAHALQSEKEQLLKDGFKGYLTKP 774
Cdd:NF040534  78 TAKDSEIDKVLGLELGADDYVTKP 101
PRK11517 PRK11517
DNA-binding response regulator HprR;
671-794 7.39e-08

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 54.13  E-value: 7.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 671 LKVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESslnEDTPIIAV 750
Cdd:PRK11517   1 MKILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTA---KQTPVICL 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489048494 751 TAHALQSEKEQLLKDGFKGYLTKPID-EDMLKQIISDHSPQTPVN 794
Cdd:PRK11517  78 TARDSVDDRVRGLDSGANDYLVKPFSfSELLARVRAQLRQHHALN 122
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
673-784 8.24e-08

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


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 51.72  E-value: 8.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDnDANLK--LLHTLLSEQIEVIETAhNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQEssLNEDTPIIAV 750
Cdd:cd17549    1 VLLVDD-DADVReaLQQTLELAGFRVRAFA-DAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRE--LDPDLPVILI 76
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489048494 751 TAH-----ALQSekeqlLKDGFKGYLTKPIDEDMLKQII 784
Cdd:cd17549   77 TGHgdvpmAVEA-----MRAGAYDFLEKPFDPERLLDVV 110
PRK11697 PRK11697
two-component system response regulator BtsR;
671-790 8.54e-08

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 54.08  E-value: 8.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 671 LKVLVVDDNDANLKLLHTLLSEQ--IEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGItacKLIqeSSLNEDT-P- 746
Cdd:PRK11697   2 IKVLIVDDEPLAREELRELLQEEgdIEIVGECSNAIEAIGAIHRLKPDVVFLDIQMPRISGL---ELV--GMLDPEHmPy 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489048494 747 IIAVTAH---ALQSEKEQLLKdgfkgYLTKPIDEDMLKQIIS----DHSPQ 790
Cdd:PRK11697  77 IVFVTAFdeyAIKAFEEHAFD-----YLLKPIDPARLAKTLArlrqERSPQ 122
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
413-511 8.67e-08

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: 51.13  E-value: 8.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 413 LLSNAIKFTEKGSikvDISHRLLDDERTSLLvSVTDTGVGIPmdKQD--SLFTPF--GQADssitRKFG-GTGLGLIITK 487
Cdd:cd16948   13 IVSNALKYSKQGG---KIEIYSETNEQGVVL-SIKDFGIGIP--EEDlpRVFDKGftGENG----RNFQeSTGMGLYLVK 82
                         90       100
                 ....*....|....*....|....
gi 489048494 488 HIVEAMSGRITLNSAPGNGTCFTF 511
Cdd:cd16948   83 KLCDKLGHKIDVESEVGEGTTFTI 106
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
672-778 1.04e-07

phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; DNA-binding transcriptional regulator NtrC is also called nitrogen regulation protein NR(I) or nitrogen regulator I (NRI). It contains an N-terminal receiver (REC) domain, followed by a sigma-54 interaction domain, and a C-terminal helix-turn-helix DNA-binding domain. It is part of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. DNA-binding response regulator NtrC is phosphorylated by NtrB; phosphorylation of the N-terminal REC domain activates the central sigma-54 interaction domain and leads to the transcriptional activation from promoters that require sigma(54)-containing RNA polymerase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 51.12  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDA-NLKLLHTLLSEQIEViETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESslNEDTPIIAV 750
Cdd:cd19919    2 TVWIVDDDSSiRWVLERALAGAGLTV-TSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQR--HPDLPVIIM 78
                         90       100
                 ....*....|....*....|....*....
gi 489048494 751 TAHA-LQSEKEQLLKDGFKgYLTKPIDED 778
Cdd:cd19919   79 TAHSdLDSAVSAYQGGAFE-YLPKPFDID 106
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
673-780 1.49e-07

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: 50.87  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLneDTPIIAVTA 752
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKV--KTPILILSG 78
                         90       100
                 ....*....|....*....|....*...
gi 489048494 753 HALQSEKEQLLKDGFKGYLTKPIDEDML 780
Cdd:cd17616   79 LADIEDKVKGLGFGADDYMTKPFHKDEL 106
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
672-789 2.44e-07

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: 50.25  E-value: 2.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQEssLNEDTPIIAVT 751
Cdd:cd17553    2 KILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKV--IDENIRVIIMT 79
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489048494 752 AHALQSEKEQLLKDGFKGYLTKPIDEDMLKQIISDHSP 789
Cdd:cd17553   80 AYGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYLP 117
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
672-774 2.47e-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: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSlneDTPIIAVT 751
Cdd:cd19939    1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHS---HVPILMLT 77
                         90       100
                 ....*....|....*....|...
gi 489048494 752 AHALQSEKEQLLKDGFKGYLTKP 774
Cdd:cd19939   78 ARTEEMDRVLGLEMGADDYLCKP 100
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
671-774 3.76e-07

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 52.23  E-value: 3.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 671 LKVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQesSLNEDTPIIAV 750
Cdd:PRK09836   1 MKLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLR--SANKGMPILLL 78
                         90       100
                 ....*....|....*....|....
gi 489048494 751 TAHALQSEKEQLLKDGFKGYLTKP 774
Cdd:PRK09836  79 TALGTIEHRVKGLELGADDYLVKP 102
PRK10693 PRK10693
two-component system response regulator RssB;
700-782 6.06e-07

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 52.30  E-value: 6.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 700 AHNGSQAYSLSKSHKYDIIFMDIQMPIMDGIT-ACKLIQESSlneDTPIIAVTAHALQSEKEQLLKDGFKGYLTKPI-DE 777
Cdd:PRK10693   3 AANGVDALELLGGFTPDLIICDLAMPRMNGIEfVEHLRNRGD---QTPVLVISATENMADIAKALRLGVQDVLLKPVkDL 79

                 ....*
gi 489048494 778 DMLKQ 782
Cdd:PRK10693  80 NRLRE 84
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
672-776 6.43e-07

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 48.98  E-value: 6.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSlneDTPIIAVT 751
Cdd:cd17594    1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARS---DVPIIIIS 77
                         90       100
                 ....*....|....*....|....*.
gi 489048494 752 AHALQ-SEKEQLLKDGFKGYLTKPID 776
Cdd:cd17594   78 GDRRDeIDRVVGLELGADDYLAKPFG 103
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
1-500 1.10e-06

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 52.42  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494   1 MTKLGLRDSVLTLTLIPTVIIGLLLGGYFTINRYIELDEILYQQGTTISEPLAIALEQPMLEKNKQLLNRLISYTHNKHS 80
Cdd:COG2770   38 ALLLLLLLLLALLLLLLLLLLLLLAALVLLALLLAAALLLLLLLLSLVALAALLLALLLLLLLALLLLLAALLLLLLLAA 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  81 PTIKSIAIFDKNNALLMTSNYHRSFEKLISQKTLINLKTTHVQKSDELVTFFTPIINHTSHDSKWDPSAFQSSLGTVIIQ 160
Cdd:COG2770  118 LALLLLLLLLLAALLALLLALALLALLLGLAAARLLLAALLALAAALALALGAGELLLLADLAAAIAALLAALLLLLLGG 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 161 LNKDQAVIGQQRALLISGIVIILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTGLNDNMIGEFELLREGLNTI 240
Cdd:COG2770  198 LLLVVLLEAALAALLLLLLLALLALLLALLLALLLARRITRPLRRLAEAARRIAAGDLDVRIPVSRKDEIGELARAFNRM 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 241 AHTMVMQKDEMQKNIDQATSDYRETLEQYETSNIELSFAKKEAQDANRVKSDFLAKMSHELRTPLNGVIGFTRQLYKTPL 320
Cdd:COG2770  278 ADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADLLLALALA 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 321 NKHQKDYLDTIMLSANSLMTIISDILDFSKLEAGAMELESIQFQLRDAVNEVMTLLAPSAHDKQLELSIYINQQVPDDLT 400
Cdd:COG2770  358 ALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALALLALAAAAAAAEAAAAA 437
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 401 GDPTRFKQVLINLLSNAIKFTEKGSIKVDISHRLLDDERTSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRKFGGTG 480
Cdd:COG2770  438 LELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEEEEEAGAAAEELAEELLLLEGLLL 517
                        490       500
                 ....*....|....*....|
gi 489048494 481 LGLIITKHIVEAMSGRITLN 500
Cdd:COG2770  518 LLLLEAEALEVAEELLELEE 537
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
673-783 2.11e-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: 47.34  E-value: 2.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQ--IEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLneDTPIIAV 750
Cdd:cd19931    1 VLLIDDHPLLRKGIKQLIELDpdFTVVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGV--SARIVIL 78
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489048494 751 TAHALQSEKEQLLKDGFKGYLTKPID-EDMLKQI 783
Cdd:cd19931   79 TVSDAEDDVVTALRAGADGYLLKDMEpEDLLEAL 112
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
402-511 2.11e-06

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: 47.07  E-value: 2.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 402 DPTRFKQVLINLLSNAIKFT-EKGSIKVDIShrlldDERTSLLVSVTDTGVGIP-MDKQDSLfTPFGQADSSITRKfGGT 479
Cdd:cd16975    1 DTLLLSRALINIISNACQYApEGGTVSISIY-----DEEEYLYFEIWDNGHGFSeQDLKKAL-ELFYRDDTSRRSG-GHY 73
                         90       100       110
                 ....*....|....*....|....*....|..
gi 489048494 480 GLGLIITKHIVEAMSGRITLNSAPGNGTCFTF 511
Cdd:cd16975   74 GMGLYIAKNLVEKHGGSLIIENSQKGGAEVTV 105
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
675-775 2.23e-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: 2.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 675 VVDDNDANLKLLHTLLSEQI--EVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITackLIQE-SSLNEDTPIIAVT 751
Cdd:cd17565    3 IVDDDKNIIKILSDIIEDDDlgEVVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQ---LVRKlKDTGSNGKFIMIS 79
                         90       100
                 ....*....|....*....|....
gi 489048494 752 AHALQSEKEQLLKDGFKGYLTKPI 775
Cdd:cd17565   80 QVSDKEMIGKAYQAGIEFFINKPI 103
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
673-774 2.45e-06

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: 46.76  E-value: 2.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLneDTPIIAVTA 752
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLP--QTPVAVITA 78
                         90       100
                 ....*....|....*....|..
gi 489048494 753 HALQSEKEQLLKDGFKGYLTKP 774
Cdd:cd19926   79 YGSLDTAIEALKAGAFDFLTKP 100
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
365-510 3.01e-06

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 50.99  E-value: 3.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 365 LRDAVN--EVMTLLAPSAHD-KQLELSIYIN-----QQVPDDLtgDPTRFKQVLINLLSNAIKF---TEKGSIKVDIshr 433
Cdd:PRK15053 386 LREAFAdrQVAGLLFGKVQRaRELGLKMVIVpgsqlSQLPPGL--DSTEFAAIVGNLLDNAFEAslrSDEGNKIVEL--- 460
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489048494 434 LLDDERTSLLVSVTDTGVGIPMDKQDSLFTpfgQADSSITRKFGGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFT 510
Cdd:PRK15053 461 FLSDEGDDVVIEVADQGCGVPESLRDKIFE---QGVSTRADEPGEHGIGLYLIASYVTRCGGVITLEDNDPCGTLFS 534
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
336-520 3.04e-06

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 50.67  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 336 NSLMTIISdILDfskLEAGAMELESIQFQLRDAVNEVMTL------LAPSAHDKQLELSIYINQQVPD------------ 397
Cdd:COG3920  308 NNLQVVSS-LLR---LQARRADDPEAREALEESQNRIQALalvhelLYQSEDWEGVDLRDYLRELLEPlrdsyggrgiri 383
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 398 DLTGDPTRFKQ-------VLIN-LLSNAIKF----TEKGSIKVDIShrlLDDERtsLLVSVTDTGVGIPmdkqdslftpf 465
Cdd:COG3920  384 ELDGPDVELPAdaavplgLILNeLVTNALKHaflsGEGGRIRVSWR---REDGR--LRLTVSDNGVGLP----------- 447
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489048494 466 gqADSSITRkfgGTGLGLIITKHIVEAMSGRITLNSapGNGTCFTFnsVFSLPNH 520
Cdd:COG3920  448 --EDVDPPA---RKGLGLRLIRALVRQLGGTLELDR--PEGTRVRI--TFPLAEL 493
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
672-798 3.49e-06

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: 46.60  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSlneDTPIIAVT 751
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFS---DVPIIMVT 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489048494 752 AHALQSEKEQLLKDGFKGYLTKPidedmlkqiisdHSPQTPVNRDKA 798
Cdd:cd19938   78 ARVEEIDRLLGLELGADDYICKP------------YSPREVVARVKA 112
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
672-780 3.83e-06

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: 46.60  E-value: 3.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSlneDTPIIAVT 751
Cdd:cd17622    2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKY---QGPILLLT 78
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489048494 752 ahALQSEKEQL--LKDGFKGYLTKPIDEDML 780
Cdd:cd17622   79 --ALDSDIDHIlgLELGADDYVVKPVEPAVL 107
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
672-780 4.50e-06

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: 46.28  E-value: 4.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQEssLNEDTPIIAVT 751
Cdd:cd17563    2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRA--LQPDARIVVLT 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489048494 752 -----AHALQSekeqlLKDGFKGYLTKPIDEDML 780
Cdd:cd17563   80 gyasiATAVEA-----IKLGADDYLAKPADADEI 108
REC_LytTR_AgrA-like cd17533
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; ...
671-786 4.51e-06

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AgrA-like group of LytTR/AlgR family response regulators are Staphylococcus aureus accessory gene regulator protein A (AgrA) and Streptococcus pneumoniae response regulator ComE, which are members of two-component regulatory systems. AgrA is a global regulator that controls the synthesis of virulence factors and other exoproteins. ComE is part of the ComD-ComE system that is part of a quorum-sensing signaling pathway that controls the development of competence, a physiological state required for genetic transformation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381088 [Multi-domain]  Cd Length: 131  Bit Score: 46.85  E-value: 4.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 671 LKVLVVDDNDANLKLLHTLLSEQIE------VIETAHNGSQ---AYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESsl 741
Cdd:cd17533    1 MNIFILEDDKIQRVRLEEIIENILKienieyVIELTGKTEElleKIKERGKNGIYFLDIDIKMEEKNGLEVAQKIRKY-- 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489048494 742 NEDTPIIAVTAHalqsekEQLLKDGFK------GYLTKPIDEDMLKQIISD 786
Cdd:cd17533   79 DPYAIIIFVTTH------SEFAPLTFEykvaalDFILKPLKLEEFKKRIEE 123
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
673-774 6.45e-06

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: 45.65  E-value: 6.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSlneDTPIIAVTA 752
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARS---NVPVIMVTA 77
                         90       100
                 ....*....|....*....|..
gi 489048494 753 HALQSEKEQLLKDGFKGYLTKP 774
Cdd:cd17621   78 KDSEIDKVVGLELGADDYVTKP 99
PRK10337 PRK10337
sensor protein QseC; Provisional
293-512 7.25e-06

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 49.65  E-value: 7.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 293 FLAKMSHELRTPLNG--VIGFTRQLYK--TPLNKHQKDYLDTIMLSANSLmtiISDILDFSKLEAGA--MELESIQFQ-- 364
Cdd:PRK10337 240 FTSDAAHELRSPLAAlkVQTEVAQLSDddPQARKKALLQLHAGIDRATRL---VDQLLTLSRLDSLDnlQDVAEIPLEdl 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 365 LRDAVNEVMtllaPSAHDKQLELSIYINQQvPDDLTGDPTRFKQVLINLLSNAIKFTEKGSIkVDIshRLldderTSLLV 444
Cdd:PRK10337 317 LQSAVMDIY----HTAQQAGIDVRLTLNAH-PVIRTGQPLLLSLLVRNLLDNAIRYSPQGSV-VDV--TL-----NARNF 383
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489048494 445 SVTDTGVGIPMDKQDSL----FTPFGQADSsitrkfgGTGLGLIITKHIVEAMSGRITLNSAPGNGTCFTFN 512
Cdd:PRK10337 384 TVRDNGPGVTPEALARIgerfYRPPGQEAT-------GSGLGLSIVRRIAKLHGMNVSFGNAPEGGFEAKVS 448
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
692-785 1.05e-05

phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is a hybrid stress regulator that contains an N-terminal sigma-like (SL) domain and a C-terminal REC domain. Phosphorylation of the REC domain is known to promote binding of the SL domain to an anti-sigma factor. PhyR thus functions as an anti-anti-sigma factor in its phosphorylated state. It is involved in the general stress response. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381095 [Multi-domain]  Cd Length: 117  Bit Score: 45.32  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 692 EQI------EVIETAHNGSQAYSLSKSHKYDIIFMDIQMPimDGITACKLIQESSLNEDTPIIAVTAH---ALQSEKEQL 762
Cdd:cd17540   17 EQIvedlghQVVGIARTRDEAVALARRERPDLILADIQLA--DGSSGIDAVNEILTTHDVPVIFVTAYperLLTGERPEP 94
                         90       100
                 ....*....|....*....|....
gi 489048494 763 LkdgfkgYL-TKPIDEDMLKQIIS 785
Cdd:cd17540   95 T------FLiTKPFDPEMVKAAIS 112
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
673-776 1.11e-05

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: 45.17  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLneDTPIIAVTA 752
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQ--SLPVLILTA 78
                         90       100
                 ....*....|....*....|....
gi 489048494 753 HALQSEKEQLLKDGFKGYLTKPID 776
Cdd:cd17624   79 RDGVDDRVAGLDAGADDYLVKPFA 102
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
395-510 1.19e-05

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


Pssm-ID: 340415 [Multi-domain]  Cd Length: 133  Bit Score: 45.91  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 395 VPDDLTGDPTRFKQVLINLLSNAIKFTEKGSI---KVDIshrllddERTSLLVSVTDTGVGIPMDKQDSLFTPFGQAD-- 469
Cdd:cd16938    1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGGGNitfRVFL-------EGGSEDRSDRDWGPWRPSMSDESVEIRFEVEInd 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489048494 470 ---SSITRKFG-------------GTGLGLIITKHIVEAMSGRITLNSAPGNGTCFT 510
Cdd:cd16938   74 sgsPSIESASMrnslnrrynlselGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMS 130
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
672-821 1.26e-05

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 48.71  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESslNEDTPIIAVT 751
Cdd:PRK10923   5 IVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQR--HPMLPVIIMT 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489048494 752 AHALQSEKEQLLKDGFKGYLTKPIDED----MLKQIISDHspqtpvnRDKAKTDTPQSPAPfQSSRIDWAQALQ 821
Cdd:PRK10923  83 AHSDLDAAVSAYQQGAFDYLPKPFDIDeavaLVERAISHY-------QEQQQPRNIQVNGP-TTDIIGEAPAMQ 148
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
671-785 1.29e-05

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: 45.51  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 671 LKVLVVDDNDANLKLLHTLLSEQIEV-IETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPII- 748
Cdd:cd17530    1 LRVLVLDDDPFQCMMAATILEDLGPGnVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMs 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489048494 749 AVTAHALQSEKEQLLKDG--FKGYLTKPIDEDMLKQIIS 785
Cdd:cd17530   81 GLDGGILESAETLAGANGlnLLGTLSKPFSPEELTELLT 119
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
18-511 1.32e-05

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 48.86  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  18 TVIIGLLLGGYFTINRYIELDEILYQQGTTISEPLAIALEQPMLEKNKQLLNRLISYTHNKHSPTIKSIAIFDKNNALLM 97
Cdd:COG2972   11 VLLLLILLLLVLLILLLSLLLIILLLLLLLILLLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLILLLLLLLL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  98 TSNYhRSFEKLISQKTLINLKTTHVQKSDELVTFFTPIINHTSHDSKWdpsafqsslgTVIIQLNKDQAVIGQQRALLIS 177
Cdd:COG2972   91 LLLI-LLLSLLLLLALILLLALLLLLSILLLILGLLLIILLLLSLLGW----------TLVSLIPKSELFRGLFSLRRLI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 178 GIVIILSLVFAAILALRLSRMFMTPLNKLVLATDKLVEGKRSTgLNDNMIGEFELLREGLNTiahtMVMQKDEMQKNIDQ 257
Cdd:COG2972  160 LLIILLLLLLALLLSYLLSRSITRPIKRLKKAMKKVEKGDLVR-LEVSGNDEIGILARSFNE----MVERIKELIEEVYE 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 258 ATSDYRETLEQYETSNIE-----------LSFAKKEaqDANRVkSDFLAKMSHELRTplngVIGFTRQLykTPLN---KH 323
Cdd:COG2972  235 LELEKKEAELKALQAQINphflfntlnsiRWLAELE--DPEEA-EEMLEALSKLLRY----SLSKGDEL--VTLEeelEL 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 324 QKDYLdtimlsanslmtiisdildfskleagameleSIQfQLRdavnevmtllapsaHDKQLELSIYINQQVPDDLTgdp 403
Cdd:COG2972  306 IKSYL-------------------------------EIQ-KLR--------------FGDRLEVEIEIDEELLDLLI--- 336
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 404 trFKQVLINLLSNAIKF-----TEKGSIKVDISHrllddERTSLLVSVTDTGVGIPMDKQDSLFtpfgqadSSITRKFGG 478
Cdd:COG2972  337 --PKLILQPLVENAIEHgiepkEGGGTIRISIRK-----EGDRLVITVEDNGVGMPEEKLEKLL-------EELSSKGEG 402
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 489048494 479 TGLGLIITKHIVEAMSG---RITLNSAPGNGTCFTF 511
Cdd:COG2972  403 RGIGLRNVRERLKLYYGeeyGLEIESEPGEGTTVTI 438
PRK15369 PRK15369
two component system response regulator;
668-773 1.34e-05

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 47.00  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 668 LLPLKVLVVDDNDANLKLLHTLLSEQ--IEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITAckLIQESSLNEDT 745
Cdd:PRK15369   1 MKNYKILLVDDHELIINGIKNMLAPYprYKIVGQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLDV--IPQLHQRWPAM 78
                         90       100
                 ....*....|....*....|....*...
gi 489048494 746 PIIAVTAHALQSEKEQLLKDGFKGYLTK 773
Cdd:PRK15369  79 NILVLTARQEEHMASRTLAAGALGYVLK 106
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
401-503 1.38e-05

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 48.86  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 401 GDPTRFKQVLINLLSNAIKFTEKgsiKVDISHRLLDDertSLLVSVTDTGVGIPMDKQDSLFTPFGQADSsiTRKfgGTG 480
Cdd:PRK10815 374 GEKNDFMEVMGNVLDNACKYCLE---FVEISARQTDE---HLHIVVEDDGPGIPESKRELIFDRGQRADT--LRP--GQG 443
                         90       100
                 ....*....|....*....|...
gi 489048494 481 LGLIITKHIVEAMSGRITLNSAP 503
Cdd:PRK10815 444 LGLSVAREITEQYEGKISAGDSP 466
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
673-774 1.75e-05

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: 44.31  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSE-QIEVIEtAHNGSQAYSL--SKSHKYDIIFMDIQMPIMDGITACKLIQESSLNEDTPIIA 749
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKcSYEVTA-ASDGLQAWDVleDEQNEIDLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIM 79
                         90       100
                 ....*....|....*....|....*
gi 489048494 750 VTAHALQSEKEQLLKDGFKGYLTKP 774
Cdd:cd17582   80 MSSQDSVGVVFKCLSKGAADYLVKP 104
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
260-506 2.09e-05

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: 47.98  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  260 SDYRETLEQYETSNIELSFAKKEAQDAnrVKSDFLAKMsHELRTPLNGVIGFTRQLYK---TPLNKHQKDYLDTIMLSAN 336
Cdd:TIGR02938 249 SNLREEQERARLSALQALMAEEERLEA--IRETLSAAI-HRLQGPMNLISAAISVLQRrgdDAGNPASAAMLQQALSAGR 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  337 SLMTIISDILDFSKLEAgameleSIQFQLRDAVNEVMTLLAPsahdKQLELSIYINQQ---VPDDLTGDPTRFKQVLINL 413
Cdd:TIGR02938 326 EHMEALRQVIPQSPQEI------VVPVNLNQILRDVITLSTP----RLLAAGIVVDWQpaaTLPAILGRELQLRSLFKAL 395
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494  414 LSNAIKFTEKGSIK---VDISHRLLDDertSLLVSVTDTGVGIPMDKQDSLFTPFGQADSSITRkfgGTGLGLIITKHIV 490
Cdd:TIGR02938 396 VDNAIEAMNIKGWKrreLSITTALNGD---LIVVSILDSGPGIPQDLRYKVFEPFFTTKGGSRK---HIGMGLSVAQEIV 469
                         250
                  ....*....|....*.
gi 489048494  491 EAMSGRITLNSAPGNG 506
Cdd:TIGR02938 470 ADHGGIIDLDDDYSEG 485
PRK13557 PRK13557
histidine kinase; Provisional
402-507 2.50e-05

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 48.13  E-value: 2.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 402 DPTRFKQVLINLLSNAIK-FTEKGSIKVDISHRLLDDERTSLL----------VSVTDTGVGIPMDKQDSLFTPFgqads 470
Cdd:PRK13557 274 DPTQAEVALLNVLINARDaMPEGGRVTIRTRNVEIEDEDLAMYhglppgryvsIAVTDTGSGMPPEILARVMDPF----- 348
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489048494 471 SITRKFG-GTGLGLIITKHIVEAMSGRITLNSAPGNGT 507
Cdd:PRK13557 349 FTTKEEGkGTGLGLSMVYGFAKQSGGAVRIYSEVGEGT 386
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
702-774 2.74e-05

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 46.60  E-value: 2.74e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489048494 702 NGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSlneDTPIIAVTAHALQSEKEQLLKDGFKGYLTKP 774
Cdd:PRK10710  42 HGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRFS---DIPIVMVTAKIEEIDRLLGLEIGADDYICKP 111
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
825-911 6.17e-05

Histidine Phosphotransfer domain; Contains an active histidine residue that mediates phosphotransfer reactions. Domain detected only in eubacteria. This alignment is an extension to that shown in the Cell structure paper.


Pssm-ID: 197502 [Multi-domain]  Cd Length: 92  Bit Score: 42.62  E-value: 6.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494   825 GKSELALEMLNMLLLSVPETLTLLAKAIESNDCQQVLSIVHKFHGACCYTGVPKLKSLAETIETSLK-----NKCLLENI 899
Cdd:smart00073   1 GGLELFREELAEFLQSLEEGLLELEKALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDalrsgEVELTPDL 80
                           90
                   ....*....|..
gi 489048494   900 EPELFELQDELE 911
Cdd:smart00073  81 LDLLLELVDVLK 92
PRK15479 PRK15479
transcriptional regulator TctD;
671-780 6.39e-05

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 45.10  E-value: 6.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 671 LKVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITAckLIQESSLNEDTPIIAV 750
Cdd:PRK15479   1 MRLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEV--LQRLRKRGQTLPVLLL 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 489048494 751 TAHALQSEKEQLLKDGFKGYLTKPIDEDML 780
Cdd:PRK15479  79 TARSAVADRVKGLNVGADDYLPKPFELEEL 108
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
673-775 6.55e-05

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: 43.51  E-value: 6.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQA-----------YSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSL 741
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRAleflgledeedSSNFNEPKVNMIITDYCMPGMTGYDLLKKVKESSA 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489048494 742 NEDTPIIAVTAHALQSEKEQLLKDGFKGYLTKPI 775
Cdd:cd17581   81 LKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPV 114
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
357-510 1.17e-04

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 44.61  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 357 ELESIQFQLRDAVNEV---MTLLAPSAHDkQLELSIYINQQVPD-----------DLTGDPTRF-KQVLINL-------L 414
Cdd:COG4585   93 ELEEIRELAREALAELrrlVRGLRPPALD-DLGLAAALEELAERllraagirvelDVDGDPDRLpPEVELALyrivqeaL 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 415 SNAIKFTEKGSIKVDISHrllddERTSLLVSVTDTGVGIPMDKQdslftpfgqadssitrkfGGTGLGLIITKHIVEAMS 494
Cdd:COG4585  172 TNALKHAGATRVTVTLEV-----DDGELTLTVRDDGVGFDPEAA------------------PGGGLGLRGMRERAEALG 228
                        170
                 ....*....|....*.
gi 489048494 495 GRITLNSAPGNGTCFT 510
Cdd:COG4585  229 GTLTIGSAPGGGTRVR 244
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
381-510 3.14e-04

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: 42.57  E-value: 3.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 381 HDKQLELSIY-----INQQVPDDLtGDPtrfkqvLINLLSNAI--------------KfTEKGSIKVDISHrllddERTS 441
Cdd:cd16916   16 LGKQVELVVEgedteLDKSVLEKL-ADP------LTHLLRNAVdhgieapeerlaagK-PPEGTITLRAEH-----QGNQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 442 LLVSVTDTGVGIPMDK------------------------QDSLFTP-FGQADSsITrKFGGTGLGLIITKHIVEAMSGR 496
Cdd:cd16916   83 VVIEVSDDGRGIDREKirekaierglitadeaatlsddevLNLIFAPgFSTAEQ-VT-DVSGRGVGMDVVKRSIESLGGT 160
                        170
                 ....*....|....
gi 489048494 497 ITLNSAPGNGTCFT 510
Cdd:cd16916  161 IEVESEPGQGTTFT 174
PLN03029 PLN03029
type-a response regulator protein; Provisional
673-775 3.42e-04

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 43.10  E-value: 3.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYD--------------------IIFMDIQMPIMDGITA 732
Cdd:PLN03029  11 VLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGLHEDDrsnpdtpsvspnshqevevnLIITDYCMPGMTGYDL 90
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489048494 733 CKLIQESSLNEDTPIIAVTAHALQSEKEQLLKDGFKGYLTKPI 775
Cdd:PLN03029  91 LKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPV 133
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
674-774 3.67e-04

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: 40.51  E-value: 3.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 674 LVVDDNDANLKLLHTLLSEQIEViETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSlneDTPIIAVTAH 753
Cdd:cd19936    3 LVDDDRNILTSVSMALEAEGFSV-ETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKS---TLPVIFLTSK 78
                         90       100
                 ....*....|....*....|...
gi 489048494 754 alQSEKEQL--LKDGFKGYLTKP 774
Cdd:cd19936   79 --DDEIDEVfgLRMGADDYITKP 99
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
401-497 4.29e-04

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


Pssm-ID: 340409 [Multi-domain]  Cd Length: 113  Bit Score: 40.72  E-value: 4.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 401 GDPTRFKQVLINLLSNAIKFT--EKG--SIKVDISHRLLDD--ERTSLLVSVTDTGVGIPMDKQDSLFtpfgQADSSITR 474
Cdd:cd16932    2 GDQIRLQQVLADFLLNAVRFTpsPGGwvEIKVSPTKKQIGDgvHVIHLEFRITHPGQGLPEELVQEMF----EENQWTTQ 77
                         90       100
                 ....*....|....*....|...
gi 489048494 475 KfggtGLGLIITKHIVEAMSGRI 497
Cdd:cd16932   78 E----GLGLSISRKLVKLMNGDV 96
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
414-507 6.34e-04

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: 39.46  E-value: 6.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 414 LSNAIKFTEKGSIKVDISHRllddeRTSLLVSVTDTGVGIPMDkqdslftpfgqadssitRKFGGTGLGLIITKHIVEAM 493
Cdd:cd16917    9 LTNALKHAGASRVRVTLSYT-----ADELTLTVVDDGVGFDGP-----------------APPGGGGFGLLGMRERAELL 66
                         90
                 ....*....|....
gi 489048494 494 SGRITLNSAPGNGT 507
Cdd:cd16917   67 GGTLTIGSRPGGGT 80
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
673-739 7.69e-04

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 39.64  E-value: 7.69e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSH-KYDIIFMDIQMPimDGITACKLIQES 739
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGpDIDLLVTDVIMP--GGMNGSQLAEEA 66
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
673-776 9.29e-04

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: 39.68  E-value: 9.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQESSlneDTPIIAVTA 752
Cdd:cd17619    3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQS---EVGIILVTG 79
                         90       100
                 ....*....|....*....|....
gi 489048494 753 HALQSEKEQLLKDGFKGYLTKPID 776
Cdd:cd17619   80 RDDEVDRIVGLEIGADDYVTKPFN 103
PRK10816 PRK10816
two-component system response regulator PhoP;
671-774 9.61e-04

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 41.65  E-value: 9.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 671 LKVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITackLIQE-SSLNEDTPIIA 749
Cdd:PRK10816   1 MRVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLS---LIRRwRSNDVSLPILV 77
                         90       100
                 ....*....|....*....|....*
gi 489048494 750 VTAHALQSEKEQLLKDGFKGYLTKP 774
Cdd:PRK10816  78 LTARESWQDKVEVLSAGADDYVTKP 102
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
673-784 1.06e-03

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: 39.50  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLsEQIEVIETAHNGSQAYsLSKSHKYD--IIFMDIQMPIMDGItacKLIQE-SSLNEDTPIIA 749
Cdd:cd17537    3 VYVVDDDEAVRDSLAFLL-RSVGLAVKTFTSASAF-LAAAPPDQpgCLVLDVRMPGMSGL---ELQDElLARGSNIPIIF 77
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489048494 750 VTAHALQSEKEQLLKDGFKGYLTKPIDEDMLKQII 784
Cdd:cd17537   78 ITGHGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAI 112
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
413-511 1.17e-03

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 39.90  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 413 LLSNAIK----FTEKGSIKVDIShrlLDDERtsLLVSVTDTGVGIPMDKqdsLFTPFGQADSSitrkfggtGLGLiitkH 488
Cdd:COG2172   42 AVTNAVRhaygGDPDGPVEVELE---LDPDG--LEIEVRDEGPGFDPED---LPDPYSTLAEG--------GRGL----F 101
                         90       100
                 ....*....|....*....|...
gi 489048494 489 IVEAMSGRITLNSAPGnGTCFTF 511
Cdd:COG2172  102 LIRRLMDEVEYESDPG-GTTVRL 123
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
673-780 1.59e-03

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 38.95  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLLSE---QIEVIETAHNGSQAYSLsksHKYDIIFMDIQMPIMDGITACKLIQESSlnEDTPIIA 749
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEkgyQADVAESLKDGEYYIDI---RNYDLVLVSDKLPDGNGLSIVSRIKEKH--PSIVVIV 75
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489048494 750 VTAHALQSEKEQLLKDGFKGYLTKPIDEDML 780
Cdd:cd17573   76 LSDNPKTEQEIEAFKEGADDYIAKPFDFKVL 106
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
672-798 2.02e-03

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 40.86  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDnDANLKLLHTLLSEQ--IEVIETAHNGSQAYSLSKSHKyDIIFMDIQMPIMDGITACKLIQESSLNEDTPIIA 749
Cdd:PRK10161   4 RILVVED-EAPIREMVCFVLEQngFQPVEAEDYDSAVNQLNEPWP-DLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVM 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489048494 750 VTAHALQSEKEQLLKDGFKGYLTKPIdedmlkqiisdhSPQTPVNRDKA 798
Cdd:PRK10161  82 LTARGEEEDRVRGLETGADDYITKPF------------SPKELVARIKA 118
PRK09191 PRK09191
two-component response regulator; Provisional
695-785 3.36e-03

two-component response regulator; Provisional


Pssm-ID: 236402 [Multi-domain]  Cd Length: 261  Bit Score: 40.22  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 695 EVIETAHNGSQAYSLSKSHKYDIIFMDIQM-PIMDGITACKLIQESSlneDTPIIAVTAHAlqsekEQLLKdGFK---GY 770
Cdd:PRK09191 163 RVTGIARTRAEAVALAKKTRPGLILADIQLaDGSSGIDAVNDILKTF---DVPVIFITAFP-----ERLLT-GERpepAF 233
                         90
                 ....*....|....*.
gi 489048494 771 L-TKPIDEDMLKQIIS 785
Cdd:PRK09191 234 LiTKPFQPDTVKAAIS 249
pleD PRK09581
response regulator PleD; Reviewed
672-780 3.81e-03

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 40.65  E-value: 3.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 672 KVLVVDDNDANLKLLHTLLSEQIEVIETAHNGSQAYSLSKShKYDIIFMDIQMPIMDGITACKliQESSLNED--TPIIA 749
Cdd:PRK09581 157 RILLVDDDVSQAERIANILKEEFRVVVVSDPSEALFNAAET-NYDLVIVSANFENYDPLRLCS--QLRSKERTryVPILL 233
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489048494 750 VTAhalQSEKEQLLKD---GFKGYLTKPIDEDML 780
Cdd:PRK09581 234 LVD---EDDDPRLVKAlelGVNDYLMRPIDKNEL 264
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
673-780 5.85e-03

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: 38.93  E-value: 5.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 673 VLVVDDNDANLKLLHTLL-SEQIEViETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQEssLNEDTPIIAVT 751
Cdd:COG4566    2 VYIVDDDEAVRDSLAFLLeSAGLRV-ETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAA--RGSPLPVIFLT 78
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489048494 752 AH-----ALQSekeqlLKDGFKGYLTKPIDEDML 780
Cdd:COG4566   79 GHgdvpmAVRA-----MKAGAVDFLEKPFDDQAL 107
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
371-507 7.37e-03

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


Pssm-ID: 340427 [Multi-domain]  Cd Length: 131  Bit Score: 37.78  E-value: 7.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 371 EVMTLLAPSAHDKQLELSIYINQQVPD-DLTGD-PTRFKQVLINLLSNAIK--FT--EKGSIKVDIShrlLDDERtsLLV 444
Cdd:cd16951    3 EYINRIASAINAIHAVGDIRINITGDTgPVSSEvATAIGLVVNELLQNALKhaFSdrEGGTITIRSV---VDGDY--LRI 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489048494 445 SVTDTGVGIPMDkqdslFTPFGQADssitrkfggtgLGLIITKHIVEAMSGRITLNSAPGNGT 507
Cdd:cd16951   78 TVIDDGVGLPQD-----EDWPNKGS-----------LGLQIVRSLVEGELKAFLEVQSAENGT 124
PRK14084 PRK14084
DNA-binding response regulator;
671-805 9.22e-03

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 38.96  E-value: 9.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489048494 671 LKVLVVDDNDANLKLLHTLLSE--QIEVIETAHNGSQAYSLSKSHKYDIIFMDIQMPIMDGITACKLIQEssLNEDTPII 748
Cdd:PRK14084   1 MKALIVDDEPLARNELTYLLNEigGFEEINEAENVKETLEALLINQYDIIFLDINLMDESGIELAAKIQK--MKEPPAII 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489048494 749 AVTAHalqsekEQLLKDGFK----GYLTKPIDEDMLKQIIS--DHSPQTPVNRDKAKTDTPQS 805
Cdd:PRK14084  79 FATAH------DQFAVKAFElnatDYILKPFEQKRIEQAVNkvRATKAKDDNNASAIANDMSA 135
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH