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Conserved domains on  [gi|2750649407|ref|WP_353038557|]
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two-component sensor histidine kinase BarA [Serratia marcescens]

Protein Classification

two-component sensor histidine kinase BarA( domain architecture ID 11485205)

two-component sensor histidine kinase BarA is part of the two-component regulatory system UvrY/BarA which is involved in the regulation of carbon metabolism via the CsrA/CsrB regulatory system; phosphorylates UvrY

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
1-878 0e+00

hybrid sensory histidine kinase BarA; Provisional


:

Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 1654.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407   1 MTKYSLRARMMILILAPTLLIGLLLSTFFVVHRYNELQEQLVDAGASIIEPLAVASEYGMTFRSRESVRQLVSLLHRRHS 80
Cdd:PRK11107    1 MTKYSLRARVMILILAPTLLIGLLLSSFFVVNRYNELQRQLIDAGASIIEPLAIASEYGMTLQNRESVRQLISVLHRRHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  81 DIVRSITVFDAQNNSFVTSNYHHNFAQLQLPKGVPLPTELMLTRRGDSLILRTPILSESQYPDETADGGSHPDNN-LGYV 159
Cdd:PRK11107   81 DIVRSIAVFDENNQLFVTSNYHLDFESMRLPEGLPIPRLLSVERDGDSLILRTPIISESYSPDESASSDAKNSQNmLGYI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 160 AIELDLQSVRLQQYKEVFVSTLLLLLCMCIAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKNGI 239
Cdd:PRK11107  161 AIELDLKSVRLQQYREIFIAFLMLLLGIGLALLFAFRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGNMLGELDMLKNGI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 240 NSMAMSLTAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQMLK 319
Cdd:PRK11107  241 NAMAMSLSAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 320 TDLSATQTDYLQTIERSANNLLTIINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVLLAPSAHDKGLELTLDVHNDVPE 399
Cdd:PRK11107  321 TPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPD 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 400 QVIGDSLRLQQIITNLLGNAIKFTETGNIDIRVELRKRLDRRVEVEVQIHDTGIGISERQQSQLFQAFRQADASISRRHG 479
Cdd:PRK11107  401 NVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHG 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 480 GTGLGLVITQKLVKEMGGDICFHSQLNRGSTFWFHITLDLNEGMLSLAPSLPDLNGKTLAYIESNPTAAQATLNMLSVTQ 559
Cdd:PRK11107  481 GTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPNPIIDGLPTDCLAGKRLLYVEPNSAAAQATLDILSETP 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 560 LVITHSPTLAQLPPGHYDFLLAGVPIPFRDNMAQHEDKLLASLKLADRVILALPCQAQIDAELLKQQGALGCLIKPITST 639
Cdd:PRK11107  561 LEVTYSPTLSQLPEAHYDILLLGLPVTFREPLTMLHERLAKAKSMTDFLILALPCHEQVLAEQLKQDGADACLSKPLSHT 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 640 RLFPLLRMETPTRLTAPP---ERKRLPLTVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQ 716
Cdd:PRK11107  641 RLLPALLEPCHHKQPPLLpptDESRLPLTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQ 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 717 MPKMDGIHASELIRQLPHHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKPIDEKMLTRVLSRYHSGDVENAVA------ 790
Cdd:PRK11107  721 MPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKPGPKFTSRVvapepp 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 791 ---DDAPLSLDWPLALRQAANKPDLARDLLQMLLDFLPQVRERVQALLDGQHDDEILDLVHKLHGSCSYSGVPRLKQLCF 867
Cdd:PRK11107  801 epvHFPNATLDWQLALRQAAGKPDLARDMLQMLLDFLPEVRNKVEEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQ 880
                         890
                  ....*....|.
gi 2750649407 868 YLERQLRQGVT 878
Cdd:PRK11107  881 LIEQQLRSGTS 891
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
1-878 0e+00

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 1654.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407   1 MTKYSLRARMMILILAPTLLIGLLLSTFFVVHRYNELQEQLVDAGASIIEPLAVASEYGMTFRSRESVRQLVSLLHRRHS 80
Cdd:PRK11107    1 MTKYSLRARVMILILAPTLLIGLLLSSFFVVNRYNELQRQLIDAGASIIEPLAIASEYGMTLQNRESVRQLISVLHRRHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  81 DIVRSITVFDAQNNSFVTSNYHHNFAQLQLPKGVPLPTELMLTRRGDSLILRTPILSESQYPDETADGGSHPDNN-LGYV 159
Cdd:PRK11107   81 DIVRSIAVFDENNQLFVTSNYHLDFESMRLPEGLPIPRLLSVERDGDSLILRTPIISESYSPDESASSDAKNSQNmLGYI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 160 AIELDLQSVRLQQYKEVFVSTLLLLLCMCIAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKNGI 239
Cdd:PRK11107  161 AIELDLKSVRLQQYREIFIAFLMLLLGIGLALLFAFRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGNMLGELDMLKNGI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 240 NSMAMSLTAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQMLK 319
Cdd:PRK11107  241 NAMAMSLSAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 320 TDLSATQTDYLQTIERSANNLLTIINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVLLAPSAHDKGLELTLDVHNDVPE 399
Cdd:PRK11107  321 TPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPD 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 400 QVIGDSLRLQQIITNLLGNAIKFTETGNIDIRVELRKRLDRRVEVEVQIHDTGIGISERQQSQLFQAFRQADASISRRHG 479
Cdd:PRK11107  401 NVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHG 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 480 GTGLGLVITQKLVKEMGGDICFHSQLNRGSTFWFHITLDLNEGMLSLAPSLPDLNGKTLAYIESNPTAAQATLNMLSVTQ 559
Cdd:PRK11107  481 GTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPNPIIDGLPTDCLAGKRLLYVEPNSAAAQATLDILSETP 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 560 LVITHSPTLAQLPPGHYDFLLAGVPIPFRDNMAQHEDKLLASLKLADRVILALPCQAQIDAELLKQQGALGCLIKPITST 639
Cdd:PRK11107  561 LEVTYSPTLSQLPEAHYDILLLGLPVTFREPLTMLHERLAKAKSMTDFLILALPCHEQVLAEQLKQDGADACLSKPLSHT 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 640 RLFPLLRMETPTRLTAPP---ERKRLPLTVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQ 716
Cdd:PRK11107  641 RLLPALLEPCHHKQPPLLpptDESRLPLTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQ 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 717 MPKMDGIHASELIRQLPHHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKPIDEKMLTRVLSRYHSGDVENAVA------ 790
Cdd:PRK11107  721 MPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKPGPKFTSRVvapepp 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 791 ---DDAPLSLDWPLALRQAANKPDLARDLLQMLLDFLPQVRERVQALLDGQHDDEILDLVHKLHGSCSYSGVPRLKQLCF 867
Cdd:PRK11107  801 epvHFPNATLDWQLALRQAAGKPDLARDMLQMLLDFLPEVRNKVEEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQ 880
                         890
                  ....*....|.
gi 2750649407 868 YLERQLRQGVT 878
Cdd:PRK11107  881 LIEQQLRSGTS 891
BarA5 COG4999
Uncharacterized domain of signal transduction histidine kinase BarA [Signal transduction ...
1-908 0e+00

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


Pssm-ID: 444023 [Multi-domain]  Cd Length: 921  Bit Score: 1033.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407   1 MTKYSLRARMMILILAPTLLIGLLLSTFFVVHRYNELQEQLVDAGASIIEPLAVASEYGMTFRSRESVRQLVSLLHRRHS 80
Cdd:COG4999     3 MTLRRRRRIILLLLLLLLILLLLLLFFFFFVYRYQLLQQQLSASIIIIIAAAAASSEYLMNKRRREQLLLLLLRRHHRHS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  81 DIVRSITVFDAQNNSFVTSNYHHNFAQLQLPKGVPLPTELMLTRRGDSLILRTPILSESQYPDETADggsHPDNNLGYVA 160
Cdd:COG4999    83 IIISAIDDNNNLNNLSNNNNNNLNLLLLQLPPPSPPLLLLTRSDLILLLIPPISIIYEDESSEPSDN---TAANPLGYIA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 161 IELDLQSVRLQQYKEVFVSTLLLLLCMCIAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKNGIN 240
Cdd:COG4999   160 IELDLSSDRLQQYQEQFVATLLLLLLLLLALLFAYRLMRDVTVPITNMVNVVDRIRRRRLDSRVEGGMLGELLLLKNGIN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 241 SMAMSLTAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQMLKT 320
Cdd:COG4999   240 NMAMSLAAYHEEMQQNIDQATSDLRETLEQLEIQNVELDLAKKRAQEAARAKSEFLANMSHELRTPLNGVIGFTRQTLKT 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 321 DLSATQTDYLQTIERSANNLLTIINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVLLAPSAHDKGLELTLDVHNDVPEQ 400
Cdd:COG4999   320 TLTPTQTDYLQTIERSANNLLNIINDILDFSKLEAGKLLLELIPFPFRDTLDEVVVLLALLAHEKGLELTLLLDNDVPED 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 401 VIGDSLRLQQIITNLLGNAIKFTETGNIDIRVELRKRLDRRVEVEVQIHDTGIGISERQQSQLFQAFRQADASISRRHGG 480
Cdd:COG4999   400 VIGDPLRIQQILQNLLGNAIKFTETGNIDIIVELRTQRQNSVELQVQVRDTGIGISERQQAQLFQAFFQADASISRRRGG 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 481 TGLGLVITQKLVKEMGGDICFHSQLNRGSTFWFHITLDLNEG-MLSLAPSLPDLNGKTLAYIESNPTAAQATLNMLSVTQ 559
Cdd:COG4999   480 TGGGLVITQKLVKEMGGEIGFISRLSQGSTFWFTFFLLLNLApALSDPLPLDRLQGKRLLYVEPNPAAAQATLDLLSQTP 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 560 LVITHSPTLAQLPPGHYDFLLAGVPIPFRDNMAQHEDKLLASLKLADRVILALPCQAQIDAELLKQQGALGCLIKPITST 639
Cdd:COG4999   560 LEVTYSPTLEQLPEAHYDILLIGLPVTYRNTLADLTDKLAQALRMADCVILALPSTAQVLAEQLKAAGARACLSKPLSAT 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 640 RLFPLLRMETPTRL---TAPPERKRLPLTVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQ 716
Cdd:COG4999   640 RLLPLLLDECLFELplpAATPEAPLPPLVVAVVDDNANNLLLIALLLELVVQVVVCCSSGEAAAAAAAQQLDDILIMDIQ 719
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 717 MPKMDGIHASELIRQLPHHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKPIDEKMLTRVLSRYHSG------DVENAVA 790
Cdd:COG4999   720 MPMMDGIAAEEIIRQLPHNNTTPIVAVAAAAAAGREELLLAGGMDDYLAKPIEEELLLLLLLRYQPGphtvpsPPPVPPS 799
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 791 DDAPLSLDWPLALRQAANKPDLARDLLQMLLDFLPQVRERVQALLDGQHDDEILDLVHKLHGSCSYSGVPRLKQLCFYLE 870
Cdd:COG4999   800 LAPLVLLQASQLSLDAAAALQQALDALLLLLELLLLLLLELLEVLILRQEIDLLGALDLLHGLHSSLLCSGLLRLKGLLS 879
                         890       900       910
                  ....*....|....*....|....*....|....*...
gi 2750649407 871 RQLRQGVTNDELEPEWLELLDEIELVIHAARAHLTQPA 908
Cdd:COG4999   880 LQLQLEPEELLLLEEEEELLEELDEELLLESEELQRLE 917
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
170-872 1.40e-92

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: 314.02  E-value: 1.40e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 170 LQQYKEVFVSTLLLLLCMCIAILFAYrLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKNGI---------- 239
Cdd:TIGR02956 326 LSVAQFGLLITGMLGLVILVFIMWRV-VYRSVILRLNQHTQALLRLALGDLDISLDARGDDELAHMGRAIeafrdtaahn 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 240 -------NSMAMSLTAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIG 312
Cdd:TIGR02956 405 lklqadeRQVAQELQEHKESLEQLVAQRTQELAETNERLNAEVKNHAKARAEAEEANRAKSAFLATMSHEIRTPLNGILG 484
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 313 FTRQMLKTDLSATQTDYLQTIERSANNLLTIINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVLLAPSAHDKGLELTLD 392
Cdd:TIGR02956 485 TLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLN 564
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 393 VHNDVPEQVIGDSLRLQQIITNLLGNAIKFTETGNIDIRVELRKRLDRRVEVEvqihDTGIGISERQQSQLFQAFRQADA 472
Cdd:TIGR02956 565 IPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDSSLLFEVE----DTGCGIAEEEQATLFDAFTQADG 640
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 473 siSRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTFWFHITLDlnegmlslapslpdlngktlayiESNPTAAQATL 552
Cdd:TIGR02956 641 --RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLT-----------------------RGKPAEDSATL 695
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 553 NMLsvtqlvithsptlaQLPPGHydfllagvpipfrdnmaqhedkllaslkladrvilalpcqaqidaellkqqgalgcl 632
Cdd:TIGR02956 696 TVI--------------DLPPQR--------------------------------------------------------- 704
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 633 ikpitstrlfpllrmetptrltapperkrlpltVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLIL 712
Cdd:TIGR02956 705 ---------------------------------VLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLAL 751
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 713 MDIQMPKMDGIHASELIRQL-PHHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKPIDEKMLTRVLSRYHSGDVENAVAD 791
Cdd:TIGR02956 752 LDINLPDGDGVTLLQQLRAIyGAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVILAGGKSNTEAP 831
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 792 DAPLSLDWPLA----LRQAANKPDLARDLLQMLLDFLPQ----------VR--------------ERVQALLDGQHDDEI 843
Cdd:TIGR02956 832 VLSASPSFDSAsvieNAQADDIPESNQASEFLLDEEQLQqdievlgvekVRqlvalfktssaeqlEELSAARAVDDDAQI 911
                         730       740
                  ....*....|....*....|....*....
gi 2750649407 844 LDLVHKLHGSCSYSGVPRLKQLCFYLERQ 872
Cdd:TIGR02956 912 KKLAHKLKGSAGSLGLTQLTQLCQQLEKQ 940
sCache_4 pfam09984
Single cache domain 4; Members of this family of domains are found in various BarA-like signal ...
31-176 2.72e-67

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: 220.96  E-value: 2.72e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  31 VHRYNELQEQLVDAGASIIEPLAVASEYGMTFRSRESVRQLVSLLHRRHSDIVRSITVFDAQNNSFVTSNYHHNFAQLQL 110
Cdd:pfam09984   1 INRYYELEDQLIDRGTSIIEPLAIASEYGLTTRNRESLRRLISALHRKNSPIVRSIAIFDANNQLFVTSNYHRDFESLRL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2750649407 111 PKGVPLPTELMLTRRGDSLILRTPILSESQYPDETADGGSHPDNNLGYVAIELDLQSVRLQQYKEV 176
Cdd:pfam09984  81 PEGAPIPTLTTVEHSGDSLILRTPIISEGLSLPGLPATAESAQRPLGYIAIELNLDSARLQQYREI 146
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
408-517 1.34e-54

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: 184.23  E-value: 1.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 408 LQQIITNLLGNAIKFTETGNIDIRVELRKRLDRRVEVEVQIHDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVI 487
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 2750649407 488 TQKLVKEMGGDICFHSQLNRGSTFWFHITL 517
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
403-515 1.61e-32

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 121.60  E-value: 1.61e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  403 GDSLRLQQIITNLLGNAIKFTETGnIDIRVELRKRLDRrveVEVQIHDTGIGISERQQSQLFQAFRQADASiSRRHGGTG 482
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEG-GRITVTLERDGDH---VEITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGTG 75
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2750649407  483 LGLVITQKLVKEMGGDICFHSQLNRGSTFWFHI 515
Cdd:smart00387  76 LGLSIVKKLVELHGGEISVESEPGGGTTFTITL 108
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
158-531 2.50e-29

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 123.21  E-value: 2.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 158 YVAIELDLQSVRLQQYKEVFVSTLLLLLCMCIAIlfAYRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKN 237
Cdd:NF040691  171 YLLFPLEDEQSTLALVRGTLLLGGLALVVLLGLI--AWLVTRQVVAPVRSAARTAERFAAGDLSERMPVKGEDDLARLAR 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 238 GINSMAMSLtayheemQQNIDQatsdlretLEQMeiqnveldlakkraqeaARIKSEFLANMSHELRTPLNgvigfTRQM 317
Cdd:NF040691  249 SFNQMADSL-------QRQIRQ--------LEEL-----------------SRLQQRFVSDVSHELRTPLT-----TIRM 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 318 LKTDLSATQTDYLQTIERSAnNLL--------TIINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVLLAPSAHDKGLEL 389
Cdd:NF040691  292 AADVIHDSRDDFDPATARSA-ELLhteldrfeSLLSDLLEISRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVEL 370
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 390 TLDVhNDVPEQVIGDSLRLQQIITNLLGNAIKFTETGNIDIRVElrkrlDRRVEVEVQIHDTGIGISERQQSQLFQAFRQ 469
Cdd:NF040691  371 RVDA-PGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTVA-----QDDTAVAVTVRDHGVGLKPGEVALVFDRFWR 444
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2750649407 470 ADASISRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTfwFHITLDLNEGMLSLAPSLP 531
Cdd:NF040691  445 ADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQ--FRLTLPRVAGDRLTTSPLP 504
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
179-505 2.62e-25

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 110.30  E-value: 2.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 179 STLLLLLCMCIAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKNGINSMAmsltayheemqqnid 258
Cdd:NF012163  166 SWLIVALALLLAALAAFLLARGLLAPVKRLVEATHRLAAGDYTTRVTPTSNDELGKLAQDFNQLA--------------- 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 259 qatsdlrETLEQMEiqnveldlakkraqeaaRIKSEFLANMSHELRTPLngvigftrQMLKTDLSATQT-------DYLQ 331
Cdd:NF012163  231 -------STLEKNE-----------------QMRRDFMADISHELRTPL--------AVLRAELEAIQDgirkftpESLD 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 332 TIERSANNLLTIINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVLLAPSAHDKGLELtldvHNDVPEQ--VIGDSLRLQ 409
Cdd:NF012163  279 SLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLEL----EVSLPDSslVFGDRDRLM 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 410 QIITNLLGNAIKFTETGNiDIRVELRKRlDRrvEVEVQIHDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQ 489
Cdd:NF012163  355 QLFNNLLENSLRYTDSGG-SLHISASQR-PK--EVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISL 430
                         330
                  ....*....|....*..
gi 2750649407 490 KLVKEMGGDICF-HSQL 505
Cdd:NF012163  431 NIVQAHGGTLHAaHSPL 447
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
156-515 5.66e-14

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: 74.26  E-value: 5.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 156 LGY----VAIE---LDLQSvrLQQYKEVF-----VSTLLLLLCMC-IAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLDS 222
Cdd:NF012226   28 LGYfiynYAIEvgwITLSS--LQEDWTEFhfvdwIWLFTVILCGSvISLIIGMKLAQRFIVPINFLADAAKKISQGDLSA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 223 RVEGYML--GELHMLKNGINSMAmsltayheemQQnidqatsdLRETLEQMEIQNveldlakkraqeaarikseflANMS 300
Cdd:NF012226  106 RAEDSQIhsAEISELMHNFNDMA----------QK--------LESSVKNAQVWN---------------------AAIA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 301 HELRTP-----------LNGVIGFTRQMLKTDLSATQtdylqtiersanNLLTIINDVLDFSKLEAGKLVLEHIPFALRE 369
Cdd:NF012226  147 HELRTPitilqgrlqgiLDGVFEPDPALFKSLLNQVE------------GLSHLVEDLRTLSLVENQQLRLNYESVDLKD 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 370 TLDEVVVLLAPSAHDKGLELTLDVHNDvpeQVIGDSLRLQQIITNLLGNAIKFTETGNIDIRveLRKRLDRRVeveVQIH 449
Cdd:NF012226  215 SIEKVLKMFEDRLEQAQLTIVLNLTAT---PVFCDRRRIEQVLIALIDNAIRYANAGKLKIS--SSVIQDDWI---LQIE 286
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2750649407 450 DTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVKEMGGDIcFHSQLNRGSTFWFHI 515
Cdd:NF012226  287 DEGPGIAEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSI-EYSNSQGNSVFTIKL 351
ActS_PrrB_HisK NF033792
ActS/PrrB/RegB family redox-sensitive histidine kinase; This redox-responsive histidine kinase, ...
301-501 1.23e-03

ActS/PrrB/RegB family redox-sensitive histidine kinase; This redox-responsive histidine kinase, found in alpha-proteobacteria, shows strong sequence conservation, including the notable motif [VA]AAAAHELGTPxTI. It always acts as a partner to an ActR/PrrA/RegA family global response regulator transcription factor in a two-component sensory transduction system. Lineage-specific names and gene symbols given to this histidine kinase reflect downstream regulator changes such as entry into stationary phase, anaerobic expression of photosynthesis genes, and survival of exposure to low pH.


Pssm-ID: 468186 [Multi-domain]  Cd Length: 423  Bit Score: 42.12  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 301 HELRTPLnGVIGFT-RQMLKT-----------DLSATQTDYLQTIERSannlLTiindvldfSKLEAGKLVLEHIPfaLR 368
Cdd:NF033792  211 HELGTPL-ATIALVaKELERElpddpplredaELLRSQAERCRDILRR----LT--------SLGEEGDAHLDRLP--LS 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 369 ETLDEVVvllAPsAHDKGLELTLDVHNDVPEQVIGdsLRLQQII---TNLLGNAIKFTETgnidiRVELRKRLDRRvEVE 445
Cdd:NF033792  276 ALIEEAA---AP-HRGFGKEIEVVVAGDPGEEPVI--RRNPEILyglGNLIENAVDFARS-----TVTVTASWDAE-SVT 343
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2750649407 446 VQIHDTGIGISERQQSQLFQAF--RQADASISRRHGGTGLGLVITQKLVKEMGGDICF 501
Cdd:NF033792  344 ITIEDDGPGFPPDVLSRIGEPYvtTRRGEERRPGGGGLGLGLFIAKTLLERSGATVTF 401
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
1-878 0e+00

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 1654.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407   1 MTKYSLRARMMILILAPTLLIGLLLSTFFVVHRYNELQEQLVDAGASIIEPLAVASEYGMTFRSRESVRQLVSLLHRRHS 80
Cdd:PRK11107    1 MTKYSLRARVMILILAPTLLIGLLLSSFFVVNRYNELQRQLIDAGASIIEPLAIASEYGMTLQNRESVRQLISVLHRRHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  81 DIVRSITVFDAQNNSFVTSNYHHNFAQLQLPKGVPLPTELMLTRRGDSLILRTPILSESQYPDETADGGSHPDNN-LGYV 159
Cdd:PRK11107   81 DIVRSIAVFDENNQLFVTSNYHLDFESMRLPEGLPIPRLLSVERDGDSLILRTPIISESYSPDESASSDAKNSQNmLGYI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 160 AIELDLQSVRLQQYKEVFVSTLLLLLCMCIAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKNGI 239
Cdd:PRK11107  161 AIELDLKSVRLQQYREIFIAFLMLLLGIGLALLFAFRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGNMLGELDMLKNGI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 240 NSMAMSLTAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQMLK 319
Cdd:PRK11107  241 NAMAMSLSAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 320 TDLSATQTDYLQTIERSANNLLTIINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVLLAPSAHDKGLELTLDVHNDVPE 399
Cdd:PRK11107  321 TPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPD 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 400 QVIGDSLRLQQIITNLLGNAIKFTETGNIDIRVELRKRLDRRVEVEVQIHDTGIGISERQQSQLFQAFRQADASISRRHG 479
Cdd:PRK11107  401 NVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHG 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 480 GTGLGLVITQKLVKEMGGDICFHSQLNRGSTFWFHITLDLNEGMLSLAPSLPDLNGKTLAYIESNPTAAQATLNMLSVTQ 559
Cdd:PRK11107  481 GTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPNPIIDGLPTDCLAGKRLLYVEPNSAAAQATLDILSETP 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 560 LVITHSPTLAQLPPGHYDFLLAGVPIPFRDNMAQHEDKLLASLKLADRVILALPCQAQIDAELLKQQGALGCLIKPITST 639
Cdd:PRK11107  561 LEVTYSPTLSQLPEAHYDILLLGLPVTFREPLTMLHERLAKAKSMTDFLILALPCHEQVLAEQLKQDGADACLSKPLSHT 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 640 RLFPLLRMETPTRLTAPP---ERKRLPLTVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQ 716
Cdd:PRK11107  641 RLLPALLEPCHHKQPPLLpptDESRLPLTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQ 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 717 MPKMDGIHASELIRQLPHHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKPIDEKMLTRVLSRYHSGDVENAVA------ 790
Cdd:PRK11107  721 MPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKPGPKFTSRVvapepp 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 791 ---DDAPLSLDWPLALRQAANKPDLARDLLQMLLDFLPQVRERVQALLDGQHDDEILDLVHKLHGSCSYSGVPRLKQLCF 867
Cdd:PRK11107  801 epvHFPNATLDWQLALRQAAGKPDLARDMLQMLLDFLPEVRNKVEEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQ 880
                         890
                  ....*....|.
gi 2750649407 868 YLERQLRQGVT 878
Cdd:PRK11107  881 LIEQQLRSGTS 891
BarA5 COG4999
Uncharacterized domain of signal transduction histidine kinase BarA [Signal transduction ...
1-908 0e+00

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


Pssm-ID: 444023 [Multi-domain]  Cd Length: 921  Bit Score: 1033.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407   1 MTKYSLRARMMILILAPTLLIGLLLSTFFVVHRYNELQEQLVDAGASIIEPLAVASEYGMTFRSRESVRQLVSLLHRRHS 80
Cdd:COG4999     3 MTLRRRRRIILLLLLLLLILLLLLLFFFFFVYRYQLLQQQLSASIIIIIAAAAASSEYLMNKRRREQLLLLLLRRHHRHS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  81 DIVRSITVFDAQNNSFVTSNYHHNFAQLQLPKGVPLPTELMLTRRGDSLILRTPILSESQYPDETADggsHPDNNLGYVA 160
Cdd:COG4999    83 IIISAIDDNNNLNNLSNNNNNNLNLLLLQLPPPSPPLLLLTRSDLILLLIPPISIIYEDESSEPSDN---TAANPLGYIA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 161 IELDLQSVRLQQYKEVFVSTLLLLLCMCIAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKNGIN 240
Cdd:COG4999   160 IELDLSSDRLQQYQEQFVATLLLLLLLLLALLFAYRLMRDVTVPITNMVNVVDRIRRRRLDSRVEGGMLGELLLLKNGIN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 241 SMAMSLTAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQMLKT 320
Cdd:COG4999   240 NMAMSLAAYHEEMQQNIDQATSDLRETLEQLEIQNVELDLAKKRAQEAARAKSEFLANMSHELRTPLNGVIGFTRQTLKT 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 321 DLSATQTDYLQTIERSANNLLTIINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVLLAPSAHDKGLELTLDVHNDVPEQ 400
Cdd:COG4999   320 TLTPTQTDYLQTIERSANNLLNIINDILDFSKLEAGKLLLELIPFPFRDTLDEVVVLLALLAHEKGLELTLLLDNDVPED 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 401 VIGDSLRLQQIITNLLGNAIKFTETGNIDIRVELRKRLDRRVEVEVQIHDTGIGISERQQSQLFQAFRQADASISRRHGG 480
Cdd:COG4999   400 VIGDPLRIQQILQNLLGNAIKFTETGNIDIIVELRTQRQNSVELQVQVRDTGIGISERQQAQLFQAFFQADASISRRRGG 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 481 TGLGLVITQKLVKEMGGDICFHSQLNRGSTFWFHITLDLNEG-MLSLAPSLPDLNGKTLAYIESNPTAAQATLNMLSVTQ 559
Cdd:COG4999   480 TGGGLVITQKLVKEMGGEIGFISRLSQGSTFWFTFFLLLNLApALSDPLPLDRLQGKRLLYVEPNPAAAQATLDLLSQTP 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 560 LVITHSPTLAQLPPGHYDFLLAGVPIPFRDNMAQHEDKLLASLKLADRVILALPCQAQIDAELLKQQGALGCLIKPITST 639
Cdd:COG4999   560 LEVTYSPTLEQLPEAHYDILLIGLPVTYRNTLADLTDKLAQALRMADCVILALPSTAQVLAEQLKAAGARACLSKPLSAT 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 640 RLFPLLRMETPTRL---TAPPERKRLPLTVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQ 716
Cdd:COG4999   640 RLLPLLLDECLFELplpAATPEAPLPPLVVAVVDDNANNLLLIALLLELVVQVVVCCSSGEAAAAAAAQQLDDILIMDIQ 719
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 717 MPKMDGIHASELIRQLPHHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKPIDEKMLTRVLSRYHSG------DVENAVA 790
Cdd:COG4999   720 MPMMDGIAAEEIIRQLPHNNTTPIVAVAAAAAAGREELLLAGGMDDYLAKPIEEELLLLLLLRYQPGphtvpsPPPVPPS 799
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 791 DDAPLSLDWPLALRQAANKPDLARDLLQMLLDFLPQVRERVQALLDGQHDDEILDLVHKLHGSCSYSGVPRLKQLCFYLE 870
Cdd:COG4999   800 LAPLVLLQASQLSLDAAAALQQALDALLLLLELLLLLLLELLEVLILRQEIDLLGALDLLHGLHSSLLCSGLLRLKGLLS 879
                         890       900       910
                  ....*....|....*....|....*....|....*...
gi 2750649407 871 RQLRQGVTNDELEPEWLELLDEIELVIHAARAHLTQPA 908
Cdd:COG4999   880 LQLQLEPEELLLLEEEEELLEELDEELLLESEELQRLE 917
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
170-872 1.40e-92

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: 314.02  E-value: 1.40e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 170 LQQYKEVFVSTLLLLLCMCIAILFAYrLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKNGI---------- 239
Cdd:TIGR02956 326 LSVAQFGLLITGMLGLVILVFIMWRV-VYRSVILRLNQHTQALLRLALGDLDISLDARGDDELAHMGRAIeafrdtaahn 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 240 -------NSMAMSLTAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIG 312
Cdd:TIGR02956 405 lklqadeRQVAQELQEHKESLEQLVAQRTQELAETNERLNAEVKNHAKARAEAEEANRAKSAFLATMSHEIRTPLNGILG 484
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 313 FTRQMLKTDLSATQTDYLQTIERSANNLLTIINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVLLAPSAHDKGLELTLD 392
Cdd:TIGR02956 485 TLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLN 564
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 393 VHNDVPEQVIGDSLRLQQIITNLLGNAIKFTETGNIDIRVELRKRLDRRVEVEvqihDTGIGISERQQSQLFQAFRQADA 472
Cdd:TIGR02956 565 IPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDSSLLFEVE----DTGCGIAEEEQATLFDAFTQADG 640
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 473 siSRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTFWFHITLDlnegmlslapslpdlngktlayiESNPTAAQATL 552
Cdd:TIGR02956 641 --RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLT-----------------------RGKPAEDSATL 695
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 553 NMLsvtqlvithsptlaQLPPGHydfllagvpipfrdnmaqhedkllaslkladrvilalpcqaqidaellkqqgalgcl 632
Cdd:TIGR02956 696 TVI--------------DLPPQR--------------------------------------------------------- 704
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 633 ikpitstrlfpllrmetptrltapperkrlpltVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLIL 712
Cdd:TIGR02956 705 ---------------------------------VLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLAL 751
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 713 MDIQMPKMDGIHASELIRQL-PHHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKPIDEKMLTRVLSRYHSGDVENAVAD 791
Cdd:TIGR02956 752 LDINLPDGDGVTLLQQLRAIyGAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVILAGGKSNTEAP 831
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 792 DAPLSLDWPLA----LRQAANKPDLARDLLQMLLDFLPQ----------VR--------------ERVQALLDGQHDDEI 843
Cdd:TIGR02956 832 VLSASPSFDSAsvieNAQADDIPESNQASEFLLDEEQLQqdievlgvekVRqlvalfktssaeqlEELSAARAVDDDAQI 911
                         730       740
                  ....*....|....*....|....*....
gi 2750649407 844 LDLVHKLHGSCSYSGVPRLKQLCFYLERQ 872
Cdd:TIGR02956 912 KKLAHKLKGSAGSLGLTQLTQLCQQLEKQ 940
PRK15347 PRK15347
two component system sensor kinase;
118-876 4.54e-85

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 292.32  E-value: 4.54e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 118 TELMLTRRGDSLILRTPILSESQYPD-----ETADGGSHPDNNLGYVAIELDLQSVRLQQ---YKEVFVS---------- 179
Cdd:PRK15347  219 INLWLDQNGELLPFSTIPLSSNQLQKilnqlENVKLHDGWQQIPDYLVLRTQLKGPGWQQvtlYPRRNLAnealkpalqq 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 180 ---TLLLLLCMciAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKNGINSMAMSLTAYHEEMQQN 256
Cdd:PRK15347  299 lpfALLILVLL--TSVLFLLLRRYLAKPLWRFVDIINKTGPAALEPRLPENRLDELGSIAKAYNQLLDTLNEQYDTLENK 376
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 257 IDQATsdlretleqmeiqnVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQMLKTDLSATQTDYLQTIERS 336
Cdd:PRK15347  377 VAERT--------------QALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQC 442
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 337 ANNLLTIINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVLLAPSAHDKGLELTLDVHNDVPEQVIGDSLRLQQIITNLL 416
Cdd:PRK15347  443 TLSLLAIINNLLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLL 522
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 417 GNAIKFTETGNIDIRVELRK-RLDRRVEvevqihDTGIGISERQQSQLFQAFRQADASIsrrhGGTGLGLVITQKLVKEM 495
Cdd:PRK15347  523 GNAVKFTETGGIRLRVKRHEqQLCFTVE------DTGCGIDIQQQQQIFTPFYQADTHS----QGTGLGLTIASSLAKMM 592
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 496 GGDICFHSQLNRGSTFWFhiTLDLNEgmlsLAPSLPdLNGKTLAyiesnPTAAQATLNMLSVTQLVITHSPTLAqlppgh 575
Cdd:PRK15347  593 GGELTLFSTPGVGSCFSL--VLPLNE----YAPPEP-LKGELSA-----PLALHRQLSAWGITCQPGHQNPALL------ 654
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 576 yDFLLAGVPIPFRDNmaqhedkllaslklADRVILALPCQAQIDAELLKQQgalgclikpitstrlfpllrmetptrlta 655
Cdd:PRK15347  655 -DPELAYLPGRLYDL--------------LQQIIQGAPNEPVINLPLQPWQ----------------------------- 690
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 656 pperkrlpLTVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHH 735
Cdd:PRK15347  691 --------LQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNN 762
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 736 NST--PIVAVTAHAASGEREHLLQAGMDDYLAKPIDEKMLTRVLSRyhsgDVENAVADDAPL----SLDWPLAlrqAANK 809
Cdd:PRK15347  763 LDPdcMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARALEL----AAEYQLLRGIELspqdSSCSPLL---DTDD 835
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2750649407 810 PDLARDLLQMLLDFLPQVRERVQALldgqhdDEILDLVHKLHGSCSYSGVPRLKQLCFYLERQLRQG 876
Cdd:PRK15347  836 MALNSKLYQSLLLLLAQIEQAVENQ------EVLSQLLHTLKGCAGQAGLTELQCAVIDLENALETG 896
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
183-515 1.35e-74

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 247.51  E-value: 1.35e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 183 LLLCMCIAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKNGINSMAMSLTAYHEEMQQNIDQATS 262
Cdd:COG0642     1 LLLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 263 DLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTrQMLKTDLSATQTDYLQTIERSANNLLT 342
Cdd:COG0642    81 LLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYL-ELLLEELDEEQREYLETILRSADRLLR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 343 IINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVLLAPSAHDKGLELTLDVHNDVPeQVIGDSLRLQQIITNLLGNAIKF 422
Cdd:COG0642   160 LINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLSNAIKY 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 423 TETGNiDIRVELRKRLDRrveVEVQIHDTGIGISERQQSQLFQAFRQADAsiSRRHGGTGLGLVITQKLVKEMGGDICFH 502
Cdd:COG0642   239 TPEGG-TVTVSVRREGDR---VRISVEDTGPGIPPEDLERIFEPFFRTDP--SRRGGGTGLGLAIVKRIVELHGGTIEVE 312
                         330
                  ....*....|...
gi 2750649407 503 SQLNRGSTFWFHI 515
Cdd:COG0642   313 SEPGKGTTFTVTL 325
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
277-515 1.09e-67

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 225.56  E-value: 1.09e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 277 ELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQMLK--TDLSATQTDYLQTIERSANNLLTIINDVLDFSKLE 354
Cdd:COG2205     1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDeeDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 355 AGKLVLEHIPFALRETLDEVVVLLAPSAHDKGLELTLDVHNDVPEqVIGDSLRLQQIITNLLGNAIKFTETGnIDIRVEL 434
Cdd:COG2205    81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPL-VYADPELLEQVLANLLDNAIKYSPPG-GTITISA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 435 RKRLDRrveVEVQIHDTGIGISERQQSQLFQAFRQADAsiSRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTFWFH 514
Cdd:COG2205   159 RREGDG---VRISVSDNGPGIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVT 233

                  .
gi 2750649407 515 I 515
Cdd:COG2205   234 L 234
sCache_4 pfam09984
Single cache domain 4; Members of this family of domains are found in various BarA-like signal ...
31-176 2.72e-67

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: 220.96  E-value: 2.72e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  31 VHRYNELQEQLVDAGASIIEPLAVASEYGMTFRSRESVRQLVSLLHRRHSDIVRSITVFDAQNNSFVTSNYHHNFAQLQL 110
Cdd:pfam09984   1 INRYYELEDQLIDRGTSIIEPLAIASEYGLTTRNRESLRRLISALHRKNSPIVRSIAIFDANNQLFVTSNYHRDFESLRL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2750649407 111 PKGVPLPTELMLTRRGDSLILRTPILSESQYPDETADGGSHPDNNLGYVAIELDLQSVRLQQYKEV 176
Cdd:pfam09984  81 PEGAPIPTLTTVEHSGDSLILRTPIISEGLSLPGLPATAESAQRPLGYIAIELNLDSARLQQYREI 146
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
285-780 2.20e-66

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 239.88  E-value: 2.20e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 285 AQEAARIKSEFLANMSHELRTPLNGVIGfTRQMLKT-DLSATQTDYLQTIERSANNLLTIINDVLDFSKLEAGKLVLEHI 363
Cdd:PRK10841  440 AEQASQSKSMFLATVSHELRTPLYGIIG-NLDLLQTkELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEPR 518
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 364 PFALRETLDEVVVLLAPSAHDKGLELTLDVHNDVPEQVIGDSLRLQQIITNLLGNAIKFTETGNIDIRVELRKRLdrrve 443
Cdd:PRK10841  519 EFSPREVINHITANYLPLVVKKRLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHVRVDGDY----- 593
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 444 VEVQIHDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTfwFHITLDLNEGM 523
Cdd:PRK10841  594 LSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQ--FTIRIPLYGAQ 671
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 524 LSLAPSLPDLNGKTLAYIESNPTAAQATLNMLSVTQLVITHsptLAQLPPGHYDFLLAgvpipfrDNMAQHEDKLLASLK 603
Cdd:PRK10841  672 YPQKKGVEGLQGKRCWLAVRNASLEQFLETLLQRSGIQVQR---YEGQEPTPEDVLIT-------DDPVQKKWQGRAVIT 741
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 604 LadrvilalpCQAQIDAELLKQQG----------ALGCLIKPITSTRLfpLLRMETPTRLTAPPERKRL-PLTVMAVDDN 672
Cdd:PRK10841  742 F---------CRRHIGIPLEIAPGewvhstatphELPALLARIYRIEL--ESDDSANALPSTDKAVSDNdDMMILVVDDH 810
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 673 PANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHnsTPIVAVTAHAASGER 752
Cdd:PRK10841  811 PINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLT--LPVIGVTANALAEEK 888
                         490       500
                  ....*....|....*....|....*...
gi 2750649407 753 EHLLQAGMDDYLAKPIDEKMLTRVLSRY 780
Cdd:PRK10841  889 QRCLEAGMDSCLSKPVTLDVLKQTLTVY 916
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
282-865 7.49e-66

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 235.99  E-value: 7.49e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 282 KKRAQE----AARIKSEFLANMSHELRTPLNGVIGFTRQMLKTDLSATQTDYLQTIERSANNLLTIINDVLDFSKLEAGK 357
Cdd:PRK11091  269 RKRYQDalekASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRK 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 358 LVLEHIPFALRETLDEVVVLLAPSAHDKGLELTLDVHNDVPEQVIGDSLRLQQIITNLLGNAIKFTETGNIDIRVELRKR 437
Cdd:PRK11091  349 LQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRYEEG 428
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 438 LDRRVEVEvqihDTGIGISERQQSQLFQAFRQADASISRRHG-GTGLGLVITQKLVKEMGGDICFHSQLNRGSTFWFHIT 516
Cdd:PRK11091  429 DMLTFEVE----DSGIGIPEDELDKIFAMYYQVKDSHGGKPAtGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIH 504
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 517 LDLNEGMLSLAPSLPDLNGKTLAY-----IESNPTAAQATLNmlsvtqlvithsptlaqlppghydfllagvpipfrdnm 591
Cdd:PRK11091  505 APAVAEEVEDAFDEDDMPLPALNIllvedIELNVIVARSVLE-------------------------------------- 546
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 592 aqhedkllaslKLADRVILAlpcqaqidaellkqqgalgclikpitstrlfpllrmetptrltapperkrlpltvmavdd 671
Cdd:PRK11091  547 -----------KLGNSVDVA------------------------------------------------------------ 555
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 672 npanlkligtllgeqvektllcESGEEALALARDNVLDLILMDIQMPKMDGIH-ASELIRQLPHHNSTPIVAVTAHAASG 750
Cdd:PRK11091  556 ----------------------MTGKEALEMFDPDEYDLVLLDIQLPDMTGLDiARELRERYPREDLPPLVALTANVLKD 613
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 751 EREhLLQAGMDDYLAKPIDEKMLTRVLSRYHSGDVENAVADDAPLS-------LDWPLaLRQAAN--KPDLARDLLQMLL 821
Cdd:PRK11091  614 KKE-YLDAGMDDVLSKPLSVPALTAMIKKFWDTQDDEESTVTTEESskanealLDIPM-LEQYVElvGPKLITDSLAVFE 691
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....
gi 2750649407 822 DFLPQVRERVQALLDGQHDDEILDLVHKLHGSCSYSGVPRLKQL 865
Cdd:PRK11091  692 KMMPGYLSVLDSNLTARDQKGIVEEAHKIKGAAGSVGLRHLQQL 735
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
212-515 1.06e-63

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 219.81  E-value: 1.06e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 212 VDRIRRGQLDSRVEGYMLGELHMLKNGINSMAMSLTAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEaaRI 291
Cdd:COG5002    87 ALLLLLLLLLLLLALLILLLLLALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLE--QM 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 292 KSEFLANMSHELRTPLNGVIGFTrQMLK---TDLSATQTDYLQTIERSANNLLTIINDVLDFSKLEAGKLVLEHIPFALR 368
Cdd:COG5002   165 RREFVANVSHELRTPLTSIRGYL-ELLLdgaADDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLA 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 369 ETLDEVVVLLAPSAHDKGLELTLDVHNDVPeQVIGDSLRLQQIITNLLGNAIKFT-ETGNIDIRVELRKRldrrvEVEVQ 447
Cdd:COG5002   244 ELLEEVVEELRPLAEEKGIELELDLPEDPL-LVLGDPDRLEQVLTNLLDNAIKYTpEGGTITVSLREEDD-----QVRIS 317
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2750649407 448 IHDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTFWFHI 515
Cdd:COG5002   318 VRDTGIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITL 385
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
408-517 1.34e-54

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: 184.23  E-value: 1.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 408 LQQIITNLLGNAIKFTETGNIDIRVELRKRLDRRVEVEVQIHDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVI 487
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 2750649407 488 TQKLVKEMGGDICFHSQLNRGSTFWFHITL 517
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
169-556 1.63e-49

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 189.35  E-value: 1.63e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 169 RLQQYKEVFVSTLLLL--LCMCIAILFAYRLM-RDVTGPIRNMVNTVDRIRRGQLDSRV-EGYMLGELHMLKNGINSMAM 244
Cdd:PRK11466  321 HLEKASARGQYSLLLLgmVSLCALILILWRVVyRSVTRPLAEQTQALQRLLDGDIDSPFpETAGVRELDTIGRLMDAFRS 400
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 245 SLTAYHEEMQQNIDQATSDLRETLEQMeiqnVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQMLKTDLSA 324
Cdd:PRK11466  401 NVHALNRHREQLAAQVKARTAELQELV----IEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALN 476
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 325 TQTDYLQTIERSANNLLTIINDVLDFSKLEAG--KLVLEHIPFALRETLDEVVVLLAPSAHDKGLELTLDVHNDVPEQVI 402
Cdd:PRK11466  477 AQRDDLRAITDSGESLLTILNDILDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALM 556
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 403 GDSLRLQQIITNLLGNAIKFTETGNIdirvELRKRLDRR---VEVEvqihDTGIGISERQQSQLFQAFRQADAsisrRHG 479
Cdd:PRK11466  557 GDPRRIRQVITNLLSNALRFTDEGSI----VLRSRTDGEqwlVEVE----DSGCGIDPAKLAEIFQPFVQVSG----KRG 624
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2750649407 480 GTGLGLVITQKLVKEMGGDICFHSQLNRGSTFWFHITLDLNEGMLSLAPSLP-DLNGKTLAYIESNPTAAQATLNMLS 556
Cdd:PRK11466  625 GTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLRVATAPVPKTVNQAvRLDGLRLLLIEDNPLTQRITAEMLN 702
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
4-515 2.11e-47

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 177.28  E-value: 2.11e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407   4 YSLRARMMILILAPTLLIGLLLSTFFVVHRYNELQEQLVDAGASIIEPLAVASEYGMTFRSRESVRQLVSLLHRRHSDIV 83
Cdd:COG4251    10 LLLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLLLLLLLEL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  84 RSITVFDAQNNSFVTSNYHHNFAQLQLPKGVPLPTELMLTRRGDSLILRTPILSESQYPDETADGGSHPDNNLGYVAIEL 163
Cdd:COG4251    90 ALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 164 DLQSVRLQQYKEVFVSTLLLLLCMCIAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKNGINSMA 243
Cdd:COG4251   170 LLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLI 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 244 MSLTAYHEEMQQNidQATSDLRETLEQMEIQNVELDlakkraqeaariksEFLANMSHELRTPLNGVIGFTrQMLKTD-- 321
Cdd:COG4251   250 LVLELLELRLELE--ELEEELEERTAELERSNEELE--------------QFAYVASHDLREPLRKISGFS-QLLEEDyg 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 322 --LSATQTDYLQTIERSANNLLTIINDVLDFSKLEAGKLVLEhiPFALRETLDEVVVLLAPSAHDKGLELTLDvhnDVPE 399
Cdd:COG4251   313 dkLDEEGREYLERIRDAAERMQALIDDLLAYSRVGRQELEFE--PVDLNELLEEVLEDLEPRIEERGAEIEVG---PLPT 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 400 qVIGDSLRLQQIITNLLGNAIKFT---ETGNIDIRVELRKRldrrvEVEVQIHDTGIGISERQQSQLFQAFRQADASisR 476
Cdd:COG4251   388 -VRGDPTLLRQVFQNLISNAIKYSrpgEPPRIEIGAEREGG-----EWVFSVRDNGIGIDPEYAEKIFEIFQRLHSR--D 459
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 2750649407 477 RHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTFWFHI 515
Cdd:COG4251   460 EYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTL 498
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
262-519 1.86e-42

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: 162.07  E-value: 1.86e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 262 SDLRETLEQMeiqnveldlakkRAQEAARIKSEFLANMSHELRTPLNGVIGFTrQMLKTDLSATQTDYLQTIERSANNLL 341
Cdd:COG5809   252 TERKKLEELL------------RKSEKLSVVGELAAGIAHEIRNPLTSLKGFI-QLLKDTIDEEQKTYLDIMLSELDRIE 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 342 TIINDVLDFSKLEAGKLVlehiPFALRETLDEVVVLLAPSAHDKGLELTLDVHNDVPeQVIGDSLRLQQIITNLLGNAIK 421
Cdd:COG5809   319 SIISEFLVLAKPQAIKYE----PKDLNTLIEEVIPLLQPQALLKNVQIELELEDDIP-DILGDENQLKQVFINLLKNAIE 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 422 FT-ETGNIDIRVelrKRLDRRVeVEVQIHDTGIGISERQQSQLFQAFrqadasISRRHGGTGLGLVITQKLVKEMGGDIC 500
Cdd:COG5809   394 AMpEGGNITIET---KAEDDDK-VVISVTDEGCGIPEERLKKLGEPF------YTTKEKGTGLGLMVSYKIIEEHGGKIT 463
                         250
                  ....*....|....*....
gi 2750649407 501 FHSQLNRGSTfwFHITLDL 519
Cdd:COG5809   464 VESEVGKGTT--FSITLPI 480
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
176-521 2.76e-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: 2.76e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 176 VFVSTLLLLLCMCIAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKNGINSMAMSLTAYHEEMQ- 254
Cdd:COG5000     8 LLLLLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARAFNRMTDQLKEQREELEe 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 255 -----QNIDQATSD----------------------------------------------LRETLEQMEIQNVELDLAKK 283
Cdd:COG5000    88 rrrylETILENLPAgvivldadgritlanpaaerllgipleeligkpleellpeldlaelLREALERGWQEEIELTRDGR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 284 --------------------------RAQEAARIKsEFLANMSHELRTPLNGVIGFTrQMLKTDLSATQTD-------YL 330
Cdd:COG5000   168 rtllvrasplrddgyvivfdditellRAERLAAWG-ELARRIAHEIKNPLTPIQLSA-ERLRRKLADKLEEdredlerAL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 331 QTIERSANNLLTIINDVLDFSKLEAGKLVlehiPFALRETLDEVVVLLAPSAHDKGLELTLDVHNDVPEqVIGDSLRLQQ 410
Cdd:COG5000   246 DTIIRQVDRLKRIVDEFLDFARLPEPQLE----PVDLNELLREVLALYEPALKEKDIRLELDLDPDLPE-VLADRDQLEQ 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 411 IITNLLGNAIKFTE-TGNIDIRVElrkRLDRRVEVEVQihDTGIGISERQQSQLFQAFrqadasISRRHGGTGLGLVITQ 489
Cdd:COG5000   321 VLINLLKNAIEAIEeGGEIEVSTR---REDGRVRIEVS--DNGPGIPEEVLERIFEPF------FTTKPKGTGLGLAIVK 389
                         410       420       430
                  ....*....|....*....|....*....|..
gi 2750649407 490 KLVKEMGGDICFHSQLNRGSTFWfhITLDLNE 521
Cdd:COG5000   390 KIVEEHGGTIELESRPGGGTTFT--IRLPLAE 419
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
666-777 4.61e-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: 137.60  E-value: 4.61e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLL---GEQVEktlLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPH-HNSTPIV 741
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLeklGYEVD---VAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGgGRRTPII 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2750649407 742 AVTAHAASGEREHLLQAGMDDYLAKPIDEKMLTRVL 777
Cdd:cd17546    78 ALTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
663-780 6.31e-37

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: 134.98  E-value: 6.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 663 PLTVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNSTPIVA 742
Cdd:COG0784     5 GKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPIIA 84
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2750649407 743 VTAHAASGEREHLLQAGMDDYLAKPIDEKMLTRVLSRY 780
Cdd:COG0784    85 LTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRL 122
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
158-515 1.01e-36

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 142.24  E-value: 1.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 158 YVAIELDLQSVRLQQYKEVFVSTLLLLLCMCIAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKN 237
Cdd:COG4191     2 LRLLLLLLLLLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 238 GINSMAMSLTAYHEEMQQNIDQATSDLRETLEQmEIQNVELDLAKKRAQEAARIKSEFLANM-------SHELRTPLNGV 310
Cdd:COG4191    82 LGLLLLLLLEALLLLLLAALDAEENAELEELER-DITELERAEEELRELQEQLVQSEKLAALgelaagiAHEINNPLAAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 311 IGFTrQMLKTDLSATQTD-----YLQTIERSANNLLTIINDVLDFSKLEAGKLVlehiPFALRETLDEVVVLLAPSAHDK 385
Cdd:COG4191   161 LGNA-ELLRRRLEDEPDPeelreALERILEGAERAAEIVRSLRAFSRRDEEERE----PVDLNELIDEALELLRPRLKAR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 386 GLELTLDVHNDVPeQVIGDSLRLQQIITNLLGNAI---KFTETGNIDIRVELRKRldrrvEVEVQIHDTGIGISERQQSQ 462
Cdd:COG4191   236 GIEVELDLPPDLP-PVLGDPGQLEQVLLNLLINAIdamEEGEGGRITISTRREGD-----YVVISVRDNGPGIPPEVLER 309
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2750649407 463 LFQAF---RQADasisrrhGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTFWFHI 515
Cdd:COG4191   310 IFEPFfttKPVG-------KGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITL 358
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
272-511 1.66e-36

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 141.52  E-value: 1.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 272 EIQNVELDLAKKRAQEAARiksEFLANMSHELRTPLNGVIGFTrQMLKTDLSATQ-TDYLQTIERSANNLLTIINDVLDF 350
Cdd:COG3852   118 ERKRLERELRRAEKLAAVG---ELAAGLAHEIRNPLTGIRGAA-QLLERELPDDElREYTQLIIEEADRLNNLVDRLLSF 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 351 SKLEAgklvLEHIPFALRETLDEVVVLLAPSAhDKGLELTLDVHNDVPEqVIGDSLRLQQIITNLLGNAIK-FTETGNID 429
Cdd:COG3852   194 SRPRP----PEREPVNLHEVLERVLELLRAEA-PKNIRIVRDYDPSLPE-VLGDPDQLIQVLLNLVRNAAEaMPEGGTIT 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 430 IRVELRK-----RLDRRVEVEVQIHDTGIGISERQQSQLFQAFrqadasISRRHGGTGLGLVITQKLVKEMGGDICFHSQ 504
Cdd:COG3852   268 IRTRVERqvtlgGLRPRLYVRIEVIDNGPGIPEEILDRIFEPF------FTTKEKGTGLGLAIVQKIVEQHGGTIEVESE 341

                  ....*..
gi 2750649407 505 LNRGSTF 511
Cdd:COG3852   342 PGKGTTF 348
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
290-515 1.30e-35

phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory histidine kinase PhoR associated with the phosphate ABC transporter in most Proteobacteria. Related proteins from Gram-positive organisms are not included in this model. The phoR gene usually is adjacent to the response regulator phoB gene (TIGR02154). [Signal transduction, Two-component systems]


Pssm-ID: 274368 [Multi-domain]  Cd Length: 333  Bit Score: 138.11  E-value: 1.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 290 RIKSEFLANMSHELRTPLNGVIGFTRQMLKT--DLSATQTDYLQTIERSANNLLTIINDVLDFSKLEAGKLVLEHIPFAL 367
Cdd:TIGR02966 112 QMRRDFVANVSHELRTPLTVLRGYLETLADGpdEDPEEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDM 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 368 RETLDEVVVLLAPSAHDKGLELTLDVHNDVPeqVIGDSLRLQQIITNLLGNAIKFT-ETGNIDIRVELRkrlDRRVEVEV 446
Cdd:TIGR02966 192 PALLDHLRDEAEALSQGKNHQITFEIDGGVD--VLGDEDELRSAFSNLVSNAIKYTpEGGTITVRWRRD---GGGAEFSV 266
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2750649407 447 QihDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTFWFHI 515
Cdd:TIGR02966 267 T--DTGIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFSFIF 333
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
665-769 8.32e-35

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: 128.43  E-value: 8.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNSTPIVAVT 744
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALT 80
                          90       100
                  ....*....|....*....|....*
gi 2750649407 745 AHAASGEREHLLQAGMDDYLAKPID 769
Cdd:cd17548    81 AYAMKGDREKILEAGCDGYISKPID 105
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
259-870 1.10e-32

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 137.17  E-value: 1.10e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  259 QATSDLRETLEQMEIQnveldlaKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQMLKTDLSATQ-TDYLQTIERSA 337
Cdd:PRK09959   686 QDITETRDLIHALEVE-------RNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQrVEAISLAYATG 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  338 NNLLTIINDVLDFSKLEAGKLVLE----HIPFALRETLDEVVVLLAPSAhdkgleLTLDVHNDVPEQ--VIGDSLRLQQI 411
Cdd:PRK09959   759 QSLLGLIGEILDVDKIESGNYQLQpqwvDIPTLVQNTCHSFGAIAASKS------IALSCSSTFPDHylVKIDPQAFKQV 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  412 ITNLLGNAIKFTETGNIDIRVELRKRLDRRVEVEVQIHDTGIGISERQQSQLFQAFRQADAsiSRRHGGTGLGLVITQKL 491
Cdd:PRK09959   833 LSNLLSNALKFTTEGAVKITTSLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSA--GRQQTGSGLGLMICKEL 910
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  492 VKEMGGDICFHSQLNRGSTFwfhitldlnegmlslapslpdlngktlayiesnptaaqatlnmlsvtqlvithsptlaql 571
Cdd:PRK09959   911 IKNMQGDLSLESHPGIGTTF------------------------------------------------------------ 930
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  572 ppghydfllaGVPIPfrdnmaqhedkllaslkladrvilalpcqaqidAELLKQQGALGClikpitstrlfpllRMETPT 651
Cdd:PRK09959   931 ----------TITIP---------------------------------VEISQQVATVEA--------------KAEQPI 953
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  652 RLtapPERkrlpLTVMAVDDNPAN---LKLIGTLLGEQVEKTllcESGEEALALARDNVLDLILMDIQMPKMDGIhasEL 728
Cdd:PRK09959   954 TL---PEK----LSILIADDHPTNrllLKRQLNLLGYDVDEA---TDGVQALHKVSMQHYDLLITDVNMPNMDGF---EL 1020
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  729 IRQLPHHNST-PIVAVTAHAASGEREHLLQAGMDDYLAKPIDEKMLTRVLSRYHSgdvenaVADDAPL--SLDWPLALRQ 805
Cdd:PRK09959  1021 TRKLREQNSSlPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQ------VAHIAPQyrHLDIEALKNN 1094
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2750649407  806 AANKPDLARDLlqmLLDFLPQVRERVQA---LLDGQHDDEILDLVHKLHGSCSYSGVPRLKQLCFYLE 870
Cdd:PRK09959  1095 TANDLQLMQEI---LMTFQHETHKDLPAafhALEAGDNRTFHQCIHRIHGAANILNLQKLINISHQLE 1159
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
403-515 1.61e-32

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 121.60  E-value: 1.61e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  403 GDSLRLQQIITNLLGNAIKFTETGnIDIRVELRKRLDRrveVEVQIHDTGIGISERQQSQLFQAFRQADASiSRRHGGTG 482
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEG-GRITVTLERDGDH---VEITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGTG 75
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2750649407  483 LGLVITQKLVKEMGGDICFHSQLNRGSTFWFHI 515
Cdd:smart00387  76 LGLSIVKKLVELHGGEISVESEPGGGTTFTITL 108
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
663-780 6.71e-31

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: 119.63  E-value: 6.71e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 663 PLTVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNSTPIVA 742
Cdd:COG3706     1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIF 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2750649407 743 VTAHAASGEREHLLQAGMDDYLAKPIDEKMLTR---VLSRY 780
Cdd:COG3706    81 LTALDDEEDRARALEAGADDYLTKPFDPEELLArvdLVARY 121
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
239-511 2.14e-29

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


Pssm-ID: 444508 [Multi-domain]  Cd Length: 412  Bit Score: 121.90  E-value: 2.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 239 INSMAMSLTAY-HEEMQQNIDqatsdLRETLEQMEIQNveldlakkraqeaarIKSEFLANMSHELRTPLNGVIGFTrQM 317
Cdd:COG5806   167 IQLLAMLIAVYlIENLIENIL-----LRKELQRAEKLE---------------VVSELAASIAHEVRNPLTVVRGFI-QL 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 318 LKTD--LSATQTDYLQT----IERsANNlltIINDVLDFSKLEAGKLvlEHIPFAlrETLDEVVVLLAPSAHDKGLELTL 391
Cdd:COG5806   226 LQEPelSDEKRKQYIRIaleeLDR-AEA---IITDYLTFAKPQPEKL--EKIDVS--EELEHVIDVLSPYANMNNVEIQT 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 392 DVHNDVpeQVIGDSLRLQQIITNLLGNAIKFTET-GNIDIRVELRKRldrrvEVEVQIHDTGIGISERQQSQLFQAFrqa 470
Cdd:COG5806   298 ELEPGL--YIEGDRQKLQQCLINIIKNGIEAMPNgGTLTIDVSIDKN-----KVIISIKDTGVGMTKEQLERLGEPY--- 367
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2750649407 471 dasISRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTF 511
Cdd:COG5806   368 ---FSTKEKGTGLGTMVSYRIIEAMNGTIRVESEVGKGTTF 405
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
158-531 2.50e-29

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 123.21  E-value: 2.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 158 YVAIELDLQSVRLQQYKEVFVSTLLLLLCMCIAIlfAYRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKN 237
Cdd:NF040691  171 YLLFPLEDEQSTLALVRGTLLLGGLALVVLLGLI--AWLVTRQVVAPVRSAARTAERFAAGDLSERMPVKGEDDLARLAR 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 238 GINSMAMSLtayheemQQNIDQatsdlretLEQMeiqnveldlakkraqeaARIKSEFLANMSHELRTPLNgvigfTRQM 317
Cdd:NF040691  249 SFNQMADSL-------QRQIRQ--------LEEL-----------------SRLQQRFVSDVSHELRTPLT-----TIRM 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 318 LKTDLSATQTDYLQTIERSAnNLL--------TIINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVLLAPSAHDKGLEL 389
Cdd:NF040691  292 AADVIHDSRDDFDPATARSA-ELLhteldrfeSLLSDLLEISRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVEL 370
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 390 TLDVhNDVPEQVIGDSLRLQQIITNLLGNAIKFTETGNIDIRVElrkrlDRRVEVEVQIHDTGIGISERQQSQLFQAFRQ 469
Cdd:NF040691  371 RVDA-PGTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTVA-----QDDTAVAVTVRDHGVGLKPGEVALVFDRFWR 444
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2750649407 470 ADASISRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTfwFHITLDLNEGMLSLAPSLP 531
Cdd:NF040691  445 ADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQ--FRLTLPRVAGDRLTTSPLP 504
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
3-513 3.27e-29

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: 122.11  E-value: 3.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407   3 KYSLRARMMILILAPTLLIGLLLSTFFVVHRYNELQEQLVDAGASIIEplAVASEYGMTFRSRESVRQLVSLLH---RRH 79
Cdd:TIGR01386   1 PRSLTLRLALLFAAVTALVFALSGFMLYSSLERHFEERDREELQGKLE--QVRRFLRDPADLDEDIKRLQEKIDdllVGH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  80 SDIVRSITVFDaqnNSFVTSNYHHNfaqlQLPKGVPLPTELMLTRRGDSLILRTPILSESQYPDETADGGSHPdnnLGYV 159
Cdd:TIGR01386  79 SDLALSILNPD---GRLLFERAQGA----ALVPAVAANDALLELDQADAKMTHYRSILRSVAALPGGKGRKPV---QITV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 160 AIELDLQSVRLQQYKE-VFVSTLLLLLcmcIAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEgymlgelhmlkng 238
Cdd:TIGR01386 149 ALDINAHTHLLDALRKwLILIAVLLVL---LTALLGWWITRLGLEPLRRLSAVAARISPESLDQRLD------------- 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 239 insmamsltayheemqqnidqaTSDLRETLEQMEIqnvELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQML 318
Cdd:TIGR01386 213 ----------------------PSRAPAELRELAQ---SFNAMLGRLEDAFQRLSQFSADLAHELRTPLTNLLGQTQVAL 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 319 KTDlsATQTDYLQTIERSA---NNLLTIINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVLLAPSAHDKGLELTLDVHN 395
Cdd:TIGR01386 268 SQP--RTGEEYREVLESNLeelERLSRMVSDMLFLARADNGQLALERVRLDLAAELAKVAEYFEPLAEERGVRIRVEGEG 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 396 dvpeQVIGDSLRLQQIITNLLGNAIKFT-ETGNIDIRVElrkrlDRRVEVEVQIHDTGIGISERQQSQLFQAFRQADASI 474
Cdd:TIGR01386 346 ----LVRGDPQMFRRAISNLLSNALRHTpDGGTITVRIE-----RRSDEVRVSVSNPGPGIPPEHLSRLFDRFYRVDPAR 416
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 2750649407 475 SRRHGGTGLGLVITQKLVKEMGGDiCFHSQLNRGSTFWF 513
Cdd:TIGR01386 417 SNSGEGTGLGLAIVRSIMEAHGGR-ASAESPDGKTRFIL 454
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
659-779 5.11e-29

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: 115.65  E-value: 5.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 659 RKRLPLTVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNST 738
Cdd:COG3437     2 RTGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDI 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2750649407 739 PIVAVTAHAASGEREHLLQAGMDDYLAKPIDEKMLTRVLSR 779
Cdd:COG3437    82 PVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRN 122
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
403-515 1.07e-28

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: 110.92  E-value: 1.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 403 GDSLRLQQIITNLLGNAIKFT-ETGNIDIRVElrkrldRRVEVEVQIHDTGIGISERQQSQLFQAFRQADasiSRRHGGT 481
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAaKAGEITVTLS------EGGELTLTVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGGT 71
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2750649407 482 GLGLVITQKLVKEMGGDICFHSQLNRGSTFWFHI 515
Cdd:pfam02518  72 GLGLSIVRKLVELLGGTITVESEPGGGTTVTLTL 105
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
666-776 4.30e-28

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: 109.16  E-value: 4.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHnsTPIVAVTA 745
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPT--TPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2750649407 746 HAASGEREHLLQAGMDDYLAKPID-EKMLTRV 776
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDpDELLAAI 110
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
179-505 2.62e-25

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 110.30  E-value: 2.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 179 STLLLLLCMCIAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKNGINSMAmsltayheemqqnid 258
Cdd:NF012163  166 SWLIVALALLLAALAAFLLARGLLAPVKRLVEATHRLAAGDYTTRVTPTSNDELGKLAQDFNQLA--------------- 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 259 qatsdlrETLEQMEiqnveldlakkraqeaaRIKSEFLANMSHELRTPLngvigftrQMLKTDLSATQT-------DYLQ 331
Cdd:NF012163  231 -------STLEKNE-----------------QMRRDFMADISHELRTPL--------AVLRAELEAIQDgirkftpESLD 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 332 TIERSANNLLTIINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVLLAPSAHDKGLELtldvHNDVPEQ--VIGDSLRLQ 409
Cdd:NF012163  279 SLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLEL----EVSLPDSslVFGDRDRLM 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 410 QIITNLLGNAIKFTETGNiDIRVELRKRlDRrvEVEVQIHDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQ 489
Cdd:NF012163  355 QLFNNLLENSLRYTDSGG-SLHISASQR-PK--EVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISL 430
                         330
                  ....*....|....*..
gi 2750649407 490 KLVKEMGGDICF-HSQL 505
Cdd:NF012163  431 NIVQAHGGTLHAaHSPL 447
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
666-777 9.38e-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: 99.45  E-value: 9.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNSTPIVAVTA 745
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTG 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2750649407 746 HAASGEREHLLQAGMDDYLAKPIDEKMLTRVL 777
Cdd:cd17580    81 YGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
663-785 3.59e-24

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: 101.19  E-value: 3.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 663 PLTVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHnsTPIVA 742
Cdd:COG0745     1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSD--IPIIM 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2750649407 743 VTAHAASGEREHLLQAGMDDYLAKPIDEKMLT---RVLSRYHSGDV 785
Cdd:COG0745    79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLariRALLRRRAAEV 124
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
669-767 1.88e-23

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 95.37  E-value: 1.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 669 VDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHnsTPIVAVTAHAA 748
Cdd:cd00156     3 VDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPD--IPVIVLTAKAD 80
                          90
                  ....*....|....*....
gi 2750649407 749 SGEREHLLQAGMDDYLAKP 767
Cdd:cd00156    81 EEDAVRALELGADDYLVKP 99
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
665-776 4.23e-23

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: 95.20  E-value: 4.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPANLKLIGTLLGEQVEKTLLC-ESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNSTPIVAV 743
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRSAGYLEVVSfTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVMI 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2750649407 744 TAHAASGEREHLLQAGMDDYLAKPID-EKMLTRV 776
Cdd:cd17551    82 TADTDREVRLRALEAGATDFLTKPFDpVELLARV 115
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
179-499 7.69e-23

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 102.79  E-value: 7.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 179 STLLLLLCMCIAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKNGINSMAMSLtayheemqqnid 258
Cdd:PRK10549  166 SWLIVALSTLLAALATFLLARGLLAPVKRLVEGTHKLAAGDFTTRVTPTSRDELGRLAQDFNQLASTL------------ 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 259 qatsdlrETLEQMeiqnveldlakKRAqeaarikseFLANMSHELRTPLngvigftrQMLKTDLSATQTDYLQTIERSAN 338
Cdd:PRK10549  234 -------EKNEQM-----------RRD---------FMADISHELRTPL--------AVLRGELEAIQDGVRKFTPESVA 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 339 NLLT-------IINDVLDFSKLEAGKLvlehipfALRETLDEVVVLLAPSA-------HDKGLELTLDVHNDVPeqVIGD 404
Cdd:PRK10549  279 SLQAevgtltkLVDDLHQLSLSDEGAL-------AYRKTPVDLVPLLEVAGgafrerfASRGLTLQLSLPDSAT--VFGD 349
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 405 SLRLQQIITNLLGNAIKFT-ETGNIDIRVELRkrlDRRVEVEVQihDTGIGISERQQSQLFQAFRQADASISRRHGGTGL 483
Cdd:PRK10549  350 PDRLMQLFNNLLENSLRYTdSGGSLHISAEQR---DKTLRLTFA--DSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGL 424
                         330
                  ....*....|....*.
gi 2750649407 484 GLVITQKLVKEMGGDI 499
Cdd:PRK10549  425 GLAICLNIVEAHNGRI 440
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
665-768 1.23e-22

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: 93.33  E-value: 1.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNSTPIVAVT 744
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                          90       100
                  ....*....|....*....|....
gi 2750649407 745 AHAASGEREHLLQAGMDDYLAKPI 768
Cdd:cd17538    81 ALDDREDRIRGLEAGADDFLSKPI 104
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
281-511 2.05e-22

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 102.74  E-value: 2.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 281 AKKRAQE----AARIKS--EFLANMSHELRTPLNGVIGFTrQML--KTDLSATQtDYLQTIERSANNLLTIINDVLDFSK 352
Cdd:PRK11360  373 ERKRLQRrvarQERLAAlgELVAGVAHEIRNPLTAIRGYV-QIWrqQTSDPPSQ-EYLSVVLREVDRLNKVIDQLLEFSR 450
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 353 LEAGKLVlehiPFALRETLDEVVVLLAPSAHDKGLELTLDVHNDVPEQVIgDSLRLQQIITNLLGNAIK-FTETGNIDIR 431
Cdd:PRK11360  451 PRESQWQ----PVSLNALVEEVLQLFQTAGVQARVDFETELDNELPPIWA-DPELLKQVLLNILINAVQaISARGKIRIR 525
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 432 VELRKrlDRRVEVEVQihDTGIGISERQQSQLFQAFrqadasISRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTF 511
Cdd:PRK11360  526 TWQYS--DGQVAVSIE--DNGCGIDPELLKKIFDPF------FTTKAKGTGLGLALSQRIINAHGGDIEVESEPGVGTTF 595
PRK09303 PRK09303
histidine kinase;
251-517 2.13e-22

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 100.41  E-value: 2.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 251 EEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPL--------------NGVIGFTRQ 316
Cdd:PRK09303  110 GENLQPSEIDSGRYSQELLQLSDELFVLRQENETLLEQLKFKDRVLAMLAHDLRTPLtaaslaletlelgqIDEDTELKP 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 317 MLKTDLSATQTDYLQTIERsannlltIINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVLLAPSAHDKGLELTLDVHND 396
Cdd:PRK09303  190 ALIEQLQDQARRQLEEIER-------LITDLLEVGRTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSD 262
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 397 VPEqVIGDSLRLQQIITNLLGNAIKFTETGNIdIRVELRKRLDRRveVEVQIHDTGIGISERQQSQLFQ-AFR-QADASI 474
Cdd:PRK09303  263 LPS-VYADQERIRQVLLNLLDNAIKYTPEGGT-ITLSMLHRTTQK--VQVSICDTGPGIPEEEQERIFEdRVRlPRDEGT 338
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2750649407 475 SrrhgGTGLGLVITQKLVKEMGGDICFHSQLNRGStfWFHITL 517
Cdd:PRK09303  339 E----GYGIGLSVCRRIVRVHYGQIWVDSEPGQGS--CFHFTL 375
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
245-646 5.51e-21

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 98.98  E-value: 5.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 245 SLTAYHEEMQQnIDQATSDLRETLEQMEIQNvELDLAKKRAQEAARIKS--EFLANMSHELRTPLNGVIGFTRQML-KTD 321
Cdd:PRK13837  403 GLRPPAGELQL-LELALDCLAHAIERRRLET-ERDALERRLEHARRLEAvgTLASGIAHNFNNILGAILGYAEMALnKLA 480
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 322 LSATQTDYLQTIERSANNLLTIINDVLDFSKLEAGKLVlehiPFALRETLDEVVVLLApSAHDKGLELTLDVHNDvPEQV 401
Cdd:PRK13837  481 RHSRAARYIDEIISAGARARLIIDQILAFGRKGERNTK----PFDLSELVTEIAPLLR-VSLPPGVELDFDQDQE-PAVV 554
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 402 IGDSLRLQQIITNLLGNAIK-FTETGNIDI---RVELR--KRLDRRVE-----VEVQIHDTGIGISERQQSQLFQAFrqa 470
Cdd:PRK13837  555 EGNPAELQQVLMNLCSNAAQaMDGAGRVDIslsRAKLRapKVLSHGVLppgryVLLRVSDTGAGIDEAVLPHIFEPF--- 631
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 471 dasISRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTF--WFHIT--LDLNEGMLSLAPSLPDLNGKTLAYIESNPt 546
Cdd:PRK13837  632 ---FTTRAGGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFdvYLPPSskVPVAPQAFFGPGPLPRGRGETVLLVEPDD- 707
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 547 aaqATLNMLSVTQLVITHSPTLAQLPPGHYDFLLAGvpiPFRDNMAQHEDKLLASLKLADRVILALPCQAQIDAE----- 621
Cdd:PRK13837  708 ---ATLERYEEKLAALGYEPVGFSTLAAAIAWISKG---PERFDLVLVDDRLLDEEQAAAALHAAAPTLPIILGGnsktm 781
                         410       420
                  ....*....|....*....|....*...
gi 2750649407 622 -LLKQQGALGCLI--KPITSTRLFPLLR 646
Cdd:PRK13837  782 aLSPDLLASVAEIlaKPISSRTLAYALR 809
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
665-767 1.04e-20

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: 87.91  E-value: 1.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPANLKLIGTLLGEQ--VEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQlpHHNSTPIVA 742
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEagFEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRE--LDPDTKIII 78
                          90       100
                  ....*....|....*....|....*
gi 2750649407 743 VTAHAASGEREHLLQAGMDDYLAKP 767
Cdd:COG4753    79 LSGYSDFEYAQEAIKLGADDYLLKP 103
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
279-517 1.40e-20

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: 96.34  E-value: 1.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 279 DLAKKRAQEAARIKSEFL-------ANMSHELRTPLNGVIGFTrQMLKTDLSaTQTDYLQTIERSANNLLTIINDVLDFS 351
Cdd:COG5805   267 DITEKKEAEELMARSEKLsiagqlaAGIAHEIRNPLTSIKGFL-QLLQPGIE-DKEEYFDIMLSELDRIESIISEFLALA 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 352 KLEAGKLVlehiPFALRETLDEVVVLLAPSAHDKGLELTLDVHNDVPEqVIGDSLRLQQIITNLLGNAIKFTET-GNIDI 430
Cdd:COG5805   345 KPQAVNKE----KENINELIQDVVTLLETEAILHNIQIRLELLDEDPF-IYCDENQIKQVFINLIKNAIEAMPNgGTITI 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 431 RVELRkrlDRRVEVEVQihDTGIGISERQQSQLFQAFrqadasISRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGST 510
Cdd:COG5805   420 HTEEE---DNSVIIRVI--DEGIGIPEERLKKLGEPF------FTTKEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTT 488

                  ....*..
gi 2750649407 511 fwFHITL 517
Cdd:COG5805   489 --FTITL 493
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
666-768 1.82e-20

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar domains; Pseudomonas aeruginosa cyclic di-GMP phosphodiesterase PA4781 contains an N-terminal REC domain and a C-terminal catalytic HD-GYP domain, characteristics of RpfG family response regulators. PA4781 is involved in cyclic di-3',5'-GMP (c-di-GMP) hydrolysis/degradation in a two-step reaction via the linear intermediate pGpG to produce GMP. Its unphosphorylated REC domain prevents accessibility of c-di-GMP to the active site. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 87.18  E-value: 1.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNSTPIVAVTA 745
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTA 80
                          90       100
                  ....*....|....*....|...
gi 2750649407 746 HAASGEREHLLQAGMDDYLAKPI 768
Cdd:cd19920    81 LTDTEDKVKGFELGAVDYITKPF 103
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
404-517 2.52e-20

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


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 86.75  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 404 DSLRLQQIITNLLGNAIKFTETGNIdIRVELRKRLDrrvEVEVQIHDTGIGISERQQSQLFQAFRQADASISRRHGGTGL 483
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTGGK-LRIRAAQTPQ---EVRLDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGL 76
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2750649407 484 GLVITQKLVKEMGGDICF-HSQLnrgSTFWFHITL 517
Cdd:cd16946    77 GLAICHNIALAHGGTISAeHSPL---GGLRLVLTL 108
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
177-515 3.12e-20

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 94.91  E-value: 3.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 177 FVSTLLLLLCMCIAILFAYRLMRdvtgPIRNMVNTVDRIRRGQldsRVE--GYMLGELhmlknginsmamsltayheemq 254
Cdd:PRK11100  186 WAGALLLGIALLIGAGVVWWLNR----SIRRLTRYADAVTEGK---PVPlpKLGSSEL---------------------- 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 255 qnidqatSDLRETLEQMEIQnveldLAKKRAQEaariksEFLANMSHELRTPLNGVIGfTRQMLKTDLS-ATQTDYLQTI 333
Cdd:PRK11100  237 -------RELAQALESMRVK-----LEGKAYVE------QYVQTLTHELKSPLAAIRG-AAELLQEDPPpEDRARFTGNI 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 334 ERSANNLLTIINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVLLAPSAHDKGLELTLDVhndVPEQVIGDSLRLQQIIT 413
Cdd:PRK11100  298 LTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEAREAQAAAKGITLRLRP---DDARVLGDPFLLRQALG 374
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 414 NLLGNAIKFTETGNiDIRVELRKRLDRrveVEVQIHDTGIGISERQQSQLFQAFrqadASISRRHGG---TGLGLVITQK 490
Cdd:PRK11100  375 NLLDNAIDFSPEGG-TITLSAEVDGEQ---VALSVEDQGPGIPDYALPRIFERF----YSLPRPANGrksTGLGLAFVRE 446
                         330       340
                  ....*....|....*....|....*..
gi 2750649407 491 LVKEMGGDICFHSQLNRG--STFWFHI 515
Cdd:PRK11100  447 VARLHGGEVTLRNRPEGGvlATLTLPR 473
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
669-767 5.07e-20

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: 85.54  E-value: 5.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 669 VDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHnsTPIVAVTAHAA 748
Cdd:cd17574     3 VEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSD--IPIIMLTAKDE 80
                          90
                  ....*....|....*....
gi 2750649407 749 SGEREHLLQAGMDDYLAKP 767
Cdd:cd17574    81 EEDKVLGLELGADDYITKP 99
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
279-513 7.85e-20

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 93.15  E-value: 7.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 279 DLAKKRAQEAARikSEFLANMSHELRTPLNGVIGFTRQMLKTDL-SATQTDYLQTIERSANNLLTIINDVLDFSKLEAGK 357
Cdd:PRK11006  193 DVTQMHQLEGAR--RNFFANVSHELRTPLTVLQGYLEMMQDQPLeGALREKALHTMREQTQRMEGLVKQLLTLSKIEAAP 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 358 LVlehipfALRETLD-----EVVVLLAPSAHDKGLELTLDVHNDVpeQVIGDSLRLQQIITNLLGNAIKFTETG-NIDIR 431
Cdd:PRK11006  271 TI------DLNEKVDvpmmlRVLEREAQTLSQGKHTITFEVDNSL--KVFGNEDQLRSAISNLVYNAVNHTPEGtHITVR 342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 432 velRKRLDRRVEVEVQihDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTF 511
Cdd:PRK11006  343 ---WQRVPQGAEFSVE--DNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRF 417

                  ..
gi 2750649407 512 WF 513
Cdd:PRK11006  418 SF 419
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
663-779 8.38e-20

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: 93.10  E-value: 8.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 663 PLTVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHnsTPIVA 742
Cdd:COG2204     2 MARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPD--LPVIL 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2750649407 743 VTAHAASGEREHLLQAGMDDYLAKPIDEKMLTRVLSR 779
Cdd:COG2204    80 LTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVER 116
PRK10490 PRK10490
sensor protein KdpD; Provisional
280-521 5.86e-19

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 92.41  E-value: 5.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 280 LAKKRAQEAARIKSE-------FLANMSHELRTPLNGVIGFTrQMLKTDLSATQTDYLQTIERSANNLLT---IINDVLD 349
Cdd:PRK10490  645 LTLTASEEQARLASEreqlrnaLLAALSHDLRTPLTVLFGQA-EILTLDLASEGSPHARQASEIRQQVLNttrLVNNLLD 723
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 350 FSKLEAGKlvlehipFALRE---TLDEVV----VLLAPSAHDKGLELTLdvhndvPEQVI---GDSLRLQQIITNLLGNA 419
Cdd:PRK10490  724 MARIQSGG-------FNLRKewlTLEEVVgsalQMLEPGLSGHPINLSL------PEPLTlihVDGPLFERVLINLLENA 790
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 420 IKFT-ETGNIDIRVELRkrlDRRVEVEVQihDTGIGISERQQSQLFQAFRQAD--ASISrrhgGTGLGLVITQKLVKEMG 496
Cdd:PRK10490  791 VKYAgAQAEIGIDAHVE---GERLQLDVW--DNGPGIPPGQEQLIFDKFARGNkeSAIP----GVGLGLAICRAIVEVHG 861
                         250       260
                  ....*....|....*....|....*
gi 2750649407 497 GDICFHSQLNRGSTfwFHITLDLNE 521
Cdd:PRK10490  862 GTIWAENRPEGGAC--FRVTLPLET 884
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
292-356 6.11e-19

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 81.46  E-value: 6.11e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2750649407  292 KSEFLANMSHELRTPLNGVIGFTRQMLKTDLSATQTDYLQTIERSANNLLTIINDVLDFSKLEAG 356
Cdd:smart00388   2 KREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
663-780 8.64e-19

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 83.48  E-value: 8.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 663 PLTVMAVDDNPANLKLIGTLLGEQ--VEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQL-PHHNSTP 739
Cdd:COG4565     3 MIRVLIVEDDPMVAELLRRYLERLpgFEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGL---ELLRELrARGPDVD 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2750649407 740 IVAVTAHAASGEREHLLQAGMDDYLAKPIDEKMLTRVLSRY 780
Cdd:COG4565    80 VIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERY 120
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
292-356 9.28e-19

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 81.10  E-value: 9.28e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2750649407 292 KSEFLANMSHELRTPLNGVIGFTRQMLKTDLSATQTDYLQTIERSANNLLTIINDVLDFSKLEAG 356
Cdd:pfam00512   2 KSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
663-780 1.12e-18

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 86.02  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 663 PLTVMAVDDNPANLKLIGTLLGE--QVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHnsTPI 740
Cdd:COG3279     1 MMKILIVDDEPLARERLERLLEKypDLEVVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPP--PPI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2750649407 741 VAVTAHaasgeREHLLQAgMD----DYLAKPIDEKMLTRVLSRY 780
Cdd:COG3279    79 IFTTAY-----DEYALEA-FEvnavDYLLKPIDEERLAKALEKA 116
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
404-511 1.38e-17

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: 79.07  E-value: 1.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 404 DSLRLQQIITNLLGNAIKFTETGNidiRVELRKRLDRRVEVEVQIHDTGIGISERQQSQLFQAFRQADASISRRHGGTGL 483
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTPDGG---RIRCILEKFRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGL 77
                          90       100
                  ....*....|....*....|....*...
gi 2750649407 484 GLVITQKLVKEMGGDICFHSQLNRGSTF 511
Cdd:cd16925    78 GLSIVKEFVELHGGTVTVSDAPGGGALF 105
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
666-779 3.35e-17

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: 78.53  E-value: 3.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLL---GEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQL-PHHNSTPIV 741
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIdweELGFEVVGEAENGEEALELIEEHKPDIVITDIRMPGMDGL---ELIEKIrELYPDIKII 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2750649407 742 AVTAHAasgEREHLLQA---GMDDYLAKPIDEKMLTRVLSR 779
Cdd:cd17536    78 ILSGYD---DFEYAQKAirlGVVDYLLKPVDEEELEEALEK 115
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
666-776 3.76e-17

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


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 77.94  E-value: 3.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQ--VEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQlpHHNSTPIVAV 743
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLESEpdIEVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRR--RYPDLKVIVL 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2750649407 744 TAHAASGEREHLLQAGMDDYLAKPID-EKMLTRV 776
Cdd:cd17535    79 TAHDDPEYVLRALKAGAAGYLLKDSSpEELIEAI 112
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
667-776 4.51e-17

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: 77.70  E-value: 4.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 667 MAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNSTPIVAVTAH 746
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAK 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2750649407 747 AASGEREHLLQAGMDDYLAKPIDEK-MLTRV 776
Cdd:cd19937    81 GEEFDKVLGLELGADDYITKPFSPReLLARV 111
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-513 5.62e-17

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: 77.37  E-value: 5.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 408 LQQIITNLLGNAIKFTETG---NIDIRVElrkrldrRVEVEVQIH--DTGIGISERQQSQLFQAFRQADASisRRHGGTG 482
Cdd:cd16921     1 LGQVLTNLLGNAIKFRRPRrppRIEVGAE-------DVGEEWTFYvrDNGIGIDPEYAEKVFGIFQRLHSR--EEYEGTG 71
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2750649407 483 LGLVITQKLVKEMGGDICFHSQLNRGSTFWF 513
Cdd:cd16921    72 VGLAIVRKIIERHGGRIWLESEPGEGTTFYF 102
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
68-522 6.49e-17

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


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 84.55  E-value: 6.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  68 VRQLVSLLHRRHSDIVRSITVFDAQNNSFVTSNYHHNFAQLQLPKGVPLPTELMLTRRGDSLILRTPILSESQYPDETAD 147
Cdd:COG3850     9 LALLRLLLALLALLLLALLLLSLLALLLLLERTLLRLLSLLASAGLLAALLAALLLLLSLGLLALLLALLLLLLLLLLAA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 148 GGSHPDNNLGYVAIELDLQSVRLQQYKEVFVSTLLLLLCMCIAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGY 227
Cdd:COG3850    89 LLSLLLLLLLLLLLLLLLLLLLLAAAINRKLALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGDFDARVPVS 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 228 MLGELHMLKNGINSMAMSLTAYHEEMQQNIDQAtsdlretleqmeiqnveldlakkRAQEAARIKSEFLANMSHELRTPL 307
Cdd:COG3850   169 GRDELGTLARAFNRMADELQELYAELEEEEELE-----------------------AELELLALLDELLLLAALLLLLAL 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 308 NGVIGFTRQMLKTDLSATQTDYLQTIERSANNLLTIINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVLLAPSAHDKGL 387
Cdd:COG3850   226 LLALLLAALLAALLLLLLLQDALAESELLALNILAGLLELLLALLLLLLASALLLLELELLALLLELVELLALAAAEEAL 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 388 ELTLDVHNDVPEQVIGDSLRLQQIITNLLGNAIKFTETGNIDIRVELRKRLDRRVEVEVQIHDTGIGISERQQSQLFQAF 467
Cdd:COG3850   306 LLLVELAALLLLLLLQAIANASLLLIALASVVAALLELASILALQAALEAAAAGAALAAAAAAAGLARALAQAGADAAEA 385
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2750649407 468 RQADASISRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTFWFHITLDLNEG 522
Cdd:COG3850   386 LGLLAEASEGAAGQGAGLVDVEGGVAGEGGLVVLIVSIIAGGEAIARGEALAARG 440
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
392-511 8.93e-17

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


Pssm-ID: 340423 [Multi-domain]  Cd Length: 125  Bit Score: 77.55  E-value: 8.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 392 DVHNDVPEQVI---GDSLRLQQIITNLLGNAIKFTETGNIdIRVELRkrlDRRVEVEVQIHDTGIGISERQQSQLFQAFR 468
Cdd:cd16947     2 QVEINIPDRPIyanANTEALQRILKNLISNAIKYGSDGKF-LGMTLR---EDEKHVYIDIWDKGKGISETEKDHVFERLY 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2750649407 469 QADASISRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTF 511
Cdd:cd16947    78 TLEDSRNSAKQGNGLGLTITKRLAESMGGSIYVNSKPYEKTVF 120
HPtr COG2198
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
63-876 1.41e-16

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


Pssm-ID: 441800 [Multi-domain]  Cd Length: 871  Bit Score: 84.71  E-value: 1.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  63 RSRESVRQLVSLLHRRHSDIVRSITVFDAQNNSFVTSNYHHNFAQLQLPKGVPLPTELMLTRRGDSLILRTPILSESQYP 142
Cdd:COG2198     4 LLLALLLLLLLLLLLLLLLLALLALLLLLLLAALALLLLLLLLLALLALLLLLVALALLLALLLLLLGVLLLLLDLLELL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 143 DETADGGSHPDNNLGYVAIELDLQSVRLQQYKEVFVSTLLLLLCMCIAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLDS 222
Cdd:COG2198    84 LLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLVLAALLLLLLL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 223 RVEGYMLGELHMLKNGINSMAMSLTAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHE 302
Cdd:COG2198   164 ALLLALLLLVLLVLLLLLLLLLLLLLLLLLLLLLLLLALTLAALLELLAAELALEALLAELAAEAAAALAAELALAELAA 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 303 LRTPLNGVIGFTRQMLKTDLSATQTDYLQTIERSANNLLTIINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVLLAPSA 382
Cdd:COG2198   244 LLLLLLLLLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLELLLLLLLALLLLLLLLLLLLLLL 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 383 HDKGLELTLDVHNDVPEQVIGDSLRLQQIITNLLGNAIKFTETGNIDIRVELRKRLDRRVEVEVQIHDTGIGISERQQSQ 462
Cdd:COG2198   324 LLLLLLLLLLLLLLLLLLLLLLLLLLALLLLALLLALLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLLLLL 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 463 LFQAFRQADASISRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTFWFH------------------------ITLD 518
Cdd:COG2198   404 LSLLLSLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLGLLLLLLLLLGLLLLlllgllllalllllllllllllllLLLL 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 519 LNEGMLSLAPSLPDLNGKTLAYIESNPTAAQATLNMLSVTQLVITHSPTLAQLPPGHYDFLLAGVPIPFRDNMAQHEDKL 598
Cdd:COG2198   484 LLLLLLLLLLLLLLLLLLLLLLLVAAALAALALLLLLALLLLLLLDLLILGLLLILLLLLLGLLALGLAALLLLLALLLG 563
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 599 LASLKLADRVILALPCQAQIDAELLKQQGALGCLIKPITSTRLFPLLRMETPTRLTAPPERKRLPLTVMAVDDNPANLKL 678
Cdd:COG2198   564 LGLLLGLLLGGLLLLLLLLLLLLLLLLLLLLLLLLLLALLLALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLLLLL 643
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 679 IGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNSTPIVAVTAHAASGEREHLLQA 758
Cdd:COG2198   644 LLLLLLLLLAVLLAAAAAAAALAALDLLLDLDDMMMMLDDMMAEAARARALAARAAAIAAAAAAAAAAAAAAAAAAAALL 723
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 759 GMDDYLAKPIDEKMLTRVLSRYHSGDVENAVADDAPLSLDWPLALRQAANKPDLARDLLQMLLDFLPQVRERVQALLDGQ 838
Cdd:COG2198   724 AALLLLLLLLLLLLLLLLLLLLAAAAAAAASPAAPALPVLDLEALRRLGGDPELLRELLELFLEELPELLAELRQALAAG 803
                         810       820       830
                  ....*....|....*....|....*....|....*...
gi 2750649407 839 HDDEILDLVHKLHGSCSYSGVPRLKQLCFYLERQLRQG 876
Cdd:COG2198   804 DLEALARLAHKLKGSAGNLGAPRLAELAAELEQAARAG 841
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
280-521 2.14e-16

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 84.21  E-value: 2.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 280 LAKKRAQEAARI-------KSEFLANMSHELRTPLNGVIGFTRQMLKTDLSATQTDYLQTIERSANNLLTIINDVLDFSK 352
Cdd:PRK10618  431 LVNKKLQQAQREyeknqqaRKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNM 510
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 353 LEAGKLVLEHIPFALRETLDEVVVLLAPSAHDKGLELTLDVHNDVPEQVIGDSLRLQQIITNLLGNAIKFTETGNIDIRV 432
Cdd:PRK10618  511 LETQDWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYGKITLEV 590
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 433 ELRKrlDRRVEVEVQIHDTGIGISERQQSQLFQAFrQADASISRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTFW 512
Cdd:PRK10618  591 DQDE--SSPDRLTIRILDTGAGVSIKELDNLHFPF-LNQTQGDRYGKASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYS 667

                  ....*....
gi 2750649407 513 FHITLDLNE 521
Cdd:PRK10618  668 IHLKMLAAD 676
pleD PRK09581
response regulator PleD; Reviewed
665-778 8.59e-16

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 81.10  E-value: 8.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPANLKLIGT-LLGEQVEkTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNSTPIVAV 743
Cdd:PRK09581    4 RILVVDDIPANVKLLEAkLLAEYYT-VLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMV 82
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2750649407 744 TAHAASGEREHLLQAGMDDYLAKPIDEKML-TRVLS 778
Cdd:PRK09581   83 TALDDPEDRVRGLEAGADDFLTKPINDVALfARVKS 118
envZ PRK09467
osmolarity sensor protein; Provisional
296-499 2.59e-15

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 79.18  E-value: 2.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 296 LANMSHELRTPLngvigfTRQMLKTDLSATQTDYL-QTIERSANNLLTIINDVLDFSKLEAgKLVLEHIpfALRETLDEV 374
Cdd:PRK09467  233 MAGVSHDLRTPL------TRIRLATEMMSEEDGYLaESINKDIEECNAIIEQFIDYLRTGQ-EMPMEMA--DLNALLGEV 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 375 VvlLAPSAHDKGLELTLdvhNDVPEQVIGDSLRLQQIITNLLGNAIKFtetGNIDIRVELRKRLDRrveVEVQIHDTGIG 454
Cdd:PRK09467  304 I--AAESGYEREIETAL---QPGPIEVPMNPIAIKRALANLVVNAARY---GNGWIKVSSGTEGKR---AWFQVEDDGPG 372
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2750649407 455 ISERQQSQLFQAFRQADasISRRHGGTGLGLVITQKLVKEMGGDI 499
Cdd:PRK09467  373 IPPEQLKHLFQPFTRGD--SARGSSGTGLGLAIVKRIVDQHNGKV 415
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
666-781 1.26e-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: 71.03  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLL--CESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNSTP-IVA 742
Cdd:cd17532     1 ALIVDDEPLAREELRYLLEEHPDIEIVgeAENGEEALEAIEELKPDVVFLDIQMPGLDGL---ELAKKLSKLAKPPlIVF 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2750649407 743 VTAHaasgeREHLLQA---GMDDYLAKPIDEKMLTRVLSRYH 781
Cdd:cd17532    78 VTAY-----DEYAVEAfelNAVDYLLKPFSEERLAEALAKLR 114
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
666-776 1.72e-14

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: 70.49  E-value: 1.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLphHNSTPIVAVTA 745
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAA--GNDLPILVLTA 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2750649407 746 HAASGEREHLLQAGMDDYLAKPID-EKMLTRV 776
Cdd:cd17627    79 RDSVSDRVAGLDAGADDYLVKPFAlEELLARV 110
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
665-779 2.23e-14

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: 70.41  E-value: 2.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPANLKLIG-TLLGEQVEKTLLCEsGEEALALARDNVLDLILMDIQMPKMDGIhasELI---RQLPHHNSTPI 740
Cdd:cd17562     2 KILAVDDSASIRQMVSfTLRGAGYEVVEAAD-GRDALSKAQSKKFDLIITDQNMPNMDGI---ELIkelRKLPAYKFTPI 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2750649407 741 VAVTAHAASGEREHLLQAGMDDYLAKPIDEKMLTRVLSR 779
Cdd:cd17562    78 LMLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKK 116
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
665-778 2.89e-14

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 69.82  E-value: 2.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLphHNSTPIVAVT 744
Cdd:COG5803     4 KILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEI--DPDIPVIMMT 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2750649407 745 AHAASGEREHLLQAGMDDYLAKP--IDE--KMLTRVLS 778
Cdd:COG5803    82 AYGELDMVEEAKELGAKGYFTKPfdIDElrEAVNKLLK 119
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
292-511 3.83e-14

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 75.96  E-value: 3.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 292 KSEFLANMSHELRTPLNGVIGFTRQMLKTDLSATQ-TDYLQTIERSANNLLTIINDVLDFSKLEAGKLVLEHIPFALRET 370
Cdd:PRK09835  262 QSNFSADIAHEIRTPITNLITQTEIALSQSRSQKElEDVLYSNLEELTRMAKMVSDMLFLAQADNNQLIPEKKMLDLADE 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 371 LDEVVVLLAPSAHDKGLELTLDvhnDVPEQVIGDSLRLQQIITNLLGNAIKFTETGNiDIRVELRKRLDrrvEVEVQIHD 450
Cdd:PRK09835  342 VGKVFDFFEAWAEERGVELRFV---GDPCQVAGDPLMLRRAISNLLSNALRYTPAGE-AITVRCQEVDH---QVQLVVEN 414
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2750649407 451 TGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVKEMGGDICFHSQLnRGSTF 511
Cdd:PRK09835  415 PGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRF 474
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
696-767 4.15e-14

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: 69.01  E-value: 4.15e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2750649407 696 GEEALALARDNVLDLILMDIQMPKMDGIhasELIRQL-PHHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKP 767
Cdd:cd19935    31 GEDGLHLALTNEYDLIILDVMLPGLDGL---EVLRRLrAAGKQTPVLMLTARDSVEDRVKGLDLGADDYLVKP 100
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
156-515 5.66e-14

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: 74.26  E-value: 5.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 156 LGY----VAIE---LDLQSvrLQQYKEVF-----VSTLLLLLCMC-IAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLDS 222
Cdd:NF012226   28 LGYfiynYAIEvgwITLSS--LQEDWTEFhfvdwIWLFTVILCGSvISLIIGMKLAQRFIVPINFLADAAKKISQGDLSA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 223 RVEGYML--GELHMLKNGINSMAmsltayheemQQnidqatsdLRETLEQMEIQNveldlakkraqeaarikseflANMS 300
Cdd:NF012226  106 RAEDSQIhsAEISELMHNFNDMA----------QK--------LESSVKNAQVWN---------------------AAIA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 301 HELRTP-----------LNGVIGFTRQMLKTDLSATQtdylqtiersanNLLTIINDVLDFSKLEAGKLVLEHIPFALRE 369
Cdd:NF012226  147 HELRTPitilqgrlqgiLDGVFEPDPALFKSLLNQVE------------GLSHLVEDLRTLSLVENQQLRLNYESVDLKD 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 370 TLDEVVVLLAPSAHDKGLELTLDVHNDvpeQVIGDSLRLQQIITNLLGNAIKFTETGNIDIRveLRKRLDRRVeveVQIH 449
Cdd:NF012226  215 SIEKVLKMFEDRLEQAQLTIVLNLTAT---PVFCDRRRIEQVLIALIDNAIRYANAGKLKIS--SSVIQDDWI---LQIE 286
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2750649407 450 DTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVKEMGGDIcFHSQLNRGSTFWFHI 515
Cdd:NF012226  287 DEGPGIAEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSI-EYSNSQGNSVFTIKL 351
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
663-777 5.74e-14

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: 71.53  E-value: 5.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 663 PLTVMAVDDNPANLKLIGTLLGEQ-VEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNSTPIV 741
Cdd:COG3707     3 GLRVLVVDDEPLRRADLREGLREAgYEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGL---EAARQISEERPAPVI 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2750649407 742 AVTAHAASGEREHLLQAGMDDYLAKPIDEKMLTRVL 777
Cdd:COG3707    80 LLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPAL 115
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
178-508 7.38e-14

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 75.49  E-value: 7.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 178 VSTLLLLLCMCIAILFA-----YRLMRDVTGPIRNMVNTVDRIRRGQLDS--RVEGymlgelhmlKNGINSMAMSLTAYH 250
Cdd:COG4192   323 QSGILLLAIALLSLLLAvlinyFYVRRRLVKRLNALSDAMAAIAAGDLDVpiPVDG---------NDEIGRIARLLRVFR 393
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 251 EEMQQnidqatsdLRETLEQmEIQNVELDLAKKRAQEAARIKSEFLA-------NMSHELRTPLNG---VIGFTRQMLKT 320
Cdd:COG4192   394 DQAIE--------KTQELET-EIEERKRIEKNLRQTQDELIQAAKMAvvgqtmtSLAHELNQPLNAmsmYLFSAKKALEQ 464
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 321 DLSATQTDYLQTIERSANNLLTIINDVLDFSKLEAGKLVlehiPFALRETLDEVVVLLAPSAhdKGLELTLDVHNDVpeQ 400
Cdd:COG4192   465 ENYAQLPTSLDKIEGLIERMDKIIKSLRQFSRKSDTPLQ----PVDLRQVIEQAWELVESRA--KPQQITLHIPDDL--M 536
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 401 VIGDSLRLQQIITNLLGNAIKFTETgNIDIRVELrkrLDRRVEVEVQIHDTGIG--ISERqqsqLFQAFrqadasISRRH 478
Cdd:COG4192   537 VQGDQVLLEQVLVNLLVNALDAVAT-QPQISVDL---LSNAENLRVAISDNGNGwpLVDK----LFTPF------TTTKE 602
                         330       340       350
                  ....*....|....*....|....*....|
gi 2750649407 479 GGTGLGLVITQKLVKEMGGDICFHSQLNRG 508
Cdd:COG4192   603 VGLGLGLSICRSIMQQFGGDLYLASTLERG 632
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
665-779 7.76e-14

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 74.88  E-value: 7.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQlpHHNSTPIVAVT 744
Cdd:PRK11361    6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRS--HETRTPVILMT 83
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2750649407 745 AHAASGEREHLLQAGMDDYLAKPIDEKMLTRVLSR 779
Cdd:PRK11361   84 AYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQR 118
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
666-767 8.94e-14

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: 68.17  E-value: 8.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEAL---------ALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHN 736
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALnklenlakeGNDLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2750649407 737 STPIVAVTAHAASGEREHLLQAGMDDYLAKP 767
Cdd:cd19924    81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
666-773 9.54e-14

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: 68.59  E-value: 9.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPanlkLIGTLLGEQVEK---TLLCES--GEEALALARDNVLDLILMDIQMPKMDGIHASeliRQLPHHNSTPI 740
Cdd:cd19932     3 VLIAEDEA----LIRMDLREMLEEagyEVVGEAsdGEEAVELAKKHKPDLVIMDVKMPRLDGIEAA---KIITSENIAPI 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2750649407 741 VAVTAHAASGEREHLLQAGMDDYLAKPIDEKML 773
Cdd:cd19932    76 VLLTAYSQQDLVERAKEAGAMAYLVKPFSESDL 108
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
290-352 1.08e-13

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


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 66.47  E-value: 1.08e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2750649407 290 RIKSEFLANMSHELRTPLNGVIGFTRQMLKTDL-SATQTDYLQTIERSANNLLTIINDVLDFSK 352
Cdd:cd00082     2 QAKGEFLANVSHELRTPLTAIRGALELLEEELLdDEEQREYLERIREEAERLLRLINDLLDLSR 65
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
398-499 1.33e-13

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: 67.82  E-value: 1.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 398 PEQVIGDSLRLQQIITNLLGNAIKFT-ETGNIDIRVELRKRLDRRVEvevqihDTGIGISERQQSQLFQAFRQADasiSR 476
Cdd:cd16940     4 DIQVQGDALLLFLLLRNLVDNAVRYSpQGSRVEIKLSADDGAVIRVE------DNGPGIDEEELEALFERFYRSD---GQ 74
                          90       100
                  ....*....|....*....|...
gi 2750649407 477 RHGGTGLGLVITQKLVKEMGGDI 499
Cdd:cd16940    75 NYGGSGLGLSIVKRIVELHGGQI 97
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
666-767 1.90e-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: 66.80  E-value: 1.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNSTPIVAVTA 745
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGL---EVIRRLREWSAVPVIVLSA 77
                          90       100
                  ....*....|....*....|..
gi 2750649407 746 HAASGEREHLLQAGMDDYLAKP 767
Cdd:cd17620    78 RDEESDKIAALDAGADDYLTKP 99
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
665-777 2.16e-13

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: 67.43  E-value: 2.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNP---ANLKLIGTLLGEQVEKTllCESGEEALALARDNVLDLILMDIQMP-KMDGIHASELIRQlphHNSTPI 740
Cdd:cd17534     2 KILIVEDEAiiaLDLKEILESLGYEVVGI--ADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIRE---KFDIPV 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2750649407 741 VAVTAHAasgEREHLLQA------GmddYLAKPIDEKMLTRVL 777
Cdd:cd17534    77 IFLTAYS---DEETLERAketnpyG---YLVKPFNERELKAAI 113
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
683-779 2.82e-13

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: 66.86  E-value: 2.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 683 LGEQVEKTL--------LCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQL-PHHNSTPIVAVTAHAASGERE 753
Cdd:cd17625     9 LSEAITKHLkkegytvdVCFDGEEGLEYALSGIYDLIILDIMLPGMDGL---EVLKSLrEEGIETPVLLLTALDAVEDRV 85
                          90       100
                  ....*....|....*....|....*....
gi 2750649407 754 HLLQAGMDDYLAKP--IDEKML-TRVLSR 779
Cdd:cd17625    86 KGLDLGADDYLPKPfsLAELLArIRALLR 114
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
666-779 6.27e-13

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: 65.95  E-value: 6.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNSTPIVAVTA 745
Cdd:cd17626     3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGI---EVCRQIRAESGVPIVMLTA 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2750649407 746 HAASGEREHLLQAGMDDYLAKPIDEKML-TRVLSR 779
Cdd:cd17626    80 KSDTVDVVLGLESGADDYVAKPFKPKELvARIRAR 114
PRK10604 PRK10604
sensor protein RstB; Provisional
298-499 9.50e-13

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 71.17  E-value: 9.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 298 NMSHELRTPLngVIGFTRQMLKTDLSATQTdylQTIERSANNLLTIINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVL 377
Cdd:PRK10604  218 GIAHELRTPL--VRLRYRLEMSDNLSAAES---QALNRDIGQLEALIEELLTYARLDRPQNELHLSEPDLPAWLSTHLAD 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 378 LAPSAHDKGLELTLDVHNDVpeqVIGDSLRLQQIITNLLGNAIKFTETgnidiRVELRKRLDRRvEVEVQIHDTGIGISE 457
Cdd:PRK10604  293 IQAVTPEKTVRLDTPHQGDY---GALDMRLMERVLDNLLNNALRYAHS-----RVRVSLLLDGN-QACLIVEDDGPGIPP 363
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2750649407 458 RQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVKEMGGDI 499
Cdd:PRK10604  364 EERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSV 405
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
665-776 1.39e-12

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


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 64.99  E-value: 1.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPANLKLIGTLL---GEQVEKTllCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLphhnsTPIV 741
Cdd:cd17542     2 KVLIVDDAAFMRMMLKDILtkaGYEVVGE--AANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKI-----DPNA 74
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2750649407 742 AVTAHAASGEREHL---LQAGMDDYLAKPID-EKMLTRV 776
Cdd:cd17542    75 KVIMCSAMGQEEMVkeaIKAGAKDFIVKPFQpERVLEAV 113
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
382-515 1.98e-12

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 69.88  E-value: 1.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 382 AHDKGLELTLDVHNDVPEQVIGDSLrLQQIITNLLGNAIKFTETGNID---IRVELRKRLDrrvEVEVQIHDTGIGISER 458
Cdd:COG3290   257 ARERGIDLTIDIDSDLPDLPLSDTD-LVTILGNLLDNAIEAVEKLPEEerrVELSIRDDGD---ELVIEVEDSGPGIPEE 332
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2750649407 459 QQSQLFQafrqaDASISRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTFWFHI 515
Cdd:COG3290   333 LLEKIFE-----RGFSTKLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRL 384
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
666-794 2.13e-12

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 67.52  E-value: 2.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALArDNVLDLILMDIQMPKMDGIHASELIRQlphHNSTPIVAVTA 745
Cdd:PRK10955    4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLL-DDSIDLLLLDVMMPKKNGIDTLKELRQ---THQTPVIMLTA 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2750649407 746 HAASGEREHLLQAGMDDYLAKPIDEKMLT----RVLSRYHSGDVENAVADDAP 794
Cdd:PRK10955   80 RGSELDRVLGLELGADDYLPKPFNDRELVarirAILRRSHWSEQQQNNDNGSP 132
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
666-767 2.13e-12

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: 64.72  E-value: 2.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGE--QVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNSTPIVAV 743
Cdd:cd17541     3 VLIVDDSAVMRKLLSRILESdpDIEVVGTARDGEEALEKIKELKPDVITLDIEMPVMDGL---EALRRIMAERPTPVVMV 79
                          90       100
                  ....*....|....*....|....*.
gi 2750649407 744 TAHAASGEREHL--LQAGMDDYLAKP 767
Cdd:cd17541    80 SSLTEEGAEITLeaLELGAVDFIAKP 105
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-513 2.20e-12

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: 63.95  E-value: 2.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 408 LQQIITNLLGNAIKFTETGNIDIRvELRKRL----DRRVEVEVqiHDTGIGISERQQSQLFQAFRQADASisrrhgGTGL 483
Cdd:cd16920     1 IQQVLINLVRNGIEAMSEGGCERR-ELTIRTspadDRAVTISV--KDTGPGIAEEVAGQLFDPFYTTKSE------GLGM 71
                          90       100       110
                  ....*....|....*....|....*....|
gi 2750649407 484 GLVITQKLVKEMGGDICFHSQLNRGSTFWF 513
Cdd:cd16920    72 GLSICRSIIEAHGGRLSVESPAGGGATFQF 101
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-511 2.24e-12

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


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 63.98  E-value: 2.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 408 LQQIITNLLGNAIK-FTETGNIDIRVELRkrlDRRVEVEVQihDTGIGISERQQSQLFQAFrqadaSISRRHG-GTGLGL 485
Cdd:cd16943     4 LNQVLLNLLVNAAQaMEGRGRITIRTWAH---VDQVLIEVE--DTGSGIDPEILGRIFDPF-----FTTKPVGeGTGLGL 73
                          90       100
                  ....*....|....*....|....*.
gi 2750649407 486 VITQKLVKEMGGDICFHSQLNRGSTF 511
Cdd:cd16943    74 SLSYRIIQKHGGTIRVASVPGGGTRF 99
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
666-781 3.15e-12

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: 64.27  E-value: 3.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNSTPIVAVTA 745
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2750649407 746 HAASGEREHLLQAGMDDYLAKPIDEKMLtrvLSRYH 781
Cdd:cd17598    81 LSDPRDVIRGLECGADNFITKPYDEKYL---LSRIK 113
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-515 3.16e-12

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: 63.76  E-value: 3.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 408 LQQIITNLLGNAIKFT-ETGNIDIRVElrkRLDRRVEVEVQihDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLV 486
Cdd:cd16952     1 LRSAFSNLVSNAVKYTpPSDTITVRWS---QEESGARLSVE--DTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLA 75
                          90       100
                  ....*....|....*....|....*....
gi 2750649407 487 ITQKLVKEMGGDICFHSQLNRGSTFWFHI 515
Cdd:cd16952    76 IVKHVMSRHDARLLIASELGKGSRFTCLF 104
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
669-798 3.58e-12

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: 65.71  E-value: 3.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 669 VDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQlpHHNSTPIVAVTAHAA 748
Cdd:COG4567    10 VDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRE--RDPDARIVVLTGYAS 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2750649407 749 SGEREHLLQAGMDDYLAKPIDEKMLTRVLSRYHSgdvENAVADDAPLSLD 798
Cdd:COG4567    88 IATAVEAIKLGADDYLAKPADADDLLAALERAEG---DAPAPPENPMSLD 134
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
666-793 4.81e-12

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 69.29  E-value: 4.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLphHNSTPIVAVTA 745
Cdd:PRK10365    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAL--NPAIPVLIMTA 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2750649407 746 HAASGEREHLLQAGMDDYLAKPID----EKMLTRVLSRYHSGDVENAVADDA 793
Cdd:PRK10365   86 YSSVETAVEALKTGALDYLIKPLDfdnlQATLEKALAHTHSIDAETPAVTAS 137
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
666-773 4.97e-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: 63.42  E-value: 4.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNP---ANLKLIGTLLGEQVEKtllCESGEEALALARDNV--LDLILMDIQMPKMDGIHASELIRQLPHhnsTPI 740
Cdd:cd17584     1 VLVVDDDPtclAILKRMLLRCGYQVTT---CTDAEEALSMLRENKdeFDLVITDVHMPDMDGFEFLELIRLEMD---LPV 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2750649407 741 VAVTAHAASGEREHLLQAGMDDYLAKPIDEKML 773
Cdd:cd17584    75 IMMSADGSTSTVMKGLAHGACDYLLKPVSIEDL 107
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
664-773 5.21e-12

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: 63.51  E-value: 5.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 664 LTVMAVDDNPANLKLIGTLLGE-QVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNSTPIVA 742
Cdd:cd19923     1 MKVLVVDDFSTMRRIIKNLLKElGFNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLM 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2750649407 743 VTAHAAsgeREHL---LQAGMDDYLAKPIDEKML 773
Cdd:cd19923    81 VTAEAK---KENViaaAQAGVNNYIVKPFTAATL 111
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-499 8.93e-12

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


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 62.34  E-value: 8.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 408 LQQIITNLLGNAIKFT-ETGNIDIRVELRkrldrrvEVEVQIHDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLV 486
Cdd:cd16949     1 LARALENVLRNALRYSpSKILLDISQDGD-------QWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLA 73
                          90
                  ....*....|...
gi 2750649407 487 ITQKLVKEMGGDI 499
Cdd:cd16949    74 IAERAIEQHGGKI 86
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
11-563 1.08e-11

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 68.60  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  11 MILILAPTLLIGLLLSTFFVVHRYNELQEQLVDAGASIIEPLAVASEYGMTFRSRESVRQLVSLLHRRHSDIVRSITVFD 90
Cdd:COG2770    46 LLALLLLLLLLLLLLLAALVLLALLLAAALLLLLLLLSLVALAALLLALLLLLLLALLLLLAALLLLLLLAALALLLLLL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407  91 AQNNSFVTSNYHHNFAQLQLPKGVPLPTELMLTRRGDSLILRTPILSESQYPDETADGGSHPDNNLGYVAIELDLQSVRL 170
Cdd:COG2770   126 LLLAALLALLLALALLALLLGLAAARLLLAALLALAAALALALGAGELLLLADLAAAIAALLAALLLLLLGGLLLVVLLE 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 171 QQYKEVFVSTLLLLLCMCIAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKNGINSMAMSLTAYH 250
Cdd:COG2770   206 AALAALLLLLLLALLALLLALLLALLLARRITRPLRRLAEAARRIAAGDLDVRIPVSRKDEIGELARAFNRMADSLRESI 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 251 EEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQMLKTDLSATQTDYL 330
Cdd:COG2770   286 EEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLAL 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 331 QTIERSANNLLTIINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVLLAPSAHDKGLELTLDVHNDVPEQVIGDSLRLQQ 410
Cdd:COG2770   366 ELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALALLALAAAAAAAEAAAAALELAAAAI 445
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 411 IITNLLGNAIKFTETGNIDIRVELRKRLDRRVEVEVQIHDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQK 490
Cdd:COG2770   446 AAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEEEEEAGAAAEELAEELLLLEGLLLLLLLEAEA 525
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2750649407 491 LVKEMGGDICFHSQLNRGSTFWFHITLDLNEGMLSLAPSLPDLNGKTLAYIESNPTAAQATLNMLSVTQLVIT 563
Cdd:COG2770   526 LEVAEELLELEEAALLLAAAAELAALLALLLALAAVEAAALLLAALLLAAVAALLELAALLLLLLAAAEALAA 598
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
666-774 1.22e-11

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 62.32  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNSTPIVAVTA 745
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGL---DVLKELRKTSQVPVLMLTA 77
                          90       100
                  ....*....|....*....|....*....
gi 2750649407 746 HAASGEREHLLQAGMDDYLAKPIDEKMLT 774
Cdd:cd17623    78 RGDDIDRILGLELGADDYLPKPFNPRELV 106
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
669-769 1.66e-11

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 62.18  E-value: 1.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 669 VDDNP-------ANLKLIGtllGEQVektLLCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNST--- 738
Cdd:cd17552     7 IDDEEdirevvqACLEKLA---GWEV---LTASSGQEGLEKAATEQPDAILLDVMMPDMDGL---ATLKKLQANPETqsi 77
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2750649407 739 PIVAVTAHAASGEREHLLQAGMDDYLAKPID 769
Cdd:cd17552    78 PVILLTAKAQPSDRQRFASLGVAGVIAKPFD 108
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
403-499 2.63e-11

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: 61.13  E-value: 2.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 403 GDSLRLQQIITNLLGNAIKFTET--GNIDIRVELRKRL----DRRVEVEVQIHDTGIGISERQQSQLFQafrqadasisR 476
Cdd:cd16932     2 GDQIRLQQVLADFLLNAVRFTPSpgGWVEIKVSPTKKQigdgVHVIHLEFRITHPGQGLPEELVQEMFE----------E 71
                          90       100
                  ....*....|....*....|....*
gi 2750649407 477 RHGGT--GLGLVITQKLVKEMGGDI 499
Cdd:cd16932    72 NQWTTqeGLGLSISRKLVKLMNGDV 96
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
297-519 2.82e-11

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 66.73  E-value: 2.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 297 ANMSHELRTPLNGVIGFTRQMLKTDLSATQTDYL-QTIERSANNLLTIINDVLDFSKleAGKLVLEhiPFALRETLDEVV 375
Cdd:PRK10364  242 AGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLaQVMAKEADRLNRVVSELLELVK--PTHLALQ--AVDLNDLINHSL 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 376 VLLAPSAHDKGLELTLDVHNDVPEqVIGDSLRLQQIITNLLGNAIK-FTETGNIDIRVelrKRLDRRVEVEVQihDTGIG 454
Cdd:PRK10364  318 QLVSQDANSREIQLRFTANDTLPE-IQADPDRLTQVLLNLYLNAIQaIGQHGVISVTA---SESGAGVKISVT--DSGKG 391
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2750649407 455 ISERQQSQLFqafrqaDASISRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTFwfhiTLDL 519
Cdd:PRK10364  392 IAADQLEAIF------TPYFTTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATF----TLWL 446
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-504 2.96e-11

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: 60.88  E-value: 2.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 408 LQQIITNLLGNAIKFTETGNIDIRveLRKRLDR---------RVEVEVQIHDTGIGISERQQSQLFQAFrqadasISRRH 478
Cdd:cd16918     1 LIQVFLNLVRNAAQALAGSGGEII--LRTRTQRqvtlghprhRLALRVSVIDNGPGIPPDLQDTIFYPM------VSGRE 72
                          90       100
                  ....*....|....*....|....*.
gi 2750649407 479 GGTGLGLVITQKLVKEMGGDICFHSQ 504
Cdd:cd16918    73 NGTGLGLAIAQNIVSQHGGVIECDSQ 98
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-514 4.79e-11

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


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 60.14  E-value: 4.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 408 LQQIITNLLGNAIKFTETgniDIRVELRKRLDRRVeveVQIHDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVI 487
Cdd:cd16939     1 MARALDNLLRNALRYAHR---TVRIALLVSGGRLT---LIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAI 74
                          90       100
                  ....*....|....*....|....*...
gi 2750649407 488 TQKLVKEMGGDI-CFHSQLNrGSTFWFH 514
Cdd:cd16939    75 VHRVALWHGGHVeCDDSELG-GACFRLT 101
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
809-877 6.81e-11

Histidine Phosphotransfer domain, involved in signalling through a two part component systems in which an autophosphorylating histidine protein kinase serves as a phosphoryl donor to a response regulator protein; the response regulator protein is modulated by phosphorylation and dephosphorylation of a conserved aspartic acid residue; two-component proteins are abundant in most eubacteria; In E. coli there are 62 two-component proteins involved in a variety of processes such as chemotaxis, osmoregulation, metabolism and transport 1; also present in both Gram positive and Gram negative pathogenic bacteria where they regulate basic housekeeping functions and control expression of toxins and other proteins important for pathogenesis; in archaea and eukaryotes, two-component pathways constitute a very small number of all signaling systems; in fungi they mediate environmental stress responses and, in pathogenic yeast, hyphal development. In Dictyostelium and in plants, they are involved in important processes such as osmoregulation, cell growth, and differentiation; to date two-component proteins have not been identified in animals; in most prokaryotic systems, the output response is effected directly by the RR, which functions as a transcription factor while in eukaryotic systems, two-component proteins are found at the beginning of signaling pathways where they interface with more conventional eukaryotic signaling strategies such as MAP kinase and cyclic nucleotide cascades


Pssm-ID: 238041 [Multi-domain]  Cd Length: 94  Bit Score: 59.70  E-value: 6.81e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2750649407 809 KPDLARDLLQMLLDFLPQVRERVQALLDGQHDDEILDLVHKLHGSCSYSGVPRLKQLCFYLERQLRQGV 877
Cdd:cd00088     1 MEELLELFLEEAEELLEELERALLELEDAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALR 69
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
665-773 6.93e-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: 60.34  E-value: 6.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNSTPIVAVT 744
Cdd:cd17618     2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIMLT 81
                          90       100
                  ....*....|....*....|....*....
gi 2750649407 745 AHAASGEREHLLQAGMDDYLAKPIDEKML 773
Cdd:cd17618    82 ARGEEEDKVRGLEAGADDYITKPFSPREL 110
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
664-780 9.68e-11

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: 59.95  E-value: 9.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 664 LTVMAVDDNP----ANLKLIGTLLGEQVEKTllCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPH-HNST 738
Cdd:cd19925     1 INVLIVEDDPmvaeIHRAYVEQVPGFTVIGT--AGTGEEALKLLKERQPDLILLDIYLPDGNGL---DLLRELRAaGHDV 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2750649407 739 PIVAVTAHAASGEREHLLQAGMDDYLAKPIDEKMLTRVLSRY 780
Cdd:cd19925    76 DVIVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRLERY 117
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
815-876 1.29e-10

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: 58.52  E-value: 1.29e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2750649407 815 DLLQMLLDFLPQVRERVQALLDGQHDDEILDLVHKLHGSCSYSGVPRLKQLCFYLERQLRQG 876
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLLREG 62
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
665-745 1.58e-10

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: 59.16  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQlpHHNSTPIVAVT 744
Cdd:cd17554     2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIRE--KKPDLPVIICT 79

                  .
gi 2750649407 745 A 745
Cdd:cd17554    80 A 80
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
665-767 1.62e-10

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: 59.29  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQlpHHNSTPIVAVT 744
Cdd:cd17615     1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRA--DGPDVPVLFLT 78
                          90       100
                  ....*....|....*....|...
gi 2750649407 745 AHAASGEREHLLQAGMDDYLAKP 767
Cdd:cd17615    79 AKDSVEDRIAGLTAGGDDYVTKP 101
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
669-773 2.12e-10

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: 58.66  E-value: 2.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 669 VDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLphHNSTPIVAVTAHaa 748
Cdd:cd17550     4 VDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEK--YPDLPVIMISGH-- 79
                          90       100
                  ....*....|....*....|....*....
gi 2750649407 749 sGEREHLLQA---GMDDYLAKPID-EKML 773
Cdd:cd17550    80 -GTIETAVKAtklGAYDFIEKPLSlDRLL 107
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
666-767 2.25e-10

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: 58.15  E-value: 2.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNSTPIVAVTA 745
Cdd:cd17602     1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTG 80
                          90       100
                  ....*....|....*....|..
gi 2750649407 746 HAASGEREHLLQAGMDDYLAKP 767
Cdd:cd17602    81 KDGLVDRIRAKMAGASGYLTKP 102
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
666-767 2.30e-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: 58.16  E-value: 2.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNSTPIVAVTA 745
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80
                          90       100
                  ....*....|....*....|..
gi 2750649407 746 HAASGEREHLLQAGMDDYLAKP 767
Cdd:cd19927    81 KGMTSDRIKGYNAGCDGYLSKP 102
PRK15115 PRK15115
response regulator GlrR; Provisional
660-796 2.45e-10

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 63.70  E-value: 2.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 660 KRLPLTVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEAL-ALARDNVlDLILMDIQMPKMDGIHA-SELIRQLPhhnS 737
Cdd:PRK15115    2 SRKPAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALrVLNREKV-DLVISDLRMDEMDGMQLfAEIQKVQP---G 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2750649407 738 TPIVAVTAHAASGEREHLLQAGMDDYLAKPIDEKMLTRVlsryhsgdVENAVADDAPLS 796
Cdd:PRK15115   78 MPVIILTAHGSIPDAVAATQQGVFSFLTKPVDRDALYKA--------IDDALEQSAPAT 128
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
664-777 2.61e-10

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: 58.56  E-value: 2.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 664 LTVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALAL--ARDNVLDLILMDIQMPKMDGIHASELIRQL-PHHNSTPI 740
Cdd:cd19933     1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLlaSAEHSFQLVLLDLCMPEMDGFEVALRIRKLfGRRERPLI 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2750649407 741 VAVTAHAASGEREHLLQAGMDDYLAKPIDEKMLTRVL 777
Cdd:cd19933    81 VALTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
689-773 3.42e-10

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: 58.36  E-value: 3.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 689 KTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQlpHHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKPI 768
Cdd:cd17572    24 KVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQE--RSLPTSVIVITAHGSVDIAVEAMRLGAYDFLEKPF 101

                  ....*
gi 2750649407 769 DEKML 773
Cdd:cd17572   102 DADRL 106
PRK10693 PRK10693
two-component system response regulator RssB;
692-831 3.58e-10

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 62.32  E-value: 3.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 692 LCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLP-HHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKPIde 770
Cdd:PRK10693    2 LAANGVDALELLGGFTPDLIICDLAMPRMNGI---EFVEHLRnRGDQTPVLVISATENMADIAKALRLGVQDVLLKPV-- 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2750649407 771 KMLTR----VLSRYHSGDVENAVADDAPLSLDWpLALRQaanKPDLARDLLQMLldfLPQVRERV 831
Cdd:PRK10693   77 KDLNRlremVFACLYPSMFNSRVEEEERLFRDW-DALVD---NPAAAAKLLKQL---QPPVQQVI 134
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
296-499 4.77e-10

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 63.03  E-value: 4.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 296 LANMSHELRTPLngvigfTRQMLKTDLsAT--QTDY--LQTIERSANNLLTIINDVLDFSKLEAgKLVLEHIPFALRETL 371
Cdd:PRK09470  247 LSDISHELRTPL------TRLQLATAL-LRrrQGESkeLERIETEAQRLDSMINDLLVLSRNQQ-KNHLERETFKANSLW 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 372 DEVVVLLAPSAHDKGLELTLDVHndvPEQ--VIGDSLRLQQIITNLLGNAIKFTETgNIDIRVELRKRldrrvEVEVQIH 449
Cdd:PRK09470  319 SEVLEDAKFEAEQMGKSLTVSAP---PGPwpINGNPNALASALENIVRNALRYSHT-KIEVAFSVDKD-----GLTITVD 389
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2750649407 450 DTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVKEMGGDI 499
Cdd:PRK09470  390 DDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAIVENAIQQHRGWV 439
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-499 5.82e-10

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: 57.07  E-value: 5.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 408 LQQIITNLLGNAIKFtetGNIDIRVELRKRLDRrveVEVQIHDTGIGISERQQSQLFQAFRQADasISRRHGGTGLGLVI 487
Cdd:cd16950     1 LKRVLSNLVDNALRY---GGGWVEVSSDGEGNR---TRIQVLDNGPGIAPEEVDELFQPFYRGD--NARGTSGTGLGLAI 72
                          90
                  ....*....|..
gi 2750649407 488 TQKLVKEMGGDI 499
Cdd:cd16950    73 VQRISDAHGGSL 84
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
809-875 7.35e-10

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: 56.49  E-value: 7.35e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2750649407  809 KPDLARDLLQMLLDFLPQVRERVQALLDGQHDDEILDLVHKLHGSCSYSGVPRLKQLCFYLERQLRQ 875
Cdd:smart00073   2 GLELFREELAEFLQSLEEGLLELEKALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDA 68
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
695-779 9.16e-10

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: 57.11  E-value: 9.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 695 SGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQlpHHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKPIDEKMLT 774
Cdd:cd17624    30 TGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRR--QGQSLPVLILTARDGVDDRVAGLDAGADDYLVKPFALEELL 107

                  ....*...
gi 2750649407 775 ---RVLSR 779
Cdd:cd17624   108 arlRALLR 115
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
669-769 9.64e-10

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


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 57.43  E-value: 9.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 669 VDDNPANLKLIGTLLGE-QVEKTLL-CESGEEALA-LARDNVL------DLILMDIQMPKMDGIHASELIRQLPHHNSTP 739
Cdd:cd17557     5 VEDNPGDAELIQEAFKEaGVPNELHvVRDGEEALDfLRGEGEYadaprpDLILLDLNMPRMDGFEVLREIKADPDLRRIP 84
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2750649407 740 IVAVTahaASGEREHLLQA---GMDDYLAKPID 769
Cdd:cd17557    85 VVVLT---TSDAEEDIERAyelGANSYIVKPVD 114
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
666-776 1.20e-09

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: 56.76  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALA-LARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNST---PIV 741
Cdd:cd17544     3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEvLEQHPDIKLVITDYNMPEMDGF---ELVREIRKKYSRdqlAII 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2750649407 742 AVTAHAASGEREHLLQAGMDDYLAKP-IDEKMLTRV 776
Cdd:cd17544    80 GISASGDNALSARFIKAGANDFLTKPfLPEEFYCRV 115
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
382-515 1.34e-09

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 61.85  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 382 AHDKGLELTLDVHNDVP----EQVIGDslrLQQIITNLLGN---AIKFTETGNIDIRVELRkrlDRRVEVEVQihDTGIG 454
Cdd:PRK11086  407 ARELGITLIISEDSQLPdsgdEDQVHE---LITILGNLIENaleAVGGEEGGEISVSLHYR---NGWLHCEVS--DDGPG 478
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2750649407 455 ISERQQSQLFqafrqaDASISRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTFWFHI 515
Cdd:PRK11086  479 IAPDEIDAIF------DKGYSTKGSNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQI 533
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-511 1.40e-09

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: 56.24  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 408 LQQIITNLLGNAIKFTETgniDIRVELRKRLDRRVeVEVQIHDTGIGISERQQSQLFQAFRQADasISRRHGGTGLGLVI 487
Cdd:cd16923     1 LQRVFSNLLSNAIKYSPE---NTRIYITSFLTDDV-VNIMFKNPSSHPLDFKLEKLFERFYRGD--NSRNTEGAGLGLSI 74
                          90       100
                  ....*....|....*....|....
gi 2750649407 488 TQKLVKEMGGDICFHSQlNRGSTF 511
Cdd:cd16923    75 AKAIIELHGGSASAEYD-DNHDLF 97
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
664-718 2.55e-09

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: 53.73  E-value: 2.55e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2750649407  664 LTVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMP 718
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
670-776 5.01e-09

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: 54.98  E-value: 5.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 670 DDNPANLKLIGTLL--GEQVEktlLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHhnSTPIVAVTAHA 747
Cdd:cd19934     6 DDALLAAQLKEQLSdaGYVVD---VAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGR--ATPVLILTARD 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 2750649407 748 ASGEREHLLQAGMDDYLAKPID-EKMLTRV 776
Cdd:cd19934    81 SWQDKVEGLDAGADDYLTKPFHiEELLARL 110
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
404-499 5.16e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CreC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli CreC of the CreC-CreB two-component regulatory system (TCS) involved in catabolic regulation. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and accessory sensory domain(s) such as HAMP, CACHE or PAS.


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 54.77  E-value: 5.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 404 DSLRLQQIITNLLGNAIKFTETGNIdirVELRKRLDRRvEVEVQIHDTGIGISERQQSQLFQAFrqadASISRRHGG--- 480
Cdd:cd16945     1 DPFLLRQAINNLLDNAIDFSPEGGL---IALQLEADTE-GIELLVFDEGSGIPDYALNRVFERF----YSLPRPHSGqks 72
                          90
                  ....*....|....*....
gi 2750649407 481 TGLGLVITQKLVKEMGGDI 499
Cdd:cd16945    73 TGLGLAFVQEVAQLHGGRI 91
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
665-847 6.42e-09

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


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 56.65  E-value: 6.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPANLKLIGTLL---GEQVEktlLCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNST-PI 740
Cdd:COG4566     1 TVYIVDDDEAVRDSLAFLLesaGLRVE---TFASAEAFLAALDPDRPGCLLLDVRMPGMSGL---ELQEELAARGSPlPV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 741 VAVTAHA-------AsgerehlLQAGMDDYLAKPIDEKMLTRVlsryhsgdVENAVADDAplsldwplALRQAANKPDLA 813
Cdd:COG4566    75 IFLTGHGdvpmavrA-------MKAGAVDFLEKPFDDQALLDA--------VRRALARDR--------ARRAERARRAEL 131
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2750649407 814 RDLLQMLLDflpqvRERvqalldgqhddEILDLV 847
Cdd:COG4566   132 RARLASLTP-----RER-----------EVLDLV 149
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
665-767 8.27e-09

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 54.31  E-value: 8.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNP--ANLkLIGTLLGEQVEKTLLCEsGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNSTPIVA 742
Cdd:cd19938     1 RILIVEDEPklAQL-LIDYLRAAGYAPTLLAH-GDQVLPYVRHTPPDLILLDLMLPGTDGL---TLCREIRRFSDVPIIM 75
                          90       100
                  ....*....|....*....|....*
gi 2750649407 743 VTAHAASGEREHLLQAGMDDYLAKP 767
Cdd:cd19938    76 VTARVEEIDRLLGLELGADDYICKP 100
PRK11697 PRK11697
two-component system response regulator BtsR;
664-825 1.38e-08

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 56.39  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 664 LTVMAVDDNP---ANLKLigtLLGEQVEKTLL--CESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNST 738
Cdd:PRK11697    2 IKVLIVDDEPlarEELRE---LLQEEGDIEIVgeCSNAIEAIGAIHRLKPDVVFLDIQMPRISGL---ELVGMLDPEHMP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 739 PIVAVTAHaasgeREHLLQAGMD---DYLAKPIDEKMLTRVLSRyhsgdvenavaddaplsldwplaLRQAANKPDLARD 815
Cdd:PRK11697   76 YIVFVTAF-----DEYAIKAFEEhafDYLLKPIDPARLAKTLAR-----------------------LRQERSPQDVLLP 127
                         170
                  ....*....|
gi 2750649407 816 LLQMLLDFLP 825
Cdd:PRK11697  128 EAQPPLKHIP 137
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
693-780 1.61e-08

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: 53.31  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 693 CESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHhnSTPIVAVTAHAASGEREHLLQAGMDDYLAKPIDEKM 772
Cdd:cd17593    31 AENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQL--ETKVIVVSGDVQPEAKERVLELGALAFLKKPFDPEK 108

                  ....*...
gi 2750649407 773 LTRVLSRY 780
Cdd:cd17593   109 LAQLLEEL 116
glnL PRK11073
nitrogen regulation protein NR(II);
286-503 1.79e-08

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 57.40  E-value: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 286 QEAARiksEFLANMSHELRTPLNGVIGFTRQMLKTDLSATQTDYLQTIERSANNLLTIINDVLDFSKLEagklvlEHIPF 365
Cdd:PRK11073  127 QVAAR---DLVRGLAHEIKNPLGGLRGAAQLLSKALPDPALTEYTKVIIEQADRLRNLVDRLLGPQRPG------THVTE 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 366 ALRETLDEVVVLLAPSAHDKgLELTLDVHNDVPEQVIgDSLRLQQIITNLLGNAIKF--TETGNIDIRVEL--------- 434
Cdd:PRK11073  198 SIHKVAERVVQLVSLELPDN-VRLIRDYDPSLPELAH-DPDQIEQVLLNIVRNALQAlgPEGGTITLRTRTafqltlhge 275
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2750649407 435 RKRLDRRVEVEvqihDTGIGISERQQSQLFQAFrqadasISRRHGGTGLGLVITQKLVKEMGGDICFHS 503
Cdd:PRK11073  276 RYRLAARIDIE----DNGPGIPPHLQDTLFYPM------VSGREGGTGLGLSIARNLIDQHSGKIEFTS 334
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
295-492 1.89e-08

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 57.29  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 295 FLANMSHELRTPLNGVIGFTRQMLKTDLSATQT-----DYLQ-TIE------RSANNLLTIINDVLDFskleagklvLEH 362
Cdd:PRK10755  140 FTADVAHELRTPLAGIRLHLELLEKQHHIDVAPliarlDQMMhTVEqllqlaRAGQSFSSGHYQTVKL---------LED 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 363 IPFALRETLDEvvvLLAPSAHdkglelTLDV-HNDVPEQVIGDSLRLQQIITNLLGNAIKFTETGNiDIRVELRKRLDrr 441
Cdd:PRK10755  211 VILPSQDELSE---MLEQRQQ------TLLLpESAADITVQGDATLLRLLLRNLVENAHRYSPEGS-TITIKLSQEDG-- 278
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2750649407 442 vEVEVQIHDTGIGISERQQSQLFQAFRQADasisRRHGGTGLGLVITQKLV 492
Cdd:PRK10755  279 -GAVLAVEDEGPGIDESKCGELSKAFVRMD----SRYGGIGLGLSIVSRIT 324
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
404-518 2.07e-08

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


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 52.92  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 404 DSLRLQQIITNLLGNAIKFTETGNID-IRVELRKRLDRRVEVEVQIHDTGIGISERQQSQLFQAFrqadasISRRHGGTG 482
Cdd:cd16944     1 DTTQISQVLTNILKNAAEAIEGRPSDvGEVRIRVEADQDGRIVLIVCDNGKGFPREMRHRATEPY------VTTRPKGTG 74
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2750649407 483 LGLVITQKLVKEMGGDICFHSQLNRGStfWFHITLD 518
Cdd:cd16944    75 LGLAIVKKIMEEHGGRISLSNREAGGA--CIRIILP 108
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
665-798 2.42e-08

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 55.85  E-value: 2.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPanlKLiGTLLGEQVE----KTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLphhNSTPI 740
Cdd:PRK10710   12 RILIVEDEP---KL-GQLLIDYLQaasyATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRF---SDIPI 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2750649407 741 VAVTAHAASGEREHLLQAGMDDYLAKPIDEK-MLTRV---LSRYHSGDVENAVADDAPLSLD 798
Cdd:PRK10710   85 VMVTAKIEEIDRLLGLEIGADDYICKPYSPReVVARVktiLRRCKPQRELQQQDAESPLIID 146
ompR PRK09468
osmolarity response regulator; Provisional
666-781 2.48e-08

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 55.75  E-value: 2.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEA-LALARDNVlDLILMDIQMPKMDGIHASELIRQlpHHNSTPIVAVT 744
Cdd:PRK09468    8 ILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMdRLLTRESF-HLMVLDLMLPGEDGLSICRRLRS--QNNPTPIIMLT 84
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2750649407 745 AHAASGEREHLLQAGMDDYLAKPIDEKMLtrvLSRYH 781
Cdd:PRK09468   85 AKGEEVDRIVGLEIGADDYLPKPFNPREL---LARIR 118
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
665-768 2.62e-08

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: 52.97  E-value: 2.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPANLKLIGTLL---GEQVektLLCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNS-TPI 740
Cdd:cd17555     2 TILVIDDDEVVRESIAAYLedsGFQV---LQAADGRQGLELFRSEQPDLVLCDLRMPEMDGL---EVLKQITKESPdTPV 75
                          90       100
                  ....*....|....*....|....*...
gi 2750649407 741 VAVTAHAASGEREHLLQAGMDDYLAKPI 768
Cdd:cd17555    76 IVVSGAGVMSDAVEALRLGAWDYLTKPI 103
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
666-774 2.94e-08

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: 52.77  E-value: 2.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNSTPIVAVTA 745
Cdd:cd17619     3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGL---SLTRELREQSEVGIILVTG 79
                          90       100
                  ....*....|....*....|....*....
gi 2750649407 746 HAASGEREHLLQAGMDDYLAKPIDEKMLT 774
Cdd:cd17619    80 RDDEVDRIVGLEIGADDYVTKPFNPRELL 108
PRK10643 PRK10643
two-component system response regulator PmrA;
695-805 3.57e-08

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 55.04  E-value: 3.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 695 SGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQlpHHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKPID-EKML 773
Cdd:PRK10643   32 TAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQ--KKYTLPVLILTARDTLEDRVAGLDVGADDYLVKPFAlEELH 109
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2750649407 774 TRV--LSRYHSGDVENAVADDApLSLDwpLALRQ 805
Cdd:PRK10643  110 ARIraLIRRHQGQGENELQVGN-LTLN--LGRQQ 140
orf27 CHL00148
Ycf27; Reviewed
666-779 3.93e-08

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 55.11  E-value: 3.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGT---LLGEQVektLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQlphHNSTPIVA 742
Cdd:CHL00148    9 ILVVDDEAYIRKILETrlsIIGYEV---ITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRK---ESDVPIIM 82
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2750649407 743 VTAHAASGEREHLLQAGMDDYLAKPIDEKML-TRVLSR 779
Cdd:CHL00148   83 LTALGDVSDRITGLELGADDYVVKPFSPKELeARIRSV 120
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
696-770 4.35e-08

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: 52.27  E-value: 4.35e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2750649407 696 GEEALALARDNVLDLILMDIQMPKMDGIHASELIRQlpHHNSTPIVAVTAHAASGEREHLLQAGMDDYLAK--PIDE 770
Cdd:cd19930    33 GQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELRE--ELPDTKVLIVTTFGRPGYFRRALAAGVDGYVLKdrPIEE 107
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-519 4.43e-08

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: 51.69  E-value: 4.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 408 LQQIITNLLGNAI-KFTETGNIDIRVELRkRLDRRVEVEVQihDTGIGISERQQSQLFQAFRQadasiSRRHG-GTGLGL 485
Cdd:cd16976     1 IQQVLMNLLQNALdAMGKVENPRIRIAAR-RLGGRLVLVVR--DNGPGIAEEHLSRVFDPFFT-----TKPVGkGTGLGL 72
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2750649407 486 VITQKLVKEMGGDICFHSQLNRGSTFwfhiTLDL 519
Cdd:cd16976    73 SISYGIVEEHGGRLSVANEEGAGARF----TFDL 102
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
663-773 4.85e-08

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 54.65  E-value: 4.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 663 PLTVMAVDDNPANLKLIGTLLGEQVEKTLLCE--SGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPhhNSTPI 740
Cdd:PRK10651    6 PATILLIDDHPMLRTGVKQLISMAPDITVVGEasNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKS--LSGRI 83
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2750649407 741 VAVTAHAASGEREHLLQAGMDDYLAKPID-EKML 773
Cdd:PRK10651   84 VVFSVSNHEEDVVTALKRGADGYLLKDMEpEDLL 117
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
665-777 5.11e-08

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


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 52.02  E-value: 5.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQL-PHHNSTPIVAV 743
Cdd:cd17569     2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGA---ELLKRVrERYPDTVRILL 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2750649407 744 TAHAasgEREHLLQA----GMDDYLAKPIDEKMLTRVL 777
Cdd:cd17569    79 TGYA---DLDAAIEAinegEIYRFLTKPWDDEELKETI 113
PRK10610 PRK10610
chemotaxis protein CheY;
664-779 5.46e-08

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 52.28  E-value: 5.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 664 LTVMAVDDNPANLKLIGTLLGE----QVEKTllcESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNSTP 739
Cdd:PRK10610    6 LKFLVVDDFSTMRRIVRNLLKElgfnNVEEA---EDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALP 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2750649407 740 IVAVTAHAasgEREHLL---QAGMDDYLAKPIDEKMLTRVLSR 779
Cdd:PRK10610   83 VLMVTAEA---KKENIIaaaQAGASGYVVKPFTAATLEEKLNK 122
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
666-767 5.61e-08

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: 51.43  E-value: 5.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGihaSELIRQLPHHNSTPIVAVTA 745
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSG---TEVCRQLRARSNVPVIMVTA 77
                          90       100
                  ....*....|....*....|..
gi 2750649407 746 HAASGEREHLLQAGMDDYLAKP 767
Cdd:cd17621    78 KDSEIDKVVGLELGADDYVTKP 99
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
696-776 1.24e-07

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


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 50.83  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 696 GEEALALARDNVLDLILMDIQMPKMDGIHASELIRQlphHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKPIDEK-MLT 774
Cdd:cd19939    32 GQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVRE---HSHVPILMLTARTEEMDRVLGLEMGADDYLCKPFSPReLLA 108

                  ..
gi 2750649407 775 RV 776
Cdd:cd19939   109 RV 110
PRK11517 PRK11517
DNA-binding response regulator HprR;
696-809 1.34e-07

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 53.36  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 696 GEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKPID-EKMLT 774
Cdd:PRK11517   33 GRDGLYLALKDDYALIILDIMLPGMDGW---QILQTLRTAKQTPVICLTARDSVDDRVRGLDSGANDYLVKPFSfSELLA 109
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2750649407 775 RVLSRYHSGDVENAVADDAPLSLDwplALRQAANK 809
Cdd:PRK11517  110 RVRAQLRQHHALNSTLEISGLRMD---SVSQSVSR 141
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
411-511 1.45e-07

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: 50.36  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 411 IITNLLGNAIKFT-ETGNIDIRVElrkrlDRRVEVEVQIHDTGIGISERQQSQLFQAF------RQADASisrrhggTGL 483
Cdd:cd16948     9 IIGQIVSNALKYSkQGGKIEIYSE-----TNEQGVVLSIKDFGIGIPEEDLPRVFDKGftgengRNFQES-------TGM 76
                          90       100
                  ....*....|....*....|....*...
gi 2750649407 484 GLVITQKLVKEMGGDICFHSQLNRGSTF 511
Cdd:cd16948    77 GLYLVKKLCDKLGHKIDVESEVGEGTTF 104
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
689-769 1.51e-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: 50.73  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 689 KTLLCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQL-PHHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKP 767
Cdd:cd19919    26 TVTSFENAQEALAALASSQPDVLISDIRMPGMDGL---ALLAQIkQRHPDLPVIIMTAHSDLDSAVSAYQGGAFEYLPKP 102

                  ..
gi 2750649407 768 ID 769
Cdd:cd19919   103 FD 104
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
253-517 1.56e-07

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


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 55.13  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 253 MQQNIDQATSDLRETLEQMEIQNV--EL-DLAKKRAQEAARIK--SEFLANMS----HELRTPLNGVIGFTRQMLKTDLS 323
Cdd:TIGR03785 437 LSDDAEAAIDSQGRISGAIPASRSrdEIgDLSRSFAQMVARLRqyTHYLENMSsrlsHELRTPVAVVRSSLENLELQALE 516
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 324 ATQTDYLQTIERSANNLLTIINDVLDFSKLEAGKLVLEHIPFALRETLDEVVVLLAPSAHDKGLELTLDVhNDVPEQVIG 403
Cdd:TIGR03785 517 QEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLSEVLSGCMQGYQMTYPPQRFELNIPE-TPLVMRGSP 595
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 404 DslRLQQIITNLLGNAIKFT-ETGNIDIRVELRKRldrrvEVEVQIHDTGIGISERQQSQLFQAFRQADASISRRHGGTG 482
Cdd:TIGR03785 596 E--LIAQMLDKLVDNAREFSpEDGLIEVGLSQNKS-----HALLTVSNEGPPLPEDMGEQLFDSMVSVRDQGAQDQPHLG 668
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2750649407 483 LGLVITQKLVKEMGGDICFHSQlNRGSTFWFHITL 517
Cdd:TIGR03785 669 LGLYIVRLIADFHQGRIQAENR-QQNDGVVFRISL 702
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
663-729 1.96e-07

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: 50.66  E-value: 1.96e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2750649407 663 PLTVMAVDDNPANLKLIGTLLGEQVEKTLLCE--SGEEALALARDNVLDLILMDIQMPKMDGIHASELI 729
Cdd:COG2197     1 MIRVLIVDDHPLVREGLRALLEAEPDIEVVGEaaDGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
411-511 2.74e-07

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


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 49.59  E-value: 2.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 411 IITNLLGNAIKF---TETGNIDIRVELRKRLDrrvEVEVQIHDTGIGISERQQSQLFQAfrqadASISRRHGGTGLGLVI 487
Cdd:cd16915     4 IVGNLIDNALDAlaaTGAPNKQVEVFLRDEGD---DLVIEVRDTGPGIAPELRDKVFER-----GVSTKGQGERGIGLAL 75
                          90       100
                  ....*....|....*....|....
gi 2750649407 488 TQKLVKEMGGDICFHSQLNRGSTF 511
Cdd:cd16915    76 VRQSVERLGGSITVESEPGGGTTF 99
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
696-776 2.98e-07

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


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 49.73  E-value: 2.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 696 GEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKPIDEK-MLT 774
Cdd:cd17614    31 GREALEKVEEEQPDLILLDLMLPEKDGL---EVCREVRKTSNVPIIMLTAKDSEVDKVLGLELGADDYVTKPFSNReLLA 107

                  ..
gi 2750649407 775 RV 776
Cdd:cd17614   108 RV 109
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
664-782 3.24e-07

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: 50.13  E-value: 3.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 664 LTVMAVDDNPANLKLIGTLLGEQVEKTLLCES-GEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNSTPIVA 742
Cdd:cd17530     1 LRVLVLDDDPFQCMMAATILEDLGPGNVDEADdGREALVILLCNAPDIIICDLKMPDMDGI---EFLRHLAESHSNAAVI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2750649407 743 VTAHAASGEREHLLQAGMD------DYLAKPIDEKMLTRVLSRYHS 782
Cdd:cd17530    78 LMSGLDGGILESAETLAGAnglnllGTLSKPFSPEELTELLTKYTA 123
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
158-515 3.27e-07

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 53.87  E-value: 3.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 158 YVAIELDLQSVRLQQYKEVFVSTLLLLLCMCIAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLdSRVEGYMLGELHMLKN 237
Cdd:COG2972   138 TLVSLIPKSELFRGLFSLRRLILLIILLLLLLALLLSYLLSRSITRPIKRLKKAMKKVEKGDL-VRLEVSGNDEIGILAR 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 238 GINSMAMSLTAYHEEMQQnidqatsdLRETLEQMEIQNVEldlakkraqeaARIKSEFLANMshelrtpLNGVIGF---- 313
Cdd:COG2972   217 SFNEMVERIKELIEEVYE--------LELEKKEAELKALQ-----------AQINPHFLFNT-------LNSIRWLaele 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 314 ----TRQMLkTDLSatqtDYLQTIERSANNLLTIiNDVLDFSKleaGKLVLEHIpfalRetldevvvllapsaHDKGLEL 389
Cdd:COG2972   271 dpeeAEEML-EALS----KLLRYSLSKGDELVTL-EEELELIK---SYLEIQKL----R--------------FGDRLEV 323
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 390 TLDVHNDVPEQVIgdsLRLqqIITNLLGNAIKF-----TETGNIDIRVELRkrlDRRVEVEVQihDTGIGISERQQSQLF 464
Cdd:COG2972   324 EIEIDEELLDLLI---PKL--ILQPLVENAIEHgiepkEGGGTIRISIRKE---GDRLVITVE--DNGVGMPEEKLEKLL 393
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2750649407 465 QAFrqadasiSRRHGGTGLGLVITQKLVKEMGGD---ICFHSQLNRGSTFWFHI 515
Cdd:COG2972   394 EEL-------SSKGEGRGIGLRNVRERLKLYYGEeygLEIESEPGEGTTVTIRI 440
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
663-767 3.40e-07

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 53.23  E-value: 3.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 663 PLTVMAVDDNPANLKLIGTLLGEQVEKTLLCES--GEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLphhNSTPI 740
Cdd:PRK00742    3 KIRVLVVDDSAFMRRLISEILNSDPDIEVVGTApdGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRL---RPTPV 79
                          90       100
                  ....*....|....*....|....*....
gi 2750649407 741 VAVTAHAASGEREHL--LQAGMDDYLAKP 767
Cdd:PRK00742   80 VMVSSLTERGAEITLraLELGAVDFVTKP 108
PRK10337 PRK10337
sensor protein QseC; Provisional
295-493 3.42e-07

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 53.88  E-value: 3.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 295 FLANMSHELRTPLngvigfTRQMLKTDLSATQTDYLQTIERSANNLLT-------IINDVLDFSKLEAGKLVLEHIPFAL 367
Cdd:PRK10337  240 FTSDAAHELRSPL------AALKVQTEVAQLSDDDPQARKKALLQLHAgidratrLVDQLLTLSRLDSLDNLQDVAEIPL 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 368 RETLDEVVVLLAPSAHDKGLELTLDVhNDVPEQVIGDSLRLQQIITNLLGNAIKFTETGNIdirVELrkRLDRRvevEVQ 447
Cdd:PRK10337  314 EDLLQSAVMDIYHTAQQAGIDVRLTL-NAHPVIRTGQPLLLSLLVRNLLDNAIRYSPQGSV---VDV--TLNAR---NFT 384
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2750649407 448 IHDTGIGISERQQSQLFQAF-RQADASISrrhgGTGLGLVITQKLVK 493
Cdd:PRK10337  385 VRDNGPGVTPEALARIGERFyRPPGQEAT----GSGLGLSIVRRIAK 427
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
665-776 5.36e-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: 5.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNSTPIVAVT 744
Cdd:cd17594     1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGL---DLLRTIRARSDVPIIIIS 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2750649407 745 AHAASGE-REHLLQAGMDDYLAKPID-EKMLTRV 776
Cdd:cd17594    78 GDRRDEIdRVVGLELGADDYLAKPFGlRELLARV 111
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
666-767 7.17e-07

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: 48.50  E-value: 7.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALA-LARDNVLDLILMDIQMPkmDGIHASELIRQ-LPHHNSTPIVAV 743
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDlLESGPDIDLLVTDVIMP--GGMNGSQLAEEaRRRRPDLKVLLT 78
                          90       100
                  ....*....|....*....|....
gi 2750649407 744 TAHAASGEREHLLQAGMdDYLAKP 767
Cdd:cd18161    79 SGYAENAIEGGDLAPGV-DVLSKP 101
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
693-798 9.75e-07

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 50.73  E-value: 9.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 693 CESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQL-PHHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKPIDEK 771
Cdd:PRK11083   33 FERGLPALDKLRQQPPDLVILDVGLPDISGF---ELCRQLlAFHPALPVIFLTARSDEVDRLVGLEIGADDYVAKPFSPR 109
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2750649407 772 MLT-RV---LSRYHSGDVENAVADDAPLSLD 798
Cdd:PRK11083  110 EVAaRVrtiLRRVKKFAAPSPVIRIGHFELD 140
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
397-499 1.07e-06

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: 48.61  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 397 VPEQVIGDSLRLQQIITNLLGNAIKFTET-GNIDIRVEL---------------RKRLDR---RVEVEVQIHDTGIGISE 457
Cdd:cd16938     1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGgGNITFRVFLeggsedrsdrdwgpwRPSMSDesvEIRFEVEINDSGSPSIE 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2750649407 458 RQQSQlfqafrqadASISRRHG----GTGLGLVITQKLVKEMGGDI 499
Cdd:cd16938    81 SASMR---------NSLNRRYNlselGEHLSFSICKQLVQLMGGNI 117
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
404-499 1.94e-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: 47.46  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 404 DSLRLQQIITNLLGNAIKFT-ETGNIDIRVELRKRLdrrveVEVQIHDTGIGISERQQSQLFQAFRQADAsiSRRHGG-T 481
Cdd:cd16975     1 DTLLLSRALINIISNACQYApEGGTVSISIYDEEEY-----LYFEIWDNGHGFSEQDLKKALELFYRDDT--SRRSGGhY 73
                          90
                  ....*....|....*...
gi 2750649407 482 GLGLVITQKLVKEMGGDI 499
Cdd:cd16975    74 GMGLYIAKNLVEKHGGSL 91
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
696-745 2.19e-06

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 50.65  E-value: 2.19e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2750649407 696 GEEALALARDNVLDLILMDIQMPKMDGIHASELI-RQLPhhnsTPIVAVTA 745
Cdd:PRK12555   35 GAQAVERCAAQPPDVILMDLEMPRMDGVEATRRImAERP----CPILIVTS 81
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
666-776 2.53e-06

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: 47.02  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLL---GEQVEKTLLcesGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHN-STPIV 741
Cdd:cd17616     1 VLLIEDDSATAQSIELMLkseGFNVYTTDL---GEEGLDLGKLYDYDIILLDLNLPDMSGY---EVLRTLRLAKvKTPIL 74
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2750649407 742 AVTAHAASGEREHLLQAGMDDYLAKPID-EKMLTRV 776
Cdd:cd17616    75 ILSGLADIEDKVKGLGFGADDYMTKPFHkDELVARI 110
Spo0A COG5801
Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell ...
663-775 3.52e-06

Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444503 [Multi-domain]  Cd Length: 264  Bit Score: 49.41  E-value: 3.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 663 PLTVMAVDDNPANLKLIGTLLGEQ--VEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNSTPI 740
Cdd:COG5801     4 KIKVLIADDNREFCELLEEYLSSQpdMEVVGVAYNGLEALELIEEKKPDVVILDIIMPHLDGLGVLEKLREMNLEKRPKV 83
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2750649407 741 VAVTAHAASGEREHLLQAGMDDYLAKPIDEKMLTR 775
Cdd:COG5801    84 IMLTAFGQEDITQRAVELGADYYILKPFDLDVLAE 118
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
696-767 3.63e-06

phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; Sinorhizobium meliloti ChvI is part of the ExoS/ChvI two-component regulatory system (TCS) that is required for nitrogen-fixing symbiosis and exopolysaccharide synthesis. ExoS/ChvI also play important roles in regulating biofilm formation, motility, nutrient utilization, and the viability of free-living bacteria. ChvI belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 46.28  E-value: 3.63e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2750649407 696 GEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKP 767
Cdd:cd19936    31 GASALDGLNARPPDLAILDIKMPRMDGM---ELLQRLRQKSTLPVIFLTSKDDEIDEVFGLRMGADDYITKP 99
HAMP pfam00672
HAMP domain;
196-248 3.81e-06

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 44.92  E-value: 3.81e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2750649407 196 RLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKNGINSMAMSLTA 248
Cdd:pfam00672   1 LLARRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERLRE 53
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
709-783 4.52e-06

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 48.65  E-value: 4.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2750649407 709 DLILMDIQMPKMDGIhasELIRQLPHHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKP--IDEKML-TRVLSRYHSG 783
Cdd:PRK10529   47 DLIILDLGLPDGDGI---EFIRDLRQWSAIPVIVLSARSEESDKIAALDAGADDYLSKPfgIGELQArLRVALRRHSA 121
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
694-780 4.56e-06

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 50.25  E-value: 4.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 694 ESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQlpHHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKP--IDE- 770
Cdd:PRK10923   34 ENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQ--RHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPfdIDEa 111
                          90
                  ....*....|.
gi 2750649407 771 -KMLTRVLSRY 780
Cdd:PRK10923  112 vALVERAISHY 122
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
665-779 4.62e-06

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: 46.43  E-value: 4.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPANLKLIGTLL---GEQVEktlLCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNST-PI 740
Cdd:cd17537     2 TVYVVDDDEAVRDSLAFLLrsvGLAVK---TFTSASAFLAAAPPDQPGCLVLDVRMPGMSGL---ELQDELLARGSNiPI 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2750649407 741 VAVTAH-----AASGerehlLQAGMDDYLAKPIDEKMLTRVLSR 779
Cdd:cd17537    76 IFITGHgdvpmAVEA-----MKAGAVDFLEKPFRDQVLLDAIEQ 114
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
666-769 4.88e-06

phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family response regulators; Streptococcus agalactiae NsrR is a lantibiotic resistance-associated response regulator and is part of the nisin resistance operon. It is a member of the NsrRK two-component system (TCS) that is involved in the regulation of lantibiotic resistance genes such as a membrane-associated lipoprotein of LanI, and the nsr gene cluster which encodes for the resistance protein NSR and the ABC transporter NsrFP, both conferring resistance against nisin. This subfamily also includes Staphylococcus epidermidis GraR, part of the GraR/GraS TCS involved in resistance against cationic antimicrobial peptides, and Bacillus subtilis BceR, part of the BceS/BceR TCS involved in the regulation of bacitracin resistance. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 46.12  E-value: 4.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQlphHNSTPIVAVTa 745
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQ---ISNVPIIFIS- 76
                          90       100
                  ....*....|....*....|....*.
gi 2750649407 746 hAASGEREHL--LQAGMDDYLAKPID 769
Cdd:cd18159    77 -SRDDNMDQVmaINMGGDDYITKPFD 101
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
665-767 4.90e-06

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: 45.96  E-value: 4.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALA-LARDNVLDLILMDIQMPKMDGIhasELIRQLPH-HNSTPIVA 742
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEkLQQGKDIDIVVTDIVMPEMDGI---ELAREARKiDPDVKILF 77
                          90       100
                  ....*....|....*....|....*
gi 2750649407 743 VTAHAASGEREHLLQAGMDDYLAKP 767
Cdd:cd18160    78 ISGGAAAAPELLSDAVGDNATLKKP 102
PRK09483 PRK09483
response regulator; Provisional
693-766 5.33e-06

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 48.56  E-value: 5.33e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2750649407 693 CESGEEALALARDNVLDLILMDIQMPKMDGIHASELI-RQLPHhnsTPIVAVTAHAASGEREHLLQAGMDDYLAK 766
Cdd:PRK09483   33 ACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKIlRYTPD---VKIIMLTVHTENPLPAKVMQAGAAGYLSK 104
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
384-511 5.51e-06

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: 46.86  E-value: 5.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 384 DKGLELTLDVHndvPEQVI-GDSLRLQQIITNLLGNAIKFTetgnidirvelrkrlDRRVEVEVQ---------IHDTGI 453
Cdd:cd16954    16 RKGVSISLDIS---PELRFpGERNDLMELLGNLLDNACKWC---------------LEFVEVTARqtdgglhliVDDDGP 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2750649407 454 GISERQQSQLFQAFRQADasisRRHGGTGLGLVITQKLVKEMGGDICFHSQLNRGSTF 511
Cdd:cd16954    78 GVPESQRSKIFQRGQRLD----EQRPGQGLGLAIAKEIVEQYGGELSLSDSPLGGARF 131
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
666-773 6.44e-06

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 46.19  E-value: 6.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCE--SGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQlpHHNSTPIVAV 743
Cdd:cd19931     1 VLLIDDHPLLRKGIKQLIELDPDFTVVGEasSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALRE--EGVSARIVIL 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 2750649407 744 TAHAASGEREHLLQAGMDDYLAKPIDEKML 773
Cdd:cd19931    79 TVSDAEDDVVTALRAGADGYLLKDMEPEDL 108
fixJ PRK09390
response regulator FixJ; Provisional
665-792 8.12e-06

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 47.69  E-value: 8.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNST-PIVAV 743
Cdd:PRK09390    5 VVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGI---ELLRRLKARGSPlPVIVM 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2750649407 744 TAHAASGEREHLLQAGMDDYLAKPIDEK----MLTRVLSRYHSGDVENAVADD 792
Cdd:PRK09390   82 TGHGDVPLAVEAMKLGAVDFIEKPFEDErligAIERALAQAPEAAKSEAVAAD 134
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
154-289 8.87e-06

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 49.25  E-value: 8.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 154 NNLGYVAIELDLQSVRLQQYKEVFVSTLLLLLCMCIAILFAYRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELH 233
Cdd:COG0840   159 AAAALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIG 238
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2750649407 234 MLKNGINSMAMSLtayhEEMQQNIDQATSDLRETLEQMEIQNVELdlaKKRAQEAA 289
Cdd:COG0840   239 QLADAFNRMIENL----RELVGQVRESAEQVASASEELAASAEEL---AAGAEEQA 287
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
666-773 1.25e-05

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: 45.06  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNSTPIVAVTA 745
Cdd:cd17622     3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGL---TLCRDLRPKYQGPILLLTA 79
                          90       100
                  ....*....|....*....|....*...
gi 2750649407 746 HAASGEREHLLQAGMDDYLAKPIDEKML 773
Cdd:cd17622    80 LDSDIDHILGLELGADDYVVKPVEPAVL 107
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
666-767 1.34e-05

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 44.84  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQlpHHNSTPIVAVTA 745
Cdd:cd19926     1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQ--RLPQTPVAVITA 78
                          90       100
                  ....*....|....*....|..
gi 2750649407 746 HAASGEREHLLQAGMDDYLAKP 767
Cdd:cd19926    79 YGSLDTAIEALKAGAFDFLTKP 100
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
666-776 1.43e-05

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


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 45.38  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLcESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNSTPIVAVta 745
Cdd:cd17539     1 VLLVDDRPSSAERIAAMLSSEHEVVVE-ADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQLPILAV-- 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2750649407 746 hAASGEREHLLQA---GMDDYLAKPID-EKMLTRV 776
Cdd:cd17539    78 -ADPGDRGRLIRAleiGVNDYLVRPIDpNELLARV 111
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
408-513 1.66e-05

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: 44.68  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 408 LQQIITNLLGNAIK-FTETGNIDIRVElRKRLDRRVE-----------VEVQIHDTGIGISERQQSQLFQAFrqadaSIS 475
Cdd:cd16919     1 LELAILNLAVNARDaMPEGGRLTIETS-NQRVDADYAlnyrdlipgnyVCLEVSDTGSGMPAEVLRRAFEPF-----FTT 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2750649407 476 RRHG-GTGLGLVITQKLVKEMGGDICFHSQLNRGSTF--WF 513
Cdd:cd16919    75 KEVGkGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVriYL 115
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
669-769 2.71e-05

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: 43.97  E-value: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 669 VDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQL-PHHNSTPIV------ 741
Cdd:cd17563     6 VDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGL---DLIPPLrALQPDARIVvltgya 82
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2750649407 742 ----AVTAhaasgerehlLQAGMDDYLAKPID 769
Cdd:cd17563    83 siatAVEA----------IKLGADDYLAKPAD 104
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
666-779 3.02e-05

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: 44.40  E-value: 3.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNST-PIVAVT 744
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGL---ELLAQIRELDPDlPVILIT 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2750649407 745 AHAASGEREHLLQAGMDDYLAKPIDEKMLTRVLSR 779
Cdd:cd17549    78 GHGDVPMAVEAMRAGAYDFLEKPFDPERLLDVVRR 112
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
199-248 3.38e-05

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


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 42.24  E-value: 3.38e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2750649407  199 RDVTGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKNGINSMAMSLTA 248
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEE 50
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
666-773 4.57e-05

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 43.57  E-value: 4.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQlpHHNSTPIVAVTA 745
Cdd:cd17573     1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKE--KHPSIVVIVLSD 78
                          90       100
                  ....*....|....*....|....*...
gi 2750649407 746 HAASGEREHLLQAGMDDYLAKPIDEKML 773
Cdd:cd17573    79 NPKTEQEIEAFKEGADDYIAKPFDFKVL 106
PRK15479 PRK15479
transcriptional regulator TctD;
710-788 5.07e-05

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 45.48  E-value: 5.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 710 LILMDIQMPKMDGIhaSELIRQLPHHNSTPIVAVTAHAASGEREHLLQAGMDDYLAKPIDEKMLT---RVLSRYHSGDVE 786
Cdd:PRK15479   47 LAVLDINMPGMDGL--EVLQRLRKRGQTLPVLLLTARSAVADRVKGLNVGADDYLPKPFELEELDarlRALLRRSAGQVQ 124

                  ..
gi 2750649407 787 NA 788
Cdd:PRK15479  125 EV 126
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
663-773 5.19e-05

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 45.61  E-value: 5.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 663 PLTVMAVDDNPANLKLIGTLLGEQVEKTLLCE--SGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQlpHHNSTPI 740
Cdd:PRK10403    6 PFQVLIVDDHPLMRRGVRQLLELDPGFEVVAEagDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRR--DGVTAQI 83
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2750649407 741 VAVTAHAASGEREHLLQAGMDDYLAKPIDEKML 773
Cdd:PRK10403   84 IILTVSDASSDVFALIDAGADGYLLKDSDPEVL 116
PRK10766 PRK10766
two-component system response regulator TorR;
662-776 1.08e-04

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 44.64  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 662 LPLTVMAVDDNP---ANLKLIGTLLGEQVEKTllcESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNST 738
Cdd:PRK10766    1 MSYHILVVEDEPvtrARLQGYFEQEGYTVSEA---ASGAGMREIMQNQHVDLILLDINLPGEDGL---MLTRELRSRSTV 74
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2750649407 739 PIVAVTAHAASGEREHLLQAGMDDYLAKPID-EKMLTRV 776
Cdd:PRK10766   75 GIILVTGRTDSIDRIVGLEMGADDYVTKPLElRELLVRV 113
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-499 1.24e-04

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: 42.17  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 408 LQQIITNLLGNAIKFTETGNIDIRVELRKRLDRrveVEVQIHDTGIGISERQQSQLFQAF---RQADASISRRhggTGLG 484
Cdd:cd16953     1 LGQVLRNLIGNAISFSPPDTGRITVSAMPTGKM---VTISVEDEGPGIPQEKLESIFDRFyteRPANEAFGQH---SGLG 74
                          90
                  ....*....|....*
gi 2750649407 485 LVITQKLVKEMGGDI 499
Cdd:cd16953    75 LSISRQIIEAHGGIS 89
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
202-246 1.29e-04

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


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 40.12  E-value: 1.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2750649407 202 TGPIRNMVNTVDRIRRGQLDSRVEGYMLGELHMLKNGINSMAMSL 246
Cdd:cd06225     1 TRPLRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
669-768 1.29e-04

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 41.87  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 669 VDDNPANLKLI---------GTLLGEQvektllcESG----EEALALArdnvLDLILMDIQMPKMDGIHaseLIRQLPHH 735
Cdd:cd17565     4 VDDDKNIIKILsdiiedddlGEVVGEA-------DNGaqayDEILFLQ----PDIVLIDLLMPGMDGIQ---LVRKLKDT 69
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2750649407 736 NSTPIVAVTAHAASGE-REHLLQAGMDDYLAKPI 768
Cdd:cd17565    70 GSNGKFIMISQVSDKEmIGKAYQAGIEFFINKPI 103
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
666-767 1.83e-04

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


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 41.83  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLL--CESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNSTPIVAV 743
Cdd:cd17561     4 VLIADDNREFVQLLEEYLNSQPDMEVVgvAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPKIIML 83
                          90       100
                  ....*....|....*....|....
gi 2750649407 744 TAHAASGEREHLLQAGMDDYLAKP 767
Cdd:cd17561    84 TAFGQEDITQRAVELGASYYILKP 107
PRK10816 PRK10816
two-component system response regulator PhoP;
666-783 2.05e-04

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 43.57  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPA---NLKLIGTLLGEQVEKTllcESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNST-PIV 741
Cdd:PRK10816    3 VLVVEDNALlrhHLKVQLQDAGHQVDAA---EDAKEADYYLNEHLPDIAIVDLGLPDEDGL---SLIRRWRSNDVSlPIL 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2750649407 742 AVTAHAASGEREHLLQAGMDDYLAKPID-EKMLTRV--LSRYHSG 783
Cdd:PRK10816   77 VLTARESWQDKVEVLSAGADDYVTKPFHiEEVMARMqaLMRRNSG 121
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
666-768 3.41e-04

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: 41.20  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEAL-----------ALARDNVLDLILMDIQMPKMDGIHASELIRQLPH 734
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALeflgledeedsSNFNEPKVNMIITDYCMPGMTGYDLLKKVKESSA 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2750649407 735 HNSTPIVAVTAHAASGEREHLLQAGMDDYLAKPI 768
Cdd:cd17581    81 LKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPV 114
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
665-782 5.80e-04

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


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 40.85  E-value: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPanlkligtLLGEQVEKTL---------LCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHH 735
Cdd:cd17575     2 MVLLVDDQA--------IIGEAVRRALadeedidfhYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPAT 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2750649407 736 NSTPIVAVTAHAASGEREHLLQAGMDDYLAKPIDE-KMLTRVlsRYHS 782
Cdd:cd17575    74 RDIPIIVLSTKEEPEVKSEAFALGANDYLVKLPDKiELVARI--RYHS 119
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
666-864 7.06e-04

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 42.01  E-value: 7.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLPHHNSTPIVAVTA 745
Cdd:PRK10161    5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLTA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 746 HAASGEREHLLQAGMDDYLAKPIDEKMLT----RVLSRYHSGDVENAVADDApLSLDwPLALR--QAANKPDLARDLLQM 819
Cdd:PRK10161   85 RGEEEDRVRGLETGADDYITKPFSPKELVarikAVMRRISPMAVEEVIEMQG-LSLD-PTSHRvmAGEEPLEMGPTEFKL 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2750649407 820 LLDFLPQ-----VRERVQALLDGQH---DDEILDL-VHKLHGSCSYSGVPRLKQ 864
Cdd:PRK10161  163 LHFFMTHpervySREQLLNHVWGTNvyvEDRTVDVhIRRLRKALEPGGHDRMVQ 216
ActS_PrrB_HisK NF033792
ActS/PrrB/RegB family redox-sensitive histidine kinase; This redox-responsive histidine kinase, ...
301-501 1.23e-03

ActS/PrrB/RegB family redox-sensitive histidine kinase; This redox-responsive histidine kinase, found in alpha-proteobacteria, shows strong sequence conservation, including the notable motif [VA]AAAAHELGTPxTI. It always acts as a partner to an ActR/PrrA/RegA family global response regulator transcription factor in a two-component sensory transduction system. Lineage-specific names and gene symbols given to this histidine kinase reflect downstream regulator changes such as entry into stationary phase, anaerobic expression of photosynthesis genes, and survival of exposure to low pH.


Pssm-ID: 468186 [Multi-domain]  Cd Length: 423  Bit Score: 42.12  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 301 HELRTPLnGVIGFT-RQMLKT-----------DLSATQTDYLQTIERSannlLTiindvldfSKLEAGKLVLEHIPfaLR 368
Cdd:NF033792  211 HELGTPL-ATIALVaKELERElpddpplredaELLRSQAERCRDILRR----LT--------SLGEEGDAHLDRLP--LS 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 369 ETLDEVVvllAPsAHDKGLELTLDVHNDVPEQVIGdsLRLQQII---TNLLGNAIKFTETgnidiRVELRKRLDRRvEVE 445
Cdd:NF033792  276 ALIEEAA---AP-HRGFGKEIEVVVAGDPGEEPVI--RRNPEILyglGNLIENAVDFARS-----TVTVTASWDAE-SVT 343
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2750649407 446 VQIHDTGIGISERQQSQLFQAF--RQADASISRRHGGTGLGLVITQKLVKEMGGDICF 501
Cdd:NF033792  344 ITIEDDGPGFPPDVLSRIGEPYvtTRRGEERRPGGGGLGLGLFIAKTLLERSGATVTF 401
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
367-521 1.59e-03

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 42.20  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 367 LRETLDEVVVLLAPSAHDKGLELTLDVHNDV--PEQVIGDSLrlqqIITNLLGNAIKF----TETGNIDIRVELRkrlDR 440
Cdd:COG3920   361 LRDYLRELLEPLRDSYGGRGIRIELDGPDVElpADAAVPLGL----ILNELVTNALKHaflsGEGGRIRVSWRRE---DG 433
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 441 RVEVEVQihDTGIGISErqqsqlfqafrqaDASISRRhggTGLGLVITQKLVKEMGGDIcfhsQLNRGSTFWFHITLDLN 520
Cdd:COG3920   434 RLRLTVS--DNGVGLPE-------------DVDPPAR---KGLGLRLIRALVRQLGGTL----ELDRPEGTRVRITFPLA 491

                  .
gi 2750649407 521 E 521
Cdd:COG3920   492 E 492
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
666-769 1.73e-03

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: 39.07  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 666 VMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKMDGIHASELIRQLphhnsTPIVAVTA 745
Cdd:cd17553     3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVI-----DENIRVII 77
                          90       100
                  ....*....|....*....|....*..
gi 2750649407 746 HAASGEREHLLQA---GMDDYLAKPID 769
Cdd:cd17553    78 MTAYGELDMIQESkelGALTHFAKPFD 104
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
692-776 2.26e-03

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 40.68  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 692 LCESGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNS-TPIVAVTAHAASGEREHLLQAGMDDYLAKPID- 769
Cdd:PRK09836   29 LADNGLNGYHLAMTGDYDLIILDIMLPDVNGW---DIVRMLRSANKgMPILLLTALGTIEHRVKGLELGADDYLVKPFAf 105

                  ....*..
gi 2750649407 770 EKMLTRV 776
Cdd:PRK09836  106 AELLARV 112
PRK10336 PRK10336
two-component system response regulator QseB;
695-767 2.88e-03

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 40.26  E-value: 2.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2750649407 695 SGEEALALARdnvLDLILMDIQMPKMDGIhasELIRQLPHH-NSTPIVAVTAHAASGEREHLLQAGMDDYLAKP 767
Cdd:PRK10336   35 QGKEALYSAP---YDAVILDLTLPGMDGR---DILREWREKgQREPVLILTARDALAERVEGLRLGADDYLCKP 102
PRK10360 PRK10360
transcriptional regulator UhpA;
664-766 3.02e-03

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 39.96  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 664 LTVMAVDDNPANLKLIGTLLGEQVEKTLLCE--SGEEALALARDNVLDLILMDIQMPKMDGIhasELIRQLPHHNSTPIV 741
Cdd:PRK10360    2 ITVALIDDHLIVRSGFAQLLGLEPDLQVVAEfgSGREALAGLPGRGVQVCICDISMPDISGL---ELLSQLPKGMATIML 78
                          90       100
                  ....*....|....*....|....*
gi 2750649407 742 AVtaHAASGEREHLLQAGMDDYLAK 766
Cdd:PRK10360   79 SV--HDSPALVEQALNAGARGFLSK 101
pleD PRK09581
response regulator PleD; Reviewed
665-770 3.19e-03

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 41.04  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNPANLKLIGTLLGEQVEKTLLCESGEEALALARDNVlDLILMDIQMPKMDGIHASELIRQLPHHNSTPIVAVt 744
Cdd:PRK09581  157 RILLVDDDVSQAERIANILKEEFRVVVVSDPSEALFNAAETNY-DLVIVSANFENYDPLRLCSQLRSKERTRYVPILLL- 234
                          90       100
                  ....*....|....*....|....*....
gi 2750649407 745 ahAASGEREHLLQA---GMDDYLAKPIDE 770
Cdd:PRK09581  235 --VDEDDDPRLVKAlelGVNDYLMRPIDK 261
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
669-768 6.69e-03

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 37.24  E-value: 6.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 669 VDDNP-ANLKLIGTLLGEQVEKTLLCESGEEALALARDNVLDLILMDIQMPKmdGIHASELIRQLPHHN----STPIVAV 743
Cdd:cd17589     4 VDDQPtFRSMLKSMLRSLGVTRIDTASSGEEALRMCENKTYDIVLCDYNLGK--GKNGQQLLEELRHKKlispSTVFIMV 81
                          90       100
                  ....*....|....*....|....*
gi 2750649407 744 TAHAASGEREHLLQAGMDDYLAKPI 768
Cdd:cd17589    82 TGESSRAMVLSALELEPDDYLLKPF 106
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
665-778 7.66e-03

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: 37.23  E-value: 7.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750649407 665 TVMAVDDNP---ANLKLIGTLLGEQVEKTLLCESgeEALALARDNVLDLILMDIQMPkmDGIHASELIRQLPHHNSTPIV 741
Cdd:cd17540     2 RVLIIEDEPliaMDLEQIVEDLGHQVVGIARTRD--EAVALARRERPDLILADIQLA--DGSSGIDAVNEILTTHDVPVI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2750649407 742 AVTAH---AASGEREHllqagmDDYL-AKPIDEKMLTRVLS 778
Cdd:cd17540    78 FVTAYperLLTGERPE------PTFLiTKPFDPEMVKAAIS 112
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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